ID F1W463_9BURK Unreviewed; 469 AA.
AC F1W463;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=IMCC9480_1624 {ECO:0000313|EMBL:EGF30356.1};
OS Oxalobacteraceae bacterium IMCC9480.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae.
OX NCBI_TaxID=937450 {ECO:0000313|EMBL:EGF30356.1, ECO:0000313|Proteomes:UP000004494};
RN [1] {ECO:0000313|EMBL:EGF30356.1, ECO:0000313|Proteomes:UP000004494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC9480 {ECO:0000313|EMBL:EGF30356.1,
RC ECO:0000313|Proteomes:UP000004494};
RX PubMed=21572000; DOI=10.1128/JB.05088-11;
RA Oh H.M., Lee K., Jang Y., Kang I., Kim H.J., Kang T.W., Kim S.Y., Cho J.C.;
RT "Genome sequence of strain IMCC9480, a xanthorhodopsin-bearing
RT betaproteobacterium isolated from the Arctic Ocean.";
RL J. Bacteriol. 193:3421-3421(2011).
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:EGF30356.1}.
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DR EMBL; AEPR01000749; EGF30356.1; -; Genomic_DNA.
DR AlphaFoldDB; F1W463; -.
DR OrthoDB; 8522822at2; -.
DR Proteomes; UP000004494; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000004494}.
FT DOMAIN 48..225
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 469 AA; 50150 MW; BC222537F4260D50 CRC64;
MNHIVNLAAL RKPLPAALLA QLRALLGERL STTQAMREHH GRDESSYAPM LPDAVAFAHS
TDEVAAIVSA CNTHGVPVIP FGSGTSLEGH ILALQGGISI DLSQFNRVIA THAEDLTATV
QAGVTRKQLN VELKDTGLFF PIDPGADASL GGMAATRASG TNAVRYGTMR ENTLALTVVT
ADGRVIKTGT RARKSSAGYD LTRLYVGSEG TLGIITEVTV RLYPQPEAIS AAVCSFASAG
DAVNAVIELI QLGVPVARVE FLDENGVRAI NAHDHLGLPE QPLLLFEFHG STASVAEQAA
QVRDIVAGHQ ATGFDWATRP EDRSRLWAAR HNAYFALLQL RPGCTAISTD CCVPISRLAE
CILDTKADCE QHQMVYSIIG HVGDGNFHVL MMVDPNDAAD IAQAEAINAR MVTRALAMDG
TCTGEHGVGL HKMDFLIEEH GVNAIDTMRA IKHALDPKNI MNPGKIIRW
//
