GAPN_SACS2
ID GAPN_SACS2 Reviewed; 509 AA.
AC Q97U30;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase;
DE EC=1.2.1.90 {ECO:0000269|PubMed:15869466};
DE AltName: Full=Glyceraldehyde phosphate dehydrogenase (NAD(P));
DE Short=GAPN;
GN Name=gapN-3; OrderedLocusNames=SSO3194;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=15869466; DOI=10.1042/bj20041711;
RA Ahmed H., Ettema T.J., Tjaden B., Geerling A.C., van der Oost J.,
RA Siebers B.;
RT "The semi-phosphorylative Entner-Doudoroff pathway in hyperthermophilic
RT archaea: a re-evaluation.";
RL Biochem. J. 390:529-540(2005).
CC -!- FUNCTION: Catalyzes the irreversible NAD(P)-dependent non-
CC phosphorylating oxidation of glyceraldehyde-3-phosphate (GAP) to 3-
CC phosphoglycerate (3PG). It is highly specific for D-GAP.
CC {ECO:0000269|PubMed:15869466}.
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=1.2.1.90;
CC Evidence={ECO:0000269|PubMed:15869466};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + H2O + NAD(+) = (2R)-3-
CC phosphoglycerate + 2 H(+) + NADH; Xref=Rhea:RHEA:42760,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58272, ChEBI:CHEBI:59776; EC=1.2.1.90;
CC Evidence={ECO:0000269|PubMed:15869466};
CC -!- ACTIVITY REGULATION: Allosterically activated by AMP, ADP, glucose 1-
CC phosphate (G1P), and fructose 6-phosphate (F6P).
CC {ECO:0000250|UniProtKB:O57693}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.099 mM for NADP (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:15869466};
CC KM=0.453 mM for GAP (at 70 degrees Celsius)
CC {ECO:0000269|PubMed:15869466};
CC Vmax=3.3 umol/min/mg enzyme with NADP as substrate (at 70 degrees
CC Celsius) {ECO:0000269|PubMed:15869466};
CC Vmax=3.4 umol/min/mg enzyme with GAP as substrate (at 70 degrees
CC Celsius) {ECO:0000269|PubMed:15869466};
CC -!- SUBUNIT: Homotetramer. Dimer of dimers. {ECO:0000250|UniProtKB:O57693}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AE006641; AAK43292.1; -; Genomic_DNA.
DR PIR; E90504; E90504.
DR RefSeq; WP_009991691.1; NC_002754.1.
DR AlphaFoldDB; Q97U30; -.
DR SMR; Q97U30; -.
DR STRING; 273057.SSO3194; -.
DR EnsemblBacteria; AAK43292; AAK43292; SSO3194.
DR GeneID; 44128911; -.
DR KEGG; sso:SSO3194; -.
DR PATRIC; fig|273057.12.peg.3298; -.
DR eggNOG; arCOG01252; Archaea.
DR HOGENOM; CLU_005391_1_0_2; -.
DR InParanoid; Q97U30; -.
DR OMA; HGIGYYP; -.
DR PhylomeDB; Q97U30; -.
DR BRENDA; 1.2.1.9; 6163.
DR SABIO-RK; Q97U30; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0008886; F:glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
DR GO; GO:0050661; F:NADP binding; ISS:UniProtKB.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
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; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; NAD; NADP; Nucleotide-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..509
FT /note="NAD(P)-dependent glyceraldehyde-3-phosphate
FT dehydrogenase"
FT /id="PRO_0000422653"
FT ACT_SITE 270
FT /evidence="ECO:0000250|UniProtKB:O57693"
FT ACT_SITE 304
FT /evidence="ECO:0000250|UniProtKB:O57693"
FT BINDING 79
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:O57693"
FT BINDING 79
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:O57693"
FT BINDING 79
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:O57693"
FT BINDING 86
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:O57693"
FT BINDING 86
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:O57693"
FT BINDING 86
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:O57693"
FT BINDING 161..162
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:O57693"
FT BINDING 161..162
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:O57693"
FT BINDING 175
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:O57693"
FT BINDING 198..201
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O57693"
FT BINDING 198
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O57693"
FT BINDING 231
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O57693"
FT BINDING 251
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O57693"
FT BINDING 251
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O57693"
FT BINDING 272
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O57693"
FT BINDING 272
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O57693"
FT BINDING 303..305
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:O57693"
FT BINDING 403
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:O57693"
FT BINDING 403
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O57693"
FT BINDING 463..464
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:O57693"
SQ SEQUENCE 509 AA; 56927 MW; A9D47247B08400E7 CRC64;
MEKTSVLIKS KELMEIYELK DGVPYFKTYL SGQWISGDEW QDVISPIDLN IIGKIPKLNW
NQIDDTLEHI YRKGRWSIRD TPGEKRLDIY KKMASLLDKF KEDFVNVLMI NNGKTKSAAE
GEVKAAIERL LRADLDVKET RGDYVPGDWS SETLETEAVV RKEPVGVVLS IVPFNYPLFD
TVNKIVYTTV IGNAIIIKPP SSTPLPILML AKVMELASFP KDSFAIITIP GRDMNKVVGD
KRIQAISLTG STETGEEVVR NAGIKQFIME LGGGDPAIVL SDADLAWAAQ RIAAGIISYT
GQRCDSVKLV LVEEEVYDTL KDLLIKELTK SVKVGDPRDP LTTVGPVIDV KTVDEWEKAI
KDAVEKGGKI LFGGKRLGPT YIEPVLIEAP KETLKDMYFY NKEVFASAAL LIKVKNIDEA
LEISNSRKYG LDAAIFGKDI NKIRKLQRFL EVGAIYINDY PRHGIGYFPF GGRKDSGIGR
EGIGYTIQYV TAYKSIVYNY KGKGIWEYL
