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Q82SM5

- FUMC_NITEU

UniProt

Q82SM5 - FUMC_NITEU

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Protein
Fumarate hydratase class II
Gene
fumC, NE2286
Organism
Nitrosomonas europaea (strain ATCC 19718 / NBRC 14298)
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 sitei188 – 1881Proton donor/acceptor By similarity
Active sitei318 – 3181 By similarity
Binding sitei319 – 3191Substrate By similarity
Sitei331 – 3311Important 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

BioCyciNEUR228410:GJNO-2331-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:NE2286
OrganismiNitrosomonas europaea (strain ATCC 19718 / NBRC 14298)
Taxonomic identifieri228410 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas
ProteomesiUP000001416: 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_0000161292Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi228410.NE2286.

Structurei

3D structure databases

ProteinModelPortaliQ82SM5.
SMRiQ82SM5. Positions 5-459.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni98 – 1003Substrate binding By similarity
Regioni129 – 1324B site By similarity
Regioni139 – 1413Substrate binding By similarity
Regioni187 – 1882Substrate binding By similarity
Regioni324 – 3263Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
KOiK01679.
OMAiMESFNIH.
OrthoDBiEOG6V1M4M.
PhylomeDBiQ82SM5.

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.

Q82SM5-1 [UniParc]FASTAAdd to Basket

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MDQYREEHDA IGTVQVPASA LWGAQTQRSL NNFNISGERM PSALIHALAL    50
VKRAAASVNH DLGLLDENIA RAIITAADEV LAGEHAGEFP LVVWQTGSGT 100
QTNMNMNEVL ANRASEILGG TRGKGRKVHP NDHVNKGQSS NDVFPTAMHI 150
AAVEAIRNRL IPALEALRKT LSSKSAAFSD IVKIGRTHLQ DATPLTLGQE 200
FSGYVSQLDH GLAHLESALP HLLELALGGT AVGTGLNTHP EFARRVAAEI 250
ARLSGYPFIT AANKFEALAA HDALVHAHGV LKTLAAILIK IANDVRWLAS 300
GPRCGIGEIL IPENEPGSSI MPGKVNPTQS EAVVMLACQV MGNDVAINLG 350
GAMGNFELNT MKPLIIHNFL QSTRLLADGA ESFNTHCAAG ITANTVRIKQ 400
HLQESLMLVT ALNPHIGYDK AAEIAKKAHH EMLTLKEAAI RLGYVTAEQF 450
DVWVDPQKMT EV 462
Length:462
Mass (Da):49,530
Last modified:June 1, 2003 - v1
Checksum:iD20178003603A48A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL954747 Genomic DNA. Translation: CAD86198.1.
RefSeqiNP_842286.1. NC_004757.1.
WP_011112773.1. NC_004757.1.

Genome annotation databases

EnsemblBacteriaiCAD86198; CAD86198; NE2286.
GeneIDi1083253.
KEGGineu:NE2286.
PATRICi22715970. VBINitEur56163_2562.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL954747 Genomic DNA. Translation: CAD86198.1 .
RefSeqi NP_842286.1. NC_004757.1.
WP_011112773.1. NC_004757.1.

3D structure databases

ProteinModelPortali Q82SM5.
SMRi Q82SM5. Positions 5-459.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 228410.NE2286.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAD86198 ; CAD86198 ; NE2286 .
GeneIDi 1083253.
KEGGi neu:NE2286.
PATRICi 22715970. VBINitEur56163_2562.

Phylogenomic databases

eggNOGi COG0114.
HOGENOMi HOG000061736.
KOi K01679.
OMAi MESFNIH.
OrthoDBi EOG6V1M4M.
PhylomeDBi Q82SM5.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci NEUR228410:GJNO-2331-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 ammonia-oxidizing bacterium and obligate chemolithoautotroph Nitrosomonas europaea."
    Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L., Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A., Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.
    J. Bacteriol. 185:2759-2773(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 19718 / NBRC 14298.

Entry informationi

Entry nameiFUMC_NITEU
AccessioniPrimary (citable) accession number: Q82SM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: September 3, 2014
This is version 77 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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