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Q88M20

- FUMC_PSEPK

UniProt

Q88M20 - FUMC_PSEPK

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Protein
Fumarate hydratase class II
Gene
fumC, fumC-2, PP_1755
Organism
Pseudomonas putida (strain KT2440)
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

BioCyciPPUT160488:GIXO-1800-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-2
Ordered Locus Names:PP_1755
OrganismiPseudomonas putida (strain KT2440)
Taxonomic identifieri160488 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000000556: 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_0000161301Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi160488.PP_1755.

Structurei

3D structure databases

ProteinModelPortaliQ88M20.
SMRiQ88M20. 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.
OMAiIPHICEL.
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.

Q88M20-1 [UniParc]FASTAAdd to Basket

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MSRIETDSLG PVEVPEDAYW GAQTQRSLIN FAIGKERMPL AVLHALALIK    50
KAAARVNDRN GDLPADIARL IEQAADEVLD GQHDDQFPLV VWQTGSGTQS 100
NMNVNEVIAG RANELAGKGR GGKAPVHPND HVNRSQSSND CFPTAMHIAA 150
AQAVHEKLLP AVTELSSGLA ELSMRHHKLV KTGRTHMMDA TPITFGQEVS 200
AFVAQLDYAQ RAIRATLPAV CELAQGGTAV GTGLNAPQGF AEAIAAELAA 250
LSGLPFITAP NKFAALAGHE PLTSLAGALK TLAVALMKIA NDLRLLGSGP 300
RAGLAEVRLP ANEPGSSIMP GKVNPTQCEA LSMLACQVLG NDAAIGFAAS 350
QGHLQLNVFK PVIIHNLLQS IELLADGCRN FQQHCVAGIE PDAEQMAAHL 400
ERGLMLVTAL NPHIGYDKAA EIAKKAYSEG TTLREAALAL KYLTNEQFDQ 450
WVRPENMLAP GGKG 464
Length:464
Mass (Da):49,131
Last modified:June 1, 2003 - v1
Checksum:i3501E4688552BF4D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE015451 Genomic DNA. Translation: AAN67375.1.
RefSeqiNP_743911.1. NC_002947.3.

Genome annotation databases

EnsemblBacteriaiAAN67375; AAN67375; PP_1755.
GeneIDi1043414.
KEGGippu:PP_1755.
PATRICi19941752. VBIPsePut30601_1850.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE015451 Genomic DNA. Translation: AAN67375.1 .
RefSeqi NP_743911.1. NC_002947.3.

3D structure databases

ProteinModelPortali Q88M20.
SMRi Q88M20. Positions 3-458.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 160488.PP_1755.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN67375 ; AAN67375 ; PP_1755 .
GeneIDi 1043414.
KEGGi ppu:PP_1755.
PATRICi 19941752. VBIPsePut30601_1850.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci PPUT160488:GIXO-1800-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: KT2440.

Entry informationi

Entry nameiFUMC_PSEPK
AccessioniPrimary (citable) accession number: Q88M20
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: May 14, 2014
This is version 80 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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