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Q8KTE1

- FUMC_METEA

UniProt

Q8KTE1 - FUMC_METEA

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Protein

Fumarate hydratase class II

Gene

fumC

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

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei195 – 1951Proton donor/acceptorBy similarity
Active sitei325 – 3251By similarity
Binding sitei326 – 3261SubstrateUniRule annotation
Sitei338 – 3381Important 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

BioCyciMEXT272630:GBY6-2704-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
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 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 IIPRO_0000161287Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ8KTE1.
SMRiQ8KTE1. Positions 12-469.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni105 – 1073Substrate bindingUniRule annotation
Regioni136 – 1394B siteUniRule annotation
Regioni146 – 1483Substrate bindingUniRule annotation
Regioni194 – 1952Substrate bindingUniRule annotation
Regioni331 – 3333Substrate 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.

Q8KTE1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSPHENPSVE TRTESDTFGP IEVPAHRYWG AQTQRSIQNF KIGTERQPAP
60 70 80 90 100
LVHALGIVKQ AAALVNKDLG GLDPKIADAI AESAAEVVAG KHDDEFPLVV
110 120 130 140 150
WQTGSGTQSN MNANEVIASL ANERLGGKRG GKSPVHPNDH CNRGQSSNDT
160 170 180 190 200
FPTAMHIAVA REVQERLLPA LSHLHTALDA KAKEFESIVK IGRTHLQDAT
210 220 230 240 250
PVSLGQEFSG YAAQVALGGA RIAATLPGVL ALAQGGTAVG TGLNAHPEFA
260 270 280 290 300
ERFAAKVAEL TGLPFTSAEN KFEALATHDA LVFLQGALTA LASGLFKIAN
310 320 330 340 350
DIRLLGSGPR SGLGELSLPE NEPGSSIMPG KVNPTQCEAL TMVCAQVVGN
360 370 380 390 400
GTTVSFAGSQ GHFELNVFKP VIANAVLQSV RILADASVSF TDNCVVGIKA
410 420 430 440 450
NTDRISDLMS RSLMLVTALA PSIGYDKAAE IAKTAHKNGT TLKEEALRLG
460 470
YVTDEEFERV VRPETMLAPS AE
Length:472
Mass (Da):49,739
Last modified:October 1, 2002 - v1
Checksum:i6B24EDD6A27775E7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF497854 Genomic DNA. Translation: AAN03819.1.
CP001510 Genomic DNA. Translation: ACS40610.1.
RefSeqiYP_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:
EMBLi
GenBanki
DDBJi
Links Updated
AF497854 Genomic DNA. Translation: AAN03819.1 .
CP001510 Genomic DNA. Translation: ACS40610.1 .
RefSeqi 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: October 29, 2014
This is version 69 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