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P64172

- FUMC_STAAM

UniProt

P64172 - FUMC_STAAM

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Protein

Fumarate hydratase class II

Gene
fumC, citG, SAV1851
Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

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

BioCyciSAUR158878:GJJ5-1875-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
Synonyms:citG
Ordered Locus Names:SAV1851
OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)
Taxonomic identifieri158878 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000002481: 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_0000161312Add
BLAST

Proteomic databases

PRIDEiP64172.

2D gel databases

World-2DPAGE0002:P64172.

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi158878.SAV1851.

Structurei

3D structure databases

ProteinModelPortaliP64172.
SMRiP64172. 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.
HOGENOMiHOG000061736.
KOiK01679.
OMAiMESFNIH.
OrthoDBiEOG6V1M4M.
PhylomeDBiP64172.

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.

P64172-1 [UniParc]FASTAAdd to Basket

« Hide

MSVRIEHDTF GEIEVPADKY WGAQTERSKR NFPVGKERMP IEVVYGFAQL    50
KRAAALANFD LGKLSEAKKD AIVYACDQIL SGELDEHFPL VVWQTGSGTQ 100
SNMNVNEVVS YVANMYLKDH QIDESIHPND DVNESQSSND TFPTAMHVAL 150
YQEVETKLEP ALKLLRNTLK EKEDKFESII 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):51,161
Last modified:October 11, 2004 - v1
Checksum:i5FB7439BBE7A559E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000017 Genomic DNA. Translation: BAB58013.1.
RefSeqiNP_372375.1. NC_002758.2.

Genome annotation databases

EnsemblBacteriaiBAB58013; BAB58013; SAV1851.
GeneIDi1121833.
KEGGisav:SAV1851.
PATRICi19564486. VBIStaAur52173_1913.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000017 Genomic DNA. Translation: BAB58013.1 .
RefSeqi NP_372375.1. NC_002758.2.

3D structure databases

ProteinModelPortali P64172.
SMRi P64172. Positions 3-457.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 158878.SAV1851.

2D gel databases

World-2DPAGE 0002:P64172.

Proteomic databases

PRIDEi P64172.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB58013 ; BAB58013 ; SAV1851 .
GeneIDi 1121833.
KEGGi sav:SAV1851.
PATRICi 19564486. VBIStaAur52173_1913.

Phylogenomic databases

eggNOGi COG0114.
HOGENOMi HOG000061736.
KOi K01679.
OMAi MESFNIH.
OrthoDBi EOG6V1M4M.
PhylomeDBi P64172.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci SAUR158878:GJJ5-1875-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Mu50 / ATCC 700699.

Entry informationi

Entry nameiFUMC_STAAM
AccessioniPrimary (citable) accession number: P64172
Secondary accession number(s): Q99T27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: July 9, 2014
This is version 68 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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