ID A0A0N0JUE2_9PROT Unreviewed; 472 AA.
AC A0A0N0JUE2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=IP84_10460 {ECO:0000313|EMBL:KPF68165.1};
OS beta proteobacterium AAP99.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1523428 {ECO:0000313|EMBL:KPF68165.1, ECO:0000313|Proteomes:UP000037960};
RN [1] {ECO:0000313|EMBL:KPF68165.1, ECO:0000313|Proteomes:UP000037960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP99 {ECO:0000313|EMBL:KPF68165.1,
RC ECO:0000313|Proteomes:UP000037960};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) 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:KPF68165.1}.
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DR EMBL; LJIA01000010; KPF68165.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0JUE2; -.
DR STRING; 1523428.IP84_10460; -.
DR PATRIC; fig|1523428.3.peg.555; -.
DR OrthoDB; 8522822at2; -.
DR Proteomes; UP000037960; 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:UP000037960}.
FT DOMAIN 47..224
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 472 AA; 50694 MW; 177DB88DC35B4230 CRC64;
MNAPLPLRTT PPLTEAFLAA LSARFGKQLS TAQAVREHHG RDESPFPLTP PDAVVFAQST
QDIADCVTLC AAHAVPVVPY GAGSSLEGNF LAVQGGVCID VSQMNAILAI NAEDLTATVQ
AGVTRKQLNE ALKDTGLFFP IDPGADASLG GMSATRASGT NAVRYGTMRE NVLGLTVVTP
ACTVIHTARR ARKSSAGYDL TRLYVGSEGT LGVIAEVTVK LYPQPEAISA AVCTFPSVDD
AVATTIEIIQ MGVPIARCEI LDANAVAAVN KHDQLTLPEQ PMLLFEFHGS PASVREQAET
VQAIAAEHGG GHFEWAEKPE DRSRLWKARH NAYFALLQMK PGCRAVTTDT CVPISRLAEC
FRETVADCER LKAEHGIPYG IVGHVGDGNF HVLMLCDPDK PEERDWVEAV NDRLVQRALD
LDGTCTGEHG VGLHKIDFLV KEHGDETLAV MRAIKRALDP QNLMNPGKIL RL
//
