ID A0A0J6WYI8_9FIRM Unreviewed; 326 AA.
AC A0A0J6WYI8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=4-phosphoerythronate dehydrogenase {ECO:0000313|EMBL:KMO87323.1};
GN ORFNames=AB840_03280 {ECO:0000313|EMBL:KMO87323.1};
OS Megasphaera cerevisiae DSM 20462.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=1122219 {ECO:0000313|EMBL:KMO87323.1, ECO:0000313|Proteomes:UP000036503};
RN [1] {ECO:0000313|EMBL:KMO87323.1, ECO:0000313|Proteomes:UP000036503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20462 {ECO:0000313|EMBL:KMO87323.1,
RC ECO:0000313|Proteomes:UP000036503};
RA Kutumbaka K., Pasmowitz J., Mategko J., Reyes D., Friedrich A., Han S.,
RA Martens-Habbena W., Neal-McKinney J., Janagama H.K., Nadala C.,
RA Samadpour M.;
RT "Draft genome sequence of beer spoilage bacterium Megasphaera cerevisiae
RT type strain 20462.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KMO87323.1}.
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DR EMBL; LEKT01000007; KMO87323.1; -; Genomic_DNA.
DR RefSeq; WP_048513481.1; NZ_LEKT01000007.1.
DR AlphaFoldDB; A0A0J6WYI8; -.
DR STRING; 39029.BSR42_12195; -.
DR PATRIC; fig|1122219.3.peg.2751; -.
DR InParanoid; A0A0J6WYI8; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000036503; 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 GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR CDD; cd05299; CtBP_dh; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR043322; CtBP.
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; 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:UP000036503}.
FT DOMAIN 17..308
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 107..282
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 326 AA; 37036 MW; 3E2A86EF5C9DE617 CRC64;
MYHISVLTGR QDEDDFGERL RDMARVEYCS SMNEDIMADR MKDTDVIICK SEKLTSSLID
RLDDLKLIVI LSTRSENVDL EAASKKGILV VNNTSYCVDD IADHTCAMIL ALIRQLPEYQ
SDIRSNSRWE YGTISWPIHR VSDNLIGLVG FGHVGRAVAF RLQAFGCKIQ AYDPFVSEKV
MMEHRVRPVD FDKLLQTSDV VSLHMPLDET TKYIFQDEQF EQMKKGAIFV NCCRGGLVDE
ASLYHAVDDG HIRSAALDVL SMEHPSPMLL KMIARPEFLL TPNVSFHSVE ADQQVHNDAE
HYIRLFLSGQ YQDLPVVPVR EGTGKF
//
