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Database: UniProt
Entry: E3C576_9LACO
LinkDB: E3C576_9LACO
Original site: E3C576_9LACO 
ID   E3C576_9LACO            Unreviewed;       328 AA.
AC   E3C576;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=4-phosphoerythronate dehydrogenase {ECO:0000313|EMBL:EFQ54150.1};
DE            EC=1.1.1.290 {ECO:0000313|EMBL:EFQ54150.1};
GN   Name=pdxB {ECO:0000313|EMBL:EFQ54150.1};
GN   ORFNames=HMPREF9265_0363 {ECO:0000313|EMBL:EFQ54150.1};
OS   Limosilactobacillus oris PB013-T2-3.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=908339 {ECO:0000313|EMBL:EFQ54150.1, ECO:0000313|Proteomes:UP000003070};
RN   [1] {ECO:0000313|EMBL:EFQ54150.1, ECO:0000313|Proteomes:UP000003070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB013-T2-3 {ECO:0000313|EMBL:EFQ54150.1,
RC   ECO:0000313|Proteomes:UP000003070};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (OCT-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:EFQ54150.1}.
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DR   EMBL; AEKL01000004; EFQ54150.1; -; Genomic_DNA.
DR   RefSeq; WP_004564465.1; NZ_AEKL01000004.1.
DR   AlphaFoldDB; E3C576; -.
DR   eggNOG; COG1052; Bacteria.
DR   OrthoDB; 9805416at2; -.
DR   Proteomes; UP000003070; 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; cd12186; LDH; 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; 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; 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}.
FT   DOMAIN          7..326
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          111..295
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
SQ   SEQUENCE   328 AA;  36683 MW;  43B39EE84BA60C9B CRC64;
     MKILMYAVLE PEKKYIREWS AKTGVEVKCV AERLDAKTVE WAQGFDGIDF QQTQPLEPVV
     YQKLHEYGIK QLTARMVGYD MIDFDLAKKY ELTVTNVPTY SPRAIAEMGL TQALRLVRKL
     GYYDQRMDNL DFRWAGLEST EIYNLTVGII GAGHIGGATA QLYSALGAKV IAVDPIHQVE
     LSPYLEYTDL DTLLKTADIV TVHTPLDEST ANLFNSETFK KMKDTAYLIN MARGGIVNAD
     DLIAALQNKE IAGAALDTLA DEGQFFEKQA TPEEIPEDYK TLRAMPNVLI SPHSAFYTDT
     AMKNMVAMGL DDVVAIVNGK RPQFEVYK
//
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