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Conserved domains on  [gi|1100259255|gb|OIK40846|]
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thiamine biosynthesis protein ThiH [Citrobacter portucalensis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
thiH super family cl31200
thiazole biosynthesis protein ThiH; Members this protein family are the ThiH protein of ...
3-369 0e+00

thiazole biosynthesis protein ThiH; Members this protein family are the ThiH protein of thiamine biosynthesis, a homolog of the BioB protein of biotin biosynthesis. Genes for the this protein generally are found in operons with other thiamin biosynthesis genes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


The actual alignment was detected with superfamily member TIGR02351:

Pssm-ID: 131404 [Multi-domain]  Cd Length: 366  Bit Score: 585.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255   3 TFSDRWRQLDWDDIRLRINGKTAADVERALNASHLSRDDLMALLSPAAADYLEPLAQRAQKLTRQRFGNTVSFYVPLYLS 82
Cdd:TIGR02351   1 TFKDEIEDILWEEVSYDIYSFTAADVERALNKRHLSLEDFLALLSPAAEPYLEEMAQKAKKLTRKRFGNTISLFTPLYLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255  83 NLCANDCTYCGFSMSNRIKRKTLDEDEIIRECAAIRELGFEHLLLVTGEHQAKVGMDYFRRHLPAIRRQFASLQMEVQPL 162
Cdd:TIGR02351  81 NYCSNKCVYCGFSMSNKIKRKKLNEEEIEREIEAIKKSGFKEILLVTGESEKAAGVEYIAEAIKLAREYFSSLAIEVQPL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255 163 SEAEYAELKTLGLDGVMVYQESYHEATYARHHLKGKKQDFFWRLETPDRLGRAGIDKIGLGALIGLSDsWRVDCYMVAEH 242
Cdd:TIGR02351 161 NEEEYKKLVEAGLDGVTVYQETYNEKKYKKHHLAGKKKDFRYRLNTPERAAKAGMRKIGIGALLGLDD-WRTDAFFTAYH 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255 243 LLWMQQHYWQSRYSISFPRLRPCTGGVEPASIMDERQLVQTICAFRLLAPEIELSLSTRESPWFRDHVIPLAINNVSAFS 322
Cdd:TIGR02351 240 LRYLQKKYWKTEISISVPRLRPCTNGLKPKVIVTDRELVQIICAYRLFDPFVEISLSTRESKKFRDNVIPLGITKMSAGS 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1100259255 323 KTQPGGYADNHPELEQFSPHDDRRPEAVAEALMAQGLQPVWKDWDSY 369
Cdd:TIGR02351 320 STEPGGYSSEKKGLEQFEISDERSVAEVEEDLRSKGLQPVWKDWDYF 366
 
Name Accession Description Interval E-value
thiH TIGR02351
thiazole biosynthesis protein ThiH; Members this protein family are the ThiH protein of ...
3-369 0e+00

thiazole biosynthesis protein ThiH; Members this protein family are the ThiH protein of thiamine biosynthesis, a homolog of the BioB protein of biotin biosynthesis. Genes for the this protein generally are found in operons with other thiamin biosynthesis genes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 131404 [Multi-domain]  Cd Length: 366  Bit Score: 585.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255   3 TFSDRWRQLDWDDIRLRINGKTAADVERALNASHLSRDDLMALLSPAAADYLEPLAQRAQKLTRQRFGNTVSFYVPLYLS 82
Cdd:TIGR02351   1 TFKDEIEDILWEEVSYDIYSFTAADVERALNKRHLSLEDFLALLSPAAEPYLEEMAQKAKKLTRKRFGNTISLFTPLYLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255  83 NLCANDCTYCGFSMSNRIKRKTLDEDEIIRECAAIRELGFEHLLLVTGEHQAKVGMDYFRRHLPAIRRQFASLQMEVQPL 162
Cdd:TIGR02351  81 NYCSNKCVYCGFSMSNKIKRKKLNEEEIEREIEAIKKSGFKEILLVTGESEKAAGVEYIAEAIKLAREYFSSLAIEVQPL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255 163 SEAEYAELKTLGLDGVMVYQESYHEATYARHHLKGKKQDFFWRLETPDRLGRAGIDKIGLGALIGLSDsWRVDCYMVAEH 242
Cdd:TIGR02351 161 NEEEYKKLVEAGLDGVTVYQETYNEKKYKKHHLAGKKKDFRYRLNTPERAAKAGMRKIGIGALLGLDD-WRTDAFFTAYH 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255 243 LLWMQQHYWQSRYSISFPRLRPCTGGVEPASIMDERQLVQTICAFRLLAPEIELSLSTRESPWFRDHVIPLAINNVSAFS 322
Cdd:TIGR02351 240 LRYLQKKYWKTEISISVPRLRPCTNGLKPKVIVTDRELVQIICAYRLFDPFVEISLSTRESKKFRDNVIPLGITKMSAGS 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1100259255 323 KTQPGGYADNHPELEQFSPHDDRRPEAVAEALMAQGLQPVWKDWDSY 369
Cdd:TIGR02351 320 STEPGGYSSEKKGLEQFEISDERSVAEVEEDLRSKGLQPVWKDWDYF 366
ThiH COG1060
2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme ...
26-365 4.64e-100

