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Conserved domains on  [gi|2502261254|ref|WP_281664222|]
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LLM class flavin-dependent oxidoreductase [Paraburkholderia fungorum]

Protein Classification

LLM class flavin-dependent oxidoreductase( domain architecture ID 10099592)

LLM (luciferase-like monooxygenase) class flavin-dependent oxidoreductase transfers one oxygen atom of an oxygen molecule to a substrate while reducing the other oxygen atom to water; similar to Niallia circulans 4-(gamma-L-glutamylamino)butanoyl-[BtrI acyl-carrier protein] monooxygenase BtrO, a monooxygenase component of a two-component system involved in the biosynthesis of the side chain of the aminoglycoside antibiotics in the biosynthetic pathway of butirosin

CATH:  3.20.20.30
EC:  1.-.-.-
Gene Ontology:  GO:0010181|GO:0016491
PubMed:  33460580|24361254
SCOP:  3000585

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Alkanesulfonate_monoxygenase cd01094
Alkanesulfonate monoxygenase is the monoxygenase of a two-component system that catalyzes the ...
46-312 6.47e-81

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: 248.73  E-value: 6.47e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254  46 LLLGLFLPIQAGGWSASTLARSTDWSFDYNLALVQKAEALGFDlvfalSQWLPKGGYGGvfngealDSFMSLAAMTARTE 125
Cdd:cd01094     1 LEFGWFIPNVSGGWSLSTPPRGRPWDFEYNRQIAQAAEELGFD-----GALSPTGSSGP-------DGWTVAAALAAATE 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 126 RIILVATSHVlyGPWHPLHFAKFTATLDHISKGRWGINVVTGHRAIEHEMFGWHrIEHDRRYELAAEFLDAVQQLWAQPE 205
Cdd:cd01094    69 RLKFLVAIRP--GLIAPTVAARQAATLDHISGGRLGLNVVTGGDPAELRMDGDF-LDHDERYARADEFLEVLRRLWTSDE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 206 NFSFAPELssWKLDKAFVTPKPRYGRPLLVNATG-SDAGIDFAARYSDIVFITSPAGSEIEGALaalpahtARVKAAAAQ 284
Cdd:cd01094   146 PFDFEGKF--YRFKNAFLRPKPPQQPHPPIYFGGsSEAAIEFAARHADVYFTWGEPPAQVAEAI-------ARVRAAAAA 216
                         250       260
                  ....*....|....*....|....*...
gi 2502261254 285 HGRKIRTLINPMVICRETEAEALAYRDA 312
Cdd:cd01094   217 AGRDVRFGIRLHVIVRDTEEEAWAYADR 244
 
Name Accession Description Interval E-value
Alkanesulfonate_monoxygenase cd01094
Alkanesulfonate monoxygenase is the monoxygenase of a two-component system that catalyzes the ...
46-312 6.47e-81

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: 248.73  E-value: 6.47e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254  46 LLLGLFLPIQAGGWSASTLARSTDWSFDYNLALVQKAEALGFDlvfalSQWLPKGGYGGvfngealDSFMSLAAMTARTE 125
Cdd:cd01094     1 LEFGWFIPNVSGGWSLSTPPRGRPWDFEYNRQIAQAAEELGFD-----GALSPTGSSGP-------DGWTVAAALAAATE 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 126 RIILVATSHVlyGPWHPLHFAKFTATLDHISKGRWGINVVTGHRAIEHEMFGWHrIEHDRRYELAAEFLDAVQQLWAQPE 205
Cdd:cd01094    69 RLKFLVAIRP--GLIAPTVAARQAATLDHISGGRLGLNVVTGGDPAELRMDGDF-LDHDERYARADEFLEVLRRLWTSDE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 206 NFSFAPELssWKLDKAFVTPKPRYGRPLLVNATG-SDAGIDFAARYSDIVFITSPAGSEIEGALaalpahtARVKAAAAQ 284
Cdd:cd01094   146 PFDFEGKF--YRFKNAFLRPKPPQQPHPPIYFGGsSEAAIEFAARHADVYFTWGEPPAQVAEAI-------ARVRAAAAA 216
                         250       260
                  ....*....|....*....|....*...
gi 2502261254 285 HGRKIRTLINPMVICRETEAEALAYRDA 312
Cdd:cd01094   217 AGRDVRFGIRLHVIVRDTEEEAWAYADR 244
Bac_luciferase pfam00296
Luciferase-like monooxygenase;
46-374 5.57e-66

Luciferase-like monooxygenase;


Pssm-ID: 425589 [Multi-domain]  Cd Length: 313  Bit Score: 212.61  E-value: 5.57e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254  46 LLLGLFLPIQAGGWSASTLarstdWSFDYNLALVQKAEALGFDLVFALSQWLPKGGyggvfngeaLDSFMSLAAMTARTE 125
Cdd:pfam00296   1 MEFGVFLPTRNGGGLGAGS-----ESLRYLVELARAAEELGFDGVWLAEHHGGPGG---------PDPFVVLAALAAATS 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 126 RIILVATSHVLYGpWHPLHFAKFTATLDHISKGRWGINVVTGHRAIEHEMFGwhrIEHDRRYELAAEFLDAVQQLWAQPE 205
Cdd:pfam00296  67 RIRLGTAVVPLPT-RHPAVLAEQAATLDHLSGGRFDLGLGTGGPAVEFRRFG---VDHDERYARLREFLEVLRRLWRGEP 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 206 NfSFAPELssWKLDKAFVTPKPRYGRPLLVnATGSDAGIDFAARYSDIVFITSPAgseiegALAALPAHTARVKAAAAQH 285
Cdd:pfam00296 143 V-DFEGEF--FTLDGAFLLPRPVQGIPVWV-AASSPAMLELAARHADGLLLWGFA------PPAAAAELIERVRAGAAEA 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 286 GR---KIRTLINPMVICRETEAEALAYRDAIVA-------------HGDEGSFHRFESDAHAWRGNAEQRNQAASRAvgg 349
Cdd:pfam00296 213 GRdpaDIRVGASLTVIVADTEEEARAEARALIAglpfyrmdsegagRLAEAREIGEEYDAGDWAGAADAVPDELVRA--- 289
                         330       340
                  ....*....|....*....|....*
gi 2502261254 350 nISIVGSPQQIADYIVRLHQAGVDG 374
Cdd:pfam00296 290 -FALVGTPEQVAERLAAYAEAGVDH 313
SsuD COG2141
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
82-399 5.05e-54

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: 181.29  E-value: 5.05e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254  82 AEALGFDLVFALSQWLPKGGYggvfngeALDSFMSLAAMTARTERIILVATSHVLyGPWHPLHFAKFTATLDHISKGRWG 161
Cdd:COG2141     1 AERLGFDRVWVADHHFPPGGA-------SPDPWVLLAALAAATSRIRLGTGVVVL-PLRHPLVVAEQFATLDHLSGGRLD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 162 INVVTGHRAIEHEMFGwhrIEHDRRYELAAEFLDAVQQLWAQpENFSFAPELssWKLDKAFVTPKPRYG-RPLLVNATGS 240
Cdd:COG2141    73 LGVGRGWGPDEFAAFG---LDHDERYERFEEALEVLRRLWTG-EPVTFEGEF--FTVEGARLVPRPVQGpHPPIWIAGSS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 241 DAGIDFAARYSDIVFITSPagseiegALAALPAHTARVKAAAAQHGR---KIRTLINPMVICRETEAEALA-YRDAIVAH 316
Cdd:COG2141   147 PAGARLAARLGDGVFTAGG-------TPEELAEAIAAYREAAAAAGRdpdDLRVSVGLHVIVAETDEEARErARPYLRAL 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 317 GDEGSFHRFESDAHAWRGNAEQRNQAASravggniSIVGSPQQIADYIVRLHQ-AGVDGVQLSFFDFQP-----GLDFFG 390
Cdd:COG2141   220 LALPRGRPPEEAEEGLTVREDLLELLGA-------ALVGTPEQVAERLEELAEaAGVDEFLLQFPGLDPedrlrSLELFA 292

                  ....*....
gi 2502261254 391 ERVLPLLRE 399
Cdd:COG2141   293 EEVLPLLRR 301
FMN_nitrolo TIGR03860
FMN-dependent oxidoreductase, nitrilotriacetate monooxygenase family; This model represents a ...
48-402 3.40e-49

