(data stored in SCRATCH3701 zone)

SWISSPROT: QUED_RICTY

ID   QUED_RICTY              Reviewed;         138 AA.
AC   Q68XI9;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 79.
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=RT0169;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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}.
DR   EMBL; AE017197; AAU03653.1; -; Genomic_DNA.
DR   RefSeq; WP_011190640.1; NC_006142.1.
DR   STRING; 257363.RT0169; -.
DR   EnsemblBacteria; AAU03653; AAU03653; RT0169.
DR   KEGG; rty:RT0169; -.
DR   eggNOG; ENOG4107XVI; Bacteria.
DR   eggNOG; COG0720; LUCA.
DR   HOGENOM; HOG000225068; -.
DR   KO; K01737; -.
DR   OMA; VHGHSYK; -.
DR   OrthoDB; 1770189at2; -.
DR   BioCyc; RTYP257363:G1G0L-173-MONOMER; -.
DR   UniPathway; UPA00391; -.
DR   Proteomes; UP000000604; 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;
DR   PRODOM; Q68XI9.
DR   SWISS-2DPAGE; Q68XI9.
KW   Lyase; Metal-binding; Queuosine biosynthesis; Zinc.
FT   CHAIN           1..138
FT                   /note="6-carboxy-5,6,7,8-tetrahydropterin synthase"
FT                   /id="PRO_0000272632"
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   METAL           14
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
FT   METAL           27
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
FT   METAL           29
FT                   /note="Zinc"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   138 AA;  16192 MW;  90FF8E94F8A22F5D CRC64;
     MIKCTRRIDF DAGHRIIGHK NKCQFLHGHH YVLEITIAAN KTDKLGMVID FGLIKNLAKK
     WIDANFDHNL ILHQDDKEIG KQIENYTGQK IYYMRNNPTA ENIAIHLKNE IFPKLFIDQN
     FFVTSLKLYE TQNCFVEV
//

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