ID A0A1J4VN28_9BACT Unreviewed; 460 AA.
AC A0A1J4VN28;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00917, ECO:0000256|HAMAP-Rule:MF_01633};
DE Includes:
DE RecName: Full=7-cyano-7-deazaguanine synthase {ECO:0000256|HAMAP-Rule:MF_01633};
DE EC=6.3.4.20 {ECO:0000256|HAMAP-Rule:MF_01633};
DE AltName: Full=7-cyano-7-carbaguanine synthase {ECO:0000256|HAMAP-Rule:MF_01633};
DE AltName: Full=PreQ(0) synthase {ECO:0000256|HAMAP-Rule:MF_01633};
DE AltName: Full=Queuosine biosynthesis protein QueC {ECO:0000256|HAMAP-Rule:MF_01633};
DE Includes:
DE RecName: Full=7-carboxy-7-deazaguanine synthase {ECO:0000256|HAMAP-Rule:MF_00917};
DE Short=CDG synthase {ECO:0000256|HAMAP-Rule:MF_00917};
DE EC=4.3.99.3 {ECO:0000256|HAMAP-Rule:MF_00917};
DE AltName: Full=Queuosine biosynthesis protein QueE {ECO:0000256|HAMAP-Rule:MF_00917};
GN Name=queE {ECO:0000256|HAMAP-Rule:MF_00917};
GN Synonyms=queC {ECO:0000256|HAMAP-Rule:MF_01633};
GN ORFNames=AUJ75_03905 {ECO:0000313|EMBL:OIO37624.1};
OS Candidatus Omnitrophica bacterium CG1_02_49_10.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1805289 {ECO:0000313|EMBL:OIO37624.1, ECO:0000313|Proteomes:UP000182804};
RN [1] {ECO:0000313|EMBL:OIO37624.1, ECO:0000313|Proteomes:UP000182804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_49_10 {ECO:0000313|EMBL:OIO37624.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
CC -!- FUNCTION: Catalyzes the ATP-dependent conversion of 7-carboxy-7-
CC deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
CC {ECO:0000256|HAMAP-Rule:MF_01633}.
CC -!- FUNCTION: Catalyzes the complex heterocyclic radical-mediated
CC conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7-carboxy-7-
CC deazaguanine (CDG), a step common to the biosynthetic pathways of all
CC 7-deazapurine-containing compounds. {ECO:0000256|HAMAP-Rule:MF_00917}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-carboxy-5,6,7,8-tetrahydropterin + H(+) = 7-carboxy-7-
CC deazaguanine + NH4(+); Xref=Rhea:RHEA:27974, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:61032, ChEBI:CHEBI:61036; EC=4.3.99.3;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00917};
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:0000256|ARBA:ARBA00037008, ECO:0000256|HAMAP-
CC Rule:MF_01633};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00917};
CC -!- COFACTOR:
CC Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00917};
CC Note=Binds 1 S-adenosyl-L-methionine per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00917};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01633};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01633};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00917};
CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC cysteines and an exchangeable S-adenosyl-L-methionine.
CC {ECO:0000256|HAMAP-Rule:MF_00917};
CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005061, ECO:0000256|HAMAP-Rule:MF_01633}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00917}.
CC -!- SIMILARITY: Belongs to the QueC family. {ECO:0000256|ARBA:ARBA00037993,
CC ECO:0000256|HAMAP-Rule:MF_01633}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. 7-carboxy-7-
CC deazaguanine synthase family. {ECO:0000256|HAMAP-Rule:MF_00917}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00917}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OIO37624.1}.
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DR EMBL; MNVT01000111; OIO37624.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4VN28; -.
DR UniPathway; UPA00391; -.
DR Proteomes; UP000182804; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016840; F:carbon-nitrogen lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; 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 CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_01633; QueC; 1.
DR HAMAP; MF_00917; QueE; 1.
DR InterPro; IPR024924; 7-CO-7-deazaguanine_synth-like.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR018317; QueC.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR00364; 7-cyano-7-deazaguanine synthase QueC; 1.
DR PANTHER; PTHR42914; 7-CYANO-7-DEAZAGUANINE SYNTHASE; 1.
DR PANTHER; PTHR42914:SF1; 7-CYANO-7-DEAZAGUANINE SYNTHASE; 1.
DR Pfam; PF13353; Fer4_12; 1.
DR Pfam; PF06508; QueC; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00917};
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01633};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00917};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_00917}; Ligase {ECO:0000256|HAMAP-Rule:MF_01633};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00917};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00917};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01633}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01633};
KW Queuosine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01633};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_00917}; Zinc {ECO:0000256|HAMAP-Rule:MF_01633}.
FT DOMAIN 247..460
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 9..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01633"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01633"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01633"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01633"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01633"
FT BINDING 241..243
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00917"
FT BINDING 256
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00917"
FT BINDING 260
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00917"
FT BINDING 264
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00917"
FT BINDING 266..268
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00917"
FT BINDING 267
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00917"
FT BINDING 303
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00917"
FT BINDING 305
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00917"
SQ SEQUENCE 460 AA; 50815 MW; 44AFF32B38D30DD6 CRC64;
MKKKAVVLLS GGLDSATTLY LAKDQGYKCH SLVFDYGQRH KRELRSARKI AAAAGADYKV
LKITLPWKGS SLLDKRGPLP RSDFKKRTGP KIPSTYVPGR NIIFLSFAIS YAEAIGADVV
FIGANAIDYS GYPDCRADFY RSFVETARLG TRRGREGKAV EVLTPLINKT KSDIVKLGTS
LGVPYRYTWS CYRGGKAPCG RCDSCLLRAK GFKEAGLKDP LLKGLKADAA KAGITEIFSS
IQGEGIFLGV KQIFVRFKKC NMACAYCDVP RELAPKVYGA GDLLGKIEEL EKNKGPHHSI
SFTGGEPLLY ADLLAEILPE LKKRRFKVYL ETNGTLPEEL KKIIDHADVI AMDLKLPSST
GERSFWKEHA EFLKIASLKK VFVKVVVTPR TNKIDISKSI EIVKDVDGKI PLIIQPASPV
FKDTKAISDN RLFEFLELAS ARGVSNTRIV PQLHKILGVR
//
