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Conserved domains on  [gi|225734347]
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Protein Classification

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List of domain hits

Name Accession Description Interval E-value
lys_2_3_AblA super family cl31474
lysine-2,3-aminomutase; This model describes lysine-2,3-aminomutase as found along with ...
11-412 0e+00

lysine-2,3-aminomutase; This model describes lysine-2,3-aminomutase as found along with beta-lysine acetyltransferase in a two-enzyme pathway for making the compatible solute N-epsilon-acetyl-beta-lysine. This compatible solute, or osmolyte, is known to protect a number of methanogenic archaea against salt stress. The trusted cutoff distinguishes a tight clade with essentially full-length homology from additional homologs that are shorter or highly diverged in the C-terminal region. All members of this family have the radical SAM motif CXXXCXXC, while some but not all have a second copy of the motif in the C-terminal region.


The actual alignment was detected with superfamily member TIGR03820:

Pssm-ID: 163532 [Multi-domain]  Cd Length: 417  Bit Score: 650.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347   11 DVSDADWNDWRWQVRNRIETVEELKKY--IPLTKEEEEGVAQCVKSLR*AITPYYLSLIDPNDP-NDPVRKQAIPTALEL 87
Cdd:TIGR03820   1 NATESEWKDWKWQLRHSIRDIDTFEKLlgITFSEEEREELKETLEKFPMSITPYYLSLIDPEDLrNDPIFMQSFPSPAEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347   88 NKAAADLEDPLHEDTDSPVPGLTHRYPDRVLLLITD*CS*YCRHCTRRRFAGQSDDS*P*ERIDKAIDYIRNTPQVRDVL 167
Cdd:TIGR03820  81 IVSNHDMEDPLAEDEDSPVPGITHRYPDRVLFLVSNTCAMYCRHCTRKRKVGDRDSIPSKEQILEGIEYIRNTPQIRDVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347  168 LSGGDALLVSDETLEYIIAKLREIPHVEIVRIGSRTPVVLPQRITPELVN*LKKYHPVWLNTHFNHPNEITEESTRACQL 247
Cdd:TIGR03820 161 LSGGDPLLLSDDYLDWILTELRAIPHVEVIRIGTRVPVVLPQRITDELVAILKKHHPVWLNTHFNHPREITASSKKALAK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347  248 LADAGVPLGNQSVLLRGVNDCVHV*KELVNKLVKIRVRPYYIYQCDLSLGLEHFRTPVSKGIEIIEGLRGHTSGYCVPTF 327
Cdd:TIGR03820 241 LADAGIPLGNQSVLLAGVNDCPRIMKKLVHKLVANRVRPYYLYQCDLSEGLSHFRTPVGKGIEIIESLIGHTSGFAVPTY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347  328 VVDAPGGGGKTPV*PNYVISQSHDKVILRNFEGVITTYSEPINYTPG-C--NCDVC------TGKKKVHKVGVAGLLNGE 398
Cdd:TIGR03820 321 VVDAPGGGGKIPVMPNYLISWSTNKVVLRNYEGVITTYKEPDSYEPTfCdrNCDDCdlqlnlEDADESRAIGIEKLLSDH 400
                         410
                  ....*....|....*.
gi 225734347  399 G--*ALEPVGLERNKR 412
Cdd:TIGR03820 401 DdtISLVPENNERLER 416
 
Name Accession Description Interval E-value
lys_2_3_AblA TIGR03820
lysine-2,3-aminomutase; This model describes lysine-2,3-aminomutase as found along with ...
11-412 0e+00

lysine-2,3-aminomutase; This model describes lysine-2,3-aminomutase as found along with beta-lysine acetyltransferase in a two-enzyme pathway for making the compatible solute N-epsilon-acetyl-beta-lysine. This compatible solute, or osmolyte, is known to protect a number of methanogenic archaea against salt stress. The trusted cutoff distinguishes a tight clade with essentially full-length homology from additional homologs that are shorter or highly diverged in the C-terminal region. All members of this family have the radical SAM motif CXXXCXXC, while some but not all have a second copy of the motif in the C-terminal region.