2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme transport and metabolism]; 2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440680 [Multi-domain]  Cd Length: 351  Bit Score: 300.51  E-value: 4.64e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255  26 ADVERALNASHLSRDDLMALLSPAAADyLEPLAQRAQKLTRQRFGNTVSF--YVPLYLSNLCANDCTYCGFSMSNR-IKR 102
Cdd:COG1060     1 EILEKALAGERLSLEDALALLSPAAAD-LEELAELADELRRRRFGNTVTFvvNRPINLTNVCVNGCKFCAFSRDNGdIDR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255 103 KTLDEDEIIRECAAIRELGFEHLLLVTGEHQaKVGMDYFRRHLPAIRRQFAslQMEVQPLSEAEYAELKTL--------- 173
Cdd:COG1060    80 YTLSPEEILEEAEEAKALGATEILLVGGEHP-DLPLEYYLDLLRAIKERFP--NIHIHALSPEEIAHLARAsglsveevl 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255 174 ------GLDGVMVYQESYHEATYaRHHLKGKKQDFFWRLETPDRLGRAGIDkIGLGALIGLSDsWRVDCYMVAEHLLWMQ 247
Cdd:COG1060   157 erlkeaGLDSLPGGGAEILDDEV-RHPIGPGKIDYEEWLEVMERAHELGIR-TTATMLYGHVE-TREERVDHLLHLRELQ 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255 248 QHYWQSRYSISFpRLRPC-TGGVEPASIMDERQLVQTICAFRLLAPEIE------LSLSTRespwFRDHVIPLAINNVSA 320
Cdd:COG1060   234 DETGGFTEFIPL-RFRPAnTPLYLERPGVSDRELLKLIAVARLFLPNIGniqaswVSLGTR----LRQLALSLGANDLGG 308
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1100259255 321 FSKTQPGGYADNHPEleqfspHDDRRPEAVAEALMAQGLQPVWKD 365
Cdd:COG1060   309 TSMEENIVRAAGGEE------GDERSVEELIRLIREAGRIPVERD 347
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
79-286 2.15e-20

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: 88.16  E-value: 2.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255  79 LYLSNLCANDCTYCGFSMSNRIKRKTLDE-DEIIRECAAIRELGFEHLLLVTGEHQAkvgMDYFRRHLPAIRRQFAS--L 155
Cdd:cd01335     1 LELTRGCNLNCGFCSNPASKGRGPESPPEiEEILDIVLEAKERGVEVVILTGGEPLL---YPELAELLRRLKKELPGfeI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255 156 QMEVQP--LSEAEYAELKTLGLDGVMVYQESYHEATYARHHlkGKKQDFFWRLETPDRLGRAGIdKIGLGALIGLSDSWR 233
Cdd:cd01335    78 SIETNGtlLTEELLKELKELGLDGVGVSLDSGDEEVADKIR--GSGESFKERLEALKELREAGL-GLSTTLLVGLGDEDE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1100259255 234 VDcymVAEHLLWMQQHYWQSRYSISFPRLRPCTGGVEPASIMDERQLVQTICA 286
Cdd:cd01335   155 ED---DLEELELLAEFRSPDRVSLFRLLPEEGTPLELAAPVVPAEKLLRLIAA 204
BATS smart00876
Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), , catalyses the last ...
258-361 2.13e-19

Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), , catalyses the last step of the biotin biosynthetic pathway. The reaction consists in the introduction of a sulphur atom into dethiobiotin. BioB functions as a homodimer. Thiamin synthesis if a complex process involving at least six gene products (ThiFSGH, ThiI and ThiJ). Two of the proteins required for the biosynthesis of the thiazole moiety of thiamine (vitamin B(1)) are ThiG and ThiH (this entry) and form a heterodimer. Both of these reactions are thought of involve the binding of co-factors, and both function as dimers.. This domain therefore may be involved in co-factor binding or dimerisation.


