QUED_RICCN
ID QUED_RICCN Reviewed; 138 AA.
AC Q92J44;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 88.
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=RC0225;
OS Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=272944;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-613 / Malish 7;
RX PubMed=11557893; DOI=10.1126/science.1061471;
RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL Science 293:2093-2098(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: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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL02763.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE006914; AAL02763.1; ALT_INIT; Genomic_DNA.
DR PIR; A97728; A97728.
DR RefSeq; WP_004996555.1; NC_003103.1.
DR AlphaFoldDB; Q92J44; -.
DR SMR; Q92J44; -.
DR EnsemblBacteria; AAL02763; AAL02763; RC0225.
DR GeneID; 57451950; -.
DR KEGG; rco:RC0225; -.
DR HOGENOM; CLU_111016_1_1_5; -.
DR OMA; HATVFNK; -.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000000816; 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; Zinc.
FT CHAIN 1..138
FT /note="6-carboxy-5,6,7,8-tetrahydropterin synthase"
FT /id="PRO_0000272630"
FT ACT_SITE 23
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 68
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 130
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 138 AA; 16144 MW; BFCB0BF13349B9FD CRC64;
MIKCTRRIEF DAGHRIIEHQ NKCQFLHGHR YVLEIAIAAN KTDKLGMVID FGLIKDLAKK
WIDENFDHSL ILHQDDKEMG QQIENCTGQK IYYMQNNPTA ENIATHLKNE IFPKLFVSQN
FFVTSLKLYE TPNCFVEV
