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LOCUS WP_002904873 336 aa linear BCT 03-JUN-2024 [Enterobacterales]. ACCESSION WP_002904873 VERSION WP_002904873.1 KEYWORDS RefSeq. SOURCE Enterobacterales ORGANISM Enterobacterales Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria. REFERENCE 1 (residues 1 to 336) 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 336) 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 336) 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 336) 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..336 /organism="Enterobacterales" /db_xref="taxon:91347" gene 1..336 /gene="gap" Protein 1..336 /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=35841 Region 2..335 /region_name="GapA" /note="Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; COG0057" /db_xref="CDD:439827" ORIGIN 1 mvkvgingfg rigrnvlraa lnnpdiqiva indltdsktl ahllkydsll gkldaevtag 61 egglvvdgkp itvfsernpa sipwrqcevd ivieatglft drekaavhih sggakrviis 121 apgknddlti vmgvneslys pdkhyvisng scttnglapa aqvlhqhfgi khglmnttha 181 ytnsqalhdq pekdlrgara aalsivpyss gaakalgkvi peldgrltgy slrvpvpvvs 241 ivdltvtler dvtveevnna freaaaagpl kgilgysdep lvssdyqgdp rssiidglst 301 lviggnmvki lawydnewgf snrlvdlalm makres