NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1609605253|gb|TGE85175|]
View 

N5,N10-methylene tetrahydromethanopterin reductase [Rhizobium sp. SEMIA 4032]

Protein Classification

LLM class flavin-dependent oxidoreductase( domain architecture ID 10023993)

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
FMN_nitrolo TIGR03860
FMN-dependent oxidoreductase, nitrilotriacetate monooxygenase family; This model represents a ...
9-432 0e+00

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: 628.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253   9 LNAFnMNCVGHiNHGLWTHPRDRSHEYKRLDYWTDLARTLERGLFDGLFLADIVGVYDiyqgSVDLTLKESIQLPVNDPS 88
Cdd:TIGR03860   1 LGAF-LNGVGH-HPGLWRHPRARADAYLDLDYWTELARTAERGKFDALFFADVLGVYD----VPDAALRRAAQLPRFEPL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253  89 MLVSAMAAVTRDLGFGITVNTGVEHPYTFARRMSTLDHLTGGRIGWNIVTGYLDSAAHALGQNGMIAHDDRYERADDYLD 168
Cdd:TIGR03860  75 TLLSALAAVTEHIGLGATASTTYEEPYNLARRFASLDHLSGGRAGWNIVTSYLDSAARNFGLDEHPPHDERYERAEEFVD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 169 LLYKLWEgSWDDDAVVLDKARRIYAEPERVRKIRHEGPYYRSHGYHLAEPSPQRTPVLYQAGASGRGKRFAARHAECIFI 248
Cdd:TIGR03860 155 VVYKLWD-SWEDDAFVRDKASGVFADPAKVHPINHKGKHFSVRGPLNIPRSPQGTPVLFQAGSSERGREFAARHAEAVFT 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 249 GATDPAAARRTVQALREEVVAAGRRPGDVKIFLGITVVAGRTVAEAEDRLSDYLDHASPEAGLAHFSAGSGVDVSRYDLD 328
Cdd:TIGR03860 234 AQPTLEDAQAFYADIKARAAAAGRDPDDVKILPGITPIVGRTEAEARAKYAELQDLISPEGGLALLSGWTGIDLSQYDLD 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 329 EPILYGKGNAIQS-----VTQVAREKGWTRRQLLKELAIGGRYPLIVGDGAKVAAELIRWVEESGIDGFNLTRTVVPESY 403
Cdd:TIGR03860 314 APLPDLPTEAGQKsrfdlILELARRENLTLRQLALRLAGGRGHPVFVGTPEQVADQLEEWFEEGAADGFNLMPPVLPGGL 393
                         410       420
                  ....*....|....*....|....*....
gi 1609605253 404 ETFIDVVVPELQARGAYKTSYAGGSLRNR 432
Cdd:TIGR03860 394 EDFVDLVVPELQRRGLFRTEYEGGTLREH 422
 
Name Accession Description Interval E-value
FMN_nitrolo TIGR03860
FMN-dependent oxidoreductase, nitrilotriacetate monooxygenase family; This model represents a ...
9-432 0e+00