Pssm-ID: 214877 [Multi-domain]  Cd Length: 94  Bit Score: 82.14  E-value: 2.13e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255  258 SFPRLRPCTGGV--EPASIMDERQLVQTICAFRLLAPEIELSLSTRESPWFRDhvipLAINNVSAFSKTQPGGYadnhpe 335
Cdd:smart00876   1 PINRLRPIEGTPleDPPPPVSPEEFLRTIAAARLALPDAGIRLSTGREALLRD----LQALCFSAGANSIFGGD------ 70
                           90       100
                   ....*....|....*....|....*.
gi 1100259255  336 lEQFSPHDDRRPEAVAeALMAQGLQP 361
Cdd:smart00876  71 -KYLTTSGPRSADDVA-MLEKLGLEP 94
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
81-235 1.19e-11

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: 62.54  E-value: 1.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255  81 LSNLCANDCTYCGFS-MSNRIKRKTLDEDEIIRECAAIRELGFEHLLLVTGEHQAKVGMDYFRRHLpAIRRQFASLQMEV 159
Cdd:pfam04055   1 ITRGCNLRCTYCAFPsIRARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERL-LKLELAEGIRITL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255 160 QP----LSEAEYAELKTLGLDGVMVYQESYHEATYARHhlkGKKQDFFWRLETPDRLGRAGID--KIGLGALIGLSDSWR 233
Cdd:pfam04055  80 ETngtlLDEELLELLKEAGLDRVSIGLESGDDEVLKLI---NRGHTFEEVLEALELLREAGIPvvTDNIVGLPGETDEDL 156

                  ..
gi 1100259255 234 VD 235
Cdd:pfam04055 157 EE 158
PRK07360 PRK07360
FO synthase subunit 2; Reviewed
29-176 2.18e-07

FO synthase subunit 2; Reviewed


Pssm-ID: 236000 [Multi-domain]  Cd Length: 371  Bit Score: 52.20  E-value: 2.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255  29 ERALNASHLSRDDLMALLSPAAADYLEPLAQRAQKLTRQRFGNTVSFYVPL--YLSNLCANDCTYCGFSMS-NRIKRKTL 105
Cdd:PRK07360   12 ERARKGKDLSKEDALELLETTEPRRIFEILELADRLRKEQVGDTVTYVVNRniNFTNICEGHCGFCAFRRDeGDHGAFWL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255 106 DEDEIIRECAAIRELGFEHLLLVTGEHQAKVGMDYFRRHLPAIRRQFASLQ------MEVQ--------PLSEAeYAELK 171
Cdd:PRK07360   92 TIAEILEKAAEAVKRGATEVCIQGGLHPAADSLEFYLEILEAIKEEFPDIHlhafspMEVYfaaredglSYEEV-LKALK 170

                  ....*
gi 1100259255 172 TLGLD 176
Cdd:PRK07360  171 DAGLD 175
 
Name Accession Description Interval E-value
thiH TIGR02351
thiazole biosynthesis protein ThiH; Members this protein family are the ThiH protein of ...
3-369 0e+00

