NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|556315485|ref|WP_023294848|]
View 

MULTISPECIES: 2-iminoacetate synthase ThiH [Enterobacter]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
3-368 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: 583.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485    3 TFTERWRQLNWDDIALRINSKTAADVERALQARHLTREDLMALLSPAASAYLEPMAQRAQRLTRQRFGNTVSFYVPLYLS 82
Cdd:TIGR02351   1 TFKDEIEDILWEEVSYDIYSFTAADVERALNKRHLSLEDFLALLSPAAEPYLEEMAQKAKKLTRKRFGNTISLFTPLYLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485   83 NLCANDCTYCGFSMSNRIKRKTLDEAEIARECAAIREMGFEHLLLVTGEHQGKVGMDYFRRHLPAIRRQFASLQMEVQPL 162
Cdd:TIGR02351  81 NYCSNKCVYCGFSMSNKIKRKKLNEEEIEREIEAIKKSGFKEILLVTGESEKAAGVEYIAEAIKLAREYFSSLAIEVQPL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485  163 SQEEYAELKTLGLDGVMVYQETYHEATYARHHLKGKKQDFFFRLETPDRLGRAGIDKIGLGALIGLSDsWRVDCYMVAEH 242
Cdd:TIGR02351 161 NEEEYKKLVEAGLDGVTVYQETYNEKKYKKHHLAGKKKDFRYRLNTPERAAKAGMRKIGIGALLGLDD-WRTDAFFTAYH 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485  243 LLWLQQHYWQSRYSISFPRLRPCAGGIEPASLMDERQLVQTICAFRLLAPEVELSLSTRESPAFRDRVIPIAINNVSAFS 322
Cdd:TIGR02351 240 LRYLQKKYWKTEISISVPRLRPCTNGLKPKVIVTDRELVQIICAYRLFDPFVEISLSTRESKKFRDNVIPLGITKMSAGS 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 556315485  323 KTQPGGYADDHPELEQFAPHDGRRPEAVAAALTAQGLQPVWKDWDS 368
Cdd:TIGR02351 320 STEPGGYSSEKKGLEQFEISDERSVAEVEEDLRSKGLQPVWKDWDY 365
 
Name Accession Description Interval E-value
thiH TIGR02351
thiazole biosynthesis protein ThiH; Members this protein family are the ThiH protein of ...
3-368 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: 583.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485    3 TFTERWRQLNWDDIALRINSKTAADVERALQARHLTREDLMALLSPAASAYLEPMAQRAQRLTRQRFGNTVSFYVPLYLS 82
Cdd:TIGR02351   1 TFKDEIEDILWEEVSYDIYSFTAADVERALNKRHLSLEDFLALLSPAAEPYLEEMAQKAKKLTRKRFGNTISLFTPLYLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485   83 NLCANDCTYCGFSMSNRIKRKTLDEAEIARECAAIREMGFEHLLLVTGEHQGKVGMDYFRRHLPAIRRQFASLQMEVQPL 162
Cdd:TIGR02351  81 NYCSNKCVYCGFSMSNKIKRKKLNEEEIEREIEAIKKSGFKEILLVTGESEKAAGVEYIAEAIKLAREYFSSLAIEVQPL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485  163 SQEEYAELKTLGLDGVMVYQETYHEATYARHHLKGKKQDFFFRLETPDRLGRAGIDKIGLGALIGLSDsWRVDCYMVAEH 242
Cdd:TIGR02351 161 NEEEYKKLVEAGLDGVTVYQETYNEKKYKKHHLAGKKKDFRYRLNTPERAAKAGMRKIGIGALLGLDD-WRTDAFFTAYH 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485  243 LLWLQQHYWQSRYSISFPRLRPCAGGIEPASLMDERQLVQTICAFRLLAPEVELSLSTRESPAFRDRVIPIAINNVSAFS 322
Cdd:TIGR02351 240 LRYLQKKYWKTEISISVPRLRPCTNGLKPKVIVTDRELVQIICAYRLFDPFVEISLSTRESKKFRDNVIPLGITKMSAGS 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 556315485  323 KTQPGGYADDHPELEQFAPHDGRRPEAVAAALTAQGLQPVWKDWDS 368
Cdd:TIGR02351 320 STEPGGYSSEKKGLEQFEISDERSVAEVEEDLRSKGLQPVWKDWDY 365
ThiH COG1060
2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme ...
26-365 5.68e-99

