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Conserved domains on  [gi|2461342585|ref|WP_275874639|]
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2-iminoacetate synthase ThiH [Aeromonas caviae]

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 ...
53-420 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: 568.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585  53 SFLDRWQDLEWDDIGMQIRAKTAADVERALTTSRRTLSDFMALISPAAEAYLPQMAAEAERLTRQRFGNTIGFYVPLYLS 132
Cdd:TIGR02351   1 TFKDEIEDILWEEVSYDIYSFTAADVERALNKRHLSLEDFLALLSPAAEPYLEEMAQKAKKLTRKRFGNTISLFTPLYLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 133 NLCANDCTYCGFSMSNRLKRKTLNSEEIERECLAIKARGFDSVLLVTGEHEHKVGLAYFRQVLPIIRRHFSTVGMEVQPL 212
Cdd:TIGR02351  81 NYCSNKCVYCGFSMSNKIKRKKLNEEEIEREIEAIKKSGFKEILLVTGESEKAAGVEYIAEAIKLAREYFSSLAIEVQPL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 213 SQAEYAELKTLGLDSVMVYQETYHAPTYARHHLRGNKRDIAWRLATPDRLGRAGIDKIGLGALIGLSaDWRADSYFVAEH 292
Cdd:TIGR02351 161 NEEEYKKLVEAGLDGVTVYQETYNEKKYKKHHLAGKKKDFRYRLNTPERAAKAGMRKIGIGALLGLD-DWRTDAFFTAYH 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 293 LAWLERHHWQSRYSLSFPRLRPCTGGLEPAVVMSDRQLAQLICAWRLFSPTLDLSLSTRESATFRNGAVRLGITQMSAES 372
Cdd:TIGR02351 240 LRYLQKKYWKTEISISVPRLRPCTNGLKPKVIVTDRELVQIICAYRLFDPFVEISLSTRESKKFRDNVIPLGITKMSAGS 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2461342585 373 RTQPGGYAEGDKeELEQFAIHDDRPVGEVAAAVRQAGLQPVFKDWEPF 420
Cdd:TIGR02351 320 STEPGGYSSEKK-GLEQFEISDERSVAEVEEDLRSKGLQPVWKDWDYF 366
 
Name Accession Description Interval E-value
thiH TIGR02351
thiazole biosynthesis protein ThiH; Members this protein family are the ThiH protein of ...
53-420 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: 568.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585  53 SFLDRWQDLEWDDIGMQIRAKTAADVERALTTSRRTLSDFMALISPAAEAYLPQMAAEAERLTRQRFGNTIGFYVPLYLS 132
Cdd:TIGR02351   1 TFKDEIEDILWEEVSYDIYSFTAADVERALNKRHLSLEDFLALLSPAAEPYLEEMAQKAKKLTRKRFGNTISLFTPLYLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 133 NLCANDCTYCGFSMSNRLKRKTLNSEEIERECLAIKARGFDSVLLVTGEHEHKVGLAYFRQVLPIIRRHFSTVGMEVQPL 212
Cdd:TIGR02351  81 NYCSNKCVYCGFSMSNKIKRKKLNEEEIEREIEAIKKSGFKEILLVTGESEKAAGVEYIAEAIKLAREYFSSLAIEVQPL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 213 SQAEYAELKTLGLDSVMVYQETYHAPTYARHHLRGNKRDIAWRLATPDRLGRAGIDKIGLGALIGLSaDWRADSYFVAEH 292
Cdd:TIGR02351 161 NEEEYKKLVEAGLDGVTVYQETYNEKKYKKHHLAGKKKDFRYRLNTPERAAKAGMRKIGIGALLGLD-DWRTDAFFTAYH 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 293 LAWLERHHWQSRYSLSFPRLRPCTGGLEPAVVMSDRQLAQLICAWRLFSPTLDLSLSTRESATFRNGAVRLGITQMSAES 372
Cdd:TIGR02351 240 LRYLQKKYWKTEISISVPRLRPCTNGLKPKVIVTDRELVQIICAYRLFDPFVEISLSTRESKKFRDNVIPLGITKMSAGS 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2461342585 373 RTQPGGYAEGDKeELEQFAIHDDRPVGEVAAAVRQAGLQPVFKDWEPF 420
Cdd:TIGR02351 320 STEPGGYSSEKK-GLEQFEISDERSVAEVEEDLRSKGLQPVWKDWDYF 366
ThiH COG1060
2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme ...
76-416 1.97e-98

