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Reviewed, UniProtKB/Swiss-Prot Q92GW0 (FUMC_RICCN)

Last modified November 3, 2009. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: RC1012
OrganismRickettsia conorii [Complete proteome] [HAMAP]
Taxonomic identifier781 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length463 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

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

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle. HAMAP MF_00743

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

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 termComplete proteome
Gene Ontology (GO)
   Biological processfumarate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: HAMAP

   Cellular componenttricarboxylic acid cycle enzyme complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionfumarate hydratase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 463463Fumarate hydratase class II HAMAP MF_00743
PRO_0000161306

Regions

Region129 – 1324B site By similarity
Region139 – 1413Substrate binding By similarity

Sites

Binding site1001Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92GW0-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: BA74C64811FC5359

FASTA46350,839
        10         20         30         40         50         60 
MKNYRTESDS FGEIQIEEKF YWGAQTQRSL ENFKIGKQKM PEILIRALAI LKKCAAQVNH 

        70         80         90        100        110        120 
EFGDLEAKIA ISIDKATDRI LEGEFEDNFP LVVWQTGSGT QTNMNMNEVI ASIANEELTG 

       130        140        150        160        170        180 
KKGGKSPVHP NDHVNKGQSS NDSFPTAMHI ATVLATKQQL IPALNNILTS LQDKSKDWDK 

       190        200        210        220        230        240 
IIKIGRTHLQ DATPLTLKQE FSGYITQIEY ALERIENALQ KVYLLAQGGT AVGTGINSKI 

       250        260        270        280        290        300 
GFDIKFAEKV AEFTKQPFKT APNKFESLAA HDALVEFSGT LNTIAVSLMK IANDIRLLGS 

       310        320        330        340        350        360 
GPRCGLGELH LPENEPGSSI MPGKVNPTQV EALTMVCSQV MGNHVTVTIA GSNGHLELNV 

       370        380        390        400        410        420 
FKPVIIYNIL QSIELLSDSV NSFVTHCVKG LEPNIARIND LRDKSLMLVT ALNPHIGYDN 

       430        440        450        460 
AAKIAKEAHK HGITLKEAAK KLNLLSEAKF DKIVVPEKMV SQS 

« Hide

References

[1]"Mechanisms of evolution in Rickettsia conorii and R. prowazekii."
Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.
Science 293:2093-2098(2001) [PubMed: 11557893] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases

AE006914 Genomic DNA. Translation: AAL03550.1.
PIRD97826.
RefSeqNP_360649.1.

3D structure databases

HSSPHSSP built from PDB template 1YFM based on UniProtKB P08417.
ModBaseSearch...

Genome annotation databases

GeneID928156.
GenomeReviewsGene locus RC1012 in contig AE006914_GR.
KEGGrco:RC1012.
NMPDRfig|272944.1.peg.1012.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ92GW0.
OMAGSQGHFE.

Enzyme and pathway databases

BioCycRCON272944:RC1012-MON.
BRENDA4.2.1.2. 267518.

Family and domain databases

HAMAPMF_00743.
[Tree]
InterProIPR003031. D_crystallin.
IPR005677. Fum_hydII.
IPR018951. Fumarase_C_C.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
[Graphical view]
PfamPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00145. ARGSUCLYASE.
PR00149. FUMRATELYASE.
TIGRFAMsTIGR00979. fumC_II. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUMC_RICCN
AccessionPrimary (citable) accession number: Q92GW0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 1, 2001
Last modified: November 3, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

Rickettsia conorii

(strain Malish 7): entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents