ID A0A0E9LZW6_9BACT Unreviewed; 535 AA.
AC A0A0E9LZW6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=JCM15548_13111 {ECO:0000313|EMBL:GAO30799.1};
OS Geofilum rubicundum JCM 15548.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC Geofilum.
OX NCBI_TaxID=1236989 {ECO:0000313|EMBL:GAO30799.1, ECO:0000313|Proteomes:UP000032900};
RN [1] {ECO:0000313|EMBL:GAO30799.1, ECO:0000313|Proteomes:UP000032900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15548 {ECO:0000313|EMBL:GAO30799.1};
RX PubMed=25736980;
RA Inoue J., Oshima K., Suda W., Sakamoto M., Iino T., Noda S., Hongoh Y.,
RA Hattori M., Ohkuma M.;
RT "Distribution and evolution of nitrogen fixation genes in the phylum
RT bacteroidetes.";
RL Microbes Environ. 30:44-50(2015).
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC (E3). {ECO:0000256|ARBA:ARBA00025211}.
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:GAO30799.1}.
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DR EMBL; BAZW01000030; GAO30799.1; -; Genomic_DNA.
DR RefSeq; WP_062126175.1; NZ_BAZW01000030.1.
DR AlphaFoldDB; A0A0E9LZW6; -.
DR STRING; 1236989.JCM15548_13111; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000032900; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; 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:SF2; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 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 Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:GAO30799.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032900};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:GAO30799.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 242..279
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 71..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..124
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..203
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 535 AA; 59688 MW; 4903AB1936FE5C90 CRC64;
MIKEIKLPEI ADNVDSAVVL NIHVSKGDKI KKEDTIAEME SDKAAFDLPS DVAGEVMEIK
VSEGDEVKVG QVVITVETEG GEDEESQDEK DQDQEKDKPK AKKKSDQQEE EEQEEEVADE
KEEEEDQEKE KKGEEVVGDE QEEDEQDDAP KKKSAEKNKK KTSNKKASEE EGQTLTEEEE
AEGKEAEEEE EVEAEDDSGS TDLDDDKEVT KSENVDDDES DARKEAQEPK HAEDTPQKKE
VAAAPSIRRL ARELGIDIYK VEGTGPHDRI SAEDVKSYSK MIAQKSKDPL SAQADEALPN
FSQYGSIERQ PLNSIRKRIA KNVQASWQTI PHVFQFDKAD ISQLETFLDK YGKEGEKEGV
KLTITAILLK ILAQALKRFP NFNASLDMKN EEIILKKYFN IGVAVDTDRG LLVPVIKDVD
KKSILELSQE LGEMAERTRN KKIKPDELQG GNIALSNLGG IGGTNFTPIV YSPNVAILGV
SQARTEPVYI DGAFQPRQIL PLSLSYDHRA IDGAEGARFL RWFCEALENP LLTLL
//