Pssm-ID: 163532 [Multi-domain]  Cd Length: 417  Bit Score: 650.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347   11 DVSDADWNDWRWQVRNRIETVEELKKY--IPLTKEEEEGVAQCVKSLR*AITPYYLSLIDPNDP-NDPVRKQAIPTALEL 87
Cdd:TIGR03820   1 NATESEWKDWKWQLRHSIRDIDTFEKLlgITFSEEEREELKETLEKFPMSITPYYLSLIDPEDLrNDPIFMQSFPSPAEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347   88 NKAAADLEDPLHEDTDSPVPGLTHRYPDRVLLLITD*CS*YCRHCTRRRFAGQSDDS*P*ERIDKAIDYIRNTPQVRDVL 167
Cdd:TIGR03820  81 IVSNHDMEDPLAEDEDSPVPGITHRYPDRVLFLVSNTCAMYCRHCTRKRKVGDRDSIPSKEQILEGIEYIRNTPQIRDVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347  168 LSGGDALLVSDETLEYIIAKLREIPHVEIVRIGSRTPVVLPQRITPELVN*LKKYHPVWLNTHFNHPNEITEESTRACQL 247
Cdd:TIGR03820 161 LSGGDPLLLSDDYLDWILTELRAIPHVEVIRIGTRVPVVLPQRITDELVAILKKHHPVWLNTHFNHPREITASSKKALAK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347  248 LADAGVPLGNQSVLLRGVNDCVHV*KELVNKLVKIRVRPYYIYQCDLSLGLEHFRTPVSKGIEIIEGLRGHTSGYCVPTF 327
Cdd:TIGR03820 241 LADAGIPLGNQSVLLAGVNDCPRIMKKLVHKLVANRVRPYYLYQCDLSEGLSHFRTPVGKGIEIIESLIGHTSGFAVPTY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347  328 VVDAPGGGGKTPV*PNYVISQSHDKVILRNFEGVITTYSEPINYTPG-C--NCDVC------TGKKKVHKVGVAGLLNGE 398
Cdd:TIGR03820 321 VVDAPGGGGKIPVMPNYLISWSTNKVVLRNYEGVITTYKEPDSYEPTfCdrNCDDCdlqlnlEDADESRAIGIEKLLSDH 400
                         410
                  ....*....|....*.
gi 225734347  399 G--*ALEPVGLERNKR 412
Cdd:TIGR03820 401 DdtISLVPENNERLER 416
EpmB COG1509
L-lysine 2,3-aminomutase (EF-P beta-lysylation pathway) [Amino acid transport and metabolism];
7-371 0e+00

L-lysine 2,3-aminomutase (EF-P beta-lysylation pathway) [Amino acid transport and metabolism];


Pssm-ID: 224426  Cd Length: 369  Bit Score: 564.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347   7 ELFKDVSDADWNDWRWQVRNRIETVEELKKYIPLTKEEEEGVAQCVKSLR*AITPYYLSLIDPNDPNDPVRKQAIPTALE 86
Cdd:COG1509    3 ILTRNVPEEEWEDWLWQLANAIRDPRELLEVLNLDEEELEGLERAAKLFALRITPYYLSLIDWGNPDDPIRRQVIPSEDE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347  87 LNKAAADLEDPLHEDTDSPVPGLTHRYPDRVLLLITD*CS*YCRHCTRRRFAGQSDDS*P*ERIDKAIDYIRNTPQVRDV 166
Cdd:COG1509   83 LEKAPGESEDPLGEDDSSPVPGLTHRYPDRVLLLVTGVCAVYCRYCFRRRFVGQDNQGFNKEEWDKALDYIAAHPEIREV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347 167 LLSGGDALLVSDETLEYIIAKLREIPHVEIVRIGSRTPVVLPQRITPELVN*LKK-YHPVWLNTHFNHPNEITEESTRAC 245
Cdd:COG1509  163 LLSGGDPLSLSDKKLEWLLKRLRAIPHVKIIRIGTRLPVVLPQRITDELCEILGKsRKPVWLVTHFNHPNEITPEAREAC 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347 246 QLLADAGVPLGNQSVLLRGVNDCVHV*KELVNKLVKIRVRPYYIYQCDLSLGLEHFRTPVSKGIEIIEGLRGHTSGYCVP 325
Cdd:COG1509  243 AKLRDAGVPLLNQSVLLRGVNDDPEVLKELSRALFDAGVKPYYLHQLDLVQGAAHFRVPIAEGLQIVEELRGRTSGYAVP 322
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 225734347 326 TFVVDAPGGGGKTPV*PNYVISQSHDKVILRNFEGVITTYSEPINY 371
Cdd:COG1509  323 TLVVDIPGGGGKTPLAPNYRESQSYGKRVLRNFEGKIMTYPEPLQY 368
LAM_C pfam12544
Lysine-2,3-aminomutase; This domain family is found in bacteria, archaea and eukaryotes, and ...
312-416 2.95e-48

Lysine-2,3-aminomutase; This domain family is found in bacteria, archaea and eukaryotes, and is typically between 111 and 127 amino acids in length. The family is found in association with pfam04055. LAM catalyzes the interconversion of L-alpha-lysine and L-beta-lysine, which proceeds by migration of the amino group from C2 to C3 concomitant with cross-migration of the 3-pro-R hydrogen of L-alpha-lysine to the 2-pro-R position of L-beta-lysine.


