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Q5R0P0 (Q5R0P0_IDILO) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 69. 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:
Acetyltransferase component of pyruvate dehydrogenase complex RuleBase RU361137

EC=2.3.1.12 RuleBase RU361137
Gene names
Name:aceF EMBL AAV81302.1
Ordered Locus Names:IL0459 EMBL AAV81302.1
OrganismIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP] EMBL AAV81302.1
Taxonomic identifier283942 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesIdiomarinaceaeIdiomarina

Protein attributes

Sequence length591 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2 By similarity. RuleBase RU361137

Catalytic activity

Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine. RuleBase RU361137

Cofactor

Binds 1 lipoyl cofactor covalently By similarity. RuleBase RU361137

Binds 2 lipoyl cofactors covalently By similarity. RuleBase RU361137

Binds 3 lipoyl cofactors covalently By similarity. RuleBase RU361137

Subunit structure

Forms a 24-polypeptide structural core with octahedral symmetry By similarity. RuleBase RU361137

Sequence similarities

Belongs to the 2-oxoacid dehydrogenase family. RuleBase RU361137

Contains 2 lipoyl-binding domains. RuleBase RU361137

Ontologies

Sequences

Sequence LengthMass (Da)Tools
Q5R0P0 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: E629A0E5DB153606

FASTA59163,846
        10         20         30         40         50         60 
MADQIELKVP DVGGEEVEVI EILVSEGDTV EQEDGIVTVE SDKASMDIPA SSGGKITELK 

        70         80         90        100        110        120 
VKVGDTISEG DVLAMIEASG GADESDESDS EEEAEDKTDD KADEEATKDK AEESEDKQEE 

       130        140        150        160        170        180 
EKDEDSEPEK KSSGGGSKVI DVEVPDIGDE EDVEIIEILV SKGDSVSAED GLITLETDKA 

       190        200        210        220        230        240 
TMDVPCPEDG EIEEMLVKVG DKVSQGSVIA KLKVSGGADD SEAEEKDSAK EEKSESNKES 

       250        260        270        280        290        300 
DKDSGKKSED KDQKKDSGSS VKPSSERQPP VPDHPSQRSD RKEGILHASP AVRRVAREFG 

       310        320        330        340        350        360 
VDLSQVKGSG PKDRILKEDV QEFVKYELSR PKAVAGATGQ GGGGLQVIDP PKVDFSKFGE 

       370        380        390        400        410        420 
VEEVQLSRIQ RKSGPNLHRN WVTIPHVTQF DEADITELEN FRKSENEVAK KKDLGFKITP 

       430        440        450        460        470        480 
LVFILKACAK GLREFPTFNS SLSESGESLY MKKYVNIGVA VDTPNGLVVP VIRDVDKKGI 

       490        500        510        520        530        540 
YELSEELVEI SSKARDGKLK ATDMQGGCFS ISSLGGIGGT AFTPIVNAPD VAILGVSRNE 

       550        560        570        580        590 
MKPKWNGKEF EPRLTLPLSL SYDHRVIDGA EAARFTAYLS GVLGDIRKLV L 

« Hide

References

[1]"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy."
Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. expand/collapse author list , Aizawa S., Shibata S., Malahoff A., Alam M.
Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017340 Genomic DNA. Translation: AAV81302.1.
RefSeqYP_154851.1. NC_006512.1.

3D structure databases

ProteinModelPortalQ5R0P0.
SMRQ5R0P0. Positions 5-82, 351-591.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING283942.IL0459.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV81302; AAV81302; IL0459.
GeneID3173448.
KEGGilo:IL0459.
PATRIC22138939. VBIIdiLoi21852_0461.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000281562.
KOK00627.
OMAFWHVSEG.
OrthoDBEOG610413.

Enzyme and pathway databases

BioCycILOI283942:GI0U-462-MONOMER.

Family and domain databases

Gene3D3.30.559.10. 1 hit.
4.10.320.10. 1 hit.
InterProIPR003016. 2-oxoA_DH_lipoyl-BS.
IPR001078. 2-oxoacid_DH_actylTfrase.
IPR006256. AcTrfase_Pyrv_DH_cplx.
IPR000089. Biotin_lipoyl.
IPR023213. CAT-like_dom.
IPR004167. E3-bd.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamPF00198. 2-oxoacid_dh. 1 hit.
PF00364. Biotin_lipoyl. 2 hits.
PF02817. E3_binding. 1 hit.
[Graphical view]
SUPFAMSSF47005. SSF47005. 1 hit.
SSF51230. SSF51230. 2 hits.
TIGRFAMsTIGR01348. PDHac_trf_long. 1 hit.
PROSITEPS50968. BIOTINYL_LIPOYL. 2 hits.
PS00189. LIPOYL. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameQ5R0P0_IDILO
AccessionPrimary (citable) accession number: Q5R0P0
Entry history
Integrated into UniProtKB/TrEMBL: January 4, 2005
Last sequence update: January 4, 2005
Last modified: July 9, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)