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Q82ID7

- FUMC_STRAW

UniProt

Q82ID7 - FUMC_STRAW

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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680)
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 sitei188 – 1881Proton donor/acceptorBy similarity
Active sitei318 – 3181By similarity
Binding sitei319 – 3191SubstrateUniRule annotation
Sitei331 – 3311Important 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

BioCyciSAVE227882:GJU1-3245-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:SAV_3221
OrganismiStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680)
Taxonomic identifieri227882 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces
ProteomesiUP000000428: 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 – 467467Fumarate hydratase class IIPRO_0000161321Add
BLAST

Proteomic databases

PRIDEiQ82ID7.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi227882.SAV_3221.

Structurei

3D structure databases

ProteinModelPortaliQ82ID7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni104 – 1063Substrate bindingUniRule annotation
Regioni129 – 1324B siteUniRule annotation
Regioni139 – 1413Substrate bindingUniRule annotation
Regioni187 – 1882Substrate bindingUniRule annotation
Regioni324 – 3263Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061737.
KOiK01679.
OMAiHANQMAS.
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.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q82ID7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTDEDDKQNY RVEHDSMGEV RVPADAKWRA QTQRAVENFP ISGQRLERAH
60 70 80 90 100
IEALARIKGA AAKVNAELGV LDKDVAEAIQ EAAAEVAEGR WDEHFPVDVF
110 120 130 140 150
QTGSGTSSNM NANEVIATLA TERLGRDVHP NDHVNASQSS NDVFPSSIHI
160 170 180 190 200
AATAAVTRDL VPALEHLAAA LGRKSEEFAD VVKAGRTHLM DATPVTLGQE
210 220 230 240 250
FGGYAAQVRY GVERLAASLP RLAELPLGGT AVGTGINTPP GFSAAVIAEV
260 270 280 290 300
ARVTGLPLTE ARDHFEAQGA RDGIVETSGQ LRTIAVGLTK IANDLRWMAS
310 320 330 340 350
GPRTGLSEIS LPDLQPGSSI MPGKVNPVIP EAVLMVAAQV TGNDATVAAA
360 370 380 390 400
GAAGNFELNV MLPVIAKNVL ESVRLLAHVS RLLADRTVDG IVAHRDRARE
410 420 430 440 450
YAESSPSVVT PLNKYIGYEE AAKVAKKALA ERQTIRQVVL ESGYVDRGDL
460
TLEQLDEALD VLRMTHP
Length:467
Mass (Da):49,801
Last modified:June 1, 2003 - v1
Checksum:i5D984D1060B87F36
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000030 Genomic DNA. Translation: BAC70932.1.
RefSeqiNP_824397.1. NC_003155.4.

Genome annotation databases

EnsemblBacteriaiBAC70932; BAC70932; SAV_3221.
GeneIDi1210693.
KEGGisma:SAV_3221.
PATRICi23720069. VBIStrAve112782_3441.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000030 Genomic DNA. Translation: BAC70932.1 .
RefSeqi NP_824397.1. NC_003155.4.

3D structure databases

ProteinModelPortali Q82ID7.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 227882.SAV_3221.

Proteomic databases

PRIDEi Q82ID7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC70932 ; BAC70932 ; SAV_3221 .
GeneIDi 1210693.
KEGGi sma:SAV_3221.
PATRICi 23720069. VBIStrAve112782_3441.

Phylogenomic databases

eggNOGi COG0114.
HOGENOMi HOG000061737.
KOi K01679.
OMAi HANQMAS.
OrthoDBi EOG6V1M4M.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci SAVE227882:GJU1-3245-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.
PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
    Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
    Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.
  2. "Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
    Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
    Nat. Biotechnol. 21:526-531(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.

Entry informationi

Entry nameiFUMC_STRAW
AccessioniPrimary (citable) accession number: Q82ID7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: October 29, 2014
This is version 79 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