Q9Z4P0 · IFCA_SHEFN
- ProteinProbable fumarate reductase Ifc3
- GeneifcA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids588 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Flavocytochrome that catalyzes the reduction of fumarate to succinate in vitro (PubMed:10455032).
Is essentially unidirectional, catalyzing only fumarate reduction (PubMed:10455032).
In vitro, can use the artificial electron donor methyl viologen (PubMed:10455032).
May be involved in an alternative route for electron transport to Fe3+ (PubMed:10455032).
Is essentially unidirectional, catalyzing only fumarate reduction (PubMed:10455032).
In vitro, can use the artificial electron donor methyl viologen (PubMed:10455032).
May be involved in an alternative route for electron transport to Fe3+ (PubMed:10455032).
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 FAD per subunit.
Note: Binds 4 heme c groups covalently per monomer.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 31 | Fe (UniProtKB | ChEBI) of heme c 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 37 | heme c 1 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 40 | heme c 1 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 41 | Fe (UniProtKB | ChEBI) of heme c 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 58 | heme c 2 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 61 | heme c 2 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 62 | Fe (UniProtKB | ChEBI) of heme c 2 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 78 | Fe (UniProtKB | ChEBI) of heme c 3 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 81 | Fe (UniProtKB | ChEBI) of heme c 4 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 87 | heme c 3 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 90 | heme c 3 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 91 | Fe (UniProtKB | ChEBI) of heme c 3 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 93 | heme c 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 94 | Fe (UniProtKB | ChEBI) of heme c 1 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 101 | heme c 4 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 104 | heme c 4 (UniProtKB | ChEBI); covalent | ||||
Sequence: C | ||||||
Binding site | 105 | Fe (UniProtKB | ChEBI) of heme c 4 (UniProtKB | ChEBI); axial binding residue | ||||
Sequence: H | ||||||
Binding site | 154 | FAD (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 173 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 181 | FAD (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 182 | FAD (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 187 | FAD (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 187 | fumarate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 187 | succinate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 188 | FAD (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 218 | heme c 2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 295 | FAD (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 361 | FAD (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 382 | succinate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 394 | fumarate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 394 | succinate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 395 | fumarate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 395 | succinate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 419 | Proton donor | ||||
Sequence: R | ||||||
Binding site | 521 | fumarate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 521 | succinate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 551 | FAD (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 561 | fumarate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 561 | succinate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 564 | FAD (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 564 | fumarate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 564 | succinate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 566 | FAD (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 567 | FAD (UniProtKB | ChEBI) | ||||
Sequence: I |
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 | |||
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Aspect | Term | |
---|---|---|
Cellular Component | periplasmic space | |
Molecular Function | FMN binding | |
Molecular Function | metal ion binding | |
Molecular Function | oxidoreductase activity | |
Biological Process | steroid metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProbable fumarate reductase Ifc3
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Alteromonadales > Shewanellaceae > Shewanella
Accessions
- Primary accessionQ9Z4P0
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-22 | |||||
Sequence: MKLKYLVSAMALVVLSSGTAMA | ||||||
Chain | PRO_0000010346 | 23-588 | Probable fumarate reductase Ifc3 | |||
Sequence: KTPDMGSFHADMGSCQSCHAKPIKVTDSETHENAQCKSCHGEYAELANDKLQFDPHNSHLGDINCTSCHKGHEEPKFYCNECHSFDIKPMPFSDAKKKKSWDDGWDQDKIQKAIAAGPSETTQVLVVGAGSAGFNASLAAKKAGANVILVDKAPFSGGNSMISAGGMNAVGTKQQTAHGVEDKVEWFIEDAMKGGRQQNDIKLVTILAEQSADGVQWLESLGANLDDLKRSGGARVDRTHRPHGGKSSGPEIIDTLRKAAKEQGIDTRLNSRVVKLVVNDDHSVVGAVVHGKHTGYYMIGAKSVVLATGGYGMNKEMIAYYRPTMKDMTSSNNITATGDGVLMAKEIGASMTDIDWVQAHPTVGKDSRILISETVRGVGAVMVNKDGNRFISELTTRDKASDAILKQPGQFAWIIFDNQLYKKAKMVRGYDHLEMLYKGDTVEQLAKSTGMKVADLAKTVSDYNGYVASGKDTAFGRADMPLNMTQSPYYAVKVAPGIHHTMGGVAINTTASVLDLQSKPIDGLFAAGEVTGGVHGYNRLGGNAIADTVVFGRIAGDNAAKHALDK |
Interaction
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 135-588 | Flavoprotein-like | ||||
Sequence: AIAAGPSETTQVLVVGAGSAGFNASLAAKKAGANVILVDKAPFSGGNSMISAGGMNAVGTKQQTAHGVEDKVEWFIEDAMKGGRQQNDIKLVTILAEQSADGVQWLESLGANLDDLKRSGGARVDRTHRPHGGKSSGPEIIDTLRKAAKEQGIDTRLNSRVVKLVVNDDHSVVGAVVHGKHTGYYMIGAKSVVLATGGYGMNKEMIAYYRPTMKDMTSSNNITATGDGVLMAKEIGASMTDIDWVQAHPTVGKDSRILISETVRGVGAVMVNKDGNRFISELTTRDKASDAILKQPGQFAWIIFDNQLYKKAKMVRGYDHLEMLYKGDTVEQLAKSTGMKVADLAKTVSDYNGYVASGKDTAFGRADMPLNMTQSPYYAVKVAPGIHHTMGGVAINTTASVLDLQSKPIDGLFAAGEVTGGVHGYNRLGGNAIADTVVFGRIAGDNAAKHALDK |
Sequence similarities
In the C-terminal section; belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length588
- Mass (Da)62,946
- Last updated1999-05-01 v1
- Checksum99C4AE25814693D2
Mass Spectrometry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ236923 EMBL· GenBank· DDBJ | CAB37062.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP000447 EMBL· GenBank· DDBJ | ABI72427.1 EMBL· GenBank· DDBJ | Genomic DNA |