ID G7SQR5_9FLAO Unreviewed; 375 AA.
AC G7SQR5;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN Name=sucB {ECO:0000313|EMBL:AER40334.1};
GN ORFNames=MADAR_005 {ECO:0000313|EMBL:AER40334.1};
OS Blattabacterium sp. (Mastotermes darwiniensis) str. MADAR.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Blattabacteriaceae; Blattabacterium.
OX NCBI_TaxID=1074889 {ECO:0000313|EMBL:AER40334.1, ECO:0000313|Proteomes:UP000006133};
RN [1] {ECO:0000313|EMBL:AER40334.1, ECO:0000313|Proteomes:UP000006133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MADAR {ECO:0000313|EMBL:AER40334.1,
RC ECO:0000313|Proteomes:UP000006133};
RX PubMed=22020505; DOI=10.1128/AEM.06540-11;
RA Sabree Z.L., Huang C.Y., Arakawa G., Tokuda G., Lo N., Watanabe H.,
RA Moran N.A.;
RT "Genome shrinkage and loss of nutrient-providing potential in the obligate
RT symbiont of the primitive termite Mastotermes darwiniensis.";
RL Appl. Environ. Microbiol. 0:0-0(2011).
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; CP003000; AER40334.1; -; Genomic_DNA.
DR RefSeq; WP_014158496.1; NC_016146.1.
DR AlphaFoldDB; G7SQR5; -.
DR STRING; 1074889.MADAR_005; -.
DR KEGG; bmm:MADAR_005; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_1_10; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000006133; 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 Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 88..128
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 375 AA; 42167 MW; EEE3FC293AA5660D CRC64;
MAEYNLTLPS MGESIAEATI IRWLKKEGDS VKKEDLLVEI ATDKVDSEIY SPVNGILKKK
LFYPNEVAKV GSSIAILEIE EKNIGTRFYS PFVRTLAHQE GISFYELESI EGTGKKGRVT
KKDILKYIQN KKENILHPHN EEIIEMDRIR QITASHMISS KNISAHVTSF VEADVTNIVK
WRNKMKDIFQ KNTGEKLTLM SVFVKCVVKA IKDLPMINIS VHGTNIIKKK NIHIGLATAL
PNGNLIVPVI KHADSYSLRG LIKIINDLIR RAKSNQLKPE ETQGGTYTIS NIGSFGNIFG
TPIIHQPQVA IMAIGLIQKK LSIIETPKGD FIGIRHKIYL SHSYDHRVIN GELGGEFAKK
VALYLEEFNC YTKII
//
