TRPG_PICAN
ID TRPG_PICAN Reviewed; 367 AA.
AC P09575;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Multifunctional tryptophan biosynthesis protein;
DE Includes:
DE RecName: Full=Anthranilate synthase component 2;
DE Short=AS;
DE EC=4.1.3.27;
DE AltName: Full=Anthranilate synthase, glutamine amidotransferase component;
DE Includes:
DE RecName: Full=Indole-3-glycerol phosphate synthase;
DE EC=4.1.1.48;
DE AltName: Full=PRAI;
DE Flags: Fragment;
OS Pichia angusta (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=870730;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC Y-5445;
RX PubMed=2582370; DOI=10.1093/nar/13.9.3063;
RA Ledeboer A.M., Edens L., Maat J., Visser C., Bos J.W., Verrips C.T.;
RT "Molecular cloning and characterization of a gene coding for methanol
RT oxidase in Hansenula polymorpha.";
RL Nucleic Acids Res. 13:3063-3082(1985).
RN [2]
RP IDENTIFICATION OF CODING REGION.
RX PubMed=3399398; DOI=10.1093/nar/16.13.6236;
RA Reid G.A.;
RT "Anthranilate synthase component II from Hansenula polymorpha.";
RL Nucleic Acids Res. 16:6236-6236(1988).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate +
CC pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58359; EC=4.1.3.27;
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 -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 4/5.
CC -!- SUBUNIT: Tetramer of two components I and two components II.
CC -!- MISCELLANEOUS: Component I catalyzes the formation of anthranilate
CC using ammonia rather than glutamine, whereas component II provides
CC glutamine amidotransferase activity.
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DR EMBL; X02425; CAA26280.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; P09575; -.
DR SMR; P09575; -.
DR MEROPS; C26.959; -.
DR UniPathway; UPA00035; UER00040.
DR UniPathway; UPA00035; UER00043.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR013798; Indole-3-glycerol_P_synth_dom.
DR InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR006221; TrpG/PapA_dom.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF00218; IGPS; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR00566; trpG_papA; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS00614; IGPS; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Glutamine amidotransferase; Lyase; Multifunctional enzyme;
KW Tryptophan biosynthesis.
FT CHAIN 1..>367
FT /note="Multifunctional tryptophan biosynthesis protein"
FT /id="PRO_0000056860"
FT DOMAIN 7..201
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT REGION 209..>367
FT /note="Indole-3-glycerol phosphate synthase"
FT ACT_SITE 86
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 175
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 177
FT /note="For GATase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT BINDING 58..60
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 90
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 136..137
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT NON_TER 367
SQ SEQUENCE 367 AA; 40899 MW; FB358D63FA6178E8 CRC64;
MPAASKNVVM IDNYDSFTWN LYEYLCQEGA NVEVFRNDQI TIPEIEQLKP DVVVISPGPG
HPRTDSGISR DVISHFKGKI PVFGVCMGQQ CIFEEFGGDV EYAGEIVHGK TSTVKHDNKG
MFKNVPQDVA VTRYHSLAGT LKSLPDCLEI TARTDNGIIM GVRHKKYTIE GVQFHPESIL
TEEGHLMIQN ILNVSGGYWE ENANGAAQRK ESILEKIYAQ RRKDYEFEMN RPGRRFADLE
LYLSMGLAPP LINFYDRLEQ NISAGKVAIL SEIKRASPSK GVIDGDANAA KQALNYAKAG
VATISVLTEP TWFKGNIQDL EVARKAIDSV ANRPCILRKE FIFNKYQILE ARLAGADTVL
LIVKMLS
