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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Staphylococcus epidermidis (strain ATCC 12228)
Status
Reviewed-Annotation score: 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

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei186 – 1861Proton donor/acceptorBy similarity
Active sitei316 – 3161By similarity
Binding sitei317 – 3171SubstrateUniRule annotation
Sitei329 – 3291Important for catalytic activityBy 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 IIUniRule annotation (EC:4.2.1.2UniRule annotation)
Short name:
Fumarase CUniRule annotation
Gene namesi
Name:fumCUniRule annotation
Ordered Locus Names:SE_1532
OrganismiStaphylococcus epidermidis (strain ATCC 12228)
Taxonomic identifieri176280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000001411 Componenti: Chromosome

Subcellular locationi

Cytoplasm 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 IIPRO_0000161317Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi176280.SE1532.

Structurei

3D structure databases

SMRiQ8CNR1. Positions 3-457.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 993Substrate bindingUniRule annotation
Regioni127 – 1304B siteUniRule annotation
Regioni137 – 1393Substrate bindingUniRule annotation
Regioni185 – 1862Substrate bindingUniRule annotation
Regioni322 – 3243Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0114.
KOiK01679.
OMAiNTPKGYD.
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

« Hide

        10         20         30         40         50
MSVRIEHDTF GEIEVPEDKY WGAQTERSKR NFPVGKEHMP IQVIYGFAQL
60 70 80 90 100
KRGAALANHE LGKLSDEKKN AIVYACDRIL NGELDNHFPL VIWQTGSGTQ
110 120 130 140 150
SNMNVNEVVS YVANEYLKKH GSKETIHPND DVNKSQSSND TFPTAMHVAL
160 170 180 190 200
FHEVETKLEP ALNHLRQTFK EKEDQYQSII KIGRTHLQDA TPIKLGQEIS
210 220 230 240 250
GWRYMLEKCE QLLSESKKHI LNLAIGGTAV GTGINAHPEF GHKVAKYISQ
260 270 280 290 300
NTGYAFVSSE NKFHALTSHD EIVQLHGTLK ALATDLMKIA NDIRWLASGP
310 320 330 340 350
RAGLAEISIP ENEPGSSIMP GKVNPTQCEM LTMVAVQVMG NDTTVGIASS
360 370 380 390 400
QGNFELNVFK PVIMHNTLQS IYLLADGMNT FNKNCAIGIQ PIEENINNYL
410 420 430 440 450
NQSLMLVTAL NPHIGYEKAA QIAKKAHKEG LTLKESAIES GYVTESQFEE
460
WIKPEDMVDP H
Length:461
Mass (Da):51,329
Last modified:February 28, 2003 - v1
Checksum:i478E748E9F13827A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AE015929 Genomic DNA. Translation: AAO05131.1.
RefSeqiNP_765087.1. NC_004461.1.

3D structure databases

SMRiQ8CNR1. Positions 3-457.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi176280.SE1532.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiCOG0114.
KOiK01679.
OMAiNTPKGYD.
OrthoDBiEOG6V1M4M.

Enzyme and pathway databases

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

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]
ProtoNetiSearch...

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(2002) [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 14, 2003
Last sequence update: February 28, 2003
Last modified: March 31, 2015
This is version 84 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).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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.