ID E2SMG3_9FIRM Unreviewed; 311 AA.
AC E2SMG3;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=4-phosphoerythronate dehydrogenase {ECO:0000313|EMBL:EFP61243.1};
DE EC=1.1.1.290 {ECO:0000313|EMBL:EFP61243.1};
GN Name=pdxB {ECO:0000313|EMBL:EFP61243.1};
GN ORFNames=HMPREF0983_02296 {ECO:0000313|EMBL:EFP61243.1};
OS Erysipelotrichaceae bacterium 3_1_53.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae.
OX NCBI_TaxID=658659 {ECO:0000313|EMBL:EFP61243.1, ECO:0000313|Proteomes:UP000006223};
RN [1] {ECO:0000313|EMBL:EFP61243.1, ECO:0000313|Proteomes:UP000006223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3_1_53 {ECO:0000313|EMBL:EFP61243.1,
RC ECO:0000313|Proteomes:UP000006223};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Pearson M., Zeng Q.,
RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T.,
RA Walk T., White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C.,
RA Daigneault M., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Erysipelotrichaceae bacterium strain 3_1_53.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC 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:EFP61243.1}.
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DR EMBL; ACTJ01000053; EFP61243.1; -; Genomic_DNA.
DR AlphaFoldDB; E2SMG3; -.
DR STRING; 658659.HMPREF0983_02296; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_3_9; -.
DR Proteomes; UP000006223; Unassembled WGS sequence.
DR GO; GO:0033711; F:4-phosphoerythronate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd12172; PGDH_like_2; 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; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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; PS00065; D_2_HYDROXYACID_DH_1; 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 31..307
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..283
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 311 AA; 34572 MW; 425E5157D89CDEC9 CRC64;
MKVLITSNSF GKFDEAPRKR MLDMGWELID NRYHHIMNEE EMMGEVTGVD AIILGSDTVS
KRVLEKADCL KIISRYGVGI DNIDVTEAEK KGIAVTVTKN CNTEAVADYT IALMLSTLRH
VCNVHTSLQK GVWKKETGLD LCHKTVGVFG LGAIGRQVVK RLKGFECKII GYDTFLDEAY
CKREGIEIAS PQEIFQQADI ITLHIPGNAD GTHFITHKEL ALMKPETVII NTARASLIDE
KDMIEALKQR RIYGYGTDVF AEEPHMNSGF IGLDNVVCSP HTAAVSVEAV NKMSHAAVDH
LIDYFKANKE V
//
