ADCS_STRGR
ID ADCS_STRGR Reviewed; 723 AA.
AC P32483; Q9EWC1;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Aminodeoxychorismate synthase {ECO:0000305};
DE Short=ADC synthase {ECO:0000305};
DE EC=2.6.1.85 {ECO:0000250|UniProtKB:Q8LPN3};
DE AltName: Full=4-amino-4-deoxychorismate synthase {ECO:0000305};
DE AltName: Full=p-aminobenzoic acid synthase {ECO:0000303|PubMed:8472954};
DE Short=PABA synthase {ECO:0000303|PubMed:8472954};
GN Name=pabAB {ECO:0000303|PubMed:8472954};
GN Synonyms=pab {ECO:0000303|PubMed:8472954};
OS Streptomyces griseus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IMRU 3570;
RX PubMed=8472954; DOI=10.1016/0378-1119(93)90602-y;
RA Criado L.M., Martin J.F., Gil J.A.;
RT "The pab gene of Streptomyces griseus, encoding p-aminobenzoic acid
RT synthase, is located between genes possibly involved in candicidin
RT biosynthesis.";
RL Gene 126:135-139(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=IMRU 3570;
RX PubMed=11782498; DOI=10.1099/00221287-148-1-51;
RA Campelo A.B., Gil J.A.;
RT "The candicidin gene cluster from Streptomyces griseus IMRU 3570.";
RL Microbiology 148:51-59(2002).
CC -!- FUNCTION: Involved in candicidin biosynthesis (PubMed:11782498).
CC Catalyzes the biosynthesis of 4-amino-4-deoxychorismate (ADC) from
CC chorismate and glutamine (By similarity).
CC {ECO:0000250|UniProtKB:Q8LPN3, ECO:0000269|PubMed:11782498}.
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:0000250|UniProtKB:Q8LPN3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11673;
CC Evidence={ECO:0000305|PubMed:11782498};
CC -!- PATHWAY: Antibiotic biosynthesis; candicidin biosynthesis.
CC {ECO:0000269|PubMed:11782498}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene abolishes production of
CC candicidin. {ECO:0000269|PubMed:11782498}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the anthranilate
CC synthase component I family. {ECO:0000305}.
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DR EMBL; M93058; AAA72111.1; -; Unassigned_DNA.
DR EMBL; AJ300302; CAC22117.1; -; Genomic_DNA.
DR PIR; JN0531; JN0531.
DR AlphaFoldDB; P32483; -.
DR SMR; P32483; -.
DR MEROPS; C26.A25; -.
DR BioCyc; MetaCyc:MON-16235; -.
DR UniPathway; UPA00101; -.
DR GO; GO:0046820; F:4-amino-4-deoxychorismate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.60.120.10; -; 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 PANTHER; PTHR11236; PTHR11236; 1.
DR Pfam; PF04715; Anth_synt_I_N; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF56322; SSF56322; 1.
DR TIGRFAMs; TIGR00553; pabB; 1.
DR TIGRFAMs; TIGR00566; trpG_papA; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW Antibiotic biosynthesis; Glutamine amidotransferase;
KW Multifunctional enzyme; Transferase.
FT CHAIN 1..723
FT /note="Aminodeoxychorismate synthase"
FT /id="PRO_0000154141"
FT DOMAIN 2..195
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT REGION 96..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..723
FT /note="PABB component"
FT /evidence="ECO:0000305"
FT REGION 693..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 169
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT CONFLICT 698
FT /note="R -> A (in Ref. 2; CAC22117)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 723 AA; 77901 MW; 1251547F82DA100F CRC64;
MRTLLVDNYD SFTYNLFHYL SRANGREPEV IRNDDPAWRP GLLDAFDNVV LSPGPGTPHR
PADFGLCARI AEEGRLPVLG VCLGHQGMAL AHGARVGRAP EPRHGRTSAV RHDGTGLFEG
LPQPLEVVRY HSLAVTELPP ELEATAWSED GVLMALRHRT LPLWGVQFHP ESIGTQDGHR
LLANFRDLTE RHGRTRHGGR AGHGTLPPPA PARETKATTG TPRRLRVIAK SLPTRWDAEV
AFDSLFRTGD HPFWLDSSRP GGELGQLSMM GDASGPLART AKADVHAGTV TVRADGASST
VESAFLTWLE NDLAGLRTEV PELPFAFALG WVGCLGYELK AECDGDAAHR SPDPDAVLVF
ADRALVLDHR TRTTYLLALV EDDAEAEARA WLAAASATLD AVAGREPEPC PEAPVCTTGP
VELRHDRDGY LKLIDVCQQE IAAGETYEVC LTNMAEADTD LTPWAAYRAL RRVSPAPFAA
FLDFGPMAVL SSSPERFLRI DRHGRMESKP IKGTRPRGAT PQEDAALVRA LATCEKDRAE
NLMIVDLVRH DLGRCAEVGS VVADPVFQVE TYATVHQLVS TVTARLREDS SPVAAVRAAF
PGGSMTGAPK IRTMQIIDRL EGGPRGVYSG AIGYFSLTGA VDLSIVIRTV VLSGGRLRYG
VGGAVIALSD PADEFEETAV KAAPLLRLLD TAFPGRERPG KDLDGEPDDG TDAGAPKDLV
LPG
