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LOCUS WP_008042848 331 aa linear BCT 03-JUN-2024 blandensis]. ACCESSION WP_008042848 VERSION WP_008042848.1 KEYWORDS RefSeq. SOURCE Reinekea blandensis ORGANISM Reinekea blandensis Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Oceanospirillales; Saccharospirillaceae; Reinekea. REFERENCE 1 (residues 1 to 331) 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 331) 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 331) 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 331) 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..331 /organism="Reinekea blandensis" /db_xref="taxon:374838" gene 1..331 /gene="gap" Protein 1..331 /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=35307 Region 1..331 /region_name="GapA" /note="Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; COG0057" /db_xref="CDD:439827" ORIGIN 1 mtikvgingf grigrfvfra sverddievv gindlidvdy maymlkydst hgrfngtvev 61 dngnlivngk kvrvtaerdp anlawgdldv dvvaeatgif ltdetarkhi eagakkvvlt 121 gpskdatpmf vmgvnhetya gqdivsnasc ttnclapvak vlndkwgikd glmttvhatt 181 atqktvdgps akdwrggrga sqniipsstg aakavgkvip elngkltgma frvptanvsv 241 vdltvnlekp atydeikaem krasgaelkg vlgytedavv sqdfigetqt svfdaeagls 301 ltdtfvkvvs wydneigysn kvldlaahis k