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Q6G884

- FUMC_STAAS

UniProt

Q6G884 - FUMC_STAAS

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Protein
Fumarate hydratase class II
Gene
fumC, citG, SAS1772
Organism
Staphylococcus aureus (strain MSSA476)
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
Complete GO annotation...

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

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
Synonyms:citG
Ordered Locus Names:SAS1772
OrganismiStaphylococcus aureus (strain MSSA476)
Taxonomic identifieri282459 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000002201: 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 annotation
PRO_0000161315Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi282459.SAS1772.

Structurei

3D structure databases

ProteinModelPortaliQ6G884.
SMRiQ6G884. Positions 3-458.

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.
HOGENOMiHOG000061736.
KOiK01679.
OMAiMESFNIH.
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.

Q6G884-1 [UniParc]FASTAAdd to Basket

« Hide

MSVRIEHDTF GEIEVPADKY WGAQTERSKR NFPVGKERMP IEVVYGFAQL    50
KRAAALANFD LGKLSEAKKD AIVYACDQIL SGELDEHFPL VVWQTGSGTQ 100
SNMNVNEVVS YVANMYLKDH QIDESIHPND DVNKSQSSND TFPTAMHVAL 150
YQEVETKLEP ALKLLRNTLK EKEDKFDSII KIGRTHLQDA TPIKLGQEIS 200
GWRYMLDRCE IMLSESKKHI LNLAIGGTAV GTGINAHPEF GDKVAHYISE 250
NTGYPFVSSE NKFHALTAHD EVVQLHGTLK ALAGDLMKIA NDVRWLASGP 300
RAGLAEISIP ENEPGSSIMP GKVNPTQCEM LTMVAVQVMG NDTVVGFASS 350
QGNFELNVYK PVIMHNTLQS IYLLADGMET FNNNCAVGIE PIEENIDNYL 400
NQSLMLVTAL NPHIGYEKAA QIAKKAHKEG LTLKESAIQT GYVTEEQFEA 450
WIKPEDMVDP H 461
Length:461
Mass (Da):51,146
Last modified:July 19, 2004 - v1
Checksum:i74BBF16CB7C3A638
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX571857 Genomic DNA. Translation: CAG43577.1.
RefSeqiYP_043889.1. NC_002953.3.

Genome annotation databases

GeneIDi2863681.
KEGGisas:SAS1772.
PATRICi19553067. VBIStaAur96780_1844.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX571857 Genomic DNA. Translation: CAG43577.1 .
RefSeqi YP_043889.1. NC_002953.3.

3D structure databases

ProteinModelPortali Q6G884.
SMRi Q6G884. Positions 3-458.
ModBasei Search...

Protein-protein interaction databases

STRINGi 282459.SAS1772.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2863681.
KEGGi sas:SAS1772.
PATRICi 19553067. VBIStaAur96780_1844.

Phylogenomic databases

eggNOGi COG0114.
HOGENOMi HOG000061736.
KOi K01679.
OMAi MESFNIH.
OrthoDBi EOG6V1M4M.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MSSA476.

Entry informationi

Entry nameiFUMC_STAAS
AccessioniPrimary (citable) accession number: Q6G884
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: July 19, 2004
Last modified: May 14, 2014
This is version 70 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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