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Database: UniProt
Entry: Q3SPC4_NITWN
LinkDB: Q3SPC4_NITWN
Original site: Q3SPC4_NITWN 
ID   Q3SPC4_NITWN            Unreviewed;       727 AA.
AC   Q3SPC4;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=Anthranilate synthase {ECO:0000256|PIRNR:PIRNR036934};
DE            EC=4.1.3.27 {ECO:0000256|PIRNR:PIRNR036934};
GN   OrderedLocusNames=Nwi_2614 {ECO:0000313|EMBL:ABA05867.1};
OS   Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 /
OS   NCIMB 11846 / Nb-255).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Nitrobacter.
OX   NCBI_TaxID=323098 {ECO:0000313|EMBL:ABA05867.1, ECO:0000313|Proteomes:UP000002531};
RN   [1] {ECO:0000313|EMBL:ABA05867.1, ECO:0000313|Proteomes:UP000002531}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255
RC   {ECO:0000313|Proteomes:UP000002531};
RX   PubMed=16517654; DOI=10.1128/AEM.72.3.2050-2063.2006;
RA   Starkenburg S.R., Chain P.S., Sayavedra-Soto L.A., Hauser L., Land M.L.,
RA   Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J.,
RA   Hickey W.J.;
RT   "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium
RT   Nitrobacter winogradskyi Nb-255.";
RL   Appl. Environ. Microbiol. 72:2050-2063(2006).
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; CP000115; ABA05867.1; -; Genomic_DNA.
DR   RefSeq; WP_011315817.1; NC_007406.1.
DR   AlphaFoldDB; Q3SPC4; -.
DR   STRING; 323098.Nwi_2614; -.
DR   MEROPS; C26.A09; -.
DR   KEGG; nwi:Nwi_2614; -.
DR   eggNOG; COG0147; Bacteria.
DR   eggNOG; COG0512; Bacteria.
DR   HOGENOM; CLU_006493_3_0_5; -.
DR   OrthoDB; 9803598at2; -.
DR   UniPathway; UPA00035; UER00040.
DR   Proteomes; UP000002531; 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   NCBIfam; TIGR00566; trpG_papA; 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, ECO:0000313|EMBL:ABA05867.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002531};
KW   Tryptophan biosynthesis {ECO:0000256|PIRNR:PIRNR036934}.
FT   DOMAIN          121..200
FT                   /note="Anthranilate synthase component I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04715"
FT   DOMAIN          246..498
FT                   /note="Chorismate-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00425"
FT   DOMAIN          529..703
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        604
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        693
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        695
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   727 AA;  79687 MW;  DAAF00B0CEFC2378 CRC64;
     MNRTAFSLPA QSEYLTAGGL SISRSIEHFT GGSRLDDLIG LLDSRRGVVL SSGTTVPGRY
     ESFDLGFADP PLKIETTGFN FTIEAANARG EVLIAFLGET LSEPCAVVTE KTARRIAGHI
     VRGDAPVEED QRTRRASVMS LVRALVAAFA STADPMLGLY GAFAYDLVFQ IEDLVQKRAR
     EPDQRDIVLF IPDRLLAYDR AAGHGVVLSY DFAWKGRSTE GQPRDTPDSV YAKTSRQGFT
     DHAPGEYQAT VETARAAFAR GDLFEAVPGQ LFAEPCERSP AEVFQRLCRI NPSPYGGLVN
     LGDGEFLVSA SPEMFVRSDG RRIETCPISG TIARGADAIG DAEQIRELLN SEKDEFELNM
     CTDVDRNDKA RICMPGTIKV LARRQIETYS KLFHTVDHVE GILRSGFDAL DGFLTHAWAV
     TVTGAPKKWA IQFVEDNERS TRRWYAGAFG VVGFDGSINT GLTIRTIRMK DGLAEVRVGA
     TCLFDSKPEL EDRECQTKAA ALFQALRGDA PKPLSAVAPD ATGSGKRVLL IDHDDSFVHM
     LADYFRQVGA RVSVVRYVHA RDMLDRQGYD LLVLSPGPGR PEDFGMARTI GLALEKKMPV
     FGVCLGLQGI GEYFGGRLGQ LAQPAHGRPS RVQNRGGRLM RNLPNEIVIG RYHSLYVERD
     RLPEVLEITA TTDDGVPMAI EHKSLPVGGV QFHPESLMSL GGEVGLRIVE NAFRLGRERR
     ENSNDAV
//
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