ID A0A1Q4YV40_9ACTN Unreviewed; 325 AA.
AC A0A1Q4YV40;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:OKI38431.1};
GN ORFNames=A6A29_10765 {ECO:0000313|EMBL:OKI38431.1};
OS Streptomyces sp. TSRI0281.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1718998 {ECO:0000313|EMBL:OKI38431.1, ECO:0000313|Proteomes:UP000186952};
RN [1] {ECO:0000313|EMBL:OKI38431.1, ECO:0000313|Proteomes:UP000186952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSRI0281 {ECO:0000313|EMBL:OKI38431.1,
RC ECO:0000313|Proteomes:UP000186952};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {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:OKI38431.1}.
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DR EMBL; LWLE01000023; OKI38431.1; -; Genomic_DNA.
DR RefSeq; WP_073723557.1; NZ_LWLE01000023.1.
DR AlphaFoldDB; A0A1Q4YV40; -.
DR STRING; 1718998.A6A29_10765; -.
DR OrthoDB; 4324715at2; -.
DR Proteomes; UP000186952; 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; 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; 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.
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:UP000186952}.
FT DOMAIN 32..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"
FT REGION 306..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 325 AA; 35454 MW; B6D55676FC42B49A CRC64;
MPEPVLLVLD SAPSPRLGRL TGRVGVRYAN ERSLAAQLPL ADVLLVWDFT SDAVRAAWPG
AGPRPRWVHT ASAGVDRLLC PELAASDTVV TNARGIFERP IAEYVAGLVL AFAKDLPGTL
DLQRQRRWHH REGQQIAGSR AVVVGAGPIG REITKLLHGL GVRVALVGRT ARRTIHGLED
LDRLTARADW VICAAPLTES TRGMFGARFF GLMQPSARFI NVGRGPMVVE GELTDALRKR
WIAGAALDVF QEEPLGPDSP LWDVPGLLIS PHMSGDTVGW RDRLGEQFVR MYELWADGQP
LPNVVDKKRG YVPSPDLNQG DAPLT
//
