ID A0A0P7HU74_9EURY Unreviewed; 546 AA.
AC A0A0P7HU74;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Anthranilate synthase component 1 {ECO:0000256|RuleBase:RU364045};
DE EC=4.1.3.27 {ECO:0000256|RuleBase:RU364045};
GN Name=trpE_1 {ECO:0000313|EMBL:KPN30184.1};
GN Synonyms=trpE {ECO:0000256|RuleBase:RU364045};
GN ORFNames=SY89_00909 {ECO:0000313|EMBL:KPN30184.1};
OS Halolamina pelagica.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae.
OX NCBI_TaxID=699431 {ECO:0000313|EMBL:KPN30184.1, ECO:0000313|Proteomes:UP000050535};
RN [1] {ECO:0000313|Proteomes:UP000050535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDK2 {ECO:0000313|Proteomes:UP000050535};
RA Hoang H.T., Killian M.L., Madson D.M., Arruda P.H.E., Sun D.,
RA Schwartz K.J., Yoon K.;
RL Submitted (NOV-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|RuleBase:RU364045}.
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 ECO:0000256|RuleBase:RU364045};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|RuleBase:RU364045};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5. {ECO:0000256|ARBA:ARBA00004873,
CC ECO:0000256|RuleBase:RU364045}.
CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a
CC beta subunit (TrpG) and a large alpha subunit (TrpE).
CC {ECO:0000256|RuleBase:RU364045}.
CC -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC {ECO:0000256|ARBA:ARBA00009562, ECO:0000256|RuleBase:RU364045}.
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:KPN30184.1}.
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DR EMBL; LGUC01000001; KPN30184.1; -; Genomic_DNA.
DR RefSeq; WP_054583252.1; NZ_LGUC01000001.1.
DR AlphaFoldDB; A0A0P7HU74; -.
DR STRING; 699431.SY89_00909; -.
DR PATRIC; fig|699431.3.peg.936; -.
DR OrthoDB; 25514at2157; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000050535; Unassembled WGS sequence.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR010116; Anthranilate_synth_I_arc_typ.
DR InterPro; IPR015890; Chorismate_C.
DR NCBIfam; TIGR01820; TrpE-arch; 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 PRINTS; PR00095; ANTSNTHASEI.
DR SUPFAM; SSF56322; ADC synthase; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU364045};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|RuleBase:RU364045};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU364045};
KW Magnesium {ECO:0000256|RuleBase:RU364045};
KW Metal-binding {ECO:0000256|RuleBase:RU364045};
KW Reference proteome {ECO:0000313|Proteomes:UP000050535};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|RuleBase:RU364045}.
FT DOMAIN 86..218
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 271..530
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT REGION 63..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 546 AA; 58048 MW; F5318C44F23C5742 CRC64;
MPAFDHSRDE FEALLAEADG PAVARLTATL DVDTEPLSAY AALSDRSDHT FLLESAEKVA
SSDPAGAFAP ADGHTDPAAG DGDADRHARF SFVGYDPEAL VSVYPDRTEV QGFGPAARFL
DGVDAAAGAE VGACGTELDD PDTLDRLRLA LPDVERVGFE ASDRQRLDGG LVGFLAYDAV
YDLHLAEVGV DRPDPVVPDA QFVLTTRTLA FDDREGTVEL VFTPVVAAGD DAGAVYDRLV
AEAESVAADL AVASTPDPGG FDRERATAGA REEYEAAVAE MQEHVLDGDV YQGVVSRSHE
IEGDLDALGL YESLREVNPS PYMYLLSFGN RSVVGASPET LVSVTGERVV SNPIAGTSAR
GASPVEDRRL AGELLADDKE RAEHTMLVDL ARNDVRQVSR QGSVRVEEFM NVLKYSHVQH
IESTVTGRLA PDFDGFDATR AAFPAGTLTG APKVRAMELL DELEVEPRGV YGGGVGYFSW
TGDADTAIVI RTATVEHGDG DESDAVRVRA GAGVVADSDP ESEYEETEQK VRGVLDALER
IEGGDP
//
