NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1021536288|gb|KZN83690|]
View 

Phenol 2-monooxygenase [Penicillium chrysogenum]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Phe_hydrox_dim pfam07976
Phenol hydroxylase, C-terminal dimerization domain; Phenol hydroxylase acts a homodimer, to ...
 110-270 3.62e-58

Phenol hydroxylase, C-terminal dimerization domain; Phenol hydroxylase acts a homodimer, to hydroxylates phenol to catechol or similar product. The enzyme is comprised of three domains. The first two domains from the active site. The third domain, this domain, is involved in forming the dimerization interface. The domain adopts a thioredoxin-like fold.


:

Pssm-ID: 429765  Cd Length: 166  Bit Score: 184.27  E-value: 3.62e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288 110 FMAGIDITYPHSTLVTqgeEDGATNFAKNLRLGMRLPSFLVVYQCDGVPIHLAKRLVSDGPWRLLVFSGDLRQPERMNAL 189
Cdd:pfam07976   1 FTSGVGVDYGPSILVA---GTSHQNLASGLPVGRRFPSAKVVRQADANPVHLQDELPSDGRFRILVFAGDISDPAQKSRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288 190 AHFAETFSRCSHLMNlqgIQVPKGRCP--ILELLLIQSSPRSAVNLLDLPELFHPFDHLTGWDYWKAFADDRD------Q 261
Cdd:pfam07976  78 EALADYLSSSSSFLS---RYTPAGADIdsVFDVLLIHSAPRTEVELEDLPEVLRPFDGKLGWDYWKVYVDDESyhegggD 154


                  ....*....
gi 1021536288 262 AYKGYGIDK 270
Cdd:pfam07976 155 AYEKYGIDP 163
PRK06184 super family cl35443
hypothetical protein; Provisional
 8-309 3.16e-36

hypothetical protein; Provisional


The actual alignment was detected with superfamily member PRK06184:

Pssm-ID: 235728 [Multi-domain]  Cd Length: 502  Bit Score: 135.88  E-value: 3.16e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288   8 RLVRHYRpHDRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAVItNGAQPTILETYETERRPVAKQLMTLDSRLVR 87
Cdd:PRK06184  273 RLADRYR-VGRVFLAGDAAHVHPPAGGQGLNTSVQDAYNLGWKLAAVL-AGAPEALLDTYEEERRPVAAAVLGLSTELLD 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288  88 AYEDEendnssgiyEVREQYAGfmAGIDITYPHSTLVTQGEEDGATnfaknLRLGMRLPSflvvYQCDGvPIHLAKRL-- 165
Cdd:PRK06184  351 AIKRG---------DMRRGRDV--QQLDLGYRGSSLAVDGPERTGG-----LRAGDRAPD----APLLG-AAGQPTRLfd 409

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288 166 VSDGP-WRLLVFSgdlrqPERMNALAHFAETFSRCshlmnlqGIQVPKGrcpilellliqssprsavnlldlpelfhpfd 244
Cdd:PRK06184  410 LFRGPhWTLLAFG-----AGAAAILARRGLRIHRV-------GDAAEGG------------------------------- 446

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1021536288 245 hltgwdywkAFADDRDQAYKGYGIdknGPGCLVLCRPDQHVAWIGSMENTSELDSYFSSiFGRSS 309
Cdd:PRK06184  447 ---------DLVDDAGHFRDAYGL---TGGTLVLVRPDGYVGLIAAGDDAAALEAYLAR-VGLGR 498
 
Name Accession Description Interval E-value
Phe_hydrox_dim pfam07976
Phenol hydroxylase, C-terminal dimerization domain; Phenol hydroxylase acts a homodimer, to ...
 110-270 3.62e-58

Phenol hydroxylase, C-terminal dimerization domain; Phenol hydroxylase acts a homodimer, to hydroxylates phenol to catechol or similar product. The enzyme is comprised of three domains. The first two domains from the active site. The third domain, this domain, is involved in forming the dimerization interface. The domain adopts a thioredoxin-like fold.


Pssm-ID: 429765  Cd Length: 166  Bit Score: 184.27  E-value: 3.62e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288 110 FMAGIDITYPHSTLVTqgeEDGATNFAKNLRLGMRLPSFLVVYQCDGVPIHLAKRLVSDGPWRLLVFSGDLRQPERMNAL 189
Cdd:pfam07976   1 FTSGVGVDYGPSILVA---GTSHQNLASGLPVGRRFPSAKVVRQADANPVHLQDELPSDGRFRILVFAGDISDPAQKSRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288 190 AHFAETFSRCSHLMNlqgIQVPKGRCP--ILELLLIQSSPRSAVNLLDLPELFHPFDHLTGWDYWKAFADDRD------Q 261
Cdd:pfam07976  78 EALADYLSSSSSFLS---RYTPAGADIdsVFDVLLIHSAPRTEVELEDLPEVLRPFDGKLGWDYWKVYVDDESyhegggD 154


