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Database: UniProt
Entry: A0A0B2AC42_9MICO
LinkDB: A0A0B2AC42_9MICO
Original site: A0A0B2AC42_9MICO 
ID   A0A0B2AC42_9MICO        Unreviewed;       673 AA.
AC   A0A0B2AC42;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=aminodeoxychorismate synthase {ECO:0000256|ARBA:ARBA00013139};
DE            EC=2.6.1.85 {ECO:0000256|ARBA:ARBA00013139};
GN   ORFNames=LK09_03140 {ECO:0000313|EMBL:KHK99298.1};
OS   Microbacterium mangrovi.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1348253 {ECO:0000313|EMBL:KHK99298.1, ECO:0000313|Proteomes:UP000031030};
RN   [1] {ECO:0000313|EMBL:KHK99298.1, ECO:0000313|Proteomes:UP000031030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUSC 115 {ECO:0000313|EMBL:KHK99298.1,
RC   ECO:0000313|Proteomes:UP000031030};
RA   Lee L.-H.;
RT   "Genome sequence of Microbacterium mangrovi MUSC 115(T).";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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:KHK99298.1}.
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DR   EMBL; JTDK01000003; KHK99298.1; -; Genomic_DNA.
DR   RefSeq; WP_039395896.1; NZ_JTDK01000003.1.
DR   AlphaFoldDB; A0A0B2AC42; -.
DR   STRING; 1348253.LK09_03140; -.
DR   OrthoDB; 3518032at2; -.
DR   Proteomes; UP000031030; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P: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; 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; 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|PROSITE-ProRule:PRU00605};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031030};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          5..186
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   DOMAIN          228..353
FT                   /note="Anthranilate synthase component I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04715"
FT   DOMAIN          405..663
FT                   /note="Chorismate-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00425"
FT   REGION          360..394
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        169
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   673 AA;  71187 MW;  957544D82C04A6DF CRC64;
     MARVLIIDNF DSFTNNIADL VAGVTGIPPL VVDNRMPFDE LPWAEVDAVV LGPGPGHPAN
     PADFGVCREV IERAPCPILG VCLGHQGIAD VFGGVVERAP SPAHGLVHEI EHDGTGLFAG
     LPSPFPVVRY HSLAVTEVPD ALRVTARTAD GVVMALEHRR LPIWGVQFHP ESIAGRHGDD
     LLRRFVALAD AYNHTRHAAV AQAFAAVGGT LAGTPRVKEV PWPGDAASLY AGLVGDADGF
     WLDSSQPEHP DADVSVLGRA TVTLTYRIAD RILTLRGPAG ERHVTGDAFT LLGELLDAFD
     HPGAGPFTAG LAGYLGYELK ALCGGDETHR SRMPDAAWIW PAEFVVLDHG TRRAFRHTLA
     PAPATPAPSP GASPVPPRAK QDEATRPYTP GPVPEHLLAL RDARPAYLDK IARAQEHIVD
     GDSYEICLTN TASVPAPADA LAAFVELRRV SPVPYGAYLR ITPPGGRPIG VLSASPETFL
     RVDRDGRVTT RPIKGTRPRG ATPMEDAALR RDLAGSAKDR AENLMIVDLS RHDLGGVCEP
     GTVAVPELFA VQSFSSVHQL VSTITGRRRA GIRTVDVVRA CFPPGSMTGA PKRRTMEIID
     DLEGAARGPY AGALGWLDAS GAAVLSVVIR TLVIEGDAAS FGIGGAITAL SDPADEFVET
     LVKASVPFHA AGR
//
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