ID A0A3N2MEZ2_9BACT Unreviewed; 317 AA.
AC A0A3N2MEZ2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=D-2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:ROT08722.1};
GN ORFNames=EEL33_03575 {ECO:0000313|EMBL:ROT08722.1};
OS Muribaculaceae bacterium Isolate-037 (Harlan).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae.
OX NCBI_TaxID=2486461 {ECO:0000313|EMBL:ROT08722.1, ECO:0000313|Proteomes:UP000275399};
RN [1] {ECO:0000313|EMBL:ROT08722.1, ECO:0000313|Proteomes:UP000275399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate-037 (Harlan) {ECO:0000313|Proteomes:UP000275399};
RA Clavel T., Strowig T.;
RT "Sequence and cultivation study of Muribaculaceae reveals novel species,
RT host preference, and functional potential of this yet undescribed family.";
RL Submitted (NOV-2018) 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:ROT08722.1}.
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DR EMBL; RIAZ01000003; ROT08722.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2MEZ2; -.
DR Proteomes; UP000275399; 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; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000275399}.
FT DOMAIN 19..316
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 107..286
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 317 AA; 34884 MW; D17F47DBC4A37F3E CRC64;
MKIVVLDGYG LNPGDLSWEW LDKYGEVTVY DRTSPDRIAD RAKDADVLFT NKVVLDKEML
QSLPHLKYVG VLATGYNVVD IDAARQAGIT VTNIPAYSTD SVAQMVFAHL LNVTNRVEHY
AEENRNGRWS RNPDFCYWDY PLTELAGKNF GIVGLGHIGM TVARIARAFG MNVIAYTSKP
QDELPEGVAK VDMDRLFADS DVLSLHCPLT PSTKHLVNAD RLRGMKPSAI VINTGRGPLV
DEDAMADALK EGRVAAFCAD VLSTEPPSPD NPLLTAPNAY ITPHIAWASV EARRRLMHIC
EDNLSAFLSG TPRNVVS
//
