(data stored in ACNUC7421 zone)

SWISSPROT: Q3IIH7_PSEHT

ID   Q3IIH7_PSEHT            Unreviewed;       654 AA.
AC   Q3IIH7;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 89.
DE   RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE            EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN   Name=aceF {ECO:0000313|EMBL:CAI85490.1};
GN   OrderedLocusNames=PSHAa0392 {ECO:0000313|EMBL:CAI85490.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85490.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85490.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2).
CC       {ECO:0000256|RuleBase:RU361137}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine
CC       = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
CC       {ECO:0000256|RuleBase:RU361137}.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU361137};
CC       Note=Binds 3 lipoyl cofactors covalently.
CC       {ECO:0000256|RuleBase:RU361137};
CC   -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC       symmetry. {ECO:0000256|RuleBase:RU361137}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU361137}.
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DR   EMBL; CR954246; CAI85490.1; -; Genomic_DNA.
DR   RefSeq; WP_011327103.1; NC_007481.1.
DR   ProteinModelPortal; Q3IIH7; -.
DR   STRING; 326442.PSHAa0392; -.
DR   EnsemblBacteria; CAI85490; CAI85490; PSHAa0392.
DR   KEGG; pha:PSHAa0392; -.
DR   PATRIC; fig|326442.8.peg.376; -.
DR   eggNOG; ENOG4107QSN; Bacteria.
DR   eggNOG; COG0508; LUCA.
DR   HOGENOM; HOG000281562; -.
DR   KO; K00627; -.
DR   OMA; TMEFESF; -.
DR   OrthoDB; POG091H05OF; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.320.10; -; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR006256; AcTrfase_Pyrv_DH_cplx.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR004167; E3-bd.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR43178:SF4; PTHR43178:SF4; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 3.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 3.
DR   TIGRFAMs; TIGR01348; PDHac_trf_long; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 3.
DR   PROSITE; PS00189; LIPOYL; 3.
PE   3: Inferred from homology;
DR   PRODOM; Q3IIH7.
DR   SWISS-2DPAGE; Q3IIH7.
KW   Acyltransferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:CAI85490.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Glycolysis {ECO:0000256|RuleBase:RU361137};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00100674};
KW   Pyruvate {ECO:0000313|EMBL:CAI85490.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   Transferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:CAI85490.1}.
FT   DOMAIN        2     75       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      116    189       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      221    294       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   654 AA;  68402 MW;  EDC3B317785CFFE9 CRC64;
     MSIEIKVPDI GGDEVEVTEI LVAVGDVVEV DQALLTVEGD KASMEVPADT AGTVKEIKVS
     VGDNVATGSL VFIFEGESEG ESADKSASAD KSDSAAEQKT PATDAKPAPA ASGSTAQDVT
     LPDIGDDEVE VTEILVAVGD SVSEDQSILS VEGDKASMEV PAPFAGTVKE IKVATGDTVK
     TGSLVFVFEV AGSESAAPAA ESTPAETKAA PAAEQSSVSS TKEVNVPDIG GDEVEVTEVL
     VAVGDSVTED QSLLNVEGDK AAMELPAPFA GTVKEIKVAT GDKVSTGSLI FVFEVAGGAP
     AAAAKPEAEK SAPAAKSEKP APKAETATQS APAASNESFA DNSAYAHASP VVRRLAREFG
     INLANVKGSG RKNRVVKDDV QNYVKNLVKQ VESGQLSADK GNAGGSELGL IPWPKVDFAK
     FGEIEEKKLS RIQKLSGKNL HRNWVQIPHV TQFDEADITS LEEFRKEQNA LNEKKKLGVK
     ITPLVFVMKA AAKALAEFPT INSSLSNDGE SLILKKYINI GVAVDTPNGL VVPVFKDVDK
     KGIIELSREL MEVSAKARDG KLTSADMQGG CFTISSLGGI GGTAFTPIVN APEVAILGVS
     KSEMKPKWNG KEFEPKLMVP LSMSYDHRVI DGALAARFTV TLASYMSDIR QLVM
//

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