ID A0A0U2U6T9_9CREN Unreviewed; 535 AA.
AC A0A0U2U6T9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=indole-3-glycerol-phosphate synthase {ECO:0000256|ARBA:ARBA00012362};
DE EC=4.1.1.48 {ECO:0000256|ARBA:ARBA00012362};
GN ORFNames=EYM_05505 {ECO:0000313|EMBL:ALU11860.1};
OS Ignicoccus islandicus DSM 13165.
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Ignicoccus.
OX NCBI_TaxID=940295 {ECO:0000313|EMBL:ALU11860.1, ECO:0000313|Proteomes:UP000060778};
RN [1] {ECO:0000313|EMBL:ALU11860.1, ECO:0000313|Proteomes:UP000060778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13165 {ECO:0000313|EMBL:ALU11860.1,
RC ECO:0000313|Proteomes:UP000060778};
RA Podar M.;
RT "Comparative genomics of Ignicoccus.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP006867; ALU11860.1; -; Genomic_DNA.
DR RefSeq; WP_075050015.1; NZ_CP006867.1.
DR AlphaFoldDB; A0A0U2U6T9; -.
DR STRING; 940295.EYM_05505; -.
DR GeneID; 30680484; -.
DR KEGG; iis:EYM_05505; -.
DR PATRIC; fig|940295.4.peg.1058; -.
DR OrthoDB; 372037at2157; -.
DR UniPathway; UPA00035; UER00043.
DR Proteomes; UP000060778; Chromosome.
DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00885; cinA; 1.
DR CDD; cd00331; IGPS; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.40.980.10; MoaB/Mog-like domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR013798; Indole-3-glycerol_P_synth_dom.
DR InterPro; IPR036425; MoaB/Mog-like_dom_sf.
DR InterPro; IPR001453; MoaB/Mog_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR NCBIfam; TIGR00177; molyb_syn; 1.
DR PANTHER; PTHR13939; NICOTINAMIDE-NUCLEOTIDE AMIDOHYDROLASE PNCC; 1.
DR PANTHER; PTHR13939:SF0; NICOTINAMIDE-NUCLEOTIDE AMIDOHYDROLASE PNCC; 1.
DR Pfam; PF00218; IGPS; 1.
DR Pfam; PF00994; MoCF_biosynth; 1.
DR SMART; SM00852; MoCF_biosynth; 1.
DR SUPFAM; SSF53218; Molybdenum cofactor biosynthesis proteins; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000060778}.
FT DOMAIN 12..182
FT /note="MoaB/Mog"
FT /evidence="ECO:0000259|SMART:SM00852"
SQ SEQUENCE 535 AA; 59920 MW; 1E8B903B5D34163F CRC64;
MTNPYLKKWS AAILVIGNEV LVGRITDTNS QKIARVLTTL GFDVVEIRKV RDDIDAIAEA
VKELCYDAGV VITTGGLGPT YDDVTAEAIA YAIGSPLCLN EEALEMVRNK LREIYGQEIE
EVDEVRRKMA VLPCLAQPIP NKVGVAPGIY VKLNRCKIFS LPGVPREMEA MLNEFVTEEL
QKENLYAKVE VCERLEDVRE AELAPLLKKF AEVYPDVYIK SHPGIEGERS FVRVCVLASG
PTKENAQEKA QKVLSEFLKR SRRRLEIEMI EEIVNYTLNR IEFERKSLAL PKRDKKGVID
FRASLEKDAF SIITEFKPSS PSGVRAKWAP IDYVNEVRPC SSAFSVLTEP KWFKGSYENL
RLISSITDKP ILMKDFVVDP FQIDIAYAFG ADAVLLMVDV LGEDELSYLA RKAKARGLQT
LVEVSNKEDL VIYDKKPYVD VLGMNSRDFK TLKVDINRLH DGGFLIRRAF PLAESGVKSP
EDAMKVASWG FRGALVGTSL MESNAPRELC VELKRKGSEA LSARLRSRGL TPSVL
//
