ID A0A1Q3L9Y4_9MICO Unreviewed; 625 AA.
AC A0A1Q3L9Y4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Anthranilate synthase component 1 {ECO:0000256|ARBA:ARBA00020653};
DE EC=4.1.3.27 {ECO:0000256|ARBA:ARBA00012266};
GN ORFNames=BGN97_05005 {ECO:0000313|EMBL:OJU42102.1};
OS Microbacterium sp. 69-10.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1895783 {ECO:0000313|EMBL:OJU42102.1, ECO:0000313|Proteomes:UP000185697};
RN [1] {ECO:0000313|EMBL:OJU42102.1, ECO:0000313|Proteomes:UP000185697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=69-10 {ECO:0000313|EMBL:OJU42102.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJU42102.1}.
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DR EMBL; MKRT01000006; OJU42102.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3L9Y4; -.
DR STRING; 1895783.BGN97_05005; -.
DR Proteomes; UP000185697; Unassembled WGS sequence.
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}.
FT DOMAIN 114..372
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT DOMAIN 441..618
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 521
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 603
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 605
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 625 AA; 67588 MW; A0AA7CDA1AA43D83 CRC64;
MTDLKRRIRA LAADPETSFV LIARDGVVEL LTGEIVDVET LSDIPLEGAD GPREVFAMVP
YRQVRERGFE AQDDGTPLRC LLVAEREGLD AEELRAALPD TPIDLRGGGF DISDDEYADI
VEQVIAEEIG RGEGANFVIR RDYRAGYECD DRIAALTWFR ALLEHERGAY WTFAVITPGQ
IAVGASPEAH VVARDGIVTM NPISGTFRHP AGGATRESLT EFLSSTKETE ELFMVVDEEL
KMMSQVCSDG GRITGPHLKE MSRLTHTEYM LRGRSRLDPR DILRETMFAP TVTGSPMQNA
CAVIRRHERA PRGYYSGVAA LFTPNADGGH DLDAPILIRT AYLDRGHLRV PVGATLVRHS
DPLGEVGETH GKAAGVLGAI GAIERDHVAE TRDDDAPAPA RLADDPEIAA LLASRNTRLA
DFWMQPQDAA AAGRFGGRSA LVVDAEDRFT TMLAHQLRHL GLDVTIAPWS EVTDEAVDAA
DLVVSGPGPG DPRDPSSPRI ARMQQVVARR RATGSPLLAV CLSHQILADG LGIDLVPLDS
PYQGVQKTVP VFGEDASVGF YNTFTARVAP GTTRVGEAEV AADAESGDVY ALRGERFASI
QGHLESILSR DGIATLERLT AHALS
//
