ID   D4LA60_RUMC1            Unreviewed;       453 AA.
AC   D4LA60;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=tryptophan synthase {ECO:0000256|ARBA:ARBA00012043};
DE            EC=4.2.1.20 {ECO:0000256|ARBA:ARBA00012043};
GN   OrderedLocusNames=RUM_02600 {ECO:0000313|EMBL:CBL16505.1};
OS   Ruminococcus champanellensis (strain DSM 18848 / JCM 17042 / KCTC 15320 /
OS   18P13).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminococcus.
OX   NCBI_TaxID=213810 {ECO:0000313|EMBL:CBL16505.1, ECO:0000313|Proteomes:UP000007054};
RN   [1] {ECO:0000313|Proteomes:UP000007054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18848 / JCM 17042 / 18P13
RC   {ECO:0000313|Proteomes:UP000007054};
RA   Pajon A., Turner K., Parkhill J., Bernalier A.;
RT   "The genome sequence of Ruminococcus sp. 18P13.";
RL   Submitted (MAR-2010) 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|ARBA:ARBA00002786}.
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};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5. {ECO:0000256|ARBA:ARBA00004733}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC       {ECO:0000256|ARBA:ARBA00011270}.
CC   -!- SIMILARITY: Belongs to the TrpB family.
CC       {ECO:0000256|ARBA:ARBA00009982}.
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DR   EMBL; FP929052; CBL16505.1; -; Genomic_DNA.
DR   RefSeq; WP_015557412.1; NZ_BBEP01000026.1.
DR   AlphaFoldDB; D4LA60; -.
DR   STRING; 213810.RUM_02600; -.
DR   GeneID; 83155096; -.
DR   KEGG; rch:RUM_02600; -.
DR   PATRIC; fig|213810.4.peg.115; -.
DR   HOGENOM; CLU_042858_1_0_9; -.
DR   OrthoDB; 9766131at2; -.
DR   BioCyc; RCHA213810:RUM_RS01235-MONOMER; -.
DR   Proteomes; UP000007054; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR006316; Trp_synth_b-like.
DR   InterPro; IPR023026; Trp_synth_beta/beta-like.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR01415; trpB_rel; 1.
DR   PANTHER; PTHR48077:SF6; TRYPTOPHAN SYNTHASE BETA CHAIN; 1.
DR   PANTHER; PTHR48077; TRYPTOPHAN SYNTHASE-RELATED; 1.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF001413; Trp_syn_beta; 1.
DR   PIRSF; PIRSF500824; TrpB_prok; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:CBL16505.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007054};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822}.
FT   DOMAIN          81..418
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
SQ   SEQUENCE   453 AA;  49718 MW;  63871D05343C1F93 CRC64;
     MAKEIPYKIY LDESEMPTAW YNLRADMKNK PAPLLNPATR QPCTAADLAP VFCEELVKQE
     LDDTTPYFEI PQEIRDFYKM YRPSPLVRAY CLEKKLGTPA KIYYKFEGNN TSGSHKLNSA
     IAQAYYAKQQ GLKGVTTETG AGQWGTALSM ACSYFDLDCK VYMVKVSYEQ KPFRREVMRT
     YGASVTPSPS TETAVGRKIL EEHPGTTGSL GCAISEAVEK ATTTEGYRYV LGSVLNQVLL
     HQSVIGLETK AALDKYGVKA DIIIGCAGGG SNLGGLIAPF MGEKLRGEAD YRIIAVEPAS
     CPSLTRGKFA YDFCDTGKVC PLAKMYTLGC DFIPAPNHAG GLRYHGMSST LSQLYADGLM
     EATSVTQTKV FEAAEYFARV EGILPAPESS HAIRVAIDEA LKCKETGEEK TIVFGLTGTG
     YFDMVAYEKY NDGKMNDYIP TDEELAESLK KLP
//