ID H6RN60_BLASD Unreviewed; 473 AA.
AC H6RN60;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:CCG02608.1};
DE EC=1.1.2.4 {ECO:0000313|EMBL:CCG02608.1};
GN OrderedLocusNames=BLASA_1687 {ECO:0000313|EMBL:CCG02608.1};
OS Blastococcus saxobsidens (strain DD2).
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=1146883 {ECO:0000313|EMBL:CCG02608.1, ECO:0000313|Proteomes:UP000007517};
RN [1] {ECO:0000313|EMBL:CCG02608.1, ECO:0000313|Proteomes:UP000007517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD2 {ECO:0000313|EMBL:CCG02608.1,
RC ECO:0000313|Proteomes:UP000007517};
RX PubMed=22535935; DOI=10.1128/JB.00320-12;
RA Chouaia B., Crotti E., Brusetti L., Daffonchio D., Essoussi I., Nouioui I.,
RA Sbissi I., Ghodhbane-Gtari F., Gtari M., Vacherie B., Barbe V., Medigue C.,
RA Gury J., Pujic P., Normand P.;
RT "Genome Sequence of Blastococcus saxobsidens DD2, a Stone-Inhabiting
RT Bacterium.";
RL J. Bacteriol. 194:2752-2753(2012).
RN [2] {ECO:0000313|Proteomes:UP000007517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD2 {ECO:0000313|Proteomes:UP000007517};
RA Genoscope.;
RT "Complete genome sequence of Blastococcus saxobsidens strain DD2.";
RL Submitted (FEB-2012) 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; FO117623; CCG02608.1; -; Genomic_DNA.
DR RefSeq; WP_014375500.1; NC_016943.1.
DR AlphaFoldDB; H6RN60; -.
DR STRING; 1146883.BLASA_1687; -.
DR KEGG; bsd:BLASA_1687; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_4_1_11; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000007517; Chromosome.
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; 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; 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 Oxidoreductase {ECO:0000313|EMBL:CCG02608.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007517}.
FT DOMAIN 37..218
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 473 AA; 49970 MW; E467DEF58CE2BD7E CRC64;
MTDPGLPGRL RAAVGEAGLV TDPARMGGYL SDWRNAYSGT AAAVVRPVST DEVAAIVRAC
RKEGVAVVPQ GGNTGLCGGA VPDTSGRQVV LSLDRMRRLR AVDPVNQTIT VEAGVVLQAV
QEAAAAEGCL FPLSLGSEGS CTIGGNLSTN AGGTGVLRYG TMRDLTLGLE VVLPDGRIWN
GLRGLRKDNT GYDLKHLFIG AEGTLGLVTA AVLKLFPAVR SRATAWVAVG SAQAAVDLFG
IVRALCGDRL TAFEIMSRQS VDFVLRHGTG ARDLFGSVHF WYVLVELSDT LPDARLDGLL
EAALAEAFDR DVAGDAVVAS GSAQVAALWA LREGISEAQN FEGPSLKHDV TVPISSIPAF
VERTDKALRA ALPGIRIVTY GHIGDGNLHY NLSKPVDSDD DTFRNLAEEL ARMVYDATSS
FGGSISAEHG LGQSKRDVIA DYKDGLELEL MRSLKHLLDP RGLMNPGKVL PAW
//
