ID A0A0J8QR00_COCIT Unreviewed; 764 AA.
AC A0A0J8QR00;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Multifunctional tryptophan biosynthesis protein {ECO:0000256|PIRNR:PIRNR001382};
DE Includes:
DE RecName: Full=Anthranilate synthase component 2 {ECO:0000256|PIRNR:PIRNR001382};
DE Short=AS {ECO:0000256|PIRNR:PIRNR001382};
DE EC=4.1.3.27 {ECO:0000256|PIRNR:PIRNR001382};
DE AltName: Full=Anthranilate synthase, glutamine amidotransferase component {ECO:0000256|PIRNR:PIRNR001382};
DE Includes:
DE RecName: Full=Indole-3-glycerol phosphate synthase {ECO:0000256|PIRNR:PIRNR001382};
DE Short=IGPS {ECO:0000256|PIRNR:PIRNR001382};
DE EC=4.1.1.48 {ECO:0000256|PIRNR:PIRNR001382};
DE Includes:
DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase {ECO:0000256|PIRNR:PIRNR001382};
DE Short=PRAI {ECO:0000256|PIRNR:PIRNR001382};
DE EC=5.3.1.24 {ECO:0000256|PIRNR:PIRNR001382};
GN ORFNames=CISG_00886 {ECO:0000313|EMBL:KMU74956.1};
OS Coccidioides immitis RMSCC 3703.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=454286 {ECO:0000313|EMBL:KMU74956.1, ECO:0000313|Proteomes:UP000054559};
RN [1] {ECO:0000313|Proteomes:UP000054559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 3703 {ECO:0000313|Proteomes:UP000054559};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
CC -!- FUNCTION: Trifunctional enzyme bearing the Gln amidotransferase
CC (GATase) domain of anthranilate synthase, indole-glycerolphosphate
CC synthase, and phosphoribosylanthranilate isomerase activities.
CC {ECO:0000256|ARBA:ARBA00003272, ECO:0000256|PIRNR:PIRNR001382}.
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,
CC ECO:0000256|PIRNR:PIRNR001382};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-
CC carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate;
CC Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613;
CC EC=5.3.1.24; Evidence={ECO:0000256|ARBA:ARBA00001164,
CC ECO:0000256|PIRNR:PIRNR001382};
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 Evidence={ECO:0000256|ARBA:ARBA00000329,
CC ECO:0000256|PIRNR:PIRNR001382};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5. {ECO:0000256|ARBA:ARBA00004873,
CC ECO:0000256|PIRNR:PIRNR001382}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 3/5. {ECO:0000256|ARBA:ARBA00004664,
CC ECO:0000256|PIRNR:PIRNR001382}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 4/5. {ECO:0000256|ARBA:ARBA00004696,
CC ECO:0000256|PIRNR:PIRNR001382}.
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DR EMBL; DS268119; KMU74956.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8QR00; -.
DR STRING; 454286.A0A0J8QR00; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000054559; Unassembled WGS sequence.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR CDD; cd00331; IGPS; 1.
DR CDD; cd00405; PRAI; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 2.
DR HAMAP; MF_00135; PRAI; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR016302; Anthranilate_synth_II.
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; IPR001240; PRAI_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR006221; TrpG/PapA_dom.
DR NCBIfam; TIGR00566; trpG_papA; 1.
DR PANTHER; PTHR43418:SF4; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1.
DR PANTHER; PTHR43418; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED; 1.
DR Pfam; PF00117; GATase; 1.
DR Pfam; PF00218; IGPS; 1.
DR Pfam; PF00697; PRAI; 1.
DR PIRSF; PIRSF001382; TrpG-trpC-trpF; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00096; GATASE.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 2.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS00614; IGPS; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|PIRNR:PIRNR001382};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|PIRNR:PIRNR001382};
KW Decarboxylase {ECO:0000256|PIRNR:PIRNR001382};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
KW Isomerase {ECO:0000256|PIRNR:PIRNR001382};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001382};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000054559};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|PIRNR:PIRNR001382}.
FT DOMAIN 27..216
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 249..511
FT /note="Indole-3-glycerol phosphate synthase"
FT /evidence="ECO:0000259|Pfam:PF00218"
FT DOMAIN 570..759
FT /note="N-(5'phosphoribosyl) anthranilate isomerase (PRAI)"
FT /evidence="ECO:0000259|Pfam:PF00697"
FT ACT_SITE 104
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 199
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 201
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 764 AA; 82547 MW; 7D36A056FE2798D2 CRC64;
MASTELVDHS PNHPTKAQRL DNASNVVLID NYDSFTWNIY QYLILEGATV TVFRNDVISL
EELIAKKPTQ LVISPGPGHP NTDSGISKEA IQYFAGKIPV FGVCMGEQCI ISSFGGEVEV
TGEILHGKTS PLKHDGKGVY ATLPPNLAVT RYHSLAGTPQ TVPECLEVTS WTECENRGGR
GIIMGVRHKK LTVEGVQFHP ESILTEHGRT MFRNFLKWKG GTWEEALSST KSQSTAASEP
TTSKQMSILE KIYAHRKAAV DLQKAIPSQR PADLQAAYDL GIAPPQISFP SRLRDSPFSL
ALMAEIKRAS PSKGIISSST SAPSQARKYA MAGASVISVL TEPEWFKGSI EDLRAVRQSL
EGLPNRPAVL RKEFIFDEYQ ILEARLAGAD TVLLIVKMLP VDLLTHLYEY SCKLGMEPLV
EVNTAEEMAI AVKLGARVIG VNNRDLTSFE VDLGTTSRLM DQVSDSTIVC ALSGISGPKD
VEAYRANGVK AVLVGEALMR AEDTSAFVQN LLGPEIQLSP NSLPCSPPLV KICGTRSGDA
ARAAIEAGAD LVGIILAQGR TRTVPDEVAL EISKVVKTTP RPSLLDNYIR QAPSSQTGLD
YFDNGCRLLR HPSRALLVGV FANQPLSYII SQQQKLGLDI IQLHGSEPIE WARLIPVPVI
KKFSPEDKDI TKRAYHALPL LDSGVGGTGE RLSLPAVEEA LERDDGLRII LAGGLNPENL
VSTVKALGEQ SRKVVGVDVS SGVEVDGSQD LGKIRAFVAA AKGL
//
