ID   TRP_NEUCR               Reviewed;         708 AA.
AC   P13228; O93879; Q7RVI6;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=Tryptophan synthase;
DE            EC=4.2.1.20;
GN   Name=trp-3; ORFNames=NCU08409;
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].
RX   PubMed=2521855; DOI=10.1016/s0021-9258(19)84927-x;
RA   Burns D.M., Yanofsky C.;
RT   "Nucleotide sequence of the Neurospora crassa trp-3 gene encoding
RT   tryptophan synthetase and comparison of the trp-3 polypeptide with its
RT   homologs in Saccharomyces cerevisiae and Escherichia coli.";
RL   J. Biol. Chem. 264:3840-3848(1989).
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-129.
RC   STRAIN=314-448A;
RA   Lacy A.M., Case M.E., Nelson W.S.;
RT   "Distribution, nature, and possible significance of the base substitutions
RT   in 27 well characterized mutants of the trp-3 (tryptophan synthase) gene of
RT   Neurospora crassa.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 358-397, AND PYRIDOXAL PHOSPHATE AT LYS-392.
RX   PubMed=2966157; DOI=10.1016/s0021-9258(18)68725-3;
RA   Pratt M.L., Demoss J.A.;
RT   "Neurospora tryptophan synthase. Characterization of the pyridoxal
RT   phosphate binding site.";
RL   J. Biol. Chem. 263:6872-6876(1988).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-
CC         glyceraldehyde 3-phosphate + H2O + L-tryptophan;
CC         Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC         ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the TrpA family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the TrpB family.
CC       {ECO:0000305}.
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DR   EMBL; J04594; AAA33616.1; -; Genomic_DNA.
DR   EMBL; CM002237; EAA34045.1; -; Genomic_DNA.
DR   EMBL; AF084886; AAD04354.1; -; Genomic_DNA.
DR   PIR; A32959; A32959.
DR   RefSeq; XP_963281.1; XM_958188.2.
DR   AlphaFoldDB; P13228; -.
DR   SMR; P13228; -.
DR   STRING; 5141.EFNCRP00000007806; -.
DR   PRIDE; P13228; -.
DR   EnsemblFungi; EAA34045; EAA34045; NCU08409.
DR   GeneID; 3879436; -.
DR   KEGG; ncr:NCU08409; -.
DR   VEuPathDB; FungiDB:NCU08409; -.
DR   HOGENOM; CLU_016734_1_0_1; -.
DR   InParanoid; P13228; -.
DR   OMA; VDTARHS; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR   CDD; cd06446; Trp-synth_B; 1.
DR   CDD; cd04724; Tryptophan_synthase_alpha; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   HAMAP; MF_00131; Trp_synth_alpha; 1.
DR   HAMAP; MF_00133; Trp_synth_beta; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   InterPro; IPR006653; Trp_synth_b_CS.
DR   InterPro; IPR006654; Trp_synth_beta.
DR   InterPro; IPR023026; Trp_synth_beta/beta-like.
DR   InterPro; IPR018204; Trp_synthase_alpha_AS.
DR   InterPro; IPR002028; Trp_synthase_suA.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF00290; Trp_syntA; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR00262; trpA; 1.
DR   TIGRFAMs; TIGR00263; trpB; 1.
DR   PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1.
DR   PROSITE; PS00168; TRP_SYNTHASE_BETA; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Direct protein sequencing; Lyase; Pyridoxal phosphate; Reference proteome;
KW   Tryptophan biosynthesis.
FT   CHAIN           1..708
FT                   /note="Tryptophan synthase"
FT                   /id="PRO_0000098724"
FT   REGION          1..305
FT                   /note="Tryptophan synthase alpha chain"
FT   REGION          306..708
FT                   /note="Tryptophan synthase beta chain"
FT   ACT_SITE        49
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        60
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         392
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT   VARIANT         67
FT                   /note="A -> ATA (in strain: 314-448A)"
SQ   SEQUENCE   708 AA;  76451 MW;  4151CB78D254435B CRC64;
     MEGIKQTFQR CKAQNRAALV TYVTAGFPHP EQTPDILLAM EKGGADVIEL GVPFTDPIAD
     GPTIQTANTI ALQHGVTLQS TLQMVRDARQ RGLKAPVMLM GYYNPLLSYG EERLLNDCKE
     AGVNGFIIVD LPPEEAVSFR QLCTRGGLSY VPLIAPATSD ARMRVLCQLA DSFIYVVSRQ
     GVTGASGTLN ANLPELLARV KKYSGNKPAA VGFGVSTHDH FTQVGAIADG VVVGSMIITT
     IQKAAKGEEV KAVQEYCSYL CGRNFEQSAH ELNMGEALEA AKEPVGTATV DGVITEADID
     AQLAALHGTI PKRFGEFGGQ YVPEALMDCL SELEEGFNKI KDDPAFWEEY RSYYPWMGRP
     GQLHKAERLT EYAGGANIWL KREDLNHTGS HKINNALGQL LLARRLGKKK IIAETGAGQH
     GVATATVCAK FGMECTVFMG AEDVRRQALN VFRMKLLGAK VVAVEAGSRT LRDAVNEALR
     YWVVNLADTH YIIGSAIGPH PFPTIVRTFQ SVIGNETKQQ MLEKRGKLPD AVVACVGGGS
     NAVGMFYPFS NDPSVKLLGV EAGGDGVDTP RHSATLTAGS KGVLHGVRTY ILQNQYGQIE
     DTHSISAGLD YPGVGPELSN WKDTERAKFV AATDAQAFEG FRLMSQLEGI IPALESSHGI
     WGALELAKTM KPDEDVVICL SGRGDKDVQS VADELPIIGP KIGWDLRF