ID A0A0A2JHC5_PENEN Unreviewed; 805 AA.
AC A0A0A2JHC5;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=PEX2_026360 {ECO:0000313|EMBL:KGO54098.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO54098.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO54098.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO54098.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
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:KGO54098.1}.
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DR EMBL; JQFZ01000238; KGO54098.1; -; Genomic_DNA.
DR RefSeq; XP_016596605.1; XM_016739911.1.
DR AlphaFoldDB; A0A0A2JHC5; -.
DR STRING; 27334.A0A0A2JHC5; -.
DR GeneID; 27675330; -.
DR HOGENOM; CLU_006493_0_0_1; -.
DR OrthoDB; 201921at2759; -.
DR UniPathway; UPA00077; UER00149.
DR Proteomes; UP000030143; 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|ARBA:ARBA00022962,
KW ECO:0000256|PROSITE-ProRule:PRU00605};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KGO54098.1}.
FT DOMAIN 31..216
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 308..443
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 495..784
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT REGION 399..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 114
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 209
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 211
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 805 AA; 89253 MW; 5FBF4C601E2BC1B0 CRC64;
MAPMLGDWDA SNIETTVPQL DPSSSTKSVL YVDAYDSFSY NVVAMLEETL GVKVTVMTID
SEWPDSNMNE FLQHYEAVVL GPGPGDPNVP TDVGIMRDIW NLHESELLPV FGICLGFQSL
CLHHGVPIER LPYPIHGQIH KISTSAKDIF EHLPEVEVTL YHSLYANSAA STSPDLEYLA
WLSLKDRPKV QIPMAVRHLK KPFWGVQFHP ESCKSEINAC KALLRNWWRM ALGYNKIVGR
GGYCSLPSTV ISPLTAPSPF PDAAYEMLNW SKTTSKFSAS RSLHRPDLTA EAISEIFNKP
GSPAVLFQSN GQYSIASVLS PSSWRFEYNV ETHKLRLLQL YGDCKEVESY LTVAQLWDAL
RYLMEMKKVD SGNSQVPFWG GFLGYLSYEL GLTCLPHPGH AQASESPKPS STGESPSNSS
FADPPDVSLL WCERSIVVDN TTGAIVIQST RDNDAGWLDE TLQQLQIFSD SGNDTSADQG
LDSILGESKI QFPEEKEYKR QIESCKAELE AGESYELCLT SETSITLPVP EAESDRVIFP
WKLYRRLKTY NPAAFSAFAD LGDTKIASSS PECFLNWDRE STLEMKPMKG TVRKSPGMTM
EKACEILGST KEMAENLMIA DLIRHDLYGI CGSGGVHVEK LLEVADYGRV YSMITHIKGK
IRPNHPGFAV RHMPQLNTPN MSVHGLTTLQ RCLPPGSMTG APKERSCMHL RTIENRKRSI
YSGVMGFLDL GGGGSFSVLI RSAFTCYGGR DYTENKQQTW RIGAGGAITT LSTAEGEWDE
MLTKLRVVCN VFTPLNAIEK SATTS
//