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: 628.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253   9 LNAFnMNCVGHiNHGLWTHPRDRSHEYKRLDYWTDLARTLERGLFDGLFLADIVGVYDiyqgSVDLTLKESIQLPVNDPS 88
Cdd:TIGR03860   1 LGAF-LNGVGH-HPGLWRHPRARADAYLDLDYWTELARTAERGKFDALFFADVLGVYD----VPDAALRRAAQLPRFEPL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253  89 MLVSAMAAVTRDLGFGITVNTGVEHPYTFARRMSTLDHLTGGRIGWNIVTGYLDSAAHALGQNGMIAHDDRYERADDYLD 168
Cdd:TIGR03860  75 TLLSALAAVTEHIGLGATASTTYEEPYNLARRFASLDHLSGGRAGWNIVTSYLDSAARNFGLDEHPPHDERYERAEEFVD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 169 LLYKLWEgSWDDDAVVLDKARRIYAEPERVRKIRHEGPYYRSHGYHLAEPSPQRTPVLYQAGASGRGKRFAARHAECIFI 248
Cdd:TIGR03860 155 VVYKLWD-SWEDDAFVRDKASGVFADPAKVHPINHKGKHFSVRGPLNIPRSPQGTPVLFQAGSSERGREFAARHAEAVFT 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 249 GATDPAAARRTVQALREEVVAAGRRPGDVKIFLGITVVAGRTVAEAEDRLSDYLDHASPEAGLAHFSAGSGVDVSRYDLD 328
Cdd:TIGR03860 234 AQPTLEDAQAFYADIKARAAAAGRDPDDVKILPGITPIVGRTEAEARAKYAELQDLISPEGGLALLSGWTGIDLSQYDLD 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 329 EPILYGKGNAIQS-----VTQVAREKGWTRRQLLKELAIGGRYPLIVGDGAKVAAELIRWVEESGIDGFNLTRTVVPESY 403
Cdd:TIGR03860 314 APLPDLPTEAGQKsrfdlILELARRENLTLRQLALRLAGGRGHPVFVGTPEQVADQLEEWFEEGAADGFNLMPPVLPGGL 393
                         410       420
                  ....*....|....*....|....*....
gi 1609605253 404 ETFIDVVVPELQARGAYKTSYAGGSLRNR 432
Cdd:TIGR03860 394 EDFVDLVVPELQRRGLFRTEYEGGTLREH 422
Nitrilotriacetate_monoxgenase cd01095
nitrilotriacetate monoxygenase oxidizes nitrilotriacetate utilizing reduced flavin ...
9-420 8.55e-94

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: 287.30  E-value: 8.55e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253   9 LNAFNMNCVGHINHGLWTHPrDRSHEYKRLDYWTDLARTLERGLFDGLFLADIVGVYDIYQGSVDLTLkesiqlpvnDPS 88
Cdd:cd01095     1 LHLGAFLHGAGHHAAAWRHP-APPDASIDFDHYVRLARTAERAKFDAVFLADGLAIRALSRPHPVARL---------EPL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253  89 MLVSAMAAVTRDLGFGITVNTGVEHPYTFARRMSTLDHLTGGRIGWNIVTGYLDSAAHALGQNGMIAHDDRYERADDYLD 168
Cdd:cd01095    71 TLLAALAAVTERIGLVATASTTYNEPYHLARRFASLDHISGGRAGWNVVTSANPGEARNFGRDEHPEHDERYARAEEFVE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 169 LLYKLWEgSWDDDAVVLDKARRIYAEPERVRKIRHEGPYYRSHGYHLAEPSPQRTPVLYQAGASGRGKRFAARHAECIFI 248
Cdd:cd01095   151 VVKGLWD-SWEDDALVRDKASGRFADPAKVHPLDHVGDHFGVRGPLNGPRSPQGRPVIVQAGSSEAGREFAARHAEAVFT 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 249 GATDPAAARRTVQALREEVVAAGRRPGDVkiflgitvvagRTVAEAEDRLSdyldhaspeaglahfsagsgvdvsrydld 328
Cdd:cd01095   230 AQQTLEEAQAFYADVKARAAAAGRLDPPP-----------PDLPDLGSRLS----------------------------- 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 329 ePILYGKGNAIQSVTQVAREKGWTRRQLlkELAIGGRYPLIVGDGAKVAAELIRWVEESGIDGFNLTRTVVPESYETFID 408
Cdd:cd01095   270 -ASRLLLADLLARGGLHRREVGTAREVA--DRLERAAGGGTVVGPEQIADELEEWFEAGAADGFNIMPPYLPGGLDDFVD 346
                         410
                  ....*....|..
gi 1609605253 409 VVVPELQARGAY 420
Cdd:cd01095   347 LVVPELQRRGLF 358
SsuD COG2141
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
49-416 3.04e-68