Pssm-ID: 378876  Cd Length: 127  Bit Score: 160.68  E-value: 2.95e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347  312 IEGLRGHTSGYCVPTFVVDAPGGGGKTPV*PNYVISQSHDKVILRNFEGVITTYSEPINYTPGcNCDVC-------TGKK 384
Cdd:pfam12544   1 IEGLRGHTSGYAVPTFVVDAPGGGGKIALQPNYLISQSPDKVVLRNFEGVITSYPEPENYVPG-KADDYfagvypdTADK 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 225734347  385 KVHkVGVAGLLNGEG*ALEPVGLERNKRHVQE 416
Cdd:pfam12544  80 KSP-VGISALLNDSEISLTPENLKRLERREAY 110
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
119-314 3.97e-19

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: 85.08  E-value: 3.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347 119 LLITD*CS*YCRHCTRRRFAGQSDDS*P*ERIDKAIDYIRNTPQVRDVLLSGGDALLVsDETLEYIIAKLREIPHVEIvR 198
Cdd:cd01335    1 LELTRGCNLNCGFCSNPASKGRGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLY-PELAELLRRLKKELPGFEI-S 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347 199 IGSRTPVvlpqrITPELVN*LKKYHPVWLNTHFNHPNEIT-----------EESTRACQLLADAGVPLGNQSVLLRGVND 267
Cdd:cd01335   79 IETNGTL-----LTEELLKELKELGLDGVGVSLDSGDEEVadkirgsgesfKERLEALKELREAGLGLSTTLLVGLGDED 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 225734347 268 CVHV*KELVNKLVKIRVRPYYIYQCDLS----LGLEHFRTPVSKGIEIIEG 314
Cdd:cd01335  154 EEDDLEELELLAEFRSPDRVSLFRLLPEegtpLELAAPVVPAEKLLRLIAA 204
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
116-252 1.61e-06

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 48.55  E-value: 1.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347   116 RVLLLITD*CS*YCRHCTRRRFAGQSDDS*P---*ERIDKAIDYIRNTPQVRDVLLSGGDALLVSDETLEYIIAKLREIp 192
Cdd:smart00729   2 LALYIITRGCPRRCTFCSFPSLRGKLRSRYLealVREIELLAEKGEKEGLVGTVFIGGGTPTLLSPEQLEELLEAIREI- 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225734347   193 hVEIVRIGSRTPVVLPQRITPELVN*LKKYHPVWLN---THFNhpNEI---------TEESTRACQLLADAG 252
Cdd:smart00729  81 -LGLAKDVEITIETRPDTLTEELLEALKEAGVNRVSlgvQSGD--DEVlkainrghtVEDVLEAVELLREAG 149
 
Name Accession Description Interval E-value
lys_2_3_AblA TIGR03820
lysine-2,3-aminomutase; This model describes lysine-2,3-aminomutase as found along with ...
11-412 0e+00

lysine-2,3-aminomutase; This model describes lysine-2,3-aminomutase as found along with beta-lysine acetyltransferase in a two-enzyme pathway for making the compatible solute N-epsilon-acetyl-beta-lysine. This compatible solute, or osmolyte, is known to protect a number of methanogenic archaea against salt stress. The trusted cutoff distinguishes a tight clade with essentially full-length homology from additional homologs that are shorter or highly diverged in the C-terminal region. All members of this family have the radical SAM motif CXXXCXXC, while some but not all have a second copy of the motif in the C-terminal region.


