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Database: UniProt
Entry: A0A291JQP5_9GAMM
LinkDB: A0A291JQP5_9GAMM
Original site: A0A291JQP5_9GAMM 
ID   A0A291JQP5_9GAMM        Unreviewed;       664 AA.
AC   A0A291JQP5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   18-SEP-2019, entry version 11.
DE   RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE            EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN   ORFNames=CLM76_02375 {ECO:0000313|EMBL:ATH76526.1};
OS   Halomonas hydrothermalis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=115561 {ECO:0000313|EMBL:ATH76526.1, ECO:0000313|Proteomes:UP000217920};
RN   [1] {ECO:0000313|EMBL:ATH76526.1, ECO:0000313|Proteomes:UP000217920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y2 {ECO:0000313|EMBL:ATH76526.1,
RC   ECO:0000313|Proteomes:UP000217920};
RX   PubMed=27315164; DOI=10.1007/s00792-016-0852-8;
RA   Cui Y., Cheng B., Meng Y., Li C., Yin H., Xu P., Yang C.;
RT   "Expression and functional analysis of two NhaD type antiporters from
RT   the halotolerant and alkaliphilic Halomonas sp. Y2.";
RL   Extremophiles 20:631-639(2016).
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:
CC       Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + acetyl-CoA =
CC         (R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysyl-[protein] + CoA;
CC         Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-
CC         COMP:10478, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:83100, ChEBI:CHEBI:83111; EC=2.3.1.12;
CC         Evidence={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; CP023656; ATH76526.1; -; Genomic_DNA.
DR   KEGG; hhh:CLM76_02375; -.
DR   KO; K00627; -.
DR   Proteomes; UP000217920; Chromosome.
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; 3.30.559.10; -; 1.
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; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR43178:SF2; PTHR43178:SF2; 4.
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.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361137};
KW   Complete proteome {ECO:0000313|Proteomes:UP000217920};
KW   Glycolysis {ECO:0000256|RuleBase:RU361137};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00065550};
KW   Pyruvate {ECO:0000313|EMBL:ATH76526.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000217920};
KW   Transferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:ATH76526.1}.
FT   DOMAIN        3     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      119    193       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      234    308       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      362    399       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       70    128       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      199    243       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      317    356       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS     82     98       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    324    338       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   664 AA;  69577 MW;  D51D8995535A2792 CRC64;
     MSSEIIKVPD IGGDTDVEII EIAVSEGDVI EAEDTLITLE SDKASMDVPA PKGGKVVKVL
     VKEGDKVSEG DDIVELEVEG GSDAEPEAKA DSAAEEAPAP KQEEAPAPAA KKASGGKQTV
     DIKVPDLGGS DNVEIIEVAV GEGDDVNAED TLITLESDKA SMDVPSPHSG KIVSLTVKEG
     DTVSEGDVIG KMEIAGGDDA ADEEPAKAEQ PAPASEPAEE EAAEEESGSG EPERKEIRVP
     DLSGSADVPI IEIGVSVGDE VDVEDPLITL ESDKASMDVP SPYKGKLVEL TVKEGDTVSE
     GDVIGYMEVA GAKKAAPKKA APEKASQSSV SPASAKPAAS GGTPSPEAQM AAHKPRDGKL
     VHAGPAVRML ARELGVDLGL VKPSGPKERV LKEDVQAYVK QVMANQGSAQ AAAPAASGGA
     GIPAVPEVDF SQFGEVEEKP MGRLLKMGAT NLHRSWLNVP HVTQFDEADI TELEDFRKAM
     KAEAEAQGAK LTPLPFLVKA CAFALRKYPQ FNVSLKGDGD TLVWKKYVHI GIAVDTPDGL
     MVPVLRDADK KSLIEIAKEM AELGKKAQTK KLKRDEMTGG CFTISSLGSI GGTAFTPIVN
     APEVAILGVS KAQMKPVWDG NAFQPRLMMP LSLSYDHRAI NGADAARFTA FLADVLTDIR
     RLLL
//
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