ID   GAPN_STREI              Reviewed;         476 AA.
AC   Q3C1A6;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=NADP-dependent glyceraldehyde-3-phosphate dehydrogenase;
DE            EC=1.2.1.9;
DE   AltName: Full=Glyceraldehyde-3-phosphate dehydrogenase [NADP(+)];
DE            Short=GAPN;
DE   AltName: Full=Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase;
DE   AltName: Full=Triosephosphate dehydrogenase;
GN   Name=gapN;
OS   Streptococcus equinus (Streptococcus bovis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1335;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND TRANSCRIPTIONAL REGULATION.
RC   STRAIN=ATCC 700410 / JB1;
RX   PubMed=16553827; DOI=10.1111/j.1574-6968.2006.00111.x;
RA   Asanuma N., Hino T.;
RT   "Presence of NADP(+)-specific glyceraldehyde-3-phosphate dehydrogenase and
RT   CcpA-dependent transcription of its gene in the ruminal bacterium
RT   Streptococcus bovis.";
RL   FEMS Microbiol. Lett. 257:17-23(2006).
CC   -!- FUNCTION: Catalyzes the irreversible NADP-dependent oxidation of
CC       glyceraldehyde-3-phosphate to 3-phosphoglycerate. Is not able to use
CC       NAD instead of NADP. May play an important role in NADPH production in
CC       S.equinus. {ECO:0000269|PubMed:16553827}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + H2O + NADP(+) = (2R)-3-
CC         phosphoglycerate + 2 H(+) + NADPH; Xref=Rhea:RHEA:14669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58272, ChEBI:CHEBI:58349, ChEBI:CHEBI:59776; EC=1.2.1.9;
CC         Evidence={ECO:0000269|PubMed:16553827};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.5. {ECO:0000269|PubMed:16553827};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius.
CC         {ECO:0000269|PubMed:16553827};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- INDUCTION: Up-regulated by the catabolite control protein A (CcpA).
CC       {ECO:0000269|PubMed:16553827}.
CC   -!- MISCELLANEOUS: S.bovis does not display glucose-6-phosphate
CC       dehydrogenase (G6PDH) and 6-phosphogluconate dehydrogenase (6PGDH)
CC       activities, indicating that it does not have the hexose monophosphate
CC       pathway.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AB239335; BAE46989.1; -; Genomic_DNA.
DR   RefSeq; WP_039697176.1; NZ_FOEX01000001.1.
DR   AlphaFoldDB; Q3C1A6; -.
DR   SMR; Q3C1A6; -.
DR   BRENDA; 1.2.1.9; 5919.
DR   GO; GO:0008886; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   1: Evidence at protein level;
KW   NADP; Oxidoreductase.
FT   CHAIN           1..476
FT                   /note="NADP-dependent glyceraldehyde-3-phosphate
FT                   dehydrogenase"
FT                   /id="PRO_0000331318"
FT   ACT_SITE        250
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        284
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         154..155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         230..251
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         283..285
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         377
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   BINDING         437
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   476 AA;  51192 MW;  349284A1181CED47 CRC64;
     MTKQYKNYVN GEWKLSKEEI KIYAPATGEE LGSVPAMSQE EVDYVYASAK AAQKAWRALS
     YVERAEYLHK AADILMRDAE KIGAVLSKEI AKGYKSAVGE VIRTAEIINY AAEEGVRLEG
     EVLEGGSFDP ASKKKIAIVR REPVGLVLAI SPFNYPINLA GSKIAPALIS GNVVALKPPT
     QGSISGLLLA EAFAEAGLPA GVFNTITGRG SVIGDYIVEH EAVNYINFTG STPVGEHIGH
     LAGMRPIMLE LGGKDSAIIL EDADLDLAAK NIVAGAYGYS GQRCTAVKRV LVMDSIADKL
     VEKVSALVNN LTVGMPEDNA DITPLIDTKA ADYVEGLIKD AQEKGAKEVI SFKREGNLIS
     PVLFDNVTTD MRLAWEEPFG PVLPFIRVNS VEEAIEISNK SEYGLQASVF TNNFPLAFKI
     AEQLEVGTVH INNKTQRGTD NFPFLGAKKS GAGVQGVKYS IEAMTTVKST VFDIAK