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D8HS12 (D8HS12_AMYMU) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Fumarate hydratase class II HAMAP-Rule MF_00743
Short name=Fumarase C HAMAP-Rule MF_00743
EC=4.2.1.2 HAMAP-Rule MF_00743
Gene names
Name:aspA EMBL ADJ43953.1
Synonyms:fumC HAMAP-Rule MF_00743
Ordered Locus Names:AMED_2149
OrganismAmycolatopsis mediterranei (strain U-32) [Complete proteome] [HAMAP] EMBL ADJ43953.1
Taxonomic identifier749927 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Pseudonocardineae › Pseudonocardiaceae › Amycolatopsis ›

Protein attributes

Sequence length463 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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. HAMAP-Rule MF_00743

Sequence similarities

Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. HAMAP-Rule MF_00743

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region140 – 1423Substrate binding By similarity HAMAP-Rule MF_00743

Sites

Binding site1011Substrate By similarity HAMAP-Rule MF_00743

Sequences

Sequence LengthMass (Da)Tools
D8HS12 [UniParc].

Last modified October 5, 2010. Version 1.
Checksum: 28089059CE8737FD

FASTA46348,788
        10         20         30         40         50         60 
MTTRREHDLL GDKDVPADAY WGVHTARARE NFPITGTTIA AYPHLVEALA SVKEAAARAN 

        70         80         90        100        110        120 
AELGLLSPDI ADAITAACRE IREGALHGEF VVDVIQGGAG TSTNMNANEV IANRALELLG 

       130        140        150        160        170        180 
HAKGDYHVVH PNEHVNLSQS TNDAYPTAVN VATIIAVRQL SEAMIVLEKA FAAKAVEFHD 

       190        200        210        220        230        240 
VLKMGRTQLQ DAVPMTLGQE FGTYAVMLGE DQQRLGEAVA LLHEINLGAT AIGTGLNAAP 

       250        260        270        280        290        300 
GYAEAACRHL REITGLPVVT AADLVEATQD CGAFVHLSGV LKRIAVKLSK SCNDLRLLSS 

       310        320        330        340        350        360 
GPRAGLNEIN LPPVQAGSSI MPGKINPVIP EVVNQVAFEV IGNDVTVTMA AEAGQLQLNA 

       370        380        390        400        410        420 
FEPIILHSLS ESITHLGAAC RTLATKCVSG ITANVDVMRA YVENSIGLVT ALNPSIGYAA 

       430        440        450        460 
ATEIAKEALE TGRGVAELVV EKGLIPAEEL ARLLRPETLA RAT

« Hide

References

[1]"Complete genome sequence of the rifamycin SV-producing Amycolatopsis mediterranei U32 revealed its genetic characteristics in phylogeny and metabolism."
Zhao W., Zhong Y., Yuan H., Wang J., Zheng H., Wang Y., Cen X., Xu F., Bai J., Han X., Lu G., Zhu Y., Shao Z., Yan H., Li C., Peng N., Zhang Z., Zhang Y. expand/collapse author list , Lin W., Fan Y., Qin Z., Hu Y., Zhu B., Wang S., Ding X., Zhao G.P.
Cell Res. 20:1096-1108(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: U-32.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002000 Genomic DNA. Translation: ADJ43953.1.
RefSeqYP_003764355.1. NC_014318.1.

3D structure databases

ProteinModelPortalD8HS12.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADJ43953; ADJ43953; AMED_2149.
GeneID9436360.
KEGGamd:AMED_2149.
PATRIC42151339. VBIAmyMed151214_2220.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000061737.
KOK01744.

Enzyme and pathway databases

UniPathwayUPA00223; UER01007.

Family and domain databases

Gene3D1.10.275.10. 1 hit.
HAMAPMF_00743. FumaraseC.
InterProIPR004708. ApsA.
IPR005677. Fum_hydII.
IPR024083. Fumarase/histidase_N.
IPR018951. Fumarase_C_C.
IPR000362. Fumarate_lyase.
IPR020557. Fumarate_lyase_CS.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]
PfamPF10415. FumaraseC_C. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSPR00149. FUMRATELYASE.
SUPFAMSSF48557. L-Aspartase-like. 1 hit.
TIGRFAMsTIGR00839. aspA. 1 hit.
PROSITEPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameD8HS12_AMYMU
AccessionPrimary (citable) accession number: D8HS12
Entry history
Integrated into UniProtKB/TrEMBL: October 5, 2010
Last sequence update: October 5, 2010
Last modified: May 1, 2013
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info