ID   A0A085EKK1_9FLAO        Unreviewed;       701 AA.
AC   A0A085EKK1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE            EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN   ORFNames=FEM08_15270 {ECO:0000313|EMBL:KFC59746.1};
OS   Flavobacterium gilvum.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1492737 {ECO:0000313|EMBL:KFC59746.1, ECO:0000313|Proteomes:UP000028636};
RN   [1] {ECO:0000313|EMBL:KFC59746.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EM1308 {ECO:0000313|EMBL:KFC59746.1};
RA   Shin S.-K., Yi H.;
RT   "Genome Sequence of Flavobacterium sp. EM1308.";
RL   Submitted (MAY-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFC59746.1}.
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DR   EMBL; JNCP01000038; KFC59746.1; -; Genomic_DNA.
DR   RefSeq; WP_051877739.1; NZ_JNCP01000038.1.
DR   AlphaFoldDB; A0A085EKK1; -.
DR   STRING; 1492737.EM308_03540; -.
DR   KEGG; fgl:EM308_03540; -.
DR   PATRIC; fig|1492737.3.peg.1516; -.
DR   eggNOG; COG0277; Bacteria.
DR   eggNOG; COG0479; Bacteria.
DR   OrthoDB; 9767256at2; -.
DR   Proteomes; UP000028636; Unassembled WGS sequence.
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:InterPro.
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; 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; 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   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; PS51379; 4FE4S_FER_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128}.
FT   DOMAIN          39..267
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
FT   DOMAIN          533..562
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   COILED          185..219
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   701 AA;  77914 MW;  E90D2DF5D33339DF CRC64;
     MLAPSYQKLK DILSVTIDSK RILTNPLQTL AYGTDASFYR LIPKIVILAH NEAEVIEIIK
     QAKKLDIALT FRAAGTSLSG QAITDSVLVV ATHGWKNFEL LEENKKIKLE PGIVGARANT
     FLAPHGLKIG PDPASIGACM IGGIVANNAS GMCCGTAQNS YQTIADIRIV LHDGTVLDTA
     DAKSVDAFKK NQTDLIQEIE NLRDQIKSDE TLYNQIKNKF KIKNTTGYSI NALVDYQDSI
     EIIKHLMVGS EGTLAFISNV TFKTIIDEKH KSCSLIFFNT IKDACNATIL LKSAPVAAVE
     LLDRESIRSV ENDDDAPAYF KTLPESACAL LVECRDNDVT VLKEKQDAIR LQIQSIPTYT
     NYEFTSNPKQ YYFNWKARKG LLPTVGGLRK NGTTVIIEDV AFPLPQLADA CLELKDLFKK
     YEYHDAVLFG HALEGNLHFV FSQDFSNQAE VDRYEKLMSE LAVLVVDRFN GSLKAEHGTG
     RNMAPFVEKE WGATAYEIMK RIKNIFDPNN KINPDVLINP DPKAHLKNLK PMPESHAIVD
     KCMECGFCEP HCVSEGLTLS PRQRIVIARE ISRLEESHDN PQRLADIRKD VTYQLDETCA
     TDGLCALACP VHIDTGKFVK TWRANELNDS NKKAGAFIGS HMAETTAVMR TGLKMVSFFH
     SLFGTKIMTT LSNGFHFISF GKVPKWIPEM PKGANKINTK N
//