ID V4YR94_9PROT Unreviewed; 468 AA.
AC V4YR94;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=MOLA814_01268 {ECO:0000313|EMBL:ESS15686.1};
OS Betaproteobacteria bacterium MOLA814.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1408164 {ECO:0000313|EMBL:ESS15686.1, ECO:0000313|Proteomes:UP000017838};
RN [1] {ECO:0000313|EMBL:ESS15686.1, ECO:0000313|Proteomes:UP000017838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MOLA814 {ECO:0000313|EMBL:ESS15686.1,
RC ECO:0000313|Proteomes:UP000017838};
RX PubMed=24356832;
RA Courties A., Riedel T., Jarek M., Intertaglia L., Lebaron P., Suzuki M.T.;
RT "Genome Sequence of Strain MOLA814, a Proteorhodopsin-Containing
RT Representative of the Betaproteobacteria Common in the Ocean.";
RL Genome Announc. 1:e01062-13(2013).
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:ESS15686.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AYMW01000001; ESS15686.1; -; Genomic_DNA.
DR AlphaFoldDB; V4YR94; -.
DR STRING; 1408164.MOLA814_01268; -.
DR PATRIC; fig|1408164.3.peg.254; -.
DR eggNOG; COG0277; Bacteria.
DR OrthoDB; 8522822at2; -.
DR Proteomes; UP000017838; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 Oxidoreductase {ECO:0000313|EMBL:ESS15686.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017838}.
FT DOMAIN 48..225
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 468 AA; 49711 MW; D9C06634BABA89FD CRC64;
MNASLPAIAI RDVPSAFTDA LVTRFGTQFS QAMAVREQHG RDESAFTHVP PPCGVVFALS
TADVSDAVAL AAHYRVPVIP FGVGSSLEGH LLAVQGGISV DVSRMNQVLR IDAEDLTVTV
QPGVTRNAVN AAVKDQGLFF PIDPGADASI GGMSATRASG TNAVRYGTMR ENVLALEVVT
ASGEIIRTGT RAKKSSAGYD LTRLMVGSEG TLGVMTEITL KLYPLPEAVS AAVCSFPSIE
AAVRATIHII QMGVPIARCE FLDAQTVGMV NKHAKLNLRE EAMLLMEFHG SPAGVKEQAE
IVQDIATDLG GQAFEWATTP EERTKLWAAR HNAYFAAIQS RPGCRAISTD TCVPISRLAD
CLLDSVEEAN ATGLPYFLLG HVGDGNFHFG YLIDPDSESE RSTAEALNHK LVNRALALGG
TCTGEHGIGL HKMDFLRTEA GEGAVAMMRA IKTALDPHNI MNPGKIFS
//
