ID A0A0D2MZ85_9CHLO Unreviewed; 422 AA.
AC A0A0D2MZ85;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=MNEG_0242 {ECO:0000313|EMBL:KIZ07710.1};
OS Monoraphidium neglectum.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Sphaeropleales; Selenastraceae; Monoraphidium.
OX NCBI_TaxID=145388 {ECO:0000313|EMBL:KIZ07710.1, ECO:0000313|Proteomes:UP000054498};
RN [1] {ECO:0000313|EMBL:KIZ07710.1, ECO:0000313|Proteomes:UP000054498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAG 48.87 {ECO:0000313|EMBL:KIZ07710.1,
RC ECO:0000313|Proteomes:UP000054498};
RX PubMed=24373495; DOI=10.1186/1471-2164-14-926;
RA Bogen C., Al-Dilaimi A., Albersmeier A., Wichmann J., Grundmann M.,
RA Rupp O., Lauersen K.J., Blifernez-Klassen O., Kalinowski J., Goesmann A.,
RA Mussgnug J.H., Kruse O.;
RT "Reconstruction of the lipid metabolism for the microalga Monoraphidium
RT neglectum from its genome sequence reveals characteristics suitable for
RT biofuel production.";
RL BMC Genomics 14:926-926(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; KK100237; KIZ07710.1; -; Genomic_DNA.
DR RefSeq; XP_013906729.1; XM_014051275.1.
DR AlphaFoldDB; A0A0D2MZ85; -.
DR STRING; 145388.A0A0D2MZ85; -.
DR GeneID; 25726360; -.
DR KEGG; mng:MNEG_0242; -.
DR OrthoDB; 1664005at2759; -.
DR Proteomes; UP000054498; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; IEA:UniProtKB-EC.
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 Oxidoreductase {ECO:0000313|EMBL:KIZ07710.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054498}.
FT DOMAIN 1..171
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 422 AA; 44111 MW; EE42341ED27849F0 CRC64;
MPPELVLFPS STEEVSRVLA ACNASRTPVV PFGAGTSIEG HVAALAPGSV CLDMSRMNAV
LQINAADMDC RVQAGVTRKQ LNAELRDSGL HFPVDPGADA TLGGMASTRA SGTNAREQVL
GLTAVLADGR VARLGTRARK SSAGYDLAHL LVGSEGTLGV ITELAIRLHA VPEATAAAVC
EFGSVEDAVE AVTAVMASSI PVARIEILDA AALRAVNAYN KTTFGESPTL FFEFIGSEAG
VKEHAAAAGE LAAAAGGRGF QWATSPEERR RLWEARHSAY WASLALRPGC KGFTTASRKV
IEEAGLQSTL VGHVGDGNFH FILLIDPDDP SEVAKAEDAV RRMVQVAWDA GGTCTGEHGI
GYGKLKYLRE EHGEAPLQMM AAIKAALDPN GILNPGKLGS DAGDAALWQG DDHVLRRRAG
EA
//
