[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1126/science.1071278; PubMed=12089438 [NCBI, ExPASy, EBI, Israel, Japan] Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.; "50 million years of genomic stasis in endosymbiotic bacteria."; Science 296:2376-2379(2002).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 15-262. DOI=10.1007/BF00296197; PubMed=7765846 [NCBI, ExPASy, EBI, Israel, Japan] Kolibachuk D., Baumann P.; "Buchnera aphidicola (aphid-endosymbiont) glyceraldehyde-3-phosphate dehydrogenase: molecular cloning and sequence analysis."; Curr. Microbiol. 30:133-136(1995).

Comments

FUNCTION: Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1) (By similarity).
CATALYTIC ACTIVITY: 7-aminomethyl-7-carbaguanine + 2 NADP⁺ = 7-cyano-7-carbaguanine + 2 NADPH.
PATHWAY: tRNA modification; queuosine-tRNA biosynthesis .
SUBCELLULAR LOCATION: Cytoplasm (Probable).
SIMILARITY: Belongs to the GTP cyclohydrolase I family. QueF type 2 subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AE013218; AAM67844.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U11045; AAC05800.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_660633.1; -.

3D structure databases

ModBase

Q8K9N6.

Enzyme and pathway databases

BioCyc

BAPH198804:BUSG288-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0003934;	Molecular function: GTP cyclohydrolase I activity (inferred from electronic annotation from InterPro).
GO:0046857;	Molecular function: oxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor (inferred from electronic annotation from HAMAP).
GO:0033739;	Molecular function: queuine synthase activity (inferred from electronic annotation from EC).
GO:0019438;	Biological process: aromatic compound biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0008616;	Biological process: queuosine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00817; atypical; 1.
PBIL [Tree]

InterPro

IPR016428; CN_OxRdtase_NADPH-dep_YqcD.
IPR001474; GTP_CycOHase_I.
Graphical view of domain structure.

Pfam

PF01227; GTP_cyclohydroI; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF004750; Nitrile_oxidored_YqcD_prd; 1.

TIGRFAMs

TIGR03138; QueF; 1.

ProtoNet

Q8K9N6.

Genome annotation databases

GeneID

1005492; -.

GenomeReviews

AE013218_GR; BUsg_288.

KEGG

bas:BUsg288; -.

Phylogenomic databases

HOGENOM

Q8K9N6; -.

Genome annotation databases

CMR

Q8K9N6; BUsg_288.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; NADP; Oxidoreductase; Queuosine biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 262`	`262`	`NADPH-dependent 7-cyano-7-deazaguanine reductase.`	`PRO_0000163023`
`CONFLICT`	`28 28`		`L -> I (in Ref. 2; AAC05800).`

Sequence information

Length: 262 AA [This is the length of the unprocessed precursor]

Molecular weight: 30731 Da [This is the MW of the unprocessed precursor]

CRC64: 2A78FCFA2D946DCE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSLKINNFNF LRPISRKKHR KKIKLNCLNL PFKGKDIWTL YELSWLNKNG LPQIAIAKIE 

        70         80         90        100        110        120 
IDVNSANIIE SKSFKIYINS FNQMKFNNNI DFINILTNDL TKCICGQISI KLFSLDAIKN 

       130        140        150        160        170        180 
ETITDFHGIC IDNQNIKIES YKYTPSFLMI NSERKIIKED LYTHLFKSNC PVTQQPDWAS 

       190        200        210        220        230        240 
IYIAYTGLSI NHASLLRYLI SFRSHNEFHE ECIERIFNDI NNICKPEELS VYARYTRRGG 

       250        260 
IDINPWRSNT NFSPFLTRLA RQ

Q8K9N6 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools