ID A0A0F4YX84_TALEM Unreviewed; 978 AA.
AC A0A0F4YX84;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=T310_3752 {ECO:0000313|EMBL:KKA22223.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA22223.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA22223.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA22223.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) 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:KKA22223.1}.
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DR EMBL; LASV01000150; KKA22223.1; -; Genomic_DNA.
DR RefSeq; XP_013328835.1; XM_013473381.1.
DR AlphaFoldDB; A0A0F4YX84; -.
DR STRING; 1408163.A0A0F4YX84; -.
DR GeneID; 25316101; -.
DR OrthoDB; 201921at2759; -.
DR UniPathway; UPA00077; UER00149.
DR Proteomes; UP000053958; 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; 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:UP000053958};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 160..356
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 450..585
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 657..935
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT ACT_SITE 243
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 350
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 352
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 978 AA; 108837 MW; 6FB387B5A86E6DD6 CRC64;
MVAKGVAGED IQFLVQVLHP DPNDRLNVRE ILETSRKDDY SNKEGGNKNR ISSLKPSHSL
VRVRVPPVPT PESRQAAALL GPAGGVLGSH QQGQITSNYY CLFFSGFLLV DRYTLHRLSF
YVTSTLLSYL SPMQIPTIEN GTSGRPAASM NGTSSGRILY VDAYDSFSYN VISMLEENLN
VKVTVITVDS EWPNGGMLQF LRLFDAVVLG PGPGNPESAP DVGIMRDLWT LDGAELVPVL
GICLGFQSLC LHHGVPIQRL PCPLHGQVRR ISTVDEDIFE GMQDFEVTLY HSLYAAVDSV
SNGVGCEPAG ISHSLELSFL AWLSISEPDS KTIPMAVRHR KKPFWGFQFH PESCKSDATS
CTSLLKRWWE EATAFNKRSG RLIYANKPGM VDTCSLIPTV DPEIRQLLEE LTAASSEKCT
FRSLPLHDLS AEKIFEMTNT PGSPSVLFQS NGRFNVISIL SPNSWRLEYY VPNKTLLLEG
LGDLAQKSVQ TVLEVDEFWN TLRHVMSKKR VRSGHDEVPF WGGFLGYFSY EMGLAGLAHP
KTSPVLGNYN SPTPQPAEAV DPPDVSLLWV ERSIVVDNES RTVYIQSTRE LDDQPDGWLA
LTHRRLQDFS CDHSLRVKSS KTDSKCPEVD RHSLLEAAET ELIGRVLDGA TVDIPDEESY
KSQVATCKSQ LEAGESYELC LTGETSITLP ALPDENLRNL RPWLLYKKLK TYNPAAFSAY
ARLGNVKIAS SSPECFLNWD RQSMLEMKPM KGTVRKSADM TLEKAKEILG TTKEMAENLM
IADLVRHDLY GICGSGNVHV EKLLEVEDHG RVYQMITHVK GIVKDHQPAE EPTNMSFYGI
TALQRCLPPG SMTGAPKERS CMHLSLIEQR KRGIYSGVMG YLDLGGAGSF SVVIRTAFSC
SDDQPGKDEL WRVGAGGAIT ILSTAEGEWD EMMTKLRTVI QFYVYMHMHL KIQHSTFPWH
GVEWRGAAFN MQFVSWGK
//
