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Database: UniProt
Entry: A0A024HMX3_PSEKB
LinkDB: A0A024HMX3_PSEKB
Original site: A0A024HMX3_PSEKB 
ID   A0A024HMX3_PSEKB        Unreviewed;       321 AA.
AC   A0A024HMX3;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Glycerate dehydrogenase {ECO:0000313|EMBL:CDF85984.1};
GN   Name=hprA {ECO:0000313|EMBL:CDF85984.1};
GN   ORFNames=PKB_4660 {ECO:0000313|EMBL:CDF85984.1};
OS   Pseudomonas knackmussii (strain DSM 6978 / LMG 23759 / B13).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1301098 {ECO:0000313|EMBL:CDF85984.1, ECO:0000313|Proteomes:UP000025241};
RN   [1] {ECO:0000313|EMBL:CDF85984.1, ECO:0000313|Proteomes:UP000025241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B13 {ECO:0000313|EMBL:CDF85984.1,
RC   ECO:0000313|Proteomes:UP000025241};
RA   Linke B.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDF85984.1, ECO:0000313|Proteomes:UP000025241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B13 {ECO:0000313|EMBL:CDF85984.1,
RC   ECO:0000313|Proteomes:UP000025241};
RA   Miyazaki R., Bertelli C., Falquet L., Robinson-Rechavi M., Gharib W.,
RA   Roy S., Van der Meer J.R.;
RT   "Genome sequence of the 3-chlorobenzoate degrading bacterium Pseudomonas
RT   knackmussii B13 shows multiple evidence for horizontal gene transfer.";
RL   Submitted (MAY-2014) 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; HG322950; CDF85984.1; -; Genomic_DNA.
DR   RefSeq; WP_043254824.1; NZ_HG322950.1.
DR   AlphaFoldDB; A0A024HMX3; -.
DR   STRING; 1301098.PKB_4660; -.
DR   KEGG; pkc:PKB_4660; -.
DR   PATRIC; fig|1301098.3.peg.4649; -.
DR   eggNOG; COG1052; Bacteria.
DR   HOGENOM; CLU_019796_1_3_6; -.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000025241; 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   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; 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:UP000025241}.
FT   DOMAIN          18..318
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          112..289
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   321 AA;  33965 MW;  95FAA51F1E596583 CRC64;
     MNSARAVFLD TASLDLGDLD LQPLRQAFGE LVTHAASTPD QVAARLQGAS VAISNKAPIN
     ADTLAQCPDL KLILVTATGT NNIDLAAARA RGIAVCNCQG YGTASVAQHA LLLLLALATR
     LPDYQSAIRA GRWQQATQFC LLDFPIVELE GKTLGLLGHG ELGSAVGRLA EAFGMRVLLG
     QLPGRPPRED RLALDELLPQ VDALSLHCPL TEQTRGMLGQ RELDLMKPGA FLINTARGGL
     IDEQALADTL RRGHLGGAAT DVLSVEPPKD GNPLLAGDIP RLIVTPHNAW GSREARQRIV
     GQVAENAAAF FAGQPLRQVN A
//
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