UniProtKB - Q79FX6 (MMAA2_MYCTU)
Protein
Cyclopropane mycolic acid synthase MmaA2
Gene
mmaA2
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
Catalyzes the conversion of a double bond to a cis cyclopropane ring at the distal position of an alpha mycolic acid via the transfer of a methylene group from S-adenosyl-L-methionine. MmaA2 also catalyzes the biosynthesis of the cis-cyclopropanated methoxymycolates. Cyclopropanated mycolic acids are key factors participating in cell envelope permeability, host immunomodulation and persistence.2 Publications
Catalytic activityi
- 1-acyl-2-(9Z)-enoyl-sn-glycero-3-phospholipid + S-adenosyl-L-methionine = 1-acyl-2-(9-cyclopronane)-acyl-sn-glycero-3-phospholipid + H+ + S-adenosyl-L-homocysteineEC:2.1.1.79
Activity regulationi
Inhibited by S-adenosyl-N-decyl-aminoethyl (SADAE) and thiacetazone (TAC).2 Publications
: mycolic acid biosynthesis Pathwayi
This protein is involved in the pathway mycolic acid biosynthesis, which is part of Lipid metabolism.View all proteins of this organism that are known to be involved in the pathway mycolic acid biosynthesis and in Lipid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 136 | S-adenosyl-L-methionine; via carbonyl oxygen | 1 | |
Active sitei | 269 | By similarity | 1 |
GO - Molecular functioni
- cyclopropane-fatty-acyl-phospholipid synthase activity Source: UniProtKB
- methyltransferase activity Source: UniProtKB
GO - Biological processi
- mycolic acid biosynthetic process Source: MTBBASE
Keywordsi
Molecular function | Methyltransferase, Transferase |
Biological process | Lipid biosynthesis, Lipid metabolism |
Ligand | S-adenosyl-L-methionine |
Enzyme and pathway databases
BioCyci | MetaCyc:G185E-4787-MONOMER MTBH37RV:G185E-4787-MONOMER |
UniPathwayi | UPA00915 |
Names & Taxonomyi
Protein namesi | Recommended name: Cyclopropane mycolic acid synthase MmaA2 (EC:2.1.1.79)Short name: CMAS Alternative name(s): Cyclopropane-fatty-acyl-phospholipid synthase Short name: CFA synthase Mycolic acid methyltransferase Short name: MA-MT S-adenosylmethionine-dependent methyltransferase Short name: AdoMet-MT Short name: SAM-MT |
Gene namesi | Name:mmaA2 Synonyms:mma2 Ordered Locus Names:Rv0644c |
Organismi | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic identifieri | 83332 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › |
Proteomesi |
|
Organism-specific databases
TubercuListi | Rv0644c |
Subcellular locationi
GO - Cellular componenti
- cell wall Source: MTBBASE
- plasma membrane Source: MTBBASE
Pathology & Biotechi
Disruption phenotypei
Disruption of this gene suppresses a cyclopropane group at the distal position of alpha mycolic acid and cause a mild impairment in methoxymycolate, but not in ketomycolate. A 2-fold reduction in the relative abundance of cis-cyclopropanated methoxymycolate is observed. Cells lacking both cmA2 and mmaA2 genes cannot cis cyclopropanate methoxymycolates or ketomycolates.1 Publication
Chemistry databases
DrugBanki | DB01718 Cetrimonium DB01752 S-adenosyl-L-homocysteine |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources | |||
ChainiPRO_0000398359 | 2 – 287 | Cyclopropane mycolic acid synthase MmaA2Add BLAST | 286 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylvalineCombined sources | 1 |
Keywords - PTMi
AcetylationProteomic databases
PaxDbi | Q79FX6 |
