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Database: UniProt
Entry: R8B3R8_9ALTE
LinkDB: R8B3R8_9ALTE
Original site: R8B3R8_9ALTE 
ID   R8B3R8_9ALTE            Unreviewed;       554 AA.
AC   R8B3R8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   05-JUN-2019, entry version 36.
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=MARLIPOL_04260 {ECO:0000313|EMBL:EON93216.1};
OS   Marinobacter lipolyticus SM19.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Marinobacter.
OX   NCBI_TaxID=1318628 {ECO:0000313|EMBL:EON93216.1, ECO:0000313|Proteomes:UP000016540};
RN   [1] {ECO:0000313|EMBL:EON93216.1, ECO:0000313|Proteomes:UP000016540}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM19 {ECO:0000313|EMBL:EON93216.1,
RC   ECO:0000313|Proteomes:UP000016540};
RX   PubMed=23814106;
RA   Papke R.T., de la Haba R.R., Infante-Dominguez C., Perez D.,
RA   Sanchez-Porro C., Lapierre P., Ventosa A.;
RT   "Draft Genome Sequence of the Moderately Halophilic Bacterium
RT   Marinobacter lipolyticus Strain SM19.";
RL   Genome Announc. 1:e00379-13(2013).
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 2 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EON93216.1}.
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DR   EMBL; ASAD01000007; EON93216.1; -; Genomic_DNA.
DR   RefSeq; WP_012136851.1; NZ_KE007306.1.
DR   STRING; 1318628.MARLIPOL_04260; -.
DR   EnsemblBacteria; EON93216; EON93216; MARLIPOL_04260.
DR   PATRIC; fig|1318628.3.peg.845; -.
DR   OrthoDB; 1626282at2; -.
DR   Proteomes; UP000016540; Unassembled WGS sequence.
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; 3.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 2.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 2.
DR   TIGRFAMs; TIGR01348; PDHac_trf_long; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361137};
KW   Complete proteome {ECO:0000313|Proteomes:UP000016540};
KW   Glycolysis {ECO:0000256|RuleBase:RU361137};
KW   Lipoyl {ECO:0000256|RuleBase:RU361137, ECO:0000256|SAAS:SAAS00065550};
KW   Pyruvate {ECO:0000313|EMBL:EON93216.1};
KW   Transferase {ECO:0000256|RuleBase:RU361137,
KW   ECO:0000313|EMBL:EON93216.1}.
FT   DOMAIN        3     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      126    200       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      254    291       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       28     52       Disordered. {ECO:0000256|MobiDB-lite:
FT                                R8B3R8}.
FT   REGION       70    138       Disordered. {ECO:0000256|MobiDB-lite:
FT                                R8B3R8}.
FT   REGION      200    256       Disordered. {ECO:0000256|MobiDB-lite:
FT                                R8B3R8}.
FT   COMPBIAS     82    126       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                R8B3R8}.
FT   COMPBIAS    214    232       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                R8B3R8}.
SQ   SEQUENCE   554 AA;  58811 MW;  223E5906FD3804B2 CRC64;
     MSEQEIKVPD LGGADEVEVI EVLVSQGDSV EEEDPILTVE SDKASVELPS PGAGKITKIT
     VKVGDKVKEG DVVGMMEAAG DAGGSDDDKG TGEQAGTDKD QEAKAQSEDK AEETKPAPKK
     SGGSRKETVK VPPLDGFDNV PVIEINVSVG DEVEVDDALV TVESDKATME IPSPFAGKIG
     KILVSEGDKI SEGLDLVEMT VVEEGGEEPA SEAEEPSGDA RQEGKSEPAG KPEEPKPAPA
     SATYEPPTPG AKVHAGPAVR KLAREFGADL TRIKGSGPKG RILKDDVQAY VKSQLQQTQQ
     GSTVAGGGGA GIPVVKLPDF SQFGDIERES MSRVMFATAN NMQRSWLNVP HVTQFEDADI
     TDMESFRKAQ KAAGEKKGVK MTPLPFLLKA CATALAELPQ FNVSLDMERK EVVRKQYIHI
     GIAVDTPHGL MVPVIRDVDK KGLWELAAES AELAQKARDK QLKPAEMQGA CFTITSLGGI
     GGTAFTPIVN TPEVAILGVS KAAMKPVWDG KDFQPRLMLP LSLSYDHRAV NGADAARFTT
     LLSQLLGDIR SLLL
//
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