ID O58256_PYRHO Unreviewed; 333 AA.
AC O58256;
DT 01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT 01-AUG-1998, sequence version 1.
DT 27-MAR-2024, entry version 135.
DE SubName: Full=333aa long hypothetical dehydrogenase {ECO:0000313|EMBL:BAA29608.1};
GN OrderedLocusNames=PH0520 {ECO:0000313|EMBL:BAA29608.1};
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601 {ECO:0000313|EMBL:BAA29608.1, ECO:0000313|Proteomes:UP000000752};
RN [1] {ECO:0000313|EMBL:BAA29608.1, ECO:0000313|Proteomes:UP000000752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3
RC {ECO:0000313|Proteomes:UP000000752};
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Nakamura Y.,
RA Robb T.F., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2] {ECO:0007829|PDB:2D0I}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
RA Lokanath N.K., Terao Y., Kunishima N.;
RT "Crystal Structure PH0520 protein from Pyrococcus horikoshii OT3.";
RL Submitted (AUG-2005) to the PDB data bank.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; BA000001; BAA29608.1; -; Genomic_DNA.
DR PIR; C71165; C71165.
DR RefSeq; WP_010884621.1; NC_000961.1.
DR PDB; 2D0I; X-ray; 1.95 A; A/B/C/D=1-333.
DR PDBsum; 2D0I; -.
DR AlphaFoldDB; O58256; -.
DR SMR; O58256; -.
DR STRING; 70601.gene:9377454; -.
DR EnsemblBacteria; BAA29608; BAA29608; BAA29608.
DR GeneID; 1444408; -.
DR KEGG; pho:PH0520; -.
DR eggNOG; arCOG01755; Archaea.
DR OrthoDB; 34275at2157; -.
DR BRENDA; 1.1.1.95; 5244.
DR EvolutionaryTrace; O58256; -.
DR Proteomes; UP000000752; 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 Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
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; 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.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:2D0I};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 10..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; 38048 MW; 2290B1368AFC210E CRC64;
MRPKVGVLLK MKREALEELK KYADVEIILY PSGEELKGVI GRFDGIIVSP TTKITREVLE
NAERLKVISC HSAGYDNIDL EEATKRGIYV TKVSGLLSEA VAEFTVGLII NLMRKIHYAD
KFIRRGEWES HAKIWTGFKR IESLYGKKVG ILGMGAIGKA IARRLIPFGV KLYYWSRHRK
VNVEKELKAR YMDIDELLEK SDIVILALPL TRDTYHIINE ERVKKLEGKY LVNIGRGALV
DEKAVTEAIK QGKLKGYATD VFEKEPVREH ELFKYEWETV LTPHYAGLAL EAQEDVGFRA
VENLLKVLRG EVPEDLVNKE VLEVRPIENV KML
//
