ID G0B044_9GAMM Unreviewed; 540 AA.
AC G0B044;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN ORFNames=Sbal175_2268 {ECO:0000313|EMBL:AEG11521.1};
OS Shewanella baltica BA175.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=693974 {ECO:0000313|EMBL:AEG11521.1, ECO:0000313|Proteomes:UP000002249};
RN [1] {ECO:0000313|EMBL:AEG11521.1, ECO:0000313|Proteomes:UP000002249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BA175 {ECO:0000313|EMBL:AEG11521.1,
RC ECO:0000313|Proteomes:UP000002249};
RX PubMed=22328742; DOI=10.1128/JB.06468-11;
RA Caro-Quintero A., Auchtung J., Deng J., Brettar I., Hofle M., Tiedje J.M.,
RA Konstantinidis K.T.;
RT "Genome sequencing of five Shewanella baltica strains recovered from the
RT oxic-anoxic interface of the Baltic Sea.";
RL J. Bacteriol. 194:1236-1236(2012).
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938,
CC ECO:0000256|RuleBase:RU003423};
CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry. {ECO:0000256|ARBA:ARBA00011484}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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DR EMBL; CP002767; AEG11521.1; -; Genomic_DNA.
DR RefSeq; WP_006081588.1; NC_017571.1.
DR AlphaFoldDB; G0B044; -.
DR KEGG; sbb:Sbal175_2268; -.
DR HOGENOM; CLU_016733_10_0_6; -.
DR Proteomes; UP000002249; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 2.
DR Gene3D; 2.40.50.100; -; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 1.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
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; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 2.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 2.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW ECO:0000313|EMBL:AEG11521.1}; Lipoyl {ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:AEG11521.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 120..195
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 232..269
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 286..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 540 AA; 58145 MW; 322CD3E3DA864AD2 CRC64;
MIKDFILPDI GEGVVECELV EWLVKEGDTV VEDQPIADVM TDKALVQIPA PFAGVVTKLY
YAKGDIAKVH APLYAVQIEG AVEIASEESI ATEPAATTSK VTEPVAATTA NTSSSSSVSI
EEFLLPDIGE GIVECELVEW LVSEGDWVEE DQPIADVMTD KALVQIPAIK AGKIAKLHYR
KGQLAKVHAP LFAIEVEQAA SAPATTNTDT VANAAPTAQI VSAEPARQGK ALASPAVRRM
ARSLDIDLSQ VPGTGKHGRV YKEDITRFQQ GASNVSASSA TQVKEAPVQA TQASQTQVPT
STVTQRADTV EPIRGVKAVM ARMMVESVSS IPHFTYCEEF DLTDLVALRE SMKVKYSSDE
VKLTMMPFFM KSMSLALSQF PVMNSQVNAD CTELTYKARH NIGMAVDSKV GLLVPNIKDV
QDKSILEVAA EITRLTQAAR SGRVAPADLK DGTISISNIG ALGGTVATPI INKPEVAIVA
LGKLQTLPRF NAKGEVEARQ IMQVSWSGDH RVIDGGTIAR FCNLWKQYLE QPQEMLLAMR
//
