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Conserved domains on  [gi|490282490|ref|WP_004178375|]
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MULTISPECIES: anaerobic ribonucleoside-triphosphate reductase-activating protein [Klebsiella]

Protein Classification

anaerobic ribonucleoside-triphosphate reductase-activating protein( domain architecture ID 10013743)

anaerobic ribonucleoside-triphosphate reductase-activating protein NrdG, the small component of class III ribonucleotide reductase, generates an organic free radical with S-adenosylmethionine and reduced flavodoxin as cosubstrates, resulting in 5'-deoxy-adenosine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
nrdG PRK11121
anaerobic ribonucleoside-triphosphate reductase-activating protein;
1-154 3.48e-129

anaerobic ribonucleoside-triphosphate reductase-activating protein;


:

Pssm-ID: 236853  Cd Length: 154  Bit Score: 357.38  E-value: 3.48e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490282490   1 MNYHQYYPVDIVNGPGTRCTLFVSGCVHECPGCYNKSTWRVNSGMPFTAEMADRIIADLNDTRIKRQGLSLSGGDPLHPQ 80
Cdd:PRK11121   1 MNYHQYYPVDVVNGPGTRCTLFVSGCVHQCPGCYNKSTWRLNSGHPFTKEMEDQIIADLNDTRIKRQGLSLSGGDPLHPQ 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490282490  81 NVADILKLVQRVRAECPGKDIWVWTGYKLDELNEAQMQVVNLINVLVDGKFVQDLKDPALIWRGSSNQVVHHLR 154
Cdd:PRK11121  81 NVPDILKLVQRVKAECPGKDIWVWTGYKLDELNAAQRQVVDLIDVLVDGKFVQDLADPSLIWRGSSNQVIHRLR 154
 
Name Accession Description Interval E-value
nrdG PRK11121
anaerobic ribonucleoside-triphosphate reductase-activating protein;
1-154 3.48e-129

anaerobic ribonucleoside-triphosphate reductase-activating protein;


Pssm-ID: 236853  Cd Length: 154  Bit Score: 357.38  E-value: 3.48e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490282490   1 MNYHQYYPVDIVNGPGTRCTLFVSGCVHECPGCYNKSTWRVNSGMPFTAEMADRIIADLNDTRIKRQGLSLSGGDPLHPQ 80
Cdd:PRK11121   1 MNYHQYYPVDVVNGPGTRCTLFVSGCVHQCPGCYNKSTWRLNSGHPFTKEMEDQIIADLNDTRIKRQGLSLSGGDPLHPQ 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490282490  81 NVADILKLVQRVRAECPGKDIWVWTGYKLDELNEAQMQVVNLINVLVDGKFVQDLKDPALIWRGSSNQVVHHLR 154
Cdd:PRK11121  81 NVPDILKLVQRVKAECPGKDIWVWTGYKLDELNAAQRQVVDLIDVLVDGKFVQDLADPSLIWRGSSNQVIHRLR 154
NrdG TIGR02491
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
 2-154 2.84e-88

anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of the radical-SAM family (pfam04055) and utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487). The two components form an alpha-2/beta-2 heterodimer. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism, Protein fate, Protein modification and repair]


Pssm-ID: 274161 [Multi-domain]  Cd Length: 154  Bit Score: 254.20  E-value: 2.84e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490282490    2 NYHQYYPVDIVNGPGTRCTLFVSGCVHECPGCYNKSTWRVNSGMPFTAEMADRIIADLNDTRiKRQGLSLSGGDPLHPQN 81
Cdd:TIGR02491   1 NYMNIKPDDIVNGEGIRVSLFVAGCKHHCEGCFNKETWNFNGGKEFTEALEKEIIRDLNDNP-LIDGLTLSGGDPLYPRN 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490282490   82 VADILKLVQRVRAECPGKDIWVWTGYKLDELNEAQMQ--VVNLINVLVDGKFVQDLKDPALIWRGSSNQVVHHLR 154
Cdd:TIGR02491  80 VEELIELVKKIKAEFPEKDIWLWTGYTWEEILEDEKHleVLKYIDVLVDGKFELSKKDLKLKFRGSSNQRIIDLK 154
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
 12-151 3.01e-80

