Q4PEM9 · FER3_USTMA
- ProteinSiderophore peptide synthetase fer3
- Genefer3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids4830 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of siderophore ferrichrome A which is contributing to organismal virulence (PubMed:17138696, PubMed:20070524).
The first step of ferrichrome A biosynthesis is performed by the HMG-CoA synthase hcs1 which catalyzes the generation of HMG-CoA and CoA using acetoacetyl-CoA and acetyl-CoA as substrates (PubMed:20070524).
The enoyl-CoA isomerase/hydratase fer4 then catalyzes the conversion of hcs1-produced HMG-CoA to methylglutaconyl-CoA (PubMed:20070524).
The acyltransferase fer5 then fuses the fer4-generated methylglutaconyl-CoA with sid1-generated hydroxyornithine to yield methylglutaconyl hydroxyornithine (PubMed:20070524).
Methylglutaconyl hydroxyornithine is then available for use by the NRPS fer3 to generate ferrichrome A (PubMed:20070524).
The first step of ferrichrome A biosynthesis is performed by the HMG-CoA synthase hcs1 which catalyzes the generation of HMG-CoA and CoA using acetoacetyl-CoA and acetyl-CoA as substrates (PubMed:20070524).
The enoyl-CoA isomerase/hydratase fer4 then catalyzes the conversion of hcs1-produced HMG-CoA to methylglutaconyl-CoA (PubMed:20070524).
The acyltransferase fer5 then fuses the fer4-generated methylglutaconyl-CoA with sid1-generated hydroxyornithine to yield methylglutaconyl hydroxyornithine (PubMed:20070524).
Methylglutaconyl hydroxyornithine is then available for use by the NRPS fer3 to generate ferrichrome A (PubMed:20070524).
Pathway
Siderophore biosynthesis.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ligase activity | |
Molecular Function | phosphopantetheine binding | |
Biological Process | amino acid activation for nonribosomal peptide biosynthetic process | |
Biological Process | secondary metabolite biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSiderophore peptide synthetase fer3
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Ustilaginomycotina > Ustilaginomycetes > Ustilaginales > Ustilaginaceae > Ustilago
Accessions
- Primary accessionQ4PEM9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Disruption phenotype
Impairs the production of ferrichrome A but does not affect the production of ferrichrome (PubMed:20070524).
