ID D2AV30_STRRD Unreviewed; 715 AA.
AC D2AV30;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Anthranilate synthase {ECO:0000256|PIRNR:PIRNR036934};
DE EC=4.1.3.27 {ECO:0000256|PIRNR:PIRNR036934};
GN OrderedLocusNames=Sros_3982 {ECO:0000313|EMBL:ACZ86892.1};
OS Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI
OS 9100).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Streptosporangium.
OX NCBI_TaxID=479432 {ECO:0000313|EMBL:ACZ86892.1, ECO:0000313|Proteomes:UP000002029};
RN [1] {ECO:0000313|EMBL:ACZ86892.1, ECO:0000313|Proteomes:UP000002029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100
RC {ECO:0000313|Proteomes:UP000002029};
RX PubMed=21304675; DOI=10.4056/sigs.631049;
RA Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A., Glavina Del Rio T.,
RA Chen F., Tice H., Pitluck S., Cheng J.F., Chertkov O., Sims D., Meincke L.,
RA Brettin T., Han C., Detter J.C., Bruce D., Goodwin L., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Ivanova N., Mavromatis K., Mikhailova N.,
RA Chen A., Palaniappan K., Chain P., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Streptosporangium roseum type strain (NI
RT 9100).";
RL Stand. Genomic Sci. 2:29-37(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate +
CC pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58359; EC=4.1.3.27;
CC Evidence={ECO:0000256|PIRNR:PIRNR036934};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5. {ECO:0000256|PIRNR:PIRNR036934}.
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DR EMBL; CP001814; ACZ86892.1; -; Genomic_DNA.
DR RefSeq; WP_012890634.1; NC_013595.1.
DR AlphaFoldDB; D2AV30; -.
DR STRING; 479432.Sros_3982; -.
DR KEGG; sro:Sros_3982; -.
DR eggNOG; COG0147; Bacteria.
DR eggNOG; COG0512; Bacteria.
DR HOGENOM; CLU_006493_3_0_11; -.
DR OrthoDB; 3518032at2; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000002029; Chromosome.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0000162; P:tryptophan biosynthetic 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; IPR010112; TrpE-G_bact.
DR InterPro; IPR006221; TrpG/PapA_dom.
DR NCBIfam; TIGR01815; TrpE-clade3; 1.
DR PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR PANTHER; PTHR11236:SF9; ANTHRANILATE SYNTHASE COMPONENT 1; 1.
DR Pfam; PF04715; Anth_synt_I_N; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR Pfam; PF00117; GATase; 1.
DR PIRSF; PIRSF036934; TrpE-G; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
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 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR036934};
KW Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR036934};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Lyase {ECO:0000256|PIRNR:PIRNR036934};
KW Reference proteome {ECO:0000313|Proteomes:UP000002029};
KW Tryptophan biosynthesis {ECO:0000256|PIRNR:PIRNR036934}.
FT DOMAIN 34..193
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 235..487
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT DOMAIN 524..698
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 599
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 688
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 690
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 715 AA; 77713 MW; 2991C8135A75E3C2 CRC64;
METSGYTTAG GIEVEVTASD VPETVLEDVV TTLGERRGGV LSSGMEYPGR YSRWHLAYVD
PCLEIVARGR RISARALNAR GRVVLPAVAS CLLATGKPTG EPTAEHVEVY VAESEDILPE
EMRSRRPTVF TAIREVIAAF KGENEHLGLY GSFGYDLAFQ FEPIRQVLTR ADDQRDLVLH
LPDRVMVIDR KRETSKEYLY EFTVDGVSTR GLAREGESIP LPPAPAELPA DPEKGTYAQV
VAAAKEKFVR GDLFEVVPGQ VFHAACTDPA AFYRGLRKAN PAPFEFLFNL GEGEHLVGAS
PEMYVRVSGD RVETCPISGT IARGGNPIED AEAIRTLLSS VKEESELTMC TDVDRNDKSR
ICVPGTVQVI GRRQIEMYSR LIHTVDHIEG RLRPEFDALD AFLTHMWAVT VTGAPKSWAM
QFIEDHEATT RRWYGGAVGY IGFDGSMNTG LTLRTAQIRG GVATVRAGAT LLFDSDPEAE
ERETELKASA LLGALAAVGA ARTPQERDVP QPVREQPGEG MKVLLVDHED SFVNTLADYF
RQQGAEVVTL RHGFPVSMID EIAPSLVVLS PGPGWPSDFG LPELVGALYE RDLPVFGVCL
GLQGMVEQAG GTLELLSHPE HGKRGQVRRT GPGALLEGLP EEFTAARYHS LHAKQPGVVG
FTATALTPDG AVMAIEDVAR RRFAVQFHPE SILTAEGGAG AKIISNVLRL CRTSG
//
