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Q7N4H8

- FUMC_PHOLL

UniProt

Q7N4H8 - FUMC_PHOLL

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Protein
Fumarate hydratase class II
Gene
fumC, plu2359
Organism
Photorhabdus luminescens subsp. laumondii (strain TT01)
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

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:plu2359
OrganismiPhotorhabdus luminescens subsp. laumondii (strain TT01)
Taxonomic identifieri243265 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePhotorhabdus
ProteomesiUP000002514: Chromosome

Organism-specific databases

GenoListiplu2359.

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 – 464464Fumarate hydratase class IIUniRule annotation
PRO_0000161295Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi243265.plu2359.

Structurei

3D structure databases

ProteinModelPortaliQ7N4H8.
SMRiQ7N4H8. Positions 5-460.

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.

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.

Q7N4H8-1 [UniParc]FASTAAdd to Basket

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MAATRIEKDS MGPIEVPADQ LWGAQTQRSL EHFRISQEKM PVALIHALAL    50
TKQAAASVNM DLGLLPQERG EAIIAAAKEV LEGKHPTEFP LAIWQTGSGT 100
QSNMNMNEVL ANRGSEILGG VRGSERLIHP NDDVNKSQSS NDVFPTAMHV 150
AAVIALSEHL IPELKILQKT LADKAEAYKD IVKIGRTHLQ DATPLTLGQE 200
ISGWAAMLTH NLKHIEDSIP HVCELALGGT AVGTGLNTHP EYAVRVAKKL 250
AELTNHSFVT APNKFEALAT CDALVHSHGA LKGLAASIMK IANDVRWLAS 300
GPRCGIGEIS IPENEPGSSI MPGKVNPTQC EAVTMLCAQV MGNDVAINIG 350
GASGNFELNV FRPMVINNFL QSVRLLADGM RSFNEHCAVG IEPNRDRITQ 400
LLNESLMLVT ALNTHIGYDK AAEIAKKAHK EGLTLKQSAM KLGYLTEAEF 450
DEWVRPEDMV GSLK 464
Length:464
Mass (Da):50,119
Last modified:December 15, 2003 - v1
Checksum:i085AB3882444AB3E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX571866 Genomic DNA. Translation: CAE14652.1.
RefSeqiNP_929605.1. NC_005126.1.

Genome annotation databases

EnsemblBacteriaiCAE14652; CAE14652; plu2359.
GeneIDi2802364.
KEGGiplu:plu2359.
PATRICi20508855. VBIPhoLum48522_2666.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX571866 Genomic DNA. Translation: CAE14652.1 .
RefSeqi NP_929605.1. NC_005126.1.

3D structure databases

ProteinModelPortali Q7N4H8.
SMRi Q7N4H8. Positions 5-460.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243265.plu2359.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAE14652 ; CAE14652 ; plu2359 .
GeneIDi 2802364.
KEGGi plu:plu2359.
PATRICi 20508855. VBIPhoLum48522_2666.

Organism-specific databases

GenoListi plu2359.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TT01.

Entry informationi

Entry nameiFUMC_PHOLL
AccessioniPrimary (citable) accession number: Q7N4H8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: May 14, 2014
This is version 74 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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