ID A0A368JGP2_9BACT Unreviewed; 329 AA.
AC A0A368JGP2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:RCR66827.1};
GN ORFNames=DUE52_25075 {ECO:0000313|EMBL:RCR66827.1};
OS Larkinella punicea.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Larkinella.
OX NCBI_TaxID=2315727 {ECO:0000313|EMBL:RCR66827.1, ECO:0000313|Proteomes:UP000253383};
RN [1] {ECO:0000313|EMBL:RCR66827.1, ECO:0000313|Proteomes:UP000253383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=zzj9 {ECO:0000313|Proteomes:UP000253383};
RA Zhou Z., Wang G.;
RT "Genome analysis of Larkinella rosea.";
RL Submitted (JUL-2018) 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:RCR66827.1}.
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DR EMBL; QOWE01000024; RCR66827.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368JGP2; -.
DR OrthoDB; 1522997at2; -.
DR Proteomes; UP000253383; 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; cd12183; LDH_like_2; 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; PTHR43026; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR PANTHER; PTHR43026:SF1; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-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.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 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 18..316
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 108..295
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 329 AA; 36063 MW; 06B0C941EB8E99C5 CRC64;
MKIAFFSTAA YERDWFIRYQ AHHTITFIDE ILTEQTSHLA SGYEAVCAFV EDDLSKPVLE
SLRSLGIQLV AMRCVGLDNV DLEAADELGI TVLHVPGYSP YSVAEHAVAL LMGLVRHIPQ
AHERVQQGNF SINGLTGQDL HGKTVGVIGT GHIGQAFCQI MLGFGCRVLA FDIKPNQPLL
NAGVRYVALP TLLAESDVIS LHCPLNAQTR QLLDAPALSQ LKPTAIVVNS SRGGLVDTAA
VLDALDANAL AGYAADVYAN EKKWFHRDFS GQPITDDLLN RLRTHPRVLL TAHQGFLTEE
ALQQIAHRLI LQISFFQNSR QEGISKMSM
//
