ID   A0A1I6RES1_9BACL        Unreviewed;       419 AA.
AC   A0A1I6RES1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=SAMN05444972_10543 {ECO:0000313|EMBL:SFS63241.1};
OS   Marininema halotolerans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC   Marininema.
OX   NCBI_TaxID=1155944 {ECO:0000313|EMBL:SFS63241.1, ECO:0000313|Proteomes:UP000198660};
RN   [1] {ECO:0000313|EMBL:SFS63241.1, ECO:0000313|Proteomes:UP000198660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45789 {ECO:0000313|EMBL:SFS63241.1,
RC   ECO:0000313|Proteomes:UP000198660};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
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DR   EMBL; FPAA01000005; SFS63241.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6RES1; -.
DR   OrthoDB; 9805770at2; -.
DR   Proteomes; UP000198660; 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; 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|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU003423};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Pyruvate {ECO:0000313|EMBL:SFS63241.1};
KW   Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:SFS63241.1}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          116..153
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          84..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          139..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..158
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   419 AA;  46509 MW;  B3B5D4DB2F55B10D CRC64;
     MSVNFHLPDV GEGVAEADVV RWLVKEGETV EEDQTVVEVQ TDKAVVELPS PSAGCVKEIC
     WQEGETVPVG EVLFVIGGKT EASQEIRSKE PSDSLTTTTT ATLPPKTKKD VRTRVLAAPS
     TRRLARELQV DICSVEGTGP QGRVTKEDVH RFSEQKTKKS LSQNDTYSSQ GLATPRTLIS
     ENTFATKHDE IYHDEPLTRT RRLIAERLLK SVTQKPHATH FDELQVDGLV AWRQRIKETG
     NTLGYLPMLI KAVTQSLRHH PLLNAHFLED TQVLRRIRQV DLGIATDTPR GLIVPVLRQV
     DQKSIHEIAE ELTNLTDRAR EGKVTADELK GSTFTISNAG SLGGKWATPI INPPEVGILA
     IHPIEERPVI KEGELTKGWR MNVSLSFDHS VIDGADAIRF TQTLNRYLAD PGTLLLELR
//