ID G3APZ8_SPAPN Unreviewed; 510 AA.
AC G3APZ8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
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};
GN ORFNames=SPAPADRAFT_55801 {ECO:0000313|EMBL:EGW32319.1};
OS Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN [1] {ECO:0000313|EMBL:EGW32319.1, ECO:0000313|Proteomes:UP000000709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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}.
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DR EMBL; GL996502; EGW32319.1; -; Genomic_DNA.
DR RefSeq; XP_007375595.1; XM_007375533.1.
DR AlphaFoldDB; G3APZ8; -.
DR STRING; 619300.G3APZ8; -.
DR MEROPS; C26.959; -.
DR GeneID; 18871974; -.
DR KEGG; spaa:SPAPADRAFT_55801; -.
DR eggNOG; KOG0026; Eukaryota.
DR eggNOG; KOG4201; Eukaryota.
DR HOGENOM; CLU_039523_0_0_1; -.
DR InParanoid; G3APZ8; -.
DR OMA; EPIEWAN; -.
DR OrthoDB; 294181at2759; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000000709; 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; PR00099; CPSGATASE.
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:UP000000709};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822}.
FT DOMAIN 9..194
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 222..499
FT /note="Indole-3-glycerol phosphate synthase"
FT /evidence="ECO:0000259|Pfam:PF00218"
FT ACT_SITE 88
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 179
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 181
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 510 AA; 56821 MW; 6C1796BD31C199BA CRC64;
MTESKRHVLM IDNYDSFTWN LYQFLHQSPK CGKVDVYRND KIDIPTIEKL NPDIIFISPG
PGHPLTDSGV SSDVIRHFSG KLPIFGVCMG QECIFDVFGG DVSYAGEIVH GKTTTISHDG
KGFFENVPQS VAVTRYHSLA GSQKTLPECL EVTAMTETSP KVIMGVRHKK YTIEGVQFHP
ESILTECGQL MIDNLLGVHG GTWEENDAIT KGNNISKSEN ILTKIYKQRQ LDYQEIEKLP
GKSFEQLETE LSLGVAPPAI NFYDRLKYTQ NKKQTPILSE FKRASPSKGN ININAHPGVQ
ALTYANNGCS TISVLTEPNW FKGSLHDLTL IRKVIDKPDS ETYKRPAVLR KEFIFSKYQI
LEARLAGADT VLLIVKMLED EQLLQELYEY SLSLGMVPLV EVNNSTELSQ ALKLTNNGNT
NDPLIIGVNN RNLTTFDVDL NTTSSLVDTA KSSPRKGEVL VLALSGITTV EDVKKYKYED
NVDGFLIGES LMRAEEKGKA GEFLHDLCNC
//
