PDX1_CERNC
ID PDX1_CERNC Reviewed; 343 AA.
AC O59905;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Pyridoxal 5'-phosphate synthase subunit PDX1;
DE Short=PLP synthase subunit PDX1;
DE EC=4.3.3.6;
DE AltName: Full=Singlet oxygen resistance protein 1;
GN Name=PDX1; Synonyms=SOR1;
OS Cercospora nicotianae (Barn spot disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=29003;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=ATCC 18366;
RX PubMed=9660944; DOI=10.1016/s1097-2765(00)80060-x;
RA Ehrenshaft M., Jenns A.E., Chung K.-R., Daub M.E.;
RT "SOR1, a gene required for photosensitizer and singlet oxygen resistance in
RT Cercospora fungi, is highly conserved in divergent organisms.";
RL Mol. Cell 1:603-609(1998).
RN [2]
RP FUNCTION, INDUCTION, MUTAGENESIS OF 133-ILE-GLY-134; CYS-176 AND SER-189,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=9933360; DOI=10.1007/s002940050423;
RA Ehrenshaft M., Chung K.-R., Jenns A.E., Daub M.E.;
RT "Functional characterization of SOR1, a gene required for resistance to
RT photosensitizing toxins in the fungus Cercospora nicotianae.";
RL Curr. Genet. 34:478-485(1999).
RN [3]
RP FUNCTION.
RX PubMed=10430950; DOI=10.1073/pnas.96.16.9374;
RA Ehrenshaft M., Bilski P., Li M.Y., Chignell C.F., Daub M.E.;
RT "A highly conserved sequence is a novel gene involved in de novo vitamin B6
RT biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:9374-9378(1999).
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:0000269|PubMed:10430950,
CC ECO:0000269|PubMed:9660944, ECO:0000269|PubMed:9933360}.
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 -!- DEVELOPMENTAL STAGE: Expressed throughout the growth cycle.
CC {ECO:0000269|PubMed:9660944}.
CC -!- INDUCTION: Accumulation is enhanced two-fold by light, but is
CC unaffected by the presence of cercosporin, a photosensitizer
CC synthesized by C.nicotianae. {ECO:0000269|PubMed:9933360}.
CC -!- DISRUPTION PHENOTYPE: Defects cause some indirect sensitivity to
CC photosensitizers, due to the inability to synthesize pyridoxal 5'-
CC phosphate. Indeed, pyridoxal 5'-phosphate quenches singlet oxygen at a
CC rate comparable to that of vitamins C and E.
CC {ECO:0000269|PubMed:9933360}.
CC -!- SIMILARITY: Belongs to the PdxS/SNZ family. {ECO:0000305}.
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DR EMBL; AF035619; AAD13386.1; -; Genomic_DNA.
DR PIR; T46646; T46646.
DR AlphaFoldDB; O59905; -.
DR SMR; O59905; -.
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 1: Evidence at protein level;
KW Lyase; Pyridoxal phosphate; Schiff base.
FT CHAIN 1..343
FT /note="Pyridoxal 5'-phosphate synthase subunit PDX1"
FT /id="PRO_0000109361"
FT ACT_SITE 130
FT /note="Schiff-base intermediate with D-ribose 5-phosphate"
FT /evidence="ECO:0000250|UniProtKB:O59080"
FT BINDING 73
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000250|UniProtKB:O59080"
FT BINDING 202
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000250|UniProtKB:O59080"
FT BINDING 214
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:Q03148"
FT BINDING 263
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000250|UniProtKB:O59080"
FT BINDING 284..285
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000250|UniProtKB:O59080"
FT MUTAGEN 133..134
FT /note="IG->NC: In CS6; induces sensitivity to singlet
FT oxygen."
FT /evidence="ECO:0000269|PubMed:9933360"
FT MUTAGEN 176
FT /note="C->R: In CS9; induces sensitivity to singlet
FT oxygen."
FT /evidence="ECO:0000269|PubMed:9933360"
FT MUTAGEN 189
FT /note="S->P: In CS8; induces sensitivity to singlet
FT oxygen."
FT /evidence="ECO:0000269|PubMed:9933360"
SQ SEQUENCE 343 AA; 36181 MW; 3C9F742BFCE1EC63 CRC64;
MASNGTSVSP FRSQKNAAMA VNDTPANGHA EPSTITAASK TNTTKITSQN DPQSSFAVKV
GLAQMLKGGV IMDVVNAEQA RIAEEAGACA VMALERVPAD IRKDGGVARM SDPQMIKDIM
NAVTIPVMAK SRIGHFVECQ ILQAIGVDYI DESEVLTPAD PVNHIDKSVY NVPFVCGCKN
LGEALRRISE GAAMIRTKGE AGTGDVVEAV RHMQTVNAEI AKASSASDAD LRMMARELQC
DYNLLKQTAQ LKRLPVVNFA AGGIATPADA ALMMQMGCDG VFVGSGIFKS GDAAKRAKAI
VQATTHYNDP KVLAEVSSGL GEAMVGINCD KLPETQKLAT RGW
