ID   GAP2_PSEAB              Reviewed;         461 AA.
AC   Q02PG5;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase-like protein {ECO:0000255|RuleBase:RU361160};
DE            EC=1.2.1.- {ECO:0000255|RuleBase:RU361160};
GN   Name=gap2; Synonyms=gapA; OrderedLocusNames=PA14_25250;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA   Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION AT THR-421.
RC   STRAIN=UCBPP-PA14;
RX   PubMed=25096199; DOI=10.1007/s00216-014-8045-8;
RA   Ouidir T., Jarnier F., Cosette P., Jouenne T., Hardouin J.;
RT   "Potential of liquid-isoelectric-focusing protein fractionation to improve
RT   phosphoprotein characterization of Pseudomonas aeruginosa PA14.";
RL   Anal. Bioanal. Chem. 406:6297-6309(2014).
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000255|RuleBase:RU000397}.
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DR   EMBL; CP000438; ABJ12239.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q02PG5; -.
DR   SMR; Q02PG5; -.
DR   iPTMnet; Q02PG5; -.
DR   PRIDE; Q02PG5; -.
DR   EnsemblBacteria; ABJ12239; ABJ12239; PA14_25250.
DR   KEGG; pau:PA14_25250; -.
DR   HOGENOM; CLU_030140_1_2_6; -.
DR   OMA; SDLWYDK; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR   InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR   InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR   InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR   InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR   InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PRINTS; PR00078; G3PDHDRGNASE.
DR   SMART; SM00846; Gp_dh_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   1: Evidence at protein level;
KW   NAD; Oxidoreductase; Phosphoprotein.
FT   CHAIN           1..461
FT                   /note="Glyceraldehyde-3-phosphate dehydrogenase-like
FT                   protein"
FT                   /id="PRO_0000431468"
FT   MOD_RES         421
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:25096199"
SQ   SEQUENCE   461 AA;  50082 MW;  F7D05FE689395705 CRC64;
     MIPLIGQLYR NNNVVTSIHG RGLINRSVIA IMKAHRFARH RMADDAELSV HETFPILKAM
     SELKLGAASV DLGKMVAKFK AEGNGRSIED FVKAELAEVA GKQNGDAREG TDVVLYGFGR
     IGRLLARILI EKTGGGDGLR LRAIVVRKGA ENDLVKRASL LRRDSVHGPF DGTITIDEEN
     NTLTANGNLI QVIYSNDPAS IDYTQYGIKN ALLVDNTGKW RDAEGLGQHL KCPGIDRVVL
     TAPGKGALKN IVHGINHTDI GADDKIISAA SCTTNAIVPV LKAVNDQYGI VNGHVETVHS
     YTNDQNLIDN FHKGSRRGRS APLNMVITKT GAATAAAKAL PVLKGKLTGN AIRVPTPNVS
     MAILNLNLEK ATTREEINEY LRQMAMHSDL QKQIDFVSSQ EVVSTDFVGS RHAGVVDAEA
     TICNDNRVVL YVWYDNEFGY SCQVVRVMED MAGVNPPAFP R