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: 171.92  E-value: 3.40e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254  48 LGLFL---PIQAGGWsASTLARSTDW-SFDYNLALVQKAEALGFDLVF------ALSQWLPKGGYGGVFNgeALDSFMSL 117
Cdd:TIGR03860   1 LGAFLngvGHHPGLW-RHPRARADAYlDLDYWTELARTAERGKFDALFfadvlgVYDVPDAALRRAAQLP--RFEPLTLL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 118 AAMTARTERIILVATSHVLYgpWHPLHFAKFTATLDHISKGRWGINVVTGHRAIEHEMFGW-HRIEHDRRYELAAEFLDA 196
Cdd:TIGR03860  78 SALAAVTEHIGLGATASTTY--EEPYNLARRFASLDHLSGGRAGWNIVTSYLDSAARNFGLdEHPPHDERYERAEEFVDV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 197 VQQLWaqpenfsfapelSSWKLDkAFV-------------------------------TPKPRYGRPLLVNATGSDAGID 245
Cdd:TIGR03860 156 VYKLW------------DSWEDD-AFVrdkasgvfadpakvhpinhkgkhfsvrgplnIPRSPQGTPVLFQAGSSERGRE 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 246 FAARYSDIVFITSPagseiegALAALPAHTARVKAAAAQHGR-----KIRTLInpMVICRETEAEALA----YRDAIVAH 316
Cdd:TIGR03860 223 FAARHAEAVFTAQP-------TLEDAQAFYADIKARAAAAGRdpddvKILPGI--TPIVGRTEAEARAkyaeLQDLISPE 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 317 G-----------------------DEGSFHRFESDAHAWRGNAEQRN----QAASRAV--GGNISIVGSPQQIADYIVRL 367
Cdd:TIGR03860 294 GglallsgwtgidlsqydldaplpDLPTEAGQKSRFDLILELARRENltlrQLALRLAggRGHPVFVGTPEQVADQLEEW 373
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 2502261254 368 HQAG-VDGVQLSFFDFQPGLDFFGERVLPLLREAGL 402
Cdd:TIGR03860 374 FEEGaADGFNLMPPVLPGGLEDFVDLVVPELQRRGL 409
PRK00719 PRK00719
alkanesulfonate monooxygenase; Provisional
101-397 6.54e-23

alkanesulfonate monooxygenase; Provisional


Pssm-ID: 234821 [Multi-domain]  Cd Length: 378  Bit Score: 99.26  E-value: 6.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 101 GYGGVF--NGEAL-DSFMSLAAMTARTERI-ILVAtshVLYGPWHPLHFAKFTATLDHISKGRWGINVVTGHRAIEHEMF 176
Cdd:PRK00719   41 GYTGVLipTGRSCeDAWLVAASLIPVTQRLkFLVA---LRPGLMSPTVAARMAATLDRLSNGRLLINLVTGGDPAELAGD 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 177 GWHrIEHDRRYELAAEFLDAVQQLwAQPENFSFAPELSSWKLDKAFVTPKPRyGRPLLVNATGSDAGIDFAARYSDiVFI 256
Cdd:PRK00719  118 GLF-LDHDERYEASAEFLRIWRRL-LEGETVDFEGKHIQVKGAKLLFPPVQQ-PYPPLYFGGSSDAAQELAAEQVD-LYL 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 257 T--SPAgseiegalAALPAHTARVKAAAAQHGRKIRTLINPMVICRETEAEALAYRDAIVAHGDE-------GSFHRFES 327
Cdd:PRK00719  194 TwgEPP--------AQVKEKIEQVRAKAAAHGRKVRFGIRLHVIVRETNEEAWQAAERLISHLDDetiaraqAAFARMDS 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 328 DAhawrgnaeQRNQAA----SRAV----------------GGNISIVGSPQQIADYIVRLHQAGVDGVQLSFFdfqPGLD 387
Cdd:PRK00719  266 VG--------QQRMAAlhggKRDNleispnlwagvglvrgGAGTALVGDPPTVAARIKEYAALGIDTFILSGY---PHLE 334
                         330
                  ....*....|...
gi 2502261254 388 ---FFGERVLPLL 397
Cdd:PRK00719  335 eayRVAELLFPLL 347
 
Name Accession Description Interval E-value
Alkanesulfonate_monoxygenase cd01094
Alkanesulfonate monoxygenase is the monoxygenase of a two-component system that catalyzes the ...
46-312 6.47e-81

