ID A0A0W1G530_9SPHN Unreviewed; 314 AA.
AC A0A0W1G530;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:KTE49925.1};
GN ORFNames=ATE69_19205 {ECO:0000313|EMBL:KTE49925.1};
OS Sphingopyxis sp. H071.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1759078 {ECO:0000313|EMBL:KTE49925.1, ECO:0000313|Proteomes:UP000054127};
RN [1] {ECO:0000313|EMBL:KTE49925.1, ECO:0000313|Proteomes:UP000054127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H071 {ECO:0000313|EMBL:KTE49925.1,
RC ECO:0000313|Proteomes:UP000054127};
RA Zhang Y., Guo Z.;
RL Submitted (NOV-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:KTE49925.1}.
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DR EMBL; LNSF01000015; KTE49925.1; -; Genomic_DNA.
DR RefSeq; WP_058457353.1; NZ_LNSF01000015.1.
DR AlphaFoldDB; A0A0W1G530; -.
DR OrthoDB; 9787219at2; -.
DR Proteomes; UP000054127; 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; cd05300; 2-Hacid_dh_1; 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; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 55..299
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 107..276
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 314 AA; 34410 MW; 621893AF3048B4CD CRC64;
MTKTVTVLSG LIRPLVENRL PDWVQPRFFA SKEEAMGLAP EAEIGWFDMY DKKDMAAVIT
AATNLKWLNS IYAGVDGMPL DLLRERGTVV TNGAGINAIT IAEYVVMGML TVAKGYREVV
RAQDRREWLM DSPGKVELFG SKALLLGYGA IGKLVEERLK AFAVDVTVVR RSPGPNTLGP
DQWRARLGDF DWVILAVPAT PETDGMIGSA ELAAMKPSAT LINIARGSVI DQDALVAALD
TQQIAAAFLD VTTPEPLPDS DPLWSLDNAH ITMHLSGRAQ DKMFLRSAQR FLENLDRWNL
GEAVEPRVDL ALGY
//
