ID   B3R912_CUPTR            Unreviewed;      1014 AA.
AC   B3R912;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   SubName: Full=D-lactate dehydrogenase (Cytochrome) contains GlcD, FAD/FMN-containing dehydrogenases GlpC, Fe-S oxidoreductase {ECO:0000313|EMBL:CAQ71387.1};
DE            EC=1.1.2.4 {ECO:0000313|EMBL:CAQ71387.1};
GN   OrderedLocusNames=RALTA_B0771 {ECO:0000313|EMBL:CAQ71387.1};
OS   Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS   107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=977880 {ECO:0000313|EMBL:CAQ71387.1, ECO:0000313|Proteomes:UP000001692};
RN   [1] {ECO:0000313|EMBL:CAQ71387.1, ECO:0000313|Proteomes:UP000001692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 /
RC   R1 {ECO:0000313|Proteomes:UP000001692};
RX   PubMed=18490699; DOI=10.1101/gr.076448.108;
RA   Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA   Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA   Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA   Masson-Boivin C.;
RT   "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT   comparative genomics of rhizobia.";
RL   Genome Res. 18:1472-1483(2008).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CU633750; CAQ71387.1; -; Genomic_DNA.
DR   RefSeq; WP_012355608.1; NC_010530.1.
DR   AlphaFoldDB; B3R912; -.
DR   GeneID; 29765053; -.
DR   KEGG; cti:RALTA_B0771; -.
DR   eggNOG; COG0247; Bacteria.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_010756_0_0_4; -.
DR   BioCyc; CTAI977880:RALTA_RS19465-MONOMER; -.
DR   Proteomes; UP000001692; Chromosome 2.
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:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004017; Cys_rich_dom.
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; IPR009051; Helical_ferredxn.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   PANTHER; PTHR11748:SF119; D-2-HYDROXYGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02754; CCG; 2.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   Pfam; PF13183; Fer4_8; 1.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000313|EMBL:CAQ71387.1}.
FT   DOMAIN          55..285
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   1014 AA;  110419 MW;  919CC7A51C6BFC7C CRC64;
     MNMTSSSLLV KPIHLVPAQQ RPTSPLSALL RKELRGDVLF DRAARGRYAT DASIYQIMPV
     GVVVPRDQAD LVRALDIARD QRVPVLARGA GTSQCGQTVG EALVIDTSKW LNNVVAFDAG
     ARTVTVEPGI VLDHLNAWLR PHGLWFPVDV STGAQCTIGG MAGNNSCGSR SIAYGNMVHN
     VLAIDAVLAD GSDCHFGSLA QPVAAGRAEG ILHGLRRIAT RERGEIAERM PKVLRRVAGY
     NIDLFDCQNP RAYTDDGHAN LAHILVGSEG TLACSRQLTL KLAPLPAHKV LGVVNFPTFY
     QAMDLTQHIV TLQPVAVELV DRTMIDLSME NPAFRPVVER ALAGDPQAIL LVEFAGDDRQ
     ALLAQLDRLA ELMADLGLPG SVVKMPEEKA QKALWDVRKA GLNIMMSMKG DGKPVSFIED
     CAVPLEHLAE YTRRLTEVFH KHETEGTWYA HASVGTLHVR PILDMRRDGA LRMREIAEEA
     AELVREYKGA YSGEHGDGLC RGEWVAWQYG PRINAAFSEI KALFDPDNRF NPDKIVRPPR
     MDARENFRFA PGYAALPLTP ALDWSAWNVR RDPMTGAETA PGTGNDSATH GLASAVEMCN
     NNGHCRKFDA GTMCPSYRVT KDEQHVTRGR ANTLRLAVTG QLGTDGLASA EVKEALDLCV
     SCKGCKRDCP TGVDMAKFKI EARHAWTRRH GISLRERMVA FLPRYAPAPS RVPGLLALAD
     RLPGVSGWIK RALGFAPQRS LPRFTAPFLA GRRSTATAAG SKADGREVLL FVDTFSNYME
     PDNARAAQAV LEAAGYTVHF NTRAGERPLC CGRTFLAAGL VDQAKAEARR LLDTLRPFVE
     RGVPVVGLEP SCLLSLRDEF LGYGYGDEAR QLASLSFLFE EFLVRERQAG RLALPLRPLQ
     VSEAIVHGHC HQKAFDAFTP VQTVLGWIPG LKVAPVESSC CGMAGSFGYE AEHFEASQAM
     AELSLLPAVR RRAGDAIVVA DGTSCRHQIR DGAQAEPMHV ARVLAMALEG GNHD
//