ID A0A0B4R9Z5_9BACL Unreviewed; 461 AA.
AC A0A0B4R9Z5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=Plano_0607 {ECO:0000313|EMBL:AIY04572.1};
OS Planococcus sp. PAMC 21323.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=1526927 {ECO:0000313|EMBL:AIY04572.1, ECO:0000313|Proteomes:UP000031496};
RN [1] {ECO:0000313|EMBL:AIY04572.1, ECO:0000313|Proteomes:UP000031496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 21323 {ECO:0000313|EMBL:AIY04572.1,
RC ECO:0000313|Proteomes:UP000031496};
RA Jung J.-H., Joe M.-H., Cho Y.-J., Lee S.G., Han S.J., Lim S., Choi J.-i.;
RT "Complete genome sequence of Planococcus sp. PAMC21323 isolated from the
RT Antarctica.";
RL Submitted (AUG-2014) 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; CP009129; AIY04572.1; -; Genomic_DNA.
DR RefSeq; WP_038702910.1; NZ_CP009129.1.
DR AlphaFoldDB; A0A0B4R9Z5; -.
DR STRING; 1526927.Plano_0607; -.
DR KEGG; pln:Plano_0607; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_3_0_9; -.
DR OrthoDB; 9767256at2; -.
DR Proteomes; UP000031496; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000031496}.
FT DOMAIN 40..217
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 461 AA; 50473 MW; BBFDDE9059ED62A9 CRC64;
MAIANQEKIL DSLKEHLTAE QISVNTTIKE LHGQDESYHQ MKLPDIVVFP ETTEQVSAIM
KVSAQHKIPV IPFGLGSSLE GHVIPQSGGM TVDFSLMNKI IEVYEEDFLV TVQPGVTRTQ
LNKELKKYGL FFTVDPGADA TLGGMVATNA SGTTTVRYGV MRDQVRDLEV VLADGAVIHT
GSKAAKSSSG LHLNGLFVGS EGTLGCFTEM TLRVYGIPEF ITAARASFET VKDAVEAVVS
ILQAGIPIAR VELLDEESMR QVNKYNDTAY LEKPTLFLEF HGNEAGLKQD VEFTQEIVQG
HGCKEVDFET DTAARNRLWE ARHSLAYAYI HAHPGKKMMV TDVCLPISEL AGAVEHAREN
LLELGLPGGV LGHVGDGNYH ALIMIDMNNL EEVERSQKFN ERIVLYALER GGTCTGEHGV
GIGKQKYQRQ EHGGAFDVME KIKVALDPAN LLNPGKNIKI E
//
