ID A0A0U3P0N3_9ACTN Unreviewed; 315 AA.
AC A0A0U3P0N3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:ALV35504.1};
GN ORFNames=AS200_28265 {ECO:0000313|EMBL:ALV35504.1};
OS Streptomyces sp. CdTB01.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV35504.1, ECO:0000313|Proteomes:UP000068029};
RN [1] {ECO:0000313|EMBL:ALV35504.1, ECO:0000313|Proteomes:UP000068029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CdTB01 {ECO:0000313|EMBL:ALV35504.1,
RC ECO:0000313|Proteomes:UP000068029};
RA Tian Y., Zhou G., Yang H., Lu X.;
RT "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT bacterium tolerant to cadmium.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP013743; ALV35504.1; -; Genomic_DNA.
DR RefSeq; WP_058925114.1; NZ_CP013743.1.
DR AlphaFoldDB; A0A0U3P0N3; -.
DR STRING; 1725411.AS200_28265; -.
DR KEGG; scx:AS200_28265; -.
DR OrthoDB; 4324715at2; -.
DR Proteomes; UP000068029; Chromosome.
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; cd05300; 2-Hacid_dh_1; 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; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000068029}.
FT DOMAIN 26..305
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 107..274
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 315 AA; 34770 MW; DC61D56A293914CD CRC64;
MTVPTLLVLD ADPLPRLGRL TGRVRVEHAD DSTLAERLPH ADVLLVWDFT STAVRDAWPG
EGPRPRWVHT ASAGVDHLMC PELAASDTVV TNARGVFDQP IAEYVAALVL SMAKELPRTW
ELQRERTWRH RETQRVAGTR AVVVGSGPIG RTIARLLKAL DVTTAIVGRT PHTGIHGPED
LDRLIARADW VIAAAPLTEQ TYGMFDARRF DVMQPSARFI NIGRGALVVE DALAEALAKR
WIAGAALDVF EHEPLAPDSP LWEVPGLIVS PHMSGDTVGW RDQLGAQFVE LWERWEAGRP
LLNVVDKKRG YVPGR
//
