ID I4A236_ORNRL Unreviewed; 443 AA.
AC I4A236;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN OrderedLocusNames=Ornrh_1875 {ECO:0000313|EMBL:AFL98020.1};
OS Ornithobacterium rhinotracheale (strain ATCC 51463 / DSM 15997 / CCUG 23171
OS / CIP 104009 / LMG 9086).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Ornithobacterium.
OX NCBI_TaxID=867902 {ECO:0000313|EMBL:AFL98020.1, ECO:0000313|Proteomes:UP000006051};
RN [1] {ECO:0000313|EMBL:AFL98020.1, ECO:0000313|Proteomes:UP000006051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51463 / DSM 15997 / CCUG 23171 / LMG 9086
RC {ECO:0000313|Proteomes:UP000006051};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA Mikhailova N., Teshima H., Kyrpides N., Mavromatis K., Pagani I.,
RA Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Lang E., Kopitz M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Ornithobacterium rhinotracheale DSM 15997.";
RL Submitted (JUN-2012) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003283; AFL98020.1; -; Genomic_DNA.
DR RefSeq; WP_014791542.1; NC_018016.1.
DR AlphaFoldDB; I4A236; -.
DR STRING; 867902.Ornrh_1875; -.
DR GeneID; 71569925; -.
DR KEGG; orh:Ornrh_1875; -.
DR PATRIC; fig|867902.3.peg.1817; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_1_10; -.
DR Proteomes; UP000006051; 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:AFL98020.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:AFL98020.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006051};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:AFL98020.1}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 132..172
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 79..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 443 AA; 47932 MW; 415547D5B3DEF13D CRC64;
MAEYKFLLPS MGEGIMEATV TAWLKNVGDS IEEDESIVEV ATDKVDSDVP SPVSGVLKEI
IIPTDSVAKV GEPMAIITTD GDEEEPAAYT PKSEAPTPEP SPEIAQAAKE AEKALNVVKT
PASIDLGESD KFLSPLVRSI AAKEGISAEE LNSIQGSGQN GRVTKDDMLR YLEQKDQQPN
TSSAPAPAAS APQTQTPSPA PKAISLGAND EIIEMDRMRK IIAQHMLDSK QISPHVTSFV
EADMTRIVQW RNRVKNAFQK REGEKITFMP IIVEAIVKAI KDFPMINVSV DGDKIIKKAN
INIGIAAARP DGNLIVPVIK NADQLNLIGL AKKINDLGYR AKNNQLKPDE IQGGTYTVSN
IGSFGNLMGT PIINQPQVAI MAIGSIQKKP AVIETPEGDT IGIRHKMYLS HSYDHRVVDG
ALGGMFVKRV AEYLESFDID RGI
//
