ID A0A423WGX9_9PEZI Unreviewed; 852 AA.
AC A0A423WGX9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=VSDG_01813 {ECO:0000313|EMBL:ROW02629.1};
OS Valsa sordida.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=252740 {ECO:0000313|EMBL:ROW02629.1, ECO:0000313|Proteomes:UP000284375};
RN [1] {ECO:0000313|EMBL:ROW02629.1, ECO:0000313|Proteomes:UP000284375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YSFL {ECO:0000313|EMBL:ROW02629.1,
RC ECO:0000313|Proteomes:UP000284375};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:ROW02629.1}.
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DR EMBL; LJZO01000004; ROW02629.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423WGX9; -.
DR STRING; 252740.A0A423WGX9; -.
DR UniPathway; UPA00077; UER00149.
DR Proteomes; UP000284375; 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; PR00097; ANTSNTHASEII.
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:UP000284375};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 25..244
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 330..480
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 531..842
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT REGION 262..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 108
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 227
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 229
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 852 AA; 94900 MW; C495548EB82DFA33 CRC64;
MGSVGEALPT SSPEPSSSGR PKVLFIDAYD SFSNNITSLL TTLLGVDVFV LPIDAAIPKA
DFRRELSHYE AVVCGPGPGS PDIESDVGLM RWLWELEGDD LLPVMGVCLG FQSLVLACGG
KVRRLRRGLH GMVRKIEHRP SYDALLPDNL FEGVEEFQAT LYHSLCANVG QDAVDDWERM
KWMSPPALPD IVPQAWVEED RGDGQGRERI LMAVQHRRKP FWGLQYHPES VCTEEEGDRV
IQNWFRLARQ WNDARGRITN KRTQDMLAKN ATRPSLLQQA SDDDHETPGG ENNWEKLVSP
ENIRLHYQSQ VVELPPNGVE VPDVVEILGL TDTEHVILDS ANANQPAPPT GVDVRGRFSI
VALGVSTCLR FQYHTGDDVV TIVGAANGPP LTRVPLRTGQ TVWHVLAEFQ ESRRLSLGNP
VTDENEVPFL GGFVGFVTYE QGLSDIGLKL PQHRGHERPD VCLAWVTRSI VVDHQDGLMY
VQDLEGDLQW LETVTVQLKT SLWQKERMSK RGRNGVSSSL EMQPVIQTPD QAKYEAKVRL
CQEYIAAGDS YELCLTDQTK ITRTVTSNDD GDQQTRLPKR RRTSTAAKVP SRNNTSWELY
RTLRTRNPAP FASYVRLGGA TLVSSSPERF LQYNRSGLCS MQPMKGTVKK SAEPGEGCAT
TLAEAEAILH VPKEEAENLM IVDLVRHDLH GICGPGRVTV PALLKVEEYQ TVYQMITTVE
GQLPQAEDWS DRTRYSGLDV LSASLPPGSM TGAPKKRSCE ILQQIENGKE RSLYSGVVGY
MCISGRGDWS VTIRSMFRWD DECRQDDEEE GTKEKEVWHI GAGGAVTILS TPEGEREEMF
VKLARPLSIF TG
//
