ID A0A166VC39_9GAMM Unreviewed; 525 AA.
AC A0A166VC39;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=N475_22600 {ECO:0000313|EMBL:KZN32474.1};
OS Pseudoalteromonas luteoviolacea DSM 6061.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1365250 {ECO:0000313|EMBL:KZN32474.1, ECO:0000313|Proteomes:UP000076643};
RN [1] {ECO:0000313|EMBL:KZN32474.1, ECO:0000313|Proteomes:UP000076643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6061 {ECO:0000313|EMBL:KZN32474.1,
RC ECO:0000313|Proteomes:UP000076643};
RA Vynne N.G., Mansson M., Gram L.;
RT "Comparative Genomic and Metabolomic Analysis of Twelve Strains of
RT Pseudoalteromonas luteoviolacea.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZN32474.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AUYB01000132; KZN32474.1; -; Genomic_DNA.
DR RefSeq; WP_063365873.1; NZ_AUYB01000132.1.
DR AlphaFoldDB; A0A166VC39; -.
DR STRING; 43657.S4054249_11770; -.
DR PATRIC; fig|1365250.3.peg.4323; -.
DR Proteomes; UP000076643; Unassembled WGS sequence.
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 Lipoyl {ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000076643};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:KZN32474.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 107..182
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 226..263
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 204..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 525 AA; 56604 MW; 03EAD28B7927E077 CRC64;
MSKEFILPDI GEGIVECEVV EWLVAVGDTV KEDQPICDVM TDKALVQIPA VHDGVITQLH
YEKGDIAKVH EPLFAMDVEG EAAVVEAPSN EDNSAPSVQS TASSSHLEDF ILPDIGEGIV
ECEIVEWLVS EGQEIKEDQA VCDVMTDKAL VQIPAKYDGV VEKLYYQKGD IAQVHSPLFQ
VRIAGAGSAA STTAQSVEEQ LEIHKPQPAP SNGTAINGKP VSGKAVASPA VRRRAREMDI
DIRLVQGSGK NGRVYKEDLE QYLKGGQSQA PVVSAPEKVT STPETAATSS GGTRVEPIRG
MKAAMAKQMV ASVSTIPHFT YSDEIDLTEL IALRLSLKEQ YAKQGIKLTM MPFFIKALSL
AINEFPILNS QVNDDCSQIT YFDDHNIGMA VDSKLGLLVP NIKGCQNKSI VDVAEAVTKL
TDAAREGRVS PDDLKGGTIS ISNIGAIGGT TATPIINKPE VAIVALGKLQ HLPRFDAEGN
VVSRSIMQVS WSGDHRVIDG GTIARFNNLW KAYLEEPAKM MMAMR
//
