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Database: UniProt
Entry: L0JXZ8_9EURY
LinkDB: L0JXZ8_9EURY
Original site: L0JXZ8_9EURY 
ID   L0JXZ8_9EURY            Unreviewed;       322 AA.
AC   L0JXZ8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Phosphoglycerate dehydrogenase-like oxidoreductase {ECO:0000313|EMBL:AGB37636.1};
GN   ORFNames=Natoc_1841 {ECO:0000313|EMBL:AGB37636.1};
OS   Natronococcus occultus SP4.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natronococcus.
OX   NCBI_TaxID=694430 {ECO:0000313|EMBL:AGB37636.1, ECO:0000313|Proteomes:UP000010878};
RN   [1] {ECO:0000313|EMBL:AGB37636.1, ECO:0000313|Proteomes:UP000010878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP4 {ECO:0000313|EMBL:AGB37636.1,
RC   ECO:0000313|Proteomes:UP000010878};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA   Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA   Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Eisen J., Klenk H.-P.,
RA   Klenk H.-P.;
RT   "FINISHED of Natronococcus occultus SP4, DSM 3396.";
RL   Submitted (NOV-2012) 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; CP003929; AGB37636.1; -; Genomic_DNA.
DR   AlphaFoldDB; L0JXZ8; -.
DR   STRING; 694430.Natoc_1841; -.
DR   KEGG; nou:Natoc_1841; -.
DR   eggNOG; arCOG01757; Archaea.
DR   HOGENOM; CLU_019796_1_0_2; -.
DR   Proteomes; UP000010878; 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; cd05300; 2-Hacid_dh_1; 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; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 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   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010878}.
FT   DOMAIN          29..316
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          111..285
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   322 AA;  35309 MW;  4CFEFFA662AB822D CRC64;
     MSKPDIVVLR EGTEGLSMES YAETLRERLP EATVELARTP KEERELVPQA RIVTGVTIEE
     ELLEDADRLE LFACTFAGTD HVPMDALAEH GVVVTNASGI HAPGIAEQSI ANMLVFARNL
     HEGWRRKSNG EWRHFQSREF TDSTVTVVGL GSIGQEIVQR LEGFSVETIG IRYTPEKGGP
     TDEILSFEED DVHEAFSRSE YVVLACPLND LTRNLVDEDA LATLPPEAVI VNAARGGIID
     TDALVSALQF NGIRGAALDV TDPEPLPNDH ELWGLENCLI TPHTGGHTPK HWDRLADIVA
     TNVDALEDGR GFENVVFRPD SS
//
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