位置:首页 > 蛋白库 > QUEC_CALBD
QUEC_CALBD
ID   QUEC_CALBD              Reviewed;         221 AA.
AC   B9MMB0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=7-cyano-7-deazaguanine synthase {ECO:0000255|HAMAP-Rule:MF_01633};
DE            EC=6.3.4.20 {ECO:0000255|HAMAP-Rule:MF_01633};
DE   AltName: Full=7-cyano-7-carbaguanine synthase {ECO:0000255|HAMAP-Rule:MF_01633};
DE   AltName: Full=PreQ(0) synthase {ECO:0000255|HAMAP-Rule:MF_01633};
DE   AltName: Full=Queuosine biosynthesis protein QueC {ECO:0000255|HAMAP-Rule:MF_01633};
GN   Name=queC {ECO:0000255|HAMAP-Rule:MF_01633}; OrderedLocusNames=Athe_0191;
OS   Caldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320)
OS   (Anaerocellum thermophilum).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis; Caldicellulosiruptor.
OX   NCBI_TaxID=521460;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1888 / DSM 6725 / Z-1320;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Kataeva I., Adams M.W.W.;
RT   "Complete sequence of chromosome of Anaerocellum thermophilum DSM 6725.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the ATP-dependent conversion of 7-carboxy-7-
CC       deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
CC       {ECO:0000255|HAMAP-Rule:MF_01633}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-
CC         deazaguanine + ADP + H(+) + H2O + phosphate; Xref=Rhea:RHEA:27982,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:45075,
CC         ChEBI:CHEBI:61036, ChEBI:CHEBI:456216; EC=6.3.4.20;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01633};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01633};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01633};
CC   -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01633}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01633}.
CC   -!- SIMILARITY: Belongs to the QueC family. {ECO:0000255|HAMAP-
CC       Rule:MF_01633}.
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; CP001393; ACM59342.1; -; Genomic_DNA.
DR   RefSeq; WP_015906813.1; NC_012034.1.
DR   AlphaFoldDB; B9MMB0; -.
DR   SMR; B9MMB0; -.
DR   STRING; 521460.Athe_0191; -.
DR   EnsemblBacteria; ACM59342; ACM59342; Athe_0191.
DR   GeneID; 31771563; -.
DR   KEGG; ate:Athe_0191; -.
DR   eggNOG; COG0603; Bacteria.
DR   HOGENOM; CLU_081854_1_0_9; -.
DR   OMA; CESCMRR; -.
DR   OrthoDB; 1681374at2; -.
DR   UniPathway; UPA00391; -.
DR   Proteomes; UP000007723; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01995; ExsB; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01633; QueC; 1.
DR   InterPro; IPR018317; QueC.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR42914; PTHR42914; 1.
DR   Pfam; PF06508; QueC; 1.
DR   PIRSF; PIRSF006293; ExsB; 1.
DR   TIGRFAMs; TIGR00364; TIGR00364; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Metal-binding; Nucleotide-binding;
KW   Queuosine biosynthesis; Zinc.
FT   CHAIN           1..221
FT                   /note="7-cyano-7-deazaguanine synthase"
FT                   /id="PRO_1000186551"
FT   BINDING         7..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT   BINDING         183
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT   BINDING         191
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT   BINDING         194
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT   BINDING         197
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
SQ   SEQUENCE   221 AA;  24769 MW;  5D0B991B286D2515 CRC64;
     MRAVVVLSGG MDSTTLLYDV KSQGYEVFAI SFLYGQKHSK ELEFAKKTCS LLSIPYKIVD
     ISFFAELAPS ALTTPDWNVP EGYYTDSTMK QTVVPNRNMV LLSISAAYAI SLGAKKLFYG
     AHAGDHPIYP DCRKEFVEAM KNALYLADYI GLELEAPYVD MKKEDILRRG LELGVNYSLT
     WSCYKGGQKA CGRCGTCTER IEAFKKVGVK DPIEYEIEID W
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024