ADCS_STRVP
ID ADCS_STRVP Reviewed; 686 AA.
AC F2RB79; Q56151;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 57.
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-aminobenzoate synthase {ECO:0000303|PubMed:8704974};
GN Name=cmlB {ECO:0000303|PubMed:25267678};
GN Synonyms=pabAB {ECO:0000303|PubMed:8704974};
GN OrderedLocusNames=SVEN_0920 {ECO:0000312|EMBL:CCA54207.1};
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=953739;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD
RC 04745;
RX PubMed=8704974; DOI=10.1099/13500872-142-6-1345;
RA Brown M.P., Aidoo K.A., Vining L.C.;
RT "A role for pabAB, a p-aminobenzoate synthase gene of Streptomyces
RT venezuelae ISP5230, in chloramphenicol biosynthesis.";
RL Microbiology 142:1345-1355(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD
RC 04745;
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Chandra G., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
RN [3]
RP NOMENCLATURE.
RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD
RC 04745;
RX PubMed=25267678; DOI=10.1128/aac.04272-14;
RA Fernandez-Martinez L.T., Borsetto C., Gomez-Escribano J.P., Bibb M.J.,
RA Al-Bassam M.M., Chandra G., Bibb M.J.;
RT "New insights into chloramphenicol biosynthesis in Streptomyces venezuelae
RT ATCC 10712.";
RL Antimicrob. Agents Chemother. 58:7441-7450(2014).
CC -!- FUNCTION: Involved in chloramphenicol biosynthesis (PubMed:8704974).
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:8704974}.
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:8704974};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:8704974}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene decreases sulfanilamide
CC resistance and blocks chloramphenicol production.
CC {ECO:0000269|PubMed:8704974}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the anthranilate
CC synthase component I family. {ECO:0000305}.
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DR EMBL; U21728; AAB30312.1; -; Genomic_DNA.
DR EMBL; FR845719; CCA54207.1; -; Genomic_DNA.
DR RefSeq; WP_015032126.1; NZ_CP029197.1.
DR AlphaFoldDB; F2RB79; -.
DR SMR; F2RB79; -.
DR STRING; 953739.SVEN_0920; -.
DR MEROPS; C26.955; -.
DR MEROPS; C26.A25; -.
DR EnsemblBacteria; CCA54207; CCA54207; SVEN_0920.
DR KEGG; sve:SVEN_0920; -.
DR PATRIC; fig|953739.5.peg.2966; -.
DR eggNOG; COG0147; Bacteria.
DR eggNOG; COG0512; Bacteria.
DR HOGENOM; CLU_006493_0_1_11; -.
DR OMA; DWSVNIR; -.
DR BioCyc; MetaCyc:MON-20700; -.
DR Proteomes; UP000006854; Chromosome.
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; Reference proteome; Transferase.
FT CHAIN 1..686
FT /note="Aminodeoxychorismate synthase"
FT /id="PRO_0000447218"
FT DOMAIN 2..194
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT REGION 233..686
FT /note="PABB component"
FT /evidence="ECO:0000305"
FT ACT_SITE 81
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 168
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT CONFLICT 14
FT /note="H -> Q (in Ref. 1; AAB30312)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="Missing (in Ref. 1; AAB30312)"
FT /evidence="ECO:0000305"
FT CONFLICT 91..99
FT /note="FGGTVGLAP -> SA (in Ref. 1; AAB30312)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="W -> M (in Ref. 1; AAB30312)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="H -> P (in Ref. 1; AAB30312)"
FT /evidence="ECO:0000305"
FT CONFLICT 201..202
FT /note="SP -> WG (in Ref. 1; AAB30312)"
FT /evidence="ECO:0000305"
FT CONFLICT 222..226
FT /note="GCLPG -> AACPA (in Ref. 1; AAB30312)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="R -> P (in Ref. 1; AAB30312)"
FT /evidence="ECO:0000305"
FT CONFLICT 280..284
FT /note="TRRPF -> DAATL (in Ref. 1; AAB30312)"
FT /evidence="ECO:0000305"
FT CONFLICT 294..297
FT /note="RRRV -> PPAG (in Ref. 1; AAB30312)"
FT /evidence="ECO:0000305"
FT CONFLICT 329..331
FT /note="HRS -> VPA (in Ref. 1; AAB30312)"
FT /evidence="ECO:0000305"
FT CONFLICT 387..389
FT /note="PAE -> RPR (in Ref. 1; AAB30312)"
FT /evidence="ECO:0000305"
FT CONFLICT 418..429
FT /note="YLKRIDECLKEI -> SAL (in Ref. 1; AAB30312)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="A -> R (in Ref. 1; AAB30312)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="Y -> S (in Ref. 1; AAB30312)"
FT /evidence="ECO:0000305"
FT CONFLICT 507..508
FT /note="GT -> AP (in Ref. 1; AAB30312)"
FT /evidence="ECO:0000305"
FT CONFLICT 558..560
FT /note="ETY -> GDL (in Ref. 1; AAB30312)"
FT /evidence="ECO:0000305"
FT CONFLICT 601
FT /note="T -> P (in Ref. 1; AAB30312)"
FT /evidence="ECO:0000305"
FT CONFLICT 616..617
FT /note="YS -> LP (in Ref. 1; AAB30312)"
FT /evidence="ECO:0000305"
FT CONFLICT 664..665
FT /note="TE -> RQ (in Ref. 1; AAB30312)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 686 AA; 74547 MW; 15EC60477BE75F5D CRC64;
MRTLLIDNYD SFTHNLFQYI GEATGQPPVV VPNDADWSRL PLEDFDAIVV SPGPGSPDRE
RDFGISRRAI TDSGLPVLGV CLGHQGIAQL FGGTVGLAPE PMHGRVSEVR HTGEDVFRGL
PSPFTAVRYH SLAATDLPDE LEPLAWSDDG VVMGLRHREK PLWGVQFHPE SIGSDFGREI
MANFRDLALA HHRARRDAAD SPYELHVRRV DVLPDAEEVR RGCLPGEGAT FWLDSSSVLE
GASRFSFLGD DRGPLAEYLT YRVADGVVSV RGSDGTTTRT RRPFFSYLEE QLERRRVPVA
PDLPFEFNLG YVGYLGYELK AETTGDPAHR SPHPDAAFLF ADRAIALDHQ EGCCYLLALD
RRGHDDGARA WLRETAETLT GLAVRVPAEP TPAMVFGVPE AAAGFGPLAR ARHDKDAYLK
RIDECLKEIR NGESYEICLT NMVTAPTEAT ALPLYSALRA ISPVPYGALL EFPELSVLSA
SPERFLTIGA DGGVESKPIK GTRPRGGTAE EDERLRADLA GREKDRAENL MIVDLVRNDL
NSVCAIGSVH VPRLFEVETY APVHQLVSTI RGRLRPGTST AACVRAAFPG GSMTGAPKKR
TMEIIDRLEE GPRGVYSGAL GWFALSGAAD LSIVIRTIVL ADGRAEFGVG GAIVSLSDQE
EEFTETVVKA RAMVTALDGS AVAGAR
