ID A0A0G4AZ05_9BACT Unreviewed; 536 AA.
AC A0A0G4AZ05;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:AKM80844.1};
DE EC=1.1.2.4 {ECO:0000313|EMBL:AKM80844.1};
GN ORFNames=UW38_C0001G1014 {ECO:0000313|EMBL:AKM80844.1};
OS Candidatus Saccharibacteria bacterium GW2011_GWC2_44_17.
OC Bacteria; Candidatus Saccharibacteria.
OX NCBI_TaxID=1619070 {ECO:0000313|EMBL:AKM80844.1, ECO:0000313|Proteomes:UP000035655};
RN [1] {ECO:0000313|EMBL:AKM80844.1, ECO:0000313|Proteomes:UP000035655}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP011211; AKM80844.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4AZ05; -.
DR STRING; 1619070.UW38_C0001G1014; -.
DR KEGG; sbag:UW38_C0001G1014; -.
DR Proteomes; UP000035655; Chromosome.
DR GO; GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 2.
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:SF103; GLYCOLATE OXIDASE SUBUNIT GLCE; 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 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:AKM80844.1}.
FT DOMAIN 34..269
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 536 AA; 59611 MW; 026401FB4982B294 CRC64;
MSGYLQPAEK LVISGDISHE WESRQAVSRD ASIFEVMPAG VISPRSVEDI RRSVVWATQE
TRAGRPVSLT ARVGGTCMSG GPLTSSYVLD LKKYLHNVGK IDTVGRSITT QSGAMHRVIE
EKTMAEGLLF APYTSSHDIC GIGGMIGNNA SGEMSIKYGP TSSNVATLKA VLSDGNQYKF
GPLTRAEVEK KKQLATYEGE IYRRVTALLE QNKDTIAANH PRTVKNAAGF QLWELWDRHE
QVFDLSRLFV GSQGTLGIVT EATLKLVKRA NFSRMIVTPI SDLMNLPEVV RTTLAYEPAT
CETFDHFTYE LAEQYHPEDA ARAHVAKGKH IVILSVFQGD DQQHTDVLAG QAKEKLESLG
HETFWIDEPA TIESFLNIRR WSFKMLLEHP TPGTRAEAFL EDTIVPLDRY GEFLTQLEAI
LREYNMIYTY AGHIGAGSIR LVPLVDMEAD GAAERVMELE TRVNDLVIEF GGSISVDHND
GIIRTPYLEK QFGSEMVRLF EEVKLLFDPL GIFNPGKKVG GTYDDALKYI IRENVA
//
