QUED_ECOLI
ID QUED_ECOLI Reviewed; 121 AA.
AC P65870; Q2MA64; Q46903;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
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; Synonyms=ygcM; OrderedLocusNames=b2765, JW2735;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP FUNCTION AS A CPH4 SYNTHASE, CATALYTIC ACTIVITY, COFACTOR, AND REACTION
RP MECHANISM.
RX PubMed=19231875; DOI=10.1021/bi9001437;
RA McCarty R.M., Somogyi A., Bandarian V.;
RT "Escherichia coli QueD is a 6-carboxy-5,6,7,8-tetrahydropterin synthase.";
RL Biochemistry 48:2301-2303(2009).
CC -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin triphosphate
CC (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde.
CC Can also convert 6-pyruvoyltetrahydropterin (PPH4) and sepiapterin to
CC CPH4; these 2 compounds are probably intermediates in the reaction from
CC H2NTP. {ECO:0000269|PubMed:19231875}.
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 Evidence={ECO:0000269|PubMed:19231875};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:19231875};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:19231875};
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; U29579; AAA69275.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75807.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76842.1; -; Genomic_DNA.
DR PIR; A65058; A65058.
DR RefSeq; NP_417245.1; NC_000913.3.
DR RefSeq; WP_000987944.1; NZ_CP011343.2.
DR PDB; 3QN0; X-ray; 2.34 A; A/B/C/D/E/F=1-121.
DR PDB; 3QN9; X-ray; 2.93 A; A/B=1-121.
DR PDB; 3QNA; X-ray; 2.50 A; A/B/C/D/E/F=1-121.
DR PDB; 4NTK; X-ray; 1.60 A; A/B/C/D/E/F=1-121.
DR PDB; 4NTM; X-ray; 2.05 A; A/B/C/D/E/F=1-121.
DR PDB; 4NTN; X-ray; 1.99 A; A/B/C/D/E/F=1-121.
DR PDBsum; 3QN0; -.
DR PDBsum; 3QN9; -.
DR PDBsum; 3QNA; -.
DR PDBsum; 4NTK; -.
DR PDBsum; 4NTM; -.
DR PDBsum; 4NTN; -.
DR AlphaFoldDB; P65870; -.
DR SMR; P65870; -.
DR BioGRID; 4262288; 21.
DR IntAct; P65870; 3.
DR STRING; 511145.b2765; -.
DR PaxDb; P65870; -.
DR PRIDE; P65870; -.
DR EnsemblBacteria; AAC75807; AAC75807; b2765.
DR EnsemblBacteria; BAE76842; BAE76842; BAE76842.
DR GeneID; 945123; -.
DR KEGG; ecj:JW2735; -.
DR KEGG; eco:b2765; -.
DR PATRIC; fig|1411691.4.peg.3972; -.
DR EchoBASE; EB2921; -.
DR eggNOG; COG0720; Bacteria.
DR HOGENOM; CLU_111016_6_1_6; -.
DR InParanoid; P65870; -.
DR OMA; KCEKLHG; -.
DR PhylomeDB; P65870; -.
DR BioCyc; EcoCyc:G7431-MON; -.
DR BioCyc; MetaCyc:G7431-MON; -.
DR BRENDA; 4.1.2.50; 2026.
DR UniPathway; UPA00391; -.
DR PRO; PR:P65870; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0070497; F:6-carboxy-5,6,7,8-tetrahydropterin synthase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0008616; P:queuosine biosynthetic process; IMP:EcoCyc.
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.
DR PIRSF; PIRSF006113; PTP_synth; 1.
DR TIGRFAMs; TIGR00039; 6PTHBS; 1.
DR TIGRFAMs; TIGR03367; queuosine_QueD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Metal-binding; Queuosine biosynthesis;
KW Reference proteome; Zinc.
FT CHAIN 1..121
FT /note="6-carboxy-5,6,7,8-tetrahydropterin synthase"
FT /id="PRO_0000057922"
FT ACT_SITE 27
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 71
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 110
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT STRAND 3..16
FT /evidence="ECO:0007829|PDB:4NTK"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:4NTK"
FT STRAND 29..42
FT /evidence="ECO:0007829|PDB:4NTK"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:4NTK"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:4NTK"
FT HELIX 55..69
FT /evidence="ECO:0007829|PDB:4NTK"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:4NTK"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:4NTK"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:4NTK"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:4NTK"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:4NTK"
SQ SEQUENCE 121 AA; 13773 MW; DEF4F2A2E72CFF0D CRC64;
MMSTTLFKDF TFEAAHRLPH VPEGHKCGRL HGHSFMVRLE ITGEVDPHTG WIIDFAELKA
AFKPTYERLD HHYLNDIPGL ENPTSEVLAK WIWDQVKPVV PLLSAVMVKE TCTAGCIYRG
E
