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Q8CUH5 (FUMC_OCEIH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:OB1132
OrganismOceanobacillus iheyensis (strain DSM 14371 / JCM 11309 / KCTC 3954 / HTE831) [Complete proteome] [HAMAP]
Taxonomic identifier221109 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeOceanobacillus

Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Pathway

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

Subunit structure

Homotetramer By similarity. HAMAP MF_00743

Subcellular location

Cytoplasm By similarity HAMAP 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. HAMAP MF_00743

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: UniProtKB-KW

   Cellular componenttricarboxylic acid cycle enzyme complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionfumarate hydratase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 461461Fumarate hydratase class II HAMAP MF_00743
PRO_0000161293

Regions

Region127 – 1304B site By similarity
Region137 – 1393Substrate binding By similarity

Sites

Binding site991Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8CUH5 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 44242B3859AA4CDF

FASTA46150,732
        10         20         30         40         50         60 
MDYRVEKDTI GEIQVPADKY WGAQTQRSKQ NFPIGNEKMP VEIIKAFAIL KRSTAEANFE 

        70         80         90        100        110        120 
LGLMERDKME AIQYAADQVL NDSLTDHFPL VVWQTGSGTQ SNMNVNEVLA FVGNKWLQEQ 

       130        140        150        160        170        180 
GSDLKLHPND DVNKSQSSND TYPTAMHIAA VLKLEDTVLP ALSQLKNTFA EKQSAFENIV 

       190        200        210        220        230        240 
KIGRTHLQDA TPLTLGQEIS GWHRMLEKSE TMISESLEHL RELAIGGTAV GTGLNAHPDF 

       250        260        270        280        290        300 
SEKVCKAIST FTNKKFISAK NKFHSLTSHD ETVYAHGALK GLAADLMKIA NDVRWLASGP 

       310        320        330        340        350        360 
RCGIGEITIP ANEPGSSIMP GKVNPTQSEA VTMVVTQVMG NDAAIGFAAS QGNFELNVFK 

       370        380        390        400        410        420 
PVIAYNFLQS SQLLADSIIS FDERCAVGIE PNHEQIEKNL NDSLMLVTAL NPHIGYENAA 

       430        440        450        460 
KIAKKAFADN STLKETAVEL GLLTEEQFDE YVNPEEMTYP K 

« Hide

References

[1]"Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge and its unexpected adaptive capabilities to extreme environments."
Takami H., Takaki Y., Uchiyama I.
Nucleic Acids Res. 30:3927-3935(2002) [PubMed: 12235376] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 14371 / JCM 11309 / KCTC 3954 / HTE831.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000028 Genomic DNA. Translation: BAC13088.1.
RefSeqNP_692053.1. NC_004193.1.

3D structure databases

ProteinModelPortalQ8CUH5.
SMRQ8CUH5. Positions 4-457.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1017212.
GenomeReviewsGene locus OB1132 in contig BA000028_GR.
KEGGoih:OB1132.
NMPDRfig|221109.1.peg.1133.
PATRIC22793268. VBIOceIhe82024_1151.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG284369.
OMARIEKDTM.
PhylomeDBQ8CUH5.
ProtClustDBPRK00485.

Enzyme and pathway databases

BioCycOIHE221109:OB1132-MONOMER.

Family and domain databases

HAMAPMF_00743. FumaraseC.
[Tree]
InterProIPR005677. Fum_hydII.
IPR018951. Fumarase_C_C.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
IPR008948. L-Aspartase-like.
IPR024083. L-Aspartase-like_N.
IPR022761. Lyase1_N.
[Graphical view]
Gene3DG3DSA:1.10.275.10. G3DSA:1.10.275.10. 1 hit.
KOK01679.
PfamPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
SUPFAMSSF48557. L-Aspartase-like. 1 hit.
TIGRFAMsTIGR00979. FumC_II. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFUMC_OCEIH
AccessionPrimary (citable) accession number: Q8CUH5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families