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Q89XM2

- FUMC2_BRADU

UniProt

Q89XM2 - FUMC2_BRADU

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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: 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei188 – 1881Proton donor/acceptorBy similarity
Active sitei318 – 3181By similarity
Binding sitei319 – 3191SubstrateUniRule annotation
Sitei331 – 3311Important for catalytic activityBy similarity

GO - Molecular functioni

  1. fumarate hydratase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. fumarate metabolic process Source: InterPro
  2. tricarboxylic acid cycle Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciBJAP224911:GJEJ-287-MONOMER.
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
ProteomesiUP000002526: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. tricarboxylic acid cycle enzyme complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 478478Fumarate hydratase class II 2PRO_0000161260Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi224911.bll0286.

Structurei

3D structure databases

ProteinModelPortaliQ89XM2.
SMRiQ89XM2. Positions 4-459.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 1003Substrate bindingUniRule annotation
Regioni129 – 1324B siteUniRule annotation
Regioni139 – 1413Substrate bindingUniRule annotation
Regioni187 – 1882Substrate bindingUniRule annotation
Regioni324 – 3263Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
InParanoidiQ89XM2.
KOiK01679.
OrthoDBiEOG6V1M4M.
PhylomeDBiQ89XM2.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00743. FumaraseC.
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 [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 BAC45551.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000040 Genomic DNA. Translation: BAC45551.1. Different initiation.
RefSeqiNP_766926.2. NC_004463.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000040 Genomic DNA. Translation: BAC45551.1 . Different initiation.
RefSeqi NP_766926.2. NC_004463.1.

3D structure databases

ProteinModelPortali Q89XM2.
SMRi Q89XM2. Positions 4-459.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224911.bll0286.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC45551 ; BAC45551 ; BAC45551 .
GeneIDi 1048934.
KEGGi bja:bll0286.
PATRICi 21184003. VBIBraJap65052_0281.

Phylogenomic databases

eggNOGi COG0114.
HOGENOMi HOG000061736.
InParanoidi Q89XM2.
KOi K01679.
OrthoDBi EOG6V1M4M.
PhylomeDBi Q89XM2.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci BJAP224911:GJEJ-287-MONOMER.

Family and domain databases

Gene3Di 1.10.275.10. 1 hit.
HAMAPi MF_00743. FumaraseC.
InterProi IPR005677. 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 ]
PANTHERi PTHR11444. PTHR11444. 1 hit.
Pfami PF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view ]
PRINTSi PR00149. FUMRATELYASE.
SUPFAMi SSF48557. SSF48557. 1 hit.
TIGRFAMsi TIGR00979. fumC_II. 1 hit.
PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110.

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: October 29, 2014
This is version 79 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

External Data

Dasty 3