ID R7JRV8_9FIRM Unreviewed; 394 AA.
AC R7JRV8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=BN630_01653 {ECO:0000313|EMBL:CDE66730.1};
OS Blautia sp. CAG:37.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=1262757 {ECO:0000313|EMBL:CDE66730.1, ECO:0000313|Proteomes:UP000018204};
RN [1] {ECO:0000313|EMBL:CDE66730.1, ECO:0000313|Proteomes:UP000018204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:37 {ECO:0000313|Proteomes:UP000018204};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDE66730.1}.
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DR EMBL; CBJJ010000175; CDE66730.1; -; Genomic_DNA.
DR AlphaFoldDB; R7JRV8; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000018204; 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:UP000018204};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00133}.
FT DOMAIN 52..375
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 85
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00133"
SQ SEQUENCE 394 AA; 43194 MW; CC71C61304D4F619 CRC64;
MSDGRFGIHG GQYIPETLMN EIINLEKQYN YYKNDPEFCQ ELDDLLKNYA GRPSLLYYAE
KMTKDLGGAK IYLKREDLNH TGAHKINNVL GQCLLAKRMG KTRVIAETGA GQHGVATATA
AALMGLECEI FMGKEDTDRQ ALNVYRMELL GAKVNAVTTG TMTLKDAVNE AMREWVSRVD
DTHYVLGSVM GPHPFPTIVR DFQAVISKEA REQILEKEGK LPKAVMACVG GGSNAMGMFY
NFINDKNVRL IGCEAAGRGV NTAETAATIA TGTLGVFHGM KSYFCQDKYG QIAPVYSISA
GLDYPGIGPE HAYLHDIGRA EYVPVTDDEA VEAFEYLART EGIICAIESA HAVAHAMKIA
KEFDPEDSII ICLSGRGDKD VAAIARYRGR DLHE
//
