GenomeNet

Database: UniProt
Entry: A0A1E7N4K8_KITAU
LinkDB: A0A1E7N4K8_KITAU
Original site: A0A1E7N4K8_KITAU 
ID   A0A1E7N4K8_KITAU        Unreviewed;       506 AA.
AC   A0A1E7N4K8; A0A8H9LML8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Anthranilate synthase component 1 {ECO:0000256|ARBA:ARBA00020653, ECO:0000256|RuleBase:RU364045};
DE            EC=4.1.3.27 {ECO:0000256|ARBA:ARBA00012266, ECO:0000256|RuleBase:RU364045};
GN   Name=trpE {ECO:0000256|RuleBase:RU364045};
GN   ORFNames=GCM10010502_11030 {ECO:0000313|EMBL:GGU62051.1}, HS99_0006695
GN   {ECO:0000313|EMBL:OEV35602.1};
OS   Kitasatospora aureofaciens (Streptomyces aureofaciens).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=1894 {ECO:0000313|EMBL:OEV35602.1, ECO:0000313|Proteomes:UP000037395};
RN   [1] {ECO:0000313|EMBL:OEV35602.1, ECO:0000313|Proteomes:UP000037395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10762 {ECO:0000313|EMBL:OEV35602.1}, and ATCC 10762 / DSM
RC   40127 / CCM 3239 / JCM 4008 / LMG 5968 / NBRC 12843 / NCIMB 8234 /
RC   A-377 {ECO:0000313|Proteomes:UP000037395};
RA   Zhang J.E., Yang H., Guo J., Deng Z., Luo H., Luo M., Zhao B.;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000037395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10762 / DSM 40127 / CCM 3239 / JCM 4008 / LMG 5968 / NBRC
RC   12843 / NCIMB 8234 / A-377 {ECO:0000313|Proteomes:UP000037395};
RA   Gradnigo J.S., Johnson N., Somerville G.A.;
RT   "Sequencing, assembly and comparative genomics of S. aureofaciens ATCC
RT   10762.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:OEV35602.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10762 {ECO:0000313|EMBL:OEV35602.1};
RA   Gradnigo J.S., Johnson N., Somerville G.A.;
RT   "Sequencing, Assembly and Comparative Genomics of S. aureofaciens ATCC
RT   10762.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:GGU62051.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 4434 {ECO:0000313|EMBL:GGU62051.1};
RX   PubMed=30832757;
RA   Wu L., Ma J.;
RT   "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT   project: providing services to taxonomists for standard genome sequencing
RT   and annotation.";
RL   Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN   [5] {ECO:0000313|EMBL:GGU62051.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 4434 {ECO:0000313|EMBL:GGU62051.1};
RA   Sun Q., Ohkuma M.;
RL   Submitted (SEP-2020) 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, 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|ARBA:ARBA00011575, 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:OEV35602.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BMUB01000002; GGU62051.1; -; Genomic_DNA.
DR   EMBL; JPRF03000032; OEV35602.1; -; Genomic_DNA.
DR   RefSeq; WP_030281927.1; NZ_LBHA01000419.1.
DR   AlphaFoldDB; A0A1E7N4K8; -.
DR   STRING; 1894.ADK78_36425; -.
DR   GeneID; 33985843; -.
DR   OrthoDB; 3518032at2; -.
DR   UniPathway; UPA00035; UER00040.
DR   Proteomes; UP000037395; Unassembled WGS sequence.
DR   Proteomes; UP000610124; 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; IPR005256; Anth_synth_I_PabB.
DR   InterPro; IPR015890; Chorismate_C.
DR   NCBIfam; TIGR00564; trpE_most; 1.
DR   PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR   PANTHER; PTHR11236:SF46; 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:UP000037395};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW   ECO:0000256|RuleBase:RU364045}.
FT   DOMAIN          25..167
FT                   /note="Anthranilate synthase component I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04715"
FT   DOMAIN          227..486
FT                   /note="Chorismate-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00425"
SQ   SEQUENCE   506 AA;  53798 MW;  14AE39EDA4367E0C CRC64;
     MDLEAFRKLA VDTRVIPVTR RLLADGLTPI GLYRSLAEER PGTFLLESAE QGVWSRYSFV
     GVRSAAVLTA GPDGGARWLG TPPVGIPTDG DPLEVLRAAL AALHTPRRAD DGLPPLTGGL
     VGYLGYDIVR RLEKLPDLNP DDLRLPELTM LLATDLAVLD HLDGTVLLIA NAVNHNDLAS
     GVDEAYADAV ARLDAMEADL LKPVDPGLAT FTPAGPGEVR SPFGGAPYRA AVEEVKERIR
     AGEAFQVVPS QRFEAPCPAS ALDVYRVLRT TNPSPYMYLF RFPGPDGGAE GGFDVVGSSP
     EALVKVADGE AMLHPIAGTR HRGATPHEDA ALAAELLADP KERAEHLMLV DLGRNDLGRV
     CEPGSVEVVD FMQIERYSHV MHIVSTVTGR VAPGRSAFDV LTACFPAGTL SGAPKPRAMR
     IIEELEPTRR GLYGGCVGYL DFAGDSDTAI AIRTAVLRDG TAYVQAGAGV VADSDPHGED
     TECRNKAAAV LRAVATANTL RRPELS
//
DBGET integrated database retrieval system