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Protein

Fumarate hydratase class II 2

Gene

fumC2

Organism
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
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 1 (fumC1), Fumarate hydratase class II 2 (fumC2)
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 sitei188Proton donor/acceptorBy similarity1
Active sitei318By similarity1
Binding sitei319SubstrateUniRule annotation1
Sitei331Important 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 II 2UniRule annotation (EC:4.2.1.2UniRule annotation)
Short name:
Fumarase C 2UniRule annotation
Gene namesi
Name:fumC2UniRule annotation
Ordered Locus Names:bll0286
OrganismiBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Taxonomic identifieri224911 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium
Proteomesi
  • UP000002526 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_00001612601 – 478Fumarate hydratase class II 2Add BLAST478

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi224911.bll0286.

Structurei

3D structure databases

ProteinModelPortaliQ89XM2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni98 – 100Substrate bindingUniRule annotation3
Regioni129 – 132B siteUniRule annotation4
Regioni139 – 141Substrate bindingUniRule annotation3
Regioni187 – 188Substrate bindingUniRule annotation2
Regioni324 – 326Substrate bindingUniRule annotation3

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C9Q. Bacteria.
COG0114. LUCA.
HOGENOMiHOG000061736.
InParanoidiQ89XM2.
KOiK01679.
OMAiYQNAAHI.
OrthoDBiPOG091H01XG.
PhylomeDBiQ89XM2.

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.

Q89XM2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNDLRKETDS LGEVNVPADK LWGAQTQRSL EHFSIGRDLM PREMIQSYAI
60 70 80 90 100
LKKAAANANY AGGRLDGKIH KLIVHTCDEI LAGQHHDMFP LHVWMTGSGT
110 120 130 140 150
QFNMNVNEVI SNRCCQLAGT ALGSKLPVHP NDHVNMSQSS NDSFPSAMYI
160 170 180 190 200
AAAMNVTQRL VPAVEALHDA IAAKSNQWDD IVKIGRTHMQ DATPLTLGQE
210 220 230 240 250
WSGYAAMLAD GLARIDDALK GVFRLALGGT AVGTGINAAP GFAEAVAAEI
260 270 280 290 300
ARLTGLPFVS APNKFAVQGA HDALVQLSGT LRTLAGSLYK IANDIRLLSC
310 320 330 340 350
GPRAGFAELR IPENEPGSSI MPGKVNPTQA EALTMIAVQV MANDVAVGFG
360 370 380 390 400
GAGGYLEMNV YKPLIIHNIA QSVTILTDGC TNFRTFLVEG TEPNRKKIKE
410 420 430 440 450
YVERSLMLVT ALAPVIGYDK ASRIAHYAMD NDLTLKSAAL KLGFVTEPEF
460 470
DRIVDPAKMV KPYVAEIKVP LAIGAKTG
Length:478
Mass (Da):51,299
Last modified:December 15, 2003 - v2
Checksum:iA33EC007B6A88B44
GO

Sequence cautioni

The sequence BAC45551 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000040 Genomic DNA. Translation: BAC45551.1. Different initiation.
RefSeqiNP_766926.2. NC_004463.1.
WP_011083118.1. NZ_CP011360.1.

Genome annotation databases

EnsemblBacteriaiBAC45551; BAC45551; BAC45551.
GeneIDi1048934.
KEGGibja:bll0286.
PATRICi21184003. VBIBraJap65052_0281.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000040 Genomic DNA. Translation: BAC45551.1. Different initiation.
RefSeqiNP_766926.2. NC_004463.1.
WP_011083118.1. NZ_CP011360.1.

3D structure databases

ProteinModelPortaliQ89XM2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224911.bll0286.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC45551; BAC45551; BAC45551.
GeneIDi1048934.
KEGGibja:bll0286.
PATRICi21184003. VBIBraJap65052_0281.

Phylogenomic databases

eggNOGiENOG4105C9Q. Bacteria.
COG0114. LUCA.
HOGENOMiHOG000061736.
InParanoidiQ89XM2.
KOiK01679.
OMAiYQNAAHI.
OrthoDBiPOG091H01XG.
PhylomeDBiQ89XM2.

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 nameiFUMC2_BRADU
AccessioniPrimary (citable) accession number: Q89XM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: November 2, 2016
This is version 88 of the entry and version 2 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.