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: 297.81  E-value: 1.97e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585  76 ADVERALTTSRRTLSDFMALISPAAEAyLPQMAAEAERLTRQRFGNTIgFYV---PLYLSNLCANDCTYCGFSMSNR-LK 151
Cdd:COG1060     1 EILEKALAGERLSLEDALALLSPAAAD-LEELAELADELRRRRFGNTV-TFVvnrPINLTNVCVNGCKFCAFSRDNGdID 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 152 RKTLNSEEIERECLAIKARGFDSVLLVTGEHeHKVGLAYFRQVLPIIRRHFStvGMEVQPLSQAEYAELKTL-------- 223
Cdd:COG1060    79 RYTLSPEEILEEAEEAKALGATEILLVGGEH-PDLPLEYYLDLLRAIKERFP--NIHIHALSPEEIAHLARAsglsveev 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 224 -------GLDSVMVYQETYHAPTYaRHHLRGNKRDIAWRLATPDRLGRAGIDkIGLGALIGLSaDWRADSYFVAEHLAWL 296
Cdd:COG1060   156 lerlkeaGLDSLPGGGAEILDDEV-RHPIGPGKIDYEEWLEVMERAHELGIR-TTATMLYGHV-ETREERVDHLLHLREL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 297 ERHHWQSRYSLSFpRLRPCTGGLEPAVV-MSDRQLAQLICAWRLFSPTLD------LSLSTResatFRNGAVRLGITQMS 369
Cdd:COG1060   233 QDETGGFTEFIPL-RFRPANTPLYLERPgVSDRELLKLIAVARLFLPNIGniqaswVSLGTR----LRQLALSLGANDLG 307
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2461342585 370 AESRTQPGGYAEGDKEeleqfaiHDDRPVGEVAAAVRQAGLQPVFKD 416
Cdd:COG1060   308 GTSMEENIVRAAGGEE-------GDERSVEELIRLIREAGRIPVERD 347
BATS smart00876
Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), , catalyses the last ...
308-412 1.00e-20

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: 86.00  E-value: 1.00e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585  308 SFPRLRPCTGG-LE-PAVVMSDRQLAQLICAWRLFSPTLDLSLSTRESATFRNgavrLGITQMSAESRTQPGGYaegdke 385
Cdd:smart00876   1 PINRLRPIEGTpLEdPPPPVSPEEFLRTIAAARLALPDAGIRLSTGREALLRD----LQALCFSAGANSIFGGD------ 70
                           90       100
                   ....*....|....*....|....*..
gi 2461342585  386 elEQFAIHDDRPVGEVaAAVRQAGLQP 412
Cdd:smart00876  71 --KYLTTSGPRSADDV-AMLEKLGLEP 94
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
129-336 1.79e-15

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: 74.68  E-value: 1.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 129 LYLSNLCANDCTYCGFSMSNRLKRKTLNSEEIERECLAIKARGFDSVL-LVTGEHEHKVGLAY----FRQVLPIIRRHFS 203
Cdd:cd01335     1 LELTRGCNLNCGFCSNPASKGRGPESPPEIEEILDIVLEAKERGVEVViLTGGEPLLYPELAEllrrLKKELPGFEISIE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 204 TVGMevqPLSQAEYAELKTLGLDSVMVYQETYHAPTYARHHLRGnkRDIAWRLATPDRLGRAGIdKIGLGALIGLSADWR 283
Cdd:cd01335    81 TNGT---LLTEELLKELKELGLDGVGVSLDSGDEEVADKIRGSG--ESFKERLEALKELREAGL-GLSTTLLVGLGDEDE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2461342585 284 ADsyfVAEHLAWLERHHWQSRYSLSFPRLRPCTGGLEPAVVMSDRQLAQLICA 336
Cdd:cd01335   155 ED---DLEELELLAEFRSPDRVSLFRLLPEEGTPLELAAPVVPAEKLLRLIAA 204
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
131-277 2.53e-09

