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Q7W4N9

- FUMC_BORPA

UniProt

Q7W4N9 - FUMC_BORPA

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Protein
Fumarate hydratase class II
Gene
fumC, BPP3619
Organism
Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
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
Complete GO annotation...

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

BioCyciBPAR257311:BPP3619-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:BPP3619
OrganismiBordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
Taxonomic identifieri257311 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
ProteomesiUP000001421: 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 annotation
PRO_0000161257Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi257311.BPP3619.

Structurei

3D structure databases

ProteinModelPortaliQ7W4N9.
SMRiQ7W4N9. Positions 4-458.

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.
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.

Q7W4N9-1 [UniParc]FASTAAdd to Basket

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MKTRTEKDTF GPIEVPEQHL WGAQTQRSLH FFAISTEKMP VPLVAAMARL    50
KRAAAKVNAE LGELDPQVAD AIMRAADEVV AGKWPDEFPL SVWQTGSGTQ 100
SNMNMNEVLA NRASELLGGE RGEGRKVHPN DHVNRGQSSN DTFPTAMHVA 150
AAVEVEHRVL PALKALRGTL AAKSAAFYDI VKIGRTHLQD ATPLTLGQEI 200
SGYVAQLDLA EQQIRATLAG LHQLAIGGTA VGTGLNAHPQ FSAKVSAELA 250
HDTGSAFVSA PNKFQALASH EALLFAHGAL KTLAAGLMKI ANDVRWLASG 300
PRSGLGEISI PENEPGSSIM PGKVNPTQCE AVTMLAAQVM GNDVAINVGG 350
ASGNFELNVF KPLVIHNFLQ SVRLLADGMV SFDKHCAAGI EPNRERITEL 400
VERSLMLVTA LNPHIGYDKA AQIAKKAHKE NLSLKEAALA LGHLTEAQFA 450
EWVVPGDMTN ARR 463
Length:463
Mass (Da):49,491
Last modified:October 1, 2003 - v1
Checksum:i8D96DAFACB625AE1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX640434 Genomic DNA. Translation: CAE38903.1.
RefSeqiNP_885778.1. NC_002928.3.

Genome annotation databases

EnsemblBacteriaiCAE38903; CAE38903; BPP3619.
GeneIDi1666559.
KEGGibpa:BPP3619.
PATRICi21151261. VBIBorPar43418_3799.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX640434 Genomic DNA. Translation: CAE38903.1 .
RefSeqi NP_885778.1. NC_002928.3.

3D structure databases

ProteinModelPortali Q7W4N9.
SMRi Q7W4N9. Positions 4-458.
ModBasei Search...

Protein-protein interaction databases

STRINGi 257311.BPP3619.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAE38903 ; CAE38903 ; BPP3619 .
GeneIDi 1666559.
KEGGi bpa:BPP3619.
PATRICi 21151261. VBIBorPar43418_3799.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci BPAR257311:BPP3619-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. "Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica."
    Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S.
    , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J.
    Nat. Genet. 35:32-40(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 12822 / ATCC BAA-587 / NCTC 13253.

Entry informationi

Entry nameiFUMC_BORPA
AccessioniPrimary (citable) accession number: Q7W4N9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 74 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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