(data stored in ACNUC7421 zone)

HOGENOM: LEGP2_1_PE1003

ID   LEGP2_1_PE1003                       STANDARD;      PRT;   350 AA.
AC   LEGP2_1_PE1003; D5TB64;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   SubName: Full=Erythronate-4-phosphate dehydrogenase; EC=1.1.1 290;
DE   (LEGP2_1.PE1003).
GN   OrderedLocusNames=lpa_01387;
OS   LEGIONELLA PNEUMOPHILA 2300/99 ALCOY.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=423212;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS LEGP2_1.PE1003.
CC       Legionella pneumophila 2300/99 Alcoy chromosome, complete genome.
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:D5TB64_LEGP2
CC   -!- FUNCTION: Catalyzes the oxidation of erythronate-4-phosphate to 3-
CC       hydroxy-2-oxo-4-phosphonooxybutanoate (By similarity).
CC   -!- CATALYTIC ACTIVITY: 4-phospho-D-erythronate + NAD(+) = (3R)-3-
CC       hydroxy-2-oxo-4-phosphonooxybutanoate + NADH.
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate
CC       biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-
CC       phosphate: step 2/5.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family.
CC   -!- GENE_FAMILY: HOG000278825 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D5TB64; -.
DR   EMBL; CP001828; ADG24248.1; -; Genomic_DNA.
DR   RefSeq; YP_003618200.1; NC_014125.1.
DR   ProteinModelPortal; D5TB64; -.
DR   GeneID; 9128777; -.
DR   GenomeReviews; CP001828_GR; lpa_01387.
DR   KEGG; lpa:lpa_01387; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033711; F:4-phosphoerythronate dehydrogenase activity; IEA:EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR006140; D-isomer_2_OHA_DH_NAD-bd.
DR   InterPro; IPR020921; Erythronate-4-P_DHase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 2.
DR   PANTHER; PTHR10996:SF4; Erythronate-4-P_DHase; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
DR   HOGENOMDNA; LEGP2_1.PE1003; -.
KW   erythronate-4-phosphate dehydrogenase;
KW   Complete proteome; Cytoplasm; NAD; Oxidoreductase;
KW   Pyridoxine biosynthesis.
SQ   SEQUENCE   350 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNILADALLP GLDSAFPPPF TVTLYHKADE IPDLLHHKDV LLCRSTLKIN GDLLKNHQIK
     VVATATSGTD HIDFPFLESQ KISIIDAKGC NATSVADYVV ACLAYLDKQQ LIQGKTAGII
     GLGQVGTKVY ERLNAAEFQL CLYDPPKAAR DTSFQSCSLE DLFECDLLCV HAELHSDAPY
     PSLNLINRDF LKELKPGCII INASRGGIVN EEALLHLGSA ILYCTDVYNN EPHIDNRIVS
     KATLCTPHIA GHSLEAKFAA VAIVSRKLHQ MLGLPYPQFA TPEKPYRLNE NSDWRELALS
     IYNPIHETLE LKHAGNLSSA FLTLRKNHHH RHDFTTYFDS DSIKKCPLLG
//

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