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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Prochlorococcus marinus (strain MIT 9301)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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
Binding sitei101SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationSAAS annotationImported

Keywords - Biological processi

Tricarboxylic acid cycleUniRule annotation

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 annotationImported
Ordered Locus Names:P9301_16561Imported
OrganismiProchlorococcus marinus (strain MIT 9301)Imported
Taxonomic identifieri167546 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaSynechococcalesProchloraceaeProchlorococcus
Proteomesi
  • UP000001430 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi167546.P9301_16561.

Structurei

3D structure databases

ProteinModelPortaliA3PEV4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini13 – 343Lyase_1InterPro annotationAdd BLAST331
Domaini409 – 461FumaraseC_CInterPro annotationAdd BLAST53

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni130 – 133B siteUniRule annotation4
Regioni140 – 142Substrate bindingUniRule annotation3

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C9Q. Bacteria.
COG0114. LUCA.
HOGENOMiHOG000061736.
KOiK01679.
OMAiIGHHTAI.
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.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A3PEV4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKNFRIEKD SMGTIKVPIE ALWGAQTQRS IINFSIGEEL IPIELIYSLT
60 70 80 90 100
LIKKAASIAN FNLGLIDKRK KDLIVEACTE ILDGLHDSQF PLKVWQTGSG
110 120 130 140 150
TQTNMNVNEV ISNIAALKTN SELGSHQPLH PNDDVNKSQS TNDTFPAAIQ
160 170 180 190 200
ISVVNEIIKN LVPTIRELTK ILDNKSEQWK DLIKIGRTHF QDAVPLTFGQ
210 220 230 240 250
EISGWSEQLK DAENAIIISL NELYFLPLGG TAVGTGINCP KGFCEESIKS
260 270 280 290 300
ISDDTNLMFY KSKNNFSIMA SHDRLAQVMS QIKILAGALF KISNDIKILS
310 320 330 340 350
SGPRSGIYEL IIPQNEPGSS IMPGKVNPTQ CEALSMVCTQ IMGLEYAVSM
360 370 380 390 400
ANSSGTLQMN EYKPLIGFNI LTSLKLLKNA IENFRTKLVY GMEPNQKKMK
410 420 430 440 450
FNLDNSLMLI TAIVPKVGYE KAAEIANLAF KESLNLKEAT LKLGYLNEDE
460
FDDAMNINSM I
Length:461
Mass (Da):51,047
Last modified:April 3, 2007 - v1
Checksum:i70155F97F223D0E4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000576 Genomic DNA. Translation: ABO18279.1.
RefSeqiWP_011863576.1. NC_009091.1.

Genome annotation databases

EnsemblBacteriaiABO18279; ABO18279; P9301_16561.
KEGGipmg:P9301_16561.
PATRICi22996813. VBIProMar103344_1581.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000576 Genomic DNA. Translation: ABO18279.1.
RefSeqiWP_011863576.1. NC_009091.1.

3D structure databases

ProteinModelPortaliA3PEV4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi167546.P9301_16561.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABO18279; ABO18279; P9301_16561.
KEGGipmg:P9301_16561.
PATRICi22996813. VBIProMar103344_1581.

Phylogenomic databases

eggNOGiENOG4105C9Q. Bacteria.
COG0114. LUCA.
HOGENOMiHOG000061736.
KOiK01679.
OMAiIGHHTAI.
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.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiA3PEV4_PROM0
AccessioniPrimary (citable) accession number: A3PEV4
Entry historyi
Integrated into UniProtKB/TrEMBL: April 3, 2007
Last sequence update: April 3, 2007
Last modified: November 2, 2016
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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.UniRule annotation

Keywords - Technical termi

Complete proteomeImported

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.