Pssm-ID: 163532 [Multi-domain]  Cd Length: 417  Bit Score: 650.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347   11 DVSDADWNDWRWQVRNRIETVEELKKY--IPLTKEEEEGVAQCVKSLR*AITPYYLSLIDPNDP-NDPVRKQAIPTALEL 87
Cdd:TIGR03820   1 NATESEWKDWKWQLRHSIRDIDTFEKLlgITFSEEEREELKETLEKFPMSITPYYLSLIDPEDLrNDPIFMQSFPSPAEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347   88 NKAAADLEDPLHEDTDSPVPGLTHRYPDRVLLLITD*CS*YCRHCTRRRFAGQSDDS*P*ERIDKAIDYIRNTPQVRDVL 167
Cdd:TIGR03820  81 IVSNHDMEDPLAEDEDSPVPGITHRYPDRVLFLVSNTCAMYCRHCTRKRKVGDRDSIPSKEQILEGIEYIRNTPQIRDVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347  168 LSGGDALLVSDETLEYIIAKLREIPHVEIVRIGSRTPVVLPQRITPELVN*LKKYHPVWLNTHFNHPNEITEESTRACQL 247
Cdd:TIGR03820 161 LSGGDPLLLSDDYLDWILTELRAIPHVEVIRIGTRVPVVLPQRITDELVAILKKHHPVWLNTHFNHPREITASSKKALAK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347  248 LADAGVPLGNQSVLLRGVNDCVHV*KELVNKLVKIRVRPYYIYQCDLSLGLEHFRTPVSKGIEIIEGLRGHTSGYCVPTF 327
Cdd:TIGR03820 241 LADAGIPLGNQSVLLAGVNDCPRIMKKLVHKLVANRVRPYYLYQCDLSEGLSHFRTPVGKGIEIIESLIGHTSGFAVPTY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347  328 VVDAPGGGGKTPV*PNYVISQSHDKVILRNFEGVITTYSEPINYTPG-C--NCDVC------TGKKKVHKVGVAGLLNGE 398
Cdd:TIGR03820 321 VVDAPGGGGKIPVMPNYLISWSTNKVVLRNYEGVITTYKEPDSYEPTfCdrNCDDCdlqlnlEDADESRAIGIEKLLSDH 400
                         410
                  ....*....|....*.
gi 225734347  399 G--*ALEPVGLERNKR 412
Cdd:TIGR03820 401 DdtISLVPENNERLER 416
EpmB COG1509
L-lysine 2,3-aminomutase (EF-P beta-lysylation pathway) [Amino acid transport and metabolism];
7-371 0e+00

L-lysine 2,3-aminomutase (EF-P beta-lysylation pathway) [Amino acid transport and metabolism];


Pssm-ID: 224426  Cd Length: 369  Bit Score: 564.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347   7 ELFKDVSDADWNDWRWQVRNRIETVEELKKYIPLTKEEEEGVAQCVKSLR*AITPYYLSLIDPNDPNDPVRKQAIPTALE 86
Cdd:COG1509    3 ILTRNVPEEEWEDWLWQLANAIRDPRELLEVLNLDEEELEGLERAAKLFALRITPYYLSLIDWGNPDDPIRRQVIPSEDE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347  87 LNKAAADLEDPLHEDTDSPVPGLTHRYPDRVLLLITD*CS*YCRHCTRRRFAGQSDDS*P*ERIDKAIDYIRNTPQVRDV 166
Cdd:COG1509   83 LEKAPGESEDPLGEDDSSPVPGLTHRYPDRVLLLVTGVCAVYCRYCFRRRFVGQDNQGFNKEEWDKALDYIAAHPEIREV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347 167 LLSGGDALLVSDETLEYIIAKLREIPHVEIVRIGSRTPVVLPQRITPELVN*LKK-YHPVWLNTHFNHPNEITEESTRAC 245
Cdd:COG1509  163 LLSGGDPLSLSDKKLEWLLKRLRAIPHVKIIRIGTRLPVVLPQRITDELCEILGKsRKPVWLVTHFNHPNEITPEAREAC 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347 246 QLLADAGVPLGNQSVLLRGVNDCVHV*KELVNKLVKIRVRPYYIYQCDLSLGLEHFRTPVSKGIEIIEGLRGHTSGYCVP 325
Cdd:COG1509  243 AKLRDAGVPLLNQSVLLRGVNDDPEVLKELSRALFDAGVKPYYLHQLDLVQGAAHFRVPIAEGLQIVEELRGRTSGYAVP 322
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 225734347 326 TFVVDAPGGGGKTPV*PNYVISQSHDKVILRNFEGVITTYSEPINY 371
Cdd:COG1509  323 TLVVDIPGGGGKTPLAPNYRESQSYGKRVLRNFEGKIMTYPEPLQY 368
Glu_2_3_NH3_mut TIGR04368
glutamate 2,3-aminomutase; Members of this family are glutamate 2,3-aminomutase, a radical SAM ...
13-366 0e+00

