PDX1_SUBDO
ID PDX1_SUBDO Reviewed; 306 AA.
AC Q8WPW2; Q9U5K9;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Pyridoxal 5'-phosphate synthase subunit SNZERR;
DE Short=PLP synthase subunit SNZERR;
DE EC=4.3.3.6;
DE AltName: Full=Ethylene response protein;
DE AltName: Full=PDX1;
GN Name=SNZERR; Synonyms=ERR;
OS Suberites domuncula (Sponge).
OC Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha; Suberitida;
OC Suberitidae; Suberites.
OX NCBI_TaxID=55567;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX PubMed=10531355; DOI=10.1074/jbc.274.44.31524;
RA Krasko A., Schroeder H.C., Perovic S., Steffen R., Kruse M., Reichert W.,
RA Mueller I.M., Mueller W.E.G.;
RT "Ethylene modulates gene expression in cells of the marine sponge Suberites
RT domuncula and reduces the degree of apoptosis.";
RL J. Biol. Chem. 274:31524-31530(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11470156; DOI=10.1016/s0167-4781(01)00246-9;
RA Seack J., Perovic S., Gamulin V., Schroeder H.C., Beutelmann P.,
RA Mueller I.M., Mueller W.E.G.;
RT "Identification of highly conserved genes: SNZ and SNO in the marine sponge
RT Suberites domuncula: their gene structure and promoter activity in
RT mammalian cells.";
RL Biochim. Biophys. Acta 1520:21-34(2001).
CC -!- FUNCTION: Catalyzes the formation of pyridoxal 5'-phosphate from ribose
CC 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The
CC ammonia is provided by PDX2. Can also use ribulose 5-phosphate and
CC dihydroxyacetone phosphate as substrates, resulting from enzyme-
CC catalyzed isomerization of RBP and G3P, respectively. Also plays an
CC indirect role in resistance to singlet oxygen-generating
CC photosensitizers. {ECO:0000250|UniProtKB:Q03148}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate +
CC L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-
CC phosphate; Xref=Rhea:RHEA:31507, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:58359, ChEBI:CHEBI:59776,
CC ChEBI:CHEBI:597326; EC=4.3.3.6;
CC Evidence={ECO:0000250|UniProtKB:Q03148};
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
CC -!- INDUCTION: By ethylene, a major product of degradation of oceanic
CC dissolved organic carbon by photochemical reactions initiated by
CC sunlight. {ECO:0000269|PubMed:10531355}.
CC -!- SIMILARITY: Belongs to the PdxS/SNZ family. {ECO:0000305}.
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DR EMBL; Y18971; CAC80278.1; -; mRNA.
DR EMBL; Y19159; CAB59635.1; -; mRNA.
DR EMBL; AJ277952; CAC81977.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8WPW2; -.
DR SMR; Q8WPW2; -.
DR UniPathway; UPA00245; -.
DR GO; GO:0036381; F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity; IEA:UniProtKB-EC.
DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04727; pdxS; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01824; PdxS; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001852; PdxS/SNZ.
DR InterPro; IPR033755; PdxS/SNZ_N.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR31829; PTHR31829; 1.
DR Pfam; PF01680; SOR_SNZ; 1.
DR PIRSF; PIRSF029271; Pdx1; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR00343; TIGR00343; 1.
DR PROSITE; PS01235; PDXS_SNZ_1; 1.
DR PROSITE; PS51129; PDXS_SNZ_2; 1.
PE 2: Evidence at transcript level;
KW Lyase; Pyridoxal phosphate; Schiff base.
FT CHAIN 1..306
FT /note="Pyridoxal 5'-phosphate synthase subunit SNZERR"
FT /id="PRO_0000109365"
FT ACT_SITE 91
FT /note="Schiff-base intermediate with D-ribose 5-phosphate"
FT /evidence="ECO:0000250|UniProtKB:O59080"
FT BINDING 34
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000250|UniProtKB:O59080"
FT BINDING 163
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000250|UniProtKB:O59080"
FT BINDING 175
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:Q03148"
FT BINDING 224
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000250|UniProtKB:O59080"
FT BINDING 245..246
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000250|UniProtKB:O59080"
FT CONFLICT 43
FT /note="V -> I (in Ref. 1; CAC81977)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="S -> T (in Ref. 1; CAC81977)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="R -> H (in Ref. 1; CAC81977)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="L -> M (in Ref. 1; CAC81977)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 306 AA; 32705 MW; 9FE1317B10A58EBB CRC64;
MSEPKTSATS ETQTGTMTVK TGLAQMLKGG IIMDVINADQ ARVAEEAGAC AVMALEKVPA
DIRKDGGVAR MADPRKIKEI MDTVTVPVMA KCRIGHFAEA QILQNLGVDF IDESEVLSPA
DDENHVDKQP FNVPFVCGAR SLGEALRRIS EGAAMIRTKG EAGTGNVVEA VRHARQINRE
IRVAQCLSSA ELYGYAKQLG VPLDLLQKTA KLGRLPVVNF AAGGLATPAD VSLLMQLGVD
GVFVGSGIFK SGNPEKRAKA MVQAVTHYND PKVLADVSED LGDPMVGLNC EHLSEKWAQR
ESVHKS
