ID F9QC85_9PAST Unreviewed; 516 AA.
AC F9QC85;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Anthranilate synthase component 1 {ECO:0000256|PIRNR:PIRNR001373};
DE EC=4.1.3.27 {ECO:0000256|PIRNR:PIRNR001373};
GN Name=trpE {ECO:0000313|EMBL:EGV04864.1};
GN ORFNames=HMPREF9952_1093 {ECO:0000313|EMBL:EGV04864.1};
OS Haemophilus pittmaniae HK 85.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=1035188 {ECO:0000313|EMBL:EGV04864.1, ECO:0000313|Proteomes:UP000006235};
RN [1] {ECO:0000313|EMBL:EGV04864.1, ECO:0000313|Proteomes:UP000006235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK 85 {ECO:0000313|EMBL:EGV04864.1,
RC ECO:0000313|Proteomes:UP000006235};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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|PIRNR:PIRNR001373};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR001373-2};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR001373-2};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5. {ECO:0000256|PIRNR:PIRNR001373}.
CC -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC {ECO:0000256|ARBA:ARBA00009562, ECO:0000256|PIRNR:PIRNR001373}.
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:EGV04864.1}.
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DR EMBL; AFUV01000025; EGV04864.1; -; Genomic_DNA.
DR AlphaFoldDB; F9QC85; -.
DR STRING; 1035188.HMPREF9952_1093; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000006235; 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; IPR005257; Anth_synth_I_TrpE.
DR InterPro; IPR015890; Chorismate_C.
DR NCBIfam; TIGR00565; trpE_proteo; 1.
DR PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR PANTHER; PTHR11236:SF49; ANTHRANILATE SYNTHASE COMPONENT 1; 1.
DR Pfam; PF04715; Anth_synt_I_N; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR PIRSF; PIRSF001373; TrpE; 1.
DR PRINTS; PR00095; ANTSNTHASEI.
DR SUPFAM; SSF56322; ADC synthase; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR001373,
KW ECO:0000256|PIRSR:PIRSR001373-1};
KW Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001373};
KW Lyase {ECO:0000256|PIRNR:PIRNR001373, ECO:0000313|EMBL:EGV04864.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR001373-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001373-2};
KW Tryptophan biosynthesis {ECO:0000256|PIRNR:PIRNR001373,
KW ECO:0000256|PIRSR:PIRSR001373-1}.
FT DOMAIN 21..194
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 242..500
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT BINDING 39
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 289..291
FT /ligand="L-tryptophan"
FT /ligand_id="ChEBI:CHEBI:57912"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-2"
FT BINDING 447
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 467
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 481..483
FT /ligand="chorismate"
FT /ligand_id="ChEBI:CHEBI:29748"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT BINDING 496
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR001373-2"
SQ SEQUENCE 516 AA; 57072 MW; 2028BE762DDD50A1 CRC64;
MKNAPFIAVT SQPVPYHADT TAIFNTLCQQ NSNSLLLDSA EIGSKNSLQS LILINAAVKI
ICLGNQVTFK ALNANGKQVL KEIHPVLSQL GTSNTAKVEE EFSVQFAPLD NQLDEDSKLQ
AATIFDGLRV ISNHYQHSST PIFLGGLFAY DLVANFIPMQ GIALQDDGIS CPDYSFYLAE
NLITIDHQSQ QATLKSFCFS QEEQVEVAKT ALSIAQKLKN IDGVLSIKAA SDEISTNFED
PEFIGIVKAL KHHINIGDVF QIVPSRRFSL ACPNTLASYA QLKHNNPSPY MFYMNDEDFI
LFGASPESAL KYAPENRQLE IYPIAGSRPR GFDAHGNIDP ELDARLELEL RLDHKEQAEH
LMLVDLARND IARVCQSGTR KVAELMQVDR YSHIMHLVSR VVGKLRPELD ALHAYQACMN
MGTLTGAPKI KAMQLIYQFE QQKRHSYGGA VGYLTSDGHF DTCIVIRSAF VQHGIAHIQA
GCGEVLDSDP QMEADETRHK AAAVLKAIRQ INTQAK
//
