ID A0A127W3T0_SPOPS Unreviewed; 455 AA.
AC A0A127W3T0;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-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 ORFNames=AZE41_18115 {ECO:0000313|EMBL:AMQ07699.1};
OS Sporosarcina psychrophila (Bacillus psychrophilus).
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1476 {ECO:0000313|EMBL:AMQ07699.1, ECO:0000313|Proteomes:UP000071057};
RN [1] {ECO:0000313|EMBL:AMQ07699.1, ECO:0000313|Proteomes:UP000071057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6497 {ECO:0000313|EMBL:AMQ07699.1,
RC ECO:0000313|Proteomes:UP000071057};
RA Yan W.;
RT "Complete genome sequence of the Sporosarcina psychrophila DSM6497, a
RT psychrophila Bacillus that can mediate the Ca2+ precipitation.";
RL Submitted (MAR-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; CP014616; AMQ07699.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A127W3T0; -.
DR STRING; 1476.AZE41_18115; -.
DR KEGG; spsy:AZE41_18115; -.
DR Proteomes; UP000071057; Chromosome.
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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128}.
FT DOMAIN 37..214
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 455 AA; 50032 MW; CCF1BB5584A8EEAA CRC64;
MEQVNLINEL KKVLTSDRVT NNQTVLEQHG RDESYHTPHL PDVVVFPEST EEVSLIMKLA
NKYKVAVVPF GVGTSLEGNI IPYNNGIMID FSLMNHILEV RENDLLVKVQ PGVTRMQLNK
ELKKYGLFFS VDPGADATLG GMAATNASGT TSVKYGVMRD QVRDLEVVLA DGKIIHTGNL
AAKSSSGYHL NGIFVGSEGT LGCFTELTLN VYGIPEHTVA ARASFTLVDD AVEAVIAILQ
AGVPVARIEL IDEHSMKQIN HYSNTIYKEV PTLFLEFHGN KAGLEQDIIF TQEILQDKNC
REILFEEETA KKNLLWEARH NAAYAYTHGH PGKKQMITDV CLPISELVGA IKDAREAVEE
SGLAAGIVGH VGDGNYHVLL MMDLNNPEEI SKANKVNERI VHYALAKGGT CSGEHGVGIG
KKKYQRLEHG NAFEVMQKIK KALDPNNILN PNKIL
//