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: 297.43  E-value: 5.68e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485  26 ADVERALQARHLTREDLMALLSPAASAyLEPMAQRAQRLTRQRFGNTVSF--YVPLYLSNLCANDCTYCGFSMSNR-IKR 102
Cdd:COG1060    1 EILEKALAGERLSLEDALALLSPAAAD-LEELAELADELRRRRFGNTVTFvvNRPINLTNVCVNGCKFCAFSRDNGdIDR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485 103 KTLDEAEIARECAAIREMGFEHLLLVTGEHQgKVGMDYFRRHLPAIRRQFAslQMEVQPLSQEEYAELKTL--------- 173
Cdd:COG1060   80 YTLSPEEILEEAEEAKALGATEILLVGGEHP-DLPLEYYLDLLRAIKERFP--NIHIHALSPEEIAHLARAsglsveevl 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485 174 ------GLDGVMVYQETYHEATYaRHHLKGKKQDFFFRLETPDRLGRAGIDkIGLGALIGLSDsWRVDCYMVAEHLLWLQ 247
Cdd:COG1060  157 erlkeaGLDSLPGGGAEILDDEV-RHPIGPGKIDYEEWLEVMERAHELGIR-TTATMLYGHVE-TREERVDHLLHLRELQ 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485 248 QHYWQSRYSISFpRLRPC----AGGIEPASlmdERQLVQTICAFRLLAPEVE------LSLSTRespaFRDRVIPIAINN 317
Cdd:COG1060  234 DETGGFTEFIPL-RFRPAntplYLERPGVS---DRELLKLIAVARLFLPNIGniqaswVSLGTR----LRQLALSLGAND 305
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 556315485 318 VSAFSKTQPGGYADDHPEleqfapHDGRRPEAVAAALTAQGLQPVWKD 365
Cdd:COG1060  306 LGGTSMEENIVRAAGGEE------GDERSVEELIRLIREAGRIPVERD 347
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
79-286 9.52e-21

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: 89.31  E-value: 9.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485  79 LYLSNLCANDCTYCGFSMSNRIKRKTLDEAEIARECAA-IREMGFEHLLLVTGEHqgkVGMDYFRRHLPAIRRQFAS--L 155
Cdd:cd01335    1 LELTRGCNLNCGFCSNPASKGRGPESPPEIEEILDIVLeAKERGVEVVILTGGEP---LLYPELAELLRRLKKELPGfeI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485 156 QMEVQP--LSQEEYAELKTLGLDGVMVYQETYHEATYARHHlkGKKQDFFFRLETPDRLGRAGIdKIGLGALIGLSDSWR 233
Cdd:cd01335   78 SIETNGtlLTEELLKELKELGLDGVGVSLDSGDEEVADKIR--GSGESFKERLEALKELREAGL-GLSTTLLVGLGDEDE 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 556315485 234 VDcymVAEHLLWLQQHYWqsRYSISFPRLRPCAGG--IEPASLMDERQLVQTICA 286
Cdd:cd01335  155 ED---DLEELELLAEFRS--PDRVSLFRLLPEEGTplELAAPVVPAEKLLRLIAA 204
BATS smart00876
Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), , catalyses the last ...
258-361 1.17e-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: 82.91  E-value: 1.17e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485   258 SFPRLRPCAGGI--EPASLMDERQLVQTICAFRLLAPEVELSLSTRESPAFRDrvIPIAInnVSAFSKTQPGGYaddhpe 335
Cdd:smart00876   1 PINRLRPIEGTPleDPPPPVSPEEFLRTIAAARLALPDAGIRLSTGREALLRD--LQALC--FSAGANSIFGGD------ 70
                           90       100
                   ....*....|....*....|....*.
gi 556315485   336 lEQFAPHDgRRPEAVAAALTAQGLQP 361
Cdd:smart00876  71 -KYLTTSG-PRSADDVAMLEKLGLEP 94
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
81-235 6.39e-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: 60.23  E-value: 6.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485   81 LSNLCANDCTYCGFS-MSNRIKRKTLDEAEIARECAAIREMGFEHLLLVTGEHQGKVGMDYFRRHLpAIRRQFASLQMEV 159
Cdd:pfam04055   1 ITRGCNLRCTYCAFPsIRARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERL-LKLELAEGIRITL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485  160 QP----LSQEEYAELKTLGLDGVMVYQETYHEATYARHhlkGKKQDFFFRLETPDRLGRAGID--KIGLGALIGLSDSWR 233
Cdd:pfam04055  80 ETngtlLDEELLELLKEAGLDRVSIGLESGDDEVLKLI---NRGHTFEEVLEALELLREAGIPvvTDNIVGLPGETDEDL 156

