ID T0KTH2_COLGC Unreviewed; 840 AA.
AC T0KTH2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=aminodeoxychorismate synthase {ECO:0000256|ARBA:ARBA00013139};
DE EC=2.6.1.85 {ECO:0000256|ARBA:ARBA00013139};
DE AltName: Full=Para-aminobenzoate synthase {ECO:0000256|ARBA:ARBA00031329};
DE AltName: Full=p-aminobenzoic acid synthase {ECO:0000256|ARBA:ARBA00031904};
GN ORFNames=CGLO_00823 {ECO:0000313|EMBL:EQB58867.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB58867.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-
CC glutamate; Xref=Rhea:RHEA:11672, ChEBI:CHEBI:29748,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58406; EC=2.6.1.85;
CC Evidence={ECO:0000256|ARBA:ARBA00001000};
CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 4-
CC aminobenzoate from chorismate: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005009}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the anthranilate
CC synthase component I family. {ECO:0000256|ARBA:ARBA00005970}.
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:EQB58867.1}.
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DR EMBL; AMYD01000191; EQB58867.1; -; Genomic_DNA.
DR AlphaFoldDB; T0KTH2; -.
DR STRING; 1237896.T0KTH2; -.
DR eggNOG; KOG1224; Eukaryota.
DR HOGENOM; CLU_006493_0_0_1; -.
DR OMA; DWSVNIR; -.
DR OrthoDB; 201921at2759; -.
DR UniPathway; UPA00077; UER00149.
DR Proteomes; UP000015530; Unassembled WGS sequence.
DR GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.60.120.10; Anthranilate synthase; 1.
DR InterPro; IPR005801; ADC_synthase.
DR InterPro; IPR019999; Anth_synth_I-like.
DR InterPro; IPR006805; Anth_synth_I_N.
DR InterPro; IPR015890; Chorismate_C.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR010117; PabB_fungal.
DR InterPro; IPR006221; TrpG/PapA_dom.
DR NCBIfam; TIGR01823; PabB-fungal; 1.
DR PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR PANTHER; PTHR11236:SF18; AMINODEOXYCHORISMATE SYNTHASE; 1.
DR Pfam; PF04715; Anth_synt_I_N; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00095; ANTSNTHASEI.
DR SUPFAM; SSF56322; ADC synthase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Reference proteome {ECO:0000313|Proteomes:UP000015530};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..235
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 320..478
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 535..829
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT ACT_SITE 98
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 215
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 217
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 840 AA; 93740 MW; 1112B8AEBC3959E0 CRC64;
MTRPQILFLD AYDSFTNNIV SLLTDLLDAD VHVLPIDTPL LNHDSPAFED EFHRELSRYH
AVVCGPGPGS PENEKDVGLM RCVWRLREEH LLPVLGICLG FQSLVLSAGG RVRRLRRGLH
GMVRAIEREM PHSPSWEDIF KGVPEFKATL YHSLCADIGQ DSVPDVDWKH KRWECRDVPD
LMPLAWAVEE REDGNERILM GVKHRTKPFW GLQYHPESVC TQQTGHAVLQ NWFVHAMQWN
KKTGRRIETE GKFLARNSLK PSLLSEVRSA ARGGHAPVLA WTEMPTSLAT VGLDCEYVFK
TMNLPAGIKV PDIVEILKSG RAEHIILDSA NSSTTATGAK DVRGRYSIIA LDVEEALRIE
YHVGDDFATA RVPSSQGLPI DLMETIPFGP QENIWHLLSS FFEKRRIPAP RVPQRPSDPP
LDVETPFRGG FMGYLTYEMG LKGIDVRVAA DRGHQRPDLC WAWVTKSIVV DHVKGLLHVQ
HLQKRKLNAD FWIDSVVASL QTSHFWQPGK SAVNGHHLDP MTVATRPVVR VPHASEYEAK
VLRCQKYIAA GESYELCLTD QTTITLPGRP SAEPYTNRVN GNHHPKSAHV TPWKLYKTLR
TRQPAPFGSF IRLGGATLIS SSPERFLEYG SDGSISMRPM KGTVRKSNEV ATLSQAEEIL
HVPKEEAENL MIVDLVCHDL HSICGSNVAV PDLMKVEEYA TVFQMVTVVC GQLQRLGAVE
EQHTGLDVLA ASLPPGSMTG APKKRSCELL QEIEEHRERS LYSGVVGYMD VTGKGDWSVT
IRTMFKWDDE AAAPEEGETE PREVWHIGAG GAVTILSTAE GEREEMFTKL AGPLGVFAEA
//
