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Q8CNR1

- FUMC_STAES

UniProt

Q8CNR1 - FUMC_STAES

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Protein

Fumarate hydratase class II

Gene
fumC, SE_1532
Organism
Staphylococcus epidermidis (strain ATCC 12228)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the reversible addition of water to fumarate to give L-malate By similarity.UniRule annotation

Catalytic activityi

(S)-malate = fumarate + H2O.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei186 – 1861Proton donor/acceptor By similarity
Active sitei316 – 3161 By similarity
Binding sitei317 – 3171Substrate By similarity
Sitei329 – 3291Important for catalytic activity By similarity

GO - Molecular functioni

  1. fumarate hydratase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. fumarate metabolic process Source: InterPro
  2. tricarboxylic acid cycle Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciSEPI176280:GCDG-1546-MONOMER.
UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase class II (EC:4.2.1.2)
Short name:
Fumarase C
Gene namesi
Name:fumC
Ordered Locus Names:SE_1532
OrganismiStaphylococcus epidermidis (strain ATCC 12228)
Taxonomic identifieri176280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000001411: Chromosome

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. tricarboxylic acid cycle enzyme complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 461461Fumarate hydratase class IIUniRule annotationPRO_0000161317Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi176280.SE1532.

Structurei

3D structure databases

ProteinModelPortaliQ8CNR1.
SMRiQ8CNR1. Positions 3-457.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 993Substrate binding By similarity
Regioni127 – 1304B site By similarity
Regioni137 – 1393Substrate binding By similarity
Regioni185 – 1862Substrate binding By similarity
Regioni322 – 3243Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0114.
KOiK01679.
OMAiLHPGLDI.
OrthoDBiEOG6V1M4M.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC.
InterProiIPR005677. Fum_hydII.
IPR024083. Fumarase/histidase_N.
IPR018951. Fumarase_C_C.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PfamiPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00979. fumC_II. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CNR1-1 [UniParc]FASTAAdd to Basket

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MSVRIEHDTF GEIEVPEDKY WGAQTERSKR NFPVGKEHMP IQVIYGFAQL    50
KRGAALANHE LGKLSDEKKN AIVYACDRIL NGELDNHFPL VIWQTGSGTQ 100
SNMNVNEVVS YVANEYLKKH GSKETIHPND DVNKSQSSND TFPTAMHVAL 150
FHEVETKLEP ALNHLRQTFK EKEDQYQSII KIGRTHLQDA TPIKLGQEIS 200
GWRYMLEKCE QLLSESKKHI LNLAIGGTAV GTGINAHPEF GHKVAKYISQ 250
NTGYAFVSSE NKFHALTSHD EIVQLHGTLK ALATDLMKIA NDIRWLASGP 300
RAGLAEISIP ENEPGSSIMP GKVNPTQCEM LTMVAVQVMG NDTTVGIASS 350
QGNFELNVFK PVIMHNTLQS IYLLADGMNT FNKNCAIGIQ PIEENINNYL 400
NQSLMLVTAL NPHIGYEKAA QIAKKAHKEG LTLKESAIES GYVTESQFEE 450
WIKPEDMVDP H 461
Length:461
Mass (Da):51,329
Last modified:March 1, 2003 - v1
Checksum:i478E748E9F13827A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE015929 Genomic DNA. Translation: AAO05131.1.
RefSeqiNP_765087.1. NC_004461.1.

Genome annotation databases

EnsemblBacteriaiAAO05131; AAO05131; SE_1532.
GeneIDi1056804.
KEGGisep:SE1532.
PATRICi19608864. VBIStaEpi113981_1497.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE015929 Genomic DNA. Translation: AAO05131.1 .
RefSeqi NP_765087.1. NC_004461.1.

3D structure databases

ProteinModelPortali Q8CNR1.
SMRi Q8CNR1. Positions 3-457.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 176280.SE1532.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAO05131 ; AAO05131 ; SE_1532 .
GeneIDi 1056804.
KEGGi sep:SE1532.
PATRICi 19608864. VBIStaEpi113981_1497.

Phylogenomic databases

eggNOGi COG0114.
KOi K01679.
OMAi LHPGLDI.
OrthoDBi EOG6V1M4M.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci SEPI176280:GCDG-1546-MONOMER.

Family and domain databases

Gene3Di 1.10.275.10. 1 hit.
HAMAPi MF_00743. FumaraseC.
InterProi IPR005677. Fum_hydII.
IPR024083. Fumarase/histidase_N.
IPR018951. Fumarase_C_C.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view ]
PANTHERi PTHR11444. PTHR11444. 1 hit.
Pfami PF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view ]
PRINTSi PR00149. FUMRATELYASE.
SUPFAMi SSF48557. SSF48557. 1 hit.
TIGRFAMsi TIGR00979. fumC_II. 1 hit.
PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genome-based analysis of virulence genes in a non-biofilm-forming Staphylococcus epidermidis strain (ATCC 12228)."
    Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.
    Mol. Microbiol. 49:1577-1593(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 12228.

Entry informationi

Entry nameiFUMC_STAES
AccessioniPrimary (citable) accession number: Q8CNR1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2003
Last modified: May 14, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

There are 2 substrate-binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors By similarity.

Keywords - Technical termi

Allosteric enzyme, Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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