glutamate 2,3-aminomutase; Members of this family are glutamate 2,3-aminomutase, a radical SAM enzyme with a pyridoxal phosphate group. It is closely related to lysine 2,3-aminomutase, but distinguished by architecture (longer N-terminal region, shorter C-terminal region) and replacement of key lysine-binding residues Asp293 and Asp330 (inferred from the crystal structure) by glutamate-binding residues Lys and Asn. Activity was demonstrated for sequences from Clostridium difficile, Thermoanaerobacter tengcongensis MB4, and Syntrophomonas wolfei str. Goettingen. The action of this enzyme creates beta-glutamate, an osmolyte. [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 275161  Cd Length: 404  Bit Score: 521.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347   13 SDADWNDWRWQVRNRIETVEELKKYIPLTKEEEEGVAQCVKSLR*AITPYYLSLIDPNDPNDPVRKQAIPTALELNKAAA 92
Cdd:TIGR04368  51 TEEDWNDWKWQLKNRISDVETLSKILNLTEEEIEEIKKVGRKYRWAISPYYLSLMDPDNPNCPIRLQSIPSIAELLDEKG 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347   93 DlEDPLHEDTDSPVPGLTHRYPDRVLLLITD*CS*YCRHCTRRRFAGQSDDS*P*ERIDKAIDYIRNTPQVRDVLLSGGD 172
Cdd:TIGR04368 131 E-LDPMGEEFTSPAPAITRRYPDRLIINVTNQCAMYCRHCQRRRNIGEVDRHASREDLEAALDYIRNNPEIRDVLITGGD 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347  173 ALLVSDETLEYIIAKLREIPHVEIVRIGSRTPVVLPQRITPELVN*LKKYHPVWLNTHFNHPNEITEESTRACQLLADAG 252
Cdd:TIGR04368 210 ALLLSDETLDWLLTELDNIPHVEIKRIGTRVPVTLPQRITDELCAILKKHPPIYINTQFNHPLEVTPEAKEACDKLIKAG 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347  253 VPLGNQSVLLRGVNDCVHV*KELVNKLVKIRVRPYYIYQCDLSLGLEHFRTPVSKGIEIIEGLRGHTSGYCVPTFVVDAP 332
Cdd:TIGR04368 290 VVLGNQAVLLKGINNDPHVMKKLNQELLKIRVRPYYIFHAKPVKGTSHFITSVEEGLEIMEKLRGYTSGLAVPTYIINAP 369
                         330       340       350
                  ....*....|....*....|....*....|....
gi 225734347  333 GGGGKTPV*PNYVISQSHDKVILRNFEGVITTYS 366
Cdd:TIGR04368 370 GGYGKTPILPQYLLSRGEDKVVIRTWEGKVFEYP 403
arg_2_3_am_muta TIGR04468
arginine 2,3-aminomutase; Members of this family are arginine 2,3-aminomutase, a radical SAM ...
16-360 7.71e-145

arginine 2,3-aminomutase; Members of this family are arginine 2,3-aminomutase, a radical SAM enzyme more closely related to lysine 2,3-aminomutase than to glutamate 2,3-aminomutase. The enzyme makes L-beta-arginine, sometimes in the context of antibiotic biosynthesis (blasticidin S, mildiomycin, etc). Activity is proven in Streptomyces griseochromogenes, which makes blasticidin S.


Pssm-ID: 275261  Cd Length: 351  Bit Score: 415.67  E-value: 7.71e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347   16 DWNDWRWQVRNRIETVEELKKYIPLTKEEEEGVAQCVKSLR*AITPYYLSLIDPNDPNDPVRKQAIPTALELNKAAADLE 95
Cdd:TIGR04468   1 QWNDWKFQLRNRIRTLEQLKEWVNVSPEEEKAIAATEGKYRWMVTPYYASLMDKTDPNCPIRLQAIPHLGEFMENQGADV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347   96 DPLHEDTDSPVPGLTHRYPDRVLLLITD*CS*YCRHCTRR----RFAGQSDDS*P*ERIDKAIDYIRNTPQVRDVLLSGG 171
Cdd:TIGR04468  81 DPVGDTKYRKTNRVVHKYPDRVIMLVTDTCPVYCRHCTRKyhttDVNGTYFERDEAESYEEDFEYIANHPEIRDVLLTGG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347  172 DALLVSDETLEYIIAKLREIPHVEIVRIGSRTPVVLPQRITPELVN*LKKYHPVWLNTHFNHPNEITEESTRACQLLADA 251
Cdd:TIGR04468 161 DPLTYSDKKLESIISRLRSIPHVEIIRIGSRYPVLLPQRITDEFCQMLEKYHPIWLNTHFNHPKEVTPEAASACDRLLRH 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347  252 GVPLGNQSVLLRGVNDCVHV*KELVNKLVKIRVRPYYIYQCDLSLGLEHFRTPVSKGIEIIEGLRGHTSGYCVPTFVVDA 331
Cdd:TIGR04468 241 GIPVQNQTVLLKGINDDLETMRALLRALLKIRVRPYYLYHCDNVTGVSHFMTSLEKGREIMRGLVGYETGFAVPQYVITT 320
                         330       340
                  ....*....|....*....|....*....
gi 225734347  332 PggGGKTPV*PNYVISQShDKVILRNFEG 360
Cdd:TIGR04468 321 K--LGKIPLNRQYVVEQG-DGLILRNYEG 346
TIGR00238 TIGR00238
KamA family protein; This model represents essentially the whole of E. coli YjeK and of some ...
5-333 3.65e-138

