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
//