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000441959 | 1-4830 | Siderophore peptide synthetase fer3 | |||
Sequence: MAATTLSRLPALHPYSAVAEPRTLDGTRCFKFMRKSCLEFVKSLVNDEKGEKLISSLAVFVGHLVGCDADEALFKVRFGDGQTRITSAGAVHAQVVDVEASSLPGIAFRFFPPQPTLPKTLDDDLVVTVNSNSDKDVEFVLEFAQTVPSEAGQGIFAYFCKQVLESTLTEDETPLSILNPSPVSKLPEHAQLHDSFLDQAEKFPDRMAVQFLERLDQEDMGQFSKLTYDELKRLATSLAVKLQATHAKTSKPQNRQVVVPMLLCPSLELYVSYLAILMAGFAFCPLPVDAPDARLISLLAQLDTTILLGANSSQPPQWMPASVEWINVTDTLAETDQFAKHLTPAKRMQECAYVLFTSGTTGTPKGVQISHYSASISIFSHAACLDPSLLQLSSNTPGSTFKWFQFASTVFDPSVMEIFVTLSSGGTLCSANRALTLSDLEKVVRLSGADIMMATPSVATLLNPERIPKLKFLWTMGECLNSTVIRRFAAENGRTTLANAYGPTEASVNCTLLQPFPADFRGSIIGAPLPSCSLAVLHDGGDSPSGEKRFQAAPRGVTGELVIGGSHVGIGYLDMPEATADAFTTFAPLGRVYRTRDRARVVWDRDGNPLIEILGRMNAEQVKLSGRRVELGEIDSILQSSHTIQNAASVIWRPPTSQLQSGGGERLVCCIVLAPSAQPQDAEADCKIIADAQLPPHMRPWRYIVLPGLPVTVSGKSDRKQLSKIVAELLSSSAEQGSTKERSSEQNQVNANEDPVTQALIEAICAVCQLDAKSVSMDGDLFELGMDSLSAMRLLQLLRQSKVTATAARQLQVAQILGAKACRDLIPLLSDTTVSRDAEENNVSYPNNTDWSTELRSFEDRCRRSALLGLDERTRMRVQKIFPTTATQSGMLTSFLTRPASIGSKRSYINHTVYHFSSVSEACKFFDAFRTVLQKHDIYRTVFVPVDDKLAPFAQCVLSPASDDDNVSAHTSSTAIDACLKQHLEQIDNAISLEQPPWHLGLLAPPQEDEVEQSVVVLSLMHAIFDGGSLDLLQQEVVSLLRDDALQTSLEVRCTELEATVQHHFTSDLESSRRFWHQRLEGVSRTRFPCANGYKATEQSALGHASEVTELYSRSSMDEIVKQARCQRTSALVLLQTAWNLVLAAYTEDESLNYITSGSVHSGRLDEQTQSCMAPTFNVIPFITRLDQGTGNSATLTSAQLLAEATQASTAGLSHLEIPLGALARSGGMPFDTLFAVQRFDAQTCSNATLPWASISYPVMANDFAVMVEVWPGSKATEKMRLRLTYSLAVLDAPSAQLLLQQYEDILHSLMREPETTTVQQLINGEGLRQSALSVCRGPLASENDDSQTEAQLLHSYFENKAATEPEAIALEFYFNQDSDTDGSMEVQRWTYFELNAQANRLARYLLSVTGKPTLRDLPIPICMERCPELYVGVLATLKAGGAWCPIDVQSPRARQLELIARTKSRVVLVTPNTSADLGEVQADGQPLTIKVNACDTSQFHHLSADNLRPTATPATLAYLIWTSGTTGAPKGVMIEHASAVASMQALQQHVKPLQQDMPPRCLQFSAYTFDVFVQDLFWTWGLGGAIIAATREIMLGSTAELIAASQTSHAHLTPAFAAGLRRDSCPSITSVTFIGEKLTESVAADWTSSCASIDKPNDSIAVYNTYGPAEVTVVATLRQLFGGEKLQSANVGVPMQGVTAIVCKNREQPIRPCAKGSIGELVLAGAQVGRGYLNDKAKTEAAFTYSPEWKQRLYYTGDYVRMLHDGSIEFIGRRDDLVKLGGIRVELSEISAALLSVQERRKQAAVVERVETMMLSRLDRPTKQVISFLACPYLAASTDRGVHGAISEPLLLTSGDAIQLAHQTLNNVRDVLPPYMVPSMVLVLSRIPQTASAKIDRAKLQAAYDSADLAQWVSLLSTTADDPDNPEGEDGDLQCQVIAAISEITGTSTQDINSSSSLVSIGLDSIRAIRLAAKLKQNGTPLPISTLLACSTVRMLIRGLATKTGDGHEVAEEDTRNRLLAVKLSEFDKNVREMLPTGSKQDFEVCIPCSTLQEGMLAETLADPAAYWSDHVLQLDSHIDLARLAEAWRRAAHNIEMLRTVFAVVSQTAGLEEVQFDKNTDVFALQMVHKSVDITLIDVCDPIRVKSDDRLHQAVSKWTRSVAQDRADNVFATPLWKVKTFVVQDDSSSGNDQVPLTYAALCIHHALYDGPSIDIILNRVRDEYSALSPDMLDDHHNIRLLPTTSLSTQSEFAYACVADEQRESILHWEQKLQPRGPAAMLPDLTSVKDLPSDAKSARFIAASRKLQCTSARPQGVGLSALIKSAFAIVLAQYVEAEDQRHVVLGEILSLRNLHATLSTEQGAVGPLLTTQPFSLLLDAALEQKSAASYLQSNVIVHPSMQHRFASLASLAKIMGTRSDQEMFTAMYVYHPRRQPVSVSTKPIWTLLEDRSSEIRVEHSTVLNVFEHDDVEDSLILELSMKEDRISKDMLETLLDQVVSLLTLLLDGAGETLQALLGKVGQDQRELASVSHVPRGSRHAGDGSEVDQGHDPLFWLQHYAKNHPSWLAVVIAAGTPETACINDAELSSWTYAQLNAKADQVARLIRSLDLPSEGPIALCMQRSLISIAVTVAIFKCGRTYLPIDDQLPTERKRLLISDSRCALVVTEGTCLGELEADCISSVLNVSKNDFEQSLAALSHRDDHTELTSIKPRADDGAYLLYTSGSTGKPKGVLVGRANLCSFIDSYAEVVSAECPSTLQLGGKGRYLGLAGRAFDVHLSQMFMSWRFGLALATGERPLLLGDLKATVQTMSITHMSCVPSLLDQCDLVPQEVPSLVFLGVGGEKLTDRVRDTLASSLTVLNAYGPTETTIMCTVNRVHPHSHVRDIGQVLPGNTAVVIDFDDKSRFAPVIRGRAGELCIRGDLVALGYHALDPSQMATSGFVTTPDGTRMYRTGDAARMMADGSLHYLGRRDEQEKIRGQRLELGEVSRCAIAGADESIQATTLICQHESLAKPLLITLIATKTSSTGDQRRDTLPQFLAPSTETGRLAQHVLQYCKQHLPSYMVPDLVVGVSHLTQLAASGKTDVRRLKAWLAAADPTQLFSFEGRGHANAQSGSESNVNRPLSSLEREIASAIRRMLPKCPAEIRPDTSIFDLGIDSLSVIRLAGQLRKEGLAISIGRLRMHPRVQDIAAELSDSKALEVDLSVGVKALESFQARHQDQVQASRVEKVTKVLPCLPSQEGMVAISLSSKDEPVYVARIAVRFNDIQPEATAFAAVSLRRAWRQLSERHSILRTCFDHVDDVTIAQIVLDAVDIQRHIVTTKTQNSTAAIARAILQDITVIPPWRIELDDEAGSEPTFVLHMHHALYDGHSLPLLLNDLARVIQSIDDDGPESHDQQPGVQEMLESILSVSEQRAERFWRNTFADFPVNDPSVWTSIASVQGRAPLRCKATVQLAPLEAAAKTLQVTLSSLVASALGIALCRSLETTAFTVGFVLWGRSLDHVSAESIVAPCLTTVPMPFALCADRGSRHVGELIRACHDWNSSCLAFQHTSMRQIRRWIGSECRGSLVDLLYSFVQAGASNSSELARTWHLDSVEAETDAPAAVEVTADRDRDELRISAMARHLLPHDGLEGMTENLQILLNKIANGTGTNMDLKAAGIPTSSVASKLARELPSHSAVSRPLTAAEEQIRDLAVTMCGVPNTEMLQLDTPFLRIGLDSIVALRFSARLRREHGLQLSAHDVLAAGTIAGLSKLLDQRQAEGRSDATVSSSLDSTAARYKATPLQAGMLNGTLASASHDLYVHHHAVLFKQPLDHDRLQRALQHVVASHDILRTSFHLEGEPSETKNAVNSLSWYAQVTPFESLRSATEIRVVRSDKTASAALKEYGTDFIFDGPEKFNVSPWCAAILHCTSSQDVLVISMHHSLYDGVSLPSMFADLRASYHDLTHELVQRPPFSKAADLIASSAHESEQYWLKTLIEFKQPSLLVKKSSRSSTTPSLYRLDERRLSVSLATLKRLSAELGATPQAIAMLSWSKVLAVAAGQRDVCFGQVVSGRYLNLPGIEDVSGPLINTVPIRINLIDDLASNAVTARDLQERIVAAQPFQHASLGRIQNAWRREHGAHSTFFDTLFVFHNIEGKSSSASSSKSELWTALDPSEGPIQTESSTSTVVTTAASEYPVNISVIQDDDGVQIKAGASDAVGGIDWLPKTLQLFEQVFLDLLERPHRSVGAFPERLAALPLTVGRDGTDKDTSASVGVDAGRRSLSTAEQDIVLRHMAKRLNVDAAIINSCPNLFLLGIDSLLAICISADARSEQVPLTPFDVLSAGTFARLTVATETRSEAPRIGVDDSTDTEREMLVGKEAEQEAIELLKVPSCEVETVLPLLTGQQQHIAQWLQRGRRFLEPTFVYACPSKLDVSKLKSAWNELRRRNAALRTAFVRLKDRRTLVQVVLAENSLVWRDHERGRLGVVDGSNNLDAAAFEAVQRLNASPTDLFRPSARLTLVQGKQSDLVLVTIHHTSYDAWSMRLMADELMQLYHNIDQGKLESMRAPVSFADFIDQTHREALRNRDATASFWETRLRGASATLVCRGATQSLEQTMHVRKPALQDVDTLEAACRARGFGLQVVVILAYARLLSSEVSDTKITSPTFGFYTAGRASAIDGVGNMIGPTTAMQPMTVATAGGDQEDLFERLRAIQTDLVSRAEHQQDYVDLPVAFDAHLNLLWHKPITTSMRPPTDDSNASAPSLLKPYRLPYDSGYFTRHPLMPGNTSVDGDIHEAGAQLYMDVGLDASTKSLSLGARCDRSAMDAQQLEAFCDRFVGELEKIRAAL | ||||||
