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Q8XQE8

- FUMC_RALSO

UniProt

Q8XQE8 - FUMC_RALSO

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Protein
Fumarate hydratase class II
Gene
fumC, RSp1279, RS05324
Organism
Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum)
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 sitei187 – 1871Proton donor/acceptor By similarity
Active sitei317 – 3171 By similarity
Binding sitei318 – 3181Substrate By similarity
Sitei330 – 3301Important for catalytic activity By similarity

GO - Molecular functioni

  1. fumarate hydratase activity Source: UniProtKB-HAMAP
Complete GO annotation...

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

BioCyciRSOL267608:GCVU-4788-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
Ordered Locus Names:RSp1279
ORF Names:RS05324
Encoded oniPlasmid megaplasmid Rsp0 Publication
OrganismiRalstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum)
Taxonomic identifieri267608 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeRalstonia
ProteomesiUP000001436: Plasmid megaplasmid Rsp

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 – 461461Fumarate hydratase class IIUniRule annotation
PRO_0000161303Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi267608.RSp1279.

Structurei

3D structure databases

ProteinModelPortaliQ8XQE8.
SMRiQ8XQE8. Positions 4-459.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 993Substrate binding By similarity
Regioni128 – 1314B site By similarity
Regioni138 – 1403Substrate binding By similarity
Regioni186 – 1872Substrate binding By similarity
Regioni323 – 3253Substrate 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.

Q8XQE8-1 [UniParc]FASTAAdd to Basket

« Hide

MTTRTERDTF GPIEVPADRL WGAQTQRSLQ NFDIAGDRMP RELIDALARI    50
KRASAAVNQR LGLLPADKAN AVIAAADEVI AGKHPGEFPL VVWQTGSGTQ 100
SNMNMNEVLA NRASELLGGE RGEARLVHPN DDVNRSQSSN DVFPTAMHVA 150
AVTAITRHLL PSLRALRETL ARKAIDFDDI IKIGRTHLQD ATPLTLGQEF 200
SGYAAQLQHS ETHLNAALPH LCELALGGTA VGTGLNAPAG YAEQVAAELA 250
ALTGLPFVTS PNKFETMASA DGLVHAHGAL KTLAASLTKI ANDIRWLASG 300
PRSGLGELSI PENEPGSSIM PGKVNPTQSE AMTMLCAQVF GNDVAVNIGG 350
ASGNFELNVF RPMIAYNFLH SARLLADGMR SFNDHCAVGI EPNRERIAEL 400
VQRSLMLVTA LNPHIGYDKS AQIAKKAHKE GTSLREAALA LGYVTAEQFD 450
AWVRPEQMVG R 461
Length:461
Mass (Da):49,403
Last modified:March 1, 2002 - v1
Checksum:i8A44D62B53EDE18B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL646053 Genomic DNA. Translation: CAD18430.1.
RefSeqiNP_522838.1. NC_003296.1.
WP_011004561.1. NC_003296.1.

Genome annotation databases

EnsemblBacteriaiCAD18430; CAD18430; RSp1279.
GeneIDi1223591.
KEGGirso:RSp1279.
PATRICi20268209. VBIRalSol70888_4772.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL646053 Genomic DNA. Translation: CAD18430.1 .
RefSeqi NP_522838.1. NC_003296.1.
WP_011004561.1. NC_003296.1.

3D structure databases

ProteinModelPortali Q8XQE8.
SMRi Q8XQE8. Positions 4-459.
ModBasei Search...

Protein-protein interaction databases

STRINGi 267608.RSp1279.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAD18430 ; CAD18430 ; RSp1279 .
GeneIDi 1223591.
KEGGi rso:RSp1279.
PATRICi 20268209. VBIRalSol70888_4772.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci RSOL267608:GCVU-4788-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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: GMI1000.

Entry informationi

Entry nameiFUMC_RALSO
AccessioniPrimary (citable) accession number: Q8XQE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2002
Last modified: September 3, 2014
This is version 81 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, Plasmid

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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