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Protein

7-cyano-7-deazaguanine synthase

Gene

queC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ0). Uses ammonia as nitrogen donor.2 Publications

Catalytic activityi

7-carboxy-7-carbaguanine + NH3 + ATP = 7-cyano-7-carbaguanine + ADP + phosphate + H2O.1 Publication

Cofactori

Zn2+2 PublicationsNote: Binds 1 zinc ion per subunit.2 Publications

Pathwayi: 7-cyano-7-deazaguanine biosynthesis

This protein is involved in the pathway 7-cyano-7-deazaguanine biosynthesis, which is part of Purine metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway 7-cyano-7-deazaguanine biosynthesis and in Purine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi186 – 1861Zinc1 Publication
Metal bindingi195 – 1951Zinc1 Publication
Metal bindingi198 – 1981Zinc1 Publication
Metal bindingi201 – 2011Zinc1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 2011ATP1 PublicationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Queuosine biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU13720-MONOMER.
MetaCyc:BSU13720-MONOMER.
BRENDAi6.3.4.20. 658.
UniPathwayiUPA00391.

Names & Taxonomyi

Protein namesi
Recommended name:
7-cyano-7-deazaguanine synthase (EC:6.3.4.201 Publication)
Alternative name(s):
7-cyano-7-carbaguanine synthase
PreQ(0) synthase
Queuosine biosynthesis protein QueC
Gene namesi
Name:queC
Synonyms:ykvJ
Ordered Locus Names:BSU13720
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2192197-cyano-7-deazaguanine synthasePRO_0000246801Add
BLAST

Proteomic databases

PaxDbiO31675.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100007596.

Structurei

Secondary structure

1
219
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95Combined sources
Helixi14 – 2613Combined sources
Beta strandi28 – 3811Combined sources
Helixi43 – 5311Combined sources
Beta strandi59 – 635Combined sources
Helixi65 – 706Combined sources
Helixi73 – 753Combined sources
Helixi97 – 11216Combined sources
Beta strandi115 – 1184Combined sources
Helixi130 – 1323Combined sources
Helixi134 – 14815Combined sources
Beta strandi153 – 1553Combined sources
Turni157 – 1604Combined sources
Helixi163 – 17210Combined sources
Helixi176 – 1827Combined sources
Helixi199 – 21315Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BL5X-ray2.95A/B/C/D/E/F1-219[»]
ProteinModelPortaliO31675.
SMRiO31675. Positions 3-215.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO31675.

Family & Domainsi

Sequence similaritiesi

Belongs to the QueC family.Curated

Phylogenomic databases

eggNOGiENOG4105FD2. Bacteria.
COG0603. LUCA.
HOGENOMiHOG000110563.
InParanoidiO31675.
KOiK06920.
OMAiAYGYGCD.
OrthoDBiEOG6091HB.
PhylomeDBiO31675.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_01633. QueC.
InterProiIPR018317. QueC.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF06508. QueC. 1 hit.
[Graphical view]
PIRSFiPIRSF006293. ExsB. 1 hit.
TIGRFAMsiTIGR00364. TIGR00364. 1 hit.

Sequencei

Sequence statusi: Complete.

O31675-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKEKAIVVF SGGQDSTTCL LWALKEFEEV ETVTFHYNQR HSQEVEVAKS
60 70 80 90 100
IAEKLGVKNH LLDMSLLNQL APNALTRNDI EIEVKDGELP STFVPGRNLV
110 120 130 140 150
FLSFASILAY QIGARHIITG VCETDFSGYP DCRDEFVKSC NVTVNLAMEK
160 170 180 190 200
PFVIHTPLMW LNKAETWKLA DELGALDFVK NNTLTCYNGI IADGCGECPA
210
CHLRSKGYEE YMVMKGERA
Length:219
Mass (Da):24,529
Last modified:January 1, 1998 - v1
Checksum:i146535A4A91EB894
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13245.1.
PIRiA69868.
RefSeqiNP_389255.1. NC_000964.3.
WP_003245417.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13245; CAB13245; BSU13720.
GeneIDi939292.
KEGGibsu:BSU13720.
PATRICi18974513. VBIBacSub10457_1448.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13245.1.
PIRiA69868.
RefSeqiNP_389255.1. NC_000964.3.
WP_003245417.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BL5X-ray2.95A/B/C/D/E/F1-219[»]
ProteinModelPortaliO31675.
SMRiO31675. Positions 3-215.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100007596.

Proteomic databases

PaxDbiO31675.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13245; CAB13245; BSU13720.
GeneIDi939292.
KEGGibsu:BSU13720.
PATRICi18974513. VBIBacSub10457_1448.

Phylogenomic databases

eggNOGiENOG4105FD2. Bacteria.
COG0603. LUCA.
HOGENOMiHOG000110563.
InParanoidiO31675.
KOiK06920.
OMAiAYGYGCD.
OrthoDBiEOG6091HB.
PhylomeDBiO31675.

Enzyme and pathway databases

UniPathwayiUPA00391.
BioCyciBSUB:BSU13720-MONOMER.
MetaCyc:BSU13720-MONOMER.
BRENDAi6.3.4.20. 658.

Miscellaneous databases

EvolutionaryTraceiO31675.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_01633. QueC.
InterProiIPR018317. QueC.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF06508. QueC. 1 hit.
[Graphical view]
PIRSFiPIRSF006293. ExsB. 1 hit.
TIGRFAMsiTIGR00364. TIGR00364. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  2. "Identification of four genes necessary for biosynthesis of the modified nucleoside queuosine."
    Reader J.S., Metzgar D., Schimmel P., de Crecy-Lagard V.
    J. Biol. Chem. 279:6280-6285(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN QUEUOSINE BIOSYNTHESIS, GENE NAME.
  3. "The deazapurine biosynthetic pathway revealed: in vitro enzymatic synthesis of PreQ(0) from guanosine 5'-triphosphate in four steps."
    McCarty R.M., Somogyi A., Lin G., Jacobsen N.E., Bandarian V.
    Biochemistry 48:3847-3852(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS PREQ(0) SYNTHASE, CATALYTIC ACTIVITY, COFACTOR, PATHWAY.
    Strain: 168.
  4. "Crystal structure of QueC from Bacillus subtilis: an enzyme involved in preQ1 biosynthesis."
    Cicmil N., Huang R.H.
    Proteins 72:1084-1088(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND ATP ANALOG, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiQUEC_BACSU
AccessioniPrimary (citable) accession number: O31675
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: January 1, 1998
Last modified: February 17, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.