ID Q1IAJ5_PSEE4 Unreviewed; 175 AA.
AC Q1IAJ5;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=6-carboxy-5,6,7,8-tetrahydropterin synthase {ECO:0000256|ARBA:ARBA00018141};
DE EC=4.1.2.50 {ECO:0000256|ARBA:ARBA00012982};
DE AltName: Full=Queuosine biosynthesis protein QueD {ECO:0000256|ARBA:ARBA00031449};
GN OrderedLocusNames=PSEEN2520 {ECO:0000313|EMBL:CAK15324.1};
OS Pseudomonas entomophila (strain L48).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=384676 {ECO:0000313|EMBL:CAK15324.1, ECO:0000313|Proteomes:UP000000658};
RN [1] {ECO:0000313|EMBL:CAK15324.1, ECO:0000313|Proteomes:UP000000658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L48 {ECO:0000313|EMBL:CAK15324.1,
RC ECO:0000313|Proteomes:UP000000658};
RX PubMed=16699499; DOI=10.1038/nbt1212;
RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT "Complete genome sequence of the entomopathogenic and metabolically
RT versatile soil bacterium Pseudomonas entomophila.";
RL Nat. Biotechnol. 24:673-679(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-dihydroneopterin 3'-triphosphate + H2O = 6-
CC carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) +
CC triphosphate; Xref=Rhea:RHEA:27966, ChEBI:CHEBI:15343,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18036,
CC ChEBI:CHEBI:58462, ChEBI:CHEBI:61032; EC=4.1.2.50;
CC Evidence={ECO:0000256|ARBA:ARBA00001293};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005061}.
CC -!- SIMILARITY: Belongs to the PTPS family. QueD subfamily.
CC {ECO:0000256|ARBA:ARBA00008900}.
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; CT573326; CAK15324.1; -; Genomic_DNA.
DR RefSeq; WP_011533721.1; NC_008027.1.
DR AlphaFoldDB; Q1IAJ5; -.
DR STRING; 384676.PSEEN2520; -.
DR GeneID; 32805690; -.
DR KEGG; pen:PSEEN2520; -.
DR eggNOG; COG0720; Bacteria.
DR HOGENOM; CLU_111016_1_1_6; -.
DR OrthoDB; 9804698at2; -.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000000658; Chromosome.
DR GO; GO:0070497; F:6-carboxy-5,6,7,8-tetrahydropterin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.479.10; 6-pyruvoyl tetrahydropterin synthase/QueD; 1.
DR InterPro; IPR007115; 6-PTP_synth/QueD.
DR InterPro; IPR038418; 6-PTP_synth/QueD_sf.
DR PANTHER; PTHR12589:SF7; 6-PYRUVOYL TETRAHYDROBIOPTERIN SYNTHASE; 1.
DR PANTHER; PTHR12589; PYRUVOYL TETRAHYDROBIOPTERIN SYNTHASE; 1.
DR Pfam; PF01242; PTPS; 1.
DR SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 175 AA; 19285 MW; 8DEC6201E76859BF CRC64;
MFKIDRKIEI DAGHRIRSHG SKCRNLHGHR YSVHMTCSAD ELATHGSETG MVLDFSFAKD
AMVQCIDELC DHALIVDAED EYLLQVLDIH GPARDVRTSG VALPLTNGEG MKIYLVPFSP
TAEALAKHWY ELLSDKVATL GHGAAQVRVD TIRVYETPNC WAEYPAGNVG GAQHV
//
