ID U1FWT0_ENDPU Unreviewed; 840 AA.
AC U1FWT0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=EPUS_04022 {ECO:0000313|EMBL:ERF69317.1};
OS Endocarpon pusillum (strain Z07020 / HMAS-L-300199) (Lichen-forming
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Verrucariales; Verrucariaceae; Endocarpon.
OX NCBI_TaxID=1263415 {ECO:0000313|EMBL:ERF69317.1, ECO:0000313|Proteomes:UP000019373};
RN [1] {ECO:0000313|Proteomes:UP000019373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z07020 / HMAS-L-300199 {ECO:0000313|Proteomes:UP000019373};
RX PubMed=24438332; DOI=10.1186/1471-2164-15-34;
RA Wang Y.-Y., Liu B., Zhang X.-Y., Zhou Q.-M., Zhang T., Li H., Yu Y.-F.,
RA Zhang X.-L., Hao X.-Y., Wang M., Wang L., Wei J.-C.;
RT "Genome characteristics reveal the impact of lichenization on lichen-
RT forming fungus Endocarpon pusillum Hedwig (Verrucariales, Ascomycota).";
RL BMC Genomics 15:34-34(2014).
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; KE721457; ERF69317.1; -; Genomic_DNA.
DR RefSeq; XP_007805075.1; XM_007806884.1.
DR AlphaFoldDB; U1FWT0; -.
DR GeneID; 19239056; -.
DR eggNOG; KOG1224; Eukaryota.
DR HOGENOM; CLU_006493_0_0_1; -.
DR OMA; QYHSLHA; -.
DR OrthoDB; 201921at2759; -.
DR UniPathway; UPA00077; UER00149.
DR Proteomes; UP000019373; 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; IPR010117; PabB_fungal.
DR InterPro; IPR006221; TrpG/PapA_dom.
DR NCBIfam; TIGR01823; PabB-fungal; 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; 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:UP000019373};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 40..187
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 363..501
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 551..828
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT REGION 192..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 263
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 265
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 840 AA; 93354 MW; 06056739E9C3AF28 CRC64;
MSVVSKKTQF LDSISFVGGF YTDSAYLQMA PNSNHGRILF IDAYDSFSEN IAALFCQILP
VEVTMIHIDT QIEELLDKPA DCTQNALALY LQNFDAVVLG PGPGNPEATS DVGLFSEIWR
LPSLDVVPVL GICLGFQSLC LAYGASIRRM LEPCHGHAKG IKHCDEDIFT NVGEVIATNY
NSLEVELGDK HSLAEDSGPT SSSPSVESGS SSPSTLCTEF YPSQPEFEPS LTCPKLRPLA
WDGFGTSMSV KHVELPFWGL QFHPESCKSN AACQSIIKNW WNTSMHWSTR TRRATNLSRS
KLLSGHVWSR PLTPIHIIAE PCDIAENHRL TSTLQEELQA LTASSAATVE FHTMMLPKSA
GQVLELCRSL SQNDQAILES TRKGRFSIYA VPGPSEFRME YNLETSTCTL NLTDQDKMQW
KMKLLHVLDE IQGLVVRRRV KAGHDSVPFF GGFIGYFSYE VGLERLGVKQ ELRSASEVLP
DINLLWVERS IVIDHVSNEA HIQSIRKDDS TWIAEMVDKL NRLGCPESPI ALRSARLQAL
LTAAKIRLPD EEIYKREIQA CQDYLHSGDS YELCLTTGAQ ISLPTHPENS WLLYHNLRHH
NPVPFSAFLR LGRTTILSSS PEQFLSWDRS SGSINMIPMK GTVAKSPSMN LALAKEILAS
PKESAENLMI ADLIRHDLYS TVGWNASVEV IKLCEVVEHE TVYQLVSHIR AMPSIPPTLS
ADERQQEIMR YGHKALRQTL PPGSMTGAPK KRSCEILRRL EQRRRGVYSG VLGYLDVGGG
GAFSVCIRTA VSNADEDRDG RQTWRVGAGG AITVLSDVDA EWEEMKTKLE SVLRAFRPDG
//
