ID G5J7N7_CROWT Unreviewed; 412 AA.
AC G5J7N7;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
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=CWATWH0003_3473 {ECO:0000313|EMBL:EHJ11800.1};
OS Crocosphaera watsonii WH 0003.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Crocosphaera.
OX NCBI_TaxID=423471 {ECO:0000313|EMBL:EHJ11800.1, ECO:0000313|Proteomes:UP000003477};
RN [1] {ECO:0000313|EMBL:EHJ11800.1, ECO:0000313|Proteomes:UP000003477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH 0003 {ECO:0000313|EMBL:EHJ11800.1,
RC ECO:0000313|Proteomes:UP000003477};
RX PubMed=22232617;
RA Bench S.R., Ilikchyan I.N., Tripp H.J., Zehr J.P.;
RT "Two Strains of Crocosphaera watsonii with Highly Conserved Genomes are
RT Distinguished by Strain-Specific Features.";
RL Front. Microbiol. 2:261-261(2011).
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:EHJ11800.1}.
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DR EMBL; AESD01000520; EHJ11800.1; -; Genomic_DNA.
DR RefSeq; WP_007306349.1; NZ_AESD01000520.1.
DR AlphaFoldDB; G5J7N7; -.
DR PATRIC; fig|423471.3.peg.3256; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000003477; 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};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00133}.
FT DOMAIN 68..396
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 106
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00133"
SQ SEQUENCE 412 AA; 45062 MW; 7CC746EA9B3E3BE9 CRC64;
MTTTPIAPSA TQTQYPDEIG RFGKYGGKYV PETLMPALSE LETAYHRYKN APEFQAELSQ
LLKDYVGRPS PLYFAERLTE YYARPDGTGP QIYLKREDLN HTGAHKINNA LGQVLLAKRM
GKKRIIAETG AGQHGVATAT VCARFGLECV IYMGIHDMER QKLNVFRMKL LGATVQPVSA
GTGTLKDATS EAIRDWVTNV ETTHYILGSV AGPHPYPMIV RDFHDIIGQE TRRQCQEKWD
SLPHILLACV GGGSNAMGLF YEFVKDTEIR LIGVEAAGES IASGKHAATL TKGRPGVLHG
AMSYLLQDEE GQVIEAHSIS AGLDYPGVGP EHSYLKDSGR AEYYSVTDAE AIAAFQRLSE
LEGIIPALET SHAIAYLETL CPQLEGSPRI IINCSGRGDK DVQTVAKYLG DE
//
