ID E2ZM69_9FIRM Unreviewed; 331 AA.
AC E2ZM69;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=4-phosphoerythronate dehydrogenase {ECO:0000313|EMBL:EFQ05721.1};
DE EC=1.1.1.290 {ECO:0000313|EMBL:EFQ05721.1};
GN Name=pdxB {ECO:0000313|EMBL:EFQ05721.1};
GN ORFNames=HMPREF9436_02780 {ECO:0000313|EMBL:EFQ05721.1};
OS Faecalibacterium cf. prausnitzii KLE1255.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Faecalibacterium.
OX NCBI_TaxID=748224 {ECO:0000313|EMBL:EFQ05721.1, ECO:0000313|Proteomes:UP000006028};
RN [1] {ECO:0000313|EMBL:EFQ05721.1, ECO:0000313|Proteomes:UP000006028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLE1255 {ECO:0000313|EMBL:EFQ05721.1,
RC ECO:0000313|Proteomes:UP000006028};
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., Hou S., Chen J., 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 (AUG-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:EFQ05721.1}.
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DR EMBL; AECU01000204; EFQ05721.1; -; Genomic_DNA.
DR RefSeq; WP_005945304.1; NZ_GL538344.1.
DR AlphaFoldDB; E2ZM69; -.
DR STRING; 748224.HMPREF9436_02780; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_1_9; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000006028; 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 CDD; cd12185; HGDH_LDH_like; 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; PTHR43026; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR PANTHER; PTHR43026:SF1; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 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 Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW ECO:0000313|EMBL:EFQ05721.1}.
FT DOMAIN 26..328
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..297
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 331 AA; 36411 MW; 5B6533BC861D31EE CRC64;
MATKVFFYTL RPYDELGIAQ RLAPQLDVEF GSTQEYPTLE NAELAKGYDA VSVTPCDMSA
PMVKRFHELG VKSICCRSIG YDHVDRETAR ELGMKVANVD YPPNGVANFA IMLMLMSLRK
AGHILKRGEA QDYSLQGKIG RDISTCTVGV IGTGRIGRTV LQHLSGFGCR LLAYDLYPND
EVKKIAEYVP LETLLAESDV ITLHTNATEE NHHLIDTKAI ESMKPGVTII NTARGKLIDS
DALIAGLESS KIGAAGLDVL ENENGLYYYN RMGDVIPNPE LAALRSMPNV ILTDHTAFYT
HEDVESMVRG VLESAVAFEK GQPTRHDVTD L
//
