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Database: UniProt
Entry: G5H8J6_9BACT
LinkDB: G5H8J6_9BACT
Original site: G5H8J6_9BACT 
ID   G5H8J6_9BACT            Unreviewed;       444 AA.
AC   G5H8J6;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=HMPREF9450_01256 {ECO:0000313|EMBL:EHB92391.1};
OS   Alistipes indistinctus YIT 12060.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae;
OC   Alistipes.
OX   NCBI_TaxID=742725 {ECO:0000313|EMBL:EHB92391.1, ECO:0000313|Proteomes:UP000006008};
RN   [1] {ECO:0000313|EMBL:EHB92391.1, ECO:0000313|Proteomes:UP000006008}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIT 12060 {ECO:0000313|EMBL:EHB92391.1,
RC   ECO:0000313|Proteomes:UP000006008};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Alistipes indistinctus YIT 12060.";
RL   Submitted (AUG-2011) 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}.
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:EHB92391.1}.
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DR   EMBL; ADLD01000011; EHB92391.1; -; Genomic_DNA.
DR   RefSeq; WP_009134062.1; NZ_JH370371.1.
DR   AlphaFoldDB; G5H8J6; -.
DR   STRING; 742725.HMPREF9450_01256; -.
DR   PATRIC; fig|742725.3.peg.1333; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_10_2_10; -.
DR   Proteomes; UP000006008; Unassembled WGS sequence.
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; 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; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006008};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          129..166
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000259|PROSITE:PS51826"
SQ   SEQUENCE   444 AA;  46400 MW;  EFB309D9EEBAF8BA CRC64;
     MATVVIMPKQ GQSVESCILT EMKKKKGDTV AVGDILFSYE TDKASFEEEA QVAGTVLDVF
     FDDGDEIPVL TNVMVIGNEG ESTAEFRPGG EAAAPAAETP VAAAAAPAAT PAIAAATAVK
     PATTEGTSPV SPRARALAEK EAVNAAALQG SGPHGRVIER DVQAAIAATP KLTPLAKAIA
     KETGAAAPEA GSGLAGMVKG ADMGALKNSV YATDSEIKPL TNMRKLIAKA MHASLQNSAQ
     LTHHLSADAR RILELRKKVK KAVDNGYPTN ITLNDMVCMA VIKALKKFPQ VNSHFLGDST
     RVFSKVHLGL AVDTDRGLMV PTVKNADDLS IQGLANQLKE VANACKKGSI DPDLLSSEAA
     SFTVSNLGNY GVEIFTPVIN LPQVAILGVN TIVPRPKDIG GGVYAFVPHI GLSLTYDHRA
     LDGGEATRFV KEVANEIEAL DFEL
//
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