4Fe-4S single cluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 433138 [Multi-domain]  Cd Length: 137  Bit Score: 233.22  E-value: 3.01e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490282490   12 VNGPGTRCTLFVSGCVHECPGCYNKSTWRVNSGMPFTAEMADRIIADLNDTRIkrQGLSLSGGDPLHpqNVADILKLVQR 91
Cdd:pfam13353   1 VNGPGVRCSLFVSGCNHHCKGCFNPETWDFKYGKPFTEELEDEIIEDLAKPYI--QGLTLSGGEPLL--NAEALLELVKR 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490282490   92 VRAECPGKDIWVWTGYKLDEL-NEAQMQVVNLINVLVDGKFVQDLKDPALIWRGSSNQVVH 151
Cdd:pfam13353  77 VREECPEKDIWLWTGYTFEELqSKDQLELLKLIDVLVDGKFEQSLKDPSLRFRGSSNQRII 137
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
 8-136 2.04e-08

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 51.34  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490282490   8 PVDIVNGPGT-RCTLFVSGCVHECPGCYNKSTWRVNSGMPFTAEMADRIIADLNDTRI---KRQGLSLSGGDPL-HPQNV 82
Cdd:COG1180   12 PFSTVDGPGSiRLSVFTQGCNLRCPYCHNPEISQGRPDAAGRELSPEELVEEALKDRGfldSCGGVTFSGGEPTlQPEFL 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490282490  83 ADILKLVQRvraecpgKDI---WVWTGY----KLDELneaqMQVVNLINVlvdgkfvqDLK 136
Cdd:COG1180   92 LDLAKLAKE-------LGLhtaLDTNGYipeeALEEL----LPYLDAVNI--------DLK 133
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 25-137 6.43e-04

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.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 38.47  E-value: 6.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490282490  25 GCVHECPGCYNKSTwrvNSGMPFTAEMADRIIADLnDTRIKRQ--GLSLSGGDPLHPQNVADILKlvqRVRAECPGKDI- 101
Cdd:cd01335    6 GCNLNCGFCSNPAS---KGRGPESPPEIEEILDIV-LEAKERGveVVILTGGEPLLYPELAELLR---RLKKELPGFEIs 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 490282490 102 WVWTGYK-----LDELNEAqmqVVNLINVLVDGKFVQDLKD 137
Cdd:cd01335   79 IETNGTLlteelLKELKEL---GLDGVGVSLDSGDEEVADK 116
 
Name Accession Description Interval E-value
nrdG PRK11121
anaerobic ribonucleoside-triphosphate reductase-activating protein;
1-154 3.48e-129

anaerobic ribonucleoside-triphosphate reductase-activating protein;


Pssm-ID: 236853  Cd Length: 154  Bit Score: 357.38  E-value: 3.48e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490282490   1 MNYHQYYPVDIVNGPGTRCTLFVSGCVHECPGCYNKSTWRVNSGMPFTAEMADRIIADLNDTRIKRQGLSLSGGDPLHPQ 80
Cdd:PRK11121   1 MNYHQYYPVDVVNGPGTRCTLFVSGCVHQCPGCYNKSTWRLNSGHPFTKEMEDQIIADLNDTRIKRQGLSLSGGDPLHPQ 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490282490  81 NVADILKLVQRVRAECPGKDIWVWTGYKLDELNEAQMQVVNLINVLVDGKFVQDLKDPALIWRGSSNQVVHHLR 154
Cdd:PRK11121  81 NVPDILKLVQRVKAECPGKDIWVWTGYKLDELNAAQRQVVDLIDVLVDGKFVQDLADPSLIWRGSSNQVIHRLR 154
NrdG TIGR02491
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
 2-154 2.84e-88

anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of the radical-SAM family (pfam04055) and utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487). The two components form an alpha-2/beta-2 heterodimer. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism, Protein fate, Protein modification and repair]


