ID A8TR13_9PROT Unreviewed; 468 AA.
AC A8TR13;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=BAL199_04794 {ECO:0000313|EMBL:EDP64749.1};
OS alpha proteobacterium BAL199.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=331869 {ECO:0000313|EMBL:EDP64749.1, ECO:0000313|Proteomes:UP000003417};
RN [1] {ECO:0000313|EMBL:EDP64749.1, ECO:0000313|Proteomes:UP000003417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL199 {ECO:0000313|EMBL:EDP64749.1,
RC ECO:0000313|Proteomes:UP000003417};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) 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:EDP64749.1}.
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DR EMBL; ABHC01000007; EDP64749.1; -; Genomic_DNA.
DR AlphaFoldDB; A8TR13; -.
DR STRING; 331869.BAL199_04794; -.
DR eggNOG; COG0277; Bacteria.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000003417; 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:UP000003417}.
FT DOMAIN 46..223
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 468 AA; 50219 MW; E7E27E17CE5DEA90 CRC64;
MQVIPVASDA TARAAALAAL QARFGDRIST GEAIRRQHGT DESYHPTVAP DAVFFAQSTE
EVSQAVTICA AHKWPVIPFG VGTSLEGGVA ALHGGLSIDL SGMNAVLEVN AEDLDVRVQA
GVTRKQLNEH LRDTGLFFPI DPGADASIGG MCATRASGTN AVRYGTMRDN VLSLTVVMAD
GRVVRTARRA KKSAAGYDLT RLFVGSEGTL CVITEIQLRV YGIPEAISAA VCQFADLESA
VNTCILTIQT GVPVARVELL DDAQMAACIA HSKLEGLEAM PTLFFEFHGT NAGVIEQAET
VQGIAQELGG TDFQWATKPE DRSKLWEARH NAYYAALAQR PGSKGWPTDV CVPISRLAEC
IIETKKDLKE TGLYAPLVGH VGDGNFHLVY VIDPSSEDEM RRAKEHSDRM VLRALAMEGT
CTGEHGVGYG KIEFLAAELP EAVPVMRAVK QALDPDNIMN PGKLFRMN
//
