ID D5E610_MYCCM Unreviewed; 345 AA.
AC D5E610;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE SubName: Full=D-lactate dehydrogenase {ECO:0000313|EMBL:ADE19955.1};
DE EC=1.1.1.28 {ECO:0000313|EMBL:ADE19955.1};
GN OrderedLocusNames=MCRO_0586 {ECO:0000313|EMBL:ADE19955.1};
OS Mycoplasma crocodyli (strain ATCC 51981 / MP145).
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=512564 {ECO:0000313|EMBL:ADE19955.1, ECO:0000313|Proteomes:UP000001845};
RN [1] {ECO:0000313|Proteomes:UP000001845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51981 / MP145 {ECO:0000313|Proteomes:UP000001845};
RA Glass J.I., Durkin A.S., Hostetler J., Jackson J., Johnson J., May M.A.,
RA Paralanov V., Radune D., Szczypinski B., Brown D.R.;
RT "The complete genome of Mycoplasma crocodyli MP145.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MP145;
RA Ma Z., Wang X., Liu H.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ADE19955.1, ECO:0000313|Proteomes:UP000001845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51981 / MP145 {ECO:0000313|Proteomes:UP000001845};
RX PubMed=21460083; DOI=10.1128/JB.00309-11;
RA Brown D.R., Farmerie W.G., May M., Benders G.A., Durkin A.S., Hlavinka K.,
RA Hostetler J., Jackson J., Johnson J., Miller R.H., Paralanov V., Radune D.,
RA Szczypinski B., Glass J.I.;
RT "Genome sequences of Mycoplasma alligatoris A21JP2T and Mycoplasma
RT crocodyli MP145T.";
RL J. Bacteriol. 193:2892-2893(2011).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP001991; ADE19955.1; -; Genomic_DNA.
DR RefSeq; WP_013054731.1; NC_014014.1.
DR AlphaFoldDB; D5E610; -.
DR STRING; 512564.MCRO_0586; -.
DR KEGG; mcd:MCRO_0586; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_1_14; -.
DR OMA; VIVTAHQ; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000001845; Chromosome.
DR GO; GO:0008720; F:D-lactate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43026; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR PANTHER; PTHR43026:SF1; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW ECO:0000313|EMBL:ADE19955.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001845}.
FT DOMAIN 3..329
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 110..304
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 345 AA; 38341 MW; 772F7A9A7E970DA0 CRC64;
MKIAFFDAKE YDIKYFDKVN NGRHEITYFK ENLGINTIKL AKGFDAVCGF VNTFGDKFIL
ELLAKEGIKV WLQRSMGYNK VDLAKAAELG ISVFRIPNYS AESVAEFAMG SMLALNRKIV
IANRRVKKYN FSLNDLDGLC VHGSTVGVIG GGKIGQSFVK IAKGMGARVL VFDSFNETNF
PNLAKELGFE YAPLTKVLKE SDFISLHAPL LPSTRYVIDE DAIKLMKHGV IIINTARGEL
MNITAVIDGL KKGIIGGLAS DVLEREEGRF YEDISNRAEE YQELDPEWYE LIKMKNVLIT
SHQAFLTNVA LTQIASITLN NADDAQKGDF SKALLMQPDG KIKNG
//