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Conserved domains on  [gi|471179932|gb|AGI04990|]
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LuxA [Promoter capture vector pTn5.7luxG6]

Protein Classification

alkanal monooxygenase( domain architecture ID 10099650)

alkanal monooxygenase alpha (LuxA) and beta (LuxB) chains are required for the light-emitting reaction in luminous bacteria

CATH:  3.20.20.30
EC:  1.14.14.3
Gene Ontology:  GO:0010181|GO:0047646|GO:0008218
SCOP:  3000585

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Alkanal_monooxygenase cd01096
Alkanal monooxygenase are flavin monoxygenases. Molecular oxygen is activated by reaction with ...
 1-343 2.98e-175

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: 489.20  E-value: 2.98e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932   1 MKFGNFLLTYQPPQFSQTEVMKRLVKLGRISEECGFDTVWLLEHHFTEFGLLGNPYVAAAYLLGATKKLNVGTAAIVLPT 80
Cdd:cd01096    1 MKFGLFFLNFQPPGESSEEVLDRMVDTGVLVDKLNFDTALVLEHHFSENGIVGAPLTAAAFLLGLTERLNVGSLNQVITT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932  81 AHPVRQLEDVNLLDQMSKGRFRFGICRGLYNKDFRVFGTDMNNSRALAECWYGLIKNGMTEGYMEADNEHIKFHKVKVNP 160
Cdd:cd01096   81 HHPVRIAEEALLLDQMSKGRFILGFSDCLYDKDMRFFGRPMESQRQLFEACYEIINDALTTGYCHPDNDFYNFPKISVNP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932 161 AAYSRGGAPVYVVAESASTTEWAAQFGLPMILSWIINTNEKKAQLELYNEVAQEYGHDIHNIDHCLSYITSVDHDSIKAK 240
Cdd:cd01096  161 HAYSKGGPPQYVTAESAETVEWAAKKGLPLVLSWIDSLAEKKAYAELYLEVAKEGGDDISNIDHQLTLIVNVNEDGEKAQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932 241 EICRKFLGHWYDSYVNATtifddsdqtrgydfnkgqwrdfvlkghkDTNRRIDYSYEINPVGTPQECIDIIQKDIDATGI 320
Cdd:cd01096  241 DECREFLENYYDEYYPAT----------------------------NTERKIDESIEENAVGTPEECIEIIQLAIEATGI 292

                        330       340
                 ....*....|....*....|...
gi 471179932 321 SNICCGFEANGTVDEIIASMKLF 343
Cdd:cd01096  293 KNILLSFESMGSEDEIIASINMF 315
 
Name Accession Description Interval E-value
Alkanal_monooxygenase cd01096
Alkanal monooxygenase are flavin monoxygenases. Molecular oxygen is activated by reaction with ...
 1-343 2.98e-175

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: 489.20  E-value: 2.98e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932   1 MKFGNFLLTYQPPQFSQTEVMKRLVKLGRISEECGFDTVWLLEHHFTEFGLLGNPYVAAAYLLGATKKLNVGTAAIVLPT 80
Cdd:cd01096    1 MKFGLFFLNFQPPGESSEEVLDRMVDTGVLVDKLNFDTALVLEHHFSENGIVGAPLTAAAFLLGLTERLNVGSLNQVITT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932  81 AHPVRQLEDVNLLDQMSKGRFRFGICRGLYNKDFRVFGTDMNNSRALAECWYGLIKNGMTEGYMEADNEHIKFHKVKVNP 160
Cdd:cd01096   81 HHPVRIAEEALLLDQMSKGRFILGFSDCLYDKDMRFFGRPMESQRQLFEACYEIINDALTTGYCHPDNDFYNFPKISVNP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932 161 AAYSRGGAPVYVVAESASTTEWAAQFGLPMILSWIINTNEKKAQLELYNEVAQEYGHDIHNIDHCLSYITSVDHDSIKAK 240
Cdd:cd01096  161 HAYSKGGPPQYVTAESAETVEWAAKKGLPLVLSWIDSLAEKKAYAELYLEVAKEGGDDISNIDHQLTLIVNVNEDGEKAQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932 241 EICRKFLGHWYDSYVNATtifddsdqtrgydfnkgqwrdfvlkghkDTNRRIDYSYEINPVGTPQECIDIIQKDIDATGI 320
Cdd:cd01096  241 DECREFLENYYDEYYPAT----------------------------NTERKIDESIEENAVGTPEECIEIIQLAIEATGI 292