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: 56.00  E-value: 2.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 131 LSNLCANDCTYCGFSMSNRLKRKTLNS-EEIERECLAIKARGFDSVLLVTGEHEHKVGLAYF------RQVLPIIRRHFS 203
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKGRELSpEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELlerllkLELAEGIRITLE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2461342585 204 TVGMEVQPlsqAEYAELKTLGLDSVMVYQETYHaPTYARhhLRGNKRDIAWRLATPDRLGRAGIDKIGLGALIG 277
Cdd:pfam04055  81 TNGTLLDE---ELLELLKEAGLDRVSIGLESGD-DEVLK--LINRGHTFEEVLEALELLREAGIPVVTDNIVGL 148
PRK07360 PRK07360
FO synthase subunit 2; Reviewed
111-228 2.66e-04

FO synthase subunit 2; Reviewed


Pssm-ID: 236000 [Multi-domain]  Cd Length: 371  Bit Score: 42.96  E-value: 2.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 111 AERLTRQRFGNTIGFYVPL--YLSNLCANDCTYCGFSMS-NRLKRKTLNSEEIERECLAIKARGFDSVLLVTGEHEHKVG 187
Cdd:PRK07360   44 ADRLRKEQVGDTVTYVVNRniNFTNICEGHCGFCAFRRDeGDHGAFWLTIAEILEKAAEAVKRGATEVCIQGGLHPAADS 123
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2461342585 188 LAYFRQVL-------PIIRRH-FSTvgMEVQ------PLSQAE-YAELKTLGLDSV 228
Cdd:PRK07360  124 LEFYLEILeaikeefPDIHLHaFSP--MEVYfaaredGLSYEEvLKALKDAGLDSM 177
 
Name Accession Description Interval E-value
thiH TIGR02351
thiazole biosynthesis protein ThiH; Members this protein family are the ThiH protein of ...
53-420 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: 568.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585  53 SFLDRWQDLEWDDIGMQIRAKTAADVERALTTSRRTLSDFMALISPAAEAYLPQMAAEAERLTRQRFGNTIGFYVPLYLS 132
Cdd:TIGR02351   1 TFKDEIEDILWEEVSYDIYSFTAADVERALNKRHLSLEDFLALLSPAAEPYLEEMAQKAKKLTRKRFGNTISLFTPLYLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 133 NLCANDCTYCGFSMSNRLKRKTLNSEEIERECLAIKARGFDSVLLVTGEHEHKVGLAYFRQVLPIIRRHFSTVGMEVQPL 212
Cdd:TIGR02351  81 NYCSNKCVYCGFSMSNKIKRKKLNEEEIEREIEAIKKSGFKEILLVTGESEKAAGVEYIAEAIKLAREYFSSLAIEVQPL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 213 SQAEYAELKTLGLDSVMVYQETYHAPTYARHHLRGNKRDIAWRLATPDRLGRAGIDKIGLGALIGLSaDWRADSYFVAEH 292
Cdd:TIGR02351 161 NEEEYKKLVEAGLDGVTVYQETYNEKKYKKHHLAGKKKDFRYRLNTPERAAKAGMRKIGIGALLGLD-DWRTDAFFTAYH 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 293 LAWLERHHWQSRYSLSFPRLRPCTGGLEPAVVMSDRQLAQLICAWRLFSPTLDLSLSTRESATFRNGAVRLGITQMSAES 372
Cdd:TIGR02351 240 LRYLQKKYWKTEISISVPRLRPCTNGLKPKVIVTDRELVQIICAYRLFDPFVEISLSTRESKKFRDNVIPLGITKMSAGS 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2461342585 373 RTQPGGYAEGDKeELEQFAIHDDRPVGEVAAAVRQAGLQPVFKDWEPF 420
Cdd:TIGR02351 320 STEPGGYSSEKK-GLEQFEISDERSVAEVEEDLRSKGLQPVWKDWDYF 366
ThiH COG1060
2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme ...
76-416 1.97e-98

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: 297.81  E-value: 1.97e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585  76 ADVERALTTSRRTLSDFMALISPAAEAyLPQMAAEAERLTRQRFGNTIgFYV---PLYLSNLCANDCTYCGFSMSNR-LK 151
Cdd:COG1060     1 EILEKALAGERLSLEDALALLSPAAAD-LEELAELADELRRRRFGNTV-TFVvnrPINLTNVCVNGCKFCAFSRDNGdID 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 152 RKTLNSEEIERECLAIKARGFDSVLLVTGEHeHKVGLAYFRQVLPIIRRHFStvGMEVQPLSQAEYAELKTL-------- 223
Cdd:COG1060    79 RYTLSPEEILEEAEEAKALGATEILLVGGEH-PDLPLEYYLDLLRAIKERFP--NIHIHALSPEEIAHLARAsglsveev 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 224 -------GLDSVMVYQETYHAPTYaRHHLRGNKRDIAWRLATPDRLGRAGIDkIGLGALIGLSaDWRADSYFVAEHLAWL 296
Cdd:COG1060   156 lerlkeaGLDSLPGGGAEILDDEV-RHPIGPGKIDYEEWLEVMERAHELGIR-TTATMLYGHV-ETREERVDHLLHLREL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 297 ERHHWQSRYSLSFpRLRPCTGGLEPAVV-MSDRQLAQLICAWRLFSPTLD------LSLSTResatFRNGAVRLGITQMS 369
Cdd:COG1060   233 QDETGGFTEFIPL-RFRPANTPLYLERPgVSDRELLKLIAVARLFLPNIGniqaswVSLGTR----LRQLALSLGANDLG 307
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2461342585 370 AESRTQPGGYAEGDKEeleqfaiHDDRPVGEVAAAVRQAGLQPVFKD 416
Cdd:COG1060   308 GTSMEENIVRAAGGEE-------GDERSVEELIRLIREAGRIPVERD 347
rSAM_HydG TIGR03955
[FeFe] hydrogenase H-cluster radical SAM maturase HydG; This model describes the radical SAM ...
106-414 3.45e-49

[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: 173.76  E-value: 3.45e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 106 QMAAEAERLTRQRFGNTIGFYVPLYLSNLCANDCTYCGFSMSNR-LKRKTLNSEEIERECLAIKARGFDSVLLVTGEHEH 184
Cdd:TIGR03955  66 EIYKLAEQIKKKFYGNRIVMFAPLYLSNYCVNGCVYCPYHAKNKhIARKKLTQEEIRREVIALQDMGHKRLALEAGEDPV 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 185 KVGLAYfrqVLPIIRRHFST---------VGMEVQPLSQAEYAELKTLGLDSVMVYQETYHAPTYARHHLRGNKRDIAWR 255
Cdd:TIGR03955 146 NNPIEY---ILESIKTIYSIkhkngairrVNVNIAATTVENYRKLKEAGIGTYILFQETYHKESYEELHPTGPKHDYAYH 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 256 LATPDRLGRAGIDKIGLGALIGLSAdWRADsyFV-----AEHlawLERHHWQSRYSLSFPRLRPcTGGLEPAVV---MSD 327
Cdd:TIGR03955 223 TEAMDRAMEGGIDDVGLGVLFGLNL-YRYD--FAgllmhAEH---LEAVFGVGPHTISVPRIRP-ADDIDPDDFdngISD 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 328 RQLAQLICAWRLFSPTLDLSLSTRESATFRNGAVRLGITQMSAESRTQPGGYAEGDKEEL--EQFAIHDDRPVGEVAAAV 405
Cdd:TIGR03955 296 DIFAKIVACIRIAVPYTGMIISTRESQKVRERVLHLGISQISGGSRTSVGGYAEPEPEDEnsAQFDVSDNRTLDEVVNWL 375

                  ....*....
gi 2461342585 406 RQAGLQPVF 414
Cdd:TIGR03955 376 MDLGYIPSF 384
BATS smart00876
Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), , catalyses the last ...
308-412 1.00e-20

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: 86.00  E-value: 1.00e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585  308 SFPRLRPCTGG-LE-PAVVMSDRQLAQLICAWRLFSPTLDLSLSTRESATFRNgavrLGITQMSAESRTQPGGYaegdke 385
Cdd:smart00876   1 PINRLRPIEGTpLEdPPPPVSPEEFLRTIAAARLALPDAGIRLSTGREALLRD----LQALCFSAGANSIFGGD------ 70
                           90       100
                   ....*....|....*....|....*..
gi 2461342585  386 elEQFAIHDDRPVGEVaAAVRQAGLQP 412
Cdd:smart00876  71 --KYLTTSGPRSADDV-AMLEKLGLEP 94
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
129-336 1.79e-15

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: 74.68  E-value: 1.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 129 LYLSNLCANDCTYCGFSMSNRLKRKTLNSEEIERECLAIKARGFDSVL-LVTGEHEHKVGLAY----FRQVLPIIRRHFS 203
Cdd:cd01335     1 LELTRGCNLNCGFCSNPASKGRGPESPPEIEEILDIVLEAKERGVEVViLTGGEPLLYPELAEllrrLKKELPGFEISIE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 204 TVGMevqPLSQAEYAELKTLGLDSVMVYQETYHAPTYARHHLRGnkRDIAWRLATPDRLGRAGIdKIGLGALIGLSADWR 283
Cdd:cd01335    81 TNGT---LLTEELLKELKELGLDGVGVSLDSGDEEVADKIRGSG--ESFKERLEALKELREAGL-GLSTTLLVGLGDEDE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2461342585 284 ADsyfVAEHLAWLERHHWQSRYSLSFPRLRPCTGGLEPAVVMSDRQLAQLICA 336
Cdd:cd01335   155 ED---DLEELELLAEFRSPDRVSLFRLLPEEGTPLELAAPVVPAEKLLRLIAA 204
BioB COG0502
Biotin synthase or related enzyme [Coenzyme transport and metabolism]; Biotin synthase or ...
88-285 1.17e-13

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: 71.23  E-value: 1.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585  88 TLSDFMALISpAAEAYLPQMAAEAERLTRQRFGNTIGFYVPLYL-SNLCANDCTYCGFSMSNR--LKRKTLNS-EEIERE 163
Cdd:COG0502     3 TREEALALLE-LPDEELEDLLAAADEVREHFFGNKVQLCGLINIkSGGCPEDCKYCGQSAHNKtgIERYRLLSvEEILEA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 164 CLAIKARGFDSVLLVT-GEhehkvGLAY--FRQVLPIIRRHFSTVGMEVq----pLSQAEYAELKTLGLDSVMVYQETyh 236
Cdd:COG0502    82 ARAAKEAGARRFCLVAsGR-----DPSDrdFEKVLEIVRAIKEELGLEVcaslgeLSEEQAKRLKEAGVDRYNHNLET-- 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2461342585 237 AP----------TYARhhlrgnkrdiawRLATPDRLGRAGIdKIGLGALIGL--SADWRAD 285
Cdd:COG0502   155 SPelypkictthTYED------------RLDTLKNAREAGL-EVCSGGIVGMgeTLEDRAD 202
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
131-277 2.53e-09

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: 56.00  E-value: 2.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 131 LSNLCANDCTYCGFSMSNRLKRKTLNS-EEIERECLAIKARGFDSVLLVTGEHEHKVGLAYF------RQVLPIIRRHFS 203
Cdd:pfam04055   1 ITRGCNLRCTYCAFPSIRARGKGRELSpEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELlerllkLELAEGIRITLE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2461342585 204 TVGMEVQPlsqAEYAELKTLGLDSVMVYQETYHaPTYARhhLRGNKRDIAWRLATPDRLGRAGIDKIGLGALIG 277
Cdd:pfam04055  81 TNGTLLDE---ELLELLKEAGLDRVSIGLESGD-DEVLK--LINRGHTFEEVLEALELLREAGIPVVTDNIVGL 148
BATS pfam06968
Biotin and Thiamin Synthesis associated domain; Biotin synthase (BioB), EC:2.8.1.6, catalyzes ...
312-409 1.36e-08

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: 51.69  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 312 LRPCTG-GLEPAVVMSDRQLAQLICAWRLFSPTLDL-SLSTRESATFRNG-AVRLGITQMSAesrtqpggyaeGDKeele 388
Cdd:pfam06968   1 LRPIPGtPLENQPPLSPEEALRTIAAFRLILPDAGIrLAGGRESMLFRQAlLFLAGANSISA-----------GSK---- 65
                          90       100
                  ....*....|....*....|.
gi 2461342585 389 qFAIHDDRPVGEVAAAVRQAG 409
Cdd:pfam06968  66 -FLTTDGRSPDEDIAMLEDLG 85
TIGR00423 TIGR00423
radical SAM domain protein, CofH subfamily; This protein family includes the CofH protein of ...
132-227 2.19e-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: 49.31  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 132 SNLCANDCTYCGFsmSNRLKRKT---LNSEEIERECLAIKARGFDSVLLVTGeHEHKVGLAYFRQVLPIIRRHFSTV--- 205
Cdd:TIGR00423  12 TNICVGKCKFCAF--RAREKDKDayvLSLEEILEKVKEAVAKGATEVCIQGG-LNPQLDIEYYEELFRAIKQEFPDVhih 88
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2461342585 206 ---GMEVQPLSQAE-------YAELKTLGLDS 227
Cdd:TIGR00423  89 afsPMEVYFLAKNEglsieevLKRLKKAGLDS 120
rSAM_HydE TIGR03956
[FeFe] hydrogenase H-cluster radical SAM maturase HydE; This model describes the radical SAM ...
87-181 1.08e-05

[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: 47.17  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585  87 RTLS--DFMALISPAAEAYLPQMAAEAERLTRQRFGNTIGFYVPLYLSNLCANDCTYCGFSMSNR-LKRKTLNSEEIERE 163
Cdd:TIGR03956   9 HTLSkeEFKRLLENRDEEDAEYLFELAREVRLRYYGNKVYIRGLIEFTNYCKNDCYYCGIRKSNPnAERYRLTKEEILSC 88
                          90
                  ....*....|....*...
gi 2461342585 164 CLAIKARGFDSVLLVTGE 181
Cdd:TIGR03956  89 CREGYELGFRTFVLQGGE 106
PRK07360 PRK07360
FO synthase subunit 2; Reviewed
111-228 2.66e-04

FO synthase subunit 2; Reviewed


Pssm-ID: 236000 [Multi-domain]  Cd Length: 371  Bit Score: 42.96  E-value: 2.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 111 AERLTRQRFGNTIGFYVPL--YLSNLCANDCTYCGFSMS-NRLKRKTLNSEEIERECLAIKARGFDSVLLVTGEHEHKVG 187
Cdd:PRK07360   44 ADRLRKEQVGDTVTYVVNRniNFTNICEGHCGFCAFRRDeGDHGAFWLTIAEILEKAAEAVKRGATEVCIQGGLHPAADS 123
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2461342585 188 LAYFRQVL-------PIIRRH-FSTvgMEVQ------PLSQAE-YAELKTLGLDSV 228
Cdd:PRK07360  124 LEFYLEILeaikeefPDIHLHaFSP--MEVYfaaredGLSYEEvLKALKDAGLDSM 177
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
135-278 1.36e-03

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: 40.08  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585  135 CANDCTYCGFSmSNRLKRKTLNSEEIERECLAIKARGFDSVLLVT-----------GEHEHKVGLAYFRQVLPIIRRHFS 203
Cdd:smart00729  11 CPRRCTFCSFP-SLRGKLRSRYLEALVREIELLAEKGEKEGLVGTvfigggtptllSPEQLEELLEAIREILGLAKDVEI 89
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2461342585  204 TVGMEVQPLSQAEYAELKTLGLDSVmvyqetYHAP-TYARHHLRGNKR--DIAWRLATPDRLGRAGIDKIGLGALIGL 278
Cdd:smart00729  90 TIETRPDTLTEELLEALKEAGVNRV------SLGVqSGDDEVLKAINRghTVEDVLEAVELLREAGPIKVSTDLIVGL 161
F420_cofH TIGR03551
7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase, CofH subunit; This enzyme, together with ...
111-227 7.48e-03

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: 38.41  E-value: 7.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461342585 111 AERLTRQRFGNTIGFYVP--LYLSNLCANDCTYCGFSMSNRLKR-KTLNSEEIERECLAIKARGFDSVLLVTGEHEHKVG 187
Cdd:TIGR03551  23 ADELRRDIVGDTVTYVVNrnINFTNVCYGGCGFCAFRKRKGDADaYLLSLEEIAERAAEAWKAGATEVCIQGGIHPDLDG 102
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2461342585 188 LAYF------RQVLPIIRRH-FSTvgMEV------QPLSQAEY-AELKTLGLDS 227
Cdd:TIGR03551 103 DFYLdilravKEEVPGMHIHaFSP--MEVyygarnSGLSVEEAlKRLKEAGLDS 154
 
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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