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Database: UniProt
Entry: A0A453SP50_AEGTS
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Original site: A0A453SP50_AEGTS 
ID   A0A453SP50_AEGTS        Unreviewed;       808 AA.
AC   A0A453SP50;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
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};
OS   Aegilops tauschii subsp. strangulata (Goatgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX   NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET7Gv21020100.8, ECO:0000313|Proteomes:UP000015105};
RN   [1] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=25035499; DOI=10.1126/science.1250092;
RG   International Wheat Genome Sequencing Consortium,;
RA   Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA   Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT   "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL   Science 345:1250092-1250092(2014).
RN   [2] {ECO:0000313|Proteomes:UP000015105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX   PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA   Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA   Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT   "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL   Nat. Plants 3:946-955(2017).
RN   [3] {ECO:0000313|EnsemblPlants:AET7Gv21020100.8}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2019) to UniProtKB.
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}.
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DR   AlphaFoldDB; A0A453SP50; -.
DR   EnsemblPlants; AET7Gv21020100.8; AET7Gv21020100.8; AET7Gv21020100.
DR   Gramene; AET7Gv21020100.8; AET7Gv21020100.8; AET7Gv21020100.
DR   UniPathway; UPA00077; UER00149.
DR   Proteomes; UP000015105; Chromosome 7D.
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; IPR005802; ADC_synth_comp_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; TIGR00553; pabB; 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; 2.
DR   PRINTS; PR00095; ANTSNTHASEI.
DR   PRINTS; PR00099; CPSGATASE.
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|ARBA:ARBA00022962,
KW   ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015105};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          6..138
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   DOMAIN          187..224
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   DOMAIN          313..453
FT                   /note="Anthranilate synthase component I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04715"
FT   DOMAIN          519..776
FT                   /note="Chorismate-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00425"
FT   REGION          786..808
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        64
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        208
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        210
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   808 AA;  89715 MW;  49C3E65757158AAD CRC64;
     AVPPVVVRND EWAWRDVYNW VYKKRAFDNI VISPGPGSPS CPTDIGVCLR ILCECGDIPI
     LGVCLGHQAL GLVHGAKIVH APEAIHGRLS EIEHNGCYLF NHIPSGINSG FKVVRYHSLV
     IEASSLPEDL VSIAWTASPK MLSFLDSDQP DNTPFWGSLN NLSITDPSER INNGEVPITI
     NNTSKPDGHK IVMGIKHSSM PHYGVQFHPE SVATHYGRQI FQNFKRITTD FGSQSSLFQE
     RKVNSADQCN YVLKGLSHTE GLELGDSVGV HMLAERNIKK KYLRLRWKRI DNFLSRTNGS
     EDIFSELFGH QNAEDTFWLD SSSVDQNRAR FSFMGGKGGP LWKQMTFHLS NQRANCGGTI
     TIRGAHGSAV KNSLKDGFLE FLHKEIQSIK YNEEDFEGLP FDFHGGFVGY LGYGLKVECD
     ASSNKAKSST PDACFFFADN LVAIDHNSGD VYILSLYDEY SLSNGNGMHH NTTHTSWLLE
     TEKRLLRMAA MSPGLPINGK SLIGSSNVNK QSFVVEKSKD QYIKDVRSCL DYIRDGESYE
     LCLTTRMRRG IEYINALQLY LQLRKQNPAP YAAWLNFSSE NLSICCSSPE RFLRLDQNAV
     LEAKPIKGTI ARGRTPEEDE CLRLQLKYSE KDQAENLMIV DLLRNDLGKV CEPGSVHVPR
     LMDVESYKSV HTMVSTIRGT KKPDLSPVDC IKAAFPGGSM TGAPKVRSME ILDALESSPR
     GIYSGSIGFF SYNRTFDLNI VIRTVVLHDG EASVGAGGAI VALSDPEAEY AEMMLKARTP
     TRVVEECSQQ AAAHSSPDRS DSVRTTIS
//
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