ID A0A0W8C6K0_PHYNI Unreviewed; 812 AA.
AC A0A0W8C6K0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=AM587_10008084 {ECO:0000313|EMBL:KUF79693.1};
OS Phytophthora nicotianae (Buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4790 {ECO:0000313|EMBL:KUF79693.1, ECO:0000313|Proteomes:UP000052943};
RN [1] {ECO:0000313|EMBL:KUF79693.1, ECO:0000313|Proteomes:UP000052943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 0 {ECO:0000313|Proteomes:UP000052943};
RA Liu H., Ma X., Yu H., Fang D., Li Y., Wang X., Wang W., Dong Y., Xiao B.;
RT "Genomes and virulence difference between two physiological races of
RT Phytophthora nicotianae.";
RL Submitted (NOV-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:KUF79693.1}.
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DR EMBL; LNFO01004734; KUF79693.1; -; Genomic_DNA.
DR STRING; 4790.A0A0W8C6K0; -.
DR EnsemblProtists; KUF79693; KUF79693; AM587_10008084.
DR OMA; DWSVNIR; -.
DR UniPathway; UPA00077; UER00149.
DR Proteomes; UP000052943; 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; IPR006221; TrpG/PapA_dom.
DR NCBIfam; TIGR00566; trpG_papA; 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:UP000052943};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 30..233
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 293..451
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 513..786
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT ACT_SITE 127
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 217
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 219
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 812 AA; 89682 MW; D00F0F6AD5E5118F CRC64;
MVAFMDDVPA PVSAEQASIT SKKSRRVFSL LIDNYDSYSY NIMQMLAQVN GTPNSVTVIK
NDDFGSQFNV AWDHFVAQAT AIASQEDVEL KLNVVISPGP GHPSEPKDFG MCSDAIRHAT
VPVLGVCLGH QGLAQVYGGQ VVEAEEVMHG RTSRVFIEGE SPLFAHIPNG FDVVRYHSLV
IDPKKIPEEL EVFAKTQDGV IMAVRHRTKQ QFGVQFHPEA VCSEFGYQLF QNFKDVTLAH
CASKCVLHHS NHPEQTAKLH DKSVQKSTDA PDYRVLIQRV STGLASLEFA EFVFSELYGA
SKRSFWLDSS NHDTVAGTDA ATQSRCSMMG DDSGPLSYCV EYDVAKVELR LRRHVNDTEE
VKVYPGQDVL THVREVMQAH XSHEVFSDAV ELPFAFRGGF VGYFGYEVLG SDQEGKKMFN
NKIEVQGERA PDASFLFADR TXVFDHQDGV IYSLSLSECK IESESISQMW HGSIKSQLKE
LSEAYTKRSG ASTSLFSSVS GKDEVIFRPS RSRAQYVADI DEIQRLIRAG ETYEVCLTNH
LRAEYALRDP LAFYRMLRCR NPAPFAGFYL SNPRNRFQTP DAINDTDTHD TYALCCSSPE
RFLRVGADGW MESKPIKGTR PRGRDSNEDS AIAEELANCE KDRAENMMIA DLVRNDFGVV
ARVGSVHVPR LMGVETYATV HQLVTTVRAQ RREDADVVDV LRATFPGGSM TGAPKKRTMH
IIRELERGPR GVYSGGLGFL SIDGSCDLNI IIRTAIVTPN SVTLGAGGAI VALSDSDDEY
DEMLLKARAL VATIGAYATG KDNGGGARVV VD
//
