GenomeNet

Database: UniProt
Entry: A0A022Q2L3_ERYGU
LinkDB: A0A022Q2L3_ERYGU
Original site: A0A022Q2L3_ERYGU 
ID   A0A022Q2L3_ERYGU        Unreviewed;       397 AA.
AC   A0A022Q2L3;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=indole-3-glycerol-phosphate synthase {ECO:0000256|ARBA:ARBA00012362};
DE            EC=4.1.1.48 {ECO:0000256|ARBA:ARBA00012362};
GN   ORFNames=MIMGU_mgv1a007723mg {ECO:0000313|EMBL:EYU22211.1};
OS   Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX   NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU22211.1, ECO:0000313|Proteomes:UP000030748};
RN   [1] {ECO:0000313|EMBL:EYU22211.1, ECO:0000313|Proteomes:UP000030748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX   PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA   Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA   Schmutz J., Willis J.H., Rokhsar D.S.;
RT   "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT   population shotgun sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 4/5. {ECO:0000256|ARBA:ARBA00004696}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KI632211; EYU22211.1; -; Genomic_DNA.
DR   RefSeq; XP_012855707.1; XM_013000253.1.
DR   AlphaFoldDB; A0A022Q2L3; -.
DR   STRING; 4155.A0A022Q2L3; -.
DR   GeneID; 105975080; -.
DR   KEGG; egt:105975080; -.
DR   eggNOG; KOG4201; Eukaryota.
DR   OMA; REIVWQK; -.
DR   OrthoDB; 294181at2759; -.
DR   PhylomeDB; A0A022Q2L3; -.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000030748; Unassembled WGS sequence.
DR   GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IBA:GO_Central.
DR   GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IBA:GO_Central.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR   CDD; cd00331; IGPS; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00134_B; IGPS_B; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR045186; Indole-3-glycerol_P_synth.
DR   InterPro; IPR013798; Indole-3-glycerol_P_synth_dom.
DR   InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   PANTHER; PTHR22854:SF2; INDOLE-3-GLYCEROL-PHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR22854; TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1.
DR   Pfam; PF00218; IGPS; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR   PROSITE; PS00614; IGPS; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030748};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822}.
FT   DOMAIN          125..388
FT                   /note="Indole-3-glycerol phosphate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF00218"
FT   REGION          35..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   397 AA;  44057 MW;  7F4A9ED77BF4325D CRC64;
     MECMNVISLR ASSSAANSTQ GFSFQQLRKS AFLRPMPPQT RVPNHSPFKH QSFPSVKSQQ
     FEVKDESETD TPKVKEGEIG IYQDEVTASQ GIKIRRRPPT GPPVHYVGPF EFRLQNEGNT
     PRNILEEIVW HKDLELAQMK VKKPLVSLRK LLDNAPPVRD FIGSLKEANL RTGFPGLIAE
     VKKASPSRGV LREDFDPVQI AKAYEKGGAA CLSVLTDEKY FQGSFENLEA IRNSGVQCPL
     LCKEFIIEAY QIYYARAKGA DAILLIAAIL PDLDIKYMLK ISKMLGLTVL VEVHDEREMD
     RVIEIQGIEL IGINNRDLGT FEVDIANTKK LLEGERGQRI REKGITVVGE SGLFTPADIA
     YVQEAGVNAV LVGESLVKQD DPSVGITQLF GKDISSS
//
DBGET integrated database retrieval system