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Conserved domains on  [gi|517053522|ref|WP_018242340|]
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MULTISPECIES: FMNH2-dependent alkanesulfonate monooxygenase [Rhizobium]

Protein Classification

FMNH2-dependent alkanesulfonate monooxygenase( domain architecture ID 10799436)

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
alk_sulf_monoox TIGR03565
alkanesulfonate monooxygenase, FMNH(2)-dependent; Members of this protein family are ...
 14-360 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: 674.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522   14 NFLWFIPTSGDGTYLGSSELNRAPEIGYLTQIAQAVDRLGYSGVLLPTGVACEESFVTAAALAAKTEKLQFLVAIRPGTA 93
Cdd:TIGR03565   1 NIFWFIPTHGDGRYLGTSEGGRAVDHGYLKQIAQAADRLGYTGVLLPTGRSCEDSWVTASSLAPLTERLKFLVAVRPGLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522   94 SPAYYARLATTLDRISNGRLLLNIVVGGSPAELAGDGIHLEHDERYAHAEEFFTVFEELLEKGTASFDGKYIKATNARLG 173
Cdd:TIGR03565  81 SPTVAARMAATLDRLSGGRLLINVVTGGDPVELAGDGIFLDHDERYEATDEFLTVWRRLLAGETVDFDGKHIKVENAKLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  174 FPSVQNPRPPLYFGGSSDAGIDFSVGRVDKYLTWGEPPAQVAEKITKVRKAAGERGREVSFGIRLHFIVRETDDEAWEAA 253
Cdd:TIGR03565 161 FPPVQQPYPPLYFGGSSDAAIELAAEHVDVYLTWGEPPAQVAEKIAKVRKRAAKRGRTVRFGIRLHVIVRETEEEAWAAA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  254 ERLIRHLDDDTIREAQERFVHeSDSVGQKRMAALHGGRRDKLEVSPNLWAGVGLVRAGAGTALVGSPKTVAARLREYQEI 333
Cdd:TIGR03565 241 DRLISHLDDDTIARAQKAFAR-MDSVGQRRMAALHGGRRDKLEISPNLWAGVGLVRGGAGTALVGDPETVAARIREYQDL 319

                         330       340
                  ....*....|....*....|....*..
gi 517053522  334 GIDTVIGSGYPHLEEAYRVAELLFPEL 360
Cdd:TIGR03565 320 GIDTFILSGYPHLEEAYRFAELVFPLL 346
 
Name Accession Description Interval E-value
alk_sulf_monoox TIGR03565
alkanesulfonate monooxygenase, FMNH(2)-dependent; Members of this protein family are ...
 14-360 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: 674.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522   14 NFLWFIPTSGDGTYLGSSELNRAPEIGYLTQIAQAVDRLGYSGVLLPTGVACEESFVTAAALAAKTEKLQFLVAIRPGTA 93
Cdd:TIGR03565   1 NIFWFIPTHGDGRYLGTSEGGRAVDHGYLKQIAQAADRLGYTGVLLPTGRSCEDSWVTASSLAPLTERLKFLVAVRPGLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522   94 SPAYYARLATTLDRISNGRLLLNIVVGGSPAELAGDGIHLEHDERYAHAEEFFTVFEELLEKGTASFDGKYIKATNARLG 173
Cdd:TIGR03565  81 SPTVAARMAATLDRLSGGRLLINVVTGGDPVELAGDGIFLDHDERYEATDEFLTVWRRLLAGETVDFDGKHIKVENAKLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  174 FPSVQNPRPPLYFGGSSDAGIDFSVGRVDKYLTWGEPPAQVAEKITKVRKAAGERGREVSFGIRLHFIVRETDDEAWEAA 253
Cdd:TIGR03565 161 FPPVQQPYPPLYFGGSSDAAIELAAEHVDVYLTWGEPPAQVAEKIAKVRKRAAKRGRTVRFGIRLHVIVRETEEEAWAAA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  254 ERLIRHLDDDTIREAQERFVHeSDSVGQKRMAALHGGRRDKLEVSPNLWAGVGLVRAGAGTALVGSPKTVAARLREYQEI 333
Cdd:TIGR03565 241 DRLISHLDDDTIARAQKAFAR-MDSVGQRRMAALHGGRRDKLEISPNLWAGVGLVRGGAGTALVGDPETVAARIREYQDL 319

