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Database: UniProt
Entry: A0A0A2GBF1_9PORP
LinkDB: A0A0A2GBF1_9PORP
Original site: A0A0A2GBF1_9PORP 
ID   A0A0A2GBF1_9PORP        Unreviewed;       318 AA.
AC   A0A0A2GBF1;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Glycerate dehydrogenase {ECO:0000313|EMBL:KGN73856.1};
GN   ORFNames=HQ47_06310 {ECO:0000313|EMBL:KGN73856.1};
OS   Porphyromonas macacae.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=28115 {ECO:0000313|EMBL:KGN73856.1, ECO:0000313|Proteomes:UP000030103};
RN   [1] {ECO:0000313|EMBL:KGN73856.1, ECO:0000313|Proteomes:UP000030103}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COT-192 OH2859 {ECO:0000313|Proteomes:UP000030103};
RA   Wallis C., Deusch O., O'Flynn C., Davis I., Horsfall A., Kirkwood N.,
RA   Harris S., Eisen J.A., Coil D.A., Darling A.E., Jospin G., Alexiev A.;
RT   "Draft Genome Sequence of Porphyromonas macacae COT-192_OH2859.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC       ECO:0000256|RuleBase:RU003719}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGN73856.1}.
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DR   EMBL; JRFA01000017; KGN73856.1; -; Genomic_DNA.
DR   RefSeq; WP_036851866.1; NZ_JRFB01000011.1.
DR   AlphaFoldDB; A0A0A2GBF1; -.
DR   STRING; 28115.HQ47_06310; -.
DR   eggNOG; COG1052; Bacteria.
DR   OrthoDB; 9777288at2; -.
DR   Proteomes; UP000030103; 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; 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; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 1.
DR   PANTHER; PTHR43761:SF1; 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; PS00065; D_2_HYDROXYACID_DH_1; 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   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030103}.
FT   DOMAIN          21..315
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          108..286
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   318 AA;  34841 MW;  79E8D5E86D31B8DD CRC64;
     MKIVILDGFA AQPGDLDWSE IQSLGECVIY DTTSAEQLHE RISDAEIVLT NKTPIKAEDM
     DRTPELKYIG IMTTGTNLID IQAARERGIV VTNLPAYSSE SVAQMVFSHL LNIVMSVNKY
     NEFIHKGLWQ KEQPMDMRRA DYIELYGQSI GIVGFGNIGS AVARIAHGFG MSVLVYTSKP
     QKQLPAYCKS VGLKELFSSA DVVSLHCPLT AETKGLVDTD KLKSMKPTAI LINTARGALV
     DEEALKTALI NGWIAAAGLD VLSEEPPGRE HPLFNLRNCY LTPHVGWATK NACRRIADHT
     AKNLTAFLSG NPINTVLP
//
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