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Conserved domains on  [gi|490370656|ref|WP_004250261|]
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MULTISPECIES: 7-carboxy-7-deazaguanine synthase QueE [Proteus]

Protein Classification

radical SAM family protein( domain architecture ID 139618)

radical SAM family protein may generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity; contains a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster; transfers a single electron from the iron-sulfur cluster to SAM leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical

Gene Ontology:  GO:0003824|GO:0051539|GO:1904047
SCOP:  3000308

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Radical_SAM super family cl18962
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
9-223 3.73e-144

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


The actual alignment was detected with superfamily member TIGR04322:

Pssm-ID: 450244  Cd Length: 215  Bit Score: 400.89  E-value: 3.73e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370656    9 FQTLQGEGVFTGVPALFVRLQGCPVGCSWCDTKHTWEKEESKKVPLGDIPIKTQESDTWGIATVEDILSLFRQQRYSAKH 88
Cdd:TIGR04322   1 FETIQGEGSFTGVPAIFIRLQGCPVGCSWCDTKHTWEVDPEDQVSLGQILAKKADSPTWANLSAEEILALIKQQGYTAKH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370656   89 VVITGGEPCLYDLRPLTEGLEKAGFDCQIETSGTHDILCSEATWVTLSPKVGMRGGLNVLSSAINRANEIKHPVAREKDI 168
Cdd:TIGR04322  81 VVITGGEPCMYDLRPLTELLEAHGYSCQIETSGTFEILCTESTWVTVSPKINMKGGYPVLASALSRANEIKHPVAMQKHI 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490370656  169 EALDDLLRLRTQQPMAIVALQPISCKESATALCIKTCIERNWRFSMQTHKYLNIA 223
Cdd:TIGR04322 161 EELDALLAGLKDLKNKVICLQPISQKKRATELAIKTCIARNWRLSVQTHKYLNIE 215
 
Name Accession Description Interval E-value
rSAM_QueE_Ecoli TIGR04322
putative 7-cyano-7-deazaguanosine (preQ0) biosynthesis protein QueE; Members of this radical ...
9-223 3.73e-144

putative 7-cyano-7-deazaguanosine (preQ0) biosynthesis protein QueE; Members of this radical SAM domain protein family appear to be the E. coli form of the queuosine biosynthesis protein QueE. QueE is involved in making preQ0 (7-cyano-7-deazaquanine), a precursor of both the bacterial/eukaryotic modified tRNA base queuosine and the archaeal modified base archaeosine. Members occur in species that lack known forms of QueE but usually are not found in queuosine biosynthesis operons. Members of this family tend to form bi-directional best hit matches to members of known (TIGR03365) and putative (TIGR03963) QueE families from other lineages.


Pssm-ID: 275126  Cd Length: 215  Bit Score: 400.89  E-value: 3.73e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370656    9 FQTLQGEGVFTGVPALFVRLQGCPVGCSWCDTKHTWEKEESKKVPLGDIPIKTQESDTWGIATVEDILSLFRQQRYSAKH 88
Cdd:TIGR04322   1 FETIQGEGSFTGVPAIFIRLQGCPVGCSWCDTKHTWEVDPEDQVSLGQILAKKADSPTWANLSAEEILALIKQQGYTAKH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370656   89 VVITGGEPCLYDLRPLTEGLEKAGFDCQIETSGTHDILCSEATWVTLSPKVGMRGGLNVLSSAINRANEIKHPVAREKDI 168
Cdd:TIGR04322  81 VVITGGEPCMYDLRPLTELLEAHGYSCQIETSGTFEILCTESTWVTVSPKINMKGGYPVLASALSRANEIKHPVAMQKHI 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490370656  169 EALDDLLRLRTQQPMAIVALQPISCKESATALCIKTCIERNWRFSMQTHKYLNIA 223
Cdd:TIGR04322 161 EELDALLAGLKDLKNKVICLQPISQKKRATELAIKTCIARNWRLSVQTHKYLNIE 215
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
2-222 5.35e-80

Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic radical activating enzyme NrdG/QueE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440367 [Multi-domain]  Cd Length: 205  Bit Score: 238.11  E-value: 5.35e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370656   2 QYPINEVFQTLQGEGVFTGVPALFVRLQGCPVGCSWCDTKHTWEKEESKKVplgdipiktqesdtwgiaTVEDILSLFrq 81
Cdd:COG0602    1 TLPIVEIFYSIQGEGALAGRPAVFVRLAGCNLRCSWCDTKYAWDGEGGKRM------------------SAEEILEEV-- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370656  82 QRYSAKHVVITGGEPCLY-DLRPLTEGLEKAGFDCQIETSGTHDILcSEATWVTLSPKVGMRGGLNV---LSSAINRANE 157
Cdd:COG0602   61 AALGARHVVITGGEPLLQdDLAELLEALKDAGYEVALETNGTLPIP-AGIDWVTVSPKLPSSGEEEDnreNLEVLRRADE 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490370656 158 IKHPVAREKDIEALDDLLRLRtqQPMAIVALQPISC--KESATALCIKTCIER-NWRFSMQTHKYLNI 222
Cdd:COG0602  140 LKFVVADETDLEEAEELLARL--DFRCPVYLQPVWGnkLEENTELLAEWCLAHpNVRLSPQLHKLLGV 205
Fer4_14 pfam13394
4Fe-4S single cluster domain;
24-125 1.41e-07

4Fe-4S single cluster domain;


Pssm-ID: 433171 [Multi-domain]  Cd Length: 115  Bit Score: 48.51  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370656   24 LFVrlQGCPVGCSWCDTKHTWeKEESKKvplgdipIKTQEsdtwgiaTVEDILSLFRQQRYSAKHVVITGGEPCLY---- 99
Cdd:pfam13394   1 LFV--SGCNHSCPGCDNKETW-KFNYGE-------PFTEE-------LEDQIIADLKDSYIKRQGLVLTGGEPLHPwnlp 63
                          90       100
                  ....*....|....*....|....*...
gi 490370656  100 DLRPLTEGL--EKAGFDCQIETSGTHDI 125
Cdd:pfam13394  64 VLLKLLKRVkeEYPSKDIWLETGYTLAI 91
 
Name Accession Description Interval E-value
rSAM_QueE_Ecoli TIGR04322
putative 7-cyano-7-deazaguanosine (preQ0) biosynthesis protein QueE; Members of this radical ...
9-223 3.73e-144

putative 7-cyano-7-deazaguanosine (preQ0) biosynthesis protein QueE; Members of this radical SAM domain protein family appear to be the E. coli form of the queuosine biosynthesis protein QueE. QueE is involved in making preQ0 (7-cyano-7-deazaquanine), a precursor of both the bacterial/eukaryotic modified tRNA base queuosine and the archaeal modified base archaeosine. Members occur in species that lack known forms of QueE but usually are not found in queuosine biosynthesis operons. Members of this family tend to form bi-directional best hit matches to members of known (TIGR03365) and putative (TIGR03963) QueE families from other lineages.


Pssm-ID: 275126  Cd Length: 215  Bit Score: 400.89  E-value: 3.73e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370656    9 FQTLQGEGVFTGVPALFVRLQGCPVGCSWCDTKHTWEKEESKKVPLGDIPIKTQESDTWGIATVEDILSLFRQQRYSAKH 88
Cdd:TIGR04322   1 FETIQGEGSFTGVPAIFIRLQGCPVGCSWCDTKHTWEVDPEDQVSLGQILAKKADSPTWANLSAEEILALIKQQGYTAKH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370656   89 VVITGGEPCLYDLRPLTEGLEKAGFDCQIETSGTHDILCSEATWVTLSPKVGMRGGLNVLSSAINRANEIKHPVAREKDI 168
Cdd:TIGR04322  81 VVITGGEPCMYDLRPLTELLEAHGYSCQIETSGTFEILCTESTWVTVSPKINMKGGYPVLASALSRANEIKHPVAMQKHI 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490370656  169 EALDDLLRLRTQQPMAIVALQPISCKESATALCIKTCIERNWRFSMQTHKYLNIA 223
Cdd:TIGR04322 161 EELDALLAGLKDLKNKVICLQPISQKKRATELAIKTCIARNWRLSVQTHKYLNIE 215
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
2-222 5.35e-80

Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic radical activating enzyme NrdG/QueE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440367 [Multi-domain]  Cd Length: 205  Bit Score: 238.11  E-value: 5.35e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370656   2 QYPINEVFQTLQGEGVFTGVPALFVRLQGCPVGCSWCDTKHTWEKEESKKVplgdipiktqesdtwgiaTVEDILSLFrq 81
Cdd:COG0602    1 TLPIVEIFYSIQGEGALAGRPAVFVRLAGCNLRCSWCDTKYAWDGEGGKRM------------------SAEEILEEV-- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370656  82 QRYSAKHVVITGGEPCLY-DLRPLTEGLEKAGFDCQIETSGTHDILcSEATWVTLSPKVGMRGGLNV---LSSAINRANE 157
Cdd:COG0602   61 AALGARHVVITGGEPLLQdDLAELLEALKDAGYEVALETNGTLPIP-AGIDWVTVSPKLPSSGEEEDnreNLEVLRRADE 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490370656 158 IKHPVAREKDIEALDDLLRLRtqQPMAIVALQPISC--KESATALCIKTCIER-NWRFSMQTHKYLNI 222
Cdd:COG0602  140 LKFVVADETDLEEAEELLARL--DFRCPVYLQPVWGnkLEENTELLAEWCLAHpNVRLSPQLHKLLGV 205
rSAM_QueE_gams TIGR04349
putative 7-cyano-7-deazaguanosine (preQ0) biosynthesis protein QueE, gammaproteobacterial type; ...
5-125 8.51e-22

putative 7-cyano-7-deazaguanosine (preQ0) biosynthesis protein QueE, gammaproteobacterial type; Members of this radical SAM domain protein family appear to be a form of the queuosine biosynthesis protein QueE. QueE is involved in making preQ0 (7-cyano-7-deazaquanine), a precursor of both the bacterial/eukaryotic modified tRNA base queuosine and the archaeal modified base archaeosine. Members occur in preQ0 operons species that lack members of related protein family TIGR03365.


Pssm-ID: 275145 [Multi-domain]  Cd Length: 210  Bit Score: 88.82  E-value: 8.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370656    5 INEVFQTLQGEGVFTGVPALFVRLQGCPVGCSWCDTKHTWEKEESkkvplgdipiktqesdtwgiATVEDILSlfRQQRY 84
Cdd:TIGR04349   3 ITEIFYSLQGETSTVGLPTVFVRLTGCPLRCVYCDTAYAFSGGER--------------------MSLDDILA--QVASY 60
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 490370656   85 SAKHVVITGGEP-----CLydlrPLTEGLEKAGFDCQIETSGTHDI 125
Cdd:TIGR04349  61 GARYVTVTGGEPlaqpaCL----PLLTALCDAGYEVSLETSGALDI 102
Bsubt_queE TIGR03365
7-cyano-7-deazaguanosine (preQ0) biosynthesis protein QueE; This uncharacterized enzyme, ...
4-160 1.07e-19

7-cyano-7-deazaguanosine (preQ0) biosynthesis protein QueE; This uncharacterized enzyme, designated QueE, participates in the biosynthesis, from GTP, of 7-cyano-7-deazaguanosine, also called preQ0 because in many species it is a precursor of queuosine. In most Archaea, it is instead the precursor of a different tRNA modified base, archaeosine. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274545  Cd Length: 238  Bit Score: 83.95  E-value: 1.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370656    4 PINEVF-QTLQGEGVFTGVPALFVRLQGCPVGCSWCDTKHTWEkeeskkvplgdipikTQESDTWGIATVEDI---LSLF 79
Cdd:TIGR03365   4 PVLEIFgPTIQGEGMVIGQKTMFVRTAGCDYRCSWCDSAFTWD---------------GSAKDDWRPMTAEEIwqeLKAL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370656   80 RQQRYSakHVVITGGEPCLYD-LRPLTEGLEKAGFDCQIETSGT--HDILcSEATWVTLSPK---VGMRGGLNVLSSAIN 153
Cdd:TIGR03365  69 GGGTFL--HVTLSGGNPALQKpLGELIDLLHEKGYRFALETQGSvwQDWF-TDIDDLTLSPKppsSGMETDWQKLDDCIE 145

