ID K7WB51_9NOST Unreviewed; 422 AA.
AC K7WB51;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=ANA_C20722 {ECO:0000313|EMBL:AFW97139.1};
OS Anabaena sp. 90.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX NCBI_TaxID=46234 {ECO:0000313|EMBL:AFW97139.1, ECO:0000313|Proteomes:UP000010101};
RN [1] {ECO:0000313|EMBL:AFW97139.1, ECO:0000313|Proteomes:UP000010101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=90 {ECO:0000313|EMBL:AFW97139.1};
RX PubMed=23148582; DOI=10.1186/1471-2164-13-613;
RA Wang H., Sivonen K., Rouhiainen L., Fewer D.P., Lyra C., Rantala-Ylinen A.,
RA Vestola J., Jokela J., Rantasarkka K., Li Z., Liu B.;
RT "Genome-derived insights into the biology of the hepatotoxic bloom-forming
RT cyanobacterium Anabaena sp. strain 90.";
RL BMC Genomics 13:613-613(2012).
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}.
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DR EMBL; CP003285; AFW97139.1; -; Genomic_DNA.
DR RefSeq; WP_015083691.1; NC_019439.1.
DR AlphaFoldDB; K7WB51; -.
DR STRING; 46234.ANA_C20722; -.
DR KEGG; anb:ANA_C20722; -.
DR PATRIC; fig|46234.3.peg.5163; -.
DR eggNOG; COG0720; Bacteria.
DR HOGENOM; CLU_651856_0_0_3; -.
DR OrthoDB; 9804698at2; -.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000010101; Chromosome chANA02.
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; 3.
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; 3.
DR SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 3.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AFW97139.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000010101};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 422 AA; 47557 MW; 5AB6DC16B54159AC CRC64;
MQCIVNRRDQ FSAVGRYWFP ELSQIENLEK FGAYSKFPGH GHNYVLFISM IGELDEYGMV
LNLSDVKHVI KEEVTSQLDF SYLNDVWTEF QQTLPTTENM ARVIWERLAP HLPLVRVQLF
EHPQLWADYQ GEGEKASLTI RTHFSAAHRL APNLSADKYG RCTQTHGHNY HLEVTVEGEI
DSRTGMIVDV AALNRVVEDY VVRIFDHSCV NEDIPYFADI VPTTENISRY IHGLLESPID
ELGVKLANIK LFESHQLWAD YPGKDRSGYL SISTHFSSAH RLAHPDLSLA KNTEIYGKCA
RVNGHGHNYQ LEVTIKGNID SSTGMVIDLG ALNQIITDYV IEPFDHTFLN KDVAFFNQVV
PTAENIALYI SNTLRSPIQE LGATLYKVKL VESPNNACEI YAADSESISV NAAVSQPVLA
IV
//
