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Q8CUH5

- FUMC_OCEIH

UniProt

Q8CUH5 - FUMC_OCEIH

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Protein

Fumarate hydratase class II

Gene
fumC, OB1132
Organism
Oceanobacillus iheyensis (strain DSM 14371 / JCM 11309 / KCTC 3954 / HTE831)
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 sitei186 – 1861Proton donor/acceptor By similarity
Active sitei316 – 3161 By similarity
Binding sitei317 – 3171Substrate By similarity
Sitei329 – 3291Important 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

BioCyciOIHE221109:GI2A-1208-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:OB1132
OrganismiOceanobacillus iheyensis (strain DSM 14371 / JCM 11309 / KCTC 3954 / HTE831)
Taxonomic identifieri221109 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeOceanobacillus
ProteomesiUP000000822: 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 – 461461Fumarate hydratase class IIUniRule annotationPRO_0000161293Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi221109.OB1132.

Structurei

3D structure databases

ProteinModelPortaliQ8CUH5.
SMRiQ8CUH5. Positions 4-457.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 993Substrate binding By similarity
Regioni127 – 1304B site By similarity
Regioni137 – 1393Substrate binding By similarity
Regioni185 – 1862Substrate binding By similarity
Regioni322 – 3243Substrate 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.

Q8CUH5-1 [UniParc]FASTAAdd to Basket

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MDYRVEKDTI GEIQVPADKY WGAQTQRSKQ NFPIGNEKMP VEIIKAFAIL    50
KRSTAEANFE LGLMERDKME AIQYAADQVL NDSLTDHFPL VVWQTGSGTQ 100
SNMNVNEVLA FVGNKWLQEQ GSDLKLHPND DVNKSQSSND TYPTAMHIAA 150
VLKLEDTVLP ALSQLKNTFA EKQSAFENIV KIGRTHLQDA TPLTLGQEIS 200
GWHRMLEKSE TMISESLEHL RELAIGGTAV GTGLNAHPDF SEKVCKAIST 250
FTNKKFISAK NKFHSLTSHD ETVYAHGALK GLAADLMKIA NDVRWLASGP 300
RCGIGEITIP ANEPGSSIMP GKVNPTQSEA VTMVVTQVMG NDAAIGFAAS 350
QGNFELNVFK PVIAYNFLQS SQLLADSIIS FDERCAVGIE PNHEQIEKNL 400
NDSLMLVTAL NPHIGYENAA KIAKKAFADN STLKETAVEL GLLTEEQFDE 450
YVNPEEMTYP K 461
Length:461
Mass (Da):50,732
Last modified:March 1, 2003 - v1
Checksum:i44242B3859AA4CDF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000028 Genomic DNA. Translation: BAC13088.1.
RefSeqiNP_692053.1. NC_004193.1.
WP_011065533.1. NC_004193.1.

Genome annotation databases

EnsemblBacteriaiBAC13088; BAC13088; BAC13088.
GeneIDi1017212.
KEGGioih:OB1132.
PATRICi22793268. VBIOceIhe82024_1151.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000028 Genomic DNA. Translation: BAC13088.1 .
RefSeqi NP_692053.1. NC_004193.1.
WP_011065533.1. NC_004193.1.

3D structure databases

ProteinModelPortali Q8CUH5.
SMRi Q8CUH5. Positions 4-457.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 221109.OB1132.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC13088 ; BAC13088 ; BAC13088 .
GeneIDi 1017212.
KEGGi oih:OB1132.
PATRICi 22793268. VBIOceIhe82024_1151.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci OIHE221109:GI2A-1208-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. "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge and its unexpected adaptive capabilities to extreme environments."
    Takami H., Takaki Y., Uchiyama I.
    Nucleic Acids Res. 30:3927-3935(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 14371 / JCM 11309 / KCTC 3954 / HTE831.

Entry informationi

Entry nameiFUMC_OCEIH
AccessioniPrimary (citable) accession number: Q8CUH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2003
Last modified: September 3, 2014
This is version 80 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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