ID A0A0A8EUC8_9ACTN Unreviewed; 420 AA.
AC A0A0A8EUC8;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Tryptophan synthase beta chain {ECO:0000256|HAMAP-Rule:MF_00133};
DE EC=4.2.1.20 {ECO:0000256|HAMAP-Rule:MF_00133};
GN Name=trpB {ECO:0000256|HAMAP-Rule:MF_00133};
GN ORFNames=GZL_06487 {ECO:0000313|EMBL:AJC59057.1};
OS Streptomyces sp. 769.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1262452 {ECO:0000313|EMBL:AJC59057.1, ECO:0000313|Proteomes:UP000031113};
RN [1] {ECO:0000313|EMBL:AJC59057.1, ECO:0000313|Proteomes:UP000031113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=769 {ECO:0000313|EMBL:AJC59057.1,
RC ECO:0000313|Proteomes:UP000031113};
RA Du Q., Wang Q., Li Q., Wang L., Zhang Z., Ren J., Wang J., Wang M.;
RT "Complete Genome Sequence of Streptomyces gongzhulingensis.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC tryptophan from indole and L-serine. {ECO:0000256|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:0000256|ARBA:ARBA00000003, ECO:0000256|HAMAP-
CC Rule:MF_00133};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00133};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5. {ECO:0000256|ARBA:ARBA00004733,
CC ECO:0000256|HAMAP-Rule:MF_00133}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC {ECO:0000256|ARBA:ARBA00011270, ECO:0000256|HAMAP-Rule:MF_00133}.
CC -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000256|ARBA:ARBA00009982,
CC ECO:0000256|HAMAP-Rule:MF_00133}.
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; CP003987; AJC59057.1; -; Genomic_DNA.
DR RefSeq; WP_039637453.1; NZ_CP003987.1.
DR AlphaFoldDB; A0A0A8EUC8; -.
DR KEGG; stre:GZL_06487; -.
DR HOGENOM; CLU_016734_3_1_11; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000031113; Chromosome.
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; IPR006653; Trp_synth_b_CS.
DR InterPro; IPR006654; Trp_synth_beta.
DR InterPro; IPR023026; Trp_synth_beta/beta-like.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR00263; trpB; 1.
DR PANTHER; PTHR48077:SF3; TRYPTOPHAN SYNTHASE; 1.
DR PANTHER; PTHR48077; TRYPTOPHAN SYNTHASE-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF001413; Trp_syn_beta; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00168; TRP_SYNTHASE_BETA; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00133};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_00133};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00133};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00133};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00133}.
FT DOMAIN 68..393
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 103
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00133"
SQ SEQUENCE 420 AA; 44687 MW; 11FF300DDC633FF1 CRC64;
MSSESSRFFL PDPEGQVPSA EGYFGAFGGK FIPEALVAAV DEVAAEYEKA KADPAFAAEL
DDLMVNYTGR PSALTEVPRF AEHAGGARVF LKREDLNHTG SHKINNVLGQ ALLTKRMGKT
RVIAETGAGQ HGVATATACA LFGLECTIYM GEVDTQRQAL NVARMRMLGA EVIAVKSGSR
TLKDAINEAF RDWVANVDRT HYLFGTVAGP HPFPALVRDF HRVIGVEARR QILERTGRLP
DAALACVGGG SNAIGLFHAF LPDAGVRLIG CEPGGHGIET GEHAATLTEG TPGILHGSRS
YVLQDEDGQI TEPYSISAGL DYPGIGPEHA YLKDVGRAEY RAVTDDAAMQ ALRLLSRTEG
IIPAIESAHA LAGALEVGRE LGPDGLLLVN LSGRGDKDMD TAARYFGLYG NDDQTGEGDK
//