                  ..
gi 556315485  234 VD 235
Cdd:pfam04055 157 EE 158
PRK07360 PRK07360
FO synthase subunit 2; Reviewed
21-176 1.30e-08

FO synthase subunit 2; Reviewed


Pssm-ID: 236000 [Multi-domain]  Cd Length: 371  Bit Score: 56.05  E-value: 1.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485  21 NSKTAADV-ERALQARHLTREDLMALLSPAASAYLEPMAQRAQRLTRQRFGNTVSFYVPL--YLSNLCANDCTYCGFSMS 97
Cdd:PRK07360   3 TDQIFEDIlERARKGKDLSKEDALELLETTEPRRIFEILELADRLRKEQVGDTVTYVVNRniNFTNICEGHCGFCAFRRD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485  98 -NRIKRKTLDEAEIARECAAIREMGFEHLLLVTGEHQGKVGMDYFRRHLPAIRRQFASLQ------MEVQ------PLSQ 164
Cdd:PRK07360  83 eGDHGAFWLTIAEILEKAAEAVKRGATEVCIQGGLHPAADSLEFYLEILEAIKEEFPDIHlhafspMEVYfaaredGLSY 162
                        170
                 ....*....|...
gi 556315485 165 EE-YAELKTLGLD 176
Cdd:PRK07360 163 EEvLKALKDAGLD 175
 
Name Accession Description Interval E-value
thiH TIGR02351
thiazole biosynthesis protein ThiH; Members this protein family are the ThiH protein of ...
3-368 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: 583.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485    3 TFTERWRQLNWDDIALRINSKTAADVERALQARHLTREDLMALLSPAASAYLEPMAQRAQRLTRQRFGNTVSFYVPLYLS 82
Cdd:TIGR02351   1 TFKDEIEDILWEEVSYDIYSFTAADVERALNKRHLSLEDFLALLSPAAEPYLEEMAQKAKKLTRKRFGNTISLFTPLYLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485   83 NLCANDCTYCGFSMSNRIKRKTLDEAEIARECAAIREMGFEHLLLVTGEHQGKVGMDYFRRHLPAIRRQFASLQMEVQPL 162
Cdd:TIGR02351  81 NYCSNKCVYCGFSMSNKIKRKKLNEEEIEREIEAIKKSGFKEILLVTGESEKAAGVEYIAEAIKLAREYFSSLAIEVQPL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485  163 SQEEYAELKTLGLDGVMVYQETYHEATYARHHLKGKKQDFFFRLETPDRLGRAGIDKIGLGALIGLSDsWRVDCYMVAEH 242
Cdd:TIGR02351 161 NEEEYKKLVEAGLDGVTVYQETYNEKKYKKHHLAGKKKDFRYRLNTPERAAKAGMRKIGIGALLGLDD-WRTDAFFTAYH 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485  243 LLWLQQHYWQSRYSISFPRLRPCAGGIEPASLMDERQLVQTICAFRLLAPEVELSLSTRESPAFRDRVIPIAINNVSAFS 322
Cdd:TIGR02351 240 LRYLQKKYWKTEISISVPRLRPCTNGLKPKVIVTDRELVQIICAYRLFDPFVEISLSTRESKKFRDNVIPLGITKMSAGS 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 556315485  323 KTQPGGYADDHPELEQFAPHDGRRPEAVAAALTAQGLQPVWKDWDS 368
Cdd:TIGR02351 320 STEPGGYSSEKKGLEQFEISDERSVAEVEEDLRSKGLQPVWKDWDY 365
ThiH COG1060
2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme ...
26-365 5.68e-99

