ID A0A2K3QGF3_9HYPO Unreviewed; 882 AA.
AC A0A2K3QGF3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=TCAP_03477 {ECO:0000313|EMBL:PNY26593.1};
OS Tolypocladium capitatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX NCBI_TaxID=45235 {ECO:0000313|EMBL:PNY26593.1, ECO:0000313|Proteomes:UP000236621};
RN [1] {ECO:0000313|EMBL:PNY26593.1, ECO:0000313|Proteomes:UP000236621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 113982 {ECO:0000313|EMBL:PNY26593.1,
RC ECO:0000313|Proteomes:UP000236621};
RA Quandt C.A., Patterson W., Spatafora J.W.;
RT "Harnessing the power of phylogenomics to disentangle the directionality
RT and signatures of interkingdom host jumping in the parasitic fungal genus
RT Tolypocladium.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PNY26593.1}.
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DR EMBL; NRSZ01000529; PNY26593.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K3QGF3; -.
DR STRING; 45235.A0A2K3QGF3; -.
DR OrthoDB; 201921at2759; -.
DR UniPathway; UPA00077; UER00149.
DR Proteomes; UP000236621; 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 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:UP000236621};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 24..255
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 332..487
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 620..870
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT ACT_SITE 118
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 237
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 239
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 882 AA; 96872 MW; D58A4BBDDC479EB6 CRC64;
MGDCLGLGAG SPDTQRPRPR RILFLDAYDS FTNNIVSLLK DALGDHVMVH VLHMDLRTLD
ADPRPAWTRR EFLDRLAGFD AVVCGPGPGS PLRDADVGAF KLLWDLPRAR AVPVLGICLG
FQSLVAHFGG RIRRLRRGLH GMVRDIDHVR GPLADVFDGV PRFRATLYHS LCADVGQDAI
PEEQWREARW EPPAGAPDLV PLAWALEKAD ADDAQGDERI LMAVRHASRP LWGVQYHPES
VCTEPAAHGV IRNWFRQALK WNEATRREVD RSVEYADSLD PSNHALPALS ADRDLTTCRW
WQDMQSGLAW TGVAPGYACR QIKLPDGVDT AEVAEVLGLG AADSIILDSS STVNGDPLAR
NSILALDVHE ALRAEFRVGD DHVTLRRPAT PGRDEECQRI ALGDAEHDPW TPWHVISEFW
RWRQTPDDGQ PSPTFKGGFM GFVTYEMGLS TLSPGLVSGD RGHRRPDICM AWVSKSVVLD
HQAGVAYVQA LAAGESDGAW IDHVVEKLEG SYAWRHPGCG CAGKARGKQA NEALLEHVRN
EGGRLGFSIP DPDRYEEDVG RCQDAIRDGE SYELCLTAQT TMTRPSGNDL PHHMRPHLNG
RLARLSDHCP EVTTPLEEAS SHGTPWQLYR TLRARQPAPF GSFIRLGGAT IISSSPERFL
THDPQGLCLM RPMKGTVRKS DAVSTLAEAE RILHVPKEEA ENLMIVDLVR HDLHGVCGTG
SVTVPDLLRV EEYAGVFQMI TVVNGQLPAA KLRSGTRPCH TEFPFTGMDV LASALPPGSM
TGAPKKRSCE ILGAIEPTER SVYAGVVGYL DAQGRGDWSV TIRTMFRWDD ETAPAHDGEV
QPREVWRVGA GGAVTTLSTP EGEREEMFTK LCGPLGVLKD VA
//
