(data stored in SCRATCH zone)

HOGENOM: TERTT_1_PE1011

ID   TERTT_1_PE1011                       STANDARD;      PRT;   370 AA.
AC   TERTT_1_PE1011; C5BR49;
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   (TERTT_1.PE1011).
GN   Name=pdxB; OrderedLocusNames=TERTU_1127;
OS   TEREDINIBACTER TURNERAE T7901.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadales genera incertae sedis; Teredinibacter.
OX   NCBI_TaxID=377629;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS TERTT_1.PE1011.
CC       Teredinibacter turnerae T7901, complete genome.
CC       1..16866 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:PDXB_TERTT
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 (Potential).
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; C5BR49; -.
DR   EMBL; CP001614; ACR11693.1; -; Genomic_DNA.
DR   RefSeq; YP_003072712.1; NC_012997.1.
DR   ProteinModelPortal; C5BR49; -.
DR   STRING; C5BR49; -.
DR   GeneID; 8210823; -.
DR   GenomeReviews; CP001614_GR; TERTU_1127.
DR   KEGG; ttu:TERTU_1127; -.
DR   OMA; SAPGCNA; -.
DR   ProtClustDB; CLSK2528525; -.
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   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   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; FALSE_NEG.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; FALSE_NEG.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
DR   HOGENOMDNA; TERTT_1.PE1011; -.
KW   Complete proteome; Cytoplasm; NAD; Oxidoreductase;
KW   Pyridoxine biosynthesis.
SQ   SEQUENCE   370 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKIVVDENIP LADALFGDLG EIIRKPGREI SSADVAEADA LLVRSVTRVN ADLLTGSKVK
     FVGTCTIGTD HLDKEFLAEA GIRFASAPGC NAQGVVQYDL AALAHLGYLA RDIRVGIIGC
     GNVGGSLHRA LTGMGVTCVC YDPFLTQDQN ADLADWDALF TCDVICVHTP LTRSGPYPTH
     HMLSTPFFRA MRDGALLLNA GRGEVIDNRA LKAYLQGDNS NHLSVVLDVW EGEPAIDAEL
     APLVKIATPH IAGYSFEGKT NGSLMIYEAL AEFLGVNATE RSARVAAVKA QAYGAAEPLD
     ADDLVTAILA THPITRDDKA LRDQLDQLPA GFDALRKGYP VRREFSHYQL TSAQIPANVT
     ALGFSLDSAK
//

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