TRPB2_SACS2
ID TRPB2_SACS2 Reviewed; 429 AA.
AC Q97TX6;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Tryptophan synthase beta chain 2;
DE EC=4.2.1.20;
GN Name=trpB2; OrderedLocusNames=SSO1145;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(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}.
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; AE006641; AAK41396.1; -; Genomic_DNA.
DR PIR; E90267; E90267.
DR RefSeq; WP_010923209.1; NC_002754.1.
DR PDB; 4QYS; X-ray; 1.94 A; A/B=1-429.
DR PDB; 6EQN; X-ray; 1.96 A; B/D=4-428.
DR PDB; 6HTE; X-ray; 1.96 A; B/D=4-428.
DR PDBsum; 4QYS; -.
DR PDBsum; 6EQN; -.
DR PDBsum; 6HTE; -.
DR AlphaFoldDB; Q97TX6; -.
DR SMR; Q97TX6; -.
DR STRING; 273057.SSO1145; -.
DR EnsemblBacteria; AAK41396; AAK41396; SSO1145.
DR GeneID; 27427452; -.
DR KEGG; sso:SSO1145; -.
DR PATRIC; fig|273057.12.peg.1136; -.
DR eggNOG; arCOG01432; Archaea.
DR HOGENOM; CLU_042858_1_0_2; -.
DR InParanoid; Q97TX6; -.
DR OMA; RYHAVAP; -.
DR PhylomeDB; Q97TX6; -.
DR BRENDA; 4.2.1.20; 6163.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0052684; F:L-serine hydro-lyase (adding indole, L-tryptophan-forming) activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Lyase; Pyridoxal phosphate; Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..429
FT /note="Tryptophan synthase beta chain 2"
FT /id="PRO_0000099056"
FT MOD_RES 111
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:4QYS"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:4QYS"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:4QYS"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:4QYS"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:4QYS"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:4QYS"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:4QYS"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:4QYS"
FT HELIX 66..74
FT /evidence="ECO:0007829|PDB:4QYS"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:4QYS"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:4QYS"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:4QYS"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:4QYS"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:4QYS"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:4QYS"
FT HELIX 138..149
FT /evidence="ECO:0007829|PDB:4QYS"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:4QYS"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:4QYS"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:4QYS"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:4QYS"
FT HELIX 189..195
FT /evidence="ECO:0007829|PDB:4QYS"
FT HELIX 205..218
FT /evidence="ECO:0007829|PDB:4QYS"
FT HELIX 230..236
FT /evidence="ECO:0007829|PDB:4QYS"
FT HELIX 238..249
FT /evidence="ECO:0007829|PDB:4QYS"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:4QYS"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:4QYS"
FT HELIX 265..281
FT /evidence="ECO:0007829|PDB:4QYS"
FT STRAND 286..293
FT /evidence="ECO:0007829|PDB:4QYS"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:4QYS"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:4QYS"
FT STRAND 318..323
FT /evidence="ECO:0007829|PDB:4QYS"
FT HELIX 344..351
FT /evidence="ECO:0007829|PDB:4QYS"
FT STRAND 354..360
FT /evidence="ECO:0007829|PDB:4QYS"
FT HELIX 362..375
FT /evidence="ECO:0007829|PDB:4QYS"
FT HELIX 382..385
FT /evidence="ECO:0007829|PDB:4QYS"
FT HELIX 388..399
FT /evidence="ECO:0007829|PDB:4QYS"
FT STRAND 405..411
FT /evidence="ECO:0007829|PDB:4QYS"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:4QYS"
FT HELIX 419..426
FT /evidence="ECO:0007829|PDB:4QYS"
SQ SEQUENCE 429 AA; 47778 MW; 2DBE2C8591335844 CRC64;
MAMRIRIDLP QDEIPAQWYN ILPDLPEELP PPQDPTGKSL ELLKEVLPSK VLELEFAKER
YVKIPDEVLE RYLQVGRPTP IIRAKRLEEY LGNNIKIYLK MESYTYTGSH KINSALAHVY
YAKLDNAKFV TTETGAGQWG SSVALASALF RMKAHIFMVR TSYYAKPYRK YMMQMYGAEV
HPSPSDLTEF GRQLLAKDSN HPGSLGIAIS DAVEYAHKNG GKYVVGSVVN SDIMFKTIAG
MEAKKQMELI GEDPDYIIGV VGGGSNYAAL AYPFLGDELR SGKVRRKYIA SGSSEVPKMT
KGVYKYDYPD TAKLLPMLKM YTIGSDFVPP PVYAGGLRYH GVAPTLSLLI SKGIVQARDY
SQEESFKWAK LFSELEGYIP APETSHALPI LAEIAEEAKK SGERKTVLVS FSGHGLLDLG
NYASVLFKE
