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Q9ZJQ9

- FUMC_HELPJ

UniProt

Q9ZJQ9 - FUMC_HELPJ

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Protein

Fumarate hydratase class II

Gene
fumC, jhp_1245
Organism
Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99)
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 sitei187 – 1871Proton donor/acceptor By similarity
Active sitei317 – 3171 By similarity
Binding sitei318 – 3181Substrate By similarity
Sitei330 – 3301Important 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

BioCyciHPYL85963:GJB9-1281-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:jhp_1245
OrganismiHelicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99)
Taxonomic identifieri85963 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
ProteomesiUP000000804: 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 – 463463Fumarate hydratase class IIUniRule annotationPRO_0000161281Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi85963.jhp1245.

Structurei

3D structure databases

ProteinModelPortaliQ9ZJQ9.
SMRiQ9ZJQ9. Positions 4-459.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 993Substrate binding By similarity
Regioni128 – 1314B site By similarity
Regioni138 – 1403Substrate binding By similarity
Regioni186 – 1872Substrate binding By similarity
Regioni323 – 3253Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0114.
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.

Q9ZJQ9-1 [UniParc]FASTAAdd to Basket

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MQFRIEHDTM GEIKVDDSQY WGAQTQRSLE NFKIGTEKMP KELIGAFAKL    50
KRSLAVVNHK LGKLSLEKSQ AIIKACDCIL KGELCGEFPL AIWQTGSGTQ 100
TNMNLNEVIA NKATEILGGN FREKKLIHPN DDVNMSQSSN DTFPTAMHVV 150
SVLEITHKLL PSLENLLKTF KEKSQQFKEI VKIGRTHLQD ATPLTLGQEF 200
SGYASMLEHS KQQILESLEH LRELAIGGTA VGTGLNAHKE LSEKVAEELS 250
QFSGVKFISA PNKFHALTSH DAIAYAHGAF KALAANLMKI ANDIRWLASG 300
PRCGLGELNI PENEPGSSIM PGKVNPTQCE AMTMVAVQVM GNDTAIGIAA 350
SQGNFELNVF KPVIIYNFLQ SLRLLSDSME SFNIHCASGI EPNKEKIDYY 400
LHHSLMLVTA LNPHVGYENA AKIAKNAHKK GISLKESALE LKLLSAEDFD 450
QFVVPEKMIG PKA 463
Length:463
Mass (Da):50,920
Last modified:May 1, 1999 - v1
Checksum:iEF8EEF9CABD1D485
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE001439 Genomic DNA. Translation: AAD06830.1.
PIRiH71830.
RefSeqiNP_223963.1. NC_000921.1.

Genome annotation databases

EnsemblBacteriaiAAD06830; AAD06830; jhp_1245.
GeneIDi890413.
KEGGihpj:jhp1245.
PATRICi20607334. VBIHelPyl98156_1348.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE001439 Genomic DNA. Translation: AAD06830.1 .
PIRi H71830.
RefSeqi NP_223963.1. NC_000921.1.

3D structure databases

ProteinModelPortali Q9ZJQ9.
SMRi Q9ZJQ9. Positions 4-459.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 85963.jhp1245.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD06830 ; AAD06830 ; jhp_1245 .
GeneIDi 890413.
KEGGi hpj:jhp1245.
PATRICi 20607334. VBIHelPyl98156_1348.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci HPYL85963:GJB9-1281-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: J99 / ATCC 700824.

Entry informationi

Entry nameiFUMC_HELPJ
AccessioniPrimary (citable) accession number: Q9ZJQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: May 14, 2014
This is version 98 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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