                        330       340
                 ....*....|....*....|...
gi 471179932 321 SNICCGFEANGTVDEIIASMKLF 343
Cdd:cd01096  293 KNILLSFESMGSEDEIIASINMF 315
Bac_luciferase pfam00296
Luciferase-like monooxygenase;
1-309 8.89e-52

Luciferase-like monooxygenase;


Pssm-ID: 425589 [Multi-domain]  Cd Length: 313  Bit Score: 174.47  E-value: 8.89e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932    1 MKFGNFLLTYQPPQF-SQTEVMKRLVKLGRISEECGFDTVWLLEHHFTEFGLlgNPYVAAAYLLGATKKLNVGTAAIVLP 79
Cdd:pfam00296   1 MEFGVFLPTRNGGGLgAGSESLRYLVELARAAEELGFDGVWLAEHHGGPGGP--DPFVVLAALAAATSRIRLGTAVVPLP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932   80 TAHPVRQLEDVNLLDQMSKGRFRFGICRGLYNKDFRVFGTDMNNSRALAECWYGLIKNGMTEGYMEADNEHIKFHKVKVN 159
Cdd:pfam00296  79 TRHPAVLAEQAATLDHLSGGRFDLGLGTGGPAVEFRRFGVDHDERYARLREFLEVLRRLWRGEPVDFEGEFFTLDGAFLL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932  160 PAaySRGGAPVYVVAESASTTEWAAQFGLPMILSWIINTNEKKAQLELYNEVAQEYGHDIHNIDHCLSYITSVDHDSIKA 239
Cdd:pfam00296 159 PR--PVQGIPVWVAASSPAMLELAARHADGLLLWGFAPPAAAAELIERVRAGAAEAGRDPADIRVGASLTVIVADTEEEA 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 471179932  240 KEICRKFLGhWYDSY--VNATTIFDDSDQTRGYDFNKGQWRdfvlkghKDTNRRIDYSYEIN-PVGTPQECID 309
Cdd:pfam00296 237 RAEARALIA-GLPFYrmDSEGAGRLAEAREIGEEYDAGDWA-------GAADAVPDELVRAFaLVGTPEQVAE 301
SsuD COG2141
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
 32-353 7.43e-50

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: 168.96  E-value: 7.43e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932  32 EECGFDTVWLLEHHFTEFGLLGNPYVAAAYLLGATKKLNVGTAAIVLPTAHPVRQLEDVNLLDQMSKGRFRFGICRGLYN 111
Cdd:COG2141    2 ERLGFDRVWVADHHFPPGGASPDPWVLLAALAAATSRIRLGTGVVVLPLRHPLVVAEQFATLDHLSGGRLDLGVGRGWGP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932 112 KDFRVFGTDMNNSRALAECWYGLIKNGMTEGYMEADNEHIKFHKVKVNPAAYSRGGAPVYVVAESASTTEWAAQFGLPmI 191
Cdd:COG2141   82 DEFAAFGLDHDERYERFEEALEVLRRLWTGEPVTFEGEFFTVEGARLVPRPVQGPHPPIWIAGSSPAGARLAARLGDG-V 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932 192 LSWIINTNEKKAQLELYNEVAQEYGHDIHNIDHCLSYITSVDHDSIKAKEICRkflgHWYDSYVNATTIFDDSDQTRGYD 271
Cdd:COG2141  161 FTAGGTPEELAEAIAAYREAAAAAGRDPDDLRVSVGLHVIVAETDEEARERAR----PYLRALLALPRGRPPEEAEEGLT 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932 272 FNKGQWrdfvlkghkdtnRRIDYSYeinpVGTPQECIDIIQKDIDATGISNICCGFeANGTVDEIIASMKLFQSDVMPFL 351
Cdd:COG2141  237 VREDLL------------ELLGAAL----VGTPEQVAERLEELAEAAGVDEFLLQF-PGLDPEDRLRSLELFAEEVLPLL 299