                  ....*....
gi 1021536288 262 AYKGYGIDK 270
Cdd:pfam07976 155 AYEKYGIDP 163
PRK08294 PRK08294
phenol 2-monooxygenase; Provisional
 5-305 4.98e-57

phenol 2-monooxygenase; Provisional


Pssm-ID: 236223 [Multi-domain]  Cd Length: 634  Bit Score: 194.05  E-value: 4.98e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288   5 IGRRLVRHY---------RPHDRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAVITNGAQPTILETYETERRPVA 75
Cdd:PRK08294  319 VGQRLTDRFddvpaeeagTRLPRVFIAGDACHTHSAKAGQGMNVSMQDGFNLGWKLAAVLSGRSPPELLHTYSAERQAIA 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288  76 KQLMTLD---SRLVRA-YEDEENDNSSGIYEVREQYAGFMAGIDITYPHSTLVTQGEEDGatnFAKNLRLGMRLPSFLVV 151
Cdd:PRK08294  399 QELIDFDrewSTMMAApPKEGGGVDPAELQDYFVKHGRFTAGTATHYAPSLLTGEATHQD---LATGFPIGKRFHSAPVI 475

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288 152 YQCDGVPIHLAKRLVSDGPWRLLVFSG--DLRQPE-RMNALAHFAETfSRCSHLMNLqgiqVPKGRCP--ILELLLIQSS 226
Cdd:PRK08294  476 RLADAKPVHLGHAATADGRWRIYAFADaaDPAGPGsALDALCEFLAE-SPDSPLRRF----TPSGADIdaVIDVRAIFQQ 550

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288 227 PRSAVNLLDLPELFHPFDHLTGW-DYWKAFADDR--DQAYKGYGIDKnGPGCLVLCRPDQHVAWIGSMENTSELDSYFSS 303
Cdd:PRK08294  551 PHRELDLEDVPALLLPRKGRFGLtDYEKVFCADLsgADIFDLRGIDR-DRGAVVVVRPDQYVANVLPLDAHAELAAFFAG 629


                  ..
gi 1021536288 304 IF 305
Cdd:PRK08294  630 FL 631
PHOX_C cd02979
FAD-dependent Phenol hydoxylase (PHOX) family, C-terminal TRX-fold domain; composed of ...
 142-304 3.52e-49

FAD-dependent Phenol hydoxylase (PHOX) family, C-terminal TRX-fold domain; composed of proteins similar to PHOX from the aerobic topsoil yeast Trichosporon cutaneum. PHOX is a flavoprotein monooxygenase that catalyzes the hydroxylation of phenol and simple phenol derivatives in the ortho position with the consumption of NADPH and oxygen. This is the first step in the biodegradation and detoxification of phenolic compounds. PHOX contains three domains. The substrate and FAD/NAD(P) binding sites are contained in the first two domains, which adopt a complicated folding pattern. The third or C-terminal domain contains a TRX fold and is involved in dimerization. The functional unit of PHOX is a dimer, although active tetramers of the recombinant enzyme can be isolated when overproduced in bacteria.


Pssm-ID: 239277 [Multi-domain]  Cd Length: 167  Bit Score: 161.30  E-value: 3.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288 142 GMRLPSFLVVYQCDGVPIHLAKRLVSDGPWRLLVFSGDLRQPERMNALAHFAETFSRcSHLMNLQGIQVPKGRCPILELL 221
Cdd:cd02979     1 GRRFPSAPVVRQADALPVHLGHRLPADGRFRIYVFAGDIAPAQQKSRLTQLCDALDS-PDSFPLRYTPRGADPDSVFDVV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288 222 LIQSSPRSAVNLLDLPELFHPFDHLTGWDYWKAFADDR------DQAYKGYGIDKNgPGCLVLCRPDQHVAWIGSMENTS 295
Cdd:cd02979    80 TIHAAPRREIELLDLPAVLRPFGEKKGWDYEKIYADDDsyheghGDAYEKYGIDPE-RGAVVVVRPDQYVALVGPLDDVE 158


                  ....*....
gi 1021536288 296 ELDSYFSSI 304
Cdd:cd02979   159 ALEAYFAGF 167
PRK06184 PRK06184
hypothetical protein; Provisional
 8-309 3.16e-36

hypothetical protein; Provisional


Pssm-ID: 235728 [Multi-domain]  Cd Length: 502  Bit Score: 135.88  E-value: 3.16e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288   8 RLVRHYRpHDRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAVItNGAQPTILETYETERRPVAKQLMTLDSRLVR 87
Cdd:PRK06184  273 RLADRYR-VGRVFLAGDAAHVHPPAGGQGLNTSVQDAYNLGWKLAAVL-AGAPEALLDTYEEERRPVAAAVLGLSTELLD 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288  88 AYEDEendnssgiyEVREQYAGfmAGIDITYPHSTLVTQGEEDGATnfaknLRLGMRLPSflvvYQCDGvPIHLAKRL-- 165
Cdd:PRK06184  351 AIKRG---------DMRRGRDV--QQLDLGYRGSSLAVDGPERTGG-----LRAGDRAPD----APLLG-AAGQPTRLfd 409

