ID A0A157QW13_9BORD Unreviewed; 467 AA.
AC A0A157QW13;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN Name=glcD2 {ECO:0000313|EMBL:SAI73446.1};
GN ORFNames=SAMEA3906487_03712 {ECO:0000313|EMBL:SAI73446.1};
OS Bordetella trematum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=123899 {ECO:0000313|EMBL:SAI73446.1, ECO:0000313|Proteomes:UP000076825};
RN [1] {ECO:0000313|EMBL:SAI73446.1, ECO:0000313|Proteomes:UP000076825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H044680328 {ECO:0000313|EMBL:SAI73446.1,
RC ECO:0000313|Proteomes:UP000076825};
RG Pathogen Informatics;
RL Submitted (APR-2016) 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}.
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DR EMBL; LT546645; SAI73446.1; -; Genomic_DNA.
DR RefSeq; WP_025514536.1; NZ_UFUJ01000001.1.
DR AlphaFoldDB; A0A157QW13; -.
DR STRING; 123899.SAMEA3906487_03712; -.
DR GeneID; 56589054; -.
DR KEGG; btrm:SAMEA390648703712; -.
DR PATRIC; fig|123899.6.peg.3713; -.
DR eggNOG; COG0277; Bacteria.
DR OrthoDB; 8522822at2; -.
DR Proteomes; UP000076825; Chromosome 1.
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:SAI73446.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076825}.
FT DOMAIN 46..223
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 467 AA; 50571 MW; 1C20E7E43F84868C CRC64;
MNAPLPDLRR PVPPACLEAL GAIFGDRLSV SAAVREHHGR DESPYPPMLP DAVVFAQNTD
EVAQVARLCN EHRVPLIPYG AGSSLEGHLL AIEGGISLDL SQMNQVLSVN AEDLTATVQA
GVTRKQLNEE IRSTGLFFPI DPGADASLGG MAATRASGTN AVRYGTMREN VMSLTVVTAD
GRVVRTAGRA RKSSAGYDLT RIFVGSEGTL GIITEVTVRL YPQPEAVSAA VCNFPSLDDA
VQSVIEIIQM GVPVARVEFM DAAAVRAVNL YSKLTLRETP MLVFEFHGSP AGVQEQAETV
QAITAEHGGM DFEWAERPED RNRLWTARHN AYFAGLQLRP GCRASTTDVC VPISRLADCV
RETVDELDQA SFPYTIVGHV GDGNFHVLML LDGDNEAEWQ ESETINHNLV RRAIAADGTC
TGEHGVGLHK MQFMQQEHGD DALALMRSLK HAFDPNNILN PGKIIAW
//