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: 248.73  E-value: 6.47e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254  46 LLLGLFLPIQAGGWSASTLARSTDWSFDYNLALVQKAEALGFDlvfalSQWLPKGGYGGvfngealDSFMSLAAMTARTE 125
Cdd:cd01094     1 LEFGWFIPNVSGGWSLSTPPRGRPWDFEYNRQIAQAAEELGFD-----GALSPTGSSGP-------DGWTVAAALAAATE 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 126 RIILVATSHVlyGPWHPLHFAKFTATLDHISKGRWGINVVTGHRAIEHEMFGWHrIEHDRRYELAAEFLDAVQQLWAQPE 205
Cdd:cd01094    69 RLKFLVAIRP--GLIAPTVAARQAATLDHISGGRLGLNVVTGGDPAELRMDGDF-LDHDERYARADEFLEVLRRLWTSDE 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 206 NFSFAPELssWKLDKAFVTPKPRYGRPLLVNATG-SDAGIDFAARYSDIVFITSPAGSEIEGALaalpahtARVKAAAAQ 284
Cdd:cd01094   146 PFDFEGKF--YRFKNAFLRPKPPQQPHPPIYFGGsSEAAIEFAARHADVYFTWGEPPAQVAEAI-------ARVRAAAAA 216
                         250       260
                  ....*....|....*....|....*...
gi 2502261254 285 HGRKIRTLINPMVICRETEAEALAYRDA 312
Cdd:cd01094   217 AGRDVRFGIRLHVIVRDTEEEAWAYADR 244
Bac_luciferase pfam00296
Luciferase-like monooxygenase;
46-374 5.57e-66

Luciferase-like monooxygenase;


Pssm-ID: 425589 [Multi-domain]  Cd Length: 313  Bit Score: 212.61  E-value: 5.57e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254  46 LLLGLFLPIQAGGWSASTLarstdWSFDYNLALVQKAEALGFDLVFALSQWLPKGGyggvfngeaLDSFMSLAAMTARTE 125
Cdd:pfam00296   1 MEFGVFLPTRNGGGLGAGS-----ESLRYLVELARAAEELGFDGVWLAEHHGGPGG---------PDPFVVLAALAAATS 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 126 RIILVATSHVLYGpWHPLHFAKFTATLDHISKGRWGINVVTGHRAIEHEMFGwhrIEHDRRYELAAEFLDAVQQLWAQPE 205
Cdd:pfam00296  67 RIRLGTAVVPLPT-RHPAVLAEQAATLDHLSGGRFDLGLGTGGPAVEFRRFG---VDHDERYARLREFLEVLRRLWRGEP 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 206 NfSFAPELssWKLDKAFVTPKPRYGRPLLVnATGSDAGIDFAARYSDIVFITSPAgseiegALAALPAHTARVKAAAAQH 285
Cdd:pfam00296 143 V-DFEGEF--FTLDGAFLLPRPVQGIPVWV-AASSPAMLELAARHADGLLLWGFA------PPAAAAELIERVRAGAAEA 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 286 GR---KIRTLINPMVICRETEAEALAYRDAIVA-------------HGDEGSFHRFESDAHAWRGNAEQRNQAASRAvgg 349
Cdd:pfam00296 213 GRdpaDIRVGASLTVIVADTEEEARAEARALIAglpfyrmdsegagRLAEAREIGEEYDAGDWAGAADAVPDELVRA--- 289
                         330       340
                  ....*....|....*....|....*
gi 2502261254 350 nISIVGSPQQIADYIVRLHQAGVDG 374
Cdd:pfam00296 290 -FALVGTPEQVAERLAAYAEAGVDH 313
SsuD COG2141
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
82-399 5.05e-54