                 ..
gi 471179932 352 KE 353
Cdd:COG2141  300 RR 301
PRK02271 PRK02271
methylenetetrahydromethanopterin reductase; Provisional
 1-244 4.48e-08

methylenetetrahydromethanopterin reductase; Provisional


Pssm-ID: 235022 [Multi-domain]  Cd Length: 325  Bit Score: 54.17  E-value: 4.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932   1 MKFGNFLLTYQPPqfsqtevmKRLVKLGRISEECGFDTVWLLEHHFTEfgllgNPYVAAAYLLGATKKLNVGTaAIVLP- 79
Cdd:PRK02271   1 MKFGIEFVPNHPV--------KKIAYLAKLAEDNGFDYAWITDHYNNR-----DVYMTLAAIAAATDTIKLGP-GVTNPy 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932  80 TAHPVRQLEDVNLLDQMSKGRFRFGICRGlynkD---FRVFGTDMNNS-RALAECwYGLIKNGMTEGYMEADNEhIKFHK 155
Cdd:PRK02271  67 TRHPAITASAIATLDEISGGRAVLGIGPG----DkatLDALGIEWEKPlRTVKEA-IEVIRKLWAGERVEHDGT-FKAAG 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932 156 VKVNPAAYSrGGAPVYVVAESASTTEWAAQFG--------LPMILSWIIntnekkaqlELYNEVAQEYGHDIHNIDHCLS 227
Cdd:PRK02271 141 AKLNVKPVQ-GEIPIYMGAQGPKMLELAGEIAdgvlinasNPKDFEWAV---------PLIKKGAEEAGKSRGEFDVAAY 210

                        250
                 ....*....|....*..
gi 471179932 228 YITSVDHDSIKAKEICR 244
Cdd:PRK02271 211 ASVSVDKDEDKAREAAK 227
F420_MSMEG_2516 TIGR03621
probable F420-dependent oxidoreductase, MSMEG_2516 family; Coenzyme F420 is produced by ...
 19-114 6.38e-07

probable F420-dependent oxidoreductase, MSMEG_2516 family; Coenzyme F420 is produced by methanogenic archaea, a number of the Actinomycetes (including Mycobacterium tuberculosis), and rare members of other lineages. The resulting information-rich phylogenetic profile identifies candidate F420-dependent oxidoreductases within the family of luciferase-like enzymes (pfam00296), where the species range for the subfamily encompasses many F420-positive genomes without straying beyond. This family is uncharacterized, and named for member MSMEG_2516 from Mycobacterium smegmatis. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 200301 [Multi-domain]  Cd Length: 295  Bit Score: 50.45  E-value: 6.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932   19 EVMKRLVKLGRISEECGFDTVWLLEHhftefglLGN--PYVAAAYLLGATKKLNVGTAAIVLPTAHPVRQLEDVNLLDQM 96
Cdd:TIGR03621  11 ESARDLVDLARRAEDAGFDVLTVPDH-------LGApaPFAALTAAAAATTTLRLGTLVLNNDFRHPALLAREAATLDAL 83

                          90
                  ....*....|....*...
gi 471179932   97 SKGRFRFGICRGLYNKDF 114
Cdd:TIGR03621  84 SDGRLELGLGAGYVRSEF 101
 
Name Accession Description Interval E-value
Alkanal_monooxygenase cd01096
Alkanal monooxygenase are flavin monoxygenases. Molecular oxygen is activated by reaction with ...
 1-343 2.98e-175

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: 489.20  E-value: 2.98e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932   1 MKFGNFLLTYQPPQFSQTEVMKRLVKLGRISEECGFDTVWLLEHHFTEFGLLGNPYVAAAYLLGATKKLNVGTAAIVLPT 80
Cdd:cd01096    1 MKFGLFFLNFQPPGESSEEVLDRMVDTGVLVDKLNFDTALVLEHHFSENGIVGAPLTAAAFLLGLTERLNVGSLNQVITT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932  81 AHPVRQLEDVNLLDQMSKGRFRFGICRGLYNKDFRVFGTDMNNSRALAECWYGLIKNGMTEGYMEADNEHIKFHKVKVNP 160
Cdd:cd01096   81 HHPVRIAEEALLLDQMSKGRFILGFSDCLYDKDMRFFGRPMESQRQLFEACYEIINDALTTGYCHPDNDFYNFPKISVNP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932 161 AAYSRGGAPVYVVAESASTTEWAAQFGLPMILSWIINTNEKKAQLELYNEVAQEYGHDIHNIDHCLSYITSVDHDSIKAK 240
Cdd:cd01096  161 HAYSKGGPPQYVTAESAETVEWAAKKGLPLVLSWIDSLAEKKAYAELYLEVAKEGGDDISNIDHQLTLIVNVNEDGEKAQ 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932 241 EICRKFLGHWYDSYVNATtifddsdqtrgydfnkgqwrdfvlkghkDTNRRIDYSYEINPVGTPQECIDIIQKDIDATGI 320
Cdd:cd01096  241 DECREFLENYYDEYYPAT----------------------------NTERKIDESIEENAVGTPEECIEIIQLAIEATGI 292

                        330       340
                 ....*....|....*....|...
gi 471179932 321 SNICCGFEANGTVDEIIASMKLF 343
Cdd:cd01096  293 KNILLSFESMGSEDEIIASINMF 315
Bac_luciferase pfam00296
Luciferase-like monooxygenase;
1-309 8.89e-52

Luciferase-like monooxygenase;


Pssm-ID: 425589 [Multi-domain]  Cd Length: 313  Bit Score: 174.47  E-value: 8.89e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932    1 MKFGNFLLTYQPPQF-SQTEVMKRLVKLGRISEECGFDTVWLLEHHFTEFGLlgNPYVAAAYLLGATKKLNVGTAAIVLP 79
Cdd:pfam00296   1 MEFGVFLPTRNGGGLgAGSESLRYLVELARAAEELGFDGVWLAEHHGGPGGP--DPFVVLAALAAATSRIRLGTAVVPLP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932   80 TAHPVRQLEDVNLLDQMSKGRFRFGICRGLYNKDFRVFGTDMNNSRALAECWYGLIKNGMTEGYMEADNEHIKFHKVKVN 159
Cdd:pfam00296  79 TRHPAVLAEQAATLDHLSGGRFDLGLGTGGPAVEFRRFGVDHDERYARLREFLEVLRRLWRGEPVDFEGEFFTLDGAFLL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932  160 PAaySRGGAPVYVVAESASTTEWAAQFGLPMILSWIINTNEKKAQLELYNEVAQEYGHDIHNIDHCLSYITSVDHDSIKA 239
Cdd:pfam00296 159 PR--PVQGIPVWVAASSPAMLELAARHADGLLLWGFAPPAAAAELIERVRAGAAEAGRDPADIRVGASLTVIVADTEEEA 236

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 471179932  240 KEICRKFLGhWYDSY--VNATTIFDDSDQTRGYDFNKGQWRdfvlkghKDTNRRIDYSYEIN-PVGTPQECID 309
Cdd:pfam00296 237 RAEARALIA-GLPFYrmDSEGAGRLAEAREIGEEYDAGDWA-------GAADAVPDELVRAFaLVGTPEQVAE 301
SsuD COG2141
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
 32-353 7.43e-50

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: 168.96  E-value: 7.43e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932  32 EECGFDTVWLLEHHFTEFGLLGNPYVAAAYLLGATKKLNVGTAAIVLPTAHPVRQLEDVNLLDQMSKGRFRFGICRGLYN 111
Cdd:COG2141    2 ERLGFDRVWVADHHFPPGGASPDPWVLLAALAAATSRIRLGTGVVVLPLRHPLVVAEQFATLDHLSGGRLDLGVGRGWGP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932 112 KDFRVFGTDMNNSRALAECWYGLIKNGMTEGYMEADNEHIKFHKVKVNPAAYSRGGAPVYVVAESASTTEWAAQFGLPmI 191
Cdd:COG2141   82 DEFAAFGLDHDERYERFEEALEVLRRLWTGEPVTFEGEFFTVEGARLVPRPVQGPHPPIWIAGSSPAGARLAARLGDG-V 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932 192 LSWIINTNEKKAQLELYNEVAQEYGHDIHNIDHCLSYITSVDHDSIKAKEICRkflgHWYDSYVNATTIFDDSDQTRGYD 271
Cdd:COG2141  161 FTAGGTPEELAEAIAAYREAAAAAGRDPDDLRVSVGLHVIVAETDEEARERAR----PYLRALLALPRGRPPEEAEEGLT 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932 272 FNKGQWrdfvlkghkdtnRRIDYSYeinpVGTPQECIDIIQKDIDATGISNICCGFeANGTVDEIIASMKLFQSDVMPFL 351
Cdd:COG2141  237 VREDLL------------ELLGAAL----VGTPEQVAERLEELAEAAGVDEFLLQF-PGLDPEDRLRSLELFAEEVLPLL 299


