GenomeNet

Database: UniProt
Entry: I4MXM9_9PSED
LinkDB: I4MXM9_9PSED
Original site: I4MXM9_9PSED 
ID   I4MXM9_9PSED            Unreviewed;       118 AA.
AC   I4MXM9;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=6-carboxy-5,6,7,8-tetrahydropterin synthase {ECO:0000256|ARBA:ARBA00018141, ECO:0000256|PIRNR:PIRNR006113};
DE            EC=4.-.-.- {ECO:0000256|PIRNR:PIRNR006113};
GN   ORFNames=PMM47T1_24583 {ECO:0000313|EMBL:EIK93969.1};
OS   Pseudomonas sp. M47T1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1179778 {ECO:0000313|EMBL:EIK93969.1, ECO:0000313|Proteomes:UP000004339};
RN   [1] {ECO:0000313|EMBL:EIK93969.1, ECO:0000313|Proteomes:UP000004339}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M47T1 {ECO:0000313|EMBL:EIK93969.1,
RC   ECO:0000313|Proteomes:UP000004339};
RX   PubMed=22887683; DOI=10.1128/JB.01116-12;
RA   Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT   "Draft Genome Sequence of Pseudomonas sp. Strain M47T1, Carried by
RT   Bursaphelenchus xylophilus Isolated from Pinus pinaster.";
RL   J. Bacteriol. 194:4789-4790(2012).
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         ECO:0000256|PIRNR:PIRNR006113};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006113,
CC         ECO:0000256|PIRSR:PIRSR006113-2};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR006113,
CC       ECO:0000256|PIRSR:PIRSR006113-2};
CC   -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005061, ECO:0000256|PIRNR:PIRNR006113}.
CC   -!- SIMILARITY: Belongs to the PTPS family. QueD subfamily.
CC       {ECO:0000256|ARBA:ARBA00008900, ECO:0000256|PIRNR:PIRNR006113}.
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:EIK93969.1}.
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; AJWX01000030; EIK93969.1; -; Genomic_DNA.
DR   RefSeq; WP_008374030.1; NZ_AJWX01000030.1.
DR   AlphaFoldDB; I4MXM9; -.
DR   STRING; 1179778.PMM47T1_24583; -.
DR   PATRIC; fig|1179778.3.peg.4887; -.
DR   eggNOG; COG0720; Bacteria.
DR   OrthoDB; 9804698at2; -.
DR   UniPathway; UPA00391; -.
DR   Proteomes; UP000004339; Unassembled WGS sequence.
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   GO; GO:0008616; P:queuosine biosynthetic process; 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   NCBIfam; TIGR03367; queuosine_QueD; 1.
DR   PANTHER; PTHR12589:SF7; 6-PYRUVOYL TETRAHYDROBIOPTERIN SYNTHASE; 1.
DR   PANTHER; PTHR12589; PYRUVOYL TETRAHYDROBIOPTERIN SYNTHASE; 1.
DR   Pfam; PF01242; PTPS; 1.
DR   PIRSF; PIRSF006113; PTP_synth; 1.
DR   SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR006113};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR006113};
KW   Queuosine biosynthesis {ECO:0000256|PIRNR:PIRNR006113};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004339};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR006113}.
FT   ACT_SITE        24
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006113-1"
FT   ACT_SITE        68
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006113-1"
FT   ACT_SITE        107
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006113-1"
FT   BINDING         13
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006113-2"
FT   BINDING         28
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006113-2"
FT   BINDING         30
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006113-2"
SQ   SEQUENCE   118 AA;  13635 MW;  7EEE1E5AF9400C3D CRC64;
     MEIFKEFTFE SAHRLPHVPE GHKCGRLHGH SFKVALHLTG PVDPHTGWIR DFSEIKAIFK
     PLYEQLDHNY LNDIPGLENP TSEVLAKWIW NQVKPLLPEL SKVRIHETCT SGCEYYGD
//
DBGET integrated database retrieval system