ID S3ZNZ9_9ACTN Unreviewed; 430 AA.
AC S3ZNZ9;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=STRAU_2438 {ECO:0000313|EMBL:EPH44519.1};
OS Streptomyces aurantiacus JA 4570.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=1286094 {ECO:0000313|EMBL:EPH44519.1, ECO:0000313|Proteomes:UP000014629};
RN [1] {ECO:0000313|EMBL:EPH44519.1, ECO:0000313|Proteomes:UP000014629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA 4570 {ECO:0000313|EMBL:EPH44519.1,
RC ECO:0000313|Proteomes:UP000014629};
RA Gruening B.A., Praeg A., Erxleben A., Guenther S., Mueller M.;
RT "Draft Genome Sequence of Streptomyces aurantiacus, Which Produces
RT Setomimycin.";
RL Submitted (FEB-2013) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPH44519.1}.
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DR EMBL; AOPZ01000090; EPH44519.1; -; Genomic_DNA.
DR RefSeq; WP_016640567.1; NZ_AOPZ01000090.1.
DR AlphaFoldDB; S3ZNZ9; -.
DR PATRIC; fig|1286094.4.peg.2411; -.
DR OrthoDB; 9766131at2; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000014629; Unassembled WGS sequence.
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}; Reference proteome {ECO:0000313|Proteomes:UP000014629};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00133}.
FT DOMAIN 66..390
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 100
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00133"
SQ SEQUENCE 430 AA; 45688 MW; 14F3FE2830E6CFB7 CRC64;
MPSEYFIPDP EGRTPSAEGY FGAFGGKFIP EALVAAVDEV AVEFDKAKAD PEFARELDDL
LMNYTGRPSA LTEVPRFAEH AGGARVFLKR EDLNHTGSHK INNVLGQALL TKRMGKTRVI
AETGAGQHGV ATATACALFG LECTIYMGEI DTQRQALNVA RMRMLGAEVI AVKSGSRTLK
DAINEAFRDW VANVDHTHYL FGTVAGPHPF PAMVRDFHRV IGVEARRQIL ERAGRLPDAA
VACVGGGSNA IGLFHAFIPD ADVRLVGCEP AGHGVETGEH AATLTAGEPG ILHGSRSYVL
QDEEGQITEP YSISAGLDYP GIGPEHAHLK DSGRGEYRAV TDDAAMEALR LLSRTEGIIP
AIESAHALAG ALEIGKELGK DGLIIVNLSG RGDKDMDTAA RYFNLYDTGA DATVAADAAG
ESAEIEGDAK
//