KamA family protein; This model represents essentially the whole of E. coli YjeK and of some of its apparent orthologs. YodO in Bacillus subtilis, a family member which is longer protein by an additional 100 residues, is characterized as a lysine 2,3-aminomutase with iron, sulphide and pyridoxal 5'-phosphate groups. The homolog MJ0634 from M. jannaschii is preceded by nearly 200 C-terminal residues. This family shows similarity to molybdenum cofactor biosynthesis protein MoaA and related proteins. Note that the E. coli homolog was expressed in E. coli and purified and found not to display display lysine 2,3-aminomutase activity. Active site residues are found in 100 residue extension in B. subtilis. Name changed to KamA family protein. [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 272980  Cd Length: 331  Bit Score: 398.05  E-value: 3.65e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347    5 RYELFKDVSDADWNDWRWQVRNRIETVEELKKYIPLTKEEEEGVAQCVKSL-R*AITPYYLSLIDPNDPNDPVRKQAIPT 83
Cdd:TIGR00238   2 IIEEFFGVTREEWFNWLWQLKNVVRDLKGLKKLLNISDEDLEEIERAAKKLiPLRVTPYYIDLMDKGNPDDPVRRQVIPS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347   84 ALELNKAAADLEDPLHEDTDSPVPGLTHRYPDRVLLLITD*CS*YCRHCTRRRFAGQSDDS*p*ERIDKAIDYIRNTPQV 163
Cdd:TIGR00238  82 SEEFVEAMGFSTDPLEEHDTSPVPGLTHRYVNRALFLVKGGCAVNCRYCFRRHFPYKENPGN-KKKWQKALDYIAEHPEI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347  164 RDVLLSGGDALLVSDETLEYIIAKLREIPHVEIVRIGSRTPVVLPQRITPELVN*LKK-YHPVWLNTHFNHPNEITEEST 242
Cdd:TIGR00238 161 IEILISGGDPLMAKDHELEWLLKRLEEIPHLVRLRIGTRLPVVIPQRITDELCELLASfELQLMLVTHINHCNEITEEFA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347  243 RACQLLADAGVPLGNQSVLLRGVNDCVHV*KELVNKLVKIRVRPYYIYQCDLSLGLEHFRTPVSKGIEIIEGLRGHTSGY 322
Cdd:TIGR00238 241 EAMKKLRTVNVTLLNQSVLLRGVNDRAQILAKLSIALFKVGIIPYYLHYLDKVQGAKHFLVPDAEAAQIVKELARLTSGY 320
                         330
                  ....*....|.
gi 225734347  323 CVPTFVVDAPG 333
Cdd:TIGR00238 321 LVPKFAVEIMG 331
AblA_like_2 TIGR03822
lysine-2,3-aminomutase-related protein; Members of this protein form a distinctive clade, ...
28-345 2.25e-104

lysine-2,3-aminomutase-related protein; Members of this protein form a distinctive clade, homologous to lysine-2,3-aminomutase (of Bacillus, Clostridium, and methanogenic archaea) and likely similar in function. Members of this family are found in Rhodopseudomonas, Caulobacter crescentus, Bradyrhizobium, etc.


