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Database: UniProt
Entry: A0A2P4UM09_9ACTN
LinkDB: A0A2P4UM09_9ACTN
Original site: A0A2P4UM09_9ACTN 
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
//
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