ID W1ND57_9GAMM Unreviewed; 561 AA.
AC W1ND57;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=BJB45_17145 {ECO:0000313|EMBL:ERL53005.1};
OS Halomonas huangheensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1178482 {ECO:0000313|EMBL:ERL53005.1, ECO:0000313|Proteomes:UP000019113};
RN [1] {ECO:0000313|EMBL:ERL53005.1, ECO:0000313|Proteomes:UP000019113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BJGMM-B45 {ECO:0000313|EMBL:ERL53005.1,
RC ECO:0000313|Proteomes:UP000019113};
RA Miao C., Wan Y., Jin W.;
RT "draft genome of Halomonas huanghegensis, strain BJGMM-B45T.";
RL Submitted (AUG-2013) 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 -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry. {ECO:0000256|ARBA:ARBA00011484}.
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:ERL53005.1}.
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DR EMBL; AVBC01000014; ERL53005.1; -; Genomic_DNA.
DR RefSeq; WP_021817634.1; NZ_CP013106.1.
DR AlphaFoldDB; W1ND57; -.
DR STRING; 1178482.AR456_09560; -.
DR KEGG; hhu:AR456_09560; -.
DR PATRIC; fig|1178482.3.peg.693; -.
DR eggNOG; COG0508; Bacteria.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000019113; 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; 2.
DR Gene3D; 2.40.50.100; -; 2.
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; 2.
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; 2.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
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:UP000019113};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 1..76
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 125..201
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 257..294
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 86..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 561 AA; 60109 MW; 291F0618911BB96F CRC64;
MKEFRLPDIG EGIVECEVVE WKVSEGDSIA EDQPVVEVMT DKALVEITAP EAGVVSRLHV
AAGEMARVHE PLFAYAASDD ESGAYIGGDA SADAEASSNT SATDDEADRL GAVAETAAEG
SAERRVDFIL PDIGEGIVEC EIVEWHARAG DTIEEDQRLV DVMTDKALVE ITAPEHGVVA
ELYVAQGQMA RVHSPLFAYI TEGGSDASGA TNSTDRGSGT AVGSHKPDSH GASSSSPLSS
SPLSNTPTPK NRYGRTPASP AVRRMVREHH LRLEEIPGSG RDGRVLKEDV LGWLENGQGG
EKRSSNKVCA ADQHRAGDTS PGRVEPLPTR VEPLKGIRAA MARQMVASAS TIPHFQYGEE
FDITELLALR ERLKPRAEAR ELRLTLMPFF MKAMALAVTE YPLLNARLAN DASEIHYQSG
CNIGMAVDGK AGLMVPNVKG VEGLSLLDIA AEVQRLTAAA REGRVSQQDL SGGTISISNI
GALGGTYAAP IINAPEVAIV AIGKTQWLPR FNEQDEVVKR AILTVTWAGD HRLLDGGTIA
RFCNSWKGYL EQPESMLLEM R
//
