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Database: UniProt
Entry: A0A367KRP7_RHIST
LinkDB: A0A367KRP7_RHIST
Original site: A0A367KRP7_RHIST 
ID   A0A367KRP7_RHIST        Unreviewed;       466 AA.
AC   A0A367KRP7;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   13-SEP-2023, entry version 15.
DE   RecName: Full=Multifunctional tryptophan biosynthesis protein {ECO:0000256|ARBA:ARBA00018819};
DE            EC=4.1.1.48 {ECO:0000256|ARBA:ARBA00012362};
DE            EC=4.1.3.27 {ECO:0000256|ARBA:ARBA00012266};
DE   Flags: Fragment;
GN   Name=TRP1_2 {ECO:0000313|EMBL:RCI04851.1};
GN   ORFNames=CU098_013118 {ECO:0000313|EMBL:RCI04851.1};
OS   Rhizopus stolonifer (Rhizopus nigricans).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=4846 {ECO:0000313|EMBL:RCI04851.1, ECO:0000313|Proteomes:UP000253551};
RN   [1] {ECO:0000313|EMBL:RCI04851.1, ECO:0000313|Proteomes:UP000253551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LSU 92-RS-03 {ECO:0000313|EMBL:RCI04851.1,
RC   ECO:0000313|Proteomes:UP000253551};
RX   PubMed=29674435; DOI=10.1534/g3.118.200235;
RA   Gryganskyi A.P., Golan J., Dolatabadi S., Mondo S., Robb S., Idnurm A.,
RA   Muszewska A., Steczkiewicz K., Masonjones S., Liao H.L., Gajdeczka M.T.,
RA   Anike F., Vuek A., Anishchenko I.M., Voigt K., de Hoog G.S., Smith M.E.,
RA   Heitman J., Vilgalys R., Stajich J.E.;
RT   "Phylogenetic and Phylogenomic Definition of Rhizopus Species.";
RL   G3 (Bethesda) 8:2007-2018(2018).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+)
CC         = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O;
CC         Xref=Rhea:RHEA:23476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:58613, ChEBI:CHEBI:58866; EC=4.1.1.48;
CC         Evidence={ECO:0000256|ARBA:ARBA00001633};
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   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 4/5. {ECO:0000256|ARBA:ARBA00004696}.
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:RCI04851.1}.
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DR   EMBL; PJQM01000559; RCI04851.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367KRP7; -.
DR   STRING; 4846.A0A367KRP7; -.
DR   EnsemblFungi; RCI04851; RCI04851; CU098_013118.
DR   UniPathway; UPA00035; UER00040.
DR   Proteomes; UP000253551; Unassembled WGS sequence.
DR   GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR   CDD; cd00331; IGPS; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR013798; Indole-3-glycerol_P_synth_dom.
DR   InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   InterPro; IPR006221; TrpG/PapA_dom.
DR   NCBIfam; TIGR00566; trpG_papA; 1.
DR   PANTHER; PTHR43418:SF4; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1.
DR   PANTHER; PTHR43418; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED; 1.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF00218; IGPS; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00096; GATASE.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
DR   PROSITE; PS00614; IGPS; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253551};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822}.
FT   DOMAIN          4..187
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   DOMAIN          226..466
FT                   /note="Indole-3-glycerol phosphate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF00218"
FT   ACT_SITE        81
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        170
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        172
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   NON_TER         466
FT                   /evidence="ECO:0000313|EMBL:RCI04851.1"
SQ   SEQUENCE   466 AA;  50971 MW;  40AB80632A91C8C9 CRC64;
     MTTLLIDNYD SFTYNVYQYL CSQGADVVVY RNDKITIEEI KQLAPRNIVI SPGPGHPAHD
     AGISREAIAT FAGKIPILGI CMGLQCMFEV YGGTVSYAGT IMHGKASSIK HDSRGVFKGV
     PQNNMVTRYH SLAGMPSTIP DALEVTATTD DGVIMGVRHK EYTVEGVQFH PESILCENGH
     TMILNFLNLQ GGRWEENPGA GVLPQKLRET PPKPVETTTS DAPSILTRIY AQRVKDVEAA
     KEIPGQTMQD LEKLLQLHVA PPLQDVVARI KQQTPALLAE VKRASPSKGS IDATANAAEQ
     ALQYALAGAS VVSVLTEPKW FRGTIHDMRQ VREAITHLPN RPCVLRKDFI VDCYQILEGR
     LYGCDTVLLI VAMLSDEVLH DLYNYSVSLG MEPLVEVNNA EEMARANALG AKLIGVNNRN
     LHSFDVDMET TSRLAEMVPE GTILCALSGI TGRADVEMYV KQGVRG
//
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