ID A0A1I4EMJ7_9RHOB Unreviewed; 408 AA.
AC A0A1I4EMJ7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=SAMN04488004_10740 {ECO:0000313|EMBL:SFL06413.1};
OS Loktanella salsilacus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Loktanella.
OX NCBI_TaxID=195913 {ECO:0000313|EMBL:SFL06413.1, ECO:0000313|Proteomes:UP000199550};
RN [1] {ECO:0000313|EMBL:SFL06413.1, ECO:0000313|Proteomes:UP000199550}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16199 {ECO:0000313|EMBL:SFL06413.1,
RC ECO:0000313|Proteomes:UP000199550};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOTF01000007; SFL06413.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4EMJ7; -.
DR STRING; 195913.SAMN04488004_10740; -.
DR OrthoDB; 9766131at2; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000199550; 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:UP000199550};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00133}.
FT DOMAIN 64..389
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 98
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00133"
SQ SEQUENCE 408 AA; 44582 MW; 87C47F526166EBF4 CRC64;
MPEDLFNSFM NGPDEKGRFG DFGGRFVSET LMPLILSLEE EYEKAKTDDS FWAEMNDLWT
HYVGRPSPLY FAERLTDHLG GAKVYMKRDE LNHTGAHKIN NVLGQIILAR RMGKTRIIAE
TGAGQHGVAT ATVCAKFGLK CVVYMGAHDV ERQAPNVFRM RLLGAEVVPV TSGRGTLKDA
MNDALRDWVT NVRDTFYCIG TVAGPHPYPA MVRDFQAIIG KETREQMHAA EGRLPDTLIA
AIGGGSNAMG LFFPFLDDKS VNIIGVEAGG KGVNAKMEHC ASLTGGRPGV LHGNRTYLLQ
DDDGQILEGF SISAGLDYPG IGPEHAWLHD IGRAQYVSIT DVEALEAFQL SCALEGIIPA
LEPSHALAHV MKIAPTLPKD HLLVMNMCGR GDKDIFTVAK HLGFDMKI
//
