ID A0A0D8CRU5_9GAMM Unreviewed; 330 AA.
AC A0A0D8CRU5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:KJE39258.1};
GN ORFNames=SG35_21450 {ECO:0000313|EMBL:KJE39258.1};
OS Thalassomonas actiniarum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Thalassomonas.
OX NCBI_TaxID=485447 {ECO:0000313|EMBL:KJE39258.1};
RN [1] {ECO:0000313|EMBL:KJE39258.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A5K-106 {ECO:0000313|EMBL:KJE39258.1};
RA Olonade I., van Zyl L.J., Tuffin M.I.;
RT "Genome sequence of Japanese sea anemone isolate Thalassomonas
RT actiniarum.";
RL Submitted (JAN-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:KJE39258.1}.
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DR EMBL; JYNI01000051; KJE39258.1; -; Genomic_DNA.
DR RefSeq; WP_044834525.1; NZ_CP059735.1.
DR AlphaFoldDB; A0A0D8CRU5; -.
DR STRING; 485447.SG35_21450; -.
DR PATRIC; fig|485447.4.peg.4715; -.
DR OrthoDB; 9805416at2; -.
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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 3..321
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 109..296
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 330 AA; 36032 MW; 601D224D5CEF274C CRC64;
MKIAVFSSKA YDQQYFGNDC DSGFTMTFFE TRLNAHTAVT AQGFEVVCCF VNDDLSEATI
KVLKEVGVKL IALRCAGFNN LDLQAAQQAG ITVCRVPAYS PHSVAEHALA LLLSLNRNIH
RAFNRVREND YSLNGLLGFD LYKKKVAVIG TGKIGSTFAR IMTGLGCEVI ACDPVQDSEL
IKLGVSYVTL EHLWHQADII SLHCPLQQDT FHLVNEQAIS QMKPGVALIN TGRGALIDTK
AVISGLKSGH IGYLGLDVYE EEADLFFEDK SNTLLQDDVF ARLLTFPNVL ITGHQGFFTK
EALTAIAQTT MANIRAFAAG DFAAMQLVGK
//
