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Q7W0A2

- FUMC_BORPE

UniProt

Q7W0A2 - FUMC_BORPE

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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
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

Catalytic activityi

(S)-malate = fumarate + H2O.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei187 – 1871Proton donor/acceptorBy similarity
Active sitei317 – 3171By similarity
Binding sitei318 – 3181SubstrateUniRule annotation
Sitei330 – 3301Important for catalytic activityBy 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

BioCyciBPER257313:BP0248-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:BP0248
OrganismiBordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Taxonomic identifieri257313 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
ProteomesiUP000002676: Chromosome

Subcellular locationi

Cytoplasm 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 IIPRO_0000161258Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi257313.BP0248.

Structurei

3D structure databases

ProteinModelPortaliQ7W0A2.
SMRiQ7W0A2. Positions 4-458.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 993Substrate bindingUniRule annotation
Regioni128 – 1314B siteUniRule annotation
Regioni138 – 1403Substrate bindingUniRule annotation
Regioni186 – 1872Substrate bindingUniRule annotation
Regioni323 – 3253Substrate bindingUniRule annotation

Sequence similaritiesi

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

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.

Q7W0A2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKTRTEKDTF GPIEVPEQHL WGAQTQRSLH FFAISTEKMP VPLVAAMARL
60 70 80 90 100
KRAAAKVNAE LGELDPQVAD AIMRAADEVI AGKWPDEFPL SVWQTGSGTQ
110 120 130 140 150
SNMNMNEVLA NRASELLGGE RGEGRKVHPN DHVNRGQSSN DTFPTAMHVA
160 170 180 190 200
AAVEVEHRVL PALKALRGTL AAKSAAFYDI VKIGRTHLQD ATPLTLGQEI
210 220 230 240 250
SGYVAQLDLA EQQIRATLAG LHQLAIGGTA VGTGLNAHPQ FSAKVSAELA
260 270 280 290 300
HDTGSAFVSA PNKFQALASH EALLFAHGAL KTLAAGLMKI ANDVRWLASG
310 320 330 340 350
PRSGLGEISI PENEPGSSIM PGKVNPTQCE AVTMLAAQVM GNDVAINVGG
360 370 380 390 400
ASGNFELNVF KPLVIHNFLQ SVRLLADGMV SFDKHCAAGI EPNRERITEL
410 420 430 440 450
VERSLMLVTA LNPHIGYDKA AQIAKKAHKE NLSLKEAALA LGHLTEAQFA
460
EWVVPGDMTN ARR
Length:463
Mass (Da):49,506
Last modified:October 1, 2003 - v1
Checksum:iF3A3E9FE37BC9532
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX640411 Genomic DNA. Translation: CAE40628.1.
RefSeqiNP_879133.1. NC_002929.2.

Genome annotation databases

EnsemblBacteriaiCAE40628; CAE40628; BP0248.
GeneIDi2664150.
KEGGibpe:BP0248.
PATRICi21153526. VBIBorPer7866_0270.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX640411 Genomic DNA. Translation: CAE40628.1 .
RefSeqi NP_879133.1. NC_002929.2.

3D structure databases

ProteinModelPortali Q7W0A2.
SMRi Q7W0A2. Positions 4-458.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 257313.BP0248.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAE40628 ; CAE40628 ; BP0248 .
GeneIDi 2664150.
KEGGi bpe:BP0248.
PATRICi 21153526. VBIBorPer7866_0270.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci BPER257313:BP0248-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: Tohama I / ATCC BAA-589 / NCTC 13251.

Entry informationi

Entry nameiFUMC_BORPE
AccessioniPrimary (citable) accession number: Q7W0A2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: October 1, 2014
This is version 73 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).By similarity

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3