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Database: UniProt
Entry: I3UDI7_ADVKW
LinkDB: I3UDI7_ADVKW
Original site: I3UDI7_ADVKW 
ID   I3UDI7_ADVKW            Unreviewed;       320 AA.
AC   I3UDI7;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase nad-binding protein {ECO:0000313|EMBL:AFK63075.1};
GN   OrderedLocusNames=TKWG_15315 {ECO:0000313|EMBL:AFK63075.1};
OS   Advenella kashmirensis (strain DSM 17095 / LMG 22695 / WT001)
OS   (Tetrathiobacter kashmirensis).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae.
OX   NCBI_TaxID=1036672 {ECO:0000313|EMBL:AFK63075.1, ECO:0000313|Proteomes:UP000005267};
RN   [1] {ECO:0000313|EMBL:AFK63075.1, ECO:0000313|Proteomes:UP000005267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17095 / LMG 22695 / WT001
RC   {ECO:0000313|Proteomes:UP000005267};
RX   PubMed=21914874; DOI=10.1128/JB.05781-11;
RA   Ghosh W., George A., Agarwal A., Raj P., Alam M., Pyne P., Das Gupta S.K.;
RT   "Whole-genome shotgun sequencing of the sulfur-oxidizing chemoautotroph
RT   Tetrathiobacter kashmirensis.";
RL   J. Bacteriol. 193:5553-5554(2011).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; CP003555; AFK63075.1; -; Genomic_DNA.
DR   RefSeq; WP_014751166.1; NC_017964.1.
DR   AlphaFoldDB; I3UDI7; -.
DR   STRING; 1036672.TKWG_15315; -.
DR   KEGG; aka:TKWG_15315; -.
DR   HOGENOM; CLU_019796_1_3_4; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000005267; 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; cd12162; 2-Hacid_dh_4; 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; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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; PS00670; D_2_HYDROXYACID_DH_2; 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}.
FT   DOMAIN          26..316
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          110..290
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   320 AA;  34752 MW;  D7394465E3FDD590 CRC64;
     MSSSARIVFL DRATLPDFIA LKAFEFEHEV IAYDQTAPAD VAQRIRNAQI VITNKVPVSA
     QDVAQAGELK LVAVAATGTN IVDIEACRDK GIVVTNIRNY AVNTVPEHTL ALIFALRRSL
     LPYHRSVGQG RWAQSGQFCY FDYPVSDLAD STIGIFGSGA LGSAVARRAQ ALGMKVLFAA
     RKGETEVKET HTPFEEVIAQ ADILTLHLPL TPATRHMIGA AELAQMKPTA LLINTARGGL
     VDEAALAEAL ENNSIGGAGF DVVTQEPMPD THPFMRLMNR PDFILTPHVA WASRQAIQSL
     ADQLVDNINA FVRNDIRNQV
//
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