thiazole biosynthesis protein ThiH; Members this protein family are the ThiH protein of thiamine biosynthesis, a homolog of the BioB protein of biotin biosynthesis. Genes for the this protein generally are found in operons with other thiamin biosynthesis genes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 131404 [Multi-domain]  Cd Length: 366  Bit Score: 585.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255   3 TFSDRWRQLDWDDIRLRINGKTAADVERALNASHLSRDDLMALLSPAAADYLEPLAQRAQKLTRQRFGNTVSFYVPLYLS 82
Cdd:TIGR02351   1 TFKDEIEDILWEEVSYDIYSFTAADVERALNKRHLSLEDFLALLSPAAEPYLEEMAQKAKKLTRKRFGNTISLFTPLYLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255  83 NLCANDCTYCGFSMSNRIKRKTLDEDEIIRECAAIRELGFEHLLLVTGEHQAKVGMDYFRRHLPAIRRQFASLQMEVQPL 162
Cdd:TIGR02351  81 NYCSNKCVYCGFSMSNKIKRKKLNEEEIEREIEAIKKSGFKEILLVTGESEKAAGVEYIAEAIKLAREYFSSLAIEVQPL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255 163 SEAEYAELKTLGLDGVMVYQESYHEATYARHHLKGKKQDFFWRLETPDRLGRAGIDKIGLGALIGLSDsWRVDCYMVAEH 242
Cdd:TIGR02351 161 NEEEYKKLVEAGLDGVTVYQETYNEKKYKKHHLAGKKKDFRYRLNTPERAAKAGMRKIGIGALLGLDD-WRTDAFFTAYH 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255 243 LLWMQQHYWQSRYSISFPRLRPCTGGVEPASIMDERQLVQTICAFRLLAPEIELSLSTRESPWFRDHVIPLAINNVSAFS 322
Cdd:TIGR02351 240 LRYLQKKYWKTEISISVPRLRPCTNGLKPKVIVTDRELVQIICAYRLFDPFVEISLSTRESKKFRDNVIPLGITKMSAGS 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1100259255 323 KTQPGGYADNHPELEQFSPHDDRRPEAVAEALMAQGLQPVWKDWDSY 369
Cdd:TIGR02351 320 STEPGGYSSEKKGLEQFEISDERSVAEVEEDLRSKGLQPVWKDWDYF 366
ThiH COG1060
2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme ...
26-365 4.64e-100

2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme transport and metabolism]; 2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440680 [Multi-domain]  Cd Length: 351  Bit Score: 300.51  E-value: 4.64e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255  26 ADVERALNASHLSRDDLMALLSPAAADyLEPLAQRAQKLTRQRFGNTVSF--YVPLYLSNLCANDCTYCGFSMSNR-IKR 102
Cdd:COG1060     1 EILEKALAGERLSLEDALALLSPAAAD-LEELAELADELRRRRFGNTVTFvvNRPINLTNVCVNGCKFCAFSRDNGdIDR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255 103 KTLDEDEIIRECAAIRELGFEHLLLVTGEHQaKVGMDYFRRHLPAIRRQFAslQMEVQPLSEAEYAELKTL--------- 173
Cdd:COG1060    80 YTLSPEEILEEAEEAKALGATEILLVGGEHP-DLPLEYYLDLLRAIKERFP--NIHIHALSPEEIAHLARAsglsveevl 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255 174 ------GLDGVMVYQESYHEATYaRHHLKGKKQDFFWRLETPDRLGRAGIDkIGLGALIGLSDsWRVDCYMVAEHLLWMQ 247
Cdd:COG1060   157 erlkeaGLDSLPGGGAEILDDEV-RHPIGPGKIDYEEWLEVMERAHELGIR-TTATMLYGHVE-TREERVDHLLHLRELQ 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255 248 QHYWQSRYSISFpRLRPC-TGGVEPASIMDERQLVQTICAFRLLAPEIE------LSLSTRespwFRDHVIPLAINNVSA 320
Cdd:COG1060   234 DETGGFTEFIPL-RFRPAnTPLYLERPGVSDRELLKLIAVARLFLPNIGniqaswVSLGTR----LRQLALSLGANDLGG 308
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1100259255 321 FSKTQPGGYADNHPEleqfspHDDRRPEAVAEALMAQGLQPVWKD 365
Cdd:COG1060   309 TSMEENIVRAAGGEE------GDERSVEELIRLIREAGRIPVERD 347
rSAM_HydG TIGR03955
[FeFe] hydrogenase H-cluster radical SAM maturase HydG; This model describes the radical SAM ...
28-361 4.94e-51

[FeFe] hydrogenase H-cluster radical SAM maturase HydG; This model describes the radical SAM protein HydG. It is part of an enzyme metallocenter maturation system, working together with GTP-binding protein HydF and another radical SAM enzyme, HydE, in H-cluster maturation in [FeFe] hydrogenases. [Protein fate, Protein modification and repair]


Pssm-ID: 274879 [Multi-domain]  Cd Length: 471  Bit Score: 177.22  E-value: 4.94e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255  28 VERALNASHLSRDDLMALLSPAAADYLEPLAQRAQKLTRQRFGNTVSFYVPLYLSNLCANDCTYCGFSMSNR-IKRKTLD 106
Cdd:TIGR03955  38 LEKAAKCKGLTHREASVLLACEDPEKIEEIYKLAEQIKKKFYGNRIVMFAPLYLSNYCVNGCVYCPYHAKNKhIARKKLT 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255 107 EDEIIRECAAIRELGFEHLLLVTGEHQAKVGMDYFR---------RHLP-AIRRqfasLQMEVQPLSEAEYAELKTLGLD 176
Cdd:TIGR03955 118 QEEIRREVIALQDMGHKRLALEAGEDPVNNPIEYILesiktiysiKHKNgAIRR----VNVNIAATTVENYRKLKEAGIG 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255 177 GVMVYQESYHEATYARHHLKGKKQDFFWRLETPDRLGRAGIDKIGLGALIGLsDSWRVD---CYMVAEHLlwmQQHYWQS 253
Cdd:TIGR03955 194 TYILFQETYHKESYEELHPTGPKHDYAYHTEAMDRAMEGGIDDVGLGVLFGL-NLYRYDfagLLMHAEHL---EAVFGVG 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255 254 RYSISFPRLRPCTG---GVEPASIMDErqLVQTICA-FRLLAPEIELSLSTRESPWFRDHVIPLAINNVSAFSKTQPGGY 329
Cdd:TIGR03955 270 PHTISVPRIRPADDidpDDFDNGISDD--IFAKIVAcIRIAVPYTGMIISTRESQKVRERVLHLGISQISGGSRTSVGGY 347
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1100259255 330 ADNHPELE---QFSPHDDRRPEAVAEALMAQGLQP 361
Cdd:TIGR03955 348 AEPEPEDEnsaQFDVSDNRTLDEVVNWLMDLGYIP 382
BioB COG0502
Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or ...
37-303 2.05e-21

Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 440268 [Multi-domain]  Cd Length: 308  Bit Score: 93.19  E-value: 2.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255  37 LSRDDLMALLSpAAADYLEPLAQRAQKLTRQRFGNTVSFYVPLYL-SNLCANDCTYCGFSMSNR--IKRKTL-DEDEIIR 112
Cdd:COG0502     2 LTREEALALLE-LPDEELEDLLAAADEVREHFFGNKVQLCGLINIkSGGCPEDCKYCGQSAHNKtgIERYRLlSVEEILE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255 113 ECAAIRELGFEHLLLVT-GEHQAKVGMDYFRRHLPAIRRQF-----ASLQMevqpLSEAEYAELKTLGLDGVMVYQESyH 186
Cdd:COG0502    81 AARAAKEAGARRFCLVAsGRDPSDRDFEKVLEIVRAIKEELglevcASLGE----LSEEQAKRLKEAGVDRYNHNLET-S 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255 187 EATYARHHLKGKKQDffwRLETPDRLGRAGIdKIGLGALIGLSDSWRvdcyMVAEHLLWMQQHYWQSrYSISF--PrlRP 264
Cdd:COG0502   156 PELYPKICTTHTYED---RLDTLKNAREAGL-EVCSGGIVGMGETLE----DRADLLLTLAELDPDS-VPINPliP--IP 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1100259255 265 CT--GGVEPASIMDErqlVQTICAFRLLAPEIELSLST-RES 303
Cdd:COG0502   225 GTplEDAPPLDPEEF---LRTIAVARLLLPDALIRLSGgRET 263
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
79-286 2.15e-20

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: 88.16  E-value: 2.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255  79 LYLSNLCANDCTYCGFSMSNRIKRKTLDE-DEIIRECAAIRELGFEHLLLVTGEHQAkvgMDYFRRHLPAIRRQFAS--L 155
Cdd:cd01335     1 LELTRGCNLNCGFCSNPASKGRGPESPPEiEEILDIVLEAKERGVEVVILTGGEPLL---YPELAELLRRLKKELPGfeI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255 156 QMEVQP--LSEAEYAELKTLGLDGVMVYQESYHEATYARHHlkGKKQDFFWRLETPDRLGRAGIdKIGLGALIGLSDSWR 233
Cdd:cd01335    78 SIETNGtlLTEELLKELKELGLDGVGVSLDSGDEEVADKIR--GSGESFKERLEALKELREAGL-GLSTTLLVGLGDEDE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1100259255 234 VDcymVAEHLLWMQQHYWQSRYSISFPRLRPCTGGVEPASIMDERQLVQTICA 286
Cdd:cd01335   155 ED---DLEELELLAEFRSPDRVSLFRLLPEEGTPLELAAPVVPAEKLLRLIAA 204
BATS smart00876
Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), , catalyses the last ...
258-361 2.13e-19

Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), , catalyses the last step of the biotin biosynthetic pathway. The reaction consists in the introduction of a sulphur atom into dethiobiotin. BioB functions as a homodimer. Thiamin synthesis if a complex process involving at least six gene products (ThiFSGH, ThiI and ThiJ). Two of the proteins required for the biosynthesis of the thiazole moiety of thiamine (vitamin B(1)) are ThiG and ThiH (this entry) and form a heterodimer. Both of these reactions are thought of involve the binding of co-factors, and both function as dimers.. This domain therefore may be involved in co-factor binding or dimerisation.


Pssm-ID: 214877 [Multi-domain]  Cd Length: 94  Bit Score: 82.14  E-value: 2.13e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255  258 SFPRLRPCTGGV--EPASIMDERQLVQTICAFRLLAPEIELSLSTRESPWFRDhvipLAINNVSAFSKTQPGGYadnhpe 335
Cdd:smart00876   1 PINRLRPIEGTPleDPPPPVSPEEFLRTIAAARLALPDAGIRLSTGREALLRD----LQALCFSAGANSIFGGD------ 70
                           90       100
                   ....*....|....*....|....*.
gi 1100259255  336 lEQFSPHDDRRPEAVAeALMAQGLQP 361
Cdd:smart00876  71 -KYLTTSGPRSADDVA-MLEKLGLEP 94
rSAM_HydE TIGR03956
[FeFe] hydrogenase H-cluster radical SAM maturase HydE; This model describes the radical SAM ...
36-131 1.53e-12

[FeFe] hydrogenase H-cluster radical SAM maturase HydE; This model describes the radical SAM protein HydE, one of a pair of radical SAM proteins, along with GTP-binding protein HydF, for maturation of [Fe] hydrogenase in Chlamydomonas reinhardtii and numerous bacteria. [Protein fate, Protein modification and repair]


Pssm-ID: 274880 [Multi-domain]  Cd Length: 340  Bit Score: 67.97  E-value: 1.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255  36 HLSRDDLMALLSPAAADYLEPLAQRAQKLTRQRFGNTVSFYVPLYLSNLCANDCTYCGFSMSNR-IKRKTLDEDEIIREC 114
Cdd:TIGR03956  10 TLSKEEFKRLLENRDEEDAEYLFELAREVRLRYYGNKVYIRGLIEFTNYCKNDCYYCGIRKSNPnAERYRLTKEEILSCC 89
                          90
                  ....*....|....*..
gi 1100259255 115 AAIRELGFEHLLLVTGE 131
Cdd:TIGR03956  90 REGYELGFRTFVLQGGE 106
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
81-235 1.19e-11

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: 62.54  E-value: 1.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255  81 LSNLCANDCTYCGFS-MSNRIKRKTLDEDEIIRECAAIRELGFEHLLLVTGEHQAKVGMDYFRRHLpAIRRQFASLQMEV 159
Cdd:pfam04055   1 ITRGCNLRCTYCAFPsIRARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERL-LKLELAEGIRITL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255 160 QP----LSEAEYAELKTLGLDGVMVYQESYHEATYARHhlkGKKQDFFWRLETPDRLGRAGID--KIGLGALIGLSDSWR 233
Cdd:pfam04055  80 ETngtlLDEELLELLKEAGLDRVSIGLESGDDEVLKLI---NRGHTFEEVLEALELLREAGIPvvTDNIVGLPGETDEDL 156

                  ..
gi 1100259255 234 VD 235
Cdd:pfam04055 157 EE 158
BATS pfam06968
Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), EC:2.8.1.6, catalyzes ...
262-358 3.32e-09

Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), EC:2.8.1.6, catalyzes the last step of the biotin biosynthetic pathway. The reaction consists in the introduction of a sulphur atom into dethiobiotin. BioB functions as a homodimer. Thiamin synthesis if a complex process involving at least six gene products (ThiFSGH, ThiI and ThiJ). Two of the proteins required for the biosynthesis of the thiazole moiety of thiamine (vitamin B(1)) are ThiG and ThiH (this family) and form a heterodimer. Both of these reactions are thought of involve the binding of co-factors, and both function as dimers. This domain therefore may be involved in co-factor binding or dimerization (Finn, RD personal observation).


Pssm-ID: 462054 [Multi-domain]  Cd Length: 85  Bit Score: 53.23  E-value: 3.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255 262 LRPCTG-GVEPASIMDERQLVQTICAFRLLAPEIEL-SLSTRESPWFRDHVIPLA-INNVSAFSKtqpggyadnhpeleq 338
Cdd:pfam06968   1 LRPIPGtPLENQPPLSPEEALRTIAAFRLILPDAGIrLAGGRESMLFRQALLFLAgANSISAGSK--------------- 65
                          90       100
                  ....*....|....*....|
gi 1100259255 339 FSPHDDRRPEAVAEALMAQG 358
Cdd:pfam06968  66 FLTTDGRSPDEDIAMLEDLG 85
PRK07360 PRK07360
FO synthase subunit 2; Reviewed
29-176 2.18e-07

FO synthase subunit 2; Reviewed


Pssm-ID: 236000 [Multi-domain]  Cd Length: 371  Bit Score: 52.20  E-value: 2.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255  29 ERALNASHLSRDDLMALLSPAAADYLEPLAQRAQKLTRQRFGNTVSFYVPL--YLSNLCANDCTYCGFSMS-NRIKRKTL 105
Cdd:PRK07360   12 ERARKGKDLSKEDALELLETTEPRRIFEILELADRLRKEQVGDTVTYVVNRniNFTNICEGHCGFCAFRRDeGDHGAFWL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255 106 DEDEIIRECAAIRELGFEHLLLVTGEHQAKVGMDYFRRHLPAIRRQFASLQ------MEVQ--------PLSEAeYAELK 171
Cdd:PRK07360   92 TIAEILEKAAEAVKRGATEVCIQGGLHPAADSLEFYLEILEAIKEEFPDIHlhafspMEVYfaaredglSYEEV-LKALK 170

                  ....*
gi 1100259255 172 TLGLD 176
Cdd:PRK07360  171 DAGLD 175
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
85-228 5.83e-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: 46.63  E-value: 5.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255   85 CANDCTYCGFSmSNRIKRKTLDEDEIIRE----CAAIRELGFEHLLLVTGEHQAKVGMDYFRRHLPAIRRQFASLQ---- 156
Cdd:smart00729  11 CPRRCTFCSFP-SLRGKLRSRYLEALVREiellAEKGEKEGLVGTVFIGGGTPTLLSPEQLEELLEAIREILGLAKdvei 89
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1100259255  157 -MEVQP--LSEAEYAELKTLGLD----GVmvyqESYHEATYARhhlKGKKQDFFWRLETPDRLGRAGIDKIGLGALIGL 228
Cdd:smart00729  90 tIETRPdtLTEELLEALKEAGVNrvslGV----QSGDDEVLKA---INRGHTVEDVLEAVELLREAGPIKVSTDLIVGL 161
PRK08444 PRK08444
aminofutalosine synthase MqnE;
28-166 9.66e-06

aminofutalosine synthase MqnE;


Pssm-ID: 181426 [Multi-domain]  Cd Length: 353  Bit Score: 47.00  E-value: 9.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255  28 VERALNASHLSRDDLMALLspaaaDY-LEPLAQRAQKLTRQRFGNTVSFYVPLYL--SNLCANDCTYCGFSMSnrikRK- 103
Cdd:PRK08444    4 IEKLENNERLNQEEAVKLY-----DLdLFTLGKYADKKRTKLHGKKVYFNVNRHInpTNICADVCKFCAFSAH----RKn 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1100259255 104 ----TLDEDEIIRECAAIRELGFEHLLLVTGeHQAKVGMDYFRRHLPAIRRQFASLQmeVQPLSEAE 166
Cdd:PRK08444   75 pnpyTMSHEEILEIVKNSVKRGIKEVHIVSA-HNPNYGYEWYLEIFKKIKEAYPNLH--VKAMTAAE 138
TIGR00423 TIGR00423
radical SAM domain protein, CofH subfamily; This protein family includes the CofH protein of ...
82-176 1.10e-05

radical SAM domain protein, CofH subfamily; This protein family includes the CofH protein of coenzyme F(420) biosynthesis from Methanocaldococcus jannaschii, but appears to hit genomes more broadly than just the subset that make coenzyme F(420), so that narrower group is being built as a separate family. [Hypothetical proteins, Conserved]


Pssm-ID: 273071 [Multi-domain]  Cd Length: 309  Bit Score: 46.62  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255  82 SNLCANDCTYCGFsmSNRIKRKT---LDEDEIIRECAAIRELGFEHLLLVTGeHQAKVGMDYFRRHLPAIRRQFASLQ-- 156
Cdd:TIGR00423  12 TNICVGKCKFCAF--RAREKDKDayvLSLEEILEKVKEAVAKGATEVCIQGG-LNPQLDIEYYEELFRAIKQEFPDVHih 88
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1100259255 157 ----MEVQPLSEAE-------YAELKTLGLD 176
Cdd:TIGR00423  89 afspMEVYFLAKNEglsieevLKRLKKAGLD 119
PRK05927 PRK05927
dehypoxanthine futalosine cyclase;
54-156 4.06e-05

dehypoxanthine futalosine cyclase;


Pssm-ID: 135660 [Multi-domain]  Cd Length: 350  Bit Score: 45.26  E-value: 4.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255  54 LEPLAQRAQKLTRQRF-GNTVSFYV---PLYlSNLCANDCTYCGFSmsnrikRKTLDEDEIIRECAAIREL-------GF 122
Cdd:PRK05927   21 LEELQEHADSLRKQRYpQNTVTYVLdanPNY-TNICKIDCTFCAFY------RKPHSSDAYLLSFDEFRSLmqryvsaGV 93
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1100259255 123 EHLLLVTGEHqAKVGMDYFRRHLPAIRRQFASLQ 156
Cdd:PRK05927   94 KTVLLQGGVH-PQLGIDYLEELVRITVKEFPSLH 126
F420_cofH TIGR03551
7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofH subunit; This enzyme, together with ...
37-176 5.46e-05

7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofH subunit; This enzyme, together with CofG, complete the biosynthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, the chromophore of coenzyme F420. The chromophore is also used in cyanobacteria DNA photolyases. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 132590 [Multi-domain]  Cd Length: 343  Bit Score: 44.57  E-value: 5.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255  37 LSRDDLMALLSPAAAdyLEPLAQRAQKLTRQRFGNTVSFYVP--LYLSNLCANDCTYCGFSMSNRIKR-KTLDEDEIIRE 113
Cdd:TIGR03551   1 ITKEEALELFEARGN--LFELFRLADELRRDIVGDTVTYVVNrnINFTNVCYGGCGFCAFRKRKGDADaYLLSLEEIAER 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1100259255 114 CAAIRELGFEHLLLVTGEHqAKVGMDYFRRHLPAIRRQF------ASLQMEV------QPLSEAEY-AELKTLGLD 176
Cdd:TIGR03551  79 AAEAWKAGATEVCIQGGIH-PDLDGDFYLDILRAVKEEVpgmhihAFSPMEVyygarnSGLSVEEAlKRLKEAGLD 153
fbiC PRK09234
FO synthase; Reviewed
12-112 1.18e-03

FO synthase; Reviewed


Pssm-ID: 236422 [Multi-domain]  Cd Length: 843  Bit Score: 41.15  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100259255  12 DWDDIRLRINGKTAA-----DVERALNASH-----LSRDDLMALLSPAAADyLEPLAQRAQKLTRQRFGNTVSFYVP--L 79
Cdd:PRK09234  452 DWESIREQVHEGRAPeridtDVLAALRAAErdpagLTDDEALALFTADGPA-LEAVCRLADDLRRDVVGDDVTYVVNrnI 530
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1100259255  80 YLSNLCANDCTYCGFSmsnriKRK------TLDEDEIIR 112
Cdd:PRK09234  531 NFTNICYTGCRFCAFA-----QRKtdadayTLSLDEVAD 564
 
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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