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288 166 VSDGP-WRLLVFSgdlrqPERMNALAHFAETFSRCshlmnlqGIQVPKGrcpilellliqssprsavnlldlpelfhpfd 244
Cdd:PRK06184  410 LFRGPhWTLLAFG-----AGAAAILARRGLRIHRV-------GDAAEGG------------------------------- 446

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1021536288 245 hltgwdywkAFADDRDQAYKGYGIdknGPGCLVLCRPDQHVAWIGSMENTSELDSYFSSiFGRSS 309
Cdd:PRK06184  447 ---------DLVDDAGHFRDAYGL---TGGTLVLVRPDGYVGLIAAGDDAAALEAYLAR-VGLGR 498
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 5-79 4.17e-31

FAD binding domain; This domain is involved in FAD binding in a number of enzymes.


Pssm-ID: 396193 [Multi-domain]  Cd Length: 348  Bit Score: 119.35  E-value: 4.17e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1021536288   5 IGRRLVRHYRpHDRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAVITNGAQPTILETYETERRPVAKQLM 79
Cdd:pfam01494 272 VASRVATRYR-KGRVFLAGDAAHIHPPTGGQGLNTAIQDAFNLAWKLAAVLRGQAGESLLDTYSAERLPVAWAVV 345
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 5-90 1.74e-26

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 106.18  E-value: 1.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288   5 IGRRLVRHYRpHDRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAVITNGAQPTILETYETERRPVAKQLMTLDSR 84
Cdd:COG0654   213 LRRRRAERWR-RGRVVLLGDAAHTMHPLGGQGANLALRDAAALAWKLAAALRGRDDEAALARYERERRPRAARVQRAADA 291


                  ....*.
gi 1021536288  85 LVRAYE 90
Cdd:COG0654   292 LGRLFH 297
COQ6 TIGR01989
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase ...
 17-89 2.70e-08

ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase responsible for the 4-hydroxylateion of the phenol ring in the aerobic biosynthesis of ubiquinone


Pssm-ID: 273914 [Multi-domain]  Cd Length: 437  Bit Score: 54.76  E-value: 2.70e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021536288  17 DRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAVITNGAQ---PTILETYETERRPVAKQLMTLDSRLVRAY 89
Cdd:TIGR01989 333 KRVALVGDAAHRVHPLAGQGVNLGFGDVASLVKALAEAVSVGADigsISSLKPYERERYAKNVVLLGLVDKLHKLY 408
 
Name Accession Description Interval E-value
Phe_hydrox_dim pfam07976
Phenol hydroxylase, C-terminal dimerization domain; Phenol hydroxylase acts a homodimer, to ...
 110-270 3.62e-58

Phenol hydroxylase, C-terminal dimerization domain; Phenol hydroxylase acts a homodimer, to hydroxylates phenol to catechol or similar product. The enzyme is comprised of three domains. The first two domains from the active site. The third domain, this domain, is involved in forming the dimerization interface. The domain adopts a thioredoxin-like fold.


Pssm-ID: 429765  Cd Length: 166  Bit Score: 184.27  E-value: 3.62e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288 110 FMAGIDITYPHSTLVTqgeEDGATNFAKNLRLGMRLPSFLVVYQCDGVPIHLAKRLVSDGPWRLLVFSGDLRQPERMNAL 189
Cdd:pfam07976   1 FTSGVGVDYGPSILVA---GTSHQNLASGLPVGRRFPSAKVVRQADANPVHLQDELPSDGRFRILVFAGDISDPAQKSRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288 190 AHFAETFSRCSHLMNlqgIQVPKGRCP--ILELLLIQSSPRSAVNLLDLPELFHPFDHLTGWDYWKAFADDRD------Q 261
Cdd:pfam07976  78 EALADYLSSSSSFLS---RYTPAGADIdsVFDVLLIHSAPRTEVELEDLPEVLRPFDGKLGWDYWKVYVDDESyhegggD 154


                  ....*....
gi 1021536288 262 AYKGYGIDK 270
Cdd:pfam07976 155 AYEKYGIDP 163
PRK08294 PRK08294
phenol 2-monooxygenase; Provisional
 5-305 4.98e-57

phenol 2-monooxygenase; Provisional


Pssm-ID: 236223 [Multi-domain]  Cd Length: 634  Bit Score: 194.05  E-value: 4.98e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288   5 IGRRLVRHY---------RPHDRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAVITNGAQPTILETYETERRPVA 75
Cdd:PRK08294  319 VGQRLTDRFddvpaeeagTRLPRVFIAGDACHTHSAKAGQGMNVSMQDGFNLGWKLAAVLSGRSPPELLHTYSAERQAIA 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288  76 KQLMTLD---SRLVRA-YEDEENDNSSGIYEVREQYAGFMAGIDITYPHSTLVTQGEEDGatnFAKNLRLGMRLPSFLVV 151
Cdd:PRK08294  399 QELIDFDrewSTMMAApPKEGGGVDPAELQDYFVKHGRFTAGTATHYAPSLLTGEATHQD---LATGFPIGKRFHSAPVI 475

