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Conserved domains on  [gi|479887385|gb|ENU37680|]
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alkanesulfonate monooxygenase [Acinetobacter parvus DSM 16617 = CIP 108168]

Protein Classification

FMNH2-dependent alkanesulfonate monooxygenase( domain architecture ID 10792051)

FMNH2-dependent alkanesulfonate monooxygenase catalyzes the desulfonation of a wide range of aliphatic sulfonates

CATH:  3.20.20.30
EC:  1.14.14.5
Gene Ontology:  GO:0010181|GO:0046306|GO:0008726
SCOP:  3000585

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK00719 PRK00719
alkanesulfonate monooxygenase; Provisional
 1-378 0e+00

alkanesulfonate monooxygenase; Provisional


:

Pssm-ID: 234821 [Multi-domain]  Cd Length: 378  Bit Score: 764.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385   1 MNIFWFIPTHGDSRYLGTSKGARQVDHAYMKQIAVAVDNLGYDGVLIPTGRSCEDPWITAASLIDATRQLKFLVALRPGI 80
Cdd:PRK00719   1 MNVFWFLPTHGDGRYLGTSEGARAVDHGYLQQIAQAADRLGYTGVLIPTGRSCEDAWLVAASLIPVTQRLKFLVALRPGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385  81 TTPALAARMAATFDRLSNGRILLNLVTGGDEQELKGDGLYEDHSTRYQTASEYVKIWREILTrshtGESFTFHGERLSVD 160
Cdd:PRK00719  81 MSPTVAARMAATLDRLSNGRLLINLVTGGDPAELAGDGLFLDHDERYEASAEFLRIWRRLLE----GETVDFEGKHIQVK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385 161 DAKLLYPPVQQPHPPLWFGGSSEAATELAAEQVDTYLTWGEPPAAVKEKIQYLRAKAAAIGRTLNYGIRLHVIVRETNEQ 240
Cdd:PRK00719 157 GAKLLFPPVQQPYPPLYFGGSSDAAQELAAEQVDLYLTWGEPPAQVKEKIEQVRAKAAAHGRKVRFGIRLHVIVRETNEE 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385 241 AWAAADELIQYLDDATIAAAQKKFAQMDSVGQQRMAALHGGRKDQLEVSPNLWAGIGLVRGGAGTALVGDPETVAARIQE 320
Cdd:PRK00719 237 AWQAAERLISHLDDETIARAQAAFARMDSVGQQRMAALHGGKRDNLEISPNLWAGVGLVRGGAGTALVGDPPTVAARIKE 316

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 479887385 321 YADLGIDTFIFSGYPHLEESIRFAELVFPLLPLKTRKKLAQPHlTGPFGEIIANNYVP 378
Cdd:PRK00719 317 YAALGIDTFILSGYPHLEEAYRVAELLFPLLDVAIPEKPQPQP-SGPFGEVVANDYLP 373
 
Name Accession Description Interval E-value
PRK00719 PRK00719
alkanesulfonate monooxygenase; Provisional
 1-378 0e+00

alkanesulfonate monooxygenase; Provisional


Pssm-ID: 234821 [Multi-domain]  Cd Length: 378  Bit Score: 764.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385   1 MNIFWFIPTHGDSRYLGTSKGARQVDHAYMKQIAVAVDNLGYDGVLIPTGRSCEDPWITAASLIDATRQLKFLVALRPGI 80
Cdd:PRK00719   1 MNVFWFLPTHGDGRYLGTSEGARAVDHGYLQQIAQAADRLGYTGVLIPTGRSCEDAWLVAASLIPVTQRLKFLVALRPGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385  81 TTPALAARMAATFDRLSNGRILLNLVTGGDEQELKGDGLYEDHSTRYQTASEYVKIWREILTrshtGESFTFHGERLSVD 160
Cdd:PRK00719  81 MSPTVAARMAATLDRLSNGRLLINLVTGGDPAELAGDGLFLDHDERYEASAEFLRIWRRLLE----GETVDFEGKHIQVK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385 161 DAKLLYPPVQQPHPPLWFGGSSEAATELAAEQVDTYLTWGEPPAAVKEKIQYLRAKAAAIGRTLNYGIRLHVIVRETNEQ 240
Cdd:PRK00719 157 GAKLLFPPVQQPYPPLYFGGSSDAAQELAAEQVDLYLTWGEPPAQVKEKIEQVRAKAAAHGRKVRFGIRLHVIVRETNEE 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385 241 AWAAADELIQYLDDATIAAAQKKFAQMDSVGQQRMAALHGGRKDQLEVSPNLWAGIGLVRGGAGTALVGDPETVAARIQE 320
Cdd:PRK00719 237 AWQAAERLISHLDDETIARAQAAFARMDSVGQQRMAALHGGKRDNLEISPNLWAGVGLVRGGAGTALVGDPPTVAARIKE 316

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 479887385 321 YADLGIDTFIFSGYPHLEESIRFAELVFPLLPLKTRKKLAQPHlTGPFGEIIANNYVP 378
Cdd:PRK00719 317 YAALGIDTFILSGYPHLEEAYRVAELLFPLLDVAIPEKPQPQP-SGPFGEVVANDYLP 373
alk_sulf_monoox TIGR03565
alkanesulfonate monooxygenase, FMNH(2)-dependent; Members of this protein family are ...
 2-351 0e+00

alkanesulfonate monooxygenase, FMNH(2)-dependent; Members of this protein family are monooxygenases that catalyze desulfonation of aliphatic sulfonates such as methane sulfonate. This enzyme uses reduced FMN, although various others members of the same luciferase-like monooxygenase family (pfam00296) are F420-dependent enzymes. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 274652  Cd Length: 346  Bit Score: 707.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385    2 NIFWFIPTHGDSRYLGTSKGARQVDHAYMKQIAVAVDNLGYDGVLIPTGRSCEDPWITAASLIDATRQLKFLVALRPGIT 81
Cdd:TIGR03565   1 NIFWFIPTHGDGRYLGTSEGGRAVDHGYLKQIAQAADRLGYTGVLLPTGRSCEDSWVTASSLAPLTERLKFLVAVRPGLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385   82 TPALAARMAATFDRLSNGRILLNLVTGGDEQELKGDGLYEDHSTRYQTASEYVKIWREILTrshtGESFTFHGERLSVDD 161
Cdd:TIGR03565  81 SPTVAARMAATLDRLSGGRLLINVVTGGDPVELAGDGIFLDHDERYEATDEFLTVWRRLLA----GETVDFDGKHIKVEN 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385  162 AKLLYPPVQQPHPPLWFGGSSEAATELAAEQVDTYLTWGEPPAAVKEKIQYLRAKAAAIGRTLNYGIRLHVIVRETNEQA 241
Cdd:TIGR03565 157 AKLLFPPVQQPYPPLYFGGSSDAAIELAAEHVDVYLTWGEPPAQVAEKIAKVRKRAAKRGRTVRFGIRLHVIVRETEEEA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385  242 WAAADELIQYLDDATIAAAQKKFAQMDSVGQQRMAALHGGRKDQLEVSPNLWAGIGLVRGGAGTALVGDPETVAARIQEY 321
Cdd:TIGR03565 237 WAAADRLISHLDDDTIARAQKAFARMDSVGQRRMAALHGGRRDKLEISPNLWAGVGLVRGGAGTALVGDPETVAARIREY 316

                         330       340       350
                  ....*....|....*....|....*....|
gi 479887385  322 ADLGIDTFIFSGYPHLEESIRFAELVFPLL 351
Cdd:TIGR03565 317 QDLGIDTFILSGYPHLEEAYRFAELVFPLL 346
Alkanesulfonate_monoxygenase cd01094
Alkanesulfonate monoxygenase is the monoxygenase of a two-component system that catalyzes the ...
 1-247 1.96e-106

Alkanesulfonate monoxygenase is the monoxygenase of a two-component system that catalyzes the conversion of alkanesulfonates to the corresponding aldehyde and sulfite. Alkanesulfonate monoxygenase (SsuD) has an absolute requirement for reduced flavin mononucleotide (FMNH2), which is provided by the NADPH-dependent FMN oxidoreductase (SsuE).


Pssm-ID: 238527 [Multi-domain]  Cd Length: 244  Bit Score: 313.06  E-value: 1.96e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385   1 MNIFWFIPTHGDSRYLGTSKGARQVDHAYMKQIAVAVDNLGYDGVLIPTGRSCEDPWITAASLIDATRQLKFLVALRPGI 80
Cdd:cd01094    1 LEFGWFIPNVSGGWSLSTPPRGRPWDFEYNRQIAQAAEELGFDGALSPTGSSGPDGWTVAAALAAATERLKFLVAIRPGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385  81 TTPALAARMAATFDRLSNGRILLNLVTGGDEQELKGDGLYEDHSTRYQTASEYVKIWREILTRshtGESFTFHGERLSVD 160
Cdd:cd01094   81 IAPTVAARQAATLDHISGGRLGLNVVTGGDPAELRMDGDFLDHDERYARADEFLEVLRRLWTS---DEPFDFEGKFYRFK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385 161 DAKLLYPPVQQPHPPLWFGGSSEAATELAAEQVDTYLTWGEPPAAVKEKIQYLRAKAAAIGRTLNYGIRLHVIVRETNEQ 240
Cdd:cd01094  158 NAFLRPKPPQQPHPPIYFGGSSEAAIEFAARHADVYFTWGEPPAQVAEAIARVRAAAAAAGRDVRFGIRLHVIVRDTEEE 237


                 ....*..
gi 479887385 241 AWAAADE 247
Cdd:cd01094  238 AWAYADR 244
Bac_luciferase pfam00296
Luciferase-like monooxygenase;
1-328 5.45e-75

Luciferase-like monooxygenase;


Pssm-ID: 425589 [Multi-domain]  Cd Length: 313  Bit Score: 235.33  E-value: 5.45e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385    1 MNIFWFIPTHGDSRYLGTSKGARqvdhaYMKQIAVAVDNLGYDGVLIPTGRSC---EDPWITAASLIDATRQLKFLVALR 77
Cdd:pfam00296   1 MEFGVFLPTRNGGGLGAGSESLR-----YLVELARAAEELGFDGVWLAEHHGGpggPDPFVVLAALAAATSRIRLGTAVV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385   78 PGIT-TPALAARMAATFDRLSNGRILLNLVTGGDEQELKGDGLyeDHSTRYQTASEYVKIWREILtrshTGESFTFHGER 156
Cdd:pfam00296  76 PLPTrHPAVLAEQAATLDHLSGGRFDLGLGTGGPAVEFRRFGV--DHDERYARLREFLEVLRRLW----RGEPVDFEGEF 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385  157 LSVDDAKLLYPPVQqpHPPLWFGGSSEAATELAAEQVDTYLTWG-EPPAAVKEKIQYLRAKAAAIGRT---LNYGIRLHV 232
Cdd:pfam00296 150 FTLDGAFLLPRPVQ--GIPVWVAASSPAMLELAARHADGLLLWGfAPPAAAAELIERVRAGAAEAGRDpadIRVGASLTV 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385  233 IVRETNEQAWAAADELIQYLDdatiaaaqkkFAQMDSVGQQRMAALhggRKDQLEVSPNLWAGIGLVRGGA---GTALVG 309
Cdd:pfam00296 228 IVADTEEEARAEARALIAGLP----------FYRMDSEGAGRLAEA---REIGEEYDAGDWAGAADAVPDElvrAFALVG 294

                         330
                  ....*....|....*....
gi 479887385  310 DPETVAARIQEYADLGIDT 328
Cdd:pfam00296 295 TPEQVAERLAAYAEAGVDH 313
SsuD COG2141
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
 38-351 4.76e-65

Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase SsuD and methylene tetrahydromethanopterin reductase) [Coenzyme transport and metabolism, General function prediction only]; Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase SsuD and methylene tetrahydromethanopterin reductase) is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 441744 [Multi-domain]  Cd Length: 301  Bit Score: 209.41  E-value: 4.76e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385  38 DNLGYDGVLI-----PTGRSCEDPWITAASLIDATRQLKFLVA-LRPGITTPALAARMAATFDRLSNGRILLNLVTGGDE 111
Cdd:COG2141    2 ERLGFDRVWVadhhfPPGGASPDPWVLLAALAAATSRIRLGTGvVVLPLRHPLVVAEQFATLDHLSGGRLDLGVGRGWGP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385 112 QELKGDGLyeDHSTRYQTASEYVKIWREILTrshtGESFTFHGERLSVDDAKLLYPPVQQPHPPLWFGGSSEAATELAAE 191
Cdd:COG2141   82 DEFAAFGL--DHDERYERFEEALEVLRRLWT----GEPVTFEGEFFTVEGARLVPRPVQGPHPPIWIAGSSPAGARLAAR 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385 192 QVDTYLTWGEPPAAVKEKIQYLRAKAAAIGR---TLNYGIRLHVIVRETNEQAWAAADEliqylddatiaaAQKKFAQMD 268
Cdd:COG2141  156 LGDGVFTAGGTPEELAEAIAAYREAAAAAGRdpdDLRVSVGLHVIVAETDEEARERARP------------YLRALLALP 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385 269 SVGQQRMAAlhggrkDQLEVSPNLWAgiglvrgGAGTALVGDPETVAARIQEYAD-LGIDTFIFS----GYPHLEESIR- 342
Cdd:COG2141  224 RGRPPEEAE------EGLTVREDLLE-------LLGAALVGTPEQVAERLEELAEaAGVDEFLLQfpglDPEDRLRSLEl 290


                 ....*....
gi 479887385 343 FAELVFPLL 351
Cdd:COG2141  291 FAEEVLPLL 299
 
Name Accession Description Interval E-value
PRK00719 PRK00719
alkanesulfonate monooxygenase; Provisional
 1-378 0e+00

alkanesulfonate monooxygenase; Provisional


Pssm-ID: 234821 [Multi-domain]  Cd Length: 378  Bit Score: 764.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385   1 MNIFWFIPTHGDSRYLGTSKGARQVDHAYMKQIAVAVDNLGYDGVLIPTGRSCEDPWITAASLIDATRQLKFLVALRPGI 80
Cdd:PRK00719   1 MNVFWFLPTHGDGRYLGTSEGARAVDHGYLQQIAQAADRLGYTGVLIPTGRSCEDAWLVAASLIPVTQRLKFLVALRPGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385  81 TTPALAARMAATFDRLSNGRILLNLVTGGDEQELKGDGLYEDHSTRYQTASEYVKIWREILTrshtGESFTFHGERLSVD 160
Cdd:PRK00719  81 MSPTVAARMAATLDRLSNGRLLINLVTGGDPAELAGDGLFLDHDERYEASAEFLRIWRRLLE----GETVDFEGKHIQVK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385 161 DAKLLYPPVQQPHPPLWFGGSSEAATELAAEQVDTYLTWGEPPAAVKEKIQYLRAKAAAIGRTLNYGIRLHVIVRETNEQ 240
Cdd:PRK00719 157 GAKLLFPPVQQPYPPLYFGGSSDAAQELAAEQVDLYLTWGEPPAQVKEKIEQVRAKAAAHGRKVRFGIRLHVIVRETNEE 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385 241 AWAAADELIQYLDDATIAAAQKKFAQMDSVGQQRMAALHGGRKDQLEVSPNLWAGIGLVRGGAGTALVGDPETVAARIQE 320
Cdd:PRK00719 237 AWQAAERLISHLDDETIARAQAAFARMDSVGQQRMAALHGGKRDNLEISPNLWAGVGLVRGGAGTALVGDPPTVAARIKE 316

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 479887385 321 YADLGIDTFIFSGYPHLEESIRFAELVFPLLPLKTRKKLAQPHlTGPFGEIIANNYVP 378
Cdd:PRK00719 317 YAALGIDTFILSGYPHLEEAYRVAELLFPLLDVAIPEKPQPQP-SGPFGEVVANDYLP 373
alk_sulf_monoox TIGR03565
alkanesulfonate monooxygenase, FMNH(2)-dependent; Members of this protein family are ...
 2-351 0e+00

alkanesulfonate monooxygenase, FMNH(2)-dependent; Members of this protein family are monooxygenases that catalyze desulfonation of aliphatic sulfonates such as methane sulfonate. This enzyme uses reduced FMN, although various others members of the same luciferase-like monooxygenase family (pfam00296) are F420-dependent enzymes. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 274652  Cd Length: 346  Bit Score: 707.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385    2 NIFWFIPTHGDSRYLGTSKGARQVDHAYMKQIAVAVDNLGYDGVLIPTGRSCEDPWITAASLIDATRQLKFLVALRPGIT 81
Cdd:TIGR03565   1 NIFWFIPTHGDGRYLGTSEGGRAVDHGYLKQIAQAADRLGYTGVLLPTGRSCEDSWVTASSLAPLTERLKFLVAVRPGLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385   82 TPALAARMAATFDRLSNGRILLNLVTGGDEQELKGDGLYEDHSTRYQTASEYVKIWREILTrshtGESFTFHGERLSVDD 161
Cdd:TIGR03565  81 SPTVAARMAATLDRLSGGRLLINVVTGGDPVELAGDGIFLDHDERYEATDEFLTVWRRLLA----GETVDFDGKHIKVEN 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385  162 AKLLYPPVQQPHPPLWFGGSSEAATELAAEQVDTYLTWGEPPAAVKEKIQYLRAKAAAIGRTLNYGIRLHVIVRETNEQA 241
Cdd:TIGR03565 157 AKLLFPPVQQPYPPLYFGGSSDAAIELAAEHVDVYLTWGEPPAQVAEKIAKVRKRAAKRGRTVRFGIRLHVIVRETEEEA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385  242 WAAADELIQYLDDATIAAAQKKFAQMDSVGQQRMAALHGGRKDQLEVSPNLWAGIGLVRGGAGTALVGDPETVAARIQEY 321
Cdd:TIGR03565 237 WAAADRLISHLDDDTIARAQKAFARMDSVGQRRMAALHGGRRDKLEISPNLWAGVGLVRGGAGTALVGDPETVAARIREY 316

                         330       340       350
                  ....*....|....*....|....*....|
gi 479887385  322 ADLGIDTFIFSGYPHLEESIRFAELVFPLL 351
Cdd:TIGR03565 317 QDLGIDTFILSGYPHLEEAYRFAELVFPLL 346
Alkanesulfonate_monoxygenase cd01094
Alkanesulfonate monoxygenase is the monoxygenase of a two-component system that catalyzes the ...
 1-247 1.96e-106

Alkanesulfonate monoxygenase is the monoxygenase of a two-component system that catalyzes the conversion of alkanesulfonates to the corresponding aldehyde and sulfite. Alkanesulfonate monoxygenase (SsuD) has an absolute requirement for reduced flavin mononucleotide (FMNH2), which is provided by the NADPH-dependent FMN oxidoreductase (SsuE).


Pssm-ID: 238527 [Multi-domain]  Cd Length: 244  Bit Score: 313.06  E-value: 1.96e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385   1 MNIFWFIPTHGDSRYLGTSKGARQVDHAYMKQIAVAVDNLGYDGVLIPTGRSCEDPWITAASLIDATRQLKFLVALRPGI 80
Cdd:cd01094    1 LEFGWFIPNVSGGWSLSTPPRGRPWDFEYNRQIAQAAEELGFDGALSPTGSSGPDGWTVAAALAAATERLKFLVAIRPGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385  81 TTPALAARMAATFDRLSNGRILLNLVTGGDEQELKGDGLYEDHSTRYQTASEYVKIWREILTRshtGESFTFHGERLSVD 160
Cdd:cd01094   81 IAPTVAARQAATLDHISGGRLGLNVVTGGDPAELRMDGDFLDHDERYARADEFLEVLRRLWTS---DEPFDFEGKFYRFK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385 161 DAKLLYPPVQQPHPPLWFGGSSEAATELAAEQVDTYLTWGEPPAAVKEKIQYLRAKAAAIGRTLNYGIRLHVIVRETNEQ 240
Cdd:cd01094  158 NAFLRPKPPQQPHPPIYFGGSSEAAIEFAARHADVYFTWGEPPAQVAEAIARVRAAAAAAGRDVRFGIRLHVIVRDTEEE 237


                 ....*..
gi 479887385 241 AWAAADE 247
Cdd:cd01094  238 AWAYADR 244
Bac_luciferase pfam00296
Luciferase-like monooxygenase;
1-328 5.45e-75

Luciferase-like monooxygenase;


Pssm-ID: 425589 [Multi-domain]  Cd Length: 313  Bit Score: 235.33  E-value: 5.45e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385    1 MNIFWFIPTHGDSRYLGTSKGARqvdhaYMKQIAVAVDNLGYDGVLIPTGRSC---EDPWITAASLIDATRQLKFLVALR 77
Cdd:pfam00296   1 MEFGVFLPTRNGGGLGAGSESLR-----YLVELARAAEELGFDGVWLAEHHGGpggPDPFVVLAALAAATSRIRLGTAVV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385   78 PGIT-TPALAARMAATFDRLSNGRILLNLVTGGDEQELKGDGLyeDHSTRYQTASEYVKIWREILtrshTGESFTFHGER 156
Cdd:pfam00296  76 PLPTrHPAVLAEQAATLDHLSGGRFDLGLGTGGPAVEFRRFGV--DHDERYARLREFLEVLRRLW----RGEPVDFEGEF 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385  157 LSVDDAKLLYPPVQqpHPPLWFGGSSEAATELAAEQVDTYLTWG-EPPAAVKEKIQYLRAKAAAIGRT---LNYGIRLHV 232
Cdd:pfam00296 150 FTLDGAFLLPRPVQ--GIPVWVAASSPAMLELAARHADGLLLWGfAPPAAAAELIERVRAGAAEAGRDpadIRVGASLTV 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385  233 IVRETNEQAWAAADELIQYLDdatiaaaqkkFAQMDSVGQQRMAALhggRKDQLEVSPNLWAGIGLVRGGA---GTALVG 309
Cdd:pfam00296 228 IVADTEEEARAEARALIAGLP----------FYRMDSEGAGRLAEA---REIGEEYDAGDWAGAADAVPDElvrAFALVG 294

                         330
                  ....*....|....*....
gi 479887385  310 DPETVAARIQEYADLGIDT 328
Cdd:pfam00296 295 TPEQVAERLAAYAEAGVDH 313
SsuD COG2141
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
 38-351 4.76e-65

Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase SsuD and methylene tetrahydromethanopterin reductase) [Coenzyme transport and metabolism, General function prediction only]; Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase SsuD and methylene tetrahydromethanopterin reductase) is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 441744 [Multi-domain]  Cd Length: 301  Bit Score: 209.41  E-value: 4.76e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385  38 DNLGYDGVLI-----PTGRSCEDPWITAASLIDATRQLKFLVA-LRPGITTPALAARMAATFDRLSNGRILLNLVTGGDE 111
Cdd:COG2141    2 ERLGFDRVWVadhhfPPGGASPDPWVLLAALAAATSRIRLGTGvVVLPLRHPLVVAEQFATLDHLSGGRLDLGVGRGWGP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385 112 QELKGDGLyeDHSTRYQTASEYVKIWREILTrshtGESFTFHGERLSVDDAKLLYPPVQQPHPPLWFGGSSEAATELAAE 191
Cdd:COG2141   82 DEFAAFGL--DHDERYERFEEALEVLRRLWT----GEPVTFEGEFFTVEGARLVPRPVQGPHPPIWIAGSSPAGARLAAR 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385 192 QVDTYLTWGEPPAAVKEKIQYLRAKAAAIGR---TLNYGIRLHVIVRETNEQAWAAADEliqylddatiaaAQKKFAQMD 268
Cdd:COG2141  156 LGDGVFTAGGTPEELAEAIAAYREAAAAAGRdpdDLRVSVGLHVIVAETDEEARERARP------------YLRALLALP 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385 269 SVGQQRMAAlhggrkDQLEVSPNLWAgiglvrgGAGTALVGDPETVAARIQEYAD-LGIDTFIFS----GYPHLEESIR- 342
Cdd:COG2141  224 RGRPPEEAE------EGLTVREDLLE-------LLGAALVGTPEQVAERLEELAEaAGVDEFLLQfpglDPEDRLRSLEl 290


                 ....*....
gi 479887385 343 FAELVFPLL 351
Cdd:COG2141  291 FAEEVLPLL 299
F420_Rv2161c TIGR03619
probable F420-dependent oxidoreductase, Rv2161c family; Coenzyme F420 has a limited ...
 32-246 2.93e-22

probable F420-dependent oxidoreductase, Rv2161c family; Coenzyme F420 has a limited phylogenetic distribution, including methanogenic archaea, Mycobacterium tuberculosis and related species, Colwellia psychrerythraea 34H, Rhodopseudomonas palustris HaA2, and others. Partial phylogenetic profiling identifies protein subfamilies, within the larger family called luciferase-like monooxygenanases (pfam00296), that appear only in F420-positive genomes and are likely to be F420-dependent. This model describes a domain found in a distinctive subset of bacterial luciferase homologs, found only in F420-biosynthesizing members of the Actinobacteria. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274680 [Multi-domain]  Cd Length: 246  Bit Score: 94.63  E-value: 2.93e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385   32 QIAVAVDNLGYDG------VLIPTGR--------------SCEDPWITAASLIDATRQLKFL--VALRPgITTPALAARM 89
Cdd:TIGR03619   2 ELARAAEELGFDSllayehVAIPARRetpwpdsgggdapdRTLDPFVALAFAAAVTSRLRLGtgVLVLP-QRDPLLLAKQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385   90 AATFDRLSNGRILLNLVTGGDEQElkgdglYEDHSTRYQTASEYVKIWREILTRSHTGESFTFHGERLSVDDAKLLYPPV 169
Cdd:TIGR03619  81 AATLDLLSGGRLRLGVGVGWLREE------FRALGVDFDERGRLLDEAIEALRALWTQDPVSFHGEFVDFDPAVVRPKPV 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 479887385  170 QQPhPPLWFGGSSEAATELAAEQVDTYLTWGEPPAAVKEKIQYLRAKAAAIGRTlnyGIRLHVIVRETNEQAWAAAD 246
Cdd:TIGR03619 155 QRP-PPIWIGGNSEAALRRAARLGDGWMPFGPPVDRLAAAVARLRDLAAAAGRD---PDAVEVVLVRTDPDGDADAD 227
Nitrilotriacetate_monoxgenase cd01095
nitrilotriacetate monoxygenase oxidizes nitrilotriacetate utilizing reduced flavin ...
 1-351 7.10e-12

nitrilotriacetate monoxygenase oxidizes nitrilotriacetate utilizing reduced flavin mononucleotide (FMNH2) and oxygen. The FMNH2 is provided by an NADH:flavin mononucleotide (FMN) oxidorductase that uses NADH to reduce FMN to FMNH2.


Pssm-ID: 238528 [Multi-domain]  Cd Length: 358  Bit Score: 66.19  E-value: 7.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385   1 MNIFWFIPTHGDSRYLGTSKGARQVDHAYMKQIAVAVDNLG------YDGVLIPTGRSCE-----DPWITAASLIDATRQ 69
Cdd:cd01095    3 LGAFLHGAGHHAAAWRHPAPPDASIDFDHYVRLARTAERAKfdavflADGLAIRALSRPHpvarlEPLTLLAALAAVTER 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385  70 LKfLVALrpgITT----PALAARMAATFDRLSNGRILLNLVTGGDEQELKGDGLYE--DHSTRYQTASEYV----KIW-- 137
Cdd:cd01095   83 IG-LVAT---ASTtynePYHLARRFASLDHISGGRAGWNVVTSANPGEARNFGRDEhpEHDERYARAEEFVevvkGLWds 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385 138 --REILTRshTGESFTFH-GERLSVDDAKL----LYPPVQQP-----HPPLWFGGSSEAATELAAEQVDTYLTWGEPPAA 205
Cdd:cd01095  159 weDDALVR--DKASGRFAdPAKVHPLDHVGdhfgVRGPLNGPrspqgRPVIVQAGSSEAGREFAARHAEAVFTAQQTLEE 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385 206 VKEKIQYLRAKAAAIGRTlnygirlhvivretneqawAAADELIQYLDDATIAAAQKKFAQMDSVGQqrMAALHGGRKDQ 285
Cdd:cd01095  237 AQAFYADVKARAAAAGRL-------------------DPPPPDLPDLGSRLSASRLLLADLLARGGL--HRREVGTAREV 295

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 479887385 286 LEvspnlwagigLVRGGAGTALVGDPETVAARIQEYADLG-IDTFIFsGYPHLEESIR-FAELVFPLL 351
Cdd:cd01095  296 AD----------RLERAAGGGTVVGPEQIADELEEWFEAGaADGFNI-MPPYLPGGLDdFVDLVVPEL 352
PRK02271 PRK02271
methylenetetrahydromethanopterin reductase; Provisional
 33-344 1.32e-06

methylenetetrahydromethanopterin reductase; Provisional


Pssm-ID: 235022 [Multi-domain]  Cd Length: 325  Bit Score: 49.55  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385  33 IAVAVDNlGYDGVLIPTGRSCEDPWITAASLIDATRQLKflvaLRPGIT-----TPALAARMAATFDRLSNGRILLNlVT 107
Cdd:PRK02271  20 AKLAEDN-GFDYAWITDHYNNRDVYMTLAAIAAATDTIK----LGPGVTnpytrHPAITASAIATLDEISGGRAVLG-IG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385 108 GGDEQELKGDGLyeDHSTRYQTASEYVKIWREILtrshTGESFTFHGErLSVDDAKLLYPPVQQpHPPLWFGGSSEAATE 187
Cdd:PRK02271  94 PGDKATLDALGI--EWEKPLRTVKEAIEVIRKLW----AGERVEHDGT-FKAAGAKLNVKPVQG-EIPIYMGAQGPKMLE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385 188 LAAEQVDTYLTWGEPP---AAVKEKIQYLRAKAAAIGRTLNYGIRLHVIVRETNEQAWAAADELIqylddATIAAAQKkf 264
Cdd:PRK02271 166 LAGEIADGVLINASNPkdfEWAVPLIKKGAEEAGKSRGEFDVAAYASVSVDKDEDKAREAAKPVV-----AFIAAGSP-- 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385 265 aqmDSVGQQrmaalHGgrkdqleVSPNLWAGIG--LVRGGAGTA-------------LVGDPETVAARIQEYADLGIDTF 329
Cdd:PRK02271 239 ---PPVLER-----HG-------IDLEAVEKIGeaLSKGDFGEAfgavtdemidafsIAGTPEDVVEKIEALLEMGVTQI 303

                        330
                 ....*....|....*...
gi 479887385 330 IFS---GyPHLEESIRFA 344
Cdd:PRK02271 304 VAGspiG-PDKEKAIKLI 320
Tetrahydromethanopterin_reductase cd01097
N5,N10-methylenetetrahydromethanopterin reductase (Mer) catalyzes the reduction of N5, ...
 94-222 5.55e-06

N5,N10-methylenetetrahydromethanopterin reductase (Mer) catalyzes the reduction of N5,N10-methylenetetrahydromethanopterin with reduced coenzyme F420 to N5-methyltetrahydromethanopterin and oxidized coenzyme F420.


Pssm-ID: 238530 [Multi-domain]  Cd Length: 202  Bit Score: 46.62  E-value: 5.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479887385  94 DRLSNGRILLNLVTGGDEQELKGDGLYEDHSTRyqTASEYVKIWREILTRSHTGESFTFHGERLSVDDAkllyPPVQQPH 173
Cdd:cd01097   37 DALSGGRFILGLGAGGPEVEEGWGGPWFKPPAR--RREELEAIRRLRALRRGDPVGEDGRFLGTRSAAL----PPPPRGE 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 479887385 174 PPLWFGGSSEAATELAAEQVDTYLTWGEPPAAVKEKIQYLRAKAAAIGR 222
Cdd:cd01097  111 IPIYIGALGPKMLELAGEIADGWLPVAAPPELYEAALPAVREGAAAAGR 159
Flavin_utilizing_monoxygenases cd00347
Flavin-utilizing monoxygenases
 175-222 5.83e-06

Flavin-utilizing monoxygenases


Pssm-ID: 238209 [Multi-domain]  Cd Length: 90  Bit Score: 44.28  E-value: 5.83e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 479887385 175 PLWFGGSSEAATELAAEQVDTYLTWG-EPPAAVKEKIQYLRAKAAAIGR 222
Cdd:cd00347   42 AIWFGGSSPPVAEQAGESGDGLLFAArEPPEEVAEALARYREAAAAAGR 90
 
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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