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Database: UniProt
Entry: A0A0M0BRF3_9ARCH
LinkDB: A0A0M0BRF3_9ARCH
Original site: A0A0M0BRF3_9ARCH 
ID   A0A0M0BRF3_9ARCH        Unreviewed;       333 AA.
AC   A0A0M0BRF3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:KON30999.1};
GN   ORFNames=AC482_02320 {ECO:0000313|EMBL:KON30999.1};
OS   miscellaneous Crenarchaeota group-15 archaeon DG-45.
OC   Archaea; Candidatus Bathyarchaeota; MCG-15.
OX   NCBI_TaxID=1685127 {ECO:0000313|EMBL:KON30999.1, ECO:0000313|Proteomes:UP000037210};
RN   [1] {ECO:0000313|EMBL:KON30999.1, ECO:0000313|Proteomes:UP000037210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG-45 {ECO:0000313|EMBL:KON30999.1};
RA   Lazar C.S., Baker B.J., Seitz K.W., Hyde A.S., Dick G.J., Hinrichs K.-U.,
RA   Teske A.P.;
RT   "New insights into the roles of widespread benthic archaea in carbon and
RT   nitrogen cycling.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC       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:KON30999.1}.
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DR   EMBL; LFWZ01000016; KON30999.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M0BRF3; -.
DR   PATRIC; fig|1685127.3.peg.632; -.
DR   Proteomes; UP000037210; 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   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
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; IPR029753; D-isomer_DH_CS.
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; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR   PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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.
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          7..322
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          112..290
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   333 AA;  36558 MW;  CF8F46F5B6D7CDDC CRC64;
     MVRPKVYVTR QLFDEALDIL KMHAEIEVFD GIDNPVPRGT LLSKVRGVEG LLCLLTEEID
     EEVIEAGSRL KVISNCAVGF DNVDVEVATR RGIYVTNTPG ILTDTTADCA WALLMSIARR
     IAEADRHVRN RGWVHPWGPM MFLGSDVHGK TLGIIGIGRI GSAIAKRARG FDMNIIYHDV
     VRRKDLEEEL GIAYKGFEEI LSEADFVTIH VPLVEETHHL IGRRELTLMK GTAYLINTSR
     GPVVDEAALA EALKNGDIAG AALDVFEREP LDPDSPLLGL NNTVLTPHIA SASVETRTKM
     AVVAATNLAS VLRGEEPPNL VNPEVRKIRP LKP
//
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