                  ....*..
gi 490370656  154 RANEIKH 160
Cdd:TIGR03365 146 RLGPGPQ 152
rSAM_QueE_Clost TIGR03963
putative 7-cyano-7-deazaguanosine (preQ0) biosynthesis protein QueE, clostridial; Members of ...
3-126 4.21e-18

putative 7-cyano-7-deazaguanosine (preQ0) biosynthesis protein QueE, clostridial; Members of this radical SAM domain protein family appear to be the Clostridial form of the queuosine biosynthesis protein QueE. QueE is involved in making preQ0 (7-cyano-7-deazaquanine), a precursor of both the bacterial/eukaryotic modified tRNA base queuosine and the archaeal modified base archaeosine. Members occur in preQ0 operons species that lack members of related protein family TIGR03365. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 188478 [Multi-domain]  Cd Length: 219  Bit Score: 79.35  E-value: 4.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370656    3 YPINEVFQTLQGEGVFTGVPALFVRLQGCPVGCSWCDTKHTWEKEESKKVplgdipiktqesdtwgiATVEDILSlfRQQ 82
Cdd:TIGR03963   1 FKVVEKFVSINGEGKRAGELATFIRFAGCNLNCSYCDTTWANDKDCPYEL-----------------LSADEIYD--YIK 61
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 490370656   83 RYSAKHVVITGGEPCLY-DLRPLTEG-LEKAGFDCQIETSGTHDIL 126
Cdd:TIGR03963  62 ETGVKNVTLTGGEPLLQeNIDELIELlLGDAGLEVEIETNGSVDIA 107
Fer4_14 pfam13394
4Fe-4S single cluster domain;
24-125 1.41e-07

4Fe-4S single cluster domain;


Pssm-ID: 433171 [Multi-domain]  Cd Length: 115  Bit Score: 48.51  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370656   24 LFVrlQGCPVGCSWCDTKHTWeKEESKKvplgdipIKTQEsdtwgiaTVEDILSLFRQQRYSAKHVVITGGEPCLY---- 99
Cdd:pfam13394   1 LFV--SGCNHSCPGCDNKETW-KFNYGE-------PFTEE-------LEDQIIADLKDSYIKRQGLVLTGGEPLHPwnlp 63
                          90       100
                  ....*....|....*....|....*...
gi 490370656  100 DLRPLTEGL--EKAGFDCQIETSGTHDI 125
Cdd:pfam13394  64 VLLKLLKRVkeEYPSKDIWLETGYTLAI 91
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
28-122 1.86e-06

Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 47.10  E-value: 1.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370656  28 LQGCPVGCSWCdtkHTWEkeeskkvplgdipIKTQESDTWGI-ATVEDILSLFRQQR---YSAKHVVITGGEPCLYD--L 101
Cdd:COG1180   28 TQGCNLRCPYC---HNPE-------------ISQGRPDAAGReLSPEELVEEALKDRgflDSCGGVTFSGGEPTLQPefL 91
                         90       100
                 ....*....|....*....|.
gi 490370656 102 RPLTEGLEKAGFDCQIETSGT 122
Cdd:COG1180   92 LDLAKLAKELGLHTALDTNGY 112
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
71-122 2.43e-04

Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, chromosome partitioning, Coenzyme transport and metabolism];


Pssm-ID: 440301 [Multi-domain]  Cd Length: 159  Bit Score: 40.27  E-value: 2.43e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490370656  71 TVEDILSLFRQ-QRYSAKHVVITGGEPCLY-DLRPLTEGLEKAGFDCQIETSGT 122
Cdd:COG0535   30 STEEAKRILDElAELGVKVVGLTGGEPLLRpDLFELVEYAKELGIRVNLSTNGT 83
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
30-123 3.58e-04

Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation.


Pssm-ID: 427681 [Multi-domain]  Cd Length: 159  Bit Score: 39.82  E-value: 3.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490370656   30 GCPVGCSWCDTKHTWEKEESKKVplgdipiktqesdtwgiaTVEDILSLFRQ-QRYSAKHVVITGGEPCLY-----DLRP 103
Cdd:pfam04055   4 GCNLRCTYCAFPSIRARGKGREL------------------SPEEILEEAKElKRLGVEVVILGGGEPLLLpdlveLLER 65
                          90       100
                  ....*....|....*....|
gi 490370656  104 LTEGLEKAGFDCQIETSGTH 123
Cdd:pfam04055  66 LLKLELAEGIRITLETNGTL 85
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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