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
//