Pssm-ID: 274161 [Multi-domain]  Cd Length: 154  Bit Score: 254.20  E-value: 2.84e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490282490    2 NYHQYYPVDIVNGPGTRCTLFVSGCVHECPGCYNKSTWRVNSGMPFTAEMADRIIADLNDTRiKRQGLSLSGGDPLHPQN 81
Cdd:TIGR02491   1 NYMNIKPDDIVNGEGIRVSLFVAGCKHHCEGCFNKETWNFNGGKEFTEALEKEIIRDLNDNP-LIDGLTLSGGDPLYPRN 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490282490   82 VADILKLVQRVRAECPGKDIWVWTGYKLDELNEAQMQ--VVNLINVLVDGKFVQDLKDPALIWRGSSNQVVHHLR 154
Cdd:TIGR02491  80 VEELIELVKKIKAEFPEKDIWLWTGYTWEEILEDEKHleVLKYIDVLVDGKFELSKKDLKLKFRGSSNQRIIDLK 154
Fer4_12 pfam13353
4Fe-4S single cluster domain; This family includes proteins containing domains which bind to ...
 12-151 3.01e-80

4Fe-4S single cluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 433138 [Multi-domain]  Cd Length: 137  Bit Score: 233.22  E-value: 3.01e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490282490   12 VNGPGTRCTLFVSGCVHECPGCYNKSTWRVNSGMPFTAEMADRIIADLNDTRIkrQGLSLSGGDPLHpqNVADILKLVQR 91
Cdd:pfam13353   1 VNGPGVRCSLFVSGCNHHCKGCFNPETWDFKYGKPFTEELEDEIIEDLAKPYI--QGLTLSGGEPLL--NAEALLELVKR 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490282490   92 VRAECPGKDIWVWTGYKLDEL-NEAQMQVVNLINVLVDGKFVQDLKDPALIWRGSSNQVVH 151
Cdd:pfam13353  77 VREECPEKDIWLWTGYTFEELqSKDQLELLKLIDVLVDGKFEQSLKDPSLRFRGSSNQRII 137
Fer4_14 pfam13394
4Fe-4S single cluster domain;
21-130 8.96e-53

4Fe-4S single cluster domain;


Pssm-ID: 433171 [Multi-domain]  Cd Length: 115  Bit Score: 162.92  E-value: 8.96e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490282490   21 LFVSGCVHECPGCYNKSTWRVNSGMPFTAEMADRIIADLNDTRIKRQGLSLSGGDPLHPQNVADILKLVQRVRAECPGKD 100
Cdd:pfam13394   1 LFVSGCNHSCPGCDNKETWKFNYGEPFTEELEDQIIADLKDSYIKRQGLVLTGGEPLHPWNLPVLLKLLKRVKEEYPSKD 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 490282490  101 IWVWTGYKLDE-----LNEAQMQVVNLINVLVDGK 130
Cdd:pfam13394  81 IWLETGYTLAIdfeypDTEEQLFTLSVIDVLVDGK 115
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
 8-136 2.04e-08

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


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 51.34  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490282490   8 PVDIVNGPGT-RCTLFVSGCVHECPGCYNKSTWRVNSGMPFTAEMADRIIADLNDTRI---KRQGLSLSGGDPL-HPQNV 82
Cdd:COG1180   12 PFSTVDGPGSiRLSVFTQGCNLRCPYCHNPEISQGRPDAAGRELSPEELVEEALKDRGfldSCGGVTFSGGEPTlQPEFL 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490282490  83 ADILKLVQRvraecpgKDI---WVWTGY----KLDELneaqMQVVNLINVlvdgkfvqDLK 136
Cdd:COG1180   92 LDLAKLAKE-------LGLhtaLDTNGYipeeALEEL----LPYLDAVNI--------DLK 133
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
 30-111 3.06e-06

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: 44.51  E-value: 3.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490282490  30 CPGCYNKSTWRVNSGMPFtaEMADRIIADLNDTRIKRqgLSLSGGDPL-HPqnvaDILKLVQRVRAEcpGKDIWVWT-GY 107
Cdd:COG0535   14 CKHCYADAGPKRPGELST--EEAKRILDELAELGVKV--VGLTGGEPLlRP----DLFELVEYAKEL--GIRVNLSTnGT 83


                 ....
gi 490282490 108 KLDE 111
Cdd:COG0535   84 LLTE 87
RNR_activ_nrdG3 TIGR02826
anaerobic ribonucleoside-triphosphate reductase activating protein; Members of this family ...
 21-154 1.22e-05

anaerobic ribonucleoside-triphosphate reductase activating protein; Members of this family represent a set of radical SAM enzymes related to, yet architecturally different from, the activating protein for the glycine radical-containing, oxygen-sensitive ribonucleoside-triphosphate reductase (RNR) as described in model TIGR02491. Members of this family are found paired with members of a similarly divergent set of anaerobic ribonucleoside-triphosphate reductases. Identification of this protein as an RNR activitating protein is partly from pairing with a candidate RNR. It is further supported by our finding that upstream of these operons are examples of a conserved regulatory element (described Rodionov and Gelfand) that is found in nearly all bacteria and that occurs specifically upstream of operons for all three classes of RNR genes. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]


