ID A0A0P0DMJ2_9MICO Unreviewed; 637 AA.
AC A0A0P0DMJ2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Anthranilate synthase component 1 {ECO:0000256|ARBA:ARBA00020653};
DE EC=4.1.3.27 {ECO:0000256|ARBA:ARBA00012266};
GN ORFNames=AOA12_15035 {ECO:0000313|EMBL:ALJ21144.1};
OS Microbacterium sp. No. 7.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1714373 {ECO:0000313|EMBL:ALJ21144.1, ECO:0000313|Proteomes:UP000059097};
RN [1] {ECO:0000313|EMBL:ALJ21144.1, ECO:0000313|Proteomes:UP000059097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=No. 7 {ECO:0000313|EMBL:ALJ21144.1,
RC ECO:0000313|Proteomes:UP000059097};
RA Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA Tsuda M., Fujita N., Kawai F.;
RT "Complete genome sequence of a polypropylene glycol-degrading strain
RT Microbacterium sp. No. 7.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the two-
CC step biosynthesis of anthranilate, an intermediate in the biosynthesis
CC of L-tryptophan. In the first step, the glutamine-binding beta subunit
CC (TrpG) of anthranilate synthase (AS) provides the glutamine
CC amidotransferase activity which generates ammonia as a substrate that,
CC along with chorismate, is used in the second step, catalyzed by the
CC large alpha subunit of AS (TrpE) to produce anthranilate. In the
CC absence of TrpG, TrpE can synthesize anthranilate directly from
CC chorismate and high concentrations of ammonia.
CC {ECO:0000256|ARBA:ARBA00025634}.
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|ARBA:ARBA00000329};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5. {ECO:0000256|ARBA:ARBA00004873}.
CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a
CC beta subunit (TrpG) and a large alpha subunit (TrpE).
CC {ECO:0000256|ARBA:ARBA00011575}.
CC -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC {ECO:0000256|ARBA:ARBA00009562}.
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DR EMBL; CP012697; ALJ21144.1; -; Genomic_DNA.
DR RefSeq; WP_054684378.1; NZ_CP012697.1.
DR AlphaFoldDB; A0A0P0DMJ2; -.
DR STRING; 1714373.AOA12_15035; -.
DR KEGG; mio:AOA12_15035; -.
DR PATRIC; fig|1714373.3.peg.3096; -.
DR OrthoDB; 8594609at2; -.
DR Proteomes; UP000059097; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P: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; IPR005801; ADC_synthase.
DR InterPro; IPR019999; Anth_synth_I-like.
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; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR PANTHER; PTHR11236:SF46; ANTHRANILATE SYNTHASE COMPONENT 1; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR Pfam; PF00117; GATase; 1.
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:UP000059097}.
FT DOMAIN 113..377
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT DOMAIN 453..631
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 533
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 615
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 617
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 637 AA; 67577 MW; 1A0A0903A10F6FF1 CRC64;
MTPNPLAAAL AGGAFALIAR DGATVEVLTG DVVDVDLLAD IPLHAPDGTP QHVLALVPFR
QVVERGYECH DDGAPLRCLV VGERVTVPLA DVLATLPSEP VPLADAGFDI PDEEYADIVR
RVIADEIGRG EGANFVIRRD FTAAVDVDAV TAGLTWFRAL LEHERGAYWT FLVCTPGHVA
VGASPEAHVS ADHGAAGDGV STVTMNPISG TFRHPAGGAT VETLTEFLGS TKETEELFMV
VDEELKMMSA VCTDGGRITG PHLKEMSRLT HTEYMLRGTS TMDPRDILRE TMFAPTVTGS
PMQNACTVIT RHERTPRGYY SGVAALFTPR EGGVHDLDAP ILIRTAYLVD GRLRVPVGAT
LVRHSDPYGE VSETHGKAAG VLGAIGAVDR DPVAVPVDVS AADEDEPTSA PRRLADDPRV
AELLAARNER LAEFWLNPQD AAGPRPLAGF SALVVDAEDR FTTMLAHQLR HLGLDVRIAH
WADADDADLA AADLVLCGPG PGDPRDEDSP RMARMRAIVA ARIAAGAPLL AVCLSHQILA
DRLGIELAPL AAPHQGLQKT IDLFGQPASI GFYNTFTARV APGTGRVGAA EVAADPASGD
VYAMRGPRYA SVQGHLESIL SRDGLVTLER LVRHALA
//
