ID   B2JQ35_PARP8            Unreviewed;      1005 AA.
AC   B2JQ35;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=D-lactate dehydrogenase (Cytochrome) {ECO:0000313|EMBL:ACC73376.1};
DE            EC=1.1.2.4 {ECO:0000313|EMBL:ACC73376.1};
GN   OrderedLocusNames=Bphy_4256 {ECO:0000313|EMBL:ACC73376.1};
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC73376.1, ECO:0000313|Proteomes:UP000001192};
RN   [1] {ECO:0000313|Proteomes:UP000001192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC   {ECO:0000313|Proteomes:UP000001192};
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA   James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA   Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA   Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT   range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP001044; ACC73376.1; -; Genomic_DNA.
DR   RefSeq; WP_012403549.1; NZ_CADFGH010000005.1.
DR   AlphaFoldDB; B2JQ35; -.
DR   STRING; 391038.Bphy_4256; -.
DR   KEGG; bph:Bphy_4256; -.
DR   eggNOG; COG0247; Bacteria.
DR   eggNOG; COG0277; Bacteria.
DR   HOGENOM; CLU_010756_0_0_4; -.
DR   OrthoDB; 9811557at2; -.
DR   Proteomes; UP000001192; 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; 3.30.70.2190; -; 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   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; 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; PS51379; 4FE4S_FER_2; 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:ACC73376.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001192}.
FT   DOMAIN          53..283
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          646..675
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   1005 AA;  110210 MW;  89DD6A7D0B5D9FEE CRC64;
     MSNATLLTKP IYLVPSAARM STPLANRLRK ELRGDVLFDA ASRGRYSTDA SIYQIMPIGV
     VVPRDQDDLR VALDIARSEN VPLLARGAGS SQCGQTVGEA LVIDTSKWLN QVVAFDKDML
     TVTVEPGIVL DHLNAWLKPH GLWFPVDVST AAQCTIGGMA GNNSCGSRSI EYGNMVHNVE
     AIDAILADGA QARFASLREE QQDARLQQIV EGVKAIAQRE RDEIVAQVPK VLRRVAGYNI
     DLFDCQNPRA YTDDGFANLA HLLVGSEGTL AFSRQLTLRL SPLPAHKMLG VVNFPTFWQA
     MDLTQHIVKL KPVAVELVDR TMIDLAMSNP AFRPVIEKAL VGRPEAILLV EFAGENRDEQ
     FASLKQLTEL MADLGLPDSV VQMPDAAEQK ALWEVRKAGL NIMMSMKGDG KPVSFIEDCA
     VPLEHLAEYT SRLTEVFHRN GTEGTWYAHA SVGTLHVRPI LDMRRDGAHK MRAIAEEAAA
     LVREYKGAYS GEHGDGLCRG EWVAWQYGPR INRAFSEIKA LFDPDNRMNP DKIVRPPKMD
     DARNFRFAPG YKERALTPAL DWSVWNVERD PMTGVESAPG AGSDLAGGLA KAVEMCNNNG
     HCRKFDAGTM CPSYRVTKDE QHVTRGRANT LRLALSGQLG DEGLASQEVK DTLDLCVSCK
     GCKRDCPTGI DMAKFKIEAR AAWAQKHGLR LREKMIAFMP RYAAIAGTMP WLFAFAGGLP
     WFKRAVGWAP QRSLPRFVKP FLGSADVKAF ASSTGAQSAQ KEVLLFVDTF NNSIEPENAR
     AAQQVLEAAG YTVHFNTRAG ERPLCCGRTF LAAGLVDEAK REARRMLDAF RPFVERGIAV
     VGLEPSCLLS LRDEFLQYGL GEEAARLSKF AMLFEEFLVR EHKAGRLTLE LKPLGHADKA
     LLHGHCHQKA FDAFSPVQTV LKWIPGLKVS TVESSCCGMA GSFGYEAEHY GASMAMAELS
     LLPAVRDVDA TTIVVADGTS CRHQIRDGAG VEAVHVARVL ASALK
//