ID A0A0K2JFM1_SPIKU Unreviewed; 219 AA.
AC A0A0K2JFM1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Pyruvate dehydrogenase E3 (Dihydrolipoamide dehydrogenase) component {ECO:0000313|EMBL:ALA97233.1};
GN Name=lpdA {ECO:0000313|EMBL:ALA97233.1};
GN ORFNames=SKUN_00316 {ECO:0000313|EMBL:ALA97233.1};
OS Spiroplasma kunkelii CR2-3x.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=273035 {ECO:0000313|EMBL:ALA97233.1, ECO:0000313|Proteomes:UP000062963};
RN [1] {ECO:0000313|EMBL:ALA97233.1, ECO:0000313|Proteomes:UP000062963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR2-3x {ECO:0000313|EMBL:ALA97233.1,
RC ECO:0000313|Proteomes:UP000062963};
RX PubMed=26494665;
RA Davis R.E., Shao J., Dally E.L., Zhao Y., Gasparich G.E., Gaynor B.J.,
RA Athey J.C., Harrison N.A., Donofrio N.;
RT "Complete Genome Sequence of Spiroplasma kunkelii Strain CR2-3x, Causal
RT Agent of Corn Stunt Disease in Zea mays L.";
RL Genome Announc. 3:e01216-e01215(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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DR EMBL; CP010899; ALA97233.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K2JFM1; -.
DR STRING; 273035.SKUN_00316; -.
DR KEGG; skn:SKUN_00316; -.
DR PATRIC; fig|273035.7.peg.373; -.
DR Proteomes; UP000062963; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR22912:SF151; DIHYDROLIPOYL DEHYDROGENASE 1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Pyruvate {ECO:0000313|EMBL:ALA97233.1}.
FT DOMAIN 2..95
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 118..218
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 219 AA; 23941 MW; 2F5AA6AF4AC3CD0E CRC64;
MLIKNKVKIE TSVKIKVIKG KTVVYDNSDG KEVKLTSDYC LVSVGQTPVT TCFENIGLKI
WERKNIEVDE QCKTNLPGVY AIGNVVGCTM LAHVDSVQGI LVIDSIKGKN VKMNYNRIPS
CIYSFPEVAT VGITEEQAIK AKIAYKAFKF LLSANGKAIA YGETDGFVKI LCDPKYGEIL
GVHIVAATAT DMIYGITACM ETEGTIHELA KTVHPYPIL
//