Pssm-ID: 274317  Cd Length: 147  Bit Score: 42.72  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490282490   21 LFVSGCVHECPGCYNKSTWRVNSGMPFTAEMADRIIaDLNDTRIkrQGLSLSGGDplhpQNVADILKLVQRVRAECPGKD 100
Cdd:TIGR02826  20 FYISGCPLGCPGCHSPELWHEDEGTPLTPEVLAQLL-DKYRSLI--TCVLFLGGE----WEPEALLSLLKYVKEHAGLKV 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 490282490  101 IWvWTGYKLDELNEAQMQVvnliNVLVDGKFVQD---LKDPAliwrgsSNQVVHHLR 154
Cdd:TIGR02826  93 CL-YTGREPKDPLELVQHL----DYLKTGPWIETlggLDSPT------TNQRFYDIR 138
pflA PRK11145
pyruvate formate lyase 1-activating protein;
3-87 3.61e-05

pyruvate formate lyase 1-activating protein;


Pssm-ID: 182994 [Multi-domain]  Cd Length: 246  Bit Score: 42.32  E-value: 3.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490282490   3 YHQYYPVDIVNGPGTRCTLFVSGCVHECPGCYNKSTWRVNSGMPFTAEmadRIIADLNDTR----IKRQGLSLSGGDP-L 77
Cdd:PRK11145   7 IHSFESCGTVDGPGIRFITFFQGCLMRCLYCHNRDTWDTHGGKEVTVE---ELMKEVVTYRhfmnASGGGVTASGGEAiL 83

                         90
                 ....*....|
gi 490282490  78 HPQNVADILK 87
Cdd:PRK11145  84 QAEFVRDWFR 93
NrdG2 TIGR02495
anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of ...
 2-95 1.27e-04

anaerobic ribonucleoside-triphosphate reductase activating protein; This enzyme is a member of the radical-SAM family (pfam04055). It is often gene clustered with the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487) and presumably fulfills the identical function as NrdG, which utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in NrdD. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism, Protein fate, Protein modification and repair]


Pssm-ID: 274164 [Multi-domain]  Cd Length: 192  Bit Score: 40.42  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490282490    2 NYHQYYPVDIVNGPG-TRCTLFVSGCVHECPGCYNkstWRVNsgMPFTAEMAD--RIIADLNDTRIKRQGLSLSGGDPLH 78
Cdd:TIGR02495   1 RIAGLVPFSTVDYPGkLAFTIFLQGCNLKCPYCHN---PLLI--PRRGSGEIEveELLEFLRRRRGLLDGVVITGGEPTL 75

                          90
                  ....*....|....*..
gi 490282490   79 PQNVADILKLVQRVRAE 95
Cdd:TIGR02495  76 QAGLPDFLREVRELGFE 92
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
 22-95 3.01e-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: 39.05  E-value: 3.01e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490282490   22 FVSGCVHECPGCYNKSTWRVNSGMPFTAEMADRIIADLNDTRIKRqgLSLSGGDP-LHPQNVADILKLVQRVRAE 95
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKGRELSPEEILEEAKELKRLGVEV--VILGGGEPlLLPDLVELLERLLKLELAE 73
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
 25-137 6.43e-04

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.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 38.47  E-value: 6.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490282490  25 GCVHECPGCYNKSTwrvNSGMPFTAEMADRIIADLnDTRIKRQ--GLSLSGGDPLHPQNVADILKlvqRVRAECPGKDI- 101
Cdd:cd01335    6 GCNLNCGFCSNPAS---KGRGPESPPEIEEILDIV-LEAKERGveVVILTGGEPLLYPELAELLR---RLKKELPGFEIs 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 490282490 102 WVWTGYK-----LDELNEAqmqVVNLINVLVDGKFVQDLKD 137
Cdd:cd01335   79 IETNGTLlteelLKELKEL---GLDGVGVSLDSGDEEVADK 116
 
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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