Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fumarate hydratase class II

Gene

fumC

Organism
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
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: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes (S)-malate from fumarate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Fumarate hydratase class II (fumC)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-malate from fumarate, the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei189Proton donor/acceptorBy similarity1
Active sitei319By similarity1
Binding sitei320SubstrateUniRule annotation1
Sitei332Important for catalytic activityBy similarity1

GO - Molecular functioni

GO - Biological processi

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 IIUniRule annotation (EC:4.2.1.2UniRule annotation)
Short name:
Fumarase CUniRule annotation
Gene namesi
Name:fumCUniRule annotation
Ordered Locus Names:CV_1120
OrganismiChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Taxonomic identifieri243365 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesChromobacteriaceaeChromobacterium
Proteomesi
  • UP000001424 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001612701 – 461Fumarate hydratase class IIAdd BLAST461

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi243365.CV_1120.

Structurei

3D structure databases

ProteinModelPortaliQ7NZ02.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni99 – 101Substrate bindingUniRule annotation3
Regioni130 – 133B siteUniRule annotation4
Regioni140 – 142Substrate bindingUniRule annotation3
Regioni188 – 189Substrate bindingUniRule annotation2
Regioni325 – 327Substrate bindingUniRule annotation3

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C9Q. Bacteria.
COG0114. LUCA.
HOGENOMiHOG000061736.
KOiK01679.
OMAiFAYLKKA.
OrthoDBiPOG091H01XG.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC. 1 hit.
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.

Q7NZ02-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKTVRSETD TFGPIDVPAA ALWGAQTQRS LAHFRISSEK MPPELILALA
60 70 80 90 100
RVKRACAEAN RGLGKLDDAK AAAIAGAADE VLAGRHDGEF PLSVWQTGSG
110 120 130 140 150
TQSNMNMNEV LANRASELLG GRRGPGRLVH PNDDVNLGQS SNDIFPTAMH
160 170 180 190 200
VAAATQVKER LLPSLDLLRH ALESKAEAFA DVVKIGRTHL QDATPLTLGQ
210 220 230 240 250
EISGWAAQLA LSEQAVRAAL PMLCQLAVGG TAVGTGLNTD PSFGAAVAAR
260 270 280 290 300
LAEQSGLPFE SAGNKFAALA GHEPLVFAHG ALKTLAAALM KIANDIRWLA
310 320 330 340 350
SGPRSGLGEL SLPENEPGSS IMPGKVNPTQ CEAMTMLCCQ VLGNDAALAI
360 370 380 390 400
GAASGNFELN VFKPLIAHNF LQSARLLADG MDSLREHCVD GMEANRARIA
410 420 430 440 450
ELMARSLMLV TALNPHIGYD KAAAIAKHAH RHGTTLREAA LALGHLSAEQ
460
FDAWVRPEDM V
Length:461
Mass (Da):48,610
Last modified:December 15, 2003 - v1
Checksum:i49B09E5DD6B0B90F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016825 Genomic DNA. Translation: AAQ58795.1.
RefSeqiWP_011134675.1. NC_005085.1.

Genome annotation databases

EnsemblBacteriaiAAQ58795; AAQ58795; CV_1120.
GeneIDi24948156.
KEGGicvi:CV_1120.
PATRICi21437054. VBIChrVio67196_1109.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016825 Genomic DNA. Translation: AAQ58795.1.
RefSeqiWP_011134675.1. NC_005085.1.

3D structure databases

ProteinModelPortaliQ7NZ02.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243365.CV_1120.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAQ58795; AAQ58795; CV_1120.
GeneIDi24948156.
KEGGicvi:CV_1120.
PATRICi21437054. VBIChrVio67196_1109.

Phylogenomic databases

eggNOGiENOG4105C9Q. Bacteria.
COG0114. LUCA.
HOGENOMiHOG000061736.
KOiK01679.
OMAiFAYLKKA.
OrthoDBiPOG091H01XG.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC. 1 hit.
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...

Entry informationi

Entry nameiFUMC_CHRVO
AccessioniPrimary (citable) accession number: Q7NZ02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: November 2, 2016
This is version 90 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.