ID A0A2P4UM09_9ACTN Unreviewed; 329 AA.
AC A0A2P4UM09;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Putative 2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:POM26082.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:POM26082.1};
GN ORFNames=BTM25_04690 {ECO:0000313|EMBL:POM26082.1};
OS Actinomadura rubteroloni.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=1926885 {ECO:0000313|EMBL:POM26082.1, ECO:0000313|Proteomes:UP000242367};
RN [1] {ECO:0000313|EMBL:POM26082.1, ECO:0000313|Proteomes:UP000242367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-2 {ECO:0000313|EMBL:POM26082.1,
RC ECO:0000313|Proteomes:UP000242367};
RX PubMed=28463423; DOI=10.1002/chem.201701005;
RA Guo H., Benndorf R., Leichnitz D., Klassen J.L., Vollmers J., Gorls H.,
RA Steinacker M., Weigel C., Dahse H.M., Kaster A.K., de Beer Z.W.,
RA Poulsen M., Beemelmanns C.;
RT "Isolation, Biosynthesis and Chemical Modifications of Rubterolones A-F:
RT Rare Tropolone Alkaloids from Actinomadura sp. 5-2.";
RL Chemistry 23:9338-9345(2017).
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:POM26082.1}.
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DR EMBL; MTBP01000001; POM26082.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P4UM09; -.
DR Proteomes; UP000242367; 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 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; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 1.
DR PANTHER; PTHR10996:SF178; GLYOXYLATE REDUCTASE 1; 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 Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW ECO:0000313|EMBL:POM26082.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000242367}.
FT DOMAIN 27..320
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 115..288
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 329 AA; 34362 MW; 5840D26918108646 CRC64;
MTDQWRVLAL PPLDVSLLRG LTDPLGGAAE LVVPEARTTA ALHRAIEDAE IVVGDYTGEL
ALDAAAVAHA RRLAFVQMPQ VGVDGVDLDA LTRAGVPVAN TAGANSRAVA EWAVGAAFAL
CRHLAWADRQ VRAGGWPQGE LLARGTREIH AQRVGVVGHG AIGALAADLF AALGAPVAYW
SRTRRENARA EYRPLDDLLA ESDIVVLALP LTGETAGLFD AARIGRMKHG ALLVNVARGG
IVDENALLAA LDDGSLAGAA LDVFEHEPPP QDAKLRTHDN VLVSPHVAGG TVQAQLAIIQ
TVADNVQAAV RGEPVDHVVN GLGPVITRR
//