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Conserved domains on  [gi|489126048|ref|WP_003035845|]
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MULTISPECIES: FMNH2-dependent alkanesulfonate monooxygenase [Citrobacter]

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
 3-380 0e+00

alkanesulfonate monooxygenase; Provisional


:

Pssm-ID: 234821 [Multi-domain]  Cd Length: 378  Bit Score: 804.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048   3 LNMFWFLPTHGDGHYLGTEEGSRPVDHGYLQQIAQTADRLGFTGVLIPTGRSCEDAWLVAASMIPVTQRLKFLVALRPSV 82
Cdd:PRK00719   1 MNVFWFLPTHGDGRYLGTSEGARAVDHGYLQQIAQAADRLGYTGVLIPTGRSCEDAWLVAASLIPVTQRLKFLVALRPGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048  83 TSPTVAARQAATLDRLSNGRALFNLVTGSDPQELAGDGVFLDHTERYEASAEFTQVWRRLLQGETVDFNGKHIHVRGAKL 162
Cdd:PRK00719  81 MSPTVAARMAATLDRLSNGRLLINLVTGGDPAELAGDGLFLDHDERYEASAEFLRIWRRLLEGETVDFEGKHIQVKGAKL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048 163 FFPPVQQPRPPLYFGGSSDVAQDLAAEQVDLYLTWGEPPEQVKAKIEQVRAKAAALGRKIRFGIRLHVIVRETTHEAWQA 242
Cdd:PRK00719 161 LFPPVQQPYPPLYFGGSSDAAQELAAEQVDLYLTWGEPPAQVKEKIEQVRAKAAAHGRKVRFGIRLHVIVRETNEEAWQA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048 243 ADRLIVHLDDDTIAKAQAAFSKTDSVGQQRMAALHNGKRDKLEISPNLWAGVGLVRGGAGTALVGDGPTVAARINEYAAL 322
Cdd:PRK00719 241 AERLISHLDDETIARAQAAFARMDSVGQQRMAALHGGKRDNLEISPNLWAGVGLVRGGAGTALVGDPPTVAARIKEYAAL 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489126048 323 GIDSFVLSGYPHLEEAYRVGELLFPHLDVAIPEIPQPQRLQQQGEAVANEFIPRKVAQ 380
Cdd:PRK00719 321 GIDTFILSGYPHLEEAYRVAELLFPLLDVAIPEKPQPQPSGPFGEVVANDYLPKKAQS 378
 
Name Accession Description Interval E-value
PRK00719 PRK00719
alkanesulfonate monooxygenase; Provisional
 3-380 0e+00

alkanesulfonate monooxygenase; Provisional


Pssm-ID: 234821 [Multi-domain]  Cd Length: 378  Bit Score: 804.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048   3 LNMFWFLPTHGDGHYLGTEEGSRPVDHGYLQQIAQTADRLGFTGVLIPTGRSCEDAWLVAASMIPVTQRLKFLVALRPSV 82
Cdd:PRK00719   1 MNVFWFLPTHGDGRYLGTSEGARAVDHGYLQQIAQAADRLGYTGVLIPTGRSCEDAWLVAASLIPVTQRLKFLVALRPGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048  83 TSPTVAARQAATLDRLSNGRALFNLVTGSDPQELAGDGVFLDHTERYEASAEFTQVWRRLLQGETVDFNGKHIHVRGAKL 162
Cdd:PRK00719  81 MSPTVAARMAATLDRLSNGRLLINLVTGGDPAELAGDGLFLDHDERYEASAEFLRIWRRLLEGETVDFEGKHIQVKGAKL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048 163 FFPPVQQPRPPLYFGGSSDVAQDLAAEQVDLYLTWGEPPEQVKAKIEQVRAKAAALGRKIRFGIRLHVIVRETTHEAWQA 242
Cdd:PRK00719 161 LFPPVQQPYPPLYFGGSSDAAQELAAEQVDLYLTWGEPPAQVKEKIEQVRAKAAAHGRKVRFGIRLHVIVRETNEEAWQA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048 243 ADRLIVHLDDDTIAKAQAAFSKTDSVGQQRMAALHNGKRDKLEISPNLWAGVGLVRGGAGTALVGDGPTVAARINEYAAL 322
Cdd:PRK00719 241 AERLISHLDDETIARAQAAFARMDSVGQQRMAALHGGKRDNLEISPNLWAGVGLVRGGAGTALVGDPPTVAARIKEYAAL 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489126048 323 GIDSFVLSGYPHLEEAYRVGELLFPHLDVAIPEIPQPQRLQQQGEAVANEFIPRKVAQ 380
Cdd:PRK00719 321 GIDTFILSGYPHLEEAYRVAELLFPLLDVAIPEKPQPQPSGPFGEVVANDYLPKKAQS 378
alk_sulf_monoox TIGR03565
alkanesulfonate monooxygenase, FMNH(2)-dependent; Members of this protein family are ...
 4-349 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: 708.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048    4 NMFWFLPTHGDGHYLGTEEGSRPVDHGYLQQIAQTADRLGFTGVLIPTGRSCEDAWLVAASMIPVTQRLKFLVALRPSVT 83
Cdd:TIGR03565   1 NIFWFIPTHGDGRYLGTSEGGRAVDHGYLKQIAQAADRLGYTGVLLPTGRSCEDSWVTASSLAPLTERLKFLVAVRPGLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048   84 SPTVAARQAATLDRLSNGRALFNLVTGSDPQELAGDGVFLDHTERYEASAEFTQVWRRLLQGETVDFNGKHIHVRGAKLF 163
Cdd:TIGR03565  81 SPTVAARMAATLDRLSGGRLLINVVTGGDPVELAGDGIFLDHDERYEATDEFLTVWRRLLAGETVDFDGKHIKVENAKLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048  164 FPPVQQPRPPLYFGGSSDVAQDLAAEQVDLYLTWGEPPEQVKAKIEQVRAKAAALGRKIRFGIRLHVIVRETTHEAWQAA 243
Cdd:TIGR03565 161 FPPVQQPYPPLYFGGSSDAAIELAAEHVDVYLTWGEPPAQVAEKIAKVRKRAAKRGRTVRFGIRLHVIVRETEEEAWAAA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048  244 DRLIVHLDDDTIAKAQAAFSKTDSVGQQRMAALHNGKRDKLEISPNLWAGVGLVRGGAGTALVGDGPTVAARINEYAALG 323
Cdd:TIGR03565 241 DRLISHLDDDTIARAQKAFARMDSVGQRRMAALHGGRRDKLEISPNLWAGVGLVRGGAGTALVGDPETVAARIREYQDLG 320

                         330       340
                  ....*....|....*....|....*.
gi 489126048  324 IDSFVLSGYPHLEEAYRVGELLFPHL 349
Cdd:TIGR03565 321 IDTFILSGYPHLEEAYRFAELVFPLL 346
Alkanesulfonate_monoxygenase cd01094
Alkanesulfonate monoxygenase is the monoxygenase of a two-component system that catalyzes the ...
 3-245 3.01e-119

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: 345.41  E-value: 3.01e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048   3 LNMFWFLPTHGDGHYLGTEEGSRPVDHGYLQQIAQTADRLGFTGVLIPTGRSCEDAWLVAASMIPVTQRLKFLVALRPSV 82
Cdd:cd01094    1 LEFGWFIPNVSGGWSLSTPPRGRPWDFEYNRQIAQAAEELGFDGALSPTGSSGPDGWTVAAALAAATERLKFLVAIRPGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048  83 TSPTVAARQAATLDRLSNGRALFNLVTGSDPQELAGDGVFLDHTERYEASAEFTQVWRRLLQGET-VDFNGKHIHVRGAK 161
Cdd:cd01094   81 IAPTVAARQAATLDHISGGRLGLNVVTGGDPAELRMDGDFLDHDERYARADEFLEVLRRLWTSDEpFDFEGKFYRFKNAF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048 162 LFFPPVQQPRPPLYFGGSSDVAQDLAAEQVDLYLTWGEPPEQVKAKIEQVRAKAAALGRKIRFGIRLHVIVRETTHEAWQ 241
Cdd:cd01094  161 LRPKPPQQPHPPIYFGGSSEAAIEFAARHADVYFTWGEPPAQVAEAIARVRAAAAAAGRDVRFGIRLHVIVRDTEEEAWA 240


