ID K7QXK8_THEOS Unreviewed; 448 AA.
AC K7QXK8;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=Theos_0082 {ECO:0000313|EMBL:AFV75165.1};
OS Thermus oshimai JL-2.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=751945 {ECO:0000313|EMBL:AFV75165.1, ECO:0000313|Proteomes:UP000000211};
RN [1] {ECO:0000313|EMBL:AFV75165.1, ECO:0000313|Proteomes:UP000000211}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JL-2 {ECO:0000313|EMBL:AFV75165.1,
RC ECO:0000313|Proteomes:UP000000211};
RX PubMed=23405355; DOI=10.1128/genomeA.00106-12;
RA Murugapiran S.K., Huntemann M., Wei C.L., Han J., Detter J.C., Han C.S.,
RA Erkkila T.H., Teshima H., Chen A., Kyrpides N., Mavrommatis K.,
RA Markowitz V., Szeto E., Ivanova N., Pagani I., Lam J., McDonald A.I.,
RA Dodsworth J.A., Pati A., Goodwin L., Peters L., Pitluck S., Woyke T.,
RA Hedlund B.P.;
RT "Whole Genome Sequencing of Thermus oshimai JL-2 and Thermus thermophilus
RT JL-18, Incomplete Denitrifiers from the United States Great Basin.";
RL Genome Announc. 1:E00106-E00112(2013).
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; CP003249; AFV75165.1; -; Genomic_DNA.
DR RefSeq; WP_016328365.1; NC_019386.1.
DR AlphaFoldDB; K7QXK8; -.
DR STRING; 751945.Theos_0082; -.
DR KEGG; tos:Theos_0082; -.
DR PATRIC; fig|751945.3.peg.76; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_3_0_0; -.
DR OrthoDB; 9767256at2; -.
DR Proteomes; UP000000211; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2740; -; 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; 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; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748:SF111; D-LACTATE DEHYDROGENASE, MITOCHONDRIAL-RELATED; 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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128}.
FT DOMAIN 32..209
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 448 AA; 48747 MW; 333028435631F6F5 CRC64;
MSLEELQGLL PGKVDLSESE RARHGKDEGY PEARPVLAVV YPEGVEDIQK ALDWARKVGV
AVIPYGAGTS LEGHLYPVRE AISLDLSRMD RILEVHPEDF YCVVEPGLTR KRLNEALKGT
GLFFPVDPGA DASLGGMAAT NASGTTTVRY GGMRQNVLGL QVVLANGEVL ELGRPVRKTS
AGYDLKDLFI GSEGTLGIIT RLTLKLHPLP AHVLTLRAFF PGVEEAVRAS LGVMALGGGV
ARLELLDELA LKALNRHLGA GFPERPALFL EFHSPTREAL EAEGALAEEV LREAGAFALE
TARTEEERRA QWEARHQAYW ALVHLFPGHR FMITDVAVPL SRLPEAVRFA QRLLSELGLT
GNILGHVGDG NFHTLVPVLP EDYPRAEAFA EHLVEKALAL GGTCTAEHGV GLRKRKYLGK
EHGPALEWMR RLKALLDPEG LLNPGKVV
//
