ID A0A1I0PQ71_9BACT Unreviewed; 464 AA.
AC A0A1I0PQ71;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=tryptophan synthase {ECO:0000256|ARBA:ARBA00012043};
DE EC=4.2.1.20 {ECO:0000256|ARBA:ARBA00012043};
GN ORFNames=SAMN04487850_1931 {ECO:0000313|EMBL:SEW16512.1};
OS Prevotella aff. ruminicola Tc2-24.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=81582 {ECO:0000313|EMBL:SEW16512.1, ECO:0000313|Proteomes:UP000199373};
RN [1] {ECO:0000313|EMBL:SEW16512.1, ECO:0000313|Proteomes:UP000199373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC2-24 {ECO:0000313|EMBL:SEW16512.1,
RC ECO:0000313|Proteomes:UP000199373};
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|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; FOIQ01000004; SEW16512.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0PQ71; -.
DR Proteomes; UP000199373; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:InterPro.
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};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000199373};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822}.
FT DOMAIN 91..428
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
SQ SEQUENCE 464 AA; 51197 MW; 8E776226C34D902A CRC64;
MHAERTILKH LIMTKQKKFI LQESEIPTQW YNIQADMPNK PMPPIHPVTK QPLGVDDLAH
IFPRECCVQE LDTEHAWIDI PEEVLEKYKY YRSTPLVRAY ALEEALGTPA HIYFKNESTN
PLGSHKINSA LPQCYYAKQE GTTNVTTETG AGQWGAALSY AAKIYGLDCA VYQVKITMQQ
KPYRSSIMRT FGAVVEGSPS MSTRAGKDIL TRDPNHSGSL GTAISEAVEL ATTTPNCKYT
LGSVLNHVAI HQSIIGLEAE KQMAMAGEYP DMVIACFGGG SNFGGIAFPF MRHNILDGKK
TEFIAAEPDS CPKLTRGQFR YDFGDEAGYT PLLPMYTLGH NFKPSNIHAG GLRYHGAGMI
VSQLIKDGFM KGVDIPQLET FEAGMLFART EGIIPAPESC HAIAATIREA NKCKQTGEEK
VILFNLSGHG LIDMPSYDSY IKGDLQNYTV TDEMIAANLA EIDQ
//