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: 219.42  E-value: 3.04e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253  49 ERGLFDGLFLADIVGVYDIyqgsvdltlkesiqlPVNDPSMLVSAMAAVTRDLGFG-ITVNTGVEHPYTFARRMSTLDHL 127
Cdd:COG2141     2 ERLGFDRVWVADHHFPPGG---------------ASPDPWVLLAALAAATSRIRLGtGVVVLPLRHPLVVAEQFATLDHL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 128 TGGRIGWNIVTGYLDSAAHALGqngmIAHDDRYERADDYLDLLYKLWEGswdddavvldkarriyaepervRKIRHEGPY 207
Cdd:COG2141    67 SGGRLDLGVGRGWGPDEFAAFG----LDHDERYERFEEALEVLRRLWTG----------------------EPVTFEGEF 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 208 YRSHGYHLAEPSPQRT-PVLYQAGASGRGKRFAARHAECIFIGATDPAAARRTVQALREEVVAAGRRPGDVKIFLGITVV 286
Cdd:COG2141   121 FTVEGARLVPRPVQGPhPPIWIAGSSPAGARLAARLGDGVFTAGGTPEELAEAIAAYREAAAAAGRDPDDLRVSVGLHVI 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 287 AGRTVAEAEDRLSDYLDhaspeaglAHFSAGSGVDvsrydldepilygkgnaiqsvtQVAREKGWTRRQLLKELAiggrY 366
Cdd:COG2141   201 VAETDEEARERARPYLR--------ALLALPRGRP----------------------PEEAEEGLTVREDLLELL----G 246
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1609605253 367 PLIVGDGAKVAAELIRWVEESGIDGFNLT-----RTVVPESYETFIDVVVPELQA 416
Cdd:COG2141   247 AALVGTPEQVAERLEELAEAAGVDEFLLQfpgldPEDRLRSLELFAEEVLPLLRR 301
Bac_luciferase pfam00296
Luciferase-like monooxygenase;
24-391 6.15e-38

Luciferase-like monooxygenase;


Pssm-ID: 425589 [Multi-domain]  Cd Length: 313  Bit Score: 140.19  E-value: 6.15e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253  24 LWTHPRDRSHEYKRLDYWTDLARTLERGLFDGLFLADivgVYDIYQGSvdltlkesiqlpvnDPSMLVSAMAAVTRDLGF 103
Cdd:pfam00296   8 PTRNGGGLGAGSESLRYLVELARAAEELGFDGVWLAE---HHGGPGGP--------------DPFVVLAALAAATSRIRL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 104 GITVNTGVE-HPYTFARRMSTLDHLTGGRIGWNIVTGYldsAAHALGQNGMiAHDDRYERADDYLDLLYKLWEGswddda 182
Cdd:pfam00296  71 GTAVVPLPTrHPAVLAEQAATLDHLSGGRFDLGLGTGG---PAVEFRRFGV-DHDERYARLREFLEVLRRLWRG------ 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 183 vvldkarriyaepervRKIRHEGPYYRSHGYHLAEPSPQRTPVlYQAGASGRGKRFAARHAECIFI-GATDPAAARRTVQ 261
Cdd:pfam00296 141 ----------------EPVDFEGEFFTLDGAFLLPRPVQGIPV-WVAASSPAMLELAARHADGLLLwGFAPPAAAAELIE 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 262 ALREEVVAAGRRPGDVKIFLGITVVAGRTVAEAEDRLSDYLDhaspeaglahfsagsGVDVSRYDLDEPILYGKGNAIQS 341
Cdd:pfam00296 204 RVRAGAAEAGRDPADIRVGASLTVIVADTEEEARAEARALIA---------------GLPFYRMDSEGAGRLAEAREIGE 268
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1609605253 342 vtqVAREKGWTRRQLLKELAIGGRyPLIVGDGAKVAAELIRWvEESGIDG 391
Cdd:pfam00296 269 ---EYDAGDWAGAADAVPDELVRA-FALVGTPEQVAERLAAY-AEAGVDH 313
PRK00719 PRK00719
alkanesulfonate monooxygenase; Provisional
86-392 3.71e-16

