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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Pseudomonas syringae pv. tomato (strain DC3000)
Status
Reviewed-Annotation score: 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

Pathway: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes (S)-malate from fumarate.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Fumarate hydratase class II (fumC-2), Fumarate hydratase class II (fumC)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-malate from fumarate, the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei186 – 1861Proton donor/acceptorBy similarity
Active sitei316 – 3161By similarity
Binding sitei317 – 3171SubstrateUniRule annotation
Sitei329 – 3291Important for catalytic activityBy similarity

GO - Molecular functioni

GO - Biological processi

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 IIUniRule annotation (EC:4.2.1.2UniRule annotation)
Short name:
Fumarase CUniRule annotation
Gene namesi
Name:fumCUniRule annotation
Synonyms:fumC-1
Ordered Locus Names:PSPTO_1731
OrganismiPseudomonas syringae pv. tomato (strain DC3000)
Taxonomic identifieri223283 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002515 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 464464Fumarate hydratase class IIPRO_0000161302Add
BLAST

2D gel databases

World-2DPAGE0008:Q885V0.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi223283.PSPTO_1731.

Structurei

3D structure databases

ProteinModelPortaliQ885V0.
SMRiQ885V0. Positions 3-458.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni96 – 983Substrate bindingUniRule annotation
Regioni127 – 1304B siteUniRule annotation
Regioni137 – 1393Substrate bindingUniRule annotation
Regioni185 – 1862Substrate bindingUniRule annotation
Regioni322 – 3243Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
KOiK01679.
OMAiARHMKLV.
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

« Hide

        10         20         30         40         50
MSRTETDSIG PIEVPEDAYW GAQTQRSLIN FAIGDQRMPL AVLHALTLIK
60 70 80 90 100
KAAARVNDRN GDLPADIARL IEQAADEVLD GQHDAQFPLV VWQTGSGTQS
110 120 130 140 150
NMNVNEVIAG RANELAGQGR GGKSPVHPND HVNRSQSSND CFPTAMHIAT
160 170 180 190 200
AQAVKEQLLP AIAELSSGLA EQAARHMKLV KTGRTHMMDA TPITFGQELS
210 220 230 240 250
GFVAQLDYAE KAIRAALPAV YELAQGGTAV GTGLNAPKGF AEAIAAELAA
260 270 280 290 300
LSGLPFVTAP NKFAALAGHE PLAALSGALK TLAGTLMKIA NDLRLLGSGP
310 320 330 340 350
RAGLAEVRLP ANEPGSSIMP GKVNPTQCEA LSMLACQVMG NDVTIGFAAS
360 370 380 390 400
QGHLQLNVYK PVIIHNVLQS IRLLADGCSN FNEHCVAGME PDAEKMAEHL
410 420 430 440 450
ERGLMLVTAL NPHIGYDKSA HIAKKAYTEG LTLREAALAL GYLTDEEFDA
460
WVRPDKMLEA GSNG
Length:464
Mass (Da):49,077
Last modified:June 1, 2003 - v1
Checksum:i6B12FFF27257FFD2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016853 Genomic DNA. Translation: AAO55251.1.
RefSeqiNP_791556.1. NC_004578.1.
WP_005766716.1. 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:
EMBLi
GenBanki
DDBJi
Links Updated
AE016853 Genomic DNA. Translation: AAO55251.1.
RefSeqiNP_791556.1. NC_004578.1.
WP_005766716.1. NC_004578.1.

3D structure databases

ProteinModelPortaliQ885V0.
SMRiQ885V0. Positions 3-458.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi223283.PSPTO_1731.

2D gel databases

World-2DPAGE0008:Q885V0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
KOiK01679.
OMAiARHMKLV.
OrthoDBiEOG6V1M4M.
PhylomeDBiQ885V0.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01007.
BioCyciPSYR223283:GJIX-1762-MONOMER.

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]
ProtoNetiSearch...

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: May 27, 2015
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).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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.