ID H6L6Z0_SAPGL Unreviewed; 441 AA.
AC H6L6Z0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
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:AFC26420.1};
GN OrderedLocusNames=SGRA_3699 {ECO:0000313|EMBL:AFC26420.1};
OS Saprospira grandis (strain Lewin).
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Saprospiraceae;
OC Saprospira.
OX NCBI_TaxID=984262 {ECO:0000313|EMBL:AFC26420.1, ECO:0000313|Proteomes:UP000007519};
RN [1] {ECO:0000313|EMBL:AFC26420.1, ECO:0000313|Proteomes:UP000007519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lewin {ECO:0000313|EMBL:AFC26420.1,
RC ECO:0000313|Proteomes:UP000007519};
RX PubMed=22675601; DOI=10.4056/sigs.2445005;
RA Saw J.H., Yuryev A., Kanbe M., Hou S., Young A.G., Aizawa S., Alam M.;
RT "Complete genome sequencing and analysis of Saprospira grandis str. Lewin,
RT a predatory marine bacterium.";
RL Stand. Genomic Sci. 6:84-93(2012).
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; CP002831; AFC26420.1; -; Genomic_DNA.
DR RefSeq; WP_015694010.1; NC_016940.1.
DR AlphaFoldDB; H6L6Z0; -.
DR STRING; 984262.SGRA_3699; -.
DR KEGG; sgn:SGRA_3699; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_1_10; -.
DR Proteomes; UP000007519; 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:AFC26420.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000007519};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:AFC26420.1}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 122..162
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 86..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 441 AA; 47616 MW; F4032B450B33F580 CRC64;
MAKVELIMPK LGESIIEATI LSWEKEVGES VELDENVLTI ATDKVDTEVP SPVEGVLLEI
LHPDGATVAV GAPIAIIETE AEGVEASPAV AEAPQAKEES SAAPQPETAA VVATDFSQSD
RFYSPLVKSI AKEEGIALEE LDNISGTGQN GRVTKHDVLA YLENRKKAPQ AAAPVKKEAP
KAVAPANNGQ QMAVQQFNLP PVDTSGNVEI IEMDRMRKLI ADHMVMSKHV SPHVTSFVEV
DVTNIVQWRK KAKAVYAEKY GEKITFTPIF VEAVTKALQD YPMVNIAVKG NQIVRYKDIN
IGMAAALPTG NLIVPVIKNA DMLNLVGLTK KVNDLANRAR GNKLKPEEIK GGTFTLTNVG
TFGNVMGTPI INQPQVAILA VGAIRKKPAV IETPTGDTIG IRHMMFLSLS YDHRVVDGML
GGSFLRRVGD YLEAFDLNRD I
//
