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Q9PL64

- FUMC_CHLMU

UniProt

Q9PL64 - FUMC_CHLMU

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Protein
Fumarate hydratase class II
Gene
fumC, TC_0244
Organism
Chlamydia muridarum (strain MoPn / Nigg)
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 sitei185 – 1851Proton donor/acceptor By similarity
Active sitei315 – 3151 By similarity
Binding sitei316 – 3161Substrate By similarity
Sitei328 – 3281Important 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

BioCyciCMUR243161:GHYU-257-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
Ordered Locus Names:TC_0244
OrganismiChlamydia muridarum (strain MoPn / Nigg)
Taxonomic identifieri243161 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
ProteomesiUP000000800: 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 – 463463Fumarate hydratase class IIUniRule annotation
PRO_0000161267Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Protein-protein interaction databases

STRINGi243161.TC0244.

Structurei

3D structure databases

ProteinModelPortaliQ9PL64.
SMRiQ9PL64. Positions 1-455.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni95 – 973Substrate binding By similarity
Regioni126 – 1294B site By similarity
Regioni136 – 1383Substrate binding By similarity
Regioni184 – 1852Substrate binding By similarity
Regioni321 – 3233Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0114.
KOiK01679.
OMAiAITNCEL.
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.

Q9PL64-1 [UniParc]FASTAAdd to Basket

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MRQENDSLGI VMVPEDKLFG AQTGRSKNFF SYGKELMPIE VIQALVKIKK    50
CAAKANGDLQ CLDAKRRDMI VAASDEILSG GLEEHFPLKV WQTGSGTQSN 100
MNVNEVIANL AIKRHGGELG SKNPVHPNDH VNKSQSSNDV FPTAMHIAAV 150
QSIKGSLIPA LEHLQKNLDA KALEFSRDIK IGRTHLMDAV PMTLGQEFSG 200
YSHQLRSCLE RIGFSLTHLY ELAIGGTAVG TGLNVPEGFV DKVIYYLRQE 250
TGEPFIPASN YFAALSNHDA LVQAHGSLAV LACSLIKIAT DLSFLGSGPR 300
CGLGEIFFPE NEPGSSIMPG KINPTQSEAL QMVCSQVIGN NQSVIFSGTK 350
GNFELNVMKP VIIYDFLQSV NLLSGAMRSF ADYFVSGLKV NRGQLQQNVE 400
RSLMLVTALA PVLGYDKCSK IALKAFHENL SLKEACVSLG FLSEQEFDTH 450
VVPGLMLGKR ERE 463
Length:463
Mass (Da):50,428
Last modified:October 1, 2000 - v1
Checksum:i7F3C5EA2F2991332
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE002160 Genomic DNA. Translation: AAF39114.1.
PIRiB81725.
RefSeqiNP_296623.1. NC_002620.2.

Genome annotation databases

EnsemblBacteriaiAAF39114; AAF39114; TC_0244.
GeneIDi1246413.
KEGGicmu:TC_0244.
PATRICi20371880. VBIChlMur19118_0267.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE002160 Genomic DNA. Translation: AAF39114.1 .
PIRi B81725.
RefSeqi NP_296623.1. NC_002620.2.

3D structure databases

ProteinModelPortali Q9PL64.
SMRi Q9PL64. Positions 1-455.
ModBasei Search...

Protein-protein interaction databases

STRINGi 243161.TC0244.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF39114 ; AAF39114 ; TC_0244 .
GeneIDi 1246413.
KEGGi cmu:TC_0244.
PATRICi 20371880. VBIChlMur19118_0267.

Phylogenomic databases

eggNOGi COG0114.
KOi K01679.
OMAi AITNCEL.
OrthoDBi EOG6V1M4M.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci CMUR243161:GHYU-257-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: MoPn / Nigg.

Entry informationi

Entry nameiFUMC_CHLMU
AccessioniPrimary (citable) accession number: Q9PL64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 83 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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