                 ....
gi 489126048 242 AADR 245
Cdd:cd01094  241 YADR 244
Bac_luciferase pfam00296
Luciferase-like monooxygenase;
6-326 1.15e-73

Luciferase-like monooxygenase;


Pssm-ID: 425589 [Multi-domain]  Cd Length: 313  Bit Score: 231.48  E-value: 1.15e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048    6 FWFLPTHGDGHYLGTEEGSRpvdhgYLQQIAQTADRLGFTGVLIPTGRSC---EDAWLVAASMIPVTQRLKFLVALRPSV 82
Cdd:pfam00296   4 GVFLPTRNGGGLGAGSESLR-----YLVELARAAEELGFDGVWLAEHHGGpggPDPFVVLAALAAATSRIRLGTAVVPLP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048   83 T-SPTVAARQAATLDRLSNGRALFNLVTGSDPQELAGDGVflDHTERYEASAEFTQVWRRLLQGETVDFNGKHIHVRGAK 161
Cdd:pfam00296  79 TrHPAVLAEQAATLDHLSGGRFDLGLGTGGPAVEFRRFGV--DHDERYARLREFLEVLRRLWRGEPVDFEGEFFTLDGAF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048  162 LFFPPVQqpRPPLYFGGSSDVAQDLAAEQVDLYLTWG-EPPEQVKAKIEQVRAKAAALGR---KIRFGIRLHVIVRETTH 237
Cdd:pfam00296 157 LLPRPVQ--GIPVWVAASSPAMLELAARHADGLLLWGfAPPAAAAELIERVRAGAAEAGRdpaDIRVGASLTVIVADTEE 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048  238 EAWQAADRLIVHLDddtiakaqaaFSKTDSVGQQRMAALHngkRDKLEISPNLWAGVGLVRGGA---GTALVGDGPTVAA 314
Cdd:pfam00296 235 EARAEARALIAGLP----------FYRMDSEGAGRLAEAR---EIGEEYDAGDWAGAADAVPDElvrAFALVGTPEQVAE 301

                         330
                  ....*....|..
gi 489126048  315 RINEYAALGIDS 326
Cdd:pfam00296 302 RLAAYAEAGVDH 313
SsuD COG2141
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
 39-349 1.54e-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: 210.18  E-value: 1.54e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048  39 ADRLGFTGVLI-----PTGRSCEDAWLVAASMIPVTQRLKFLVA-LRPSVTSPTVAARQAATLDRLSNGRALFNLVTGSD 112
Cdd:COG2141    1 AERLGFDRVWVadhhfPPGGASPDPWVLLAALAAATSRIRLGTGvVVLPLRHPLVVAEQFATLDHLSGGRLDLGVGRGWG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048 113 PQELAGDGvfLDHTERYEASAEFTQVWRRLLQGETVDFNGKHIHVRGAKLFFPPVQQPRPPLYFGGSSDVAQDLAAEQVD 192
Cdd:COG2141   81 PDEFAAFG--LDHDERYERFEEALEVLRRLWTGEPVTFEGEFFTVEGARLVPRPVQGPHPPIWIAGSSPAGARLAARLGD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048 193 LYLTWGEPPEQVKAKIEQVRAKAAALGR---KIRFGIRLHVIVRETTHEAWQAADRlivhldddtiakAQAAFSKTDSVG 269
Cdd:COG2141  159 GVFTAGGTPEELAEAIAAYREAAAAAGRdpdDLRVSVGLHVIVAETDEEARERARP------------YLRALLALPRGR 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048 270 QQRMAAlhngkrDKLEISPNLWAGVglvrggaGTALVGDGPTVAARINEYA-ALGIDSFVLS-----GYPHLEEAYRVGE 343
Cdd:COG2141  227 PPEEAE------EGLTVREDLLELL-------GAALVGTPEQVAERLEELAeAAGVDEFLLQfpgldPEDRLRSLELFAE 293


