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Q7VR50

- FUMC_BLOFL

UniProt

Q7VR50 - FUMC_BLOFL

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Protein

Fumarate hydratase class II

Gene
fumC, Bfl373
Organism
Blochmannia floridanus
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 sitei172 – 1721Proton donor/acceptor By similarity
Active sitei302 – 3021 By similarity
Binding sitei303 – 3031Substrate By similarity
Sitei315 – 3151Important 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

BioCyciBFLO203907:GHF7-373-MONOMER.
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:Bfl373
OrganismiBlochmannia floridanus
Taxonomic identifieri203907 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeant endosymbiontsCandidatus Blochmannia
ProteomesiUP000002192: Chromosome

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 – 448448Fumarate hydratase class IIUniRule annotationPRO_0000161264Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi203907.Bfl373.

Structurei

3D structure databases

ProteinModelPortaliQ7VR50.
SMRiQ7VR50. Positions 4-444.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni83 – 853Substrate binding By similarity
Regioni113 – 1164B site By similarity
Regioni123 – 1253Substrate binding By similarity
Regioni171 – 1722Substrate binding By similarity
Regioni308 – 3103Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0114.
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.

Q7VR50-1 [UniParc]FASTAAdd to Basket

« Hide

MICNRLWGDQ TESSLKFFNI STEKMPWELI KALAQIKRVS AQVNYDLKLL    50
DYERSQAIIA AVDEILSGNH KNEFPLSVWQ TGSGTQSNMN MNEVLANRAN 100
ELLRKNQINI VVHPNDHVNK SQSSNDVFPS AMHIAAVVNL KTKLIPVIKL 150
LQKTFLKKSI EFRNIIKIGR THLQDAIPLT LGQEISGWDF MLKNNTNHIQ 200
STILDLSALA LGGTAVGTGF SAHVEYAERV VLGLSKLIHH SFFSAPNKFE 250
SLSTCDAIVY SHGTLKGLAI SMMKIANDIR LLSSGPQCGL GELIIPANEP 300
GSSIMPGKVN PTQCESMTMS CCQVMGNDLS ISLGGSSGQL QLNTYRPLII 350
YNFLQSIRLL TDSIKNFHDY CIVGIRPKFK RIEKLLNKSL MLVTALSSHI 400
GYDKSAQIAQ TAYLNGITLK AASIQSGYVT EKQFDDWVCP ENMIYPDM 448
Length:448
Mass (Da):49,649
Last modified:October 1, 2003 - v1
Checksum:iCDEC7863B7D10F2D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX248583 Genomic DNA. Translation: CAD83439.1.
RefSeqiNP_878664.1. NC_005061.1.
WP_011126647.1. NC_005061.1.

Genome annotation databases

EnsemblBacteriaiCAD83439; CAD83439; Bfl373.
GeneIDi1499573.
KEGGibfl:Bfl373.
PATRICi31964347. VBICanBlo38691_0363.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX248583 Genomic DNA. Translation: CAD83439.1 .
RefSeqi NP_878664.1. NC_005061.1.
WP_011126647.1. NC_005061.1.

3D structure databases

ProteinModelPortali Q7VR50.
SMRi Q7VR50. Positions 4-444.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 203907.Bfl373.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAD83439 ; CAD83439 ; Bfl373 .
GeneIDi 1499573.
KEGGi bfl:Bfl373.
PATRICi 31964347. VBICanBlo38691_0363.

Phylogenomic databases

eggNOGi COG0114.
HOGENOMi HOG000061736.
KOi K01679.
OMAi MESFNIH.
OrthoDBi EOG6V1M4M.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci BFLO203907:GHF7-373-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].

Entry informationi

Entry nameiFUMC_BLOFL
AccessioniPrimary (citable) accession number: Q7VR50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: September 3, 2014
This is version 75 of the entry and version 1 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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