                 ..
gi 471179932 352 KE 353
Cdd:COG2141  300 RR 301
PRK02271 PRK02271
methylenetetrahydromethanopterin reductase; Provisional
 1-244 4.48e-08

methylenetetrahydromethanopterin reductase; Provisional


Pssm-ID: 235022 [Multi-domain]  Cd Length: 325  Bit Score: 54.17  E-value: 4.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932   1 MKFGNFLLTYQPPqfsqtevmKRLVKLGRISEECGFDTVWLLEHHFTEfgllgNPYVAAAYLLGATKKLNVGTaAIVLP- 79
Cdd:PRK02271   1 MKFGIEFVPNHPV--------KKIAYLAKLAEDNGFDYAWITDHYNNR-----DVYMTLAAIAAATDTIKLGP-GVTNPy 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932  80 TAHPVRQLEDVNLLDQMSKGRFRFGICRGlynkD---FRVFGTDMNNS-RALAECwYGLIKNGMTEGYMEADNEhIKFHK 155
Cdd:PRK02271  67 TRHPAITASAIATLDEISGGRAVLGIGPG----DkatLDALGIEWEKPlRTVKEA-IEVIRKLWAGERVEHDGT-FKAAG 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932 156 VKVNPAAYSrGGAPVYVVAESASTTEWAAQFG--------LPMILSWIIntnekkaqlELYNEVAQEYGHDIHNIDHCLS 227
Cdd:PRK02271 141 AKLNVKPVQ-GEIPIYMGAQGPKMLELAGEIAdgvlinasNPKDFEWAV---------PLIKKGAEEAGKSRGEFDVAAY 210

                        250
                 ....*....|....*..
gi 471179932 228 YITSVDHDSIKAKEICR 244
Cdd:PRK02271 211 ASVSVDKDEDKAREAAK 227
F420_MSMEG_2516 TIGR03621
probable F420-dependent oxidoreductase, MSMEG_2516 family; Coenzyme F420 is produced by ...
 19-114 6.38e-07

probable F420-dependent oxidoreductase, MSMEG_2516 family; Coenzyme F420 is produced by methanogenic archaea, a number of the Actinomycetes (including Mycobacterium tuberculosis), and rare members of other lineages. The resulting information-rich phylogenetic profile identifies candidate F420-dependent oxidoreductases within the family of luciferase-like enzymes (pfam00296), where the species range for the subfamily encompasses many F420-positive genomes without straying beyond. This family is uncharacterized, and named for member MSMEG_2516 from Mycobacterium smegmatis. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 200301 [Multi-domain]  Cd Length: 295  Bit Score: 50.45  E-value: 6.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932   19 EVMKRLVKLGRISEECGFDTVWLLEHhftefglLGN--PYVAAAYLLGATKKLNVGTAAIVLPTAHPVRQLEDVNLLDQM 96
Cdd:TIGR03621  11 ESARDLVDLARRAEDAGFDVLTVPDH-------LGApaPFAALTAAAAATTTLRLGTLVLNNDFRHPALLAREAATLDAL 83

                          90
                  ....*....|....*...
gi 471179932   97 SKGRFRFGICRGLYNKDF 114
Cdd:TIGR03621  84 SDGRLELGLGAGYVRSEF 101
Alkanesulfonate_monoxygenase cd01094
Alkanesulfonate monoxygenase is the monoxygenase of a two-component system that catalyzes the ...
 24-186 2.59e-06

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: 48.04  E-value: 2.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932  24 LVKLGRISEECGFDTVWLLEHHFTEfgllgNPYVAAAYLLGATKKLNVGTAA--IVLPTAHPVRQLEdvnLLDQMSKGRF 101
Cdd:cd01094   30 NRQIAQAAEELGFDGALSPTGSSGP-----DGWTVAAALAAATERLKFLVAIrpGLIAPTVAARQAA---TLDHISGGRL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932 102 RFGICRGLYNKDFRVFGTDMNNSR--ALAECWYGLIKNGMTEGymEADNEHIKFHKVKVN---PAAYSRGGAPVYVVAES 176
Cdd:cd01094  102 GLNVVTGGDPAELRMDGDFLDHDEryARADEFLEVLRRLWTSD--EPFDFEGKFYRFKNAflrPKPPQQPHPPIYFGGSS 179

