TRPB_STAA8
ID TRPB_STAA8 Reviewed; 404 AA.
AC Q2FYR4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Tryptophan synthase beta chain {ECO:0000255|HAMAP-Rule:MF_00133};
DE EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00133};
GN Name=trpB {ECO:0000255|HAMAP-Rule:MF_00133};
GN OrderedLocusNames=SAOUHSC_01371;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
CC -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC tryptophan from indole and L-serine. {ECO:0000255|HAMAP-Rule:MF_00133}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00133};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00133};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5. {ECO:0000255|HAMAP-
CC Rule:MF_00133}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000255|HAMAP-
CC Rule:MF_00133}.
CC -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000255|HAMAP-
CC Rule:MF_00133}.
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DR EMBL; CP000253; ABD30466.1; -; Genomic_DNA.
DR RefSeq; WP_001041337.1; NZ_LS483365.1.
DR RefSeq; YP_499898.1; NC_007795.1.
DR AlphaFoldDB; Q2FYR4; -.
DR SMR; Q2FYR4; -.
DR STRING; 1280.SAXN108_1388; -.
DR EnsemblBacteria; ABD30466; ABD30466; SAOUHSC_01371.
DR GeneID; 3920780; -.
DR KEGG; sao:SAOUHSC_01371; -.
DR PATRIC; fig|93061.5.peg.1255; -.
DR eggNOG; COG0133; Bacteria.
DR HOGENOM; CLU_016734_3_1_9; -.
DR OMA; HGMKSYF; -.
DR UniPathway; UPA00035; UER00044.
DR PRO; PR:Q2FYR4; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; 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 Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF001413; Trp_syn_beta; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR00263; trpB; 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..404
FT /note="Tryptophan synthase beta chain"
FT /id="PRO_1000018406"
FT MOD_RES 94
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ SEQUENCE 404 AA; 43965 MW; 5DD7414223101237 CRC64;
MNKQIQTEAD ELGFFGEYGG QYVPETLMPA IIELKKAYKE AKADPEFQRE LEYYLSEYVG
RATPLTYAAS YTESLGGAKI YLKREDLNHT GAHKINNALG QALLAKRMGK KKLVAETGAG
QHGVASATVA ALFDMELVVF MGSEDIKRQQ LNVFRMELLG AKVVAVEDGQ GTLSDAVNKA
LQYWVSHVDD THYLLGSALG PDPFPTIVRD FQSVIGKEIK SQILKKEGRL PDAIVACIGG
GSNAIGTFYP FIKDDVALYG VEAAGQGDDT DKHALAIGKG SPGVLHGTKM YLIQDEDGQV
QLAHSISAGL DYPGIGPEHS YYHDIGRVTF ENASDTQAMN ALINFTKHEG IIPAIESAHA
LSYVERLAPT MSKEDIIVVT ISGRGDKDME TIRQYMVERG LAND