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Database: UniProt
Entry: I3UGT1_ADVKW
LinkDB: I3UGT1_ADVKW
Original site: I3UGT1_ADVKW 
ID   I3UGT1_ADVKW            Unreviewed;       317 AA.
AC   I3UGT1;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=Phosphoglycerate dehydrogenase {ECO:0000313|EMBL:AFK64219.1};
GN   OrderedLocusNames=TKWG_23075 {ECO:0000313|EMBL:AFK64219.1};
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:AFK64219.1, ECO:0000313|Proteomes:UP000005267};
RN   [1] {ECO:0000313|EMBL:AFK64219.1, 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|ARBA:ARBA00005854,
CC       ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; CP003555; AFK64219.1; -; Genomic_DNA.
DR   AlphaFoldDB; I3UGT1; -.
DR   STRING; 1036672.TKWG_23075; -.
DR   KEGG; aka:TKWG_23075; -.
DR   HOGENOM; CLU_019796_1_3_4; -.
DR   OMA; QSDLHEA; -.
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   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; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR   PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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|RuleBase:RU003719}.
FT   DOMAIN          14..304
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          111..282
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   317 AA;  33587 MW;  DEC1105B700C798C CRC64;
     MTTARPKILV TGADLAAQAL HVLQDYEVIY TGALPSEAQL IALVKAHDPV GIIVRYGRIT
     RSVIEHARGL KVISKHGSGI DTIDVAAAKD NGIVVCAAAG ANAAAVAEHA LALLLACAKS
     IAQQNARMHD GHWDKARHKS IELRNKTIGL IGLGSIGRKM ATMCRAMQLN VIAHDPFVTH
     DDNLTLVPLE QIWSEADFIS LHCPLTDDNR NLINEVTLAA CRKGIILINT ARGGLIDETA
     LLAAVQSGQV FAAGLDSFAQ EPPASDHAFF GESQIILSPH VGGVTGQAYI DMGVAAAKNL
     LRSLVDSGIQ SRKQETA
//
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