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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Rhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei100 – 1001SubstrateUniRule annotation

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

BioCyciRSPH349101:GHC8-828-MONOMER.
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:Rsph17029_0812Imported
OrganismiRhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9)Imported
Taxonomic identifieri349101 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter
Proteomesi
  • UP000002606 Componenti: Chromosome 1

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA3PHV7.
SMRiA3PHV7. Positions 5-460.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 342331Lyase_1InterPro annotationAdd
BLAST
Domaini408 – 46154FumaraseC_CInterPro annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni129 – 1324B siteUniRule annotation
Regioni139 – 1413Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000061736.
KOiK01679.
OMAiFAYLKKA.

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.

A3PHV7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTATRTETDS FGPLEVPADK YWGAQTQRSI QNFPIGWEKQ PVAIVRALGV
60 70 80 90 100
IKKACALVNV AQGDMPEELA QAIAAAATEV IEGRFDDNFP LVVWQTGSGT
110 120 130 140 150
QSNMNANEVI SNRAIEMLGG TMGSKKPVHP NDHVNMGQSS NDTFPTAMHV
160 170 180 190 200
AIGMMARDVL LPGLEKLHAA LVAKSEEFKD IIKIGRTHTQ DATPLTLGQE
210 220 230 240 250
FSGYAKQVEK GIARVKACLP DIYELAQGGT AVGTGLNTRQ GWDSRVAAKI
260 270 280 290 300
AEITGLPFVT AENKFEALAA HDAMVMFSGA LKTVAASLFK IANDMRLLGS
310 320 330 340 350
GPRSGLGELI LPENEPGSSI MPGKVNPTQA EALTMVCAHV MGNDAAIGFA
360 370 380 390 400
GSQGHFELNV YNPMMSYNVL QSMQLLGDAA GSFTDNMVVG TQANVARIDK
410 420 430 440 450
LMKESLMLVT ALAPTIGYDN ATKVAKTAHR NGTTLREEAI ALGLVDAETF
460
DRVVRPEDMI GPKG
Length:464
Mass (Da):49,425
Last modified:April 3, 2007 - v1
Checksum:iFD5CE8484EB8EBAF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000577 Genomic DNA. Translation: ABN75923.1.
RefSeqiWP_011840618.1. NC_009049.1.

Genome annotation databases

EnsemblBacteriaiABN75923; ABN75923; Rsph17029_0812.
KEGGirsh:Rsph17029_0812.
PATRICi23169298. VBIRhoSph114483_0962.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000577 Genomic DNA. Translation: ABN75923.1.
RefSeqiWP_011840618.1. NC_009049.1.

3D structure databases

ProteinModelPortaliA3PHV7.
SMRiA3PHV7. Positions 5-460.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABN75923; ABN75923; Rsph17029_0812.
KEGGirsh:Rsph17029_0812.
PATRICi23169298. VBIRhoSph114483_0962.

Phylogenomic databases

HOGENOMiHOG000061736.
KOiK01679.
OMAiFAYLKKA.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.
BioCyciRSPH349101:GHC8-828-MONOMER.

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 nameiA3PHV7_RHOS1
AccessioniPrimary (citable) accession number: A3PHV7
Entry historyi
Integrated into UniProtKB/TrEMBL: April 3, 2007
Last sequence update: April 3, 2007
Last modified: September 7, 2016
This is version 70 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.