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Q83CL8

- FUMC_COXBU

UniProt

Q83CL8 - FUMC_COXBU

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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
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

BioCyciCBUR227377:GJ7S-1090-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:CBU_1096
OrganismiCoxiella burnetii (strain RSA 493 / Nine Mile phase I)
Taxonomic identifieri227377 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella
ProteomesiUP000002671: 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 – 459459Fumarate hydratase class IIPRO_0000161273Add
BLAST

Proteomic databases

PRIDEiQ83CL8.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi227377.CBU_1096.

Structurei

3D structure databases

ProteinModelPortaliQ83CL8.
SMRiQ83CL8. Positions 1-457.
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.
HOGENOMiHOG000061736.
KOiK01679.
OMAiMESFNIH.
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.

Q83CL8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRKESDSMGT IEVPSEKYYG AQSQRSLINF AIGRETMPPE LIRAFGVLKK
60 70 80 90 100
AAVLTNVELG KVSQEKANFI LKACEELIAG KLNDHFPLKI WQTGSGTQTN
110 120 130 140 150
MNVNEVISNR AIELAGGKLG SKEPVHPNDH VNMSQSSNDT FPTAMHITAA
160 170 180 190 200
EMITHQLIPN LTVLRDTLEK KSKEFSEIIK IGRTHLQDAV PLTLGQEFSG
210 220 230 240 250
YVAQLNHNLE AINDVLPTLY RLALGGTAVG TGLNTHPQFA KKAADHIAEL
260 270 280 290 300
TGIPFYSASN KFAALAANDE IVLVSGVLKT LACSLMKIAN DIRWLASGPR
310 320 330 340 350
CGIGEIVIPE NEPGSSIMPG KVNPTQSEAM TMVCVQVIGN DTTITIAGSQ
360 370 380 390 400
GNFELNVYKP VMAYNLIQSI YLLSDACRSF NDHCAVGIKP NQEKINDYLN
410 420 430 440 450
NSLMLVTALN QIIGYDKASE IAKKAYKEGT TLKEAALQLG YLTASEFDKA

VDPKKMVAI
Length:459
Mass (Da):49,850
Last modified:December 15, 2003 - v2
Checksum:i15153802D24B2359
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016828 Genomic DNA. Translation: AAO90609.2.
RefSeqiNP_820095.2. NC_002971.3.

Genome annotation databases

EnsemblBacteriaiAAO90609; AAO90609; CBU_1096.
GeneIDi1208998.
KEGGicbu:CBU_1096.
PATRICi17930925. VBICoxBur82552_1090.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016828 Genomic DNA. Translation: AAO90609.2 .
RefSeqi NP_820095.2. NC_002971.3.

3D structure databases

ProteinModelPortali Q83CL8.
SMRi Q83CL8. Positions 1-457.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 227377.CBU_1096.

Proteomic databases

PRIDEi Q83CL8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAO90609 ; AAO90609 ; CBU_1096 .
GeneIDi 1208998.
KEGGi cbu:CBU_1096.
PATRICi 17930925. VBICoxBur82552_1090.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER01007 .
BioCyci CBUR227377:GJ7S-1090-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: RSA 493 / Nine Mile phase I.

Entry informationi

Entry nameiFUMC_COXBU
AccessioniPrimary (citable) accession number: Q83CL8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: October 1, 2014
This is version 75 of the entry and version 2 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, Reference proteome

Documents

  1. Coxiella burnetii
    Coxiella burnetii (strain RSA 493): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3