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Q822D5

- FUMC_CHLCV

UniProt

Q822D5 - FUMC_CHLCV

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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Chlamydophila caviae (strain GPIC)
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

BioCyciCCAV227941:GH8L-778-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:CCA_00748
OrganismiChlamydophila caviae (strain GPIC)
Taxonomic identifieri227941 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydophila
ProteomesiUP000002193: 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 – 460460Fumarate hydratase class IIPRO_0000161266Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi227941.CCA00748.

Structurei

3D structure databases

ProteinModelPortaliQ822D5.
SMRiQ822D5. Positions 1-456.
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.

Q822D5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRQENDSLGI VEVPEDKLYG AQTARSQKYF SWAPEVMPKE VIRALVLIKQ
60 70 80 90 100
CAAKANHDLG FLDSKYCDMI VSAASEILEG GFEEHFPLKV WQTGSGTQSN
110 120 130 140 150
MNVNEVIANL AIQRHGGVVG SKTPIHPNDH VNKSQSSNDV FPTAMHIAAV
160 170 180 190 200
INLKKKLIPA MDHLQRALDA KVAEFRDCVK IGRTHLMDAV PMTLGQEFSG
210 220 230 240 250
YSNQIRQSLE RVAFSLTHMY ELAIGGTAVG TGLNVPNGFI DKVIHYLRQE
260 270 280 290 300
TGEPFVAASN YFSALSNHDT LVNAHGVLAT LACALTKIAT DLSFLGSGPR
310 320 330 340 350
CGLGELLFPE NEPGSSIMPG KINPTQCEAL QMVCAQVIGN NQAVIMGGSR
360 370 380 390 400
GNFELNVMKP VIIYNFLQSV DILAGGMQAF ADYFVSGLRV NKPRLKEYLD
410 420 430 440 450
NSLMLVTALT PVLGYDKCSK MALKAFHDNI NLKEACIQMG YLSAEEFDRL
460
VVPESMVGKF
Length:460
Mass (Da):50,259
Last modified:June 1, 2003 - v1
Checksum:i8F68DE2F0046AFDA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE015925 Genomic DNA. Translation: AAP05489.1.
RefSeqiNP_829611.1. NC_003361.3.
WP_011006703.1. NC_003361.3.

Genome annotation databases

EnsemblBacteriaiAAP05489; AAP05489; CCA_00748.
GeneIDi1218433.
KEGGicca:CCA00748.
PATRICi20270625. VBIChlCav107360_0795.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE015925 Genomic DNA. Translation: AAP05489.1 .
RefSeqi NP_829611.1. NC_003361.3.
WP_011006703.1. NC_003361.3.

3D structure databases

ProteinModelPortali Q822D5.
SMRi Q822D5. Positions 1-456.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 227941.CCA00748.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAP05489 ; AAP05489 ; CCA_00748 .
GeneIDi 1218433.
KEGGi cca:CCA00748.
PATRICi 20270625. VBIChlCav107360_0795.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci CCAV227941:GH8L-778-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. "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC): examining the role of niche-specific genes in the evolution of the Chlamydiaceae."
    Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T., Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A., Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O., Salzberg S.L., Hsia R.-C., McClarty G.
    , Rank R.G., Bavoil P.M., Fraser C.M.
    Nucleic Acids Res. 31:2134-2147(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: GPIC.

Entry informationi

Entry nameiFUMC_CHLCV
AccessioniPrimary (citable) accession number: Q822D5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: October 1, 2014
This is version 77 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