ID   PDX1_NEUCR              Reviewed;         308 AA.
AC   Q9C1K6;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Probable pyridoxal 5'-phosphate synthase subunit pdx-1;
DE            Short=PLP synthase subunit pdx-1;
DE            EC=4.3.3.6;
GN   Name=pdx-1; ORFNames=NCU06550;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=11238395; DOI=10.1093/genetics/157.3.1067;
RA   Bean L.E., Dvorachek W.H. Jr., Braun E.L., Errett A., Saenz G.S.,
RA   Giles M.D., Werner-Washburne M., Nelson M.A., Natvig D.O.;
RT   "Analysis of the pdx-1 (snz-1/sno-1) region of the Neurospora crassa
RT   genome. Correlation of pyridoxine-requiring phenotypes with mutations in
RT   two structural genes.";
RL   Genetics 157:1067-1075(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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 pdx-2. 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   -!- SIMILARITY: Belongs to the PdxS/SNZ family. {ECO:0000305}.
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DR   EMBL; AF309689; AAK07850.1; -; Genomic_DNA.
DR   EMBL; CM002239; EAA33021.1; -; Genomic_DNA.
DR   RefSeq; XP_962257.1; XM_957164.3.
DR   AlphaFoldDB; Q9C1K6; -.
DR   SMR; Q9C1K6; -.
DR   STRING; 5141.EFNCRP00000006310; -.
DR   PRIDE; Q9C1K6; -.
DR   EnsemblFungi; EAA33021; EAA33021; NCU06550.
DR   GeneID; 3878415; -.
DR   KEGG; ncr:NCU06550; -.
DR   VEuPathDB; FungiDB:NCU06550; -.
DR   HOGENOM; CLU_055352_1_0_1; -.
DR   InParanoid; Q9C1K6; -.
DR   OMA; RYANRGW; -.
DR   UniPathway; UPA00245; -.
DR   Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR   GO; GO:0016843; F:amine-lyase activity; IBA:GO_Central.
DR   GO; GO:0036381; F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:EnsemblFungi.
DR   GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IBA:GO_Central.
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   3: Inferred from homology;
KW   Lyase; Pyridoxal phosphate; Reference proteome; Schiff base.
FT   CHAIN           1..308
FT                   /note="Probable pyridoxal 5'-phosphate synthase subunit
FT                   pdx-1"
FT                   /id="PRO_0000109363"
FT   ACT_SITE        87
FT                   /note="Schiff-base intermediate with D-ribose 5-phosphate"
FT                   /evidence="ECO:0000250|UniProtKB:O59080"
FT   BINDING         30
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000250|UniProtKB:O59080"
FT   BINDING         159
FT                   /ligand="D-ribose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:78346"
FT                   /evidence="ECO:0000250|UniProtKB:O59080"
FT   BINDING         171
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"
SQ   SEQUENCE   308 AA;  32355 MW;  47D73BB4CAD284D7 CRC64;
     MTSTSTTTNG DSFTVKAGLA QMLKGGVIMD VTTPAEARIA EEAGACAVMA LERIPSDIRA
     AGGVARMSNP SMIKEIQAAV TIPVMAKARI GHVTECRILE QLGVDYIDES EVLTPADDTY
     HVQKDQFKAP FVCGCRNLGE ALRRIKEGAA MIRTKGEAGT GDVVEAVKHI RTVNAEIAQA
     KAALASGGEL AVAKMAREIG ADVELLKKTA ELGRLPVVNF AAGGVATPAD AALMMEFGCD
     GVFVGSGIFK DAKTPEHALQ RARAVVKAVA NWNDYGALVE ACIEHGEAMK GISNAGMKPE
     ERMAGRGW