ID R4K7G8_CLOPA Unreviewed; 728 AA.
AC R4K7G8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Anthranilate synthase {ECO:0000256|PIRNR:PIRNR036934};
DE EC=4.1.3.27 {ECO:0000256|PIRNR:PIRNR036934};
GN ORFNames=Clopa_1534 {ECO:0000313|EMBL:AGK96474.1};
OS Clostridium pasteurianum BC1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=86416 {ECO:0000313|EMBL:AGK96474.1, ECO:0000313|Proteomes:UP000013523};
RN [1] {ECO:0000313|EMBL:AGK96474.1, ECO:0000313|Proteomes:UP000013523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC1 {ECO:0000313|EMBL:AGK96474.1,
RC ECO:0000313|Proteomes:UP000013523};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Dunn J.,
RA Taghavi S., Francis A., van der Lelie D., Woyke T.;
RT "Complete sequence of chromosome of Clostridium pasteurianum BC1.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003261; AGK96474.1; -; Genomic_DNA.
DR AlphaFoldDB; R4K7G8; -.
DR STRING; 86416.Clopa_1534; -.
DR KEGG; cpas:Clopa_1534; -.
DR PATRIC; fig|86416.3.peg.1510; -.
DR eggNOG; COG0147; Bacteria.
DR eggNOG; COG0512; Bacteria.
DR HOGENOM; CLU_006493_3_0_9; -.
DR OrthoDB; 9803598at2; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000013523; 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:UP000013523};
KW Tryptophan biosynthesis {ECO:0000256|PIRNR:PIRNR036934}.
FT DOMAIN 38..205
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 250..501
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT DOMAIN 535..711
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 610
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 698
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 700
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 728 AA; 83150 MW; 40E639B88FCADA53 CRC64;
MYNFTENTNC KSEYITKGGI KVIRTKESLK DDDSIAKISK KLVHNKGAIF ASDYEYPNRY
SRWEFAFTNP CLELRCFQRK FTINSLNKRG DLLLDIIACK LKEIKEVEIC VESKEHIEGI
VQEANEFFCE EDRSKQVSVF LIIRKIKDIF ESKEDSNLGL YGAFGYDLVF QFEPEIELKK
ERSDKQQDLV LYLPDRLTVV DNESKDGYVL SYEFTTAKGS TEGLKRIERL NNNKIQQCEN
FNNESSKLGE YASIVSKALD SFRKGDLFEV VPSHLLSKEI NMTADEIFYN LREINPSPYG
FFINLGDKFL VGSSPEMYVR VEKNRVETCP ISGTTKRGKN AIDDSEQIKK LINSNKDEEE
LTMCTDVDRN DKSRICIPGS VKVIGRRQIE MYSHLIHTVD HVEGYLNDEY DCIDAFLTHM
WAVTITGSPK RAAIEWIEEQ EKAPREWYGG AVGYILFNGD MNTGLTLRTI RIKNNIAQVR
VGATLLIHSQ PNEEEEETYT KAAALLESLN RKESLIKDNE KREVDFNVCK NKKILIVDHE
DSFVNTLASY IKQLGAHTVT LRYDLAENVL KEDSFDAVVL SPGPGRPKRF NLSNTIKLCL
NKKIPIFGVC LGMQGLIEYF GGKLKQLNYP RHGKKLNVKN DLSFNVWSDI GENLQAGLYH
SIYCDNIPDS FNIIAKDEEG IAMGIQHKQL PIIAVQFHPE SILTAAGNSG IKLLNNVFEE
LFNFYTVK
//
