ID A7TE28_VANPO Unreviewed; 488 AA.
AC A7TE28;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 13-SEP-2023, entry version 78.
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=Kpol_1018p188 {ECO:0000313|EMBL:EDO19648.1};
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN [1] {ECO:0000313|EMBL:EDO19648.1, ECO:0000313|Proteomes:UP000000267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480378; EDO19648.1; -; Genomic_DNA.
DR RefSeq; XP_001647506.1; XM_001647456.1.
DR AlphaFoldDB; A7TE28; -.
DR STRING; 436907.A7TE28; -.
DR MEROPS; C26.959; -.
DR GeneID; 5548014; -.
DR KEGG; vpo:Kpol_1018p188; -.
DR eggNOG; KOG0026; Eukaryota.
DR eggNOG; KOG4201; Eukaryota.
DR HOGENOM; CLU_039523_0_0_1; -.
DR InParanoid; A7TE28; -.
DR OMA; FLHMQGG; -.
DR OrthoDB; 294181at2759; -.
DR PhylomeDB; A7TE28; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000000267; 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:UP000000267};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822}.
FT DOMAIN 8..189
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT DOMAIN 218..486
FT /note="Indole-3-glycerol phosphate synthase"
FT /evidence="ECO:0000259|Pfam:PF00218"
FT ACT_SITE 84
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 173
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 175
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 488 AA; 54180 MW; 4BD6F2634C8D3733 CRC64;
MVNKKVILID NYDSFTWNIY EYLCQEGARV DVYRNDKITV EEVANLEPDL LLISPGPGHP
KTDSGISRDC IKYFAGKIPV IGVCMGQQCM FEVFGGEVAF AGEIVHGKTS PIYHDNKGFF
RNVPQGVTVT RYHSLAGTQQ SLPECLEVTA RTDKNIIMGI RHKKYTIEGV QFHPESILTE
EGHLMIKNIL NITGGTWEEN DRNLSLTKTI SNSGNSILDK IYNQRMKDIE ALSATPGFTE
KDLEANFKLG LAPSVINFYD KLSSVTKSAS VIAEIKRASP SKGDIFIDAI ASEQALKYAN
AGASAISVLT EPHWFKGSLE DLRNARKVLD KEYMSHPLAR PCLLRKEFIF SKYQIIEARL
AGADTVLLIV KMLTDERLSE LYNYATKEMN IEPLVEVNSK EELDRALRIG AKVIGVNNRD
LHSFNVDLST TSSLVDSIPK GTILLALSGI CTGADGDRYK KEGVNGFLVG EALMKSKNVE
ELIQQLTE
//