ID Q9A3P4_CAUVC Unreviewed; 121 AA.
AC Q9A3P4;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 100.
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 OrderedLocusNames=CC_3158 {ECO:0000313|EMBL:AAK25120.1};
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650 {ECO:0000313|EMBL:AAK25120.1, ECO:0000313|Proteomes:UP000001816};
RN [1] {ECO:0000313|EMBL:AAK25120.1, ECO:0000313|Proteomes:UP000001816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15 {ECO:0000313|Proteomes:UP000001816};
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R., Ohta N., Maddock J.R., Potocka I.,
RA Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B., DeBoy R.T.,
RA Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F., Smit J.,
RA Craven M.B., Khouri H., Shetty J., Berry K., Utterback T., Tran K.,
RA Wolf A., Vamathevan J., Ermolaeva M., White O., Salzberg S.L., Venter J.C.,
RA Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
CC -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin triphosphate
CC (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde.
CC {ECO:0000256|ARBA:ARBA00002285}.
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}.
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DR EMBL; AE005673; AAK25120.1; -; Genomic_DNA.
DR PIR; D87640; D87640.
DR RefSeq; NP_421952.1; NC_002696.2.
DR RefSeq; WP_010920994.1; NC_002696.2.
DR AlphaFoldDB; Q9A3P4; -.
DR SMR; Q9A3P4; -.
DR STRING; 190650.CC_3158; -.
DR EnsemblBacteria; AAK25120; AAK25120; CC_3158.
DR KEGG; ccr:CC_3158; -.
DR PATRIC; fig|190650.5.peg.3167; -.
DR eggNOG; COG0720; Bacteria.
DR HOGENOM; CLU_111016_6_1_5; -.
DR BioCyc; CAULO:CC3158-MONOMER; -.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000001816; 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 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 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:UP000001816};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR006113}.
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR006113-2"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR006113-2"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR006113-2"
SQ SEQUENCE 121 AA; 13537 MW; 86DE035A6D4C292D CRC64;
MKPVFEITKA AYFDAAHYIE QGPSDHRYRR LHGHSFKVEV SVRGEMLDAG WVADLDTLDV
ALKAVAVELD HGLLNDKPGL EVPTLERLCL YFAERLRSQF PGLSRVALSR PTIGETCVLS
L
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