ID   K0E1C0_9BURK            Unreviewed;       992 AA.
AC   K0E1C0;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:AFT90218.1};
GN   ORFNames=BUPH_05061 {ECO:0000313|EMBL:AFT90218.1};
OS   Paraburkholderia phenoliruptrix BR3459a.
OG   Plasmid pSYMBR3459 {ECO:0000313|EMBL:AFT90218.1,
OG   ECO:0000313|Proteomes:UP000010105}.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1229205 {ECO:0000313|EMBL:AFT90218.1, ECO:0000313|Proteomes:UP000010105};
RN   [1] {ECO:0000313|EMBL:AFT90218.1, ECO:0000313|Proteomes:UP000010105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BR3459a {ECO:0000313|EMBL:AFT90218.1,
RC   ECO:0000313|Proteomes:UP000010105};
RC   PLASMID=pSYMBR3459 {ECO:0000313|EMBL:AFT90218.1,
RC   ECO:0000313|Proteomes:UP000010105};
RX   PubMed=23144415; DOI=10.1128/JB.01821-12;
RA   de Oliveira Cunha C., Goda Zuleta L.F., Paula de Almeida L.G.,
RA   Prioli Ciapina L., Lustrino Borges W., Pitard R.M., Baldani J.I.,
RA   Straliotto R., de Faria S.M., Hungria M., Sousa Cavada B., Mercante F.M.,
RA   Ribeiro de Vasconcelos A.T.;
RT   "Complete Genome Sequence of Burkholderia phenoliruptrix BR3459a (CLA1), a
RT   Heat-Tolerant, Nitrogen-Fixing Symbiont of Mimosa flocculosa.";
RL   J. Bacteriol. 194:6675-6676(2012).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP003865; AFT90218.1; -; Genomic_DNA.
DR   RefSeq; WP_015004415.1; NC_018696.1.
DR   AlphaFoldDB; K0E1C0; -.
DR   GeneID; 27801515; -.
DR   KEGG; bpx:BUPH_05061; -.
DR   PATRIC; fig|1229205.11.peg.6937; -.
DR   eggNOG; COG0247; Bacteria.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_010756_0_0_4; -.
DR   Proteomes; UP000010105; Plasmid pSYMBR3459.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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; 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; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   PANTHER; PTHR11748:SF119; D-2-HYDROXYGLUTARATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02754; CCG; 1.
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   Plasmid {ECO:0000313|EMBL:AFT90218.1}.
FT   DOMAIN          46..274
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   992 AA;  108481 MW;  482F7AA36BF31678 CRC64;
     MKAATPFQAS KSLLQEVEAE LRRSIRGEVR FDSSSKALYA SDASNYRQIP LGVVVPADVN
     DLVAALDACR RKDVPFLTRG GGTSQNGQCV NVAVVADASK YVNRVVSVDP ESRTAIVEPG
     VVCDTLRDAA EKHGLTFAPD PATHSRCTLG GMIANNSCGA HSVMAGKTVE NVEALEIVTY
     DGARFWIGPT TDAELEDIIA QGGRRGEIYR KLRDLRDRYA DHIRDEFPQI RRRVSGFNLD
     QLLPENGFNV ARALVGTEGT CAVTLQAKVR LVHSPSCRVL LVLGFCDIYT AADAVPHFNR
     FSPIAIEGLD RGIIRGLQAR GLKAEEIALL PAGDAWVVLE FGADTVADAI QRANDAHAWF
     AAGEGGAGVT GFVVEDKAKQ QKIWSIRETG ASAVSLSIDP SKPDPMVGWE DAAVDPLRLG
     DYLRQFQALV DRYGYETCLY GHFGDGCVHA RITFDVRTAE GVLTWRGFLR EAAQLVVDFG
     GSLSGEHGDG QAKAEFLPIM YGPEIMQAME AFKAIWDPAN RLNPGKVVNA YRADENLRMG
     PSYKPVKLTT RLTFASPEGD GMQRAVERCI GMGKCRSLEG GTMCPSFRAT REEKYSTRGR
     AHLFWEMLQG EVITNGWNSH EVKEALDACL ACKGCKSDCP THTDMASYKA EFLSHYYESH
     RLPRQAMFMG RIGQWAPVAS RFPWLVNFLV STPPLARLSK WFAGVAPRRN LPVFAPRTFR
     ALANRRGLRN GQAASKPANK VILWVDTFND HFSPEIATAA LDVLTRIGYQ VVLPRKRLCC
     GRPLYDYGLL DEAKALLRSA VDELADDVRA GVPVVGLEPG CLSVFKDELL KQLPDDVMAR
     KLSEQTFLFP DFVASADFDW PQLDAEVVVH GHCHQKSLFG MKGETMLLDK LGVTWKLLDA
     GCCGMAGSFG FDAGHYDLSM KIAEDGLLPL VRKVPSNAFI VTNGFSCREQ IEQGAGKTPL
     HIAQLALKAL ENVSSIQSAA RSRVTGDLTS VS
//