ID A0A0J8UFJ1_COCIT Unreviewed; 606 AA.
AC A0A0J8UFJ1;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Anthranilate synthase component 2 {ECO:0000313|EMBL:KMU86138.1};
GN ORFNames=CIHG_03926 {ECO:0000313|EMBL:KMU86138.1};
OS Coccidioides immitis H538.4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU86138.1, ECO:0000313|Proteomes:UP000054563};
RN [1] {ECO:0000313|Proteomes:UP000054563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H538.4 {ECO:0000313|Proteomes:UP000054563};
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 -!- 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 -!- 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 -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5. {ECO:0000256|ARBA:ARBA00004873}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 3/5. {ECO:0000256|ARBA:ARBA00004664}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 4/5. {ECO:0000256|ARBA:ARBA00004696}.
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DR EMBL; DS016991; KMU86138.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8UFJ1; -.
DR STRING; 396776.A0A0J8UFJ1; -.
DR VEuPathDB; FungiDB:CIHG_03926; -.
DR eggNOG; KOG0026; Eukaryota.
DR eggNOG; KOG4201; Eukaryota.
DR eggNOG; KOG4202; Eukaryota.
DR UniPathway; UPA00035; UER00042.
DR Proteomes; UP000054563; Unassembled WGS sequence.
DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01743; GATase1_Anthranilate_Synthase; 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; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR013798; Indole-3-glycerol_P_synth_dom.
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 PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00099; CPSGATASE.
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.
PE 3: Inferred from homology;
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Reference proteome {ECO:0000313|Proteomes:UP000054563}.
FT DOMAIN 27..216
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 303..353
FT /note="Indole-3-glycerol phosphate synthase"
FT /evidence="ECO:0000259|Pfam:PF00218"
FT DOMAIN 434..601
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 606 AA; 65246 MW; 78BE049BB524F5B6 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 GIISSSTSAP SQARKYAMAG
AMDQVSYSTI VWALSGISGP KDVEAYRANG VKGVLVGEAL MQAEDTSAFV QNLLGPEIQL
SPNSLPCSPP LVKICGTRSG DAARAAIEAG ADLVVIILAQ GRTRTVPDEV ALKISKGVKT
TPRPSLWNNY FRQAPSSQTG LDYFDNGCRL LRHPSRALLV GVFANQPLSY IISQQQKLGL
DIIQLHGSEP IEWARLIPVP VIKKFSPEDK DITKRAYHAL PLLDSGVGGT GERLSLPAVE
EALERDDGLR IILAGGLNPE NLVSTVKALG EQSRKVVGVD VSSGVEVDGS QDLGKIRAFV
AAAKGL
//
