ID D4CDS9_9CLOT Unreviewed; 314 AA.
AC D4CDS9;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=4-phosphoerythronate dehydrogenase {ECO:0000313|EMBL:EFE12294.1};
DE EC=1.1.1.290 {ECO:0000313|EMBL:EFE12294.1};
GN Name=pdxB {ECO:0000313|EMBL:EFE12294.1};
GN ORFNames=CLOM621_07580 {ECO:0000313|EMBL:EFE12294.1};
OS Clostridium sp. M62/1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=411486 {ECO:0000313|EMBL:EFE12294.1, ECO:0000313|Proteomes:UP000004936};
RN [1] {ECO:0000313|EMBL:EFE12294.1, ECO:0000313|Proteomes:UP000004936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M62/1 {ECO:0000313|EMBL:EFE12294.1,
RC ECO:0000313|Proteomes:UP000004936};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-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:EFE12294.1}.
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DR EMBL; ACFX02000023; EFE12294.1; -; Genomic_DNA.
DR RefSeq; WP_008397660.1; NZ_GG730312.1.
DR AlphaFoldDB; D4CDS9; -.
DR HOGENOM; CLU_019796_1_3_9; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000004936; 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; cd05303; PGDH_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; IPR029753; D-isomer_DH_CS.
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.
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 4..311
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 107..290
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 314 AA; 34166 MW; D7C99790791ED1A0 CRC64;
MKCLIIDKVY AGIAEELGKF MEVKTAEHLP SSKEQVLAEI GDVDVLIMRV DPKIDKDILG
AAKNLKIIGV CSVGLNHIDM EYAKEKGIQI FNAPGLNANA VAELTISKML DISRGTMTAN
YDVKVKHEWD KYKFVGRELR GKTLGVMGFG RIGRRVGELG RAFGMTVVAY DPFLKPEDFE
KEHATGMGID ELLKVSDFVS IHVPLTPETK DLFNAKSIAE MKDDAVVLNM SRGGIVNEKD
MYEALKAGKI GGYATDVMEN ELAGSGLTGN DTFASPLFEC DNFIVSPHIG AQSVDASKDI
GIHIIAKVKE ALGL
//
