ID A0A0E9MLL0_9SPHN Unreviewed; 311 AA.
AC A0A0E9MLL0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:GAO38015.1};
GN ORFNames=SCH01S_02_00120 {ECO:0000313|EMBL:GAO38015.1};
OS Sphingomonas changbaiensis NBRC 104936.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1219043 {ECO:0000313|EMBL:GAO38015.1, ECO:0000313|Proteomes:UP000033202};
RN [1] {ECO:0000313|EMBL:GAO38015.1, ECO:0000313|Proteomes:UP000033202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 104936 {ECO:0000313|EMBL:GAO38015.1,
RC ECO:0000313|Proteomes:UP000033202};
RA Katano-Makiyama Y., Hosoyama A., Hashimoto M., Noguchi M., Tsuchikane K.,
RA Ohji S., Yamazoe A., Ichikawa N., Kimura A., Fujita N.;
RT "Whole genome shotgun sequence of Sphingomonas changbaiensis NBRC 104936.";
RL Submitted (APR-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:GAO38015.1}.
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DR EMBL; BBWU01000002; GAO38015.1; -; Genomic_DNA.
DR RefSeq; WP_046346885.1; NZ_BBWU01000002.1.
DR AlphaFoldDB; A0A0E9MLL0; -.
DR STRING; 1219043.SCH01S_02_00120; -.
DR OrthoDB; 9787219at2; -.
DR Proteomes; UP000033202; 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; IPR029753; D-isomer_DH_CS.
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.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000033202}.
FT DOMAIN 54..305
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 104..273
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 311 AA; 33674 MW; 8AFE935A0903ED2F CRC64;
MILTLPALAR PLLEPHLPAD AEARWFASAE DACQMAPGAE VGWLDMYEAR DMVAALERAD
ALKWLNTIYA GIDWMPKDTL ARQGVTVTNG AGINAITIAE YVVMGMLTIA KGYREVVRAQ
DRHEWLRSPP GRLELAETSA LILGGGAIGS LVRTRLAAFD VAVTTVRRRP GPGELGTDAW
RARLGEFDWV ILAAPATAET QGMIGAAELD AMKPDAVLIN IARGSVVDQE ALVTALTENR
IGGAFLDVTT PEPLPSDHPL WTLPNAHVTM HLSGQSQSKM FQRGARLFLD NLARYRSGEP
LINAVDLDLG Y
//
