ID I1GWM7_BRADI Unreviewed; 904 AA.
AC I1GWM7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 58.
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 Name=100842215 {ECO:0000313|EnsemblPlants:KQK17375};
GN ORFNames=BRADI_1g34070v3 {ECO:0000313|EMBL:KQK17375.1};
OS Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX NCBI_TaxID=15368 {ECO:0000313|EnsemblPlants:KQK17375};
RN [1] {ECO:0000313|EMBL:KQK17375.1, ECO:0000313|EnsemblPlants:KQK17375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK17375.1,
RC ECO:0000313|EnsemblPlants:KQK17375};
RX PubMed=20148030; DOI=10.1038/nature08747;
RG International Brachypodium Initiative;
RT "Genome sequencing and analysis of the model grass Brachypodium
RT distachyon.";
RL Nature 463:763-768(2010).
RN [2] {ECO:0000313|EMBL:KQK17375.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bd21 {ECO:0000313|EMBL:KQK17375.1};
RG The International Brachypodium Initiative;
RA Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT "WGS assembly of Brachypodium distachyon.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:KQK17375}
RP IDENTIFICATION.
RC STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK17375};
RG EnsemblPlants;
RL Submitted (AUG-2018) 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 EMBL; CM000880; KQK17375.1; -; Genomic_DNA.
DR RefSeq; XP_010227413.1; XM_010229111.2.
DR AlphaFoldDB; I1GWM7; -.
DR STRING; 15368.I1GWM7; -.
DR EnsemblPlants; KQK17375; KQK17375; BRADI_1g34070v3.
DR GeneID; 100842215; -.
DR Gramene; KQK17375; KQK17375; BRADI_1g34070v3.
DR eggNOG; KOG1224; Eukaryota.
DR HOGENOM; CLU_006493_0_2_1; -.
DR InParanoid; I1GWM7; -.
DR OMA; DWSVNIR; -.
DR OrthoDB; 201921at2759; -.
DR UniPathway; UPA00077; UER00149.
DR Proteomes; UP000008810; Chromosome 1.
DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; IBA:GO_Central.
DR GO; GO:0046417; P:chorismate metabolic process; IEA:EnsemblPlants.
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:0008153; P:para-aminobenzoic acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
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; PR00097; ANTSNTHASEII.
DR PRINTS; PR00099; CPSGATASE.
DR PRINTS; PR00096; GATASE.
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:UP000008810};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 66..224
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 269..310
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 409..550
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 618..875
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 150
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 294
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 296
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 904 AA; 100210 MW; 9BAA0E867B128D47 CRC64;
MAALRLPAPP TAARWPQPPP SPAGSASARL LQPPGQGSSC PRRLAARWAK GRRGDDGAEA
PPVRTLLIDN YDSYTYNIFQ ELSVVNGVPP VVVRNNEWAW KDVYNWVYKE RAFDNIVISP
GPGSPACPSD IGVCLRILCE CGDIPILGVC LGHQALGLVH GAKIVHAPEA IHGRLSEIEH
NGCYLFNRIP SGINSGFKVV RYHSLVIEAS SLPEDLVSIA WTASPKMLSF LDSDQPDNTP
FWGSLNNLPL IGPSECTNNG ELPITLNNAS KSDSYKIVMG IKHSSRPHYG VQFHPESVAT
HYGRQIFQNF KRITTEFGLQ SSLFQERKVH RIGKLERSQV NSLNQCDFVP KGLLHTERVD
LCNSVGSLKL PERSNENKYL RLRWKRIDNF LSHTGGSEDI FSVLFGHQNA EDTFWLDSSS
IDQNRARFSF MGGKGGPLWK QMTFSLSSQG ANCGGTITTR GAHGSAVRNS LKDGFLEFLN
KEIQSIQYNE KDFEGLPFDF HGGFVGYLGY GLKVECDASS NKAKSRTPDA CFFFADNLVV
VDHNNGDVYI LSLHDEYSSS HGNGDGNYSN TTHASWLVET EKKLLRMVPM APVPLINGKP
LIRSSNLKTQ SFVVEKSKDQ YVKDVRSCLD YIKDGESYEL CLTTRMRREI EYINALQLYL
KLRKKNPAPY AAWLNFSSES LSICCSSPER FLRLDRNAIL EAKPIKGTIA RGRTPEEDDC
LRLQLKYSEK DQAENLMIVD LLRNDLGKVC EPGSVHVPHL MDVESYKSVH TMVSTIRGTK
KPNLSPVDCV KAAFPGGSMT GAPKVRSMEI LDSLESSPRG IYSGSIGFFS YNRTFDLNIV
IRTIVLHGRE ASVGAGGAIV ALSDPEAEYE EMMLKARMPT KVVEECSLTA HNPDRSDSMQ
TTVS
//