                         330       340
                  ....*....|....*....|....*..
gi 517053522  334 GIDTVIGSGYPHLEEAYRVAELLFPEL 360
Cdd:TIGR03565 320 GIDTFILSGYPHLEEAYRFAELVFPLL 346
PRK00719 PRK00719
alkanesulfonate monooxygenase; Provisional
 13-370 0e+00

alkanesulfonate monooxygenase; Provisional


Pssm-ID: 234821 [Multi-domain]  Cd Length: 378  Bit Score: 599.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  13 INFLWFIPTSGDGTYLGSSELNRAPEIGYLTQIAQAVDRLGYSGVLLPTGVACEESFVTAAALAAKTEKLQFLVAIRPGT 92
Cdd:PRK00719   1 MNVFWFLPTHGDGRYLGTSEGARAVDHGYLQQIAQAADRLGYTGVLIPTGRSCEDAWLVAASLIPVTQRLKFLVALRPGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  93 ASPAYYARLATTLDRISNGRLLLNIVVGGSPAELAGDGIHLEHDERYAHAEEFFTVFEELLEKGTASFDGKYIKATNARL 172
Cdd:PRK00719  81 MSPTVAARMAATLDRLSNGRLLINLVTGGDPAELAGDGLFLDHDERYEASAEFLRIWRRLLEGETVDFEGKHIQVKGAKL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522 173 GFPSVQNPRPPLYFGGSSDAGIDFSVGRVDKYLTWGEPPAQVAEKITKVRKAAGERGREVSFGIRLHFIVRETDDEAWEA 252
Cdd:PRK00719 161 LFPPVQQPYPPLYFGGSSDAAQELAAEQVDLYLTWGEPPAQVKEKIEQVRAKAAAHGRKVRFGIRLHVIVRETNEEAWQA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522 253 AERLIRHLDDDTIREAQERFVhESDSVGQKRMAALHGGRRDKLEVSPNLWAGVGLVRAGAGTALVGSPKTVAARLREYQE 332
Cdd:PRK00719 241 AERLISHLDDETIARAQAAFA-RMDSVGQQRMAALHGGKRDNLEISPNLWAGVGLVRGGAGTALVGDPPTVAARIKEYAA 319

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 517053522 333 IGIDTVIGSGYPHLEEAYRVAELLFPELGITREQQRLG 370
Cdd:PRK00719 320 LGIDTFILSGYPHLEEAYRVAELLFPLLDVAIPEKPQP 357
Alkanesulfonate_monoxygenase cd01094
Alkanesulfonate monoxygenase is the monoxygenase of a two-component system that catalyzes the ...
 13-255 6.71e-104

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: 306.89  E-value: 6.71e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  13 INFLWFIPTSGDGTYLGSSELNRAPEIGYLTQIAQAVDRLGYSGVLLPTGVACEESFVTAAALAAKTEKLQFLVAIRPGT 92
Cdd:cd01094    1 LEFGWFIPNVSGGWSLSTPPRGRPWDFEYNRQIAQAAEELGFDGALSPTGSSGPDGWTVAAALAAATERLKFLVAIRPGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  93 ASPAYYARLATTLDRISNGRLLLNIVVGGSPAELAGDGIHLEHDERYAHAEEFFTVFEELLEKGT-ASFDGKYIKATNAR 171
Cdd:cd01094   81 IAPTVAARQAATLDHISGGRLGLNVVTGGDPAELRMDGDFLDHDERYARADEFLEVLRRLWTSDEpFDFEGKFYRFKNAF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522 172 LGFPSVQNPRPPLYFGGSSDAGIDFSVGRVDKYLTWGEPPAQVAEKITKVRKAAGERGREVSFGIRLHFIVRETDDEAWE 251
Cdd:cd01094  161 LRPKPPQQPHPPIYFGGSSEAAIEFAARHADVYFTWGEPPAQVAEAIARVRAAAAAAGRDVRFGIRLHVIVRDTEEEAWA 240


                 ....
gi 517053522 252 AAER 255
Cdd:cd01094  241 YADR 244
Bac_luciferase pfam00296
Luciferase-like monooxygenase;
13-337 3.67e-67

Luciferase-like monooxygenase;