                 ....*.
gi 489126048 344 LLFPHL 349
Cdd:COG2141  294 EVLPLL 299
 
Name Accession Description Interval E-value
PRK00719 PRK00719
alkanesulfonate monooxygenase; Provisional
 3-380 0e+00

alkanesulfonate monooxygenase; Provisional


Pssm-ID: 234821 [Multi-domain]  Cd Length: 378  Bit Score: 804.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048   3 LNMFWFLPTHGDGHYLGTEEGSRPVDHGYLQQIAQTADRLGFTGVLIPTGRSCEDAWLVAASMIPVTQRLKFLVALRPSV 82
Cdd:PRK00719   1 MNVFWFLPTHGDGRYLGTSEGARAVDHGYLQQIAQAADRLGYTGVLIPTGRSCEDAWLVAASLIPVTQRLKFLVALRPGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048  83 TSPTVAARQAATLDRLSNGRALFNLVTGSDPQELAGDGVFLDHTERYEASAEFTQVWRRLLQGETVDFNGKHIHVRGAKL 162
Cdd:PRK00719  81 MSPTVAARMAATLDRLSNGRLLINLVTGGDPAELAGDGLFLDHDERYEASAEFLRIWRRLLEGETVDFEGKHIQVKGAKL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048 163 FFPPVQQPRPPLYFGGSSDVAQDLAAEQVDLYLTWGEPPEQVKAKIEQVRAKAAALGRKIRFGIRLHVIVRETTHEAWQA 242
Cdd:PRK00719 161 LFPPVQQPYPPLYFGGSSDAAQELAAEQVDLYLTWGEPPAQVKEKIEQVRAKAAAHGRKVRFGIRLHVIVRETNEEAWQA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048 243 ADRLIVHLDDDTIAKAQAAFSKTDSVGQQRMAALHNGKRDKLEISPNLWAGVGLVRGGAGTALVGDGPTVAARINEYAAL 322
Cdd:PRK00719 241 AERLISHLDDETIARAQAAFARMDSVGQQRMAALHGGKRDNLEISPNLWAGVGLVRGGAGTALVGDPPTVAARIKEYAAL 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489126048 323 GIDSFVLSGYPHLEEAYRVGELLFPHLDVAIPEIPQPQRLQQQGEAVANEFIPRKVAQ 380
Cdd:PRK00719 321 GIDTFILSGYPHLEEAYRVAELLFPLLDVAIPEKPQPQPSGPFGEVVANDYLPKKAQS 378
alk_sulf_monoox TIGR03565
alkanesulfonate monooxygenase, FMNH(2)-dependent; Members of this protein family are ...
 4-349 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: 708.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048    4 NMFWFLPTHGDGHYLGTEEGSRPVDHGYLQQIAQTADRLGFTGVLIPTGRSCEDAWLVAASMIPVTQRLKFLVALRPSVT 83
Cdd:TIGR03565   1 NIFWFIPTHGDGRYLGTSEGGRAVDHGYLKQIAQAADRLGYTGVLLPTGRSCEDSWVTASSLAPLTERLKFLVAVRPGLM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048   84 SPTVAARQAATLDRLSNGRALFNLVTGSDPQELAGDGVFLDHTERYEASAEFTQVWRRLLQGETVDFNGKHIHVRGAKLF 163
Cdd:TIGR03565  81 SPTVAARMAATLDRLSGGRLLINVVTGGDPVELAGDGIFLDHDERYEATDEFLTVWRRLLAGETVDFDGKHIKVENAKLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048  164 FPPVQQPRPPLYFGGSSDVAQDLAAEQVDLYLTWGEPPEQVKAKIEQVRAKAAALGRKIRFGIRLHVIVRETTHEAWQAA 243
Cdd:TIGR03565 161 FPPVQQPYPPLYFGGSSDAAIELAAEHVDVYLTWGEPPAQVAEKIAKVRKRAAKRGRTVRFGIRLHVIVRETEEEAWAAA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048  244 DRLIVHLDDDTIAKAQAAFSKTDSVGQQRMAALHNGKRDKLEISPNLWAGVGLVRGGAGTALVGDGPTVAARINEYAALG 323
Cdd:TIGR03565 241 DRLISHLDDDTIARAQKAFARMDSVGQRRMAALHGGRRDKLEISPNLWAGVGLVRGGAGTALVGDPETVAARIREYQDLG 320

