ID A0A0E0ADW9_9ORYZ Unreviewed; 842 AA.
AC A0A0E0ADW9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
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 Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM06G27720.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM06G27720.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM06G27720.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A0E0ADW9; -.
DR STRING; 40148.A0A0E0ADW9; -.
DR EnsemblPlants; OGLUM06G27720.1; OGLUM06G27720.1; OGLUM06G27720.
DR Gramene; OGLUM06G27720.1; OGLUM06G27720.1; OGLUM06G27720.
DR eggNOG; KOG1224; Eukaryota.
DR HOGENOM; CLU_006493_0_2_1; -.
DR UniPathway; UPA00077; UER00149.
DR Proteomes; UP000026961; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:EnsemblPlants.
DR GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; IEA:UniProtKB-EC.
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: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; 2.
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 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; 2.
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|PROSITE-ProRule:PRU00605};
KW Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 47..217
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 260..293
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 380..522
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 594..665
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT DOMAIN 666..813
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 131
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 277
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 279
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 842 AA; 93175 MW; 0F55786B73C7F06F CRC64;
MAALRLPTPP PPRAPAPWLH SSHRRRVAAP RGAGGGGAAP PPPVRTLLID NYDSYTYNIF
QELSVVNGVP PVVVRNDEWT WRDVYRWVYK ERAFDNIVIS PGPGSPACPS DIGICLRILC
ECGDIPILGV CLGHQALGFV HGAKIVHAPE AIHGRLSELE HSGCYLFNHI PSGINSGFKV
VRYHSLVIEP DSLSEDLISI AWTASPKMLS FLESDKPDIT SSTLWGSLDN LFVTNQSECS
TTGGKMPSIN DASELDGYRV LMGVRHSARP HYGVQFHPES VATHYGRQIF QNFKKITTDF
GLQTPLLQER KISSPDLKNF VANDLLHSAR LKLWDSVGPC ALPKRSSGDK CLRLQWKKID
NFLNRIGGSE NIFSVLFGHH SAEDTFWLDS SSVDQNRARF SFMGGKGGPL WKQMTFHLAS
QRANCGGNLT IRDAHGCTVR NFLKDGFLDF LDKEMQSIQY NEKDYEGLPF DFHGGFVGYI
GYGLKVECDA SSNSAKSSTP DACFFFADNL VVVDHNNGDV YILSLHDEYS SGNGDGDYQN
SIHSLWLANT EKKLLRMDAM APRLSINGNS SINGNSFTIS SSVNKQRFVI EKSKDEYIRD
VQSCLDYIRD GESYELCLTT QMKRRTDYMD ALKLYLKLRK QNPAPYAAWL NFSSENLSIC
CSSPESEKDQ AENLMIVDLL RNDLGKVCEP GSVHVPRLMD VESYKTVHTM VSTIRGTKMS
DLSPVDCVKA AFPGGSMTGA PKVRSMEILD SLETSPRGIY SGSVGFFSYN KTFDLNIVIR
TVVLHNGEAS IGAGGAIVAL SDPEAEYNEM LLKAKAPTKV VEECSQQIYN PDRSDSMQTT
VS
//
