ID A0A3G8WJX4_BIFBR Unreviewed; 695 AA. AC A0A3G8WJX4; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 13-NOV-2019, entry version 4. 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=EH245_05680 {ECO:0000313|EMBL:AZI16721.1}; OS Bifidobacterium breve. OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=1685 {ECO:0000313|EMBL:AZI16721.1, ECO:0000313|Proteomes:UP000278881}; RN [1] {ECO:0000313|EMBL:AZI16721.1, ECO:0000313|Proteomes:UP000278881} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=lw01 {ECO:0000313|Proteomes:UP000278881}; RA Wang L., Wang Y., Li Q., Tian K., Xu L., Guo C.; RT "Genetic and biochemical evidence that exopolysacchride from a novel RT strain Bifidobacterium breve lw01."; RL Submitted (NOV-2018) 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- CC Rule:MF_00133, ECO:0000256|SAAS:SAAS00565555}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = CC D-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; CC EC=4.2.1.20; Evidence={ECO:0000256|HAMAP-Rule:MF_00133, CC ECO:0000256|SAAS:SAAS01118361}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + CC H(+) = (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; CC EC=4.1.1.48; Evidence={ECO:0000256|HAMAP-Rule:MF_00134, CC ECO:0000256|SAAS:SAAS01121249}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00133, CC ECO:0000256|SAAS:SAAS00166768}; CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 4/5. {ECO:0000256|HAMAP- CC Rule:MF_00134, ECO:0000256|SAAS:SAAS00745759}. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 5/5. {ECO:0000256|HAMAP- CC Rule:MF_00133, ECO:0000256|SAAS:SAAS00015996}. CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. CC {ECO:0000256|HAMAP-Rule:MF_00133, ECO:0000256|SAAS:SAAS00239408}. CC -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000256|HAMAP- CC Rule:MF_00133, ECO:0000256|SAAS:SAAS00565571}. CC -!- SIMILARITY: Belongs to the TrpC family. {ECO:0000256|HAMAP- CC Rule:MF_00134, ECO:0000256|SAAS:SAAS00745742}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP034192; AZI16721.1; -; Genomic_DNA. DR UniPathway; UPA00035; UER00043. DR Proteomes; UP000278881; Chromosome. 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; 3.20.20.70; -; 1. DR Gene3D; 3.40.50.1100; -; 2. 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. DR InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS. DR InterPro; IPR001926; PLP-dep. 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; IPR036052; Trypto_synt_PLP_dependent. DR PANTHER; PTHR42882; PTHR42882; 1. DR Pfam; PF00218; IGPS; 1. DR Pfam; PF00291; PALP; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR SUPFAM; SSF53686; SSF53686; 1. DR TIGRFAMs; TIGR00263; trpB; 1. DR PROSITE; PS00614; IGPS; 1. DR PROSITE; PS00168; TRP_SYNTHASE_BETA; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00133, KW ECO:0000256|SAAS:SAAS00015918}; KW Aromatic amino acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00133, KW ECO:0000256|SAAS:SAAS00015879}; KW Complete proteome {ECO:0000313|Proteomes:UP000278881}; KW Decarboxylase {ECO:0000256|HAMAP-Rule:MF_00134, KW ECO:0000256|SAAS:SAAS00745753}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00133, KW ECO:0000256|SAAS:SAAS00015853}; KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00133, KW ECO:0000256|SAAS:SAAS00015971}; KW Tryptophan biosynthesis {ECO:0000256|HAMAP-Rule:MF_00133, KW ECO:0000256|SAAS:SAAS00015947}. FT DOMAIN 4 256 IGPS. {ECO:0000259|Pfam:PF00218}. FT DOMAIN 323 655 PALP. {ECO:0000259|Pfam:PF00291}. FT MOD_RES 363 363 N6-(pyridoxal phosphate)lysine. FT {ECO:0000256|HAMAP-Rule:MF_00133}. SQ SEQUENCE 695 AA; 74911 MW; 06DB2E885C07FF4B CRC64; MSVLDELVAG ALEDQQTREL TVSLEDVKKA ALAAPAPIDA TRWLKRADGI PVIAEIKRAS PSKGHLSDIP DPAALAREYE KGGASAISVL TEGRRFLGSL DDFDKVRAAV HIPVLRKDFI VTDYQIYEAR AHGADLVLLI VAALDDAQLK HLLDLAHELS MTVLVETHTR EEIERACQAG AKVIGINARN LKNLKVDVNK YNELAADLPD AVIKVAESGV FGAVEVEDYA RAGADAVLVG EGVATADDHE LAVERLVKAG AQVKASETTP LSEHQGPYWG QFGGRYVPEA LITALDELER VYTQAKADPE FHKEFMTLQQ RYVGRPSPLT EAPRFAALVK EKTGLDARIF LKREDLNHTG AHKINNALGQ ALLVKRMGKT RVIAETGAGQ HGVATATVCA MLGLKCRIYM GQIDARRQAL NVARMRMLGA EVVEVTLGDK ILKDAINEAL RDWVTNVKDT HYLLGTVAGP HPFPAMVRDF QKIIGEEAKQ QLQDWYGIDH PDAICACVGG GSNAIGVMNA FLDDDRVNLY GYEAGGNGPE SGRHAIRFAP GTGQLGMFQG AKSYLLETDE GQTLDTYSIS AGLDYASVGP EHAWLKDIGR VNYSWATDEE AMNAFRDLSQ SEGIIPAIES SHAVAGAYKA AADLKAKGYN KAVMIVNISG RGDKDMATAG KWFGYLTDDQ AAALDVAGAH GDTAA //