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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Blochmannia floridanus
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

Pathway:itricarboxylic 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
Active sitei172 – 1721Proton donor/acceptorBy similarity
Active sitei302 – 3021By similarity
Binding sitei303 – 3031SubstrateUniRule annotation
Sitei315 – 3151Important for catalytic activityBy similarity

GO - Molecular functioni

GO - Biological processi

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 IIUniRule annotation (EC:4.2.1.2UniRule annotation)
Short name:
Fumarase CUniRule annotation
Gene namesi
Name:fumCUniRule annotation
Ordered Locus Names:Bfl373
OrganismiBlochmannia floridanus
Taxonomic identifieri203907 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeant endosymbiontsCandidatus Blochmannia
ProteomesiUP000002192 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 448448Fumarate hydratase class IIPRO_0000161264Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi203907.Bfl373.

Structurei

3D structure databases

ProteinModelPortaliQ7VR50.
SMRiQ7VR50. Positions 4-444.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni83 – 853Substrate bindingUniRule annotation
Regioni113 – 1164B siteUniRule annotation
Regioni123 – 1253Substrate bindingUniRule annotation
Regioni171 – 1722Substrate bindingUniRule annotation
Regioni308 – 3103Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
KOiK01679.
OMAiIEKDTMG.
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

        10         20         30         40         50
MICNRLWGDQ TESSLKFFNI STEKMPWELI KALAQIKRVS AQVNYDLKLL
60 70 80 90 100
DYERSQAIIA AVDEILSGNH KNEFPLSVWQ TGSGTQSNMN MNEVLANRAN
110 120 130 140 150
ELLRKNQINI VVHPNDHVNK SQSSNDVFPS AMHIAAVVNL KTKLIPVIKL
160 170 180 190 200
LQKTFLKKSI EFRNIIKIGR THLQDAIPLT LGQEISGWDF MLKNNTNHIQ
210 220 230 240 250
STILDLSALA LGGTAVGTGF SAHVEYAERV VLGLSKLIHH SFFSAPNKFE
260 270 280 290 300
SLSTCDAIVY SHGTLKGLAI SMMKIANDIR LLSSGPQCGL GELIIPANEP
310 320 330 340 350
GSSIMPGKVN PTQCESMTMS CCQVMGNDLS ISLGGSSGQL QLNTYRPLII
360 370 380 390 400
YNFLQSIRLL TDSIKNFHDY CIVGIRPKFK RIEKLLNKSL MLVTALSSHI
410 420 430 440
GYDKSAQIAQ TAYLNGITLK AASIQSGYVT EKQFDDWVCP ENMIYPDM
Length:448
Mass (Da):49,649
Last modified:October 1, 2003 - v1
Checksum:iCDEC7863B7D10F2D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX248583 Genomic DNA. Translation: CAD83439.1.
RefSeqiWP_011126647.1. NC_005061.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX248583 Genomic DNA. Translation: CAD83439.1.
RefSeqiWP_011126647.1. NC_005061.1.

3D structure databases

ProteinModelPortaliQ7VR50.
SMRiQ7VR50. Positions 4-444.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi203907.Bfl373.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
KOiK01679.
OMAiIEKDTMG.
OrthoDBiEOG6V1M4M.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.
BioCyciBFLO203907:GHF7-373-MONOMER.

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]
ProtoNetiSearch...

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: July 22, 2015
This is version 79 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).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

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 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.