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O69294

- FUMC_CAMJE

UniProt

O69294 - FUMC_CAMJE

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Protein
Fumarate hydratase class II
Gene
fumC, Cj1364c
Organism
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
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 sitei187 – 1871Proton donor/acceptor By similarity
Active sitei317 – 3171 By similarity
Binding sitei318 – 3181Substrate By similarity
Sitei330 – 3301Important 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

BioCyciCJEJ192222:GJTS-1337-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:Cj1364c
OrganismiCampylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Taxonomic identifieri192222 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
ProteomesiUP000000799: 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 – 463463Fumarate hydratase class IIUniRule annotation
PRO_0000161263Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

IntActiO69294. 10 interactions.
STRINGi192222.Cj1364c.

Structurei

3D structure databases

ProteinModelPortaliO69294.
SMRiO69294. Positions 4-459.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 993Substrate binding By similarity
Regioni128 – 1314B site By similarity
Regioni138 – 1403Substrate binding By similarity
Regioni186 – 1872Substrate binding By similarity
Regioni323 – 3253Substrate 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.

O69294-1 [UniParc]FASTAAdd to Basket

« Hide

MEYRVEHDTM GEVKVPNDKY WGAQTERSFE NFKIGCEKMP KVLIYAFANL    50
KKSLALVNNK LGKLDDAKKN AIVQACDEII AGKFDDNFPL AIWQTGSGTQ 100
SNMNMNEVIA NRATEIMGGD FRKEKLVHPN DHVNMSQSSN DTFPTAMSIV 150
AVEQVEKKLI PALDELIATF EKKVKEFDGI IKIGRTHLQD ATPLTLAQEF 200
SGYLSMLLHS KEQIIASLPT LRELAIGGTA VGTGLNAHPE LSQKVSEELT 250
QLIGTKFISS PNKFHALTSH DAINFTHGAM KGLAANLMKI ANDIRWLASG 300
PRCGLGELII PENEPGSSIM PGKVNPTQCE AVTMVAVQVM GNDVAIGFAA 350
SQGNFELNVF KPVIIYNFLQ SLDLLADSMH SFNIHCAVGI EPNRAKIDHN 400
LHNSLMLVTA LNPHIGYENA AKVAKNAHKK GISLKESTME LGLVSEEDFN 450
KFVDPTKMIG PKA 463
Length:463
Mass (Da):50,710
Last modified:August 1, 1998 - v1
Checksum:iE281B37B5791FFC0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y16882 Genomic DNA. Translation: CAA76499.1.
AL111168 Genomic DNA. Translation: CAL35476.1.
PIRiA81281.
RefSeqiWP_002857888.1. NC_002163.1.
YP_002344752.1. NC_002163.1.

Genome annotation databases

EnsemblBacteriaiCAL35476; CAL35476; Cj1364c.
GeneIDi905657.
KEGGicje:Cj1364c.
PATRICi20059693. VBICamJej33762_1345.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y16882 Genomic DNA. Translation: CAA76499.1 .
AL111168 Genomic DNA. Translation: CAL35476.1 .
PIRi A81281.
RefSeqi WP_002857888.1. NC_002163.1.
YP_002344752.1. NC_002163.1.

3D structure databases

ProteinModelPortali O69294.
SMRi O69294. Positions 4-459.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O69294. 10 interactions.
STRINGi 192222.Cj1364c.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAL35476 ; CAL35476 ; Cj1364c .
GeneIDi 905657.
KEGGi cje:Cj1364c.
PATRICi 20059693. VBICamJej33762_1345.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci CJEJ192222:GJTS-1337-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

« Hide 'large scale' publications
  1. Griffiths P.L., Connerton I.F.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: NCTC 11168.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NCTC 11168.

Entry informationi

Entry nameiFUMC_CAMJE
AccessioniPrimary (citable) accession number: O69294
Secondary accession number(s): Q0P8P5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: September 3, 2014
This is version 100 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, Reference 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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