ID A0A022RLJ8_ERYGU Unreviewed; 839 AA.
AC A0A022RLJ8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
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};
DE Flags: Fragment;
GN ORFNames=MIMGU_mgv1a022054mg {ECO:0000313|EMBL:EYU39820.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU39820.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU39820.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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; KI630443; EYU39820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A022RLJ8; -.
DR STRING; 4155.A0A022RLJ8; -.
DR eggNOG; KOG1224; Eukaryota.
DR UniPathway; UPA00077; UER00149.
DR Proteomes; UP000030748; Unassembled WGS sequence.
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: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 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; 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:UP000030748};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 35..196
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 228..266
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 373..517
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 566..824
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT ACT_SITE 119
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 249
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 251
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EYU39820.1"
SQ SEQUENCE 839 AA; 94082 MW; 50F681076B0B63F6 CRC64;
ACVPSRSVSG HLEGSYVGKK QLIEPSSKLG FIRTLLIDNY DSYTYNIYQE LSVVNGLPPV
VIRNDEWSWE DICHYLYEEK AFDNIVISPG PGSPTCAADI GICLRLLHEC RDIPILGVCL
GHQALGYVHG AQIIHAPEPI HGRLSDIEHN GCGLFHGVPS GRNSEFKVVR YHSLVIDPSS
LPRQLIPIAW TSSSETNSFL GIENLDDFDR RATNPENGLK SSNSQEMQSG SILMGIMHSS
RPHYGLQFHP ESVATFHGRQ IFKNFAKITK DYWLTRTSSS NKVHYSVALS SDLYLACMQV
PNVTRLFQDV ARSNKHSVNG LYRKKHATLS NLVNSSYSRN SKLLKLKWRK IERSISQVGG
AENIFRELFG DNRAENTFWL DSSSTEMNRA RFSFMGGKGG PLWKQVTYKL AEKSDSKLNH
GGNLSIEDAE GSVTSTYLEN GFFDLLNQEL QSFGYNAADY EGLPFDFYGG YIGYIGYDLK
VECGAQSNRH KSTAPDACFF FTDNLVVLDH HTDDIYITSL YENTSTNPWL DEIEHKLLNL
KIPPLKTKSV SSKKIPREGF VAEKSRENYI KDIEKCQKFI KDGESYELCL TTQMTRNVGK
KINSLDLYLN LREKNPAPYA AWLNFPKQNL SICCSSPERF LRLDRNGILE AKPIKGTIAR
GISPEEDDLR KQQLQYSEKD QAENLMIVDL LRNDLGLVCE AGSVHVPHLM EIESYATVHT
MVSTIRGEKR SDVTAVDCVR AAFPGGSMTG APKLRSMEIL DTLETRSRGI YSGCIGYFSY
NQTFDLNIVI RTIVINGEDA SIGAGGAITA LSKPEEEYEE MLLKTRAPTK AVVEFQEDN
//