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: 297.43  E-value: 5.68e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485  26 ADVERALQARHLTREDLMALLSPAASAyLEPMAQRAQRLTRQRFGNTVSF--YVPLYLSNLCANDCTYCGFSMSNR-IKR 102
Cdd:COG1060    1 EILEKALAGERLSLEDALALLSPAAAD-LEELAELADELRRRRFGNTVTFvvNRPINLTNVCVNGCKFCAFSRDNGdIDR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485 103 KTLDEAEIARECAAIREMGFEHLLLVTGEHQgKVGMDYFRRHLPAIRRQFAslQMEVQPLSQEEYAELKTL--------- 173
Cdd:COG1060   80 YTLSPEEILEEAEEAKALGATEILLVGGEHP-DLPLEYYLDLLRAIKERFP--NIHIHALSPEEIAHLARAsglsveevl 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485 174 ------GLDGVMVYQETYHEATYaRHHLKGKKQDFFFRLETPDRLGRAGIDkIGLGALIGLSDsWRVDCYMVAEHLLWLQ 247
Cdd:COG1060  157 erlkeaGLDSLPGGGAEILDDEV-RHPIGPGKIDYEEWLEVMERAHELGIR-TTATMLYGHVE-TREERVDHLLHLRELQ 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485 248 QHYWQSRYSISFpRLRPC----AGGIEPASlmdERQLVQTICAFRLLAPEVE------LSLSTRespaFRDRVIPIAINN 317
Cdd:COG1060  234 DETGGFTEFIPL-RFRPAntplYLERPGVS---DRELLKLIAVARLFLPNIGniqaswVSLGTR----LRQLALSLGAND 305
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 556315485 318 VSAFSKTQPGGYADDHPEleqfapHDGRRPEAVAAALTAQGLQPVWKD 365
Cdd:COG1060  306 LGGTSMEENIVRAAGGEE------GDERSVEELIRLIREAGRIPVERD 347
rSAM_HydG TIGR03955
[FeFe] hydrogenase H-cluster radical SAM maturase HydG; This model describes the radical SAM ...
5-361 7.09e-55

[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: 187.24  E-value: 7.09e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485    5 TERWRQLNWDDIALrINSKtaadVERALQARHLTREDLMALLSPAASAYLEPMAQRAQRLTRQRFGNTVSFYVPLYLSNL 84
Cdd:TIGR03955  20 TLAYAEENKDNKEL-IDSI----LEKAAKCKGLTHREASVLLACEDPEKIEEIYKLAEQIKKKFYGNRIVMFAPLYLSNY 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485   85 CANDCTYCGFSMSNR-IKRKTLDEAEIARECAAIREMGFEHLLLVTGEHQGKVGMDYFR---------RHLP-AIRRqfa 153
Cdd:TIGR03955  95 CVNGCVYCPYHAKNKhIARKKLTQEEIRREVIALQDMGHKRLALEAGEDPVNNPIEYILesiktiysiKHKNgAIRR--- 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485  154 sLQMEVQPLSQEEYAELKTLGLDGVMVYQETYHEATYARHHLKGKKQDFFFRLETPDRLGRAGIDKIGLGALIGLsDSWR 233
Cdd:TIGR03955 172 -VNVNIAATTVENYRKLKEAGIGTYILFQETYHKESYEELHPTGPKHDYAYHTEAMDRAMEGGIDDVGLGVLFGL-NLYR 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485  234 VD---CYMVAEHllwLQQHYWQSRYSISFPRLRPcAGGIEPA----SLMDErqLVQTICA-FRLLAPEVELSLSTRESPA 305
Cdd:TIGR03955 250 YDfagLLMHAEH---LEAVFGVGPHTISVPRIRP-ADDIDPDdfdnGISDD--IFAKIVAcIRIAVPYTGMIISTRESQK 323
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 556315485  306 FRDRVIPIAINNVSAFSKTQPGGYADDHPELE---QFAPHDGRRPEAVAAALTAQGLQP 361
Cdd:TIGR03955 324 VRERVLHLGISQISGGSRTSVGGYAEPEPEDEnsaQFDVSDNRTLDEVVNWLMDLGYIP 382
BioB COG0502
Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or ...
37-303 4.22e-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: 92.42  E-value: 4.22e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485  37 LTREDLMALLSpAASAYLEPMAQRAQRLTRQRFGNTVSFYVPLYL-SNLCANDCTYCGFSMSNR--IKRKTL-DEAEIAR 112
Cdd:COG0502    2 LTREEALALLE-LPDEELEDLLAAADEVREHFFGNKVQLCGLINIkSGGCPEDCKYCGQSAHNKtgIERYRLlSVEEILE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485 113 ECAAIREMGFEHLLLVT-GEHQGKVGMDYFRRHLPAIRRQF-----ASLQMevqpLSQEEYAELKTLGLDGVMVYQETyH 186
Cdd:COG0502   81 AARAAKEAGARRFCLVAsGRDPSDRDFEKVLEIVRAIKEELglevcASLGE----LSEEQAKRLKEAGVDRYNHNLET-S 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485 187 EATYARHHLKGKKQDfffRLETPDRLGRAGIdKIGLGALIGLSDSWRvdcyMVAEHLLWLQQHYWQSrYSISFprLRPCA 266
Cdd:COG0502  156 PELYPKICTTHTYED---RLDTLKNAREAGL-EVCSGGIVGMGETLE----DRADLLLTLAELDPDS-VPINP--LIPIP 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 556315485 267 G----GIEPASLMDErqlVQTICAFRLLAPEVELSLST-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 9.52e-21

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: 89.31  E-value: 9.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485  79 LYLSNLCANDCTYCGFSMSNRIKRKTLDEAEIARECAA-IREMGFEHLLLVTGEHqgkVGMDYFRRHLPAIRRQFAS--L 155
Cdd:cd01335    1 LELTRGCNLNCGFCSNPASKGRGPESPPEIEEILDIVLeAKERGVEVVILTGGEP---LLYPELAELLRRLKKELPGfeI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485 156 QMEVQP--LSQEEYAELKTLGLDGVMVYQETYHEATYARHHlkGKKQDFFFRLETPDRLGRAGIdKIGLGALIGLSDSWR 233
Cdd:cd01335   78 SIETNGtlLTEELLKELKELGLDGVGVSLDSGDEEVADKIR--GSGESFKERLEALKELREAGL-GLSTTLLVGLGDEDE 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 556315485 234 VDcymVAEHLLWLQQHYWqsRYSISFPRLRPCAGG--IEPASLMDERQLVQTICA 286
Cdd:cd01335  155 ED---DLEELELLAEFRS--PDRVSLFRLLPEEGTplELAAPVVPAEKLLRLIAA 204
BATS smart00876
Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), , catalyses the last ...
258-361 1.17e-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: 82.91  E-value: 1.17e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485   258 SFPRLRPCAGGI--EPASLMDERQLVQTICAFRLLAPEVELSLSTRESPAFRDrvIPIAInnVSAFSKTQPGGYaddhpe 335
Cdd:smart00876   1 PINRLRPIEGTPleDPPPPVSPEEFLRTIAAARLALPDAGIRLSTGREALLRD--LQALC--FSAGANSIFGGD------ 70
                           90       100
                   ....*....|....*....|....*.
gi 556315485   336 lEQFAPHDgRRPEAVAAALTAQGLQP 361
Cdd:smart00876  71 -KYLTTSG-PRSADDVAMLEKLGLEP 94
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
81-235 6.39e-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: 60.23  E-value: 6.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485   81 LSNLCANDCTYCGFS-MSNRIKRKTLDEAEIARECAAIREMGFEHLLLVTGEHQGKVGMDYFRRHLpAIRRQFASLQMEV 159
Cdd:pfam04055   1 ITRGCNLRCTYCAFPsIRARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERL-LKLELAEGIRITL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485  160 QP----LSQEEYAELKTLGLDGVMVYQETYHEATYARHhlkGKKQDFFFRLETPDRLGRAGID--KIGLGALIGLSDSWR 233
Cdd:pfam04055  80 ETngtlLDEELLELLKEAGLDRVSIGLESGDDEVLKLI---NRGHTFEEVLEALELLREAGIPvvTDNIVGLPGETDEDL 156

                  ..
gi 556315485  234 VD 235
Cdd:pfam04055 157 EE 158
rSAM_HydE TIGR03956
[FeFe] hydrogenase H-cluster radical SAM maturase HydE; This model describes the radical SAM ...
28-194 8.33e-11

[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: 62.58  E-value: 8.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485   28 VERALQARHLTREDLMALLSPAASAYLEPMAQRAQRLTRQRFGNTVSFYVPLYLSNLCANDCTYCGFSMSNR-IKRKTLD 106
Cdd:TIGR03956   2 IDKLRKEHTLSKEEFKRLLENRDEEDAEYLFELAREVRLRYYGNKVYIRGLIEFTNYCKNDCYYCGIRKSNPnAERYRLT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485  107 EAEIARECAAIREMGFEHLLLvtgehQGkvGMD-YFRRH-----LPAIRRQF--ASLQMEVQPLSQEEYAELKTLGLDGV 178
Cdd:TIGR03956  82 KEEILSCCREGYELGFRTFVL-----QG--GEDpYFTDEriveiVSAIKEEYpdCAITLSLGEKSYESYQRYFDAGADRY 154
                         170
                  ....*....|....*.
gi 556315485  179 MVYQETYHEATYARHH 194
Cdd:TIGR03956 155 LLRHETANEEHYRKLH 170
BATS pfam06968
Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), EC:2.8.1.6, catalyzes ...
262-358 2.21e-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: 53.61  E-value: 2.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485  262 LRPCAG-GIEPASLMDERQLVQTICAFRLLAPEVEL-SLSTRESPAFRDRVI-PIAINNVSAFSKtqpggyaddhpeleq 338
Cdd:pfam06968   1 LRPIPGtPLENQPPLSPEEALRTIAAFRLILPDAGIrLAGGRESMLFRQALLfLAGANSISAGSK--------------- 65
                          90       100
                  ....*....|....*....|
gi 556315485  339 FAPHDGRRPEAVAAALTAQG 358
Cdd:pfam06968  66 FLTTDGRSPDEDIAMLEDLG 85
PRK07360 PRK07360
FO synthase subunit 2; Reviewed
21-176 1.30e-08

FO synthase subunit 2; Reviewed


Pssm-ID: 236000 [Multi-domain]  Cd Length: 371  Bit Score: 56.05  E-value: 1.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485  21 NSKTAADV-ERALQARHLTREDLMALLSPAASAYLEPMAQRAQRLTRQRFGNTVSFYVPL--YLSNLCANDCTYCGFSMS 97
Cdd:PRK07360   3 TDQIFEDIlERARKGKDLSKEDALELLETTEPRRIFEILELADRLRKEQVGDTVTYVVNRniNFTNICEGHCGFCAFRRD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485  98 -NRIKRKTLDEAEIARECAAIREMGFEHLLLVTGEHQGKVGMDYFRRHLPAIRRQFASLQ------MEVQ------PLSQ 164
Cdd:PRK07360  83 eGDHGAFWLTIAEILEKAAEAVKRGATEVCIQGGLHPAADSLEFYLEILEAIKEEFPDIHlhafspMEVYfaaredGLSY 162
                        170
                 ....*....|...
gi 556315485 165 EE-YAELKTLGLD 176
Cdd:PRK07360 163 EEvLKALKDAGLD 175
TIGR00423 TIGR00423
radical SAM domain protein, CofH subfamily; This protein family includes the CofH protein of ...
82-176 7.61e-06