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288 152 YQCDGVPIHLAKRLVSDGPWRLLVFSG--DLRQPE-RMNALAHFAETfSRCSHLMNLqgiqVPKGRCP--ILELLLIQSS 226
Cdd:PRK08294  476 RLADAKPVHLGHAATADGRWRIYAFADaaDPAGPGsALDALCEFLAE-SPDSPLRRF----TPSGADIdaVIDVRAIFQQ 550

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288 227 PRSAVNLLDLPELFHPFDHLTGW-DYWKAFADDR--DQAYKGYGIDKnGPGCLVLCRPDQHVAWIGSMENTSELDSYFSS 303
Cdd:PRK08294  551 PHRELDLEDVPALLLPRKGRFGLtDYEKVFCADLsgADIFDLRGIDR-DRGAVVVVRPDQYVANVLPLDAHAELAAFFAG 629


                  ..
gi 1021536288 304 IF 305
Cdd:PRK08294  630 FL 631
PHOX_C cd02979
FAD-dependent Phenol hydoxylase (PHOX) family, C-terminal TRX-fold domain; composed of ...
 142-304 3.52e-49

FAD-dependent Phenol hydoxylase (PHOX) family, C-terminal TRX-fold domain; composed of proteins similar to PHOX from the aerobic topsoil yeast Trichosporon cutaneum. PHOX is a flavoprotein monooxygenase that catalyzes the hydroxylation of phenol and simple phenol derivatives in the ortho position with the consumption of NADPH and oxygen. This is the first step in the biodegradation and detoxification of phenolic compounds. PHOX contains three domains. The substrate and FAD/NAD(P) binding sites are contained in the first two domains, which adopt a complicated folding pattern. The third or C-terminal domain contains a TRX fold and is involved in dimerization. The functional unit of PHOX is a dimer, although active tetramers of the recombinant enzyme can be isolated when overproduced in bacteria.


Pssm-ID: 239277 [Multi-domain]  Cd Length: 167  Bit Score: 161.30  E-value: 3.52e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288 142 GMRLPSFLVVYQCDGVPIHLAKRLVSDGPWRLLVFSGDLRQPERMNALAHFAETFSRcSHLMNLQGIQVPKGRCPILELL 221
Cdd:cd02979     1 GRRFPSAPVVRQADALPVHLGHRLPADGRFRIYVFAGDIAPAQQKSRLTQLCDALDS-PDSFPLRYTPRGADPDSVFDVV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288 222 LIQSSPRSAVNLLDLPELFHPFDHLTGWDYWKAFADDR------DQAYKGYGIDKNgPGCLVLCRPDQHVAWIGSMENTS 295
Cdd:cd02979    80 TIHAAPRREIELLDLPAVLRPFGEKKGWDYEKIYADDDsyheghGDAYEKYGIDPE-RGAVVVVRPDQYVALVGPLDDVE 158


                  ....*....
gi 1021536288 296 ELDSYFSSI 304
Cdd:cd02979   159 ALEAYFAGF 167
PRK06184 PRK06184
hypothetical protein; Provisional
 8-309 3.16e-36

hypothetical protein; Provisional


Pssm-ID: 235728 [Multi-domain]  Cd Length: 502  Bit Score: 135.88  E-value: 3.16e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288   8 RLVRHYRpHDRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAVItNGAQPTILETYETERRPVAKQLMTLDSRLVR 87
Cdd:PRK06184  273 RLADRYR-VGRVFLAGDAAHVHPPAGGQGLNTSVQDAYNLGWKLAAVL-AGAPEALLDTYEEERRPVAAAVLGLSTELLD 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288  88 AYEDEendnssgiyEVREQYAGfmAGIDITYPHSTLVTQGEEDGATnfaknLRLGMRLPSflvvYQCDGvPIHLAKRL-- 165
Cdd:PRK06184  351 AIKRG---------DMRRGRDV--QQLDLGYRGSSLAVDGPERTGG-----LRAGDRAPD----APLLG-AAGQPTRLfd 409

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288 166 VSDGP-WRLLVFSgdlrqPERMNALAHFAETFSRCshlmnlqGIQVPKGrcpilellliqssprsavnlldlpelfhpfd 244
Cdd:PRK06184  410 LFRGPhWTLLAFG-----AGAAAILARRGLRIHRV-------GDAAEGG------------------------------- 446

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1021536288 245 hltgwdywkAFADDRDQAYKGYGIdknGPGCLVLCRPDQHVAWIGSMENTSELDSYFSSiFGRSS 309
Cdd:PRK06184  447 ---------DLVDDAGHFRDAYGL---TGGTLVLVRPDGYVGLIAAGDDAAALEAYLAR-VGLGR 498
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 5-79 4.17e-31

FAD binding domain; This domain is involved in FAD binding in a number of enzymes.


Pssm-ID: 396193 [Multi-domain]  Cd Length: 348  Bit Score: 119.35  E-value: 4.17e-31
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1021536288   5 IGRRLVRHYRpHDRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAVITNGAQPTILETYETERRPVAKQLM 79
Cdd:pfam01494 272 VASRVATRYR-KGRVFLAGDAAHIHPPTGGQGLNTAIQDAFNLAWKLAAVLRGQAGESLLDTYSAERLPVAWAVV 345
PRK07190 PRK07190
FAD-binding protein;
12-124 3.90e-28

FAD-binding protein;


Pssm-ID: 235955 [Multi-domain]  Cd Length: 487  Bit Score: 113.37  E-value: 3.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288  12 HYRPHDRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAVITNGAQPTILETYETERRPVAKQLMTLDSRLVRAYED 91
Cdd:PRK07190  270 HFFIQDRIFLAGDACHIHSVNGGQGLNTGLADAFNLIWKLNMVIHHGASPELLQSYEAERKPVAQGVIETSGELVRSTKY 349

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1021536288  92 EENDNSSGIY-EVREQYAGFMAGIDITYPHSTLV 124
Cdd:PRK07190  350 SANGTHAQDYvKIVEKRAGYITGMGIRYGEEGLC 383
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 5-90 1.74e-26

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 106.18  E-value: 1.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288   5 IGRRLVRHYRpHDRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAVITNGAQPTILETYETERRPVAKQLMTLDSR 84
Cdd:COG0654   213 LRRRRAERWR-RGRVVLLGDAAHTMHPLGGQGANLALRDAAALAWKLAAALRGRDDEAALARYERERRPRAARVQRAADA 291


                  ....*.
gi 1021536288  85 LVRAYE 90
Cdd:COG0654   292 LGRLFH 297
PRK06834 PRK06834
hypothetical protein; Provisional
 18-118 1.29e-24

hypothetical protein; Provisional


Pssm-ID: 235870 [Multi-domain]  Cd Length: 488  Bit Score: 103.17  E-value: 1.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288  18 RVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAVITNGAQPTILETYETERRPVAKQ----------LMTLDSRlVR 87
Cdd:PRK06834  266 RVLLAGDAAHVHSPVGGQGLNTGVQDAVNLGWKLAQVVKGTSPESLLDTYHAERHPVAARvlrntmaqvaLLRPDDR-TE 344

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1021536288  88 AYEDEENDnSSGIYEVREQYAGFMAGIDITY 118
Cdd:PRK06834  345 ALRDIVAE-LLGMDEPRKRIAAMMSGLDIHY 374
PRK08244 PRK08244
monooxygenase;
8-190 3.52e-23

monooxygenase;


Pssm-ID: 236199 [Multi-domain]  Cd Length: 493  Bit Score: 99.05  E-value: 3.52e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288   8 RLVRHYRpHDRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAVITNGAQPTILETYETERRPVAKQLM------TL 81
Cdd:PRK08244  264 RQAERYR-SGRIFLAGDAAHIHFPAGGQGLNVGLQDAMNLGWKLAAAIKGWAPDWLLDSYHAERHPVGTALLrntevqTK 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288  82 DSRLVRAYEDEENDNSS--GIYEVREQYAGFMAGIDITYphstlvtqgEEDGatNFAKNLRLGMRLPSFLVVYQcDGVPI 159
Cdd:PRK08244  343 LFDFTRPGLALRSMLSDllGFPEVNRYLAGQISALDVHY---------EPDA--EMPPHPLNGKRLPDLELTLS-DGESE 410

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1021536288 160 HLAKrLVSDGPWRLLVFSGDLRQPERMNALA 190
Cdd:PRK08244  411 RLYS-LLHKGTFLLLSFGSEPQDWSRYPHVR 440
PRK06126 PRK06126
hypothetical protein; Provisional
 5-290 1.13e-22

hypothetical protein; Provisional


Pssm-ID: 235704 [Multi-domain]  Cd Length: 545  Bit Score: 97.76  E-value: 1.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288   5 IGRRLV-RHYRpHDRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAVITNGAQPTILETYETERRPVAKQLMTLDS 83
Cdd:PRK06126  291 TGRRLVaDSYR-RGRVFLAGDAAHLFTPTGGYGMNTGIGDAVNLAWKLAAVLNGWAGPALLDSYEAERRPIAARNTDYAR 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288  84 RLVRA------YEDEENDNSSG----------IYEV-REQYAgfMAGIDITY-----PHstLVTQGE---EDGATNFAKN 138
Cdd:PRK06126  370 RNADAlgsfpvPPEIEDDGPAGdaarrkvgdaLSEHaRQEFN--SPGITLGYrydgsPI--IVPDGTpppPDDPGVYVPS 445

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288 139 LRLGMRLPSFLVVyqcDGVPihLAKRLvsdGP-WRLLVFSGdlrqpeRMNALAHFAETFSRcshlmnlQGIQvpkgrcpi 217
Cdd:PRK06126  446 ACPGGRAPHAWLS---DGRS--LYDLF---GPgFTLLRFGD------AAVDVAPLEAAAAA-------LGVP-------- 496

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021536288 218 lellliqssprsaVNLLDLPElfhpfdhltgwdywkafaddrDQAYKGYGIDkngpgcLVLCRPDQHVAWIGS 290
Cdd:PRK06126  497 -------------LAVVDLPG---------------------PEAAALYEAD------LVLVRPDQHVAWRGD 529
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
8-81 4.83e-21

bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 93.05  E-value: 4.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288   8 RLVRH--YRPH---------DRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAVITNGAQPTILETYETERRPVAK 76
Cdd:PRK06183  266 ELIRHavYTFHarvadrwrsGRVLLAGDAAHLMPPFAGQGMNSGIRDAANLAWKLAAVLRGRAGDALLDTYEQERRPHAR 345


                  ....*
gi 1021536288  77 QLMTL 81
Cdd:PRK06183  346 AMIDL 350
PRK08132 PRK08132
FAD-dependent oxidoreductase; Provisional
 7-286 1.70e-17

FAD-dependent oxidoreductase; Provisional


Pssm-ID: 236158 [Multi-domain]  Cd Length: 547  Bit Score: 82.61  E-value: 1.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288   7 RRLVRhYRpHDRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAVITNGAQPTILETYETERRPVAKQ--------- 77
Cdd:PRK08132  291 RRMDR-FR-HGRVLFAGDAAHQVSPFGARGANSGIQDADNLAWKLALVLRGRAPDSLLDSYASEREFAADEnirnstrst 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288  78 -LMTLDSRLVRAYEDeendnssGIYEVREQYAGFMAGID-------ITYPHSTLVTQGEEDgatnFAKNLRLGMRLPSfl 149
Cdd:PRK08132  369 dFITPKSPVSRLFRD-------AVLRLARDHPFARRLVNsgrlsvpAVYADSPLNTPDGDA----FAGGPVPGAPAPD-- 435

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288 150 VVYQCDGVPIHLAKRLvsDGPWRLLVFSGDLRQPERMNALAhfaetfsrcshlmnlqGIQVPkgrcpiLELLLIQSSPRS 229
Cdd:PRK08132  436 APVRADGEPGWLLDLL--GGGFTLLLFGDDAAAAALLQALA----------------AAALP------VRVVAVVPAGAA 491

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1021536288 230 AVNLLDLpelfhpfdhltgwdywkafADDRDQAYKGYGIdknGPGCLVLCRPDQHVA 286
Cdd:PRK08132  492 QAAAGVL-------------------EDADGLAAERYDA---RPGTVYLIRPDQHVA 526
COQ6 TIGR01989
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase ...
 17-89 2.70e-08

ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase responsible for the 4-hydroxylateion of the phenol ring in the aerobic biosynthesis of ubiquinone


Pssm-ID: 273914 [Multi-domain]  Cd Length: 437  Bit Score: 54.76  E-value: 2.70e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1021536288  17 DRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAVITNGAQ---PTILETYETERRPVAKQLMTLDSRLVRAY 89
Cdd:TIGR01989 333 KRVALVGDAAHRVHPLAGQGVNLGFGDVASLVKALAEAVSVGADigsISSLKPYERERYAKNVVLLGLVDKLHKLY 408
Ubi-OHases TIGR01988
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ...
 3-89 2.66e-07

Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a family of FAD-dependent hydroxylases (monooxygenases) which are all believed to act in the aerobic ubiquinone biosynthesis pathway. A separate set of hydroxylases, as yet undiscovered, are believed to be active under anaerobic conditions. In E. coli three enzyme activities have been described, UbiB (which acts first at position 6, see TIGR01982), UbiH (which acts at position 4) and UbiF (which acts at position 5). UbiH and UbiF are similar to one another and form the basis of this subfamily. Interestingly, E. coli contains another hydroxylase gene, called visC, that is highly similar to UbiF, adjacent to UbiH and, when mutated, results in a phenotype similar to that of UbiH (which has also been named visB). Several other species appear to have three homologs in this family, although they assort themselves differently on phylogenetic trees (e.g. Xylella and Mesorhizobium) making it difficult to ascribe a specific activity to each one. Eukaryotes appear to have only a single homolog in this subfamily (COQ6) which complements UbiH, but also possess a non-orthologous gene, COQ7 which complements UbiF. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273913 [Multi-domain]  Cd Length: 385  Bit Score: 51.44  E-value: 2.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288   3 LKIGRRLVRHyrphdRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAVITNG---AQPTILETYETERRPVAKQLM 79
Cdd:TIGR01988 267 LTHAKRYVAP-----RLALIGDAAHTIHPLAGQGLNLGLRDVAALAEVLEDARRRGediGSLRVLQRYERRRRFDNAAML 341

