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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Bacillus thuringiensis (strain Al Hakam)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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), 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
Binding sitei99 – 991SubstrateUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotationSAAS annotationImported

Keywords - Biological processi

Tricarboxylic acid cycleUniRule annotation

Enzyme and pathway databases

BioCyciBTHU412694:GH1W-1581-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:BALH_1553Imported
OrganismiBacillus thuringiensis (strain Al Hakam)Imported
Taxonomic identifieri412694 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
Proteomesi
  • UP000000761 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotationSAAS annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA0RCE6.
SMRiA0RCE6. Positions 4-458.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 340330Lyase_1InterPro annotationAdd
BLAST
Domaini406 – 45853FumaraseC_CInterPro annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni127 – 1304B siteUniRule annotation
Regioni137 – 1393Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000061736.
KOiK01679.
OMAiFELNVYN.
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.

A0RCE6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEYRIERDTL GEIKVPADKL WAAQTQRSKE NFPIGTEQMP LEIVKAFAIL
60 70 80 90 100
KKSAALSNQK LGKLSEEKAE AIVVAADEII AGKWNEHFPL VVWQTGSGTQ
110 120 130 140 150
SNMNVNEVIA NRGNQILKEK GSDVHIHPND DVNMSQSSND TFPTALHVAC
160 170 180 190 200
VLAVENHVLP AITKLKETLA EKVTAFEYII KIGRTHLQDA TPLTLGQEIS
210 220 230 240 250
GWHRMLEKTE RMIAESNTYM KELAIGGTAV GTGINAHPKF GEMVSEEISQ
260 270 280 290 300
FTGKQFISAP NKFHALTSHD EVVYTHGALK ALAADLMKIA NDVRWLASGP
310 320 330 340 350
RSGLGEIIIP ANEPGSSIMP GKVNPTQSEA LTMVVAQVMG NDATIGFAAS
360 370 380 390 400
QGNFELNVFK PVIAYNFLQS AHLLADAIVS FNDNCAVGIE ADEEVIKENV
410 420 430 440 450
NRSLMLVTAL NPHIGYENAA KIAKHAHKEG LTLKEAALQS GLLTEEQFDE
460
IVDPKKMIAP KE
Length:462
Mass (Da):50,358
Last modified:January 9, 2007 - v1
Checksum:iC3E7322499603DDA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000485 Genomic DNA. Translation: ABK84889.1.
RefSeqiWP_000456620.1. NC_008600.1.

Genome annotation databases

EnsemblBacteriaiABK84889; ABK84889; BALH_1553.
KEGGibtl:BALH_1553.
PATRICi18995539. VBIBacThu63319_1772.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000485 Genomic DNA. Translation: ABK84889.1.
RefSeqiWP_000456620.1. NC_008600.1.

3D structure databases

ProteinModelPortaliA0RCE6.
SMRiA0RCE6. Positions 4-458.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK84889; ABK84889; BALH_1553.
KEGGibtl:BALH_1553.
PATRICi18995539. VBIBacThu63319_1772.

Phylogenomic databases

HOGENOMiHOG000061736.
KOiK01679.
OMAiFELNVYN.
OrthoDBiEOG6V1M4M.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.
BioCyciBTHU412694:GH1W-1581-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].
    Strain: Al HakamImported.

Entry informationi

Entry nameiA0RCE6_BACAH
AccessioniPrimary (citable) accession number: A0RCE6
Entry historyi
Integrated into UniProtKB/TrEMBL: January 9, 2007
Last sequence update: January 9, 2007
Last modified: July 6, 2016
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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.UniRule annotation

Keywords - Technical termi

Complete proteomeImported

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.