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: 181.29  E-value: 5.05e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254  82 AEALGFDLVFALSQWLPKGGYggvfngeALDSFMSLAAMTARTERIILVATSHVLyGPWHPLHFAKFTATLDHISKGRWG 161
Cdd:COG2141     1 AERLGFDRVWVADHHFPPGGA-------SPDPWVLLAALAAATSRIRLGTGVVVL-PLRHPLVVAEQFATLDHLSGGRLD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 162 INVVTGHRAIEHEMFGwhrIEHDRRYELAAEFLDAVQQLWAQpENFSFAPELssWKLDKAFVTPKPRYG-RPLLVNATGS 240
Cdd:COG2141    73 LGVGRGWGPDEFAAFG---LDHDERYERFEEALEVLRRLWTG-EPVTFEGEF--FTVEGARLVPRPVQGpHPPIWIAGSS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 241 DAGIDFAARYSDIVFITSPagseiegALAALPAHTARVKAAAAQHGR---KIRTLINPMVICRETEAEALA-YRDAIVAH 316
Cdd:COG2141   147 PAGARLAARLGDGVFTAGG-------TPEELAEAIAAYREAAAAAGRdpdDLRVSVGLHVIVAETDEEARErARPYLRAL 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 317 GDEGSFHRFESDAHAWRGNAEQRNQAASravggniSIVGSPQQIADYIVRLHQ-AGVDGVQLSFFDFQP-----GLDFFG 390
Cdd:COG2141   220 LALPRGRPPEEAEEGLTVREDLLELLGA-------ALVGTPEQVAERLEELAEaAGVDEFLLQFPGLDPedrlrSLELFA 292

                  ....*....
gi 2502261254 391 ERVLPLLRE 399
Cdd:COG2141   293 EEVLPLLRR 301
FMN_nitrolo TIGR03860
FMN-dependent oxidoreductase, nitrilotriacetate monooxygenase family; This model represents a ...
48-402 3.40e-49

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: 171.92  E-value: 3.40e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254  48 LGLFL---PIQAGGWsASTLARSTDW-SFDYNLALVQKAEALGFDLVF------ALSQWLPKGGYGGVFNgeALDSFMSL 117
Cdd:TIGR03860   1 LGAFLngvGHHPGLW-RHPRARADAYlDLDYWTELARTAERGKFDALFfadvlgVYDVPDAALRRAAQLP--RFEPLTLL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 118 AAMTARTERIILVATSHVLYgpWHPLHFAKFTATLDHISKGRWGINVVTGHRAIEHEMFGW-HRIEHDRRYELAAEFLDA 196
Cdd:TIGR03860  78 SALAAVTEHIGLGATASTTY--EEPYNLARRFASLDHLSGGRAGWNIVTSYLDSAARNFGLdEHPPHDERYERAEEFVDV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 197 VQQLWaqpenfsfapelSSWKLDkAFV-------------------------------TPKPRYGRPLLVNATGSDAGID 245
Cdd:TIGR03860 156 VYKLW------------DSWEDD-AFVrdkasgvfadpakvhpinhkgkhfsvrgplnIPRSPQGTPVLFQAGSSERGRE 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 246 FAARYSDIVFITSPagseiegALAALPAHTARVKAAAAQHGR-----KIRTLInpMVICRETEAEALA----YRDAIVAH 316
Cdd:TIGR03860 223 FAARHAEAVFTAQP-------TLEDAQAFYADIKARAAAAGRdpddvKILPGI--TPIVGRTEAEARAkyaeLQDLISPE 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 317 G-----------------------DEGSFHRFESDAHAWRGNAEQRN----QAASRAV--GGNISIVGSPQQIADYIVRL 367
Cdd:TIGR03860 294 GglallsgwtgidlsqydldaplpDLPTEAGQKSRFDLILELARRENltlrQLALRLAggRGHPVFVGTPEQVADQLEEW 373
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 2502261254 368 HQAG-VDGVQLSFFDFQPGLDFFGERVLPLLREAGL 402
Cdd:TIGR03860 374 FEEGaADGFNLMPPVLPGGLEDFVDLVVPELQRRGL 409
Nitrilotriacetate_monoxgenase cd01095
nitrilotriacetate monoxygenase oxidizes nitrilotriacetate utilizing reduced flavin ...
48-403 5.35e-40

