ID A0A0F2L1C7_9CREN Unreviewed; 299 AA.
AC A0A0F2L1C7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:KJR71412.1};
GN ORFNames=TU36_08115 {ECO:0000313|EMBL:KJR71412.1};
OS Vulcanisaeta sp. AZ3.
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Vulcanisaeta.
OX NCBI_TaxID=1609231 {ECO:0000313|EMBL:KJR71412.1, ECO:0000313|Proteomes:UP000054362};
RN [1] {ECO:0000313|EMBL:KJR71412.1, ECO:0000313|Proteomes:UP000054362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Servin-Garciduenas L.E., Martinez-Romero E.;
RT "Metagenome Sequencing of an Archaeal-Dominated Microbial Community from a
RT Hot Spring at the Los Azufres Geothermal Field, Mexico.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {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:KJR71412.1}.
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DR EMBL; JZWU01000389; KJR71412.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2L1C7; -.
DR PATRIC; fig|1609231.3.peg.1331; -.
DR Proteomes; UP000054362; 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 CDD; cd12165; 2-Hacid_dh_6; 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; 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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 8..293
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 83..261
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 299 AA; 33140 MW; 8E103693E006DBBC CRC64;
MYELPKLSAE GLSNVLARAE VLLCWCSKEF DLARMITQMP SLRVIQTFSA GVDHLPFSVI
PRHVRVYSNA GAYSVPVAEH AWALILALSK GLHRHTLDAK EYLNDVFTAP RSVIGATLLV
LGTGGIGREI ARVGKLGFGT HNIGVNRSGR PVEYFDEVYP TDRLREVLPR ADIIALALPL
TKYTRKLIGE GELRLVKANA IIVNVGRGDV VDEEALYKVL RERTDIRFGT DVWWVHDGHE
EIPPRTPLTT LPNFLGTPHI AGGARRDVAE NAMVMAVENV ARYLRGETPI NEVSINDYN
//