PRIDEi | Q79FX6 |
PTM databases
iPTMneti | Q79FX6 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q79FX6 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q79FX6 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 33 – 34 | S-adenosyl-L-methionine binding | 2 | |
Regioni | 72 – 74 | S-adenosyl-L-methionine binding | 3 | |
Regioni | 94 – 99 | S-adenosyl-L-methionine binding | 6 | |
Regioni | 123 – 124 | S-adenosyl-L-methionine binding | 2 |
Sequence similaritiesi
Belongs to the CFA/CMAS family.Curated
Phylogenomic databases
eggNOGi | ENOG4108NUI Bacteria COG2230 LUCA |
HOGENOMi | HOG000245191 |
InParanoidi | Q79FX6 |
KOi | K00574 |
OMAi | LHCITAQ |
PhylomeDBi | Q79FX6 |
Family and domain databases
InterProi | View protein in InterPro IPR003333 Mycolic_cyclopropane_synthase IPR029063 SAM-dependent_MTases |
PIRSFi | PIRSF003085 CMAS, 1 hit |
SUPFAMi | SSF53335 SSF53335, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q79FX6-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MVNDLTPHFE DVQAHYDLSD DFFRLFLDPT QTYSCAHFER EDMTLEEAQI
60 70 80 90 100
AKIDLALGKL GLQPGMTLLD IGCGWGATMR RAIAQYDVNV VGLTLSKNQA
110 120 130 140 150
AHVQKSFDEM DTPRDRRVLL AGWEQFNEPV DRIVSIGAFE HFGHDRHADF
160 170 180 190 200
FARAHKILPP DGVLLLHTIT GLTRQQMVDH GLPLTLWLAR FLKFIATEIF
210 220 230 240 250
PGGQPPTIEM VEEQSAKTGF TLTRRQSLQP HYARTLDLWA EALQEHKSEA
260 270 280
IAIQSEEVYE RYMKYLTGCA KLFRVGYIDV NQFTLAK
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP43387.1 |
RefSeqi | NP_215158.1, NC_000962.3 WP_003900985.1, NZ_NVQJ01000007.1 |
Genome annotation databases
EnsemblBacteriai | CCP43387; CCP43387; Rv0644c |
GeneIDi | 888061 |
KEGGi | mtu:Rv0644c mtv:RVBD_0644c |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP43387.1 |
RefSeqi | NP_215158.1, NC_000962.3 WP_003900985.1, NZ_NVQJ01000007.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1TPY | X-ray | 2.20 | A | 1-287 | [»] | |
SMRi | Q79FX6 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 83332.Rv0644c |
Chemistry databases
DrugBanki | DB01718 Cetrimonium DB01752 S-adenosyl-L-homocysteine |
PTM databases
iPTMneti | Q79FX6 |
Proteomic databases
PaxDbi | Q79FX6 |
PRIDEi | Q79FX6 |
Genome annotation databases
EnsemblBacteriai | CCP43387; CCP43387; Rv0644c |
GeneIDi | 888061 |
KEGGi | mtu:Rv0644c mtv:RVBD_0644c |
Organism-specific databases
TubercuListi | Rv0644c |
Phylogenomic databases
eggNOGi | ENOG4108NUI Bacteria COG2230 LUCA |
HOGENOMi | HOG000245191 |
InParanoidi | Q79FX6 |
KOi | K00574 |
OMAi | LHCITAQ |
PhylomeDBi | Q79FX6 |
Enzyme and pathway databases
UniPathwayi | UPA00915 |
BioCyci | MetaCyc:G185E-4787-MONOMER MTBH37RV:G185E-4787-MONOMER |
Miscellaneous databases
EvolutionaryTracei | Q79FX6 |
Family and domain databases
InterProi | View protein in InterPro IPR003333 Mycolic_cyclopropane_synthase IPR029063 SAM-dependent_MTases |
PIRSFi | PIRSF003085 CMAS, 1 hit |
SUPFAMi | SSF53335 SSF53335, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | MMAA2_MYCTU | |
Accessioni | Q79FX6Primary (citable) accession number: Q79FX6 Secondary accession number(s): L0T7B6 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 5, 2010 |
Last sequence update: | July 5, 2004 | |
Last modified: | September 18, 2019 | |
This is version 102 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families - Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references