Modified residue | 788 | O-(pantetheine 4'-phosphoryl)serine | ||||
Sequence: S | ||||||
Modified residue | 1966 | O-(pantetheine 4'-phosphoryl)serine | ||||
Sequence: S | ||||||
Modified residue | 3159 | O-(pantetheine 4'-phosphoryl)serine | ||||
Sequence: S | ||||||
Modified residue | 3720 | O-(pantetheine 4'-phosphoryl)serine | ||||
Sequence: S | ||||||
Modified residue | 4301 | O-(pantetheine 4'-phosphoryl)serine | ||||
Sequence: S |
Keywords
- PTM
Expression
Induction
Expression regulated by iron through the urbs1 transcription factor (PubMed:17138696).
Interaction
Protein-protein interaction databases
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 197-623 | Adenylation 1 | ||||
Sequence: LDQAEKFPDRMAVQFLERLDQEDMGQFSKLTYDELKRLATSLAVKLQATHAKTSKPQNRQVVVPMLLCPSLELYVSYLAILMAGFAFCPLPVDAPDARLISLLAQLDTTILLGANSSQPPQWMPASVEWINVTDTLAETDQFAKHLTPAKRMQECAYVLFTSGTTGTPKGVQISHYSASISIFSHAACLDPSLLQLSSNTPGSTFKWFQFASTVFDPSVMEIFVTLSSGGTLCSANRALTLSDLEKVVRLSGADIMMATPSVATLLNPERIPKLKFLWTMGECLNSTVIRRFAAENGRTTLANAYGPTEASVNCTLLQPFPADFRGSIIGAPLPSCSLAVLHDGGDSPSGEKRFQAAPRGVTGELVIGGSHVGIGYLDMPEATADAFTTFAPLGRVYRTRDRARVVWDRDGNPLIEILGRMNAEQVK | ||||||
Domain | 751-833 | Carrier 1 | ||||
Sequence: ANEDPVTQALIEAICAVCQLDAKSVSMDGDLFELGMDSLSAMRLLQLLRQSKVTATAARQLQVAQILGAKACRDLIPLLSDTT | ||||||
Region | 879-1317 | Condensation 1 | ||||
Sequence: QKIFPTTATQSGMLTSFLTRPASIGSKRSYINHTVYHFSSVSEACKFFDAFRTVLQKHDIYRTVFVPVDDKLAPFAQCVLSPASDDDNVSAHTSSTAIDACLKQHLEQIDNAISLEQPPWHLGLLAPPQEDEVEQSVVVLSLMHAIFDGGSLDLLQQEVVSLLRDDALQTSLEVRCTELEATVQHHFTSDLESSRRFWHQRLEGVSRTRFPCANGYKATEQSALGHASEVTELYSRSSMDEIVKQARCQRTSALVLLQTAWNLVLAAYTEDESLNYITSGSVHSGRLDEQTQSCMAPTFNVIPFITRLDQGTGNSATLTSAQLLAEATQASTAGLSHLEIPLGALARSGGMPFDTLFAVQRFDAQTCSNATLPWASISYPVMANDFAVMVEVWPGSKATEKMRLRLTYSLAVLDAPSAQLLLQQYEDILHSLMREPETT | ||||||
Region | 1358-1781 | Adenylation 2 | ||||
