ID   TRPB2_AERPE             Reviewed;         449 AA.
AC   Q9Y9H2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Tryptophan synthase beta chain 2;
DE            EC=4.2.1.20;
GN   Name=trpB2; OrderedLocusNames=APE_2316;
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; BAA81328.1; -; Genomic_DNA.
DR   PIR; H72458; H72458.
DR   AlphaFoldDB; Q9Y9H2; -.
DR   SMR; Q9Y9H2; -.
DR   STRING; 272557.APE_2316; -.
DR   PRIDE; Q9Y9H2; -.
DR   EnsemblBacteria; BAA81328; BAA81328; APE_2316.
DR   KEGG; ape:APE_2316; -.
DR   PATRIC; fig|272557.25.peg.1545; -.
DR   eggNOG; arCOG01432; Archaea.
DR   OMA; MLHQTII; -.
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   CDD; cd06446; Trp-synth_B; 1.
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; IPR006654; Trp_synth_beta.
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..449
FT                   /note="Tryptophan synthase beta chain 2"
FT                   /id="PRO_0000099031"
FT   MOD_RES         116
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   449 AA;  49535 MW;  7715911C236E2421 CRC64;
     MDLARYRFDL SIEEVPTSWY NILPDLPEEV PPPLNPKTGE PVDPSALAKL FPKALIEQEV
     SRERYIEIPG EVHEAYISFA RRPTPLLRAV NLERALNTPA EIYYKYEGVT PTGSHKINTA
     LAQAYYNKLE GVERLVTETG AGQWGSALSA AGAYFGVKVR VYMVRVSYLQ KPYRRTLMEL
     YGAEVYPSPS DKTEFGRKLL AENPNHPGSL GIAISEAIED VINSGGNAKY SLGSVLNHVL
     LHQTVIGLEA EKQFREAGVY PDIMIGAVGG GSNFAGFTYP FIRHRLKGSS STRFIAVEPK
     ASPSMTRGVY TYDYGDTAGL TPLLKMHTLG HTYQVPPIHA GGLRYHGVAP TLSVLLKHGI
     VEARAYHQRE VFRAAHMFAK AEGIVPAPES AHAVKAAIDE AIKARDEGRR VVIAFNLSGH
     GLLDLQGYRE YLDGTLEDYE PEEIPASRR