ID   TRPB1_AERPE             Reviewed;         427 AA.
AC   Q9Y8T5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 118.
DE   RecName: Full=Tryptophan synthase beta chain 1;
DE            EC=4.2.1.20;
GN   Name=trpB1; OrderedLocusNames=APE_2548;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
CC   -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC       tryptophan from indole and L-serine. {ECO:0000250}.
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         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000305}.
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DR   EMBL; BA000002; BAA81565.1; -; Genomic_DNA.
DR   PIR; E72488; E72488.
DR   AlphaFoldDB; Q9Y8T5; -.
DR   SMR; Q9Y8T5; -.
DR   STRING; 272557.APE_2548; -.
DR   EnsemblBacteria; BAA81565; BAA81565; APE_2548.
DR   KEGG; ape:APE_2548; -.
DR   PATRIC; fig|272557.25.peg.1692; -.
DR   eggNOG; arCOG01432; Archaea.
DR   OMA; QWGMAVS; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000002518; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   HAMAP; MF_00133; Trp_synth_beta; 1.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR006316; Trp_synth_b-like.
DR   InterPro; IPR006653; Trp_synth_b_CS.
DR   InterPro; IPR023026; Trp_synth_beta/beta-like.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   PANTHER; PTHR48077:SF6; PTHR48077:SF6; 1.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF001413; Trp_syn_beta; 1.
DR   PIRSF; PIRSF500824; TrpB_prok; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR01415; trpB_rel; 1.
DR   PROSITE; PS00168; TRP_SYNTHASE_BETA; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Pyridoxal phosphate; Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..427
FT                   /note="Tryptophan synthase beta chain 1"
FT                   /id="PRO_0000099030"
FT   MOD_RES         107
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   427 AA;  45992 MW;  DC8E165B40B65750 CRC64;
     MVSVPLRWYN IAADLPEPLP PLRDPEGLRE ESRIALLSRI LPSRLIEDEY ILARWVDIPG
     EVRKALARIG RPTPLIRAEG LEKVLGVKGR VRIYYKSEAV LPTGSHKINT AIAQAYYAKL
     DGAKEIVTET GAGQWGLAAS TAAALMGLKA TVFMTASSFK SKIQRRLLME AQGARVISSP
     SKLTDTGREA LEEYGSTHPG SLGLAIAEAV EYTLESGDRR YLPGSVLEAV LMHQTVIGLE
     ALDQLPEEPD VVVACVGGGS NFGGFTYPMI GARLRGEGFE KTRFIAAEST AAPKLTRGEY
     RYDGLDSSLI LPLAKMYTLG HRYTPPPSHA AGLRYHGVSP SLSILRRLGL VEAEAIPQEE
     ALASILLMAR SEGVVPAPES SHAVALAARI ARKLPDGSVV AFNLSGHGLL DLDALQKALE
     IRGASMW