                         330       340
                  ....*....|....*....|....*.
gi 489126048  324 IDSFVLSGYPHLEEAYRVGELLFPHL 349
Cdd:TIGR03565 321 IDTFILSGYPHLEEAYRFAELVFPLL 346
Alkanesulfonate_monoxygenase cd01094
Alkanesulfonate monoxygenase is the monoxygenase of a two-component system that catalyzes the ...
 3-245 3.01e-119

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: 345.41  E-value: 3.01e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048   3 LNMFWFLPTHGDGHYLGTEEGSRPVDHGYLQQIAQTADRLGFTGVLIPTGRSCEDAWLVAASMIPVTQRLKFLVALRPSV 82
Cdd:cd01094    1 LEFGWFIPNVSGGWSLSTPPRGRPWDFEYNRQIAQAAEELGFDGALSPTGSSGPDGWTVAAALAAATERLKFLVAIRPGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048  83 TSPTVAARQAATLDRLSNGRALFNLVTGSDPQELAGDGVFLDHTERYEASAEFTQVWRRLLQGET-VDFNGKHIHVRGAK 161
Cdd:cd01094   81 IAPTVAARQAATLDHISGGRLGLNVVTGGDPAELRMDGDFLDHDERYARADEFLEVLRRLWTSDEpFDFEGKFYRFKNAF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048 162 LFFPPVQQPRPPLYFGGSSDVAQDLAAEQVDLYLTWGEPPEQVKAKIEQVRAKAAALGRKIRFGIRLHVIVRETTHEAWQ 241
Cdd:cd01094  161 LRPKPPQQPHPPIYFGGSSEAAIEFAARHADVYFTWGEPPAQVAEAIARVRAAAAAAGRDVRFGIRLHVIVRDTEEEAWA 240


                 ....
gi 489126048 242 AADR 245
Cdd:cd01094  241 YADR 244
Bac_luciferase pfam00296
Luciferase-like monooxygenase;
6-326 1.15e-73

Luciferase-like monooxygenase;


Pssm-ID: 425589 [Multi-domain]  Cd Length: 313  Bit Score: 231.48  E-value: 1.15e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048    6 FWFLPTHGDGHYLGTEEGSRpvdhgYLQQIAQTADRLGFTGVLIPTGRSC---EDAWLVAASMIPVTQRLKFLVALRPSV 82
Cdd:pfam00296   4 GVFLPTRNGGGLGAGSESLR-----YLVELARAAEELGFDGVWLAEHHGGpggPDPFVVLAALAAATSRIRLGTAVVPLP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048   83 T-SPTVAARQAATLDRLSNGRALFNLVTGSDPQELAGDGVflDHTERYEASAEFTQVWRRLLQGETVDFNGKHIHVRGAK 161
Cdd:pfam00296  79 TrHPAVLAEQAATLDHLSGGRFDLGLGTGGPAVEFRRFGV--DHDERYARLREFLEVLRRLWRGEPVDFEGEFFTLDGAF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048  162 LFFPPVQqpRPPLYFGGSSDVAQDLAAEQVDLYLTWG-EPPEQVKAKIEQVRAKAAALGR---KIRFGIRLHVIVRETTH 237
Cdd:pfam00296 157 LLPRPVQ--GIPVWVAASSPAMLELAARHADGLLLWGfAPPAAAAELIERVRAGAAEAGRdpaDIRVGASLTVIVADTEE 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048  238 EAWQAADRLIVHLDddtiakaqaaFSKTDSVGQQRMAALHngkRDKLEISPNLWAGVGLVRGGA---GTALVGDGPTVAA 314
Cdd:pfam00296 235 EARAEARALIAGLP----------FYRMDSEGAGRLAEAR---EIGEEYDAGDWAGAADAVPDElvrAFALVGTPEQVAE 301

                         330
                  ....*....|..
gi 489126048  315 RINEYAALGIDS 326
Cdd:pfam00296 302 RLAAYAEAGVDH 313
SsuD COG2141
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
 39-349 1.54e-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: 210.18  E-value: 1.54e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048  39 ADRLGFTGVLI-----PTGRSCEDAWLVAASMIPVTQRLKFLVA-LRPSVTSPTVAARQAATLDRLSNGRALFNLVTGSD 112
Cdd:COG2141    1 AERLGFDRVWVadhhfPPGGASPDPWVLLAALAAATSRIRLGTGvVVLPLRHPLVVAEQFATLDHLSGGRLDLGVGRGWG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048 113 PQELAGDGvfLDHTERYEASAEFTQVWRRLLQGETVDFNGKHIHVRGAKLFFPPVQQPRPPLYFGGSSDVAQDLAAEQVD 192
Cdd:COG2141   81 PDEFAAFG--LDHDERYERFEEALEVLRRLWTGEPVTFEGEFFTVEGARLVPRPVQGPHPPIWIAGSSPAGARLAARLGD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048 193 LYLTWGEPPEQVKAKIEQVRAKAAALGR---KIRFGIRLHVIVRETTHEAWQAADRlivhldddtiakAQAAFSKTDSVG 269
Cdd:COG2141  159 GVFTAGGTPEELAEAIAAYREAAAAAGRdpdDLRVSVGLHVIVAETDEEARERARP------------YLRALLALPRGR 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048 270 QQRMAAlhngkrDKLEISPNLWAGVglvrggaGTALVGDGPTVAARINEYA-ALGIDSFVLS-----GYPHLEEAYRVGE 343
Cdd:COG2141  227 PPEEAE------EGLTVREDLLELL-------GAALVGTPEQVAERLEELAeAAGVDEFLLQfpgldPEDRLRSLELFAE 293


                 ....*.
gi 489126048 344 LLFPHL 349
Cdd:COG2141  294 EVLPLL 299
F420_Rv1855c TIGR03560
probable F420-dependent oxidoreductase, Rv1855c family; Coenzyme F420 has a limited ...
 32-220 1.38e-24

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: 100.47  E-value: 1.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048   32 LQQIAQTADRLGFT-----------GVLIPTGRSCEDAWLVAASMIPVTQRLKFLvALRPSVT--SPTVAARQAATLDRL 98
Cdd:TIGR03560  15 LLAVARAAEDAGFDalfrsdhflqmPMVGPPEGPTLEAWTTLAGLARETSRIRLG-TLVTGVTyrHPGLLAKMVATVDVL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048   99 SNGRALFNLVTGSDPQELAGDGV-FLDHTERYEASAEFTQVWRRLLQGETVDFNGKHIHVRGAKLFFPPVQQPRPPLYFG 177
Cdd:TIGR03560  94 SGGRAELGLGAGWYEREHRAYGIpFPPLAERFERLEEALQIITGMWSGEGVTFDGRHYRLADAIALPKPLQRPHPPILIG 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 489126048  178 GSSD-VAQDLAAEQVDLYLTWGEPPEQVKAKIEQVRAKAAALGR 220
Cdd:TIGR03560 174 GGGEkRTLRLAARYADEFNLVFGPPDELAHKFEVLRAHCEAAGR 217
Nitrilotriacetate_monoxgenase cd01095
nitrilotriacetate monoxygenase oxidizes nitrilotriacetate utilizing reduced flavin ...
 3-220 2.61e-20

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: 90.84  E-value: 2.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048   3 LNMFWFLptHGDGHYLGT----EEGSRPVDHGYLQQIAQTADRLGF------TGVLIPTGRSCEDAW-----LVAASMIP 67
Cdd:cd01095    1 LHLGAFL--HGAGHHAAAwrhpAPPDASIDFDHYVRLARTAERAKFdavflaDGLAIRALSRPHPVArleplTLLAALAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048  68 VTQRLKFLVALRPSVTSPTVAARQAATLDRLSNGRALFNLVTGSDPQELA--GDGVFLDHTERYEASAEFTQVWRRL--- 142
Cdd:cd01095   79 VTERIGLVATASTTYNEPYHLARRFASLDHISGGRAGWNVVTSANPGEARnfGRDEHPEHDERYARAEEFVEVVKGLwds 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048 143 ------------------LQGETVDFNGKHIHVRGaKLFFPPVQQPRPPLYFGGSSDVAQDLAAEQVDLYLTWGEPPEQV 204
Cdd:cd01095  159 weddalvrdkasgrfadpAKVHPLDHVGDHFGVRG-PLNGPRSPQGRPVIVQAGSSEAGREFAARHAEAVFTAQQTLEEA 237

                        250
                 ....*....|....*.
gi 489126048 205 KAKIEQVRAKAAALGR 220
Cdd:cd01095  238 QAFYADVKARAAAAGR 253
PRK02271 PRK02271
methylenetetrahydromethanopterin reductase; Provisional
 80-220 5.62e-09

methylenetetrahydromethanopterin reductase; Provisional


Pssm-ID: 235022 [Multi-domain]  Cd Length: 325  Bit Score: 56.87  E-value: 5.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048  80 PSVTSPTVAARQAATLDRLSNGRALFNLVTGsDPQELAGDGvfLDHTERYEASAEFTQVWRRLLQGETVDFNGKhIHVRG 159
Cdd:PRK02271  65 PYTRHPAITASAIATLDEISGGRAVLGIGPG-DKATLDALG--IEWEKPLRTVKEAIEVIRKLWAGERVEHDGT-FKAAG 140

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489126048 160 AKLFFPPVQQpRPPLYFGGSSDVAQDLAAEQVDLYLTWGEPPEQVKAKIEQVRAKAAALGR 220
Cdd:PRK02271 141 AKLNVKPVQG-EIPIYMGAQGPKMLELAGEIADGVLINASNPKDFEWAVPLIKKGAEEAGK 200
Tetrahydromethanopterin_reductase cd01097
N5,N10-methylenetetrahydromethanopterin reductase (Mer) catalyzes the reduction of N5, ...
 93-220 9.52e-08

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: 52.01  E-value: 9.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126048  93 ATLDRLSNGRALFNLVTGsDPQelAGDGVFLDHTERYEASAEFTQVWRRLLQG-ETVDFNGKHIHVRGAKLFFPPVQQPR 171
Cdd:cd01097   34 VSLDALSGGRFILGLGAG-GPE--VEEGWGGPWFKPPARRREELEAIRRLRALrRGDPVGEDGRFLGTRSAALPPPPRGE 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 489126048 172 PPLYFGGSSDVAQDLAAEQVDLYLTWGEPPEQVKAKIEQVRAKAAALGR 220
Cdd:cd01097  111 IPIYIGALGPKMLELAGEIADGWLPVAAPPELYEAALPAVREGAAAAGR 159
Flavin_utilizing_monoxygenases cd00347
Flavin-utilizing monoxygenases
 173-220 8.88e-06

Flavin-utilizing monoxygenases


Pssm-ID: 238209 [Multi-domain]  Cd Length: 90  Bit Score: 43.89  E-value: 8.88e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 489126048 173 PLYFGGSSDVAQDLAAEQVDLYLTWG-EPPEQVKAKIEQVRAKAAALGR 220
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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