Pssm-ID: 425589 [Multi-domain]  Cd Length: 313  Bit Score: 215.30  E-value: 3.67e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522   13 INFLWFIPTSGDGTYLGSSelnraPEIGYLTQIAQAVDRLGYSGVLLPTGVAC---EESFVTAAALAAKTEKLQFLVAIR 89
Cdd:pfam00296   1 MEFGVFLPTRNGGGLGAGS-----ESLRYLVELARAAEELGFDGVWLAEHHGGpggPDPFVVLAALAAATSRIRLGTAVV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522   90 PGTA-SPAYYARLATTLDRISNGRLLLNIVVGGSPAELAGDGIhlEHDERYAHAEEFFTVFEELLEKGTASFDGKYIKAT 168
Cdd:pfam00296  76 PLPTrHPAVLAEQAATLDHLSGGRFDLGLGTGGPAVEFRRFGV--DHDERYARLREFLEVLRRLWRGEPVDFEGEFFTLD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  169 NARLGFPSVQnpRPPLYFGGSSDAGIDFSVGRVDKYLTWG-EPPAQVAEKITKVRKAAGERGR---EVSFGIRLHFIVRE 244
Cdd:pfam00296 154 GAFLLPRPVQ--GIPVWVAASSPAMLELAARHADGLLLWGfAPPAAAAELIERVRAGAAEAGRdpaDIRVGASLTVIVAD 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  245 TDDEAWEAAERLIRHLDDDtireaqerfvhESDSVGQKRMAALhggRRDKLEVSPNLWAGVGLVRAGA---GTALVGSPK 321
Cdd:pfam00296 232 TEEEARAEARALIAGLPFY-----------RMDSEGAGRLAEA---REIGEEYDAGDWAGAADAVPDElvrAFALVGTPE 297

                         330
                  ....*....|....*.
gi 517053522  322 TVAARLREYQEIGIDT 337
Cdd:pfam00296 298 QVAERLAAYAEAGVDH 313
SsuD COG2141
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
 50-361 7.00e-61

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: 198.62  E-value: 7.00e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  50 DRLGYSGVLL-----PTGVACEESFVTAAALAAKTEKLQFLVA-IRPGTASPAYYARLATTLDRISNGRLLLNIVVGGSP 123
Cdd:COG2141    2 ERLGFDRVWVadhhfPPGGASPDPWVLLAALAAATSRIRLGTGvVVLPLRHPLVVAEQFATLDHLSGGRLDLGVGRGWGP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522 124 AELAGDGihLEHDERYAHAEEFFTVFEELLEKGTASFDGKYIKATNARLGFPSVQNPRPPLYFGGSSDAGIDFSVGRVDK 203
Cdd:COG2141   82 DEFAAFG--LDHDERYERFEEALEVLRRLWTGEPVTFEGEFFTVEGARLVPRPVQGPHPPIWIAGSSPAGARLAARLGDG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522 204 YLTWGEPPAQVAEKITKVRKAAGERGR---EVSFGIRLHFIVRETDDEAWEAAERLIRhldddtireaqerfvhesdsvg 280
Cdd:COG2141  160 VFTAGGTPEELAEAIAAYREAAAAAGRdpdDLRVSVGLHVIVAETDEEARERARPYLR---------------------- 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522 281 qkRMAALHGGRRdkLEVSPNLWAGVGLVRAGAGTALVGSPKTVAARLREYQE-IGIDTVI-----GSGYPHLEEAYRVAE 354
Cdd:COG2141  218 --ALLALPRGRP--PEEAEEGLTVREDLLELLGAALVGTPEQVAERLEELAEaAGVDEFLlqfpgLDPEDRLRSLELFAE 293


