ID G3A764_9RALS Unreviewed; 605 AA.
AC G3A764;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Putative lactate dehydrogenase {ECO:0000313|EMBL:CCA86329.1};
DE EC=1.1.2.4 {ECO:0000313|EMBL:CCA86329.1};
GN ORFNames=RALSY_40549 {ECO:0000313|EMBL:CCA86329.1};
OS Ralstonia syzygii R24.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=907261 {ECO:0000313|EMBL:CCA86329.1};
RN [1] {ECO:0000313|EMBL:CCA86329.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R24 {ECO:0000313|EMBL:CCA86329.1};
RX PubMed=21931687; DOI=10.1371/journal.pone.0024356;
RA Remenant B., de Cambiaire J.C., Cellier G., Jacobs J.M., Mangenot S.,
RA Barbe V., Lajus A., Vallenet D., Medigue C., Fegan M., Allen C., Prior P.;
RT "Ralstonia syzygii, the Blood Disease Bacterium and some Asian R.
RT solanacearum strains form a single genomic species despite divergent
RT lifestyles.";
RL PLoS ONE 6:e24356-e24356(2011).
RN [2] {ECO:0000313|EMBL:CCA86329.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R24 {ECO:0000313|EMBL:CCA86329.1};
RA Genoscope - CEA;
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
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DR EMBL; FR854089; CCA86329.1; -; Genomic_DNA.
DR AlphaFoldDB; G3A764; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2190; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR018643; DUF2069_membrane.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF09842; DUF2069; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:CCA86329.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 13..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 96..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 172..353
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 605 AA; 65034 MW; C87A6797C5C6B11F CRC64;
MTPTDPPVPH SRALYRLSAG SLVALIVLCA AWELWLAPLR PGGSWLALKA LLLAWPLPGV
LRRNRYTMQW ASMFILLFFT EGIVRATSDQ GASRALAWAE VVLSLVFFFA TIFYLRPFKR
AAKARARQDA CPPPAMTHDA FLQACADAIG SAHVLTAPED QAPYLTDWRK RFTGRARAVL
RPAHPEEVAA LVRLCGGHGV PIVPQGGNTG LCGGATPDTA GHAVVISLQR MQRVRAVDPI
NNTITVDAGC ILASVQEAAA AAGRLFPLSL AAEGSCTIGG NLATNAGGTA VLRYGNAREL
CLGVEAVLPN GELWNGLRGL RKDNTGYDLR DLLIGAEGTL GIITGAMLKL FPQPRAQVTA
LAALASPRQA LAFLSLTQSH AGMLLTGFEL MSAFCLELVR KHYPQLRLPF SQAYPQYVLL
ELSDLESEAH ARGVFETLME DALAREVILD AAVAESVAQS RELWNLREHI PLAQADEGKN
IKHDIAVPIS RIADFIDVTD RALAAACPGI RMVTFGHLGD GNLHYNVSPP TGQDHEAFLA
NQPGINRMVH DSVHAHGGSI SAEHGIGQLK REDNARYKSP VELAAMRAIK QALDPLGLMN
PGKVL
//
