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Database: UniProt
Entry: A0A060QE71_9PROT
LinkDB: A0A060QE71_9PROT
Original site: A0A060QE71_9PROT 
ID   A0A060QE71_9PROT        Unreviewed;       303 AA.
AC   A0A060QE71;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Indole-3-glycerol phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00134};
DE            Short=IGPS {ECO:0000256|HAMAP-Rule:MF_00134};
DE            EC=4.1.1.48 {ECO:0000256|HAMAP-Rule:MF_00134};
GN   Name=trpC {ECO:0000256|HAMAP-Rule:MF_00134};
GN   ORFNames=ASAP_1389 {ECO:0000313|EMBL:CDG39434.1};
OS   Asaia bogorensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Asaia.
OX   NCBI_TaxID=91915 {ECO:0000313|EMBL:CDG39434.1, ECO:0000313|Proteomes:UP000027583};
RN   [1] {ECO:0000313|EMBL:CDG39434.1, ECO:0000313|Proteomes:UP000027583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SF2.1 {ECO:0000313|EMBL:CDG39434.1,
RC   ECO:0000313|Proteomes:UP000027583};
RX   PubMed=24682158; DOI=10.1093/gbe/evu062;
RA   Chouaia B., Gaiarsa S., Crotti E., Comandatore F., Degli Esposti M.,
RA   Ricci I., Alma A., Favia G., Bandi C., Daffonchio D.;
RT   "Acetic acid bacteria genomes reveal functional traits for adaptation to
RT   life in insect guts.";
RL   Genome Biol. Evol. 6:912-920(2014).
RN   [2] {ECO:0000313|EMBL:CDG39434.1, ECO:0000313|Proteomes:UP000027583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SF2.1 {ECO:0000313|EMBL:CDG39434.1,
RC   ECO:0000313|Proteomes:UP000027583};
RX   PubMed=24804722; DOI=10.1371/journal.pone.0096566;
RA   Degli Esposti M., Chouaia B., Comandatore F., Crotti E., Sassera D.,
RA   Lievens P.M., Daffonchio D., Bandi C.;
RT   "Evolution of mitochondria reconstructed from the energy metabolism of
RT   living bacteria.";
RL   PLoS ONE 9:e96566-e96566(2014).
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, ECO:0000256|HAMAP-
CC         Rule:MF_00134};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 4/5. {ECO:0000256|ARBA:ARBA00004696,
CC       ECO:0000256|HAMAP-Rule:MF_00134}.
CC   -!- SIMILARITY: Belongs to the TrpC family. {ECO:0000256|HAMAP-
CC       Rule:MF_00134}.
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:CDG39434.1}.
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DR   EMBL; CBLX010000009; CDG39434.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A060QE71; -.
DR   eggNOG; COG0134; Bacteria.
DR   UniPathway; UPA00035; UER00043.
DR   Proteomes; UP000027583; Unassembled WGS sequence.
DR   GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
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, ECO:0000256|HAMAP-
KW   Rule:MF_00134};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|HAMAP-Rule:MF_00134};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW   Rule:MF_00134};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00134};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, ECO:0000256|HAMAP-
KW   Rule:MF_00134}.
FT   DOMAIN          43..299
FT                   /note="Indole-3-glycerol phosphate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF00218"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   303 AA;  32496 MW;  C40EFA5AC5E53447 CRC64;
     MTDHSSTPTH DTPAGFPDVQ VPGTIVQEET ALPVSGVDMP DVLARICART RIDVEQRSQI
     MPLKEITARA REVSVPTRGF GQALKQMAAD RRVGLIAEIK KASPSAGILR PDFDPVGIAK
     AYEAAGAICL SILTEGSCFH GSIEDLKAVK EICPLPILRK DFILEPWQVH ESRLIGADCI
     LIILSALTDA EAAELIALAR GLDMDVLCEV HDEAELNRAL ALDTSLIGIN NRNLRTLVTD
     LDTTAKLAPL VPPDRILVSE SGIRTLEDVT RVGEVGASGV LVGESLLREQ DPGIAARRLL
     GTL
//
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