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Q8X769

- FUMC_ECO57

UniProt

Q8X769 - FUMC_ECO57

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Protein
Fumarate hydratase class II
Gene
fumC, Z2614, ECs2317
Organism
Escherichia coli O157:H7
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 sitei188 – 1881Proton donor/acceptor By similarity
Active sitei318 – 3181 By similarity
Binding sitei319 – 3191Substrate By similarity
Sitei331 – 3311Important 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

BioCyciECOL386585:GJFA-2291-MONOMER.
ECOO157:FUMC-MONOMER.
SABIO-RKQ8X769.
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:Z2614, ECs2317
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000558: Chromosome, UP000002519: 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 – 467467Fumarate hydratase class IIUniRule annotation
PRO_0000161276Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi155864.Z2614.

Structurei

3D structure databases

ProteinModelPortaliQ8X769.
SMRiQ8X769. Positions 4-459.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 1003Substrate binding By similarity
Regioni129 – 1324B site By similarity
Regioni139 – 1413Substrate binding By similarity
Regioni187 – 1882Substrate binding By similarity
Regioni324 – 3263Substrate 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.

Q8X769-1 [UniParc]FASTAAdd to Basket

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MNTVRSEKDS MGAIDVPADK LWGAQTQRSL EHFRISTEKM PTSLIHALAL    50
TKRAAAKVNE DLGLLSEEKA SAIRQAADEV LAGQHDDEFP LAIWQTGSGT 100
QSNMNMNEVL ANRASELLGG VRGMERKVHP NDDVNKSQSS NDVFPTAMHV 150
AALLALRKQL IPQLKTLTQT LSEKSRAFAD IVKIGRTHLQ DATPLTLGQE 200
ISGWVAMLEH NLKHIEYSLP HVAELALGGT AVGTGLNTHP EYARRVADEL 250
AVITCAPFVT APNKFEALAT CDALVQAHGA LKGLAASLMK IANDVRWLAS 300
GPRCGIGEIS IPENEPGSSI MPGKVNPTQC EALTMLCCQV MGNDVAINMG 350
GASGNFELNV FRPMVIHNFL QSVRLLADGM ESFNKHCAVG IEPNRERINQ 400
LLNESLMLVT ALNTHIGYDK AAEIAKKAHK EGLTLKAAAL ALGYLSEAEF 450
DSWVRPEQMV GSMKAGR 467
Length:467
Mass (Da):50,462
Last modified:March 1, 2002 - v1
Checksum:i6A4F47D2FC0E343F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005174 Genomic DNA. Translation: AAG56598.1.
BA000007 Genomic DNA. Translation: BAB35740.1.
PIRiB85767.
E90918.
RefSeqiNP_288046.1. NC_002655.2.
NP_310344.1. NC_002695.1.

Genome annotation databases

EnsemblBacteriaiAAG56598; AAG56598; Z2614.
BAB35740; BAB35740; BAB35740.
GeneIDi913708.
961561.
KEGGiece:Z2614.
ecs:ECs2317.
PATRICi18353962. VBIEscCol44059_2194.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005174 Genomic DNA. Translation: AAG56598.1 .
BA000007 Genomic DNA. Translation: BAB35740.1 .
PIRi B85767.
E90918.
RefSeqi NP_288046.1. NC_002655.2.
NP_310344.1. NC_002695.1.

3D structure databases

ProteinModelPortali Q8X769.
SMRi Q8X769. Positions 4-459.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 155864.Z2614.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG56598 ; AAG56598 ; Z2614 .
BAB35740 ; BAB35740 ; BAB35740 .
GeneIDi 913708.
961561.
KEGGi ece:Z2614.
ecs:ECs2317.
PATRICi 18353962. VBIEscCol44059_2194.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci ECOL386585:GJFA-2291-MONOMER.
ECOO157:FUMC-MONOMER.
SABIO-RK Q8X769.

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: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry nameiFUMC_ECO57
AccessioniPrimary (citable) accession number: Q8X769
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2002
Last modified: May 14, 2014
This is version 82 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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