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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Brucella suis (strain ATCC 23445 / NCTC 10510)
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 annotation

Keywords - Biological processi

Tricarboxylic acid cycleUniRule annotation

Enzyme and pathway databases

BioCyciBSUI470137:GJIC-2207-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 annotationImported
Ordered Locus Names:BSUIS_B0195Imported
OrganismiBrucella suis (strain ATCC 23445 / NCTC 10510)Imported
Taxonomic identifieri470137 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
Proteomesi
  • UP000008545 Componenti: Chromosome II

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

ProteinModelPortaliA9WXP7.
SMRiA9WXP7. Positions 5-460.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 342331Lyase_1InterPro annotationAdd
BLAST
Domaini408 – 46053FumaraseC_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.

A9WXP7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATRTETDT FGPIDVPADR YWGAQTQRSL QNFRIGGERM PLPLVHALGV
60 70 80 90 100
VKRAAAETNI ALGKLDPVLG QVIAVAASEV IEGKLDDHFP LVVWQTGSGT
110 120 130 140 150
QSNMNANEVI SNRAIELLGG EMGSKKPIHP NDHVNMSQSS NDSFPTAIHI
160 170 180 190 200
AMAVETVNRL YPALEHLTKA LKVKEEAFKD IIKIGRTHTQ DATPVTLGQE
210 220 230 240 250
FSGYRAALEY ARHRLEQSLA DVFLLAQGGT AVGTGLNAPV GFDKGFAEAV
260 270 280 290 300
SEITGLSFKT APNKFEALAS HGAVLNFHGS LNALAADLFK IANDIRFLGS
310 320 330 340 350
GPRSGLGELS LPENEPGSSI MPGKVNPTQA EAMTMVATQV FGNQTAVTVA
360 370 380 390 400
ASQGHFELNV FKPVIAYNVL QSIRLLSDTM VSFADHCVEG IEPNTARIKE
410 420 430 440 450
LLERSLMLVT ALAPAIGYDN AARIAKTAHK NGTTLREEAL ASGLVSEEDY
460
DRLVRAERMI APQ
Length:463
Mass (Da):49,654
Last modified:February 5, 2008 - v1
Checksum:i14CBDB121C29BAC2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000912 Genomic DNA. Translation: ABY39213.1.
RefSeqiWP_006199006.1. NC_010167.1.

Genome annotation databases

EnsemblBacteriaiABY39213; ABY39213; BSUIS_B0195.
KEGGibmt:BSUIS_B0195.
PATRICi17864756. VBIBruSui83806_0197.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000912 Genomic DNA. Translation: ABY39213.1.
RefSeqiWP_006199006.1. NC_010167.1.

3D structure databases

ProteinModelPortaliA9WXP7.
SMRiA9WXP7. Positions 5-460.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABY39213; ABY39213; BSUIS_B0195.
KEGGibmt:BSUIS_B0195.
PATRICi17864756. VBIBruSui83806_0197.

Phylogenomic databases

HOGENOMiHOG000061736.
KOiK01679.
OMAiFAYLKKA.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.
BioCyciBSUI470137:GJIC-2207-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 nameiA9WXP7_BRUSI
AccessioniPrimary (citable) accession number: A9WXP7
Entry historyi
Integrated into UniProtKB/TrEMBL: February 5, 2008
Last sequence update: February 5, 2008
Last modified: September 7, 2016
This is version 62 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.