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Conserved domains on  [gi|197245788|gb|AAI68676|]
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Pcyox1l protein [Rattus norvegicus]

Protein Classification

prenylcysteine oxidase family protein( domain architecture ID 10602892)

prenylcysteine oxidase family protein similar to Arabidopsis thaliana farnesylcysteine lyase that cleaves specifically the thioether bond of S-farnesyl-L-cysteine and has no activity with S-geranylgeranyl-L-cysteine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Prenylcys_lyase pfam07156
Prenylcysteine lyase; This family contains prenylcysteine lyases (EC:1.8.3.5) that are ...
 120-483 0e+00

Prenylcysteine lyase; This family contains prenylcysteine lyases (EC:1.8.3.5) that are approximately 500 residues long. Prenylcysteine lyase is a FAD-dependent thioether oxidase that degrades a variety of prenylcysteines, producing free cysteine, an isoprenoid aldehyde and hydrogen peroxide as products of the reaction. It has been noted that this enzyme has considerable homology with ClP55, a 55 kDa protein that is associated with chloride ion pumps.


:

Pssm-ID: 462104 [Multi-domain]  Cd Length: 364  Bit Score: 556.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788  120 LEETDWYLLNLFRLWWYYGISFLRLQMWVEEVMEKFMRIYKYQAHGYAFSGTEELLYSLGEATFVNMTQRSVAESLLQVG 199
Cdd:pfam07156   1 FEESSWSWINLAKLLWRYGFSPLRMQMWVEDILDKFMRIYEYQAHGYAFSSVEELLHALGGDGFLNLTNQTLEEALLKAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788  200 VTQRFIDDVVSAVLRASYGQSASMPAFAGAMSLAGAQGNLWSVEGGNKLVCSGLLKLAKATVIHATVTSVTL-HSTEGKA 278
Cdd:pfam07156  81 FSQLFINEIVQAVTRVNYGQSVNINGFVGAVSLAGAQSGLWAVEGGNKLVCSGLLKASKANLINGTVTSIELkQSGGSTS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788  279 LYQVGYETDKGNSSDFYDIVVIATPLHldNSSSNITFEGFTPPIDDIQGSFQPTVVSLVHGYLNSSYFGFPDPKLFPFAN 358
Cdd:pfam07156 161 LYEVTYKTESGTHSDLYDIVVIATPLH--RKMSNITFDNFSPPIPEFPGPYQHTVATLVHGRLNPSYFGLPDPSLFPLAT 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788  359 ILTTDFPS-FFCSLDNICPVNISASFRRKQPQEAAVWRVQSPKPLFRTELKTLFRSYYSVQTAEWQAHPLYGSRRTLPKF 437
Cdd:pfam07156 239 ILTTDNPSlFINSISSVSPVNISDNPRRKPPKEAAVWKIFSPEPLSKEQLKSLFSSYDSVQEKDWLAYPHYSPPETFPPF 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 197245788  438 ALHDQLFYLNALEWAASSVEVAAVAAKNVALLAYNRWYQDLDKIDQ 483
Cdd:pfam07156 319 ILHDGLYYLNGIEWAASAMEMSAIAAKNVALLAYHRWYGNTDKIDQ 364
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
31-96 1.80e-09

NAD(P)-binding Rossmann-like domain;


:

Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 53.69  E-value: 1.80e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 197245788   31 VIGAGIGGSAVAHFLQQHfgpRVQIVVYEKGT-VGGRLATISVNKQNYESGAASFHSLS-LHMQDFVK 96
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKR---GFRVLVLEKRDrLGGNAYSYRVPGYVFDYGAHIFHGSDePNVRDLLD 65
 
Name Accession Description Interval E-value
Prenylcys_lyase pfam07156
Prenylcysteine lyase; This family contains prenylcysteine lyases (EC:1.8.3.5) that are ...
 120-483 0e+00

Prenylcysteine lyase; This family contains prenylcysteine lyases (EC:1.8.3.5) that are approximately 500 residues long. Prenylcysteine lyase is a FAD-dependent thioether oxidase that degrades a variety of prenylcysteines, producing free cysteine, an isoprenoid aldehyde and hydrogen peroxide as products of the reaction. It has been noted that this enzyme has considerable homology with ClP55, a 55 kDa protein that is associated with chloride ion pumps.


Pssm-ID: 462104 [Multi-domain]  Cd Length: 364  Bit Score: 556.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788  120 LEETDWYLLNLFRLWWYYGISFLRLQMWVEEVMEKFMRIYKYQAHGYAFSGTEELLYSLGEATFVNMTQRSVAESLLQVG 199
Cdd:pfam07156   1 FEESSWSWINLAKLLWRYGFSPLRMQMWVEDILDKFMRIYEYQAHGYAFSSVEELLHALGGDGFLNLTNQTLEEALLKAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788  200 VTQRFIDDVVSAVLRASYGQSASMPAFAGAMSLAGAQGNLWSVEGGNKLVCSGLLKLAKATVIHATVTSVTL-HSTEGKA 278
Cdd:pfam07156  81 FSQLFINEIVQAVTRVNYGQSVNINGFVGAVSLAGAQSGLWAVEGGNKLVCSGLLKASKANLINGTVTSIELkQSGGSTS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788  279 LYQVGYETDKGNSSDFYDIVVIATPLHldNSSSNITFEGFTPPIDDIQGