ID A0A0F0KG56_9MICO Unreviewed; 636 AA.
AC A0A0F0KG56;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Anthranilate synthase component 1 {ECO:0000256|ARBA:ARBA00020653};
DE EC=4.1.3.27 {ECO:0000256|ARBA:ARBA00012266};
GN Name=trpE {ECO:0000313|EMBL:KJL19414.1};
GN ORFNames=RL72_03062 {ECO:0000313|EMBL:KJL19414.1};
OS Microbacterium azadirachtae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=582680 {ECO:0000313|EMBL:KJL19414.1, ECO:0000313|Proteomes:UP000033448};
RN [1] {ECO:0000313|EMBL:KJL19414.1, ECO:0000313|Proteomes:UP000033448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23848 {ECO:0000313|EMBL:KJL19414.1,
RC ECO:0000313|Proteomes:UP000033448};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-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}.
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:KJL19414.1}.
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DR EMBL; JYIT01000084; KJL19414.1; -; Genomic_DNA.
DR RefSeq; WP_045251729.1; NZ_JYIT01000084.1.
DR AlphaFoldDB; A0A0F0KG56; -.
DR PATRIC; fig|582680.7.peg.3122; -.
DR OrthoDB; 8594609at2; -.
DR Proteomes; UP000033448; Unassembled WGS sequence.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
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 Lyase {ECO:0000313|EMBL:KJL19414.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033448}.
FT DOMAIN 113..375
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT DOMAIN 450..627
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT REGION 388..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 530
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 612
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 614
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 636 AA; 67475 MW; 1D7C7D4FF8B5ACBA CRC64;
MTTADRIHAL PTESAFVLLA REGSDSVELL TGEIVDVLDL ADIPLGADGA RREVFALVPY
RQVRERGFEA QDDGAPLRCL LVDEHLHLPA DEVRAALPAE PLPLHDGGFD LSDDEYAAIV
ERVIAEEIGR GEGANFVIRR DYTARIDAAT PETERIAALT WFRALLEHER GAYWTFAVVT
PGVVAVGASP EAHVVAQGGV VTMNPISGTF RHPAGGSTTA ALGEFLSSAK ETEELFMVVD
EELKMMSAVC SDGGRITGPH LKQMSRLTHT EYMLRGSSRL DPRDILRETM FAPTVTGSPM
QNACTVIRRH ERKPRGYYSG VAALFTPNDA GGHDLDAPIL IRTVYLADGR LSVPVGATLV
RHSDPAGEVG ETHGKAAGVL GAIGAVARDT AAESREDPDA PSPAGTPAED PGIQALLASR
NARLAEFWIN PQDGGAQSTA AAPFAGRTAV VVDAEDRFTT MLAHQLRHLG LEVHIQPWAQ
SDDAEIDAAD LLVAGPGPGD PRDGSSARIA RMRELVARRR ASGRPLLAVC LSHQILADSL
GIELAPLASP HQGLQKSVPV FGQDASIGFY NTFTARVAPG TTAVGVAEVS ADPGSGDVYA
LRGPGFASVQ GHLESILSRD GMTTLQRLVG HALEGR
//
