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Conserved domains on  [gi|502791144|ref|WP_013026120|]
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MULTISPECIES: FMNH2-dependent alkanesulfonate monooxygenase [Pantoea]

Protein Classification

LLM class oxidoreductase( domain architecture ID 139659)

LLM (luciferase-like monooxygenase) class oxidoreductase may be a flavin-utilizing monoxygenase or a F420-dependent oxidoreductase

CATH:  3.20.20.30
EC:  1.-.-.-
Gene Ontology:  GO:0016491
SCOP:  3000585

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Flavin_utilizing_monoxygenases super family cl19096
Flavin-utilizing monoxygenases
 9-388 0e+00

Flavin-utilizing monoxygenases


The actual alignment was detected with superfamily member PRK00719:

Pssm-ID: 450250 [Multi-domain]  Cd Length: 378  Bit Score: 687.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144   9 INLFWFLPTHGDGRYLGTTQGGRAVDLPYLQQVALAADNLGFYGVLIPTGKSCEDAWLVASALVPITKQLRYLVAVRPGL 88
Cdd:PRK00719   1 MNVFWFLPTHGDGRYLGTSEGARAVDHGYLQQIAQAADRLGYTGVLIPTGRSCEDAWLVAASLIPVTQRLKFLVALRPGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144  89 QPPSLAARMAATLDRLSEGRLLINVVTGGDPVENKGDGIFLSHAERYQVTREFLDVYSRLLKGEKVDYHGEHIHVEGAEI 168
Cdd:PRK00719  81 MSPTVAARMAATLDRLSNGRLLINLVTGGDPAELAGDGLFLDHDERYEASAEFLRIWRRLLEGETVDFEGKHIQVKGAKL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144 169 LFPPVQAEGPPLYFGGSSDEAVDVAARQVDTYLTWGEPLAQVAAKLEGVRKRAEERGRTLSYGIRLHVIVRETEEEAWAA 248
Cdd:PRK00719 161 LFPPVQQPYPPLYFGGSSDAAQELAAEQVDLYLTWGEPPAQVKEKIEQVRAKAAAHGRKVRFGIRLHVIVRETNEEAWQA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144 249 ADKLIAHLDEDTIAAAQKIFARMDSTGQARMSALHGGSRDGLRIGPNLWAGVGLVRGGAGTALVGNPQQVAERIREYQAL 328
Cdd:PRK00719 241 AERLISHLDDETIARAQAAFARMDSVGQQRMAALHGGKRDNLEISPNLWAGVGLVRGGAGTALVGDPPTVAARIKEYAAL 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144 329 GIDNFILSGYPHLEEAHRVADLLMPLLPLSTPAGNKQRtvNTGPFGETIGGDRRPEKQAS 388
Cdd:PRK00719 321 GIDTFILSGYPHLEEAYRVAELLFPLLDVAIPEKPQPQ--PSGPFGEVVANDYLPKKAQS 378
 
Name Accession Description Interval E-value
PRK00719 PRK00719
alkanesulfonate monooxygenase; Provisional
 9-388 0e+00

alkanesulfonate monooxygenase; Provisional


Pssm-ID: 234821 [Multi-domain]  Cd Length: 378  Bit Score: 687.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144   9 INLFWFLPTHGDGRYLGTTQGGRAVDLPYLQQVALAADNLGFYGVLIPTGKSCEDAWLVASALVPITKQLRYLVAVRPGL 88
Cdd:PRK00719   1 MNVFWFLPTHGDGRYLGTSEGARAVDHGYLQQIAQAADRLGYTGVLIPTGRSCEDAWLVAASLIPVTQRLKFLVALRPGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144  89 QPPSLAARMAATLDRLSEGRLLINVVTGGDPVENKGDGIFLSHAERYQVTREFLDVYSRLLKGEKVDYHGEHIHVEGAEI 168
Cdd:PRK00719  81 MSPTVAARMAATLDRLSNGRLLINLVTGGDPAELAGDGLFLDHDERYEASAEFLRIWRRLLEGETVDFEGKHIQVKGAKL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144 169 LFPPVQAEGPPLYFGGSSDEAVDVAARQVDTYLTWGEPLAQVAAKLEGVRKRAEERGRTLSYGIRLHVIVRETEEEAWAA 248
Cdd:PRK00719 161 LFPPVQQPYPPLYFGGSSDAAQELAAEQVDLYLTWGEPPAQVKEKIEQVRAKAAAHGRKVRFGIRLHVIVRETNEEAWQA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144 249 ADKLIAHLDEDTIAAAQKIFARMDSTGQARMSALHGGSRDGLRIGPNLWAGVGLVRGGAGTALVGNPQQVAERIREYQAL 328
Cdd:PRK00719 241 AERLISHLDDETIARAQAAFARMDSVGQQRMAALHGGKRDNLEISPNLWAGVGLVRGGAGTALVGDPPTVAARIKEYAAL 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144 329 GIDNFILSGYPHLEEAHRVADLLMPLLPLSTPAGNKQRtvNTGPFGETIGGDRRPEKQAS 388
Cdd:PRK00719 321 GIDTFILSGYPHLEEAYRVAELLFPLLDVAIPEKPQPQ--PSGPFGEVVANDYLPKKAQS 378
alk_sulf_monoox TIGR03565
alkanesulfonate monooxygenase, FMNH(2)-dependent; Members of this protein family are ...
 10-355 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: 647.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144   10 NLFWFLPTHGDGRYLGTTQGGRAVDLPYLQQVALAADNLGFYGVLIPTGKSCEDAWLVASALVPITKQLRYLVAVRPGLQ 89
Cdd:TIGR03565   1 NIFWFIPTHGDGRYLGTSEGGRAVDHGYLKQIAQAADRLGYTGVLLPTGRSCEDSWVTASSLAPLTERLKFLVAVRPGLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144   90 PPSLAARMAATLDRLSEGRLLINVVTGGDPVENKGDGIFLSHAERYQVTREFLDVYSRLLKGEKVDYHGEHIHVEGAEIL 169
Cdd:TIGR03565  81 SPTVAARMAATLDRLSGGRLLINVVTGGDPVELAGDGIFLDHDERYEATDEFLTVWRRLLAGETVDFDGKHIKVENAKLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144  170 FPPVQAEGPPLYFGGSSDEAVDVAARQVDTYLTWGEPLAQVAAKLEGVRKRAEERGRTLSYGIRLHVIVRETEEEAWAAA 249
Cdd:TIGR03565 161 FPPVQQPYPPLYFGGSSDAAIELAAEHVDVYLTWGEPPAQVAEKIAKVRKRAAKRGRTVRFGIRLHVIVRETEEEAWAAA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144  250 DKLIAHLDEDTIAAAQKIFARMDSTGQARMSALHGGSRDGLRIGPNLWAGVGLVRGGAGTALVGNPQQVAERIREYQALG 329
Cdd:TIGR03565 241 DRLISHLDDDTIARAQKAFARMDSVGQRRMAALHGGRRDKLEISPNLWAGVGLVRGGAGTALVGDPETVAARIREYQDLG 320

                         330       340
                  ....*....|....*....|....*.
gi 502791144  330 IDNFILSGYPHLEEAHRVADLLMPLL 355
Cdd:TIGR03565 321 IDTFILSGYPHLEEAYRFAELVFPLL 346
Alkanesulfonate_monoxygenase cd01094
Alkanesulfonate monoxygenase is the monoxygenase of a two-component system that catalyzes the ...
 9-239 4.03e-98

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: 291.87  E-value: 4.03e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144   9 INLFWFLPTHGDGRYLGTTQGGRAVDLPYLQQVALAADNLGFYGVLIPTGKSCEDAWLVASALVPITKQLRYLVAVRPGL 88
Cdd:cd01094    1 LEFGWFIPNVSGGWSLSTPPRGRPWDFEYNRQIAQAAEELGFDGALSPTGSSGPDGWTVAAALAAATERLKFLVAIRPGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144  89 QPPSLAARMAATLDRLSEGRLLINVVTGGDPVENKGDGIFLSHAERYQVTREFLDVYSRLLKGEK-VDYHGEHIHVEGAE 167
Cdd:cd01094   81 IAPTVAARQAATLDHISGGRLGLNVVTGGDPAELRMDGDFLDHDERYARADEFLEVLRRLWTSDEpFDFEGKFYRFKNAF 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502791144 168 ILFPPVQAEGPPLYFGGSSDEAVDVAARQVDTYLTWGEPLAQVAAKLEGVRKRAEERGRTLSYGIRLHVIVR 239
Cdd:cd01094  161 LRPKPPQQPHPPIYFGGSSEAAIEFAARHADVYFTWGEPPAQVAEAIARVRAAAAAAGRDVRFGIRLHVIVR 232
Bac_luciferase pfam00296
Luciferase-like monooxygenase;
9-331 4.65e-71

Luciferase-like monooxygenase;


Pssm-ID: 425589 [Multi-domain]  Cd Length: 313  Bit Score: 225.32  E-value: 4.65e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144    9 INLFWFLPTHGDGRYLGTtqggrAVDLPYLQQVALAADNLGFYGVLIPTGKSC---EDAWLVASALVPITKQLRYLVAVR 85
Cdd:pfam00296   1 MEFGVFLPTRNGGGLGAG-----SESLRYLVELARAAEELGFDGVWLAEHHGGpggPDPFVVLAALAAATSRIRLGTAVV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144   86 PG-LQPPSLAARMAATLDRLSEGRLLINVVTGGDPVENKGDGIflSHAERYQVTREFLDVYSRLLKGEKVDYHGEHIHVE 164
Cdd:pfam00296  76 PLpTRHPAVLAEQAATLDHLSGGRFDLGLGTGGPAVEFRRFGV--DHDERYARLREFLEVLRRLWRGEPVDFEGEFFTLD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144  165 GAEILFPPVQaeGPPLYFGGSSDEAVDVAARQVDTYLTWG-EPLAQVAAKLEGVRKRAEERGRTLS---YGIRLHVIVRE 240
Cdd:pfam00296 154 GAFLLPRPVQ--GIPVWVAASSPAMLELAARHADGLLLWGfAPPAAAAELIERVRAGAAEAGRDPAdirVGASLTVIVAD 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144  241 TEEEAWAAADKLIAHLDedtiaaaqkiFARMDSTGQARMSALHggsRDGLRIGPNLWAGVGLVRGGA---GTALVGNPQQ 317
Cdd:pfam00296 232 TEEEARAEARALIAGLP----------FYRMDSEGAGRLAEAR---EIGEEYDAGDWAGAADAVPDElvrAFALVGTPEQ 298

                         330
                  ....*....|....
gi 502791144  318 VAERIREYQALGID 331
Cdd:pfam00296 299 VAERLAAYAEAGVD 312
SsuD COG2141
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
 45-355 1.85e-58

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: 192.46  E-value: 1.85e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144  45 ADNLGFYGVLI-----PTGKSCEDAWLVASALVPITKQLRYLVAV-RPGLQPPSLAARMAATLDRLSEGRLLINVVTGGD 118
Cdd:COG2141    1 AERLGFDRVWVadhhfPPGGASPDPWVLLAALAAATSRIRLGTGVvVLPLRHPLVVAEQFATLDHLSGGRLDLGVGRGWG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144 119 PVENKGDGifLSHAERYQVTREFLDVYSRLLKGEKVDYHGEHIHVEGAEILFPPVQAEGPPLYFGGSSDEAVDVAARQVD 198
Cdd:COG2141   81 PDEFAAFG--LDHDERYERFEEALEVLRRLWTGEPVTFEGEFFTVEGARLVPRPVQGPHPPIWIAGSSPAGARLAARLGD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144 199 TYLTWGEPLAQVAAKLEGVRKRAEERGR---TLSYGIRLHVIVReteeeawaaadkliahldeDTIAAAQKIFA-RMDST 274
Cdd:COG2141  159 GVFTAGGTPEELAEAIAAYREAAAAAGRdpdDLRVSVGLHVIVA-------------------ETDEEARERARpYLRAL 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144 275 GQARMSALHGGSRDGLRIGPNLWAGVglvrggaGTALVGNPQQVAERIREY-QALGIDNFILS-----GYPHLEEAHRVA 348
Cdd:COG2141  220 LALPRGRPPEEAEEGLTVREDLLELL-------GAALVGTPEQVAERLEELaEAAGVDEFLLQfpgldPEDRLRSLELFA 292


                 ....*..
gi 502791144 349 DLLMPLL 355
Cdd:COG2141  293 EEVLPLL 299
 
Name Accession Description Interval E-value
PRK00719 PRK00719
alkanesulfonate monooxygenase; Provisional
 9-388 0e+00

alkanesulfonate monooxygenase; Provisional


Pssm-ID: 234821 [Multi-domain]  Cd Length: 378  Bit Score: 687.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144   9 INLFWFLPTHGDGRYLGTTQGGRAVDLPYLQQVALAADNLGFYGVLIPTGKSCEDAWLVASALVPITKQLRYLVAVRPGL 88
Cdd:PRK00719   1 MNVFWFLPTHGDGRYLGTSEGARAVDHGYLQQIAQAADRLGYTGVLIPTGRSCEDAWLVAASLIPVTQRLKFLVALRPGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144  89 QPPSLAARMAATLDRLSEGRLLINVVTGGDPVENKGDGIFLSHAERYQVTREFLDVYSRLLKGEKVDYHGEHIHVEGAEI 168
Cdd:PRK00719  81 MSPTVAARMAATLDRLSNGRLLINLVTGGDPAELAGDGLFLDHDERYEASAEFLRIWRRLLEGETVDFEGKHIQVKGAKL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144 169 LFPPVQAEGPPLYFGGSSDEAVDVAARQVDTYLTWGEPLAQVAAKLEGVRKRAEERGRTLSYGIRLHVIVRETEEEAWAA 248
Cdd:PRK00719 161 LFPPVQQPYPPLYFGGSSDAAQELAAEQVDLYLTWGEPPAQVKEKIEQVRAKAAAHGRKVRFGIRLHVIVRETNEEAWQA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144 249 ADKLIAHLDEDTIAAAQKIFARMDSTGQARMSALHGGSRDGLRIGPNLWAGVGLVRGGAGTALVGNPQQVAERIREYQAL 328
Cdd:PRK00719 241 AERLISHLDDETIARAQAAFARMDSVGQQRMAALHGGKRDNLEISPNLWAGVGLVRGGAGTALVGDPPTVAARIKEYAAL 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144 329 GIDNFILSGYPHLEEAHRVADLLMPLLPLSTPAGNKQRtvNTGPFGETIGGDRRPEKQAS 388
Cdd:PRK00719 321 GIDTFILSGYPHLEEAYRVAELLFPLLDVAIPEKPQPQ--PSGPFGEVVANDYLPKKAQS 378
alk_sulf_monoox TIGR03565
alkanesulfonate monooxygenase, FMNH(2)-dependent; Members of this protein family are ...
 10-355 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: 647.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144   10 NLFWFLPTHGDGRYLGTTQGGRAVDLPYLQQVALAADNLGFYGVLIPTGKSCEDAWLVASALVPITKQLRYLVAVRPGLQ 89
Cdd:TIGR03565   1 NIFWFIPTHGDGRYLGTSEGGRAVDHGYLKQIAQAADRLGYTGVLLPTGRSCEDSWVTASSLAPLTERLKFLVAVRPGLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144   90 PPSLAARMAATLDRLSEGRLLINVVTGGDPVENKGDGIFLSHAERYQVTREFLDVYSRLLKGEKVDYHGEHIHVEGAEIL 169
Cdd:TIGR03565  81 SPTVAARMAATLDRLSGGRLLINVVTGGDPVELAGDGIFLDHDERYEATDEFLTVWRRLLAGETVDFDGKHIKVENAKLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144  170 FPPVQAEGPPLYFGGSSDEAVDVAARQVDTYLTWGEPLAQVAAKLEGVRKRAEERGRTLSYGIRLHVIVRETEEEAWAAA 249
Cdd:TIGR03565 161 FPPVQQPYPPLYFGGSSDAAIELAAEHVDVYLTWGEPPAQVAEKIAKVRKRAAKRGRTVRFGIRLHVIVRETEEEAWAAA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144  250 DKLIAHLDEDTIAAAQKIFARMDSTGQARMSALHGGSRDGLRIGPNLWAGVGLVRGGAGTALVGNPQQVAERIREYQALG 329
Cdd:TIGR03565 241 DRLISHLDDDTIARAQKAFARMDSVGQRRMAALHGGRRDKLEISPNLWAGVGLVRGGAGTALVGDPETVAARIREYQDLG 320

                         330       340
                  ....*....|....*....|....*.
gi 502791144  330 IDNFILSGYPHLEEAHRVADLLMPLL 355
Cdd:TIGR03565 321 IDTFILSGYPHLEEAYRFAELVFPLL 346
Alkanesulfonate_monoxygenase cd01094
Alkanesulfonate monoxygenase is the monoxygenase of a two-component system that catalyzes the ...
 9-239 4.03e-98

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: 291.87  E-value: 4.03e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144   9 INLFWFLPTHGDGRYLGTTQGGRAVDLPYLQQVALAADNLGFYGVLIPTGKSCEDAWLVASALVPITKQLRYLVAVRPGL 88
Cdd:cd01094    1 LEFGWFIPNVSGGWSLSTPPRGRPWDFEYNRQIAQAAEELGFDGALSPTGSSGPDGWTVAAALAAATERLKFLVAIRPGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144  89 QPPSLAARMAATLDRLSEGRLLINVVTGGDPVENKGDGIFLSHAERYQVTREFLDVYSRLLKGEK-VDYHGEHIHVEGAE 167
Cdd:cd01094   81 IAPTVAARQAATLDHISGGRLGLNVVTGGDPAELRMDGDFLDHDERYARADEFLEVLRRLWTSDEpFDFEGKFYRFKNAF 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502791144 168 ILFPPVQAEGPPLYFGGSSDEAVDVAARQVDTYLTWGEPLAQVAAKLEGVRKRAEERGRTLSYGIRLHVIVR 239
Cdd:cd01094  161 LRPKPPQQPHPPIYFGGSSEAAIEFAARHADVYFTWGEPPAQVAEAIARVRAAAAAAGRDVRFGIRLHVIVR 232
Bac_luciferase pfam00296
Luciferase-like monooxygenase;
9-331 4.65e-71

Luciferase-like monooxygenase;


Pssm-ID: 425589 [Multi-domain]  Cd Length: 313  Bit Score: 225.32  E-value: 4.65e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144    9 INLFWFLPTHGDGRYLGTtqggrAVDLPYLQQVALAADNLGFYGVLIPTGKSC---EDAWLVASALVPITKQLRYLVAVR 85
Cdd:pfam00296   1 MEFGVFLPTRNGGGLGAG-----SESLRYLVELARAAEELGFDGVWLAEHHGGpggPDPFVVLAALAAATSRIRLGTAVV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144   86 PG-LQPPSLAARMAATLDRLSEGRLLINVVTGGDPVENKGDGIflSHAERYQVTREFLDVYSRLLKGEKVDYHGEHIHVE 164
Cdd:pfam00296  76 PLpTRHPAVLAEQAATLDHLSGGRFDLGLGTGGPAVEFRRFGV--DHDERYARLREFLEVLRRLWRGEPVDFEGEFFTLD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144  165 GAEILFPPVQaeGPPLYFGGSSDEAVDVAARQVDTYLTWG-EPLAQVAAKLEGVRKRAEERGRTLS---YGIRLHVIVRE 240
Cdd:pfam00296 154 GAFLLPRPVQ--GIPVWVAASSPAMLELAARHADGLLLWGfAPPAAAAELIERVRAGAAEAGRDPAdirVGASLTVIVAD 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144  241 TEEEAWAAADKLIAHLDedtiaaaqkiFARMDSTGQARMSALHggsRDGLRIGPNLWAGVGLVRGGA---GTALVGNPQQ 317
Cdd:pfam00296 232 TEEEARAEARALIAGLP----------FYRMDSEGAGRLAEAR---EIGEEYDAGDWAGAADAVPDElvrAFALVGTPEQ 298

                         330
                  ....*....|....
gi 502791144  318 VAERIREYQALGID 331
Cdd:pfam00296 299 VAERLAAYAEAGVD 312
SsuD COG2141
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
 45-355 1.85e-58

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: 192.46  E-value: 1.85e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144  45 ADNLGFYGVLI-----PTGKSCEDAWLVASALVPITKQLRYLVAV-RPGLQPPSLAARMAATLDRLSEGRLLINVVTGGD 118
Cdd:COG2141    1 AERLGFDRVWVadhhfPPGGASPDPWVLLAALAAATSRIRLGTGVvVLPLRHPLVVAEQFATLDHLSGGRLDLGVGRGWG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144 119 PVENKGDGifLSHAERYQVTREFLDVYSRLLKGEKVDYHGEHIHVEGAEILFPPVQAEGPPLYFGGSSDEAVDVAARQVD 198
Cdd:COG2141   81 PDEFAAFG--LDHDERYERFEEALEVLRRLWTGEPVTFEGEFFTVEGARLVPRPVQGPHPPIWIAGSSPAGARLAARLGD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144 199 TYLTWGEPLAQVAAKLEGVRKRAEERGR---TLSYGIRLHVIVReteeeawaaadkliahldeDTIAAAQKIFA-RMDST 274
Cdd:COG2141  159 GVFTAGGTPEELAEAIAAYREAAAAAGRdpdDLRVSVGLHVIVA-------------------ETDEEARERARpYLRAL 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144 275 GQARMSALHGGSRDGLRIGPNLWAGVglvrggaGTALVGNPQQVAERIREY-QALGIDNFILS-----GYPHLEEAHRVA 348
Cdd:COG2141  220 LALPRGRPPEEAEEGLTVREDLLELL-------GAALVGTPEQVAERLEELaEAAGVDEFLLQfpgldPEDRLRSLELFA 292


                 ....*..
gi 502791144 349 DLLMPLL 355
Cdd:COG2141  293 EEVLPLL 299
F420_Rv2161c TIGR03619
probable F420-dependent oxidoreductase, Rv2161c family; Coenzyme F420 has a limited ...
 91-227 4.90e-19

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: 85.39  E-value: 4.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144   91 PSLAARMAATLDRLSEGRLLINVVTGGDPVEnkgdgiFLSH----AERYQVTREFLDVYSRLLKGEKVDYHGEHIHVEGA 166
Cdd:TIGR03619  74 PLLLAKQAATLDLLSGGRLRLGVGVGWLREE------FRALgvdfDERGRLLDEAIEALRALWTQDPVSFHGEFVDFDPA 147

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502791144  167 EILFPPVQAeGPPLYFGGSSDEAVDVAARQVDTYLTWGEPLAQVAAKLEGVRKRAEERGRT 227
Cdd:TIGR03619 148 VVRPKPVQR-PPPIWIGGNSEAALRRAARLGDGWMPFGPPVDRLAAAVARLRDLAAAAGRD 207
Nitrilotriacetate_monoxgenase cd01095
nitrilotriacetate monoxygenase oxidizes nitrilotriacetate utilizing reduced flavin ...
 95-226 2.64e-11

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: 64.27  E-value: 2.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144  95 ARMAATLDRLSEGRLLINVVTGGDPVENKGDGI--FLSHAERYQVTREFLDV---------------------YSRLLKG 151
Cdd:cd01095  100 ARRFASLDHISGGRAGWNVVTSANPGEARNFGRdeHPEHDERYARAEEFVEVvkglwdsweddalvrdkasgrFADPAKV 179

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502791144 152 EKVDYHGEHIHVEGAeiLFPPVQAEGPPLYF-GGSSDEAVDVAARQVDTYLTWGEPLAQVAAKLEGVRKRAEERGR 226
Cdd:cd01095  180 HPLDHVGDHFGVRGP--LNGPRSPQGRPVIVqAGSSEAGREFAARHAEAVFTAQQTLEEAQAFYADVKARAAAAGR 253
Tetrahydromethanopterin_reductase cd01097
N5,N10-methylenetetrahydromethanopterin reductase (Mer) catalyzes the reduction of N5, ...
 99-226 2.43e-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: 47.78  E-value: 2.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502791144  99 ATLDRLSEGRLLINVVTGGDPVENKGDGIFLSHAERYqvTREFLDVYSRLLKGEKVDYHGEHIHVEGAEILFPPVQAEGP 178
Cdd:cd01097   34 VSLDALSGGRFILGLGAGGPEVEEGWGGPWFKPPARR--REELEAIRRLRALRRGDPVGEDGRFLGTRSAALPPPPRGEI 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 502791144 179 PLYFGGSSDEAVDVAARQVDTYLTWGEPLAQVAAKLEGVRKRAEERGR 226
Cdd:cd01097  112 PIYIGALGPKMLELAGEIADGWLPVAAPPELYEAALPAVREGAAAAGR 159
Flavin_utilizing_monoxygenases cd00347
Flavin-utilizing monoxygenases
 179-226 7.28e-06

Flavin-utilizing monoxygenases


Pssm-ID: 238209 [Multi-domain]  Cd Length: 90  Bit Score: 43.89  E-value: 7.28e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 502791144 179 PLYFGGSSDEAVDVAARQVDTYLTWG-EPLAQVAAKLEGVRKRAEERGR 226
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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