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Database: UniProt
Entry: A0A0B8T7H6_9SPHI
LinkDB: A0A0B8T7H6_9SPHI
Original site: A0A0B8T7H6_9SPHI 
ID   A0A0B8T7H6_9SPHI        Unreviewed;       451 AA.
AC   A0A0B8T7H6;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
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=DI53_2581 {ECO:0000313|EMBL:KGE13660.1};
OS   Sphingobacterium deserti.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=1229276 {ECO:0000313|EMBL:KGE13660.1, ECO:0000313|Proteomes:UP000031802};
RN   [1] {ECO:0000313|Proteomes:UP000031802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACCC05744 {ECO:0000313|Proteomes:UP000031802};
RA   Teng C., Zhou Z., Li X., Chen M., Lin M., Wang L., Su S., Zhang C.,
RA   Zhang W.;
RT   "Whole-Genome optical mapping and complete genome sequence of
RT   Sphingobacterium deserti sp. nov., a new spaces isolated from desert in the
RT   west of China.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KGE13660.1, ECO:0000313|Proteomes:UP000031802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACCC05744 {ECO:0000313|Proteomes:UP000031802};
RX   PubMed=25830331;
RA   Teng C., Zhou Z., Molnar I., Li X., Tang R., Chen M., Wang L., Su S.,
RA   Zhang W., Lin M.;
RT   "Whole-Genome Optical Mapping and Finished Genome Sequence of
RT   Sphingobacterium deserti sp. nov., a New Species Isolated from the Western
RT   Desert of China.";
RL   PLoS ONE 10:E0122254-E0122254(2015).
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:KGE13660.1}.
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DR   EMBL; JJMU01000047; KGE13660.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B8T7H6; -.
DR   STRING; 1229276.DI53_2581; -.
DR   PATRIC; fig|1229276.3.peg.2654; -.
DR   eggNOG; COG0508; Bacteria.
DR   Proteomes; UP000031802; 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|RuleBase:RU003423};
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031802};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          1..68
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          137..177
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
FT   REGION          182..214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..214
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   451 AA;  49368 MW;  3014AC8D44F0E235 CRC64;
     MGESVSEATI TKWVKSVGDT IEEDEAVVEI ATDKVDSDVP SPVSGTLTKV LFEENQVVQV
     GDAIALIETD GDDILRDDDQ HTPAFTNPST VADEEIIDQQ AETTGHHDQS KEEVIPGVDL
     LPREEQTQNV VSSGNRFYSP LVKNIAQEEG MSQEELDEIP GSGSDGRVTK QDVLDHLQNR
     NKVDHTKAAA QVAVQKQSPD STKEPTQTAP KSVTSGNDEI IEMDRMRKLI ADHMVHSVKT
     SPHVASFVEA DVTHLVNWRN KVKDSYKQRE GENITFTPIF IEAISKAIKD FPMINVSVDG
     HNIIKRKNIN IGMAAALPSG NLIVPVIKNA DQLSLVGLSK AVNDLANRSR SNKLKPDDTQ
     GGTFTFSNIG AFGNIMGFPI INQPQAAILA VGTIKKRPAV LETADGDVIA IRHMMYLSMS
     YDHRVIDGAL GGTFLKRVAD YLENWDTNRE I
//
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