Sequence: FENKAATEPEAIALEFYFNQDSDTDGSMEVQRWTYFELNAQANRLARYLLSVTGKPTLRDLPIPICMERCPELYVGVLATLKAGGAWCPIDVQSPRARQLELIARTKSRVVLVTPNTSADLGEVQADGQPLTIKVNACDTSQFHHLSADNLRPTATPATLAYLIWTSGTTGAPKGVMIEHASAVASMQALQQHVKPLQQDMPPRCLQFSAYTFDVFVQDLFWTWGLGGAIIAATREIMLGSTAELIAASQTSHAHLTPAFAAGLRRDSCPSITSVTFIGEKLTESVAADWTSSCASIDKPNDSIAVYNTYGPAEVTVVATLRQLFGGEKLQSANVGVPMQGVTAIVCKNREQPIRPCAKGSIGELVLAGAQVGRGYLNDKAKTEAAFTYSPEWKQRLYYTGDYVRMLHDGSIEFIGRRDDLVKL | ||||||
Domain | 1929-2005 | Carrier 2 | ||||
Sequence: GEDGDLQCQVIAAISEITGTSTQDINSSSSLVSIGLDSIRAIRLAAKLKQNGTPLPISTLLACSTVRMLIRGLATKT | ||||||
Region | 2048-2503 | Condensation 2 | ||||
Sequence: IPCSTLQEGMLAETLADPAAYWSDHVLQLDSHIDLARLAEAWRRAAHNIEMLRTVFAVVSQTAGLEEVQFDKNTDVFALQMVHKSVDITLIDVCDPIRVKSDDRLHQAVSKWTRSVAQDRADNVFATPLWKVKTFVVQDDSSSGNDQVPLTYAALCIHHALYDGPSIDIILNRVRDEYSALSPDMLDDHHNIRLLPTTSLSTQSEFAYACVADEQRESILHWEQKLQPRGPAAMLPDLTSVKDLPSDAKSARFIAASRKLQCTSARPQGVGLSALIKSAFAIVLAQYVEAEDQRHVVLGEILSLRNLHATLSTEQGAVGPLLTTQPFSLLLDAALEQKSAASYLQSNVIVHPSMQHRFASLASLAKIMGTRSDQEMFTAMYVYHPRRQPVSVSTKPIWTLLEDRSSEIRVEHSTVLNVFEHDDVEDSLILELSMKEDRISKDMLETLLDQVVSLLT | ||||||
Region | 2573-2977 | Adenylation 3 | ||||
Sequence: AGTPETACINDAELSSWTYAQLNAKADQVARLIRSLDLPSEGPIALCMQRSLISIAVTVAIFKCGRTYLPIDDQLPTERKRLLISDSRCALVVTEGTCLGELEADCISSVLNVSKNDFEQSLAALSHRDDHTELTSIKPRADDGAYLLYTSGSTGKPKGVLVGRANLCSFIDSYAEVVSAECPSTLQLGGKGRYLGLAGRAFDVHLSQMFMSWRFGLALATGERPLLLGDLKATVQTMSITHMSCVPSLLDQCDLVPQEVPSLVFLGVGGEKLTDRVRDTLASSLTVLNAYGPTETTIMCTVNRVHPHSHVRDIGQVLPGNTAVVIDFDDKSRFAPVIRGRAGELCIRGDLVALGYHALDPSQMATSGFVTTPDGTRMYRTGDAARMMADGSLHYLGRRDEQEKI | ||||||
Domain | 3122-3198 | Carrier 3 | ||||
Sequence: RPLSSLEREIASAIRRMLPKCPAEIRPDTSIFDLGIDSLSVIRLAGQLRKEGLAISIGRLRMHPRVQDIAAELSDSK | ||||||
Region | 3232-3621 | Condensation 3 | ||||
Sequence: KVLPCLPSQEGMVAISLSSKDEPVYVARIAVRFNDIQPEATAFAAVSLRRAWRQLSERHSILRTCFDHVDDVTIAQIVLDAVDIQRHIVTTKTQNSTAAIARAILQDITVIPPWRIELDDEAGSEPTFVLHMHHALYDGHSLPLLLNDLARVIQSIDDDGPESHDQQPGVQEMLESILSVSEQRAERFWRNTFADFPVNDPSVWTSIASVQGRAPLRCKATVQLAPLEAAAKTLQVTLSSLVASALGIALCRSLETTAFTVGFVLWGRSLDHVSAESIVAPCLTTVPMPFALCADRGSRHVGELIRACHDWNSSCLAFQHTSMRQIRRWIGSECRGSLVDLLYSFVQAGASNSSELARTWHLDSVEAETDAPAAVEVTADRDRDELRISA | ||||||
Domain | 3685-3760 | Carrier 4 | ||||
Sequence: TAAEEQIRDLAVTMCGVPNTEMLQLDTPFLRIGLDSIVALRFSARLRREHGLQLSAHDVLAAGTIAGLSKLLDQRQ | ||||||
Region | 3779-4199 | Condensation 4 | ||||
