QUED_HAEIN
ID QUED_HAEIN Reviewed; 141 AA.
AC P44123;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=HI_1190;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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; L42023; AAC22843.1; -; Genomic_DNA.
DR PIR; F64021; F64021.
DR RefSeq; NP_439346.1; NC_000907.1.
DR RefSeq; WP_005663812.1; NC_000907.1.
DR AlphaFoldDB; P44123; -.
DR SMR; P44123; -.
DR STRING; 71421.HI_1190; -.
DR EnsemblBacteria; AAC22843; AAC22843; HI_1190.
DR KEGG; hin:HI_1190; -.
DR PATRIC; fig|71421.8.peg.1242; -.
DR eggNOG; COG0720; Bacteria.
DR HOGENOM; CLU_111016_1_1_6; -.
DR OMA; HATVFNK; -.
DR PhylomeDB; P44123; -.
DR BioCyc; HINF71421:G1GJ1-1221-MON; -.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0070497; F:6-carboxy-5,6,7,8-tetrahydropterin synthase activity; IBA:GO_Central.
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.
DR PIRSF; PIRSF006113; PTP_synth; 1.
DR TIGRFAMs; TIGR00039; 6PTHBS; 1.
DR TIGRFAMs; TIGR03367; queuosine_QueD; 1.
PE 3: Inferred from homology;
KW Lyase; Metal-binding; Queuosine biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..141
FT /note="6-carboxy-5,6,7,8-tetrahydropterin synthase"
FT /id="PRO_0000057925"
FT ACT_SITE 23
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 71
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 131
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 141 AA; 16322 MW; 6843517DEA5A7C3E CRC64;
MFKISKEFSF DMAHLLDGHD GKCQNLHGHT YKLQVEISGD LYKSGAKKAM VIDFSDLKSI
VKKVILDPMD HAFIYDQTNE RESQIATLLQ KLNSKTFGVP FRTTAEEIAR FIFNRLKHDE
QLSISSIRLW ETPTSFCEYQ E