MULTISPECIES: type I glyceraldehyde-3-phosphate dehydrogenase

LOCUS       WP_003114837             334 aa            linear   BCT 03-JUN-2024
            [Pseudomonas].
ACCESSION   WP_003114837
VERSION     WP_003114837.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 334)
  AUTHORS   Mittenhuber,G.
  TITLE     Phylogenetic analyses and comparative genomics of vitamin B6
            (pyridoxine) and pyridoxal phosphate biosynthesis pathways
  JOURNAL   J Mol Microbiol Biotechnol 3 (1), 1-20 (2001)
   PUBMED   11200221
REFERENCE   2  (residues 1 to 334)
  AUTHORS   Fillinger,S., Boschi-Muller,S., Azza,S., Dervyn,E., Branlant,G. and
            Aymerich,S.
  TITLE     Two glyceraldehyde-3-phosphate dehydrogenases with opposite
            physiological roles in a nonphotosynthetic bacterium
  JOURNAL   J Biol Chem 275 (19), 14031-14037 (2000)
   PUBMED   10799476
REFERENCE   3  (residues 1 to 334)
  AUTHORS   Boschi-Muller,S., Azza,S., Pollastro,D., Corbier,C. and Branlant,G.
  TITLE     Comparative enzymatic properties of GapB-encoded
            erythrose-4-phosphate dehydrogenase of Escherichia coli and
            phosphorylating glyceraldehyde-3-phosphate dehydrogenase
  JOURNAL   J Biol Chem 272 (24), 15106-15112 (1997)
   PUBMED   9182530
REFERENCE   4  (residues 1 to 334)
  AUTHORS   Zhao,G., Pease,A.J., Bharani,N. and Winkler,M.E.
  TITLE     Biochemical characterization of gapB-encoded erythrose 4-phosphate
            dehydrogenase of Escherichia coli K-12 and its possible role in
            pyridoxal 5'-phosphate biosynthesis
  JOURNAL   J Bacteriol 177 (10), 2804-2812 (1995)
   PUBMED   7751290
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR01534.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..334
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     gene            1..334
                     /gene="gap"
     Protein         1..334
                     /product="type I glyceraldehyde-3-phosphate dehydrogenase"
                     /GO_function="GO:0016620 - oxidoreductase activity, acting
                     on the aldehyde or oxo group of donors, NAD or NADP as
                     acceptor [Evidence IEA]"
                     /GO_function="GO:0050661 - NADP binding [Evidence IEA]"
                     /GO_function="GO:0051287 - NAD binding [Evidence IEA]"
                     /GO_process="GO:0006006 - glucose metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=36039
     Region          1..324
                     /region_name="GapA"
                     /note="Glyceraldehyde-3-phosphate
                     dehydrogenase/erythrose-4-phosphate dehydrogenase
                     [Carbohydrate transport and metabolism]; COG0057"
                     /db_xref="CDD:439827"
ORIGIN      
        1 mtirlaingf grigrnvlra lytghyreql qvvaindlgd aavnahlfqy dsvhghfpge
       61 vehdaeslrv mgdriavsai rnpaelpwks lgvdivlect glftsrdkaa ahlqagagkv
      121 lisapgkdve atvvygvnhe vlrashrivs nascttncla pvaqvlhrel giehglmtti
      181 haytndqnls dvyhpdlyra rsatqsmipt ktgaaeavgl vlpelagklt glavrvpvin
      241 vslvdltvqv ardtsvdevn rllreasegs pvlgyntqpl vsvdfnhdpr ssifdanhtk
      301 vsgrlvkama wydnewgfsn rmldsalala aard