ID A0A179DMJ2_9SPHI Unreviewed; 462 AA.
AC A0A179DMJ2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=A5893_03905 {ECO:0000313|EMBL:OAQ42265.1};
OS Pedobacter psychrophilus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1826909 {ECO:0000313|EMBL:OAQ42265.1, ECO:0000313|Proteomes:UP000078459};
RN [1] {ECO:0000313|EMBL:OAQ42265.1, ECO:0000313|Proteomes:UP000078459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 8644 {ECO:0000313|EMBL:OAQ42265.1,
RC ECO:0000313|Proteomes:UP000078459};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAQ42265.1, ECO:0000313|Proteomes:UP000078459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 8644 {ECO:0000313|EMBL:OAQ42265.1,
RC ECO:0000313|Proteomes:UP000078459};
RA Svec P.;
RT "Pedobacter psychrophilus sp. nov., isolated from Antarctic fragmentary
RT rock.";
RL Submitted (JUN-2016) 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 -!- 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:OAQ42265.1}.
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DR EMBL; LWHJ01000011; OAQ42265.1; -; Genomic_DNA.
DR RefSeq; WP_068821294.1; NZ_LWHJ01000011.1.
DR AlphaFoldDB; A0A179DMJ2; -.
DR STRING; 1826909.A5893_03905; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000078459; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 1.
DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
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; 1.
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; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000078459};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 141..181
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 181..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 462 AA; 50908 MW; 192969BE5C89B232 CRC64;
MAQYELLLPK MGESVAEATV IRWEKNPGDN IAIDDTILEI ATDKVDSEVP SPVSGKMVKH
LFNENDVAQV GDVIAIIEIE SDTAVAEEVK DAELESLEKA TEIPFVPEEK EETIEDKVEE
VKTEETDEVK QPNNFSSSDR FYSPLVKSIA QEEGISVEQL DNIKGSGSEG RVTKDDLLDF
ISSKNNNNSQ TKDQINTTSS QEPVESKKQE TPATEPAKVV QPVAKSGGDE IIEMDRMRKL
IADHMVSSKQ TSPHVTSFIE VDVTNMVNWR NKVKTSFEKR EGEKITFTPI FVEAVAKALK
DLPMVNVSVK GSQIIKKKDI NIGMATALPS GNLIVPVIKN ADQLNLVGLT KSVNDLARRS
RANKLLPDEV QGGTFTVTNL GTFDNTMGTP IINQPQVAIL AVGAIKKKPA VLETEYGDVI
AIRHLMYLSM SYDHRVVDGS LGGMFIKKVA DNLEQWDVNR EI
//