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Q9PL64

- FUMC_CHLMU

UniProt

Q9PL64 - FUMC_CHLMU

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Protein

Fumarate hydratase class II

Gene

fumC

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

Catalytic activityi

(S)-malate = fumarate + H2O.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei185 – 1851Proton donor/acceptorBy similarity
Active sitei315 – 3151By similarity
Binding sitei316 – 3161SubstrateUniRule annotation
Sitei328 – 3281Important for catalytic activityBy 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

BioCyciCMUR243161:GHYU-257-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
Ordered Locus Names:TC_0244
OrganismiChlamydia muridarum (strain MoPn / Nigg)
Taxonomic identifieri243161 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
ProteomesiUP000000800: Chromosome

Subcellular locationi

Cytoplasm 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 IIPRO_0000161267Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi243161.TC0244.

Structurei

3D structure databases

ProteinModelPortaliQ9PL64.
SMRiQ9PL64. Positions 1-455.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni95 – 973Substrate bindingUniRule annotation
Regioni126 – 1294B siteUniRule annotation
Regioni136 – 1383Substrate bindingUniRule annotation
Regioni184 – 1852Substrate bindingUniRule annotation
Regioni321 – 3233Substrate bindingUniRule annotation

Sequence similaritiesi

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

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

« Hide

        10         20         30         40         50
MRQENDSLGI VMVPEDKLFG AQTGRSKNFF SYGKELMPIE VIQALVKIKK
60 70 80 90 100
CAAKANGDLQ CLDAKRRDMI VAASDEILSG GLEEHFPLKV WQTGSGTQSN
110 120 130 140 150
MNVNEVIANL AIKRHGGELG SKNPVHPNDH VNKSQSSNDV FPTAMHIAAV
160 170 180 190 200
QSIKGSLIPA LEHLQKNLDA KALEFSRDIK IGRTHLMDAV PMTLGQEFSG
210 220 230 240 250
YSHQLRSCLE RIGFSLTHLY ELAIGGTAVG TGLNVPEGFV DKVIYYLRQE
260 270 280 290 300
TGEPFIPASN YFAALSNHDA LVQAHGSLAV LACSLIKIAT DLSFLGSGPR
310 320 330 340 350
CGLGEIFFPE NEPGSSIMPG KINPTQSEAL QMVCSQVIGN NQSVIFSGTK
360 370 380 390 400
GNFELNVMKP VIIYDFLQSV NLLSGAMRSF ADYFVSGLKV NRGQLQQNVE
410 420 430 440 450
RSLMLVTALA PVLGYDKCSK IALKAFHENL SLKEACVSLG FLSEQEFDTH
460
VVPGLMLGKR ERE
Length:463
Mass (Da):50,428
Last modified:October 1, 2000 - v1
Checksum:i7F3C5EA2F2991332
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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...
MobiDBi 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: October 1, 2014
This is version 84 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3