ID A0A1Y2G946_9FUNG Unreviewed; 1049 AA.
AC A0A1Y2G946;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=p-aminobenzoic acid synthase {ECO:0000256|ARBA:ARBA00031904};
DE AltName: Full=Para-aminobenzoate synthase {ECO:0000256|ARBA:ARBA00031329};
GN ORFNames=BCR41DRAFT_328170 {ECO:0000313|EMBL:ORZ04542.1};
OS Lobosporangium transversale.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Lobosporangium.
OX NCBI_TaxID=64571 {ECO:0000313|EMBL:ORZ04542.1, ECO:0000313|Proteomes:UP000193648};
RN [1] {ECO:0000313|EMBL:ORZ04542.1, ECO:0000313|Proteomes:UP000193648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 3116 {ECO:0000313|EMBL:ORZ04542.1,
RC ECO:0000313|Proteomes:UP000193648};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) 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:ORZ04542.1}.
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DR EMBL; MCFF01000056; ORZ04542.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2G946; -.
DR STRING; 64571.A0A1Y2G946; -.
DR InParanoid; A0A1Y2G946; -.
DR OrthoDB; 201921at2759; -.
DR UniPathway; UPA00077; UER00149.
DR Proteomes; UP000193648; 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; IPR015890; Chorismate_C.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR006221; TrpG/PapA_dom.
DR PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR PANTHER; PTHR11236:SF18; AMINODEOXYCHORISMATE SYNTHASE; 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; 2.
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:UP000193648}.
FT DOMAIN 47..198
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 219..267
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 839..1033
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT ACT_SITE 128
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"
SQ SEQUENCE 1049 AA; 117703 MW; CCBF1D62258F7272 CRC64;
MPNPVNSGLP GILSSIDILA TLPTGLHIDS AIELTKSLSP GSILRTLIVD NYDSYTFNLL
QLFDQEHLQQ VVVIRNDQFT WPEFKQQILP FFDQIILSPG PGRPERPHDF GICAQILEKS
RIPVFGICLG HQGIGWIHGA KITYSPEPVH GQIAHIQHNG AGIFHGIPQD FKVVRYHSLV
IQEQDLPDDL IITAWCYSTP LIADDTTIRK DNTFRNNSKD RAISCNTWGE KSIMGVKHRY
LPHYGVQFHP ESICTQYGQK MMNNFFMLTH EFYREHKRNS IAGCIPDHVR AHSVIATKSP
AVIPQPMLTS SSLKDNPPSQ YSLFIHMLDP TIFPAPEIVF SSLFLTGPRS KAAAWWLDSA
RQPHPMSRFS FMGGIETRRC CSQSSNGYLN TPSAAQAVIQ YSTLHREICI RHYKRQSNAS
SIKRVYLNQN RRSAHGAAET FWDWVSQLMA GFSKDDIETI LTGPNGEQRD FEEAPFDFFT
GMVGYFGYEM KRESLDGYQT PLEQQCQCDG HSGRSECFCT CNCLRQPDAS FILATQAVVF
DHVDKRVYVL GVVNNQPEKL QKNLEAPIGF LDRQACDTWI KEVTRSITHV ATIHTKAGSS
ATGATFLPSA AKSDKPYRQR RRSSVSLLSP FKVDVSEENY LKAIRDSLDY IHEGESYELC
LTTQFRAKIP LHKQYQEDHL VNSDEQQGDP AYDLYKILRK LNPAPFSAFL SLPIAMDEGV
ALKSQYLNGH SSVPEKNEIV RRLVILSSSP ERFLKIGRIS DDKLTTQDDK NASCSLRTVE
MKPIKGTVAV AKGCFCEENE GCNISQSTDG EHFEDIELSY QGDKTYASHR STYDRCTEAR
KRENQRRIDT LSNNVKERAE NLMIVDLIRN DLAHVCSSYS VRVPYLMKVE SYETVHQLVT
TVRGELFDHI DSTQTVRACF PPGSMTGAPK LRSVQLLDSL EHHVKRGVYS GCLGYIGIPA
RAASSAGANT KSHKKARSST DFAVVIRTAV LSVEPNVDND GKMILSGDLS VGAGGALTIL
SDAQEEWKEV LLKSRSVVPS VLTYLHQKY
//
