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Database: UniProt
Entry: A0A075LVF9_9EURY
LinkDB: A0A075LVF9_9EURY
Original site: A0A075LVF9_9EURY 
ID   A0A075LVF9_9EURY        Unreviewed;       333 AA.
AC   A0A075LVF9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:AIF69997.1};
GN   ORFNames=PAP_08045 {ECO:0000313|EMBL:AIF69997.1};
OS   Palaeococcus pacificus DY20341.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Palaeococcus.
OX   NCBI_TaxID=1343739 {ECO:0000313|EMBL:AIF69997.1, ECO:0000313|Proteomes:UP000027981};
RN   [1] {ECO:0000313|Proteomes:UP000027981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY20341 {ECO:0000313|Proteomes:UP000027981};
RA   Zeng X., Shao Z.;
RT   "Complete Genome Sequence of Hyperthermophilic Palaeococcus pacificus
RT   DY20341T, Isolated from a Deep-Sea Hydrothermal Sediments.";
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AIF69997.1, ECO:0000313|Proteomes:UP000027981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY20341 {ECO:0000313|EMBL:AIF69997.1,
RC   ECO:0000313|Proteomes:UP000027981};
RX   PubMed=26383653;
RA   Zeng X., Jebbar M., Shao Z.;
RT   "Complete Genome Sequence of Hyperthermophilic Piezophilic Archaeon
RT   Palaeococcus pacificus DY20341T, Isolated from Deep-Sea Hydrothermal
RT   Sediments.";
RL   Genome Announc. 3:e01080-e01015(2015).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR   EMBL; CP006019; AIF69997.1; -; Genomic_DNA.
DR   RefSeq; WP_048165494.1; NZ_CP006019.1.
DR   AlphaFoldDB; A0A075LVF9; -.
DR   STRING; 1343739.PAP_08045; -.
DR   GeneID; 24842710; -.
DR   KEGG; ppac:PAP_08045; -.
DR   eggNOG; arCOG01755; Archaea.
DR   HOGENOM; CLU_019796_1_3_2; -.
DR   OrthoDB; 34275at2157; -.
DR   Proteomes; UP000027981; 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; cd05301; GDH; 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; 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.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003719}.
FT   DOMAIN          6..318
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          106..286
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   333 AA;  37675 MW;  B25FFBCC71D99B45 CRC64;
     MRPKVLVLFK MKSKPLEELK KYCDVDLLVY PSKEELLKVI AKYDALIVSP LNRIDGEVIE
     KAERLKVIST HSAGYDHIDV EAATKKGIYV TKVSGVLSEA VAEFAIGLMI ALLRKIAYTD
     KFIRLGKWES HRTVWSKFKD IETVYGKKVG ILGMGPIGKA IAKRAKALGT EIYYWSRHRK
     EDIEEEVGAK YLPLEEVLTE SDIVVLALPA AKETYHIINE ERLKLLEGKY LINIGRGTLI
     DEKALIKALK EGKLKGFATD VYEKEPLQES ELFEMGWETV LTPHHAGLSE EAMEDMGFQA
     VKNLLAIFRG EIPKDLVNGE VFKIKRIDEV KML
//
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