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Database: UniProt
Entry: A0A1M7H5Y8_9BACT
LinkDB: A0A1M7H5Y8_9BACT
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ID   A0A1M7H5Y8_9BACT        Unreviewed;       309 AA.
AC   A0A1M7H5Y8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=D-3-phosphoglycerate dehydrogenase {ECO:0000313|EMBL:SHM24011.1};
GN   ORFNames=SAMN05444266_10798 {ECO:0000313|EMBL:SHM24011.1};
OS   Chitinophaga jiangningensis.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=1419482 {ECO:0000313|EMBL:SHM24011.1, ECO:0000313|Proteomes:UP000184420};
RN   [1] {ECO:0000313|EMBL:SHM24011.1, ECO:0000313|Proteomes:UP000184420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27406 {ECO:0000313|EMBL:SHM24011.1,
RC   ECO:0000313|Proteomes:UP000184420};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FRBL01000007; SHM24011.1; -; Genomic_DNA.
DR   RefSeq; WP_073084033.1; NZ_FRBL01000007.1.
DR   AlphaFoldDB; A0A1M7H5Y8; -.
DR   STRING; 1419482.SAMN05444266_10798; -.
DR   OrthoDB; 9777288at2; -.
DR   Proteomes; UP000184420; 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   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.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184420}.
FT   DOMAIN          5..306
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          107..288
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   309 AA;  34382 MW;  D0DFC20D8CDA2DF1 CRC64;
     MSKKVLITAK VHPYLVDQLE TKGFEVDYQP SITYEEVYAA IPGCVGLIVT TRIRVDKQII
     DHGRELQWIG RLGSGMELID VPYAESKGIH CVSSPEGNRD PVGEQAVGML LSLMHNVLKS
     NLELRKGIWE RDGNRAYELG GKTVAIIGYG NTGSTFARKL KGFDVNIIAY DKYRKGFGTN
     EVKEVTLEEV YANADVVSLH LPLTEETRYI ANDSFFSAFA HPVWFMNTAR GKLVKNSDLI
     AALEDGRVRG ACLDVLENEK LTTYSAEDKE QLAYFLAASN VVLTPHIAGY SHEASIRMPR
     VVLEKLNIL
//
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