TRPB1_SACS2
ID TRPB1_SACS2 Reviewed; 425 AA.
AC P50383;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Tryptophan synthase beta chain 1;
DE EC=4.2.1.20;
GN Name=trpB1; Synonyms=trpB; OrderedLocusNames=SSO0888;
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 [GENOMIC DNA].
RC STRAIN=DSM 5833 / MT-4;
RA Tutino M.L., Cubellis M., Sannia G., Marino G.;
RT "The tryptophan operon in Sulfolobus solfataricus.";
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
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}.
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DR EMBL; Z50014; CAA90307.1; -; Genomic_DNA.
DR EMBL; AE006641; AAK41171.1; -; Genomic_DNA.
DR PIR; D90239; D90239.
DR RefSeq; WP_009992302.1; NC_002754.1.
DR PDB; 6HUL; X-ray; 2.55 A; B=1-425.
DR PDBsum; 6HUL; -.
DR AlphaFoldDB; P50383; -.
DR SMR; P50383; -.
DR STRING; 273057.SSO0888; -.
DR EnsemblBacteria; AAK41171; AAK41171; SSO0888.
DR GeneID; 44129819; -.
DR KEGG; sso:SSO0888; -.
DR PATRIC; fig|273057.12.peg.892; -.
DR eggNOG; arCOG01432; Archaea.
DR HOGENOM; CLU_042858_1_0_2; -.
DR InParanoid; P50383; -.
DR OMA; QWGMAVS; -.
DR PhylomeDB; P50383; -.
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..425
FT /note="Tryptophan synthase beta chain 1"
FT /id="PRO_0000099055"
FT MOD_RES 108
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT CONFLICT 127
FT /note="V -> A (in Ref. 1; CAA90307)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="W -> R (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="T -> N (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="M -> T (in Ref. 1; CAA90307)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="G -> A (in Ref. 1; CAA90307)"
FT /evidence="ECO:0000305"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:6HUL"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:6HUL"
FT HELIX 36..43
FT /evidence="ECO:0007829|PDB:6HUL"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:6HUL"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:6HUL"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:6HUL"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:6HUL"
FT HELIX 82..88
FT /evidence="ECO:0007829|PDB:6HUL"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:6HUL"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:6HUL"
FT HELIX 109..122
FT /evidence="ECO:0007829|PDB:6HUL"
FT STRAND 126..134
FT /evidence="ECO:0007829|PDB:6HUL"
FT HELIX 135..146
FT /evidence="ECO:0007829|PDB:6HUL"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:6HUL"
FT HELIX 157..162
FT /evidence="ECO:0007829|PDB:6HUL"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:6HUL"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:6HUL"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:6HUL"
FT HELIX 186..193
FT /evidence="ECO:0007829|PDB:6HUL"
FT HELIX 202..216
FT /evidence="ECO:0007829|PDB:6HUL"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:6HUL"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:6HUL"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:6HUL"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:6HUL"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:6HUL"
FT HELIX 262..273
FT /evidence="ECO:0007829|PDB:6HUL"
FT STRAND 280..288
FT /evidence="ECO:0007829|PDB:6HUL"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:6HUL"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:6HUL"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:6HUL"
FT STRAND 309..315
FT /evidence="ECO:0007829|PDB:6HUL"
FT HELIX 336..343
FT /evidence="ECO:0007829|PDB:6HUL"
FT STRAND 346..352
FT /evidence="ECO:0007829|PDB:6HUL"
FT HELIX 354..367
FT /evidence="ECO:0007829|PDB:6HUL"
FT HELIX 374..391
FT /evidence="ECO:0007829|PDB:6HUL"
FT TURN 392..394
FT /evidence="ECO:0007829|PDB:6HUL"
FT STRAND 398..403
FT /evidence="ECO:0007829|PDB:6HUL"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:6HUL"
FT HELIX 411..417
FT /evidence="ECO:0007829|PDB:6HUL"
SQ SEQUENCE 425 AA; 47707 MW; C026C989E4262324 CRC64;
MVKEDEILPK YWYNIIPDLP KPLPPPRDPQ GAYFSRIDLL RSILPKEVLR QQFTIERYIK
IPEEVRDRYL SIGRPTPLFR AKRLEEYLKT PARIYFKYEG ATPTGSHKIN TAIPQAYFAK
EEGIEHVVTE TGAGQWGTAV ALAASMYNMK STIFMVKVSY EQKPMRRSIM QLYGANVYAS
PTNLTEYGRK ILETNPQHPG SLGIAMSEAI EYALKNEFRY LVGSVLDVVL LHQSVIGQET
ITQLDLLGED ADILIGCVGG GSNFGGFTYP FIGNKKGKRY IAVSSAEIPK FSKGEYKYDF
PDSAGLLPLV KMITLGKDYV PPPIYAGGLR YHGVAPTLSL LTKEGIVEWR EYNEREIFEA
AKIFIENQGI VPAPESAHAI RAVVDEAIEA RKNNERKVIV FNLSGHGLLD LSNYESMMKR
LNGNG
