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Q8KTE1

- FUMC_METEA

UniProt

Q8KTE1 - FUMC_METEA

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Protein
Fumarate hydratase class II
Gene
fumC, fumA, MexAM1_META1p2857
Organism
Methylobacterium extorquens (strain ATCC 14718 / DSM 1338 / AM1)
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 sitei195 – 1951Proton donor/acceptor By similarity
Active sitei325 – 3251 By similarity
Binding sitei326 – 3261Substrate By similarity
Sitei338 – 3381Important 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

BioCyciMEXT272630:GBY6-2704-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
Synonyms:fumA
Ordered Locus Names:MexAM1_META1p2857
OrganismiMethylobacterium extorquens (strain ATCC 14718 / DSM 1338 / AM1)
Taxonomic identifieri272630 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium
ProteomesiUP000009081: 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 – 472472Fumarate hydratase class IIUniRule annotation
PRO_0000161287Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ8KTE1.
SMRiQ8KTE1. Positions 12-469.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni105 – 1073Substrate binding By similarity
Regioni136 – 1394B site By similarity
Regioni146 – 1483Substrate binding By similarity
Regioni194 – 1952Substrate binding By similarity
Regioni331 – 3333Substrate 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.

Q8KTE1-1 [UniParc]FASTAAdd to Basket

« Hide

MSPHENPSVE TRTESDTFGP IEVPAHRYWG AQTQRSIQNF KIGTERQPAP    50
LVHALGIVKQ AAALVNKDLG GLDPKIADAI AESAAEVVAG KHDDEFPLVV 100
WQTGSGTQSN MNANEVIASL ANERLGGKRG GKSPVHPNDH CNRGQSSNDT 150
FPTAMHIAVA REVQERLLPA LSHLHTALDA KAKEFESIVK IGRTHLQDAT 200
PVSLGQEFSG YAAQVALGGA RIAATLPGVL ALAQGGTAVG TGLNAHPEFA 250
ERFAAKVAEL TGLPFTSAEN KFEALATHDA LVFLQGALTA LASGLFKIAN 300
DIRLLGSGPR SGLGELSLPE NEPGSSIMPG KVNPTQCEAL TMVCAQVVGN 350
GTTVSFAGSQ GHFELNVFKP VIANAVLQSV RILADASVSF TDNCVVGIKA 400
NTDRISDLMS RSLMLVTALA PSIGYDKAAE IAKTAHKNGT TLKEEALRLG 450
YVTDEEFERV VRPETMLAPS AE 472
Length:472
Mass (Da):49,739
Last modified:October 1, 2002 - v1
Checksum:i6B24EDD6A27775E7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF497854 Genomic DNA. Translation: AAN03819.1.
CP001510 Genomic DNA. Translation: ACS40610.1.
RefSeqiWP_003597776.1. NC_012808.1.
YP_002963887.1. NC_012808.1.

Genome annotation databases

EnsemblBacteriaiACS40610; ACS40610; MexAM1_META1p2857.
GeneIDi7992744.
KEGGimea:Mex_1p2857.
PATRICi22511447. VBIMetExt101010_2790.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF497854 Genomic DNA. Translation: AAN03819.1 .
CP001510 Genomic DNA. Translation: ACS40610.1 .
RefSeqi WP_003597776.1. NC_012808.1.
YP_002963887.1. NC_012808.1.

3D structure databases

ProteinModelPortali Q8KTE1.
SMRi Q8KTE1. Positions 12-469.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACS40610 ; ACS40610 ; MexAM1_META1p2857 .
GeneIDi 7992744.
KEGGi mea:Mex_1p2857.
PATRICi 22511447. VBIMetExt101010_2790.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci MEXT272630:GBY6-2704-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

« Hide 'large scale' publications
  1. "Reconstruction of C3 and C4 metabolism in Methylobacterium extorquens AM1 using transposon mutagenesis."
    Van Dien S.J., Okubo Y., Hough M.T., Taitano T., Lidstrom M.E.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 14718 / DSM 1338 / AM1.

Entry informationi

Entry nameiFUMC_METEA
AccessioniPrimary (citable) accession number: Q8KTE1
Secondary accession number(s): C5AUK0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2002
Last modified: September 3, 2014
This is version 67 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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