ID A0A124ID88_9ACTN Unreviewed; 132 AA.
AC A0A124ID88;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=6-carboxy-5,6,7,8-tetrahydropterin synthase {ECO:0000256|ARBA:ARBA00018141};
DE EC=4.1.2.50 {ECO:0000256|ARBA:ARBA00012982};
DE AltName: Full=Queuosine biosynthesis protein QueD {ECO:0000256|ARBA:ARBA00031449};
GN ORFNames=AQJ91_47070 {ECO:0000313|EMBL:KUO14392.1};
OS Streptomyces dysideae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=909626 {ECO:0000313|EMBL:KUO14392.1, ECO:0000313|Proteomes:UP000053260};
RN [1] {ECO:0000313|EMBL:KUO14392.1, ECO:0000313|Proteomes:UP000053260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RV15 {ECO:0000313|EMBL:KUO14392.1,
RC ECO:0000313|Proteomes:UP000053260};
RA Ruckert C., Abdelmohsen U.R., Winkler A., Hentschel U., Kalinowski J.,
RA Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces sp. RV15, isolated from a marine
RT sponge.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7,8-dihydroneopterin 3'-triphosphate + H2O = 6-
CC carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + 2 H(+) +
CC triphosphate; Xref=Rhea:RHEA:27966, ChEBI:CHEBI:15343,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18036,
CC ChEBI:CHEBI:58462, ChEBI:CHEBI:61032; EC=4.1.2.50;
CC Evidence={ECO:0000256|ARBA:ARBA00001293};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005061}.
CC -!- SIMILARITY: Belongs to the PTPS family. QueD subfamily.
CC {ECO:0000256|ARBA:ARBA00008900}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUO14392.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMXB01000153; KUO14392.1; -; Genomic_DNA.
DR RefSeq; WP_067036162.1; NZ_KQ949143.1.
DR AlphaFoldDB; A0A124ID88; -.
DR STRING; 909626.AQJ91_47070; -.
DR OrthoDB; 9787853at2; -.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000053260; Unassembled WGS sequence.
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 Gene3D; 3.30.479.10; 6-pyruvoyl tetrahydropterin synthase/QueD; 1.
DR InterPro; IPR007115; 6-PTP_synth/QueD.
DR InterPro; IPR038418; 6-PTP_synth/QueD_sf.
DR PANTHER; PTHR12589:SF7; 6-PYRUVOYL TETRAHYDROBIOPTERIN SYNTHASE; 1.
DR PANTHER; PTHR12589; PYRUVOYL TETRAHYDROBIOPTERIN SYNTHASE; 1.
DR Pfam; PF01242; PTPS; 1.
DR SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053260};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 132 AA; 14437 MW; 11D2A7CA51F751F8 CRC64;
MFSITVRDHI MIAHSFRGEV FGPAQRLHGA TFLVDATFRR EQLDDDNIVV DIGLATQELG
AVVAELNYRN LDNEPDFAGV NTSTEFLAKV IADRLAERIE KGGLGEGAKG LAGLTVTLHE
SHVAWASYER AL
//