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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
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 (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)DescriptionActionsGraphical viewLength
Active sitei186Proton donor/acceptorBy similarity1
Active sitei316By similarity1
Binding sitei317SubstrateUniRule annotation1
Sitei329Important 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 IIUniRule annotation (EC:4.2.1.2UniRule annotation)
Short name:
Fumarase CUniRule annotation
Gene namesi
Name:fumCUniRule annotation
Ordered Locus Names:BC_1712
OrganismiBacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
Taxonomic identifieri226900 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000001417 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_00001612531 – 462Fumarate hydratase class IIAdd BLAST462

Proteomic databases

PRIDEiQ81F85.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi226900.BC1712.

Structurei

3D structure databases

ProteinModelPortaliQ81F85.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni97 – 99Substrate bindingUniRule annotation3
Regioni127 – 130B siteUniRule annotation4
Regioni137 – 139Substrate bindingUniRule annotation3
Regioni185 – 186Substrate bindingUniRule annotation2
Regioni322 – 324Substrate bindingUniRule annotation3

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C9Q. Bacteria.
COG0114. LUCA.
KOiK01679.
OMAiFAYLKKA.

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.

Q81F85-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEYRIERDTL GEIKVPADKL WAAQTQRSKE NFPIGTEQMP LEIVKAFAIL
60 70 80 90 100
KKSAALSNQK LGKLSEEKAE AIVEAADEVI AGKWNEHFPL VVWQTGSGTQ
110 120 130 140 150
SNMNVNEVIA NRGNQILKEK GSDVHIHPND DVNMSQSSND TFPTALHVAC
160 170 180 190 200
VIAVENHVLP AITKLKETLV EKVTAFEHII KIGRTHLQDA TPLTLGQEIS
210 220 230 240 250
GWHRMLEKTE RMIAESNTYM KELAIGGTAV GTGINAHPKF GEMVSEEISQ
260 270 280 290 300
FTGKQFVSAP NKFHALTSHD EVVYTHGALK ALAADLMKIA NDVRWLASGP
310 320 330 340 350
RSGLGEIIIP ANEPGSSIMP GKVNPTQSEA LTMVVAQVMG NDATIGFAAS
360 370 380 390 400
QGNFELNVFK PVIAYNFLQS AHLLADAIVS FNDNCAVGIE ADEEVINENV
410 420 430 440 450
NRSLMLVTAL NPHIGYENAA KIAKHAHKEG LTLKEAALQS GLLTEEQFDE
460
IVDPKKMIAP KE
Length:462
Mass (Da):50,347
Last modified:June 1, 2003 - v1
Checksum:iD87CF7C737840676
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA. Translation: AAP08688.1.
RefSeqiNP_831487.1. NC_004722.1.
WP_000456610.1. NC_004722.1.

Genome annotation databases

EnsemblBacteriaiAAP08688; AAP08688; BC_1712.
GeneIDi1204061.
KEGGibce:BC1712.
PATRICi32599183. VBIBacCer54481_1700.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016877 Genomic DNA. Translation: AAP08688.1.
RefSeqiNP_831487.1. NC_004722.1.
WP_000456610.1. NC_004722.1.

3D structure databases

ProteinModelPortaliQ81F85.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226900.BC1712.

Proteomic databases

PRIDEiQ81F85.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP08688; AAP08688; BC_1712.
GeneIDi1204061.
KEGGibce:BC1712.
PATRICi32599183. VBIBacCer54481_1700.

Phylogenomic databases

eggNOGiENOG4105C9Q. Bacteria.
COG0114. LUCA.
KOiK01679.
OMAiFAYLKKA.

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 nameiFUMC_BACCR
AccessioniPrimary (citable) accession number: Q81F85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 92 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

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.