ID G0S7H8_CHATD Unreviewed; 837 AA.
AC G0S7H8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=CTHT_0028190 {ECO:0000313|EMBL:EGS20980.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS20980.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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 EMBL; GL988041; EGS20980.1; -; Genomic_DNA.
DR RefSeq; XP_006693276.1; XM_006693213.1.
DR AlphaFoldDB; G0S7H8; -.
DR STRING; 759272.G0S7H8; -.
DR GeneID; 18256857; -.
DR KEGG; cthr:CTHT_0028190; -.
DR eggNOG; KOG1224; Eukaryota.
DR HOGENOM; CLU_006493_0_0_1; -.
DR OMA; DWSVNIR; -.
DR OrthoDB; 201921at2759; -.
DR UniPathway; UPA00077; UER00149.
DR Proteomes; UP000008066; 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; 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:UP000008066};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..238
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 327..469
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 532..825
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT REGION 505..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 112
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 223
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 225
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 837 AA; 93289 MW; 804E81DBABB18414 CRC64;
MTSETTNGGN HRPRILFLDA FDSFSNNITS LLTTLLDVEV SVLPIDSPLL IPSPSSTNDD
TVLQNFARLL SHYDALVCGP GPGSPTIPSD VGLMRLVWHL PEKDLLPVLG VCLGFQSLVH
AFGGEVRRLR YGGLHGMIRE VVHSKGDVFT GVGGFRATLY HSLCGDVGQD HEEEGDDWRW
KPLKRCPELV PLAWADEKND SGEERILMAV RHRKKPFWGV QYHPESVCTE KEGNKVIVNW
FRRAMEWNRE RGRVRVESEE RLARAAKRPS LLSQLPTSVN GRRVNGLAQW WELVGIDPVL
HTRTIPLPRG VQVTDIVEVV EPDALERIVL DSANASPTIS RPDVRGRFSI IATCLGEAVR
IEYHTGDDSA IVRTGALRGN TAGGRRERVP LAKFRGIWGF LAAFHERRSI HGDEVAAEES
TPFVGGFMGY ITYEQGLADI NVALDEFRKH HRPDVCLTWV TKSVVVDHTL GLIHIQHLQG
RGDNDTDNWL DGTVEKLLSL ENTRPRSSLK EGYQQKQRPQ PWSTTIQTPR TKEYEEKVRI
CQEYIAAGES YELCLTDQTT ITRPLSDRPL TVSTNPKTIP KQPYSSSSWI LFKHLRARQP
APFASYLRLG AATLVSASPE RFLTYSRSGL CSMRPMKGTV RKCPDTCATL ADAERILHVP
KEMAENLMIV DLVRHDLHGV CGAGRVSVPE LMKVEEYQSV FQMITVVEGQ LDVKRGGYTG
LDVLAASLPP GSMTGAPKKR SCELLKQIEG HLERSLYSGV VGYMCATGRG DWSVTIRSLF
RWEDENVVVK VGEEEVVHEV WRIGAGGAVT ALSTPEGERE EMFTKLAGPL RVFGEAR
//
