TRPB1_SULTO
ID TRPB1_SULTO Reviewed; 422 AA.
AC Q971Z5;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Tryptophan synthase beta chain 1;
DE EC=4.2.1.20;
GN Name=trpB1; OrderedLocusNames=STK_12330;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
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; BA000023; BAB66274.1; -; Genomic_DNA.
DR RefSeq; WP_010979252.1; NC_003106.2.
DR AlphaFoldDB; Q971Z5; -.
DR SMR; Q971Z5; -.
DR STRING; 273063.STK_12330; -.
DR EnsemblBacteria; BAB66274; BAB66274; STK_12330.
DR GeneID; 1459231; -.
DR KEGG; sto:STK_12330; -.
DR PATRIC; fig|273063.9.peg.1392; -.
DR eggNOG; arCOG01432; Archaea.
DR OMA; QWGMAVS; -.
DR OrthoDB; 24741at2157; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000001015; 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..422
FT /note="Tryptophan synthase beta chain 1"
FT /id="PRO_0000099057"
FT MOD_RES 107
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 422 AA; 47166 MW; 00CE463FA830BBCE CRC64;
MVNKDLIPKY WYNIIPDLPK PLPPPRDPPD AEFSRIELLK KILPKEVLRQ QFTIERFIKI
PEEVRDRYAI IGRPTPLMRA KRLEEYLDTP AKIYFKFEGA TPTGSHKINT AVPQAYFAAE
EGISHVVTET GAGQWGTAVA LAASMYDLSS TIFMVRVSYE QKPMRKTIME LYGGKVYASP
TDLTEFGRKI LKENPNHPGS LGIAMSEAIE FALNHNFRYL VGSVLDVVLL HQSVIGMEAI
AQLDELGEEP DILIGCVGGG SNFGGFTYPF IGAKKGKKYI AVGAAEIPKF STGKYEYDYP
DTAGLLPLVK MITLGKDYVP PPIYAGGLRY HGVAPTLSLL IKEKIVEWRE YKEEEIYEAA
KIFMKTQGIV PAPESAHAIK AVIDEALKAK TEKERRVIVF NLSGHGLLDL GNYESIRRRV
EK