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: 47.39  E-value: 7.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485   82 SNLCANDCTYCGFsmSNRIKRKT---LDEAEIARECAAIREMGFEHLLLVTGeHQGKVGMDYFRRHLPAIRRQFASLQ-- 156
Cdd:TIGR00423  12 TNICVGKCKFCAF--RAREKDKDayvLSLEEILEKVKEAVAKGATEVCIQGG-LNPQLDIEYYEELFRAIKQEFPDVHih 88
                          90       100       110
                  ....*....|....*....|....*....|.
gi 556315485  157 ----MEVQPLSQ-------EEYAELKTLGLD 176
Cdd:TIGR00423  89 afspMEVYFLAKneglsieEVLKRLKKAGLD 119
F420_cofH TIGR03551
7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofH subunit; This enzyme, together with ...
37-176 8.05e-06

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: 47.27  E-value: 8.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485   37 LTREDLMALLspAASAYLEPMAQRAQRLTRQRFGNTVSFYVP--LYLSNLCANDCTYCGFSMSNRIKR-KTLDEAEIARE 113
Cdd:TIGR03551   1 ITKEEALELF--EARGNLFELFRLADELRRDIVGDTVTYVVNrnINFTNVCYGGCGFCAFRKRKGDADaYLLSLEEIAER 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556315485  114 CAAIREMGFEHLLLVTGEHqGKVGMDYFRRHLPAIRRQF------ASLQMEV------QPLSQEEY-AELKTLGLD 176
Cdd:TIGR03551  79 AAEAWKAGATEVCIQGGIH-PDLDGDFYLDILRAVKEEVpgmhihAFSPMEVyygarnSGLSVEEAlKRLKEAGLD 153
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
85-228 6.35e-05

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: 43.54  E-value: 6.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485    85 CANDCTYCGFSmSNRIKRKTLDEAEIARECAAIREMGFEHLLLVT----GEHQGKVGMDYFRRHLPAIRRQFASLQ---- 156
Cdd:smart00729  11 CPRRCTFCSFP-SLRGKLRSRYLEALVREIELLAEKGEKEGLVGTvfigGGTPTLLSPEQLEELLEAIREILGLAKdvei 89
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556315485   157 -MEVQP--LSQEEYAELKTLGLD----GVmvyqETYHEATYARhhlKGKKQDFFFRLETPDRLGRAGIDKIGLGALIGL 228
Cdd:smart00729  90 tIETRPdtLTEELLEALKEAGVNrvslGV----QSGDDEVLKA---INRGHTVEDVLEAVELLREAGPIKVSTDLIVGL 161
PRK05927 PRK05927
dehypoxanthine futalosine cyclase;
51-156 4.34e-04

dehypoxanthine futalosine cyclase;


Pssm-ID: 135660 [Multi-domain]  Cd Length: 350  Bit Score: 41.79  E-value: 4.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485  51 SAYLEPMAQRAQRLTRQRF-GNTVSFYV---PLYlSNLCANDCTYCGFSMSNRIKRKTLDEAEIARECAA-IREMGFEHL 125
Cdd:PRK05927  18 YSPLEELQEHADSLRKQRYpQNTVTYVLdanPNY-TNICKIDCTFCAFYRKPHSSDAYLLSFDEFRSLMQrYVSAGVKTV 96
                         90       100       110
                 ....*....|....*....|....*....|.
gi 556315485 126 LLVTGEHQgKVGMDYFRRHLPAIRRQFASLQ 156
Cdd:PRK05927  97 LLQGGVHP-QLGIDYLEELVRITVKEFPSLH 126
fbiC PRK09234
FO synthase; Reviewed
8-112 9.84e-04

FO synthase; Reviewed


Pssm-ID: 236422 [Multi-domain]  Cd Length: 843  Bit Score: 41.15  E-value: 9.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556315485   8 WRQLNWDDIALRINSKTAADVERALQARH-----LTREDLMALLSpAASAYLEPMAQRAQRLTRQRFGNTVSFYVP--LY 80
Cdd:PRK09234 453 WESIREQVHEGRAPERIDTDVLAALRAAErdpagLTDDEALALFT-ADGPALEAVCRLADDLRRDVVGDDVTYVVNrnIN 531
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 556315485  81 LSNLCANDCTYCGFSmsnriKRK------TLDEAEIAR 112
Cdd:PRK09234 532 FTNICYTGCRFCAFA-----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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH