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Database: UniProt
Entry: H9UM38_SPIAZ
LinkDB: H9UM38_SPIAZ
Original site: H9UM38_SPIAZ 
ID   H9UM38_SPIAZ            Unreviewed;       469 AA.
AC   H9UM38;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 47.
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   OrderedLocusNames=Spiaf_2551 {ECO:0000313|EMBL:AFG38581.1};
OS   Spirochaeta africana (strain ATCC 700263 / DSM 8902 / Z-7692).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC   Spirochaeta.
OX   NCBI_TaxID=889378 {ECO:0000313|EMBL:AFG38581.1, ECO:0000313|Proteomes:UP000007383};
RN   [1] {ECO:0000313|Proteomes:UP000007383}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 700263 / DSM 8902 / Z-7692
RC   {ECO:0000313|Proteomes:UP000007383};
RX   PubMed=23991249; DOI=10.4056/sigs.3607108;
RA   Liolos K., Abt B., Scheuner C., Teshima H., Held B., Lapidus A., Nolan M.,
RA   Lucas S., Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S.,
RA   Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Huntemann M., Pati A.,
RA   Chen A., Palaniappan K., Land M., Rohde M., Tindall B.J., Detter J.C.,
RA   Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Woyke T.,
RA   Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of the halophilic bacterium Spirochaeta africana
RT   type strain (Z-7692(T)) from the alkaline Lake Magadi in the East African
RT   Rift.";
RL   Stand. Genomic Sci. 8:165-176(2013).
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|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}.
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DR   EMBL; CP003282; AFG38581.1; -; Genomic_DNA.
DR   RefSeq; WP_014456563.1; NC_017098.1.
DR   AlphaFoldDB; H9UM38; -.
DR   STRING; 889378.Spiaf_2551; -.
DR   KEGG; sfc:Spiaf_2551; -.
DR   PATRIC; fig|889378.3.peg.2527; -.
DR   eggNOG; COG0147; Bacteria.
DR   HOGENOM; CLU_006493_9_2_12; -.
DR   OMA; SRVMHIV; -.
DR   OrthoDB; 9803598at2; -.
DR   UniPathway; UPA00035; UER00040.
DR   Proteomes; UP000007383; Chromosome.
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: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:UP000007383};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW   ECO:0000256|RuleBase:RU364045}.
FT   DOMAIN          18..153
FT                   /note="Anthranilate synthase component I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04715"
FT   DOMAIN          202..455
FT                   /note="Chorismate-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00425"
SQ   SEQUENCE   469 AA;  53092 MW;  9CFE1C24E3D9D9E8 CRC64;
     MQKRQDGIVK IMPGERFTPF GLAKKLSARA MLESSSYQRG RERYSVLMVD EAFRVEQRGS
     KVLFRCGDQV SRIRSSARDI LGVLRYFADQ HTPLHQDFPY PAGGVGYLSY EFARMCDSVQ
     FRKKRDPLDL PDASFLFGHV FVIFDHYTDL LYLIGLNYAE HEVDLPSAVA KVEARINDLN
     FTYLQQDERS YTAEVVNPGA DREDYLAGVR QVRQEIIRGN LLQGVLSRRV QVKTDMDALE
     AYRRLRTTNP SPYLFYIDFN EYQLFGSSPE MHVKVKEDEV TIRPIAGTRR RGEDQAQDEA
     LAQELLGDEK ERAEHLMLID LARNDIGRVC EPGSVEVVEN MAIERFSRVM HIVSKVKGRL
     LPGKTGVEAI RATFPAGTVS GAPKISAMQI IDGIEPIQRK FYAGLVGYME PEGNLDTCIT
     IRSALCRDGN FYLQAGAGVV FDSTPEREYQ ETEEKLSALM RALGLEVQS
//
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