Sequence: RYKATPLQAGMLNGTLASASHDLYVHHHAVLFKQPLDHDRLQRALQHVVASHDILRTSFHLEGEPSETKNAVNSLSWYAQVTPFESLRSATEIRVVRSDKTASAALKEYGTDFIFDGPEKFNVSPWCAAILHCTSSQDVLVISMHHSLYDGVSLPSMFADLRASYHDLTHELVQRPPFSKAADLIASSAHESEQYWLKTLIEFKQPSLLVKKSSRSSTTPSLYRLDERRLSVSLATLKRLSAELGATPQAIAMLSWSKVLAVAAGQRDVCFGQVVSGRYLNLPGIEDVSGPLINTVPIRINLIDDLASNAVTARDLQERIVAAQPFQHASLGRIQNAWRREHGAHSTFFDTLFVFHNIEGKSSSASSSKSELWTALDPSEGPIQTESSTSTVVTTAASEYPVNISVIQDDDGVQIKAGASD | ||||||
Domain | 4264-4340 | Carrier 5 | ||||
Sequence: SLSTAEQDIVLRHMAKRLNVDAAIINSCPNLFLLGIDSLLAICISADARSEQVPLTPFDVLSAGTFARLTVATETRS | ||||||
Region | 4381-4708 | Condensation 5 | ||||
Sequence: VLPLLTGQQQHIAQWLQRGRRFLEPTFVYACPSKLDVSKLKSAWNELRRRNAALRTAFVRLKDRRTLVQVVLAENSLVWRDHERGRLGVVDGSNNLDAAAFEAVQRLNASPTDLFRPSARLTLVQGKQSDLVLVTIHHTSYDAWSMRLMADELMQLYHNIDQGKLESMRAPVSFADFIDQTHREALRNRDATASFWETRLRGASATLVCRGATQSLEQTMHVRKPALQDVDTLEAACRARGFGLQVVVILAYARLLSSEVSDTKITSPTFGFYTAGRASAIDGVGNMIGPTTAMQPMTVATAGGDQEDLFERLRAIQTDLVSRAEHQQ |
Domain
NRP synthetases are composed of discrete domains (adenylation (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation (C) domains) which when grouped together are referred to as a single module. Each module is responsible for the recognition (via the A domain) and incorporation of a single amino acid into the growing peptide product. Thus, an NRP synthetase is generally composed of one or more modules and can terminate in a thioesterase domain (TE) that releases the newly synthesized peptide from the enzyme. Occasionally, epimerase (E) domains (responsible for l- to d- amino acid conversion) are present within the NRP synthetase. Fer3 has the following architecture: A-T-C-A-T-C-A-T-C-T-C-T-C (PubMed:20070524).
The lack of corresponding A domains in the 2 last modules suggests that A domains have to be used iteratively to incorporate the six amino acids in ferrichrome A (PubMed:20070524).
The lack of corresponding A domains in the 2 last modules suggests that A domains have to be used iteratively to incorporate the six amino acids in ferrichrome A (PubMed:20070524).
Sequence similarities
Belongs to the NRP synthetase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length4,830
- Mass (Da)528,064
- Last updated2005-07-19 v1
- ChecksumB740ACB148A2F13B
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CM003141 EMBL· GenBank· DDBJ | KIS71541.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK004083 EMBL· GenBank· DDBJ | DAA04939.1 EMBL· GenBank· DDBJ | Genomic DNA |