ID   TRP_SCHPO               Reviewed;         697 AA.
AC   O13831; P78765;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Tryptophan synthase;
DE            EC=4.2.1.20;
GN   Name=trp2; ORFNames=SPAC19A8.15;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 261-679.
RC   STRAIN=PR745;
RX   PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CU329670; CAB11651.1; -; Genomic_DNA.
DR   EMBL; D89113; BAA13775.1; -; mRNA.
DR   PIR; T37946; T37946.
DR   PIR; T42090; T42090.
DR   RefSeq; NP_593777.1; NM_001019206.2.
DR   AlphaFoldDB; O13831; -.
DR   SMR; O13831; -.
DR   BioGRID; 278712; 4.
DR   STRING; 4896.SPAC19A8.15.1; -.
DR   MaxQB; O13831; -.
DR   PaxDb; O13831; -.
DR   PRIDE; O13831; -.
DR   EnsemblFungi; SPAC19A8.15.1; SPAC19A8.15.1:pep; SPAC19A8.15.
DR   GeneID; 2542240; -.
DR   KEGG; spo:SPAC19A8.15; -.
DR   PomBase; SPAC19A8.15; trp2.
DR   VEuPathDB; FungiDB:SPAC19A8.15; -.
DR   eggNOG; KOG1395; Eukaryota.
DR   eggNOG; KOG4175; Eukaryota.
DR   HOGENOM; CLU_016734_1_1_1; -.
DR   InParanoid; O13831; -.
DR   OMA; VDTARHS; -.
DR   PhylomeDB; O13831; -.
DR   UniPathway; UPA00035; UER00044.
DR   PRO; PR:O13831; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0004834; F:tryptophan synthase activity; ISO:PomBase.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; ISO:PomBase.
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   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Pyridoxal phosphate; Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..697
FT                   /note="Tryptophan synthase"
FT                   /id="PRO_0000098725"
FT   REGION          1..298
FT                   /note="Tryptophan synthase alpha chain"
FT   REGION          298..697
FT                   /note="Tryptophan synthase beta chain"
FT   ACT_SITE        50
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        61
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         381
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        417
FT                   /note="A -> P (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        420..435
FT                   /note="FGMKCTIYMGAEDCRR -> IWYEMYYPTWVQKIVVV (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        482
FT                   /note="I -> T (in Ref. 2; BAA13775)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        670..679
FT                   /note="SGRGDKDVQS -> QVVVTRMFKA (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   697 AA;  75437 MW;  B96E5B7449EC5335 CRC64;
     MTEQIKKTFL KAKEENKNVL VTFVTCGFPN VDETIKIMQG LQNGGAGIIE LGIPFSDAVA
     DGPTICKGNE IALKNNITLE KVFETVKLAR DAGVTIPIIL MGYYNPIFSY GDAKTIQKAK
     EVGANGFIIV DLPPEEAVGF REECKKQGVS FVPLVAPSTT DRRMELLASV ADSFIYVVSR
     MGSTGSSATG VINTALPQLC QRVRKFAGDT PLAVGFGVNT SEHFHQVGSV SDGVVVGSKI
     IDLILKAEPG TAATVVEEYC KYLTKEDPSA PVPKQFQSGG SVATAPPAAV VEPINEMYLP
     QKYGMFGGMY VPEALTQCLV ELESVFYKAL HDEKFWEEFR SYYEYMGRPS ALDYAKRLTE
     YCGGAHIWLK REDLNHGGSH KINNCIGQIL LAKRLGKNRI IAETGAGQHG VATAICAAKF
     GMKCTIYMGA EDCRRQALNV FRIRLLGAEV VPVTSGTQTL RDAVNEALKA WVEQIDTTHY
     LIGSAIGPHP FPTIVKTFQS VIGEETKAQM QEKRKKLPDA VVACVGGGSN SIGMFSPFKA
     DKSVMMLGCE AGGDGVDTPK HSATLTMGKV GVFHGVRTYV LQREDGQIQD THSISAGLDY
     PGVGPELSEL KYTNRAEFIA VTDAQCLEGF RALCHLEGII PALESSHAVY GGMELAKKLP
     KDKDIVITIS GRGDKDVQSV AEQLPILGPK IGWDLRF