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Q8YB50

- FUMC_BRUME

UniProt

Q8YB50 - FUMC_BRUME

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Protein

Fumarate hydratase class II

Gene
fumC, BMEII1051
Organism
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
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.UniRule annotation

Catalytic activityi

(S)-malate = fumarate + H2O.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei188 – 1881Proton donor/acceptor By similarity
Active sitei318 – 3181 By similarity
Binding sitei319 – 3191Substrate By similarity
Sitei331 – 3311Important for catalytic activity By 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

UniPathwayiUPA00223; UER01007.

Names & Taxonomyi

Protein namesi
Recommended name:
Fumarate hydratase class II (EC:4.2.1.2)
Short name:
Fumarase C
Gene namesi
Name:fumC
Ordered Locus Names:BMEII1051
OrganismiBrucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Taxonomic identifieri224914 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
ProteomesiUP000000419: Chromosome II

Subcellular locationi

Cytoplasm By similarity 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 – 463463Fumarate hydratase class IIUniRule annotationPRO_0000161261Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

IntActiQ8YB50. 1 interaction.
STRINGi224914.BMEII1051.

Structurei

3D structure databases

ProteinModelPortaliQ8YB50.
SMRiQ8YB50. Positions 5-463.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 1003Substrate binding By similarity
Regioni129 – 1324B site By similarity
Regioni139 – 1413Substrate binding By similarity
Regioni187 – 1882Substrate binding By similarity
Regioni324 – 3263Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000061736.
KOiK01679.
OMAiMESFNIH.
OrthoDBiEOG6V1M4M.

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.

Q8YB50-1 [UniParc]FASTAAdd to Basket

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MAATRTETDT FGPIDVPADR YWGAQTQRSL QNFRIGGERM PLPLVHALGV    50
VKRAAAETNI ALGKLDPVLG QVIAVAASEV IEGKLDDHFP LVVWQTGSGT 100
QSNMNANEVI SNRAIELLGG EMGSKKPIHP NDHVNMSQSS NDSFPTAIHI 150
ATAVETVNRL YPALEHLTKA LKVKEEAFKD IIKIGRTHTQ DATPVTLGQE 200
FSGYRAALEY ARHRLEQSLA DVFLLAQGGT AVGTGLNAPV GFDKGFAEAV 250
SEITGLSFKT APNKFEALAS HGAVLNFHGS LNALAADLFK IANDIRFLGS 300
GPRSGLGELS LPENEPGSSI MPGKVNPTQA EAMTMVATQV FGNQTAVTVA 350
ASQGHFELNV FKPVIAYNVL QSIRLLSDTM VSFADHCVEG IEPNTARIKE 400
LLERSLMLVT ALAPAIGYDN AARIAKTAHK NGTTLREEAL ASGLVSEEDY 450
DRLVRAERMI APQ 463
Length:463
Mass (Da):49,624
Last modified:December 15, 2003 - v2
Checksum:iC2F6DD271F19B4F8
GO

Sequence cautioni

The sequence AAL54293.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE008918 Genomic DNA. Translation: AAL54293.1. Different initiation.
PIRiAB3641.
RefSeqiNP_542029.2. NC_003318.1.

Genome annotation databases

EnsemblBacteriaiAAL54293; AAL54293; BMEII1051.
GeneIDi1198823.
KEGGibme:BMEII1051.
PATRICi17856895. VBIBruMel92729_3406.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE008918 Genomic DNA. Translation: AAL54293.1 . Different initiation.
PIRi AB3641.
RefSeqi NP_542029.2. NC_003318.1.

3D structure databases

ProteinModelPortali Q8YB50.
SMRi Q8YB50. Positions 5-463.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8YB50. 1 interaction.
STRINGi 224914.BMEII1051.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL54293 ; AAL54293 ; BMEII1051 .
GeneIDi 1198823.
KEGGi bme:BMEII1051.
PATRICi 17856895. VBIBruMel92729_3406.

Phylogenomic databases

HOGENOMi HOG000061736.
KOi K01679.
OMAi MESFNIH.
OrthoDBi EOG6V1M4M.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .

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: 16M / ATCC 23456 / NCTC 10094.

Entry informationi

Entry nameiFUMC_BRUME
AccessioniPrimary (citable) accession number: Q8YB50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: May 14, 2014
This is version 83 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.

Keywords - Technical termi

Allosteric enzyme, Complete proteome

Documents

  1. Brucella melitensis
    Brucella melitensis (strain 16M): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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