alkanesulfonate monooxygenase; Provisional


Pssm-ID: 234821 [Multi-domain]  Cd Length: 378  Bit Score: 79.61  E-value: 3.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253  86 DPSMLVSAMAAVTRDLGFGITVNTGVEHPYTFARRMSTLDHLTGGRIGWNIVTGYlDSAAHAlGQNGMIAHDDRYERADD 165
Cdd:PRK00719   55 DAWLVAASLIPVTQRLKFLVALRPGLMSPTVAARMAATLDRLSNGRLLINLVTGG-DPAELA-GDGLFLDHDERYEASAE 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 166 YLDLLYKLWEGSwdddavvldkarriyaepervrKIRHEGPYYRSHGYHLAEPSPQRT-PVLYQAGASGRGKRFAARHAE 244
Cdd:PRK00719  133 FLRIWRRLLEGE----------------------TVDFEGKHIQVKGAKLLFPPVQQPyPPLYFGGSSDAAQELAAEQVD 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 245 CIFIGATDPAAARRTVQALREEVVAAGRrpgdvKIFLGIT--VVAGRTVAEA---EDRLSDYLDHASPEAGLAHFsagsg 319
Cdd:PRK00719  191 LYLTWGEPPAQVKEKIEQVRAKAAAHGR-----KVRFGIRlhVIVRETNEEAwqaAERLISHLDDETIARAQAAF----- 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 320 vdvSRYDldepilygkgnaiqSVTQ--VAREKGWTRRQLlkE----------LAIGGRYPLIVGDGAKVAAElIRWVEES 387
Cdd:PRK00719  261 ---ARMD--------------SVGQqrMAALHGGKRDNL--EispnlwagvgLVRGGAGTALVGDPPTVAAR-IKEYAAL 320

                  ....*
gi 1609605253 388 GIDGF 392
Cdd:PRK00719  321 GIDTF 325
 
Name Accession Description Interval E-value
FMN_nitrolo TIGR03860
FMN-dependent oxidoreductase, nitrilotriacetate monooxygenase family; This model represents a ...
9-432 0e+00

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: 628.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253   9 LNAFnMNCVGHiNHGLWTHPRDRSHEYKRLDYWTDLARTLERGLFDGLFLADIVGVYDiyqgSVDLTLKESIQLPVNDPS 88
Cdd:TIGR03860   1 LGAF-LNGVGH-HPGLWRHPRARADAYLDLDYWTELARTAERGKFDALFFADVLGVYD----VPDAALRRAAQLPRFEPL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253  89 MLVSAMAAVTRDLGFGITVNTGVEHPYTFARRMSTLDHLTGGRIGWNIVTGYLDSAAHALGQNGMIAHDDRYERADDYLD 168
Cdd:TIGR03860  75 TLLSALAAVTEHIGLGATASTTYEEPYNLARRFASLDHLSGGRAGWNIVTSYLDSAARNFGLDEHPPHDERYERAEEFVD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 169 LLYKLWEgSWDDDAVVLDKARRIYAEPERVRKIRHEGPYYRSHGYHLAEPSPQRTPVLYQAGASGRGKRFAARHAECIFI 248
Cdd:TIGR03860 155 VVYKLWD-SWEDDAFVRDKASGVFADPAKVHPINHKGKHFSVRGPLNIPRSPQGTPVLFQAGSSERGREFAARHAEAVFT 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 249 GATDPAAARRTVQALREEVVAAGRRPGDVKIFLGITVVAGRTVAEAEDRLSDYLDHASPEAGLAHFSAGSGVDVSRYDLD 328
Cdd:TIGR03860 234 AQPTLEDAQAFYADIKARAAAAGRDPDDVKILPGITPIVGRTEAEARAKYAELQDLISPEGGLALLSGWTGIDLSQYDLD 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 329 EPILYGKGNAIQS-----VTQVAREKGWTRRQLLKELAIGGRYPLIVGDGAKVAAELIRWVEESGIDGFNLTRTVVPESY 403
Cdd:TIGR03860 314 APLPDLPTEAGQKsrfdlILELARRENLTLRQLALRLAGGRGHPVFVGTPEQVADQLEEWFEEGAADGFNLMPPVLPGGL 393
                         410       420
                  ....*....|....*....|....*....
gi 1609605253 404 ETFIDVVVPELQARGAYKTSYAGGSLRNR 432
Cdd:TIGR03860 394 EDFVDLVVPELQRRGLFRTEYEGGTLREH 422
Nitrilotriacetate_monoxgenase cd01095
nitrilotriacetate monoxygenase oxidizes nitrilotriacetate utilizing reduced flavin ...
9-420 8.55e-94

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: 287.30  E-value: 8.55e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253   9 LNAFNMNCVGHINHGLWTHPrDRSHEYKRLDYWTDLARTLERGLFDGLFLADIVGVYDIYQGSVDLTLkesiqlpvnDPS 88
Cdd:cd01095     1 LHLGAFLHGAGHHAAAWRHP-APPDASIDFDHYVRLARTAERAKFDAVFLADGLAIRALSRPHPVARL---------EPL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253  89 MLVSAMAAVTRDLGFGITVNTGVEHPYTFARRMSTLDHLTGGRIGWNIVTGYLDSAAHALGQNGMIAHDDRYERADDYLD 168
Cdd:cd01095    71 TLLAALAAVTERIGLVATASTTYNEPYHLARRFASLDHISGGRAGWNVVTSANPGEARNFGRDEHPEHDERYARAEEFVE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 169 LLYKLWEgSWDDDAVVLDKARRIYAEPERVRKIRHEGPYYRSHGYHLAEPSPQRTPVLYQAGASGRGKRFAARHAECIFI 248
Cdd:cd01095   151 VVKGLWD-SWEDDALVRDKASGRFADPAKVHPLDHVGDHFGVRGPLNGPRSPQGRPVIVQAGSSEAGREFAARHAEAVFT 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 249 GATDPAAARRTVQALREEVVAAGRRPGDVkiflgitvvagRTVAEAEDRLSdyldhaspeaglahfsagsgvdvsrydld 328
Cdd:cd01095   230 AQQTLEEAQAFYADVKARAAAAGRLDPPP-----------PDLPDLGSRLS----------------------------- 269
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 329 ePILYGKGNAIQSVTQVAREKGWTRRQLlkELAIGGRYPLIVGDGAKVAAELIRWVEESGIDGFNLTRTVVPESYETFID 408
Cdd:cd01095   270 -ASRLLLADLLARGGLHRREVGTAREVA--DRLERAAGGGTVVGPEQIADELEEWFEAGAADGFNIMPPYLPGGLDDFVD 346
                         410
                  ....*....|..
gi 1609605253 409 VVVPELQARGAY 420
Cdd:cd01095   347 LVVPELQRRGLF 358
SsuD COG2141
Flavin-dependent oxidoreductase, luciferase family (includes alkanesulfonate monooxygenase ...
49-416 3.04e-68

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: 219.42  E-value: 3.04e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253  49 ERGLFDGLFLADIVGVYDIyqgsvdltlkesiqlPVNDPSMLVSAMAAVTRDLGFG-ITVNTGVEHPYTFARRMSTLDHL 127
Cdd:COG2141     2 ERLGFDRVWVADHHFPPGG---------------ASPDPWVLLAALAAATSRIRLGtGVVVLPLRHPLVVAEQFATLDHL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 128 TGGRIGWNIVTGYLDSAAHALGqngmIAHDDRYERADDYLDLLYKLWEGswdddavvldkarriyaepervRKIRHEGPY 207
Cdd:COG2141    67 SGGRLDLGVGRGWGPDEFAAFG----LDHDERYERFEEALEVLRRLWTG----------------------EPVTFEGEF 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 208 YRSHGYHLAEPSPQRT-PVLYQAGASGRGKRFAARHAECIFIGATDPAAARRTVQALREEVVAAGRRPGDVKIFLGITVV 286
Cdd:COG2141   121 FTVEGARLVPRPVQGPhPPIWIAGSSPAGARLAARLGDGVFTAGGTPEELAEAIAAYREAAAAAGRDPDDLRVSVGLHVI 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 287 AGRTVAEAEDRLSDYLDhaspeaglAHFSAGSGVDvsrydldepilygkgnaiqsvtQVAREKGWTRRQLLKELAiggrY 366
Cdd:COG2141   201 VAETDEEARERARPYLR--------ALLALPRGRP----------------------PEEAEEGLTVREDLLELL----G 246
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1609605253 367 PLIVGDGAKVAAELIRWVEESGIDGFNLT-----RTVVPESYETFIDVVVPELQA 416
Cdd:COG2141   247 AALVGTPEQVAERLEELAEAAGVDEFLLQfpgldPEDRLRSLELFAEEVLPLLRR 301
Alkanesulfonate_monoxygenase cd01094
Alkanesulfonate monoxygenase is the monoxygenase of a two-component system that catalyzes the ...
38-298 5.90e-41

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: 146.27  E-value: 5.90e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253  38 LDYWTDLARTLERGLFDGLFLAdivgvydiYQGSVdltlkesiqlpvNDPSMLVSAMAAVTRDLGFGITVNTGVEHPYTF 117
Cdd:cd01094    27 FEYNRQIAQAAEELGFDGALSP--------TGSSG------------PDGWTVAAALAAATERLKFLVAIRPGLIAPTVA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 118 ARRMSTLDHLTGGRIGWNIVTGYLDSAAHALGqnGMIAHDDRYERADDYLDLLYKLWEGSWDDDavvldkarriyaeper 197
Cdd:cd01094    87 ARQAATLDHISGGRLGLNVVTGGDPAELRMDG--DFLDHDERYARADEFLEVLRRLWTSDEPFD---------------- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 198 vrkirHEGPYYRSHGYHLAEPSPQR-TPVLYQAGASGRGKRFAARHAECIFIGATDPAAARRTVQALREEVVAAGRrpgD 276
Cdd:cd01094   149 -----FEGKFYRFKNAFLRPKPPQQpHPPIYFGGSSEAAIEFAARHADVYFTWGEPPAQVAEAIARVRAAAAAAGR---D 220
                         250       260
                  ....*....|....*....|..
gi 1609605253 277 VKIFLGITVVAGRTVAEAEDRL 298
Cdd:cd01094   221 VRFGIRLHVIVRDTEEEAWAYA 242
Bac_luciferase pfam00296
Luciferase-like monooxygenase;
24-391 6.15e-38

Luciferase-like monooxygenase;


Pssm-ID: 425589 [Multi-domain]  Cd Length: 313  Bit Score: 140.19  E-value: 6.15e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253  24 LWTHPRDRSHEYKRLDYWTDLARTLERGLFDGLFLADivgVYDIYQGSvdltlkesiqlpvnDPSMLVSAMAAVTRDLGF 103
Cdd:pfam00296   8 PTRNGGGLGAGSESLRYLVELARAAEELGFDGVWLAE---HHGGPGGP--------------DPFVVLAALAAATSRIRL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 104 GITVNTGVE-HPYTFARRMSTLDHLTGGRIGWNIVTGYldsAAHALGQNGMiAHDDRYERADDYLDLLYKLWEGswddda 182
Cdd:pfam00296  71 GTAVVPLPTrHPAVLAEQAATLDHLSGGRFDLGLGTGG---PAVEFRRFGV-DHDERYARLREFLEVLRRLWRG------ 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 183 vvldkarriyaepervRKIRHEGPYYRSHGYHLAEPSPQRTPVlYQAGASGRGKRFAARHAECIFI-GATDPAAARRTVQ 261
Cdd:pfam00296 141 ----------------EPVDFEGEFFTLDGAFLLPRPVQGIPV-WVAASSPAMLELAARHADGLLLwGFAPPAAAAELIE 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 262 ALREEVVAAGRRPGDVKIFLGITVVAGRTVAEAEDRLSDYLDhaspeaglahfsagsGVDVSRYDLDEPILYGKGNAIQS 341
Cdd:pfam00296 204 RVRAGAAEAGRDPADIRVGASLTVIVADTEEEARAEARALIA---------------GLPFYRMDSEGAGRLAEAREIGE 268
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1609605253 342 vtqVAREKGWTRRQLLKELAIGGRyPLIVGDGAKVAAELIRWvEESGIDG 391
Cdd:pfam00296 269 ---EYDAGDWAGAADAVPDELVRA-FALVGTPEQVAERLAAY-AEAGVDH 313
F420_Rv2161c TIGR03619
probable F420-dependent oxidoreductase, Rv2161c family; Coenzyme F420 has a limited ...
42-296 1.46e-21

probable F420-dependent oxidoreductase, Rv2161c family; Coenzyme F420 has a limited phylogenetic distribution, including methanogenic archaea, Mycobacterium tuberculosis and related species, Colwellia psychrerythraea 34H, Rhodopseudomonas palustris HaA2, and others. Partial phylogenetic profiling identifies protein subfamilies, within the larger family called luciferase-like monooxygenanases (pfam00296), that appear only in F420-positive genomes and are likely to be F420-dependent. This model describes a domain found in a distinctive subset of bacterial luciferase homologs, found only in F420-biosynthesizing members of the Actinobacteria. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274680 [Multi-domain]  Cd Length: 246  Bit Score: 93.09  E-value: 1.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253  42 TDLARTLERGLFDGLFLADIVGVYDIYQGSVDLTLKESIQLPVNDPSMLVSAMAAVTRDLGFGitvnTGV-----EHPYT 116
Cdd:TIGR03619   1 AELARAAEELGFDSLLAYEHVAIPARRETPWPDSGGGDAPDRTLDPFVALAFAAAVTSRLRLG----TGVlvlpqRDPLL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 117 FARRMSTLDHLTGGRIGWNIVTGYLDSAAHALGQngmiAHDDRYERADDYLDLLYKLWEGswdddavvldkarriyaepe 196
Cdd:TIGR03619  77 LAKQAATLDLLSGGRLRLGVGVGWLREEFRALGV----DFDERGRLLDEAIEALRALWTQ-------------------- 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 197 rvRKIRHEGPYYRSHGYHLAEPSPQRTPVLYQAGASGRGKRFAARHAECIFIGATDPAAARRTVQALREEVVAAGRRPGD 276
Cdd:TIGR03619 133 --DPVSFHGEFVDFDPAVVRPKPVQRPPPIWIGGNSEAALRRAARLGDGWMPFGPPVDRLAAAVARLRDLAAAAGRDPDA 210
                         250       260
                  ....*....|....*....|
gi 1609605253 277 VKIFLGITVVAGRTVAEAED 296
Cdd:TIGR03619 211 VEVVLVRTDPDGDADADAED 230
PRK00719 PRK00719
alkanesulfonate monooxygenase; Provisional
86-392 3.71e-16

alkanesulfonate monooxygenase; Provisional


Pssm-ID: 234821 [Multi-domain]  Cd Length: 378  Bit Score: 79.61  E-value: 3.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253  86 DPSMLVSAMAAVTRDLGFGITVNTGVEHPYTFARRMSTLDHLTGGRIGWNIVTGYlDSAAHAlGQNGMIAHDDRYERADD 165
Cdd:PRK00719   55 DAWLVAASLIPVTQRLKFLVALRPGLMSPTVAARMAATLDRLSNGRLLINLVTGG-DPAELA-GDGLFLDHDERYEASAE 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 166 YLDLLYKLWEGSwdddavvldkarriyaepervrKIRHEGPYYRSHGYHLAEPSPQRT-PVLYQAGASGRGKRFAARHAE 244
Cdd:PRK00719  133 FLRIWRRLLEGE----------------------TVDFEGKHIQVKGAKLLFPPVQQPyPPLYFGGSSDAAQELAAEQVD 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 245 CIFIGATDPAAARRTVQALREEVVAAGRrpgdvKIFLGIT--VVAGRTVAEA---EDRLSDYLDHASPEAGLAHFsagsg 319
Cdd:PRK00719  191 LYLTWGEPPAQVKEKIEQVRAKAAAHGR-----KVRFGIRlhVIVRETNEEAwqaAERLISHLDDETIARAQAAF----- 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 320 vdvSRYDldepilygkgnaiqSVTQ--VAREKGWTRRQLlkE----------LAIGGRYPLIVGDGAKVAAElIRWVEES 387
Cdd:PRK00719  261 ---ARMD--------------SVGQqrMAALHGGKRDNL--EispnlwagvgLVRGGAGTALVGDPPTVAAR-IKEYAAL 320

                  ....*
gi 1609605253 388 GIDGF 392
Cdd:PRK00719  321 GIDTF 325
PRK02271 PRK02271
methylenetetrahydromethanopterin reductase; Provisional
86-279 8.30e-05

methylenetetrahydromethanopterin reductase; Provisional


Pssm-ID: 235022 [Multi-domain]  Cd Length: 325  Bit Score: 44.54  E-value: 8.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253  86 DPSMLVSAMAAVTRD--LGFGITvNTGVEHPYTFARRMSTLDHLTGGRIGWNIVTGylDSAA-HALGqngmIAHDDRYER 162
Cdd:PRK02271   41 DVYMTLAAIAAATDTikLGPGVT-NPYTRHPAITASAIATLDEISGGRAVLGIGPG--DKATlDALG----IEWEKPLRT 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1609605253 163 ADDYLDLLYKLWEGswdddavvldkarriyaepervRKIRHEGPyYRSHGYHLA-EPSPQRTPVlYqAGASG-RGKRFAA 240
Cdd:PRK02271  114 VKEAIEVIRKLWAG----------------------ERVEHDGT-FKAAGAKLNvKPVQGEIPI-Y-MGAQGpKMLELAG 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1609605253 241 RHAECIFIGATDP---AAARRTVQALREEvvaAGRRPGDVKI 279
Cdd:PRK02271  169 EIADGVLINASNPkdfEWAVPLIKKGAEE---AGKSRGEFDV 207
Flavin_utilizing_monoxygenases cd00347
Flavin-utilizing monoxygenases
226-272 2.15e-03

Flavin-utilizing monoxygenases


Pssm-ID: 238209 [Multi-domain]  Cd Length: 90  Bit Score: 37.34  E-value: 2.15e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1609605253 226 LYQAGASGRGKRFAARHAECIFI-GATDPAAARRTVQALREEVVAAGR 272
Cdd:cd00347    43 IWFGGSSPPVAEQAGESGDGLLFaAREPPEEVAEALARYREAAAAAGR 90
Flavin_utilizing_monoxygenases cd00347
Flavin-utilizing monoxygenases
20-64 5.44e-03

Flavin-utilizing monoxygenases


Pssm-ID: 238209 [Multi-domain]  Cd Length: 90  Bit Score: 36.19  E-value: 5.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1609605253  20 INHGLWTHPRDRSHE--YKRLDYWTDLARTLERGLFDGLFLADIVGV 64
Cdd:cd00347     1 MKFGLFLPPPGGGGAtaAEDLEYLVELARLAERLGFDAAWVAIWFGG 47
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH