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Database: UniProt
Entry: A0A2M8LTE9_9ACTN
LinkDB: A0A2M8LTE9_9ACTN
Original site: A0A2M8LTE9_9ACTN 
ID   A0A2M8LTE9_9ACTN        Unreviewed;       334 AA.
AC   A0A2M8LTE9;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:PJE95227.1};
GN   ORFNames=CUT44_26155 {ECO:0000313|EMBL:PJE95227.1};
OS   Streptomyces carminius.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2665496 {ECO:0000313|EMBL:PJE95227.1, ECO:0000313|Proteomes:UP000230407};
RN   [1] {ECO:0000313|EMBL:PJE95227.1, ECO:0000313|Proteomes:UP000230407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TRM SA0054 {ECO:0000313|EMBL:PJE95227.1,
RC   ECO:0000313|Proteomes:UP000230407};
RA   Wang Y., Luo X., Wan C., Zhang L.;
RT   "Streptomyces carmine sp. nov., a novel actinomycete isolated from Sophora
RT   alopecuroides in Xinjiang, China.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC       ECO:0000256|RuleBase:RU003719}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PJE95227.1}.
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DR   EMBL; PGGW01000067; PJE95227.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M8LTE9; -.
DR   Proteomes; UP000230407; Unassembled WGS sequence.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   CDD; cd12183; LDH_like_2; 1.
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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230407}.
FT   DOMAIN          11..326
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          110..296
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   334 AA;  36481 MW;  CB899F575FC55FD4 CRC64;
     MDIVAYGVVT DELPLLERAF KGQHRLRCLD LVLNRDTAAT AAGCTVVCSS VNDVLDEEVL
     TTLADGGTKL VTQRATGYNN IDLDAARKLG LAVSRVSSYS PYSVAEFAWT LALAVNRRVA
     RSVARTRDFD FRLNGLLGRD FHGRTAGVVG TGKIGAAFAR IAAGFGMRLL GWDIAENPEC
     LELGMEYVER ERLFAEADLV SLHVPLLPDT YHLVDRAALA RMKDDAILIN TSRGGLIDAQ
     ALVDTLRAGR LDGVGLDVYE EEAGVFFFDR SLDVITDDTL ARLMTFRNVL VSSHQAYFTH
     DAVEEIVRTT ARNVEDHLAG RANTNTLVPP PDRG
//
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