ID   A0A1X4NPR6_9RHOB        Unreviewed;       429 AA.
AC   A0A1X4NPR6;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:OSQ52702.1};
GN   ORFNames=MGEO_04970 {ECO:0000313|EMBL:OSQ52702.1};
OS   Marivita geojedonensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Marivita.
OX   NCBI_TaxID=1123756 {ECO:0000313|EMBL:OSQ52702.1, ECO:0000313|Proteomes:UP000193926};
RN   [1] {ECO:0000313|EMBL:OSQ52702.1, ECO:0000313|Proteomes:UP000193926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DPG-138 {ECO:0000313|EMBL:OSQ52702.1,
RC   ECO:0000313|Proteomes:UP000193926};
RA   Lai Q., Shao Z.;
RT   "The draft genome sequence of Marivita geojedonensis KCTC 23882.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|ARBA:ARBA00001938};
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:OSQ52702.1}.
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DR   EMBL; JFKC01000002; OSQ52702.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X4NPR6; -.
DR   STRING; 1123756.MGEO_04970; -.
DR   OrthoDB; 9804723at2; -.
DR   Proteomes; UP000193926; Unassembled WGS sequence.
DR   GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR   CDD; cd06849; lipoyl_domain; 2.
DR   Gene3D; 2.40.50.100; -; 2.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR000089; Biotin_lipoyl.
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; PF00364; Biotin_lipoyl; 2.
DR   SUPFAM; SSF51230; Single hybrid motif; 2.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
PE   4: Predicted;
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823};
KW   Pyruvate {ECO:0000313|EMBL:OSQ52702.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193926}.
FT   DOMAIN          2..77
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   DOMAIN          102..177
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          191..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   429 AA;  44017 MW;  0E71E29AD27AD9D2 CRC64;
     MPHDVTMPQL GMAQDAGKIV SWLKAPGDPV AEGDALFEVE TDKATMEVEA PASGFLTAVT
     AAAGDDVPVG QIIARISDQA DIPAEAATAP EDATPSSDLP DGVQVTMPQL GMAQDSGILV
     GWLKSPGDPV KADDVLFEVE TDKSTMEVPA GAEGYLAATL AQAGEEVPVG DPVAIISAEA
     LQETVVRSVK DVAPATNPAP SKASKPDKPK SGDTPAPAKP KPAVTEPSGR ILASPKLRRL
     AMEQGLDLNR LVEAGHPQPY HAADLDVLKA LPTQATAYPA TATRHLTAEV PADGFADFAD
     WAAENAGLSN PAQLLAGLAA ASLPDGHAAV AVEHLGTTQV FSVSPGPFGA IAEAAPDSAY
     DLLVRDLRMS RITSLALGAN TTPVLSLTRA GTGLSITLEC AGDQLGASEA VTLLSEFAGR
     MEQPLRHLL
//