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Q83CL8 (FUMC_COXBU) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fumarate hydratase class II

Short name=Fumarase C
EC=4.2.1.2
Gene names
Name:fumC
Ordered Locus Names:CBU_1096
OrganismCoxiella burnetii (strain RSA 493 / Nine Mile phase I) [Reference proteome] [HAMAP]
Taxonomic identifier227377 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length459 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible addition of water to fumarate to give L-malate By similarity. HAMAP-Rule MF_00743

Catalytic activity

(S)-malate = fumarate + H2O. HAMAP-Rule MF_00743

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. HAMAP-Rule MF_00743

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00743

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00743.

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.

Sequence similarities

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

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentCytoplasm
   Molecular functionLyase
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfumarate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componenttricarboxylic acid cycle enzyme complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionfumarate hydratase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 459459Fumarate hydratase class II HAMAP-Rule MF_00743
PRO_0000161273

Regions

Region95 – 973Substrate binding By similarity
Region126 – 1294B site By similarity
Region136 – 1383Substrate binding By similarity
Region184 – 1852Substrate binding By similarity
Region321 – 3233Substrate binding By similarity

Sites

Active site1851Proton donor/acceptor By similarity
Active site3151 By similarity
Binding site3161Substrate By similarity
Site3281Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q83CL8 [UniParc].

Last modified December 15, 2003. Version 2.
Checksum: 15153802D24B2359

FASTA45949,850
        10         20         30         40         50         60 
MRKESDSMGT IEVPSEKYYG AQSQRSLINF AIGRETMPPE LIRAFGVLKK AAVLTNVELG 

        70         80         90        100        110        120 
KVSQEKANFI LKACEELIAG KLNDHFPLKI WQTGSGTQTN MNVNEVISNR AIELAGGKLG 

       130        140        150        160        170        180 
SKEPVHPNDH VNMSQSSNDT FPTAMHITAA EMITHQLIPN LTVLRDTLEK KSKEFSEIIK 

       190        200        210        220        230        240 
IGRTHLQDAV PLTLGQEFSG YVAQLNHNLE AINDVLPTLY RLALGGTAVG TGLNTHPQFA 

       250        260        270        280        290        300 
KKAADHIAEL TGIPFYSASN KFAALAANDE IVLVSGVLKT LACSLMKIAN DIRWLASGPR 

       310        320        330        340        350        360 
CGIGEIVIPE NEPGSSIMPG KVNPTQSEAM TMVCVQVIGN DTTITIAGSQ GNFELNVYKP 

       370        380        390        400        410        420 
VMAYNLIQSI YLLSDACRSF NDHCAVGIKP NQEKINDYLN NSLMLVTALN QIIGYDKASE 

       430        440        450 
IAKKAYKEGT TLKEAALQLG YLTASEFDKA VDPKKMVAI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016828 Genomic DNA. Translation: AAO90609.2.
RefSeqNP_820095.2. NC_002971.3.

3D structure databases

ProteinModelPortalQ83CL8.
SMRQ83CL8. Positions 1-457.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227377.CBU_1096.

Proteomic databases

PRIDEQ83CL8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO90609; AAO90609; CBU_1096.
GeneID1208998.
KEGGcbu:CBU_1096.
PATRIC17930925. VBICoxBur82552_1090.

Phylogenomic databases

eggNOGCOG0114.
HOGENOMHOG000061736.
KOK01679.
OMARIEKDTM.
OrthoDBEOG6V1M4M.
ProtClustDBPRK00485.

Enzyme and pathway databases

BioCycCBUR227377:GJ7S-1090-MONOMER.
UniPathwayUPA00223; UER01007.

Family and domain databases

Gene3D1.10.275.10. 1 hit.
HAMAPMF_00743. FumaraseC.
InterProIPR005677. 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]
PANTHERPTHR11444. PTHR11444. 1 hit.
PfamPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
SUPFAMSSF48557. SSF48557. 1 hit.
TIGRFAMsTIGR00979. fumC_II. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUMC_COXBU
AccessionPrimary (citable) accession number: Q83CL8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: March 19, 2014
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Coxiella burnetii

Coxiella burnetii (strain RSA 493): entries and gene names