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Database: UniProt
Entry: A0A1I1HZA5_9RHOB
LinkDB: A0A1I1HZA5_9RHOB
Original site: A0A1I1HZA5_9RHOB 
ID   A0A1I1HZA5_9RHOB        Unreviewed;       322 AA.
AC   A0A1I1HZA5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Phosphoglycerate dehydrogenase {ECO:0000313|EMBL:SFC29539.1};
GN   ORFNames=SAMN04488094_103346 {ECO:0000313|EMBL:SFC29539.1};
OS   Tropicimonas isoalkanivorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Tropicimonas.
OX   NCBI_TaxID=441112 {ECO:0000313|EMBL:SFC29539.1, ECO:0000313|Proteomes:UP000198728};
RN   [1] {ECO:0000313|EMBL:SFC29539.1, ECO:0000313|Proteomes:UP000198728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19548 {ECO:0000313|EMBL:SFC29539.1,
RC   ECO:0000313|Proteomes:UP000198728};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; FOLG01000003; SFC29539.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1HZA5; -.
DR   STRING; 441112.SAMN04488094_103346; -.
DR   OrthoDB; 7374922at2; -.
DR   Proteomes; UP000198728; 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   CDD; cd05300; 2-Hacid_dh_1; 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; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR   PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-RELATED; 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|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198728}.
FT   DOMAIN          30..314
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          108..284
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   322 AA;  33891 MW;  9D4449F00E90479F CRC64;
     MKLVVRSQLP LGNRIARALE DLPFVSEVVV PADAEALYAA LPGATGLITM NSLYDAALAD
     ALERTPSLRW LQLLSAGFEN LAAHGVPFGV TVTNAGNGRT ANVAEHALAL ALALYRGIPV
     AVASQQACRW APPIAESMGT LEGARATVLG YGSIGQAIAR RLAAFDAHVV ALNRSPRQDG
     IVGETRPLED LDAVLAETEI LFVAVALVPE TKHLVDARRL ALMPRGARLV NIARGEVLDT
     DGLVDALGSG LLFGAGIDTT DPEPLPPDHP LWRAPGALVT PHLGGTETER SSERIVALAI
     ENARRLNAKR PLKARIASLA AQ
//
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