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Database: UniProt
Entry: A0A0A2JHC5_PENEN
LinkDB: A0A0A2JHC5_PENEN
Original site: A0A0A2JHC5_PENEN 
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
//
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