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Q9KCX4

- FUMC_BACHD

UniProt

Q9KCX4 - FUMC_BACHD

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Protein
Fumarate hydratase class II
Gene
fumC, citG, BH1445
Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
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

BioCyciBHAL272558:GJC5-1528-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
Synonyms:citG
Ordered Locus Names:BH1445
OrganismiBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Taxonomic identifieri272558 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001258: 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 – 462462Fumarate hydratase class IIUniRule annotation
PRO_0000161254Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi272558.BH1445.

Structurei

3D structure databases

ProteinModelPortaliQ9KCX4.
SMRiQ9KCX4. Positions 4-458.

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.
OMAiAARHMKL.
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.

Q9KCX4-1 [UniParc]FASTAAdd to Basket

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MNTRIERDTL GEMHVPQDKL WGAQTQRSYE NFHIGTEKMP MEIIYAFALL    50
KKAAANVNKK LGQLSAEKAD AITWAANEVL AGKHDDHFPL FVWQTGSGTQ 100
SNMNMNEVLA RRGNQLLQEK GLDVTIHPND DVNRSQSSND TFPTAMHIAA 150
YNKLDDHLLP TLQMFKQTLH QKAKQFDDVI KLGRTHLQDA TPLTLGQEIS 200
GWARMLEKTE QMIRESMIYL QELAIGGTAV GTGVNAHPKF GEMVAADIAN 250
ETGKPFKSAA NKFHALTSHD ELVHTHGALK ALAADLFKIA NDIRWLASGP 300
RGGLGELIIP ANEPGSSIMP GKVNPTQSEA LTMITSQVIG NDATIAFAAS 350
QGNFELNVFK PVIIYNFLQS TTLLTDGLRT FHDKCLIGLE ANETIIKKHL 400
NESLMLVTAL NPHIGYENAA KIAKKAHAEG LTLKEAAMQS GLLTEEEFEK 450
MVDPAKMVHP QG 462
Length:462
Mass (Da):50,785
Last modified:October 1, 2000 - v1
Checksum:i72601B22909B4899
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000004 Genomic DNA. Translation: BAB05164.1.
PIRiE83830.
RefSeqiNP_242311.1. NC_002570.2.
WP_010897610.1. NC_002570.2.

Genome annotation databases

EnsemblBacteriaiBAB05164; BAB05164; BAB05164.
GeneIDi890532.
KEGGibha:BH1445.
PATRICi18939985. VBIBacHal18977_1506.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000004 Genomic DNA. Translation: BAB05164.1 .
PIRi E83830.
RefSeqi NP_242311.1. NC_002570.2.
WP_010897610.1. NC_002570.2.

3D structure databases

ProteinModelPortali Q9KCX4.
SMRi Q9KCX4. Positions 4-458.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272558.BH1445.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB05164 ; BAB05164 ; BAB05164 .
GeneIDi 890532.
KEGGi bha:BH1445.
PATRICi 18939985. VBIBacHal18977_1506.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci BHAL272558:GJC5-1528-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. "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
    Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
    Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Entry informationi

Entry nameiFUMC_BACHD
AccessioniPrimary (citable) accession number: Q9KCX4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2000
Last modified: September 3, 2014
This is version 84 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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