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Q885V0

- FUMC_PSESM

UniProt

Q885V0 - FUMC_PSESM

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Protein
Fumarate hydratase class II
Gene
fumC, fumC-1, PSPTO_1731
Organism
Pseudomonas syringae pv. tomato (strain DC3000)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

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
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

BioCyciPSYR223283:GJIX-1762-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:fumC-1
Ordered Locus Names:PSPTO_1731
OrganismiPseudomonas syringae pv. tomato (strain DC3000)
Taxonomic identifieri223283 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002515: 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 – 464464Fumarate hydratase class IIUniRule annotation
PRO_0000161302Add
BLAST

2D gel databases

World-2DPAGEi0008:Q885V0.

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi223283.PSPTO_1731.

Structurei

3D structure databases

ProteinModelPortaliQ885V0.
SMRiQ885V0. 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.
PhylomeDBiQ885V0.

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.

Q885V0-1 [UniParc]FASTAAdd to Basket

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MSRTETDSIG PIEVPEDAYW GAQTQRSLIN FAIGDQRMPL AVLHALTLIK    50
KAAARVNDRN GDLPADIARL IEQAADEVLD GQHDAQFPLV VWQTGSGTQS 100
NMNVNEVIAG RANELAGQGR GGKSPVHPND HVNRSQSSND CFPTAMHIAT 150
AQAVKEQLLP AIAELSSGLA EQAARHMKLV KTGRTHMMDA TPITFGQELS 200
GFVAQLDYAE KAIRAALPAV YELAQGGTAV GTGLNAPKGF AEAIAAELAA 250
LSGLPFVTAP NKFAALAGHE PLAALSGALK TLAGTLMKIA NDLRLLGSGP 300
RAGLAEVRLP ANEPGSSIMP GKVNPTQCEA LSMLACQVMG NDVTIGFAAS 350
QGHLQLNVYK PVIIHNVLQS IRLLADGCSN FNEHCVAGME PDAEKMAEHL 400
ERGLMLVTAL NPHIGYDKSA HIAKKAYTEG LTLREAALAL GYLTDEEFDA 450
WVRPDKMLEA GSNG 464
Length:464
Mass (Da):49,077
Last modified:June 1, 2003 - v1
Checksum:i6B12FFF27257FFD2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016853 Genomic DNA. Translation: AAO55251.1.
RefSeqiNP_791556.1. NC_004578.1.

Genome annotation databases

EnsemblBacteriaiAAO55251; AAO55251; PSPTO_1731.
GeneIDi1183368.
KEGGipst:PSPTO_1731.
PATRICi19994714. VBIPseSyr93040_1758.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016853 Genomic DNA. Translation: AAO55251.1 .
RefSeqi NP_791556.1. NC_004578.1.

3D structure databases

ProteinModelPortali Q885V0.
SMRi Q885V0. Positions 3-458.
ModBasei Search...

Protein-protein interaction databases

STRINGi 223283.PSPTO_1731.

2D gel databases

World-2DPAGEi 0008:Q885V0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAO55251 ; AAO55251 ; PSPTO_1731 .
GeneIDi 1183368.
KEGGi pst:PSPTO_1731.
PATRICi 19994714. VBIPseSyr93040_1758.

Phylogenomic databases

eggNOGi COG0114.
HOGENOMi HOG000061736.
KOi K01679.
OMAi AARHMKL.
OrthoDBi EOG6V1M4M.
PhylomeDBi Q885V0.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci PSYR223283:GJIX-1762-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: DC3000.

Entry informationi

Entry nameiFUMC_PSESM
AccessioniPrimary (citable) accession number: Q885V0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: July 9, 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

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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