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: 145.93  E-value: 5.35e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254  48 LGLFLPI-QAGGWSASTLARSTDW-SFDYNLALVQKAEALGFDLVF-ALSQWLPKGGYGGVFNGeaLDSFMSLAAMTART 124
Cdd:cd01095     3 LGAFLHGaGHHAAAWRHPAPPDASiDFDHYVRLARTAERAKFDAVFlADGLAIRALSRPHPVAR--LEPLTLLAALAAVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 125 ERIILVATSHVLYgpWHPLHFAKFTATLDHISKGRWGINVVTGHRAIEHEMFGWHR-IEHDRRYELAAEFLDAVQQLWAq 203
Cdd:cd01095    81 ERIGLVATASTTY--NEPYHLARRFASLDHISGGRAGWNVVTSANPGEARNFGRDEhPEHDERYARAEEFVEVVKGLWD- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 204 penfsfapelsSWK-----LDKA---FVTPK----------------------PRYGRPLLVNATGSDAGIDFAARYSDI 253
Cdd:cd01095   158 -----------SWEddalvRDKAsgrFADPAkvhpldhvgdhfgvrgplngprSPQGRPVIVQAGSSEAGREFAARHAEA 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 254 VFITSPAgseIEGALAALpahtARVKAAAAQHGRkirtLINPmvicreteAEALAYRDAIvaHGDEGSFHRFESDAH--A 331
Cdd:cd01095   227 VFTAQQT---LEEAQAFY----ADVKARAAAAGR----LDPP--------PPDLPDLGSR--LSASRLLLADLLARGglH 285
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2502261254 332 WRGNAEQRNQAASRAVGGNISIVGSPQQIADYIVRLHQAG-VDGVQLSFFDFQPGLDFFGERVLPLLREAGLR 403
Cdd:cd01095   286 RREVGTAREVADRLERAAGGGTVVGPEQIADELEEWFEAGaADGFNIMPPYLPGGLDDFVDLVVPELQRRGLF 358
PRK00719 PRK00719
alkanesulfonate monooxygenase; Provisional
101-397 6.54e-23

alkanesulfonate monooxygenase; Provisional


Pssm-ID: 234821 [Multi-domain]  Cd Length: 378  Bit Score: 99.26  E-value: 6.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 101 GYGGVF--NGEAL-DSFMSLAAMTARTERI-ILVAtshVLYGPWHPLHFAKFTATLDHISKGRWGINVVTGHRAIEHEMF 176
Cdd:PRK00719   41 GYTGVLipTGRSCeDAWLVAASLIPVTQRLkFLVA---LRPGLMSPTVAARMAATLDRLSNGRLLINLVTGGDPAELAGD 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 177 GWHrIEHDRRYELAAEFLDAVQQLwAQPENFSFAPELSSWKLDKAFVTPKPRyGRPLLVNATGSDAGIDFAARYSDiVFI 256
Cdd:PRK00719  118 GLF-LDHDERYEASAEFLRIWRRL-LEGETVDFEGKHIQVKGAKLLFPPVQQ-PYPPLYFGGSSDAAQELAAEQVD-LYL 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 257 T--SPAgseiegalAALPAHTARVKAAAAQHGRKIRTLINPMVICRETEAEALAYRDAIVAHGDE-------GSFHRFES 327
Cdd:PRK00719  194 TwgEPP--------AQVKEKIEQVRAKAAAHGRKVRFGIRLHVIVRETNEEAWQAAERLISHLDDetiaraqAAFARMDS 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254 328 DAhawrgnaeQRNQAA----SRAV----------------GGNISIVGSPQQIADYIVRLHQAGVDGVQLSFFdfqPGLD 387
Cdd:PRK00719  266 VG--------QQRMAAlhggKRDNleispnlwagvglvrgGAGTALVGDPPTVAARIKEYAALGIDTFILSGY---PHLE 334
                         330
                  ....*....|...
gi 2502261254 388 ---FFGERVLPLL 397
Cdd:PRK00719  335 eayRVAELLFPLL 347
PRK02271 PRK02271
methylenetetrahydromethanopterin reductase; Provisional
78-159 2.68e-03

methylenetetrahydromethanopterin reductase; Provisional


Pssm-ID: 235022 [Multi-domain]  Cd Length: 325  Bit Score: 39.54  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502261254  78 LVQKAEALGFDLVFALSQwlpkggyggvFNGEalDSFMSLAAMTARTERIIL---VATSHVLygpwHPLHFAKFTATLDH 154
Cdd:PRK02271   19 LAKLAEDNGFDYAWITDH----------YNNR--DVYMTLAAIAAATDTIKLgpgVTNPYTR----HPAITASAIATLDE 82

                  ....*
gi 2502261254 155 ISKGR 159
Cdd:PRK02271   83 ISGGR 87
 
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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