ID M4ZRJ9_9FLAO Unreviewed; 397 AA.
AC M4ZRJ9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=BPAA_005 {ECO:0000313|EMBL:BAM99312.1};
OS Blattabacterium cuenoti BPAA.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Blattabacteriaceae; Blattabacterium.
OX NCBI_TaxID=1229512 {ECO:0000313|EMBL:BAM99312.1, ECO:0000313|Proteomes:UP000011815};
RN [1] {ECO:0000313|EMBL:BAM99312.1, ECO:0000313|Proteomes:UP000011815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BPAA {ECO:0000313|EMBL:BAM99312.1,
RC ECO:0000313|Proteomes:UP000011815};
RX PubMed=23515978; DOI=10.1098/rsbl.2012.1153;
RA Tokuda G., Elbourne L.D.H., Kinjo Y., Saitoh S., Sabree Z., Hojo M.,
RA Yamada A., Hayashi Y., Shigenobu S., Bandi C., Paulsen I.T., Watanabe H.,
RA Lo N.;
RT "Maintenance of essential amino acid synthesis pathways in the
RT Blattabacterium cuenoti symbiont of a wood-feeding cockroach.";
RL Biol. Lett. 9:20121153-20121153(2013).
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; AP012548; BAM99312.1; -; Genomic_DNA.
DR RefSeq; WP_015429631.1; NC_020510.1.
DR AlphaFoldDB; M4ZRJ9; -.
DR STRING; 1229512.BPAA_005; -.
DR KEGG; blp:BPAA_005; -.
DR PATRIC; fig|1229512.3.peg.5; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_1_10; -.
DR Proteomes; UP000011815; Chromosome.
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|RuleBase:RU003423,
KW ECO:0000313|EMBL:BAM99312.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:BAM99312.1}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 97..137
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 397 AA; 44903 MW; C7914BCBD897598A CRC64;
MAEYNLPLPA MGESIAEATI IRWLKKEGDF VKKEDLLVEI ATDKVNSEIS SPVNGILKKK
LFAPNEVAKV GNFIAILETE EKFLEDIPII EKRKKRFYSP LVRTIAQREG ISFYELETIE
GTGEKERVTK KDILKYIRIK KNNIVIPKYN RYNSIQSINK NQNEKIVEMD RMRRITAEHM
IRSKNISAHV TSFVEADVTN IVKWREKIKD TFQKNTGEKL TLMSIFVECV VKAIKDLPMI
NISVNGTSII KKKNIHIGLA TALPNGNLIV PVIKNADSYN LIGLIKIIND LIKRAKSNQL
KPEEIQGGTY TISNIGSFGN LFGTPIIHQP QVAILAIGVI QKKLSIIETP KGDLIGIRHK
IYLSHSYDHR VIDGVLGGCF AKKVALYLEE FNCYTKI
//
