ID A0A1N7ABL0_9BACI Unreviewed; 275 AA.
AC A0A1N7ABL0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=SAMN05443094_107143 {ECO:0000313|EMBL:SIR36381.1};
OS Domibacillus enclensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX NCBI_TaxID=1017273 {ECO:0000313|EMBL:SIR36381.1, ECO:0000313|Proteomes:UP000186385};
RN [1] {ECO:0000313|EMBL:SIR36381.1, ECO:0000313|Proteomes:UP000186385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIO-1016 {ECO:0000313|EMBL:SIR36381.1,
RC ECO:0000313|Proteomes:UP000186385};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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}.
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DR EMBL; FTLX01000007; SIR36381.1; -; Genomic_DNA.
DR RefSeq; WP_045849447.1; NZ_MWSK01000007.1.
DR AlphaFoldDB; A0A1N7ABL0; -.
DR STRING; 1017273.SAMN05443094_107143; -.
DR OrthoDB; 9804698at2; -.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000186385; Unassembled WGS sequence.
DR GO; GO:0070497; F:6-carboxy-5,6,7,8-tetrahydropterin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0003874; F:6-pyruvoyltetrahydropterin synthase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:InterPro.
DR Gene3D; 3.30.479.10; 6-pyruvoyl tetrahydropterin synthase/QueD; 2.
DR InterPro; IPR007115; 6-PTP_synth/QueD.
DR InterPro; IPR038418; 6-PTP_synth/QueD_sf.
DR InterPro; IPR022470; PTPS_Cys_AS.
DR PANTHER; PTHR12589:SF7; 6-PYRUVOYL TETRAHYDROBIOPTERIN SYNTHASE; 1.
DR PANTHER; PTHR12589; PYRUVOYL TETRAHYDROBIOPTERIN SYNTHASE; 1.
DR Pfam; PF01242; PTPS; 2.
DR SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 2.
DR PROSITE; PS00987; PTPS_1; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ SEQUENCE 275 AA; 32203 MW; 1512EBAA2FB4F4F3 CRC64;
MTVYLSRKLS FSAMHSYRIE QWSDEKNQAV FGLCSNPNGH GHDYVLKVMA GGQIKQDSGI
VVNITDIDKT VKTFIEEQMD GKFLNKENAY FQTNIPTTEN IVKYVWNSLR DKLEGCRLHT
IRLYESDYLY AEKGEDDMVR LTKRYHFCTA HRLHSEQLSQ EENDRLFGKC NNPYGHGHNY
YLEVTVSDRP DPITGMIVDL SQLDALVEKE IMERFDHKHL NLDTEEFKEL NPTSENVTIV
IWDLLKDSLK NLYKIGLYET EKNYFEYYGP DQELV
//
