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Database: UniProt
Entry: A0A136HSN2_9ALTE
LinkDB: A0A136HSN2_9ALTE
Original site: A0A136HSN2_9ALTE 
ID   A0A136HSN2_9ALTE        Unreviewed;       318 AA.
AC   A0A136HSN2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Glycerate dehydrogenase {ECO:0000313|EMBL:KXJ58369.1};
GN   ORFNames=AXW14_06380 {ECO:0000313|EMBL:KXJ58369.1};
OS   Alteromonas sp. Nap_26.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1795869 {ECO:0000313|EMBL:KXJ58369.1, ECO:0000313|Proteomes:UP000070342};
RN   [1] {ECO:0000313|Proteomes:UP000070342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Donaho J.A., Gutierrez T., Seitz K.W., Teske A.P.,
RA   Baker B.J.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {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:KXJ58369.1}.
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DR   EMBL; LSMP01000249; KXJ58369.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136HSN2; -.
DR   Proteomes; UP000070342; 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; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR43761; 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; 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}.
FT   DOMAIN          21..312
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          111..288
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   318 AA;  34393 MW;  8770C5094E1D4951 CRC64;
     MTLPHVVFLD AETLDLATLD TSVLQQLNAD VVIHDHTFAQ DIGERIANAD AVLVNKVVLD
     EEVLKSAPQL KYIGVTATGM NNIDLQFCAS NGIHVQNVEG YGTDSVAQHT LTLLLNLATR
     FVQYQQDVTK GKWSASPHFC LLEHPVIELA GKHAVIVGHG ALGKRVEALF KAMGMRVTIA
     ARPGNEGDVR PSLESLLPSA DVVSLHCPLT SDNEKMINAK TLSLMKPTSF LINTARGGLV
     DEPALLEALK THRIGGAGLD VLTVEPPPKD HILLNANLPN LLITPHNAWI GNTARQTLFN
     MAIEHLKSFL SSIEVAEK
//
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