ID B9L965_NAUPA Unreviewed; 401 AA.
AC B9L965;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 97.
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=NAMH_0770 {ECO:0000313|EMBL:ACM92443.1};
OS Nautilia profundicola (strain ATCC BAA-1463 / DSM 18972 / AmH).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Nautiliales;
OC Nautiliaceae; Nautilia.
OX NCBI_TaxID=598659 {ECO:0000313|EMBL:ACM92443.1, ECO:0000313|Proteomes:UP000000448};
RN [1] {ECO:0000313|EMBL:ACM92443.1, ECO:0000313|Proteomes:UP000000448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1463 / DSM 18972 / AmH
RC {ECO:0000313|Proteomes:UP000000448};
RX PubMed=19197347; DOI=10.1371/journal.pgen.1000362;
RA Campbell B.J., Smith J.L., Hanson T.E., Klotz M.G., Stein L.Y., Lee C.K.,
RA Wu D., Robinson J.M., Khouri H.M., Eisen J.A., Cary S.C.;
RT "Adaptations to submarine hydrothermal environments exemplified by the
RT genome of Nautilia profundicola.";
RL PLoS Genet. 5:E1000362-E1000362(2009).
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; CP001279; ACM92443.1; -; Genomic_DNA.
DR RefSeq; WP_012663814.1; NC_012115.1.
DR AlphaFoldDB; B9L965; -.
DR STRING; 598659.NAMH_0770; -.
DR KEGG; nam:NAMH_0770; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_2_7; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000000448; Chromosome.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:RHEA.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
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 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; IPR045257; E2/Pdx1.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR23151:SF90; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00189; LIPOYL; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:ACM92443.1};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:ACM92443.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 84..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 401 AA; 45227 MW; FF1D30A8862FB226 CRC64;
MEYKVTMPIL SDTMDKGKIT KWYVKAGDFV KKGDKLCEVE SDKAVMDIES FEEGVVKEIL
VKEGEEVPVK SVIAIIETME NGKLTMENEE KKEPENEKPK PKQPEEKNEI NLDDIINSIV
SKPKSEIKGT ASPAAKKEAA RFGIDIEKLQ ENNKIPKPAH IKDIKEHIIS RYFTPKAVKL
LKEYNIEYDM FKLDHKIDSE EVLNYIKQNN IPKITPLTPN QLAVIKNLQN SLTKPTFFVF
EEIEITKKEG IKLTALILKA LANAMQKNPL TRTVLQNDTL LTFPSSNISV AVSREDGLFM
CVIKNAEQKD LNEINEWLKE IKSKRLSVED LSGSTFGVSN LGMFDIERFT ALINDKDAGI
AAFGKLSGGK IKVSFTFDHR ILNGTDAAVF VNSFKEEIKN V
//
