ID QUEF_ANAD2 Reviewed; 122 AA. AC B8JAR2; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 27-NOV-2024, entry version 74. DE RecName: Full=NADPH-dependent 7-cyano-7-deazaguanine reductase {ECO:0000255|HAMAP-Rule:MF_00818}; DE EC=1.7.1.13 {ECO:0000255|HAMAP-Rule:MF_00818}; DE AltName: Full=7-cyano-7-carbaguanine reductase {ECO:0000255|HAMAP-Rule:MF_00818}; DE AltName: Full=NADPH-dependent nitrile oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00818}; DE AltName: Full=PreQ(0) reductase {ECO:0000255|HAMAP-Rule:MF_00818}; GN Name=queF {ECO:0000255|HAMAP-Rule:MF_00818}; OrderedLocusNames=A2cp1_4244; OS Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258). OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae; OC Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=455488; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2CP-1 / ATCC BAA-258; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., RA Beliaev A.S., Richardson P.; RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of 7-cyano-7- CC deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1). CC {ECO:0000255|HAMAP-Rule:MF_00818}. CC -!- CATALYTIC ACTIVITY: CC Reaction=7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7- CC deazaguanine + 2 NADPH + 3 H(+); Xref=Rhea:RHEA:13409, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:45075, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349, ChEBI:CHEBI:58703; EC=1.7.1.13; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00818}; CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00818}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00818}. CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I family. QueF type 1 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00818}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001359; ACL67561.1; -; Genomic_DNA. DR RefSeq; WP_012528175.1; NC_011891.1. DR AlphaFoldDB; B8JAR2; -. DR SMR; B8JAR2; -. DR KEGG; acp:A2cp1_4244; -. DR HOGENOM; CLU_102489_1_0_7; -. DR UniPathway; UPA00392; -. DR Proteomes; UP000007089; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0033739; F:preQ1 synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule. DR Gene3D; 3.30.1130.10; -; 1. DR HAMAP; MF_00818; QueF_type1; 1. DR InterPro; IPR043133; GTP-CH-I_C/QueF. DR InterPro; IPR050084; NADPH_dep_7-cyano-7-deazaG_red. DR InterPro; IPR029500; QueF. DR InterPro; IPR016856; QueF_type1. DR NCBIfam; TIGR03139; QueF-II; 1. DR PANTHER; PTHR34354; NADPH-DEPENDENT 7-CYANO-7-DEAZAGUANINE REDUCTASE; 1. DR PANTHER; PTHR34354:SF1; NADPH-DEPENDENT 7-CYANO-7-DEAZAGUANINE REDUCTASE; 1. DR Pfam; PF14489; QueF; 1. DR PIRSF; PIRSF027377; Nitrile_oxidored_QueF; 1. DR SUPFAM; SSF55620; Tetrahydrobiopterin biosynthesis enzymes-like; 1. PE 3: Inferred from homology; KW Cytoplasm; NADP; Oxidoreductase; Queuosine biosynthesis. FT CHAIN 1..122 FT /note="NADPH-dependent 7-cyano-7-deazaguanine reductase" FT /id="PRO_1000148662" FT ACT_SITE 34 FT /note="Thioimide intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00818" FT ACT_SITE 41 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00818" FT BINDING 56..58 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00818" FT BINDING 75..76 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00818" SQ SEQUENCE 122 AA; 13700 MW; 01C81A29DCFD9678 CRC64; MPTQPSRDLQ TFPNPKPGRP FEIAMECPEF TCVCPMTGQP DFATIRLRYV PAERCVELKS LKLYLWSFRN EGTFHEAVTN RICDDLVAAL APRWIEVVGD FAVRGGIHTV VTARHGERPA GV //