                          90
                  ....*....|
gi 1021536288  80 TLDSRLVRAY 89
Cdd:TIGR01988 342 GATDGLNRLF 351
PRK07045 PRK07045
putative monooxygenase; Reviewed
 5-91 8.75e-07

putative monooxygenase; Reviewed


Pssm-ID: 136171 [Multi-domain]  Cd Length: 388  Bit Score: 49.91  E-value: 8.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288   5 IGR-RLVRHYRphDRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAVITNG-AQPTILETYETERRPVAKQLMTLD 82
Cdd:PRK07045  274 LGRmNLDRYHK--RNVVLLGDAAHSIHPITGQGMNLAIEDAGELGACLDLHLSGQiALADALERFERIRRPVNEAVISYG 351


                  ....*....
gi 1021536288  83 SRLVRAYED 91
Cdd:PRK07045  352 HALATTYHD 360
PRK06185 PRK06185
FAD-dependent oxidoreductase;
8-44 5.37e-06

FAD-dependent oxidoreductase;


Pssm-ID: 235729 [Multi-domain]  Cd Length: 407  Bit Score: 47.55  E-value: 5.37e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1021536288   8 RLVRHYRPHdrVFLAGDAAHTHSPKGGQGMNVSIQDA 44
Cdd:PRK06185  277 RLRRWHRPG--LLCIGDAAHAMSPVGGVGINLAIQDA 311
PRK07364 PRK07364
FAD-dependent hydroxylase;
6-73 6.59e-06

FAD-dependent hydroxylase;


Pssm-ID: 236001 [Multi-domain]  Cd Length: 415  Bit Score: 47.32  E-value: 6.59e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021536288   6 GRRLVRHyrphdRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLI------WKLGAVItnGAQpTILETYETERRP 73
Cdd:PRK07364  288 SDRYVQH-----RLALVGDAAHCCHPVGGQGLNLGIRDAAALAqvlqtaHQRGEDI--GSL-AVLKRYERWRKR 353
PRK07333 PRK07333
ubiquinone biosynthesis hydroxylase;
18-91 7.28e-06

ubiquinone biosynthesis hydroxylase;


Pssm-ID: 180935 [Multi-domain]  Cd Length: 403  Bit Score: 46.90  E-value: 7.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288  18 RVFLAGDAAHTHSPKGGQGMNVSIQDAYnliwKLGAVITNGA-------QPTILETYETERRP----------VAKQLMT 80
Cdd:PRK07333  281 RFALVGDAAHGIHPIAGQGLNLGLKDVA----ALAEVVVEAArlgldigSLDVLERYQRWRRFdtvrmgvttdVLNRLFS 356

                          90
                  ....*....|.
gi 1021536288  81 LDSRLVRAYED 91
Cdd:PRK07333  357 NDSTLLRSVRD 367
PRK05732 PRK05732
2-octaprenyl-6-methoxyphenyl hydroxylase; Validated
 3-87 3.72e-05

2-octaprenyl-6-methoxyphenyl hydroxylase; Validated


Pssm-ID: 235584 [Multi-domain]  Cd Length: 395  Bit Score: 44.84  E-value: 3.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288   3 LKIGRRLVRHyrphdRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAVITNGAQP---TILETYETERRPVAKQLM 79
Cdd:PRK05732  273 LVTAAQQISH-----RLALVGNAAQTLHPIAGQGFNLGLRDVMSLAETLTQALARGEDIgdyAVLQRYQQRRQQDREATI 347


                  ....*...
gi 1021536288  80 TLDSRLVR 87
Cdd:PRK05732  348 GFTDGLVR 355
PRK07538 PRK07538
hypothetical protein; Provisional
 16-78 6.17e-05

hypothetical protein; Provisional


Pssm-ID: 236046 [Multi-domain]  Cd Length: 413  Bit Score: 44.12  E-value: 6.17e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021536288  16 HDRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAvitNGAQPTILETYETERRPVAKQL 78
Cdd:PRK07538  296 RGRVTLLGDAAHPMYPVGSNGASQAILDARALADALAA---HGDPEAALAAYEAERRPATAQI 355
PRK08849 PRK08849
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
 7-73 8.51e-05

2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional


Pssm-ID: 181564 [Multi-domain]  Cd Length: 384  Bit Score: 43.61  E-value: 8.51e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021536288   7 RRLVRHYRPHdRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIwklgAVITNGAQPTI--LETYETERRP 73
Cdd:PRK08849  270 RRHAQQYVKN-NCVLLGDAAHTINPLAGQGVNLGFKDVDVLL----AETEKQGVLNDasFARYERRRRP 333
PRK08773 PRK08773
UbiH/UbiF family hydroxylase;
7-72 9.75e-05

UbiH/UbiF family hydroxylase;


Pssm-ID: 181552 [Multi-domain]  Cd Length: 392  Bit Score: 43.70  E-value: 9.75e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1021536288   7 RRLVRHYRPhDRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAVITNGAQ---PTILETYETERR 72
Cdd:PRK08773  273 RQLVQQYVS-GRVLTLGDAAHVVHPLAGQGVNLGLRDVAALQQLVRQAHARRADwaaPHRLQRWARTRR 340
PRK08243 PRK08243
4-hydroxybenzoate 3-monooxygenase; Validated
 16-58 1.43e-04

