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Q9I587

- FUMC2_PSEAE

UniProt

Q9I587 - FUMC2_PSEAE

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Protein

Fumarate hydratase class II 2

Gene
fumC2, PA0854
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
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 sitei186 – 1861Proton donor/acceptor By similarity
Active sitei316 – 3161 By similarity
Binding sitei317 – 3171Substrate By similarity
Sitei329 – 3291Important 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 2 (EC:4.2.1.2)
Short name:
Fumarase C 2
Gene namesi
Name:fumC2
Ordered Locus Names:PA0854
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438: Chromosome

Organism-specific databases

PseudoCAPiPA0854.

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 II 2UniRule annotationPRO_0000161300Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi208964.PA0854.

Structurei

3D structure databases

ProteinModelPortaliQ9I587.
SMRiQ9I587. Positions 3-458.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni96 – 983Substrate binding By similarity
Regioni127 – 1304B site By similarity
Regioni137 – 1393Substrate binding By similarity
Regioni185 – 1862Substrate binding By similarity
Regioni322 – 3243Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
KOiK01679.
OMAiAARHMKL.
OrthoDBiEOG6V1M4M.
PhylomeDBiQ9I587.

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.

Q9I587-1 [UniParc]FASTAAdd to Basket

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MSRTETDSLG TIEVPDDAYW GAQTQRSLEN FAIGGQRMPL AVIHALALIK    50
KAAARVNDHL GELPPEVARL IEQAADEVLA GRHDEHFPLV VWQTGSGTQT 100
NMNVNEVIAG RANELAGNPR GGKSPVHPND HVNRAQSSND SFPTAMHIAA 150
AKAVHEQLLP AIAELSGGLA EQSARHASLV KTGRTHLMDA TPITFGQELS 200
AFVAQLDYAE RAIRAALPAV YQLAQGGTAV GTGLNAPKGF ADAIAAEIAA 250
ESGLPFVAAP NKFAALAGHE PLVILSGALK SLAVALMKIA NDLRLLGSGP 300
RAGFAEVKLP ANEPGSSIMP GKVNPTQCEA LSMLACQVMG NDSTISFAAS 350
QGHLQLNVFK PVIVYNLLES IRLLADGCRN FNKHCVAGLE PDAQRMADLL 400
ERGLMLVTAL NPHIGYDKAA EIAKKAYAEG TTLRAAALQL GYLDEAQFDE 450
WVRPEQMLEA GHHG 464
Length:464
Mass (Da):49,122
Last modified:March 1, 2001 - v1
Checksum:iB0520F835C0DDF61
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE004091 Genomic DNA. Translation: AAG04243.1.
PIRiH83538.
RefSeqiNP_249545.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG04243; AAG04243; PA0854.
GeneIDi878044.
KEGGipae:PA0854.
PATRICi19835988. VBIPseAer58763_0886.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE004091 Genomic DNA. Translation: AAG04243.1 .
PIRi H83538.
RefSeqi NP_249545.1. NC_002516.2.

3D structure databases

ProteinModelPortali Q9I587.
SMRi Q9I587. Positions 3-458.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 208964.PA0854.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG04243 ; AAG04243 ; PA0854 .
GeneIDi 878044.
KEGGi pae:PA0854.
PATRICi 19835988. VBIPseAer58763_0886.

Organism-specific databases

PseudoCAPi PA0854.

Phylogenomic databases

eggNOGi COG0114.
HOGENOMi HOG000061736.
KOi K01679.
OMAi AARHMKL.
OrthoDBi EOG6V1M4M.
PhylomeDBi Q9I587.

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: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Entry informationi

Entry nameiFUMC2_PSEAE
AccessioniPrimary (citable) accession number: Q9I587
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 85 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, 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

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