QUED_AQUAE
ID QUED_AQUAE Reviewed; 162 AA.
AC O66626;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=6-carboxy-5,6,7,8-tetrahydropterin synthase;
DE Short=CPH4 synthase;
DE EC=4.1.2.50;
DE AltName: Full=Queuosine biosynthesis protein QueD;
GN Name=queD; OrderedLocusNames=aq_269;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-dihydroneopterin 3'-triphosphate + H2O = 6-carboxy-
CC 5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) + triphosphate;
CC Xref=Rhea:RHEA:27966, ChEBI:CHEBI:15343, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18036, ChEBI:CHEBI:58462,
CC ChEBI:CHEBI:61032; EC=4.1.2.50;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
CC -!- MISCELLANEOUS: The active site is at the interface between 2 subunits.
CC The proton acceptor Cys is on one subunit, and the charge relay system
CC is on the other subunit (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PTPS family. QueD subfamily. {ECO:0000305}.
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DR EMBL; AE000657; AAC06591.1; -; Genomic_DNA.
DR PIR; F70324; F70324.
DR RefSeq; NP_213186.1; NC_000918.1.
DR RefSeq; WP_010880124.1; NC_000918.1.
DR AlphaFoldDB; O66626; -.
DR SMR; O66626; -.
DR STRING; 224324.aq_269; -.
DR EnsemblBacteria; AAC06591; AAC06591; aq_269.
DR KEGG; aae:aq_269; -.
DR eggNOG; COG0720; Bacteria.
DR HOGENOM; CLU_111016_1_2_0; -.
DR InParanoid; O66626; -.
DR OMA; HATVFNK; -.
DR OrthoDB; 1770189at2; -.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000000798; 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; -; 1.
DR InterPro; IPR007115; 6-PTP_synth/QueD.
DR InterPro; IPR038418; 6-PTP_synth/QueD_sf.
DR PANTHER; PTHR12589; PTHR12589; 1.
DR Pfam; PF01242; PTPS; 1.
PE 3: Inferred from homology;
KW Lyase; Metal-binding; Queuosine biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..162
FT /note="6-carboxy-5,6,7,8-tetrahydropterin synthase"
FT /id="PRO_0000057920"
FT ACT_SITE 39
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 83
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 151
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 162 AA; 18719 MW; CEA62835FA26773B CRC64;
MKWEISKTFR FEAGHRVWKQ NLTYGRGAQF TKEKPVNKCV NLHGHSYVLE VTVGSDTLSE
QDMVMDFYHV KNALKGLIEE IDHSFIIDVN DPMYPELKDV AEKYGAMKIF PVEFCPTAEA
LAKFFYDFLK KRLEEAGLLG EVKVVKVVLW ETATSKAEYK EE
