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Database: UniProt
Entry: C9ZEF6_STRSW
LinkDB: C9ZEF6_STRSW
Original site: C9ZEF6_STRSW 
ID   C9ZEF6_STRSW            Unreviewed;       727 AA.
AC   C9ZEF6;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   RecName: Full=aminodeoxychorismate synthase {ECO:0000256|ARBA:ARBA00013139};
DE            EC=2.6.1.85 {ECO:0000256|ARBA:ARBA00013139};
GN   OrderedLocusNames=SCAB_1971 {ECO:0000313|EMBL:CBG67415.1};
OS   Streptomyces scabiei (strain 87.22).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG67415.1, ECO:0000313|Proteomes:UP000001444};
RN   [1] {ECO:0000313|EMBL:CBG67415.1, ECO:0000313|Proteomes:UP000001444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=87.22 {ECO:0000313|EMBL:CBG67415.1,
RC   ECO:0000313|Proteomes:UP000001444};
RX   PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA   Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA   Loria R.;
RT   "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT   cluster that contributes to plant-microbe interactions.";
RL   Mol. Plant Microbe Interact. 23:161-175(2010).
CC   -!- SIMILARITY: In the C-terminal section; belongs to the anthranilate
CC       synthase component I family. {ECO:0000256|ARBA:ARBA00005970}.
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DR   EMBL; FN554889; CBG67415.1; -; Genomic_DNA.
DR   RefSeq; WP_012998152.1; NC_013929.1.
DR   AlphaFoldDB; C9ZEF6; -.
DR   STRING; 680198.SCAB_1971; -.
DR   MEROPS; C26.A25; -.
DR   GeneID; 24312133; -.
DR   KEGG; scb:SCAB_1971; -.
DR   eggNOG; COG0147; Bacteria.
DR   eggNOG; COG0512; Bacteria.
DR   HOGENOM; CLU_006493_0_2_11; -.
DR   OMA; DWSVNIR; -.
DR   Proteomes; UP000001444; Chromosome.
DR   GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
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; IPR005802; ADC_synth_comp_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; IPR006221; TrpG/PapA_dom.
DR   NCBIfam; TIGR00553; pabB; 1.
DR   NCBIfam; TIGR00566; trpG_papA; 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   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001444};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          4..186
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   DOMAIN          246..383
FT                   /note="Anthranilate synthase component I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04715"
FT   DOMAIN          438..692
FT                   /note="Chorismate-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00425"
FT   REGION          195..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          705..727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        170
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        172
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   727 AA;  79386 MW;  922FBCC1A80B52A7 CRC64;
     MRTLLVDNYD SYTYNLFQLI AQVNGAEPVV VHNDSPDCAT LDLNDFDNVV ISPGPGDPTR
     PKDFGACAPI IESARLPLLG VCLGHQGIAA GSGARIERAP AARHGHLTAV RHDGRELFHG
     LPQDFTAVRY HSLCVREPLP PELEPTAWAE DGVLMGLRHR TRPLWGVQFH PESVATEFGY
     ELLGNFRDLT ERFHHERGRA RRRTPARSAS HLVPVKTGTR PTPRNVEPRP YRLHTRIMES
     AVDTEAAFTR LFADSSHAFW LDSSLIDPRL SRFSFLGDAS GPLSEIVRYR VGDGAVEVTA
     AGGQPQRVEG TVFDYLQTAL RARRVENPAL PVDFSCGYVG YFGYELKADC GATTTHTSPT
     PDAFWIFSDR LIAVDHQQGA TYLLALSDGS PRSDRDATVW MERTAAGLAA LPRPRPTPVP
     DQQAVDNALL EPSLVRDRAQ YLADIATCKQ ELLAGESYEI CLTNAVQAPR PADGLRFYRN
     LRRSNPAPYA AYLRLDGMEI ACSSPERFLR ITRDGMVETK PIKGTARRGA DEAEDARLRR
     ELTTSPKVRA ENLMIVDLLR NDLGRVCEVG SVTVPRLMRT ETYATVHQLV STIRGRLRAD
     ADALDCVRAC FPGGSMTGAP KLRTLDIIDS LETRARGVYS GAIGFLSCNG TADLNIVIRT
     AVLTKEGLHA GAGGAIVLDS DLVEEYEEML LKAATSLRVL LAGTSGQDSA PTTDGPAPAH
     AAEGGLR
//
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