QUED_BACSU
ID QUED_BACSU Reviewed; 146 AA.
AC O31676;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 120.
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=ykvK; OrderedLocusNames=BSU13730;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP FUNCTION IN QUEUOSINE BIOSYNTHESIS, AND GENE NAME.
RX PubMed=14660578; DOI=10.1074/jbc.m310858200;
RA Reader J.S., Metzgar D., Schimmel P., de Crecy-Lagard V.;
RT "Identification of four genes necessary for biosynthesis of the modified
RT nucleoside queuosine.";
RL J. Biol. Chem. 279:6280-6285(2004).
RN [3]
RP SUBUNIT, AND CRYSTALLIZATION.
RX PubMed=18259064; DOI=10.1107/s1744309108000924;
RA Cicmil N., Shi L.;
RT "Crystallization and preliminary X-ray characterization of queD from
RT Bacillus subtilis, an enzyme involved in queuosine biosynthesis.";
RL Acta Crystallogr. F 64:119-122(2008).
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, ECO:0000269|PubMed:14660578}.
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 -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:18259064}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB13246.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL009126; CAB13246.1; ALT_INIT; Genomic_DNA.
DR PIR; B69868; B69868.
DR RefSeq; NP_389256.1; NC_000964.3.
DR AlphaFoldDB; O31676; -.
DR SMR; O31676; -.
DR STRING; 224308.BSU13730; -.
DR PaxDb; O31676; -.
DR PRIDE; O31676; -.
DR EnsemblBacteria; CAB13246; CAB13246; BSU_13730.
DR GeneID; 939282; -.
DR KEGG; bsu:BSU13730; -.
DR PATRIC; fig|224308.179.peg.1490; -.
DR eggNOG; COG0720; Bacteria.
DR InParanoid; O31676; -.
DR BioCyc; BSUB:BSU13730-MON; -.
DR BioCyc; MetaCyc:BSU13730-MON; -.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000001570; Chromosome.
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 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 1: Evidence at protein level;
KW Lyase; Metal-binding; Queuosine biosynthesis; Reference proteome; Zinc.
FT CHAIN 1..146
FT /note="6-carboxy-5,6,7,8-tetrahydropterin synthase"
FT /id="PRO_0000392070"
FT ACT_SITE 37
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 78
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 129
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 146 AA; 16468 MW; 74E6FC06C4C9D668 CRC64;
MLSQIYPQAQ HPYSFELNKD MHISAAHFIP RESAGACSRV HGHTYTVNIT VAGDELDDSG
FLVNFSVLKK LVHGNYDHTL LNDHEDFSQD DRYSLPTTEV VAKTIYDNVQ AYLDTLENKP
TCVQVFVRET PTSYCVYRPK KGGLNG
