ID A0A087AVZ3_9BIFI Unreviewed; 694 AA.
AC A0A087AVZ3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|HAMAP-Rule:MF_00134};
DE Includes:
DE RecName: Full=Indole-3-glycerol phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00134};
DE Short=IGPS {ECO:0000256|HAMAP-Rule:MF_00134};
DE EC=4.1.1.48 {ECO:0000256|HAMAP-Rule:MF_00134};
DE Includes:
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=trpC {ECO:0000256|HAMAP-Rule:MF_00134};
GN Synonyms=trpB {ECO:0000256|HAMAP-Rule:MF_00133};
GN ORFNames=BCUN_0774 {ECO:0000313|EMBL:KFI62943.1};
OS Bifidobacterium cuniculi.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1688 {ECO:0000313|EMBL:KFI62943.1, ECO:0000313|Proteomes:UP000029067};
RN [1] {ECO:0000313|EMBL:KFI62943.1, ECO:0000313|Proteomes:UP000029067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 10738 {ECO:0000313|EMBL:KFI62943.1,
RC ECO:0000313|Proteomes:UP000029067};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+)
CC = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O;
CC Xref=Rhea:RHEA:23476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58613, ChEBI:CHEBI:58866; EC=4.1.1.48;
CC Evidence={ECO:0000256|ARBA:ARBA00001633, ECO:0000256|HAMAP-
CC Rule:MF_00134};
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 4/5. {ECO:0000256|ARBA:ARBA00004696,
CC ECO:0000256|HAMAP-Rule:MF_00134}.
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 -!- SIMILARITY: Belongs to the TrpC family. {ECO:0000256|HAMAP-
CC Rule:MF_00134}.
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:KFI62943.1}.
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DR EMBL; JGYV01000010; KFI62943.1; -; Genomic_DNA.
DR RefSeq; WP_033515891.1; NZ_JGYV01000010.1.
DR AlphaFoldDB; A0A087AVZ3; -.
DR STRING; 1688.BCUN_0774; -.
DR eggNOG; COG0133; Bacteria.
DR OrthoDB; 9766131at2; -.
DR UniPathway; UPA00035; UER00043.
DR Proteomes; UP000029067; Unassembled WGS sequence.
DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR CDD; cd00331; IGPS; 1.
DR CDD; cd06446; Trp-synth_B; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00134_B; IGPS_B; 1.
DR HAMAP; MF_00133; Trp_synth_beta; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR013798; Indole-3-glycerol_P_synth_dom.
DR InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
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; PF00218; IGPS; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00614; IGPS; 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_00134};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|HAMAP-Rule:MF_00134};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW Rule:MF_00134};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00134};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00133}; Reference proteome {ECO:0000313|Proteomes:UP000029067};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW Rule:MF_00134}.
FT DOMAIN 4..256
FT /note="Indole-3-glycerol phosphate synthase"
FT /evidence="ECO:0000259|Pfam:PF00218"
FT DOMAIN 324..647
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 363
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00133"
SQ SEQUENCE 694 AA; 74947 MW; 067B25721D2C5400 CRC64;
MSVLDELVAG AQHDQRAREQ ATTLAQLKEQ AATMPAPLDA TRWLKRPDAI PVIAEIKRAS
PSKGHLADIP DPGALAAQYA AGGASAISVL TEEQRFHGSL DDLDAVRANV DIPVLRKDFI
TTDYQVWEAR AHGADLILLI VAALADDDLR RLLDLTHDLG MTALVETHTV EEIDRARAAG
AKVIGINARN LKDLRVDVGK YRELADGLPD DVVKVAESGV FGSVELEDYA RAGADAVLVG
EGVATADDHV LAVQRLVKAG ATVKASEQTP LSEHEGPYFG QYGGRFVPEA LVSALDELER
VYEDAKRDPE FHRELARLNQ QYVGRPSPLT EAPRFAARLK EKTGVEARVF LKREDLNHTG
AHKINNAIGQ ALLVKRMGKT RVIAETGAGQ HGVATATVCA MMGLKCRIYM GQVDARRQAL
NVARMRMLGA EVVEVTLGDR ILKDAINEAL RDWVTNVEDT HYLLGTVAGP HPFPAMVRDF
QKIIGEEAKQ QLNDWYGIDH PDAVVACVGG GSNAIGVMNA FLDDERVNLY GYEAGGDGPE
SGRHAIRFAP GTGELGMFQG AKSYLLENSE GQTLDTYSIS AGLDYASVGP EHAWLKDIGR
VRYSWATDGE AMAAFKDLCE TEGIIPAIES SHAVAGAYKA ALDLKERGVE HPVMIVNISG
RGDKDMNTAG KWFGYLTDEQ SKALEANGAQ GNNA
//
