ID A0A0F7NFC6_9ACTN Unreviewed; 709 AA.
AC A0A0F7NFC6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=aminodeoxychorismate synthase {ECO:0000256|ARBA:ARBA00013139};
DE EC=2.6.1.85 {ECO:0000256|ARBA:ARBA00013139};
GN ORFNames=AA958_32560 {ECO:0000313|EMBL:AKH86169.1};
OS Streptomyces sp. CNQ-509.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=444103 {ECO:0000313|EMBL:AKH86169.1, ECO:0000313|Proteomes:UP000034283};
RN [1] {ECO:0000313|EMBL:AKH86169.1, ECO:0000313|Proteomes:UP000034283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNQ-509 {ECO:0000313|EMBL:AKH86169.1,
RC ECO:0000313|Proteomes:UP000034283};
RA Ruckert C., Albersmeier A., Leipoldt F., Winkler A., Zeyhle P.,
RA Kalinowski J., Heide L., Kaysser L.;
RT "Complete Genome Sequence of Streptomyces sp. CNQ-509, a Prolific Producer
RT of Meroterpenoid Chemistry.";
RL Submitted (MAY-2015) 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}.
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DR EMBL; CP011492; AKH86169.1; -; Genomic_DNA.
DR RefSeq; WP_047019396.1; NZ_CP011492.1.
DR AlphaFoldDB; A0A0F7NFC6; -.
DR STRING; 444103.AA958_32560; -.
DR KEGG; strc:AA958_32560; -.
DR PATRIC; fig|444103.5.peg.6873; -.
DR OrthoDB; 3518032at2; -.
DR Proteomes; UP000034283; 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|PROSITE-ProRule:PRU00605};
KW Reference proteome {ECO:0000313|Proteomes:UP000034283};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..185
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 250..380
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 430..684
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT REGION 204..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..526
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 709 AA; 77500 MW; E694B5DFD5C9EC30 CRC64;
MRTLLVDNYD SFTYNLFHYL AEVNGREPVV LRNDDAGWDP GMLAEFDSVL ISPGPGRPER
PEDFGICQEI IDNGSLPILG VCLGHQGIAH AFGARVTRAP EPRHGRVSPV FHEGNRLFAG
LPEPFDVVRY HSLAVTDLPW ELRPTAWTDD GVLMGIEHRD RPLWGVQFHP ESISTAHGHR
LLRNFRELAE EFGGAGRGTA VVAAPTPAAG GTSRASSRSV APRSRSPRRL RVLTTALPTR
WSDEVAFDRL FGAHEHAFWL DSSAAASEHG RFSIMGDASG PLARVARADT WDGSVTVERS
TGVETVRGEL FTWLEEDLRS LSVELPELPC DFALGWVGYL GYELKAECGG AASYRSDEPD
AAMIFADRAL VFDHATSTTH LLALTEDGDE GPGRAWLADT AERLGEIAGQ EPHYVPPPAK
DATLRLRHDR DRYLELIAHC QEQIAAGETY EICLTNLLQA DVAVPPWQSY QFLRRLTPAP
FASLLRFGEI SVLSTSPERF LRISADGTAE SKPIKGTRPR GDSESEDILL RKDLAASEKD
RSENLMIVDL VRNDLGRTAE VGSVRVPRIY DVETHPTTHQ LVSTVTSQLR PSVSAVECVR
AAFPGGSMTG APKIRTMKII DSLEAGPRGV YSGAIGYFSL SGACDLSIVI RTLVVTPSRV
KYGVGGAIVA LSEPDEEFEE IAVKATPLLR LLGAEFPGRL PVDLIRTGR
//