                 ....*..
gi 517053522 355 LLFPELG 361
Cdd:COG2141  294 EVLPLLR 300
 
Name Accession Description Interval E-value
alk_sulf_monoox TIGR03565
alkanesulfonate monooxygenase, FMNH(2)-dependent; Members of this protein family are ...
 14-360 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: 674.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522   14 NFLWFIPTSGDGTYLGSSELNRAPEIGYLTQIAQAVDRLGYSGVLLPTGVACEESFVTAAALAAKTEKLQFLVAIRPGTA 93
Cdd:TIGR03565   1 NIFWFIPTHGDGRYLGTSEGGRAVDHGYLKQIAQAADRLGYTGVLLPTGRSCEDSWVTASSLAPLTERLKFLVAVRPGLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522   94 SPAYYARLATTLDRISNGRLLLNIVVGGSPAELAGDGIHLEHDERYAHAEEFFTVFEELLEKGTASFDGKYIKATNARLG 173
Cdd:TIGR03565  81 SPTVAARMAATLDRLSGGRLLINVVTGGDPVELAGDGIFLDHDERYEATDEFLTVWRRLLAGETVDFDGKHIKVENAKLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  174 FPSVQNPRPPLYFGGSSDAGIDFSVGRVDKYLTWGEPPAQVAEKITKVRKAAGERGREVSFGIRLHFIVRETDDEAWEAA 253
Cdd:TIGR03565 161 FPPVQQPYPPLYFGGSSDAAIELAAEHVDVYLTWGEPPAQVAEKIAKVRKRAAKRGRTVRFGIRLHVIVRETEEEAWAAA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  254 ERLIRHLDDDTIREAQERFVHeSDSVGQKRMAALHGGRRDKLEVSPNLWAGVGLVRAGAGTALVGSPKTVAARLREYQEI 333
Cdd:TIGR03565 241 DRLISHLDDDTIARAQKAFAR-MDSVGQRRMAALHGGRRDKLEISPNLWAGVGLVRGGAGTALVGDPETVAARIREYQDL 319

                         330       340
                  ....*....|....*....|....*..
gi 517053522  334 GIDTVIGSGYPHLEEAYRVAELLFPEL 360
Cdd:TIGR03565 320 GIDTFILSGYPHLEEAYRFAELVFPLL 346
PRK00719 PRK00719
alkanesulfonate monooxygenase; Provisional
 13-370 0e+00

alkanesulfonate monooxygenase; Provisional


Pssm-ID: 234821 [Multi-domain]  Cd Length: 378  Bit Score: 599.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  13 INFLWFIPTSGDGTYLGSSELNRAPEIGYLTQIAQAVDRLGYSGVLLPTGVACEESFVTAAALAAKTEKLQFLVAIRPGT 92
Cdd:PRK00719   1 MNVFWFLPTHGDGRYLGTSEGARAVDHGYLQQIAQAADRLGYTGVLIPTGRSCEDAWLVAASLIPVTQRLKFLVALRPGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  93 ASPAYYARLATTLDRISNGRLLLNIVVGGSPAELAGDGIHLEHDERYAHAEEFFTVFEELLEKGTASFDGKYIKATNARL 172
Cdd:PRK00719  81 MSPTVAARMAATLDRLSNGRLLINLVTGGDPAELAGDGLFLDHDERYEASAEFLRIWRRLLEGETVDFEGKHIQVKGAKL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522 173 GFPSVQNPRPPLYFGGSSDAGIDFSVGRVDKYLTWGEPPAQVAEKITKVRKAAGERGREVSFGIRLHFIVRETDDEAWEA 252
Cdd:PRK00719 161 LFPPVQQPYPPLYFGGSSDAAQELAAEQVDLYLTWGEPPAQVKEKIEQVRAKAAAHGRKVRFGIRLHVIVRETNEEAWQA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522 253 AERLIRHLDDDTIREAQERFVhESDSVGQKRMAALHGGRRDKLEVSPNLWAGVGLVRAGAGTALVGSPKTVAARLREYQE 332
Cdd:PRK00719 241 AERLISHLDDETIARAQAAFA-RMDSVGQQRMAALHGGKRDNLEISPNLWAGVGLVRGGAGTALVGDPPTVAARIKEYAA 319

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 517053522 333 IGIDTVIGSGYPHLEEAYRVAELLFPELGITREQQRLG 370
Cdd:PRK00719 320 LGIDTFILSGYPHLEEAYRVAELLFPLLDVAIPEKPQP 357
Alkanesulfonate_monoxygenase cd01094
Alkanesulfonate monoxygenase is the monoxygenase of a two-component system that catalyzes the ...
 13-255 6.71e-104

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: 306.89  E-value: 6.71e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  13 INFLWFIPTSGDGTYLGSSELNRAPEIGYLTQIAQAVDRLGYSGVLLPTGVACEESFVTAAALAAKTEKLQFLVAIRPGT 92
Cdd:cd01094    1 LEFGWFIPNVSGGWSLSTPPRGRPWDFEYNRQIAQAAEELGFDGALSPTGSSGPDGWTVAAALAAATERLKFLVAIRPGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  93 ASPAYYARLATTLDRISNGRLLLNIVVGGSPAELAGDGIHLEHDERYAHAEEFFTVFEELLEKGT-ASFDGKYIKATNAR 171
Cdd:cd01094   81 IAPTVAARQAATLDHISGGRLGLNVVTGGDPAELRMDGDFLDHDERYARADEFLEVLRRLWTSDEpFDFEGKFYRFKNAF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522 172 LGFPSVQNPRPPLYFGGSSDAGIDFSVGRVDKYLTWGEPPAQVAEKITKVRKAAGERGREVSFGIRLHFIVRETDDEAWE 251
Cdd:cd01094  161 LRPKPPQQPHPPIYFGGSSEAAIEFAARHADVYFTWGEPPAQVAEAIARVRAAAAAAGRDVRFGIRLHVIVRDTEEEAWA 240


                 ....
gi 517053522 252 AAER 255
Cdd:cd01094  241 YADR 244
Bac_luciferase pfam00296
Luciferase-like monooxygenase;
13-337 3.67e-67

Luciferase-like monooxygenase;


Pssm-ID: 425589 [Multi-domain]  Cd Length: 313  Bit Score: 215.30  E-value: 3.67e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522   13 INFLWFIPTSGDGTYLGSSelnraPEIGYLTQIAQAVDRLGYSGVLLPTGVAC---EESFVTAAALAAKTEKLQFLVAIR 89
Cdd:pfam00296   1 MEFGVFLPTRNGGGLGAGS-----ESLRYLVELARAAEELGFDGVWLAEHHGGpggPDPFVVLAALAAATSRIRLGTAVV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522   90 PGTA-SPAYYARLATTLDRISNGRLLLNIVVGGSPAELAGDGIhlEHDERYAHAEEFFTVFEELLEKGTASFDGKYIKAT 168
Cdd:pfam00296  76 PLPTrHPAVLAEQAATLDHLSGGRFDLGLGTGGPAVEFRRFGV--DHDERYARLREFLEVLRRLWRGEPVDFEGEFFTLD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  169 NARLGFPSVQnpRPPLYFGGSSDAGIDFSVGRVDKYLTWG-EPPAQVAEKITKVRKAAGERGR---EVSFGIRLHFIVRE 244
Cdd:pfam00296 154 GAFLLPRPVQ--GIPVWVAASSPAMLELAARHADGLLLWGfAPPAAAAELIERVRAGAAEAGRdpaDIRVGASLTVIVAD 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  245 TDDEAWEAAERLIRHLDDDtireaqerfvhESDSVGQKRMAALhggRRDKLEVSPNLWAGVGLVRAGA---GTALVGSPK 321
Cdd:pfam00296 232 TEEEARAEARALIAGLPFY-----------RMDSEGAGRLAEA---REIGEEYDAGDWAGAADAVPDElvrAFALVGTPE 297

                         330
                  ....*....|....*.
gi 517053522  322 TVAARLREYQEIGIDT 337
Cdd:pfam00296 298 QVAERLAAYAEAGVDH 313
SsuD COG2141
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
 50-361 7.00e-61

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: 198.62  E-value: 7.00e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  50 DRLGYSGVLL-----PTGVACEESFVTAAALAAKTEKLQFLVA-IRPGTASPAYYARLATTLDRISNGRLLLNIVVGGSP 123
Cdd:COG2141    2 ERLGFDRVWVadhhfPPGGASPDPWVLLAALAAATSRIRLGTGvVVLPLRHPLVVAEQFATLDHLSGGRLDLGVGRGWGP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522 124 AELAGDGihLEHDERYAHAEEFFTVFEELLEKGTASFDGKYIKATNARLGFPSVQNPRPPLYFGGSSDAGIDFSVGRVDK 203
Cdd:COG2141   82 DEFAAFG--LDHDERYERFEEALEVLRRLWTGEPVTFEGEFFTVEGARLVPRPVQGPHPPIWIAGSSPAGARLAARLGDG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522 204 YLTWGEPPAQVAEKITKVRKAAGERGR---EVSFGIRLHFIVRETDDEAWEAAERLIRhldddtireaqerfvhesdsvg 280
Cdd:COG2141  160 VFTAGGTPEELAEAIAAYREAAAAAGRdpdDLRVSVGLHVIVAETDEEARERARPYLR---------------------- 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522 281 qkRMAALHGGRRdkLEVSPNLWAGVGLVRAGAGTALVGSPKTVAARLREYQE-IGIDTVI-----GSGYPHLEEAYRVAE 354
Cdd:COG2141  218 --ALLALPRGRP--PEEAEEGLTVREDLLELLGAALVGTPEQVAERLEELAEaAGVDEFLlqfpgLDPEDRLRSLELFAE 293


                 ....*..
gi 517053522 355 LLFPELG 361
Cdd:COG2141  294 EVLPLLR 300
F420_Rv2161c TIGR03619
probable F420-dependent oxidoreductase, Rv2161c family; Coenzyme F420 has a limited ...
 43-256 3.91e-21

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: 91.55  E-value: 3.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522   43 TQIAQAVDRLGYSGVLLPTGVA--------------------CEESFVTAAALAAKTEKLQFL--VAIRPgTASPAYYAR 100
Cdd:TIGR03619   1 AELARAAEELGFDSLLAYEHVAiparretpwpdsgggdapdrTLDPFVALAFAAAVTSRLRLGtgVLVLP-QRDPLLLAK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  101 LATTLDRISNGRLLLNIVVGGSPAELAGDGIHLehDERYAHAEEFFTVFEELLEKGTASFDGKYIKATNARLGFPSVQNP 180
Cdd:TIGR03619  80 QAATLDLLSGGRLRLGVGVGWLREEFRALGVDF--DERGRLLDEAIEALRALWTQDPVSFHGEFVDFDPAVVRPKPVQRP 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  181 rPPLYFGGSSDAGIDFSVGRVDKYLTWGEPPAQVAEKITKVRKAAGERGR-----EVSFGIRLHFIVRETDDEAWEAAER 255
Cdd:TIGR03619 158 -PPIWIGGNSEAALRRAARLGDGWMPFGPPVDRLAAAVARLRDLAAAAGRdpdavEVVLVRTDPDGDADADAEDLAAYAD 236


                  .
gi 517053522  256 L 256
Cdd:TIGR03619 237 L 237
FMN_nitrolo TIGR03860
FMN-dependent oxidoreductase, nitrilotriacetate monooxygenase family; This model represents a ...
 31-368 6.53e-21

FMN-dependent oxidoreductase, nitrilotriacetate monooxygenase family; This model represents a distinctive clade, in which all characterized members are FMN-binding, within the larger family of luciferase-like monooxygenases (LLM), among which there are both FMN- and F420-binding enzymes. A well-characterized member is nitrilotriacetate monooxygenase from Aminobacter aminovorans (Chelatobacter heintzii), where nitrilotriacetate is a chelating agent used in detergents. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274819 [Multi-domain]  Cd Length: 422  Bit Score: 93.73  E-value: 6.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522   31 SELNRAPEIGYLTQIAQAV-----------DRLGYSGVLLPTG-----VACEESFVTAAALAAKTEKLQFLVairpgTAS 94
Cdd:TIGR03860  20 ARADAYLDLDYWTELARTAergkfdalffaDVLGVYDVPDAALrraaqLPRFEPLTLLSALAAVTEHIGLGA-----TAS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522   95 PAYY-----ARLATTLDRISNGRLLLNIVVGGSPAELA--GDGIHLEHDERYAHAEEFFTVFEELLE----------KGT 157
Cdd:TIGR03860  95 TTYEepynlARRFASLDHLSGGRAGWNIVTSYLDSAARnfGLDEHPPHDERYERAEEFVDVVYKLWDsweddafvrdKAS 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  158 ASF-----------DGKYIKATNARLGFPSVQNpRPPLYFGGSSDAGIDFSVGRVDKYLTWGEPPAQVAEKITKVRKAAG 226
Cdd:TIGR03860 175 GVFadpakvhpinhKGKHFSVRGPLNIPRSPQG-TPVLFQAGSSERGREFAARHAEAVFTAQPTLEDAQAFYADIKARAA 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  227 ERGR---EVSF--GIRlhFIVRETDDEAWEAAERLIRHLD---------------------DDTIREAQERFVHESdsvG 280
Cdd:TIGR03860 254 AAGRdpdDVKIlpGIT--PIVGRTEAEARAKYAELQDLISpegglallsgwtgidlsqydlDAPLPDLPTEAGQKS---R 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  281 QKRMAALhgGRRDKLEVSPNLWAgvgLVRAGAGTALVGSPKTVAARLREYQEIG-IDTVIgSGYPHLEEAYR-VAELLFP 358
Cdd:TIGR03860 329 FDLILEL--ARRENLTLRQLALR---LAGGRGHPVFVGTPEQVADQLEEWFEEGaADGFN-LMPPVLPGGLEdFVDLVVP 402

                         410
                  ....*....|
gi 517053522  359 ELgitreQQR 368
Cdd:TIGR03860 403 EL-----QRR 407
F420_Rv1855c TIGR03560
probable F420-dependent oxidoreductase, Rv1855c family; Coenzyme F420 has a limited ...
 42-230 4.00e-18

probable F420-dependent oxidoreductase, Rv1855c 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 one such subfamily, exemplified by Rv1855c from Mycobacterium tuberculosis. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274648 [Multi-domain]  Cd Length: 227  Bit Score: 82.75  E-value: 4.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522   42 LTQIAQAVDRLGYS-----------GVLLPTGVACEESFVTAAALAAKTEKLQFLVAIRPGT-ASPAYYARLATTLDRIS 109
Cdd:TIGR03560  15 LLAVARAAEDAGFDalfrsdhflqmPMVGPPEGPTLEAWTTLAGLARETSRIRLGTLVTGVTyRHPGLLAKMVATVDVLS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  110 NGRLLLNIVVGGSPAELAGDGIHL-EHDERYAHAEEFFTVFEELLEKGTASFDGKYIKATNARLGFPSVQNPRPPLYFGG 188
Cdd:TIGR03560  95 GGRAELGLGAGWYEREHRAYGIPFpPLAERFERLEEALQIITGMWSGEGVTFDGRHYRLADAIALPKPLQRPHPPILIGG 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 517053522  189 SSDAGIDFSVGR-VDKYLTWGEPPAQVAEKITKVRKAAGERGR 230
Cdd:TIGR03560 175 GGEKRTLRLAARyADEFNLVFGPPDELAHKFEVLRAHCEAAGR 217
Nitrilotriacetate_monoxgenase cd01095
nitrilotriacetate monoxygenase oxidizes nitrilotriacetate utilizing reduced flavin ...
 34-196 1.39e-14

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: 74.28  E-value: 1.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  34 NRAPEIGYLTQIAQAVDRLGYSGVLLPTGVACE-----------ESFVTAAALAAKTEKLQfLVAirpgTASPAYY---- 98
Cdd:cd01095   24 DASIDFDHYVRLARTAERAKFDAVFLADGLAIRalsrphpvarlEPLTLLAALAAVTERIG-LVA----TASTTYNepyh 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  99 -ARLATTLDRISNGRLLLNIVVGGSPAELAGDGI--HLEHDERYAHAEEFFTVFEEL--------LEKGTAS---FDGKY 164
Cdd:cd01095   99 lARRFASLDHISGGRAGWNVVTSANPGEARNFGRdeHPEHDERYARAEEFVEVVKGLwdsweddaLVRDKASgrfADPAK 178

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 517053522 165 IKATNARLGFPSVQNP---------RPPLYFGGSSDAGIDF 196
Cdd:cd01095  179 VHPLDHVGDHFGVRGPlngprspqgRPVIVQAGSSEAGREF 219
PRK02271 PRK02271
methylenetetrahydromethanopterin reductase; Provisional
 69-253 1.92e-09

methylenetetrahydromethanopterin reductase; Provisional


Pssm-ID: 235022 [Multi-domain]  Cd Length: 325  Bit Score: 58.41  E-value: 1.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  69 FVTAAALAAKTEKLQFLVAI-RPGTASPAYYARLATTLDRISNGRLLLNIvvG-GSPAELAGDGIhlEHDERYAHAEEFF 146
Cdd:PRK02271  43 YMTLAAIAAATDTIKLGPGVtNPYTRHPAITASAIATLDEISGGRAVLGI--GpGDKATLDALGI--EWEKPLRTVKEAI 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522 147 TVFEELLEKGTASFDGKYiKATNARLGFPSVQNpRPPLYFGGSSDAGIDFSVGRVDKYLTWGEPPAQVAEKITKVRKAAG 226
Cdd:PRK02271 119 EVIRKLWAGERVEHDGTF-KAAGAKLNVKPVQG-EIPIYMGAQGPKMLELAGEIADGVLINASNPKDFEWAVPLIKKGAE 196

                        170       180       190
                 ....*....|....*....|....*....|
gi 517053522 227 ERGR---EVSFGIRLHFIVRETDDEAWEAA 253
Cdd:PRK02271 197 EAGKsrgEFDVAAYASVSVDKDEDKAREAA 226
Tetrahydromethanopterin_reductase cd01097
N5,N10-methylenetetrahydromethanopterin reductase (Mer) catalyzes the reduction of N5, ...
 98-272 4.47e-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: 47.01  E-value: 4.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  98 YARLATTLDRISNGRLLLNIVVGGSPAElagDGIHLEHDERYAHAEEFFTVFEELLEKGTASFDGKYIKATNARLGFPS- 176
Cdd:cd01097   29 FDSVWVSLDALSGGRFILGLGAGGPEVE---EGWGGPWFKPPARRREELEAIRRLRALRRGDPVGEDGRFLGTRSAALPp 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522 177 VQNPRPPLYFGGSSDAGIDFsVGRV-DKYLTWGEPPAQVAEKITKVRKAAGERGREVSFGIRL-HFIVRETDDEAWEAAE 254
Cdd:cd01097  106 PPRGEIPIYIGALGPKMLEL-AGEIaDGWLPVAAPPELYEAALPAVREGAAAAGRVVGDPDDVaEALRRYREAGVTEVVL 184

                        170
                 ....*....|....*...
gi 517053522 255 RLIRHLDDDTIREAQERF 272
Cdd:cd01097  185 DVVGGAIDGDVERLIDLL 202
Flavin_utilizing_monoxygenases cd00347
Flavin-utilizing monoxygenases
 183-230 2.27e-03

Flavin-utilizing monoxygenases


Pssm-ID: 238209 [Multi-domain]  Cd Length: 90  Bit Score: 36.96  E-value: 2.27e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 517053522 183 PLYFGGSSDAGIDFSVGRVDKYLTWG-EPPAQVAEKITKVRKAAGERGR 230
Cdd:cd00347   42 AIWFGGSSPPVAEQAGESGDGLLFAArEPPEEVAEALARYREAAAAAGR 90
Alkanal_monooxygenase cd01096
Alkanal monooxygenase are flavin monoxygenases. Molecular oxygen is activated by reaction with ...
 69-180 8.14e-03

Alkanal monooxygenase are flavin monoxygenases. Molecular oxygen is activated by reaction with reduced flavin mononucleotide (FMNH2) and reacts with an aldehyde to yield the carboxylic acid, oxidized flavin (FMN) and a blue-green light. Bacterial luciferases are heterodimers made of alpha and beta subunits which are homologous. The single activer center is on the alpha subunit. The alpha subunit has a stretch of 30 amino acid residues that is not present in the beta subunit. The beta subunit does not contain the active site and is required for the formation of the fully active heterodimer. The beta subunit does not contribute anything directly to the active site. Its role is probably to stabilize the high quantum yield conformation of the alpha subunit through interactionbs across the subunit interface.


Pssm-ID: 238529 [Multi-domain]  Cd Length: 315  Bit Score: 37.75  E-value: 8.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517053522  69 FVTAAALAAKTEKLQF-LVAIRPGTASPAYYARLATTLDRISNGRLLLNIVVGGSPAELAGDGIHLEhdERYAHAEEFFT 147
Cdd:cd01096   56 LTAAAFLLGLTERLNVgSLNQVITTHHPVRIAEEALLLDQMSKGRFILGFSDCLYDKDMRFFGRPME--SQRQLFEACYE 133

                         90       100       110
                 ....*....|....*....|....*....|....
gi 517053522 148 VFEELLEKGTASFDGKYIKatnarlgFPSVQ-NP 180
Cdd:cd01096  134 IINDALTTGYCHPDNDFYN-------FPKISvNP 160
 
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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