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Q8Y551

- FUMC_LISMO

UniProt

Q8Y551 - FUMC_LISMO

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Protein

Fumarate hydratase class II

Gene
fumC, citG, lmo2225
Organism
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
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 sitei181 – 1811Proton donor/acceptor By similarity
Active sitei311 – 3111 By similarity
Binding sitei312 – 3121Substrate By similarity
Sitei324 – 3241Important 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

BioCyciLMON169963:LMO2225-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:citG
Ordered Locus Names:lmo2225
OrganismiListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Taxonomic identifieri169963 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
ProteomesiUP000000817: Chromosome

Organism-specific databases

GenoListiLMO2225.

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 – 455455Fumarate hydratase class IIUniRule annotationPRO_0000161286Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi169963.lmo2225.

Structurei

3D structure databases

ProteinModelPortaliQ8Y551.
SMRiQ8Y551. Positions 3-452.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni96 – 983Substrate binding By similarity
Regioni122 – 1254B site By similarity
Regioni132 – 1343Substrate binding By similarity
Regioni180 – 1812Substrate binding By similarity
Regioni317 – 3193Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0114.
HOGENOMiHOG000061736.
KOiK01679.
OMAiMESFNIH.
OrthoDBiEOG6V1M4M.
PhylomeDBiQ8Y551.

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.

Q8Y551-1 [UniParc]FASTAAdd to Basket

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MERIERDTLG EISVDATKYW GAQTERSKRN FAIGDNPMPI EIIYAFAQLK    50
KATAKVNAAE GKLAEEKAIA IGQVCDQIIQ GELDEHFPLV VWQTGSGTQS 100
NMNVNEVIAH VANLTLGEGQ IHPNDDVNMS QSSNDTFPTA MHIAAYGALV 150
TKLLPEITKM EAVLTEKKNK YMHLVKIGRT HLQDATPLTL GQEISGWEAC 200
LTNNKNYLET SMKAILPLAI GGTAVGTGLN ASRDFGDKVA EELMKQTGYP 250
FTSDSNKYFA LTSHSPINFV HGAIRSLASD LMKIANDIRL LASGPRSGIG 300
ELEIPANEPG SSIMPGKVNP TQCEAITMVA AQVMGNDVTI NVAASQGNFE 350
LNVYKPVIIF NFLESIKLLA DSMRSFRVHC LEGLTANEKV IETKVNDSLM 400
LVTALNPHIG YEKAAKIAKL AFDENTTLKE AAIKTGFVTE KEFDLWINPL 450
KMTNL 455
Length:455
Mass (Da):49,626
Last modified:March 1, 2002 - v1
Checksum:i5AF66C261A8F844A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL591982 Genomic DNA. Translation: CAD00303.1.
PIRiAI1352.
RefSeqiNP_465749.1. NC_003210.1.

Genome annotation databases

EnsemblBacteriaiCAD00303; CAD00303; CAD00303.
GeneIDi987997.
KEGGilmo:lmo2225.
PATRICi20313670. VBILisMon69206_2277.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL591982 Genomic DNA. Translation: CAD00303.1 .
PIRi AI1352.
RefSeqi NP_465749.1. NC_003210.1.

3D structure databases

ProteinModelPortali Q8Y551.
SMRi Q8Y551. Positions 3-452.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 169963.lmo2225.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAD00303 ; CAD00303 ; CAD00303 .
GeneIDi 987997.
KEGGi lmo:lmo2225.
PATRICi 20313670. VBILisMon69206_2277.

Organism-specific databases

GenoListi LMO2225.

Phylogenomic databases

eggNOGi COG0114.
HOGENOMi HOG000061736.
KOi K01679.
OMAi MESFNIH.
OrthoDBi EOG6V1M4M.
PhylomeDBi Q8Y551.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci LMON169963:LMO2225-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: ATCC BAA-679 / EGD-e.

Entry informationi

Entry nameiFUMC_LISMO
AccessioniPrimary (citable) accession number: Q8Y551
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2002
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, 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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