Pssm-ID: 163534  Cd Length: 321  Bit Score: 311.69  E-value: 2.25e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347   28 IETVEELKKYIPLTKEEEEGVAQCVKSLR*AITPYYLSLIDPNDPNDPVRKQAIPTALELNKAAADLEDPLHEDTDSPVP 107
Cdd:TIGR03822   1 LRTADDLIEAGLIPAAALAALEAVAARYAIAITPALAALIDRDDPDDPIARQFVPDPAELVTAPEERADPIGDDAHSPVP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347  108 GLTHRYPDRVLLLITD*CS*YCRHCTRRRFAG-QSDDS*P*ERIDKAIDYIRNTPQVRDVLLSGGDALLVSDETLEYIIA 186
Cdd:TIGR03822  81 GIVHRYPDRVLLKPVHVCPVYCRFCFRREMVGpEGLGVLSPAELDAAFAYIADHPEIWEVILTGGDPLVLSPRRLGDIMA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347  187 KLREIPHVEIVRIGSRTPVVLPQRITPELVN*LKKY-HPVWLNTHFNHPNEITEESTRACQLLADAGVPLGNQSVLLRGV 265
Cdd:TIGR03822 161 RLAAIDHVKIVRFHTRVPVADPARVTPALIAALKTSgKTVYVALHANHARELTAEARAACARLIDAGIPMVSQSVLLRGV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347  266 NDCVHV*KELVNKLVKIRVRPYYIYQCDLSLGLEHFRTPVSKGIEIIEGLRGHTSGYCVPTFVVDAPGGGGKTPV*PNYV 345
Cdd:TIGR03822 241 NDDPETLAALMRAFVECRIKPYYLHHLDLAPGTAHFRVTIEEGQALVRALRGRISGLAQPTYVLDIPGGHGKAPVGPSYL 320
EFP_modif_epmB TIGR03821
EF-P beta-lysylation protein EpmB; Members of this radical SAM protein subfamily, including ...
63-340 4.08e-76

EF-P beta-lysylation protein EpmB; Members of this radical SAM protein subfamily, including yjeK in E. coli, form a distinctive clade, homologous to lysine-2,3-aminomutase of Bacillus, Clostridium, and methanogenic archaea. Members of this family are found in E. coli, Buchnera, Yersinia, etc. The gene symbol is now reassigned as EpmB (Elongation factor P Modification B). [Protein fate, Protein modification and repair]


Pssm-ID: 163533  Cd Length: 321  Bit Score: 239.14  E-value: 4.08e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347   63 YLSLIDPNDPNDPVRKQAIPTALELNKAAADLEDPLHEDTDSPVPGLTHRYPDRVLLLITD*CS*YCRHCTRRRFAGQsD 142
Cdd:TIGR03821  44 FVARMKKGDPDDPLLRQVLPLHAEFEQHPGYSADPLDEQDANPVPGLLHKYHGRVLLIVTGGCAINCRYCFRRHFPYQ-E 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347  143 DS*P*ERIDKAIDYIRNTPQVRDVLLSGGDALLVSDETLEYIIAKLREIPHVEIVRIGSRTPVVLPQRITPELVN*LKK- 221
Cdd:TIGR03821 123 NQPNKAQWKEALEYIAQHPEINEVILSGGDPLMAKDHRLDWLLNLLEQIPHLKRLRIHTRLPVVIPDRITSGLCDLLANs 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347  222 -YHPVWLnTHFNHPNEITEESTRACQLLADAGVPLGNQSVLLRGVNDCVHV*KELVNKLVKIRVRPYYIYQCDLSLGLEH 300
Cdd:TIGR03821 203 rLQTVLV-VHINHANEIDAEVADALAKLRNAGITLLNQSVLLRGVNDNADTLAALSERLFDAGVLPYYLHLLDKVQGAAH 281
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 225734347  301 FRTPVSKGIEIIEGLRGHTSGYCVPTFVVDAPGGGGKTPV 340
Cdd:TIGR03821 282 FDVDDERARALMAELLARLPGYLVPRLVREIPGEPSKTPL 321
LAM_C pfam12544
Lysine-2,3-aminomutase; This domain family is found in bacteria, archaea and eukaryotes, and ...
312-416 2.95e-48

Lysine-2,3-aminomutase; This domain family is found in bacteria, archaea and eukaryotes, and is typically between 111 and 127 amino acids in length. The family is found in association with pfam04055. LAM catalyzes the interconversion of L-alpha-lysine and L-beta-lysine, which proceeds by migration of the amino group from C2 to C3 concomitant with cross-migration of the 3-pro-R hydrogen of L-alpha-lysine to the 2-pro-R position of L-beta-lysine.


Pssm-ID: 378876  Cd Length: 127  Bit Score: 160.68  E-value: 2.95e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347  312 IEGLRGHTSGYCVPTFVVDAPGGGGKTPV*PNYVISQSHDKVILRNFEGVITTYSEPINYTPGcNCDVC-------TGKK 384
Cdd:pfam12544   1 IEGLRGHTSGYAVPTFVVDAPGGGGKIALQPNYLISQSPDKVVLRNFEGVITSYPEPENYVPG-KADDYfagvypdTADK 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 225734347  385 KVHkVGVAGLLNGEG*ALEPVGLERNKRHVQE 416
Cdd:pfam12544  80 KSP-VGISALLNDSEISLTPENLKRLERREAY 110
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
119-314 3.97e-19

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: 85.08  E-value: 3.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347 119 LLITD*CS*YCRHCTRRRFAGQSDDS*P*ERIDKAIDYIRNTPQVRDVLLSGGDALLVsDETLEYIIAKLREIPHVEIvR 198
Cdd:cd01335    1 LELTRGCNLNCGFCSNPASKGRGPESPPEIEEILDIVLEAKERGVEVVILTGGEPLLY-PELAELLRRLKKELPGFEI-S 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347 199 IGSRTPVvlpqrITPELVN*LKKYHPVWLNTHFNHPNEIT-----------EESTRACQLLADAGVPLGNQSVLLRGVND 267
Cdd:cd01335   79 IETNGTL-----LTEELLKELKELGLDGVGVSLDSGDEEVadkirgsgesfKERLEALKELREAGLGLSTTLLVGLGDED 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 225734347 268 CVHV*KELVNKLVKIRVRPYYIYQCDLS----LGLEHFRTPVSKGIEIIEG 314
Cdd:cd01335  154 EEDDLEELELLAEFRSPDRVSLFRLLPEegtpLELAAPVVPAEKLLRLIAA 204
Radical_SAM pfam04055
Radical SAM superfamily. Radical SAM proteins catalyze diverse reactions, including unusual ...
121-267 7.41e-15

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


Pssm-ID: 367788  Cd Length: 160  Bit Score: 71.78  E-value: 7.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347  121 ITD*CS*YCRHCTRRRFAGQSD-DS*P*ERIDKAIDYIRNTPQVRDVLLSGGDALLVSDetLEYIIAKLREIPHVEIVRI 199
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRGRGKgRELSPEEILEEAKELKARLGVEVVILGGGEPLLLPD--LVELLLRLLKLELAEGIRI 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225734347  200 GSRTPvvlPQRITPELVN*LKKYHPVWLNTHFNHPNEIT----------EESTRACQLLADAGVP-LGNQSVLLRGVND 267
Cdd:pfam04055  79 TLETN---GTLLDEELLELLKEAGLDRVSIGLESGDDEVlklinrkhtfEEVLEAIELLREAGIPvVTDNIVGLPGETD 154
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
116-252 1.61e-06

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 48.55  E-value: 1.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347   116 RVLLLITD*CS*YCRHCTRRRFAGQSDDS*P---*ERIDKAIDYIRNTPQVRDVLLSGGDALLVSDETLEYIIAKLREIp 192
Cdd:smart00729   2 LALYIITRGCPRRCTFCSFPSLRGKLRSRYLealVREIELLAEKGEKEGLVGTVFIGGGTPTLLSPEQLEELLEAIREI- 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225734347   193 hVEIVRIGSRTPVVLPQRITPELVN*LKKYHPVWLN---THFNhpNEI---------TEESTRACQLLADAG 252
Cdd:smart00729  81 -LGLAKDVEITIETRPDTLTEELLEALKEAGVNRVSlgvQSGD--DEVlkainrghtVEDVLEAVELLREAG 149
COG1244 COG1244
Uncharacterized Fe-S cluster-containing protein. MiaB family [General function prediction only] ...
101-224 1.44e-03

Uncharacterized Fe-S cluster-containing protein. MiaB family [General function prediction only];


Pssm-ID: 224165 [Multi-domain]  Cd Length: 358  Bit Score: 40.46  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225734347 101 DTDSPV-----PGLTHRYPDRVLLLI--TD*CS*Y----CRHCTRrrFAGQSDDS*P*ERIDKAIDYIRNT------PQV 163
Cdd:COG1244   26 DPDKPVavwieEDRLRGYPGKSLTVIlrTRGCRWYreggCYMCGY--PADSAGEPVSEENLINQFDEAYSKyegkfdEFV 103
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225734347 164 RDVLLSGG--DALLVSDETLEYIIAKLREIPHVEIVRIGSRtpvvlPQRITPELVN*LKKYHP 224
Cdd:COG1244  104 VKIFTSGSflDPEEVPREARRYILERISENDNVKEVVVESR-----PEFIREERLEEITEILE 161
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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