(data stored in SCRATCH zone)

HOGENOM: HALED_1_PE1012

ID   HALED_1_PE1012                       STANDARD;      PRT;   379 AA.
AC   HALED_1_PE1012; E1V9R1;
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   RecName: Full=Erythronate-4-phosphate dehydrogenase; EC=1.1.1 290;
DE   (HALED_1.PE1012).
GN   Name=pdxB; OrderedLocusNames=HELO_2011;
OS   HALOMONAS ELONGATA DSM 2581.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=768066;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HALED_1.PE1012.
CC       Halomonas elongata DSM 2581, complete genome.
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:E1V9R1_HALED
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. PdxB subfamily.
CC   -!- GENE_FAMILY: HOG000234432 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; E1V9R1; -.
DR   EMBL; FN869568; CBV41895.1; -; Genomic_DNA.
DR   RefSeq; YP_003897080.1; NC_014532.1.
DR   ProteinModelPortal; E1V9R1; -.
DR   GeneID; 9745815; -.
DR   GenomeReviews; FN869568_GR; HELO_2011.
DR   KEGG; hel:HELO_2011; -.
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:HAMAP.
DR   HAMAP; MF_01825; PdxB; 1; -.
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   HOGENOMDNA; HALED_1.PE1012; -.
KW   Complete proteome; Cytoplasm; NAD; Oxidoreductase;
KW   Pyridoxine biosynthesis.
SQ   SEQUENCE   379 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRIVVDANVP EAQRCFGALG QVVSVPGREI DAATVRDADA LVVRSVTRVD EALVADSRLR
     FVGTCTIGTD HVDDRALSER GIGFASAPGC NAEAVVDYVL ASLATLAERG GFRLTERRVG
     IVGVGNVGGR LLARLKALGI DCLACDPPRA EEEGGTGFVD LDTLIDDCDV LCLHTPLVED
     GPHATRHLLD ARRIAELTPG TLVLNAGRGD CVDGRALRSR LSGQGDIPAV LDVWENEPAI
     DAALRDQSAL ATPHVAGYSL DGKLRGTHQV YRALARHVGL PARLGEADLM PAPPVPRLVL
     DGGLEMEEAL RLCMRAVYDP RRDHDALEHL ARTRGMAKGF DACRAGYPLR REFSTLEVVL
     EDAAADLAEP LSAAGFRVG
//

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