ID A6VXE9_MARMS Unreviewed; 312 AA.
AC A6VXE9;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding {ECO:0000313|EMBL:ABR71128.1};
GN OrderedLocusNames=Mmwyl1_2206 {ECO:0000313|EMBL:ABR71128.1};
OS Marinomonas sp. (strain MWYL1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=400668 {ECO:0000313|EMBL:ABR71128.1};
RN [1] {ECO:0000313|EMBL:ABR71128.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWYL1 {ECO:0000313|EMBL:ABR71128.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA Richardson P.;
RT "Complete sequence of Marinomonas sp. MWYL1.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP000749; ABR71128.1; -; Genomic_DNA.
DR AlphaFoldDB; A6VXE9; -.
DR STRING; 400668.Mmwyl1_2206; -.
DR KEGG; mmw:Mmwyl1_2206; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_3_6; -.
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; cd12162; 2-Hacid_dh_4; 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; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 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; PS00670; D_2_HYDROXYACID_DH_2; 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}.
FT DOMAIN 22..310
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 106..286
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 312 AA; 34074 MW; 5BCF697060AB3A00 CRC64;
MKAVFLDRGS FPEYIKIQLP TQISEVVVYE NTALEQVAER IKNATIVLTN KVVVNAAAIN
SALDLKLIQV MATGTNNVDL KACKDKNIAV QNVADYSTIS VPEHTFAMLL ALRRNLVSYL
DAVNSGRWAT SEYFCFLDYP IKDLSGSTMA IVGGGTLGKK VAAIALAFGM KVIFADRKGA
TNARPGYINF EEALKLADVI SINCPLTPET NNLISDAEFS LMKKSCLLLN ISRGGIVDEH
ALLRAFENNT ITGAAFDVST QEPMPLDHPL QALTKQPNFL LTPHIAWASD EAMQTLVDMA
MDKITTFIDK PE
//