4-hydroxybenzoate 3-monooxygenase; Validated


Pssm-ID: 236198 [Multi-domain]  Cd Length: 392  Bit Score: 42.86  E-value: 1.43e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1021536288  16 HDRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAVITNG 58
Cdd:PRK08243  278 YGRLFLAGDAAHIVPPTGAKGLNLAASDVRYLARALVEFYREG 320
PRK07494 PRK07494
UbiH/UbiF family hydroxylase;
17-73 1.50e-04

UbiH/UbiF family hydroxylase;


Pssm-ID: 181001 [Multi-domain]  Cd Length: 388  Bit Score: 42.97  E-value: 1.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1021536288  17 DRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAVITNGAQPTILETYETERRP 73
Cdd:PRK07494  280 GRTALVGEAAHVFPPIGAQGLNLGLRDVATLVEIVEDRPEDPGSAAVLAAYDRARRP 336
PRK08850 PRK08850
2-octaprenyl-6-methoxyphenol hydroxylase; Validated
 17-80 2.36e-04

2-octaprenyl-6-methoxyphenol hydroxylase; Validated


Pssm-ID: 236341 [Multi-domain]  Cd Length: 405  Bit Score: 42.45  E-value: 2.36e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288  17 DRVFLAGDAAHTHSPKGGQGMNVSIQDAYNL------IWKLGAVItngAQPTILETYETERRPVAKQLMT 80
Cdd:PRK08850  282 ERVALVGDAAHTIHPLAGQGVNLGLLDAASLaqeilaLWQQGRDI---GLKRNLRGYERWRKAEAAKMIA 348
PRK08013 PRK08013
oxidoreductase; Provisional
 8-72 5.11e-04

oxidoreductase; Provisional


Pssm-ID: 236139 [Multi-domain]  Cd Length: 400  Bit Score: 41.18  E-value: 5.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1021536288   8 RLVRHYRPHdRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAVITNG---AQPTILETYETERR 72
Cdd:PRK08013  274 RYARQFAAH-RLALVGDAAHTIHPLAGQGVNLGFMDAAELIAELRRLHRQGkdiGQHLYLRRYERSRK 340
PRK07608 PRK07608
UbiH/UbiF family hydroxylase;
18-80 5.71e-04

UbiH/UbiF family hydroxylase;


Pssm-ID: 181057 [Multi-domain]  Cd Length: 388  Bit Score: 41.09  E-value: 5.71e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1021536288  18 RVFLAGDAAHTHSPKGGQGMNVSIQDAYnliwKLGAVItNGAQP-------TILETYETERR--PVAKQLMT 80
Cdd:PRK07608  281 RVALVGDAAHLIHPLAGQGMNLGLRDVA----ALADVL-AGREPfrdlgdlRLLRRYERARRedILALQVAT 347
PRK08255 PRK08255
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
11-110 1.81e-03

bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;


Pssm-ID: 236203 [Multi-domain]  Cd Length: 765  Bit Score: 39.92  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021536288  11 RHYRPHDRVFLAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAviTNGAQPTILETYETERRPVAkqlmtldSRLVRAYE 90
Cdd:PRK08255  263 VHWNRRVPVVLMGDAAHTAHFSIGSGTKLALEDAIELARCLHE--HPGDLPAALAAYEEERRVEV-------LRIQNAAR 333

                          90       100
                  ....*....|....*....|
gi 1021536288  91 deendNSSGIYEVREQYAGF 110
Cdd:PRK08255  334 -----NSTEWFENVERYAGL 348
PRK05714 PRK05714
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
 21-80 6.28e-03

2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional


Pssm-ID: 168201 [Multi-domain]  Cd Length: 405  Bit Score: 37.89  E-value: 6.28e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1021536288  21 LAGDAAHTHSPKGGQGMNVSIQDAYNLIWKLGAVITNGAQPT---ILETYETERRPVAKQLMT 80
Cdd:PRK05714  289 LIGDAAHTIHPLAGQGVNLGFLDAAVLAEVLLHAAERGERLAdvrVLSRFERRRMPHNLALMA 351
PRK06617 PRK06617
2-octaprenyl-6-methoxyphenyl hydroxylase; Validated
 16-72 7.79e-03

2-octaprenyl-6-methoxyphenyl hydroxylase; Validated


Pssm-ID: 168629 [Multi-domain]  Cd Length: 374  Bit Score: 37.60  E-value: 7.79e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1021536288  16 HDRVFLAGDAAHTHSPKGGQGMNVSIQDaynlIWKLGAVITNGAqptILETYETERR 72
Cdd:PRK06617  272 HNRIVLIADTAHTVHPLAGQGLNQGIKD----IEILSMIVSNNG---TLQEYQKLRQ 321
 
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