                        170
                 ....*....|
gi 471179932 177 ASTTEWAAQF 186
Cdd:cd01094  180 EAAIEFAARH 189
Flavin_utilizing_monoxygenases cd00347
Flavin-utilizing monoxygenases
 169-217 6.46e-06

Flavin-utilizing monoxygenases


Pssm-ID: 238209 [Multi-domain]  Cd Length: 90  Bit Score: 43.89  E-value: 6.46e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 471179932 169 PVYVVAESASTTEWAAQFGLPMILSWIINTNEKKAQLELYNEVAQEYGH 217
Cdd:cd00347   42 AIWFGGSSPPVAEQAGESGDGLLFAAREPPEEVAEALARYREAAAAAGR 90
Flavin_utilizing_monoxygenases cd00347
Flavin-utilizing monoxygenases
 1-41 7.06e-06

Flavin-utilizing monoxygenases


Pssm-ID: 238209 [Multi-domain]  Cd Length: 90  Bit Score: 43.89  E-value: 7.06e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 471179932   1 MKFGNFLLTYQPPQFSQTEVMKRLVKLGRISEECGFDTVWL 41
Cdd:cd00347    1 MKFGLFLPPPGGGGATAAEDLEYLVELARLAERLGFDAAWV 41
PRK10508 PRK10508
luciferase-like monooxygenase;
16-189 1.03e-05

luciferase-like monooxygenase;


Pssm-ID: 182505 [Multi-domain]  Cd Length: 333  Bit Score: 46.70  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932  16 SQTEVMKRLVKLGRISEECGFDTVWLLEHHftefGLLGNPYVAAAYLLG----ATKKLNVGTAAIVLPTAHPVRQLEDVN 91
Cdd:PRK10508  21 SAREAFSHSLDLARLAEKRGYHRYWLAEHH----NMTGIASAATSVLIGylaaNTTTLHLGSGGVMLPNHSPLVIAEQFG 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932  92 LLDQMSKGRFRFGICRGLynkdfrvfGTDMNNSRALAECWYGLIKNgmtegyMEADNEHIK--FHKVKVNPAAYSRGG-- 167
Cdd:PRK10508  97 TLNTLYPGRIDLGLGRAP--------GSDQRTMMALRRHMSGDIDN------FPRDVAELVdwFDARDPNPHVRPVPGyg 162

                        170       180
                 ....*....|....*....|....
gi 471179932 168 --APVYVVAESASTTEWAAQFGLP 189
Cdd:PRK10508 163 ekIPVWLLGSSLYSAQLAAQLGLP 186
F420_MSMEG_4879 TIGR03564
F420-dependent oxidoreductase, MSMEG_4879 family; Coenzyme F420 is produced by methanogenic ...
 24-123 2.89e-04

F420-dependent oxidoreductase, MSMEG_4879 family; Coenzyme F420 is produced by methanogenic archaea, a number of the Actinomycetes (including Mycobacterium tuberculosis), and rare members of other lineages. The resulting information-rich phylogenetic profile identifies candidate F420-dependent oxidoreductases within the family of luciferase-like enzymes (pfam00296), where the species range for the subfamily encompasses many F420-positive genomes without straying beyond. This family is uncharacterized, and named for member MSMEG_4879 from Mycobacterium smegmatis. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274651  Cd Length: 265  Bit Score: 41.95  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471179932   24 LVKLGRISEECGFDTVWLLEhhftefGLLGNPYVAAAYLLGATKKLNVGTAAIVLPTAHPVRQLEDVNLLDQMSKGRFRF 103
Cdd:TIGR03564   1 LVADARRAAAAGLDSAWLGQ------VYGYDALTALALVGRAVPGIELGTAVVPTYPRHPLALASQALTAQAAAHGRLTL 74

                          90       100
                  ....*....|....*....|..
gi 471179932  104 GIcrGLYNKDF--RVFGTDMNN 123
Cdd:TIGR03564  75 GL--GLSHRWIveDMFGLPFDR 94
 
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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