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Q8FQP8

- FUMC_COREF

UniProt

Q8FQP8 - FUMC_COREF

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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
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 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

BioCyciCEFF196164:GJW8-1090-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:CE1071
OrganismiCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Taxonomic identifieri196164 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
ProteomesiUP000001409: 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 – 473473Fumarate hydratase class IIPRO_0000161271Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi196164.CE1071.

Structurei

3D structure databases

ProteinModelPortaliQ8FQP8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni104 – 1063Substrate bindingUniRule annotation
Regioni128 – 1314B siteUniRule annotation
Regioni138 – 1403Substrate bindingUniRule annotation
Regioni186 – 1872Substrate bindingUniRule annotation
Regioni324 – 3263Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000061737.
KOiK01679.
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.

Q8FQP8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSDFMTEQEF RIEHDTMGEV KVPAQALWRA QTQRAVENFP ISGRGLESAQ
60 70 80 90 100
IRAMGLLKAA CAQVNKDSGA LDAAKADAII AAGKEIATGK HDAEFPIDVF
110 120 130 140 150
QTGSGTSSNM NTNEVIASIA KANGTEVHPN DDVNMGQSSN DTFPTATHVA
160 170 180 190 200
ATEAAVNDLI PGLKVLHESL AKKANEWDSV VKSGRTHLMD AVPVTLGQEF
210 220 230 240 250
GGYARQIQLG IERIEATLPR LGELAIGGTA VGTGINTSAD FGGKVVAELV
260 270 280 290 300
ELTGVTQLQE AANHFEAQAN RDALVEFSGA MRVVAVSLYK IANDIRLMGS
310 320 330 340 350
GPLTGLGEIQ LPDLQPGSSI MPGKVNPVLC ETATQVSAQV IGNDAAVAFA
360 370 380 390 400
GSQGQFELNV FIPVMARNVL ESARLLANTA RVFATRLVDG IVPNEEHMKQ
410 420 430 440 450
LAESSPSIVT PLNSAIGYEA AAKVAKAALA EGKTIRQTVI DMGFVDGEKL
460 470
TEEELDKRLD VLAMANTDRK QKF
Length:473
Mass (Da):50,073
Last modified:December 15, 2003 - v2
Checksum:iC4CC4FFA6F3EA1A3
GO

Sequence cautioni

The sequence BAC17881.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000035 Genomic DNA. Translation: BAC17881.1. Different initiation.
RefSeqiNP_737681.2. NC_004369.1.

Genome annotation databases

EnsemblBacteriaiBAC17881; BAC17881; BAC17881.
GeneIDi1033250.
KEGGicef:CE1071.
PATRICi21488278. VBICorEff9312_1073.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000035 Genomic DNA. Translation: BAC17881.1 . Different initiation.
RefSeqi NP_737681.2. NC_004369.1.

3D structure databases

ProteinModelPortali Q8FQP8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 196164.CE1071.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAC17881 ; BAC17881 ; BAC17881 .
GeneIDi 1033250.
KEGGi cef:CE1071.
PATRICi 21488278. VBICorEff9312_1073.

Phylogenomic databases

HOGENOMi HOG000061737.
KOi K01679.
OrthoDBi EOG6V1M4M.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci CEFF196164:GJW8-1090-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. "Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
    Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
    Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Entry informationi

Entry nameiFUMC_COREF
AccessioniPrimary (citable) accession number: Q8FQP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: October 1, 2014
This is version 73 of the entry and version 2 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