ID   U2RJV3_LEIAQ            Unreviewed;       372 AA.
AC   U2RJV3;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Anthranilate synthase component 1 {ECO:0000256|ARBA:ARBA00020653};
DE            EC=4.1.3.27 {ECO:0000256|ARBA:ARBA00012266};
GN   ORFNames=N136_04490 {ECO:0000313|EMBL:ERK69186.1};
OS   Leifsonia aquatica ATCC 14665.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leifsonia.
OX   NCBI_TaxID=1358026 {ECO:0000313|EMBL:ERK69186.1, ECO:0000313|Proteomes:UP000016605};
RN   [1] {ECO:0000313|EMBL:ERK69186.1, ECO:0000313|Proteomes:UP000016605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14665 {ECO:0000313|EMBL:ERK69186.1,
RC   ECO:0000313|Proteomes:UP000016605};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA   O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA   Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL   Submitted (AUG-2013) 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:ERK69186.1}.
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DR   EMBL; AWVQ01000793; ERK69186.1; -; Genomic_DNA.
DR   AlphaFoldDB; U2RJV3; -.
DR   PATRIC; fig|1358026.3.peg.3652; -.
DR   HOGENOM; CLU_006493_9_2_11; -.
DR   Proteomes; UP000016605; Unassembled WGS sequence.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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   PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR   PANTHER; PTHR11236:SF46; ANTHRANILATE SYNTHASE COMPONENT 1; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   PRINTS; PR00095; ANTSNTHASEI.
DR   SUPFAM; SSF56322; ADC synthase; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000016605}.
FT   DOMAIN          89..347
FT                   /note="Chorismate-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00425"
SQ   SEQUENCE   372 AA;  39904 MW;  61D12B8D9DE5C7C1 CRC64;
     MPDQPPADYD IPGQALAFAA DLAVVDHRSG TVKLIANALA DGAEPAEVLW ADAQARLDRM
     QRELAQPSEA WLAEVDLDTP AEPVSRTREE DFLASVEVAK ERIVAGDIFQ VVISQRFELE
     CSASSLDVYR VLRALNPSPY MYLLSLERPD GGAYQIVGSS PEALVKVQEG RAFTHPIAGS
     RPRGATPEED LELETSLLAD DKERAEHLML VDLARNDLLK VCAAGSVEVT EFMRIERFSH
     IMHIVSSVEG DLLPDASAID VFRATFPAGT LSGAPKPMAL RIIDELEPAQ RGVYGGVIGY
     FDFAGDADLA IAIRTATIMD GVARVQAGGG LVADSVPRSE FQESQNKAAA PLRAVAVANA
     MRRVTGAADG GR
//