ID M9R3W6_9RHOB Unreviewed; 457 AA.
AC M9R3W6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=OAN307_c12110 {ECO:0000313|EMBL:AGI66912.1};
OS Octadecabacter antarcticus 307.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Octadecabacter.
OX NCBI_TaxID=391626 {ECO:0000313|EMBL:AGI66912.1, ECO:0000313|Proteomes:UP000005307};
RN [1] {ECO:0000313|EMBL:AGI66912.1, ECO:0000313|Proteomes:UP000005307}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=307 {ECO:0000313|EMBL:AGI66912.1,
RC ECO:0000313|Proteomes:UP000005307};
RX PubMed=23671678;
RA Vollmers J., Voget S., Dietrich S., Gollnow K., Smits M., Meyer K.,
RA Brinkhoff T., Simon M., Daniel R.;
RT "Poles Apart: Arctic and Antarctic Octadecabacter strains Share High Genome
RT Plasticity and a New Type of Xanthorhodopsin.";
RL PLoS ONE 8:E63422-E63422(2013).
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; CP003740; AGI66912.1; -; Genomic_DNA.
DR RefSeq; WP_015498954.1; NC_020911.1.
DR AlphaFoldDB; M9R3W6; -.
DR STRING; 391626.OAN307_c12110; -.
DR KEGG; oat:OAN307_c12110; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_3_0_5; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000005307; 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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128}.
FT DOMAIN 35..213
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 457 AA; 47956 MW; 86BEF1279E461186 CRC64;
MSIDAALRAL APVLGDRLSL SKSDLAAHGQ SETHFDPTPP DAVAYPRTTQ EVSQIVKICA
QHRCPVVGYG AGTSLEGHTL ATQGGITVDF RHMAQVLEVH SEDMTVRVQP GITREALNED
LRATGLFFPV DPGANATLGG MAATRASGTT AVRYGTMRDN VMALEVVLAD GRVIRTGSGA
RKSSAGYDLT ALLVGSEGTL GLITELTLKL QGQPEAIAAA TCAFDTIDAA VQAVTATIAM
GIPMARIEFL DAASVAAVNA YSRADFLVTP HLMVEFHGSD AGVAEQAERF GDIAQDCGGS
AFSWASKPED RTRLWQMRHH AYWAIIASRK NTTAIVTDVC VPISKLAQAV AETQADIDAA
PIPAPILGHV GDGNFHAILL IDPDNADEKR AAVDLSAGMA ERALALGGTV TGEHGVGLGK
LPYMAAEHGA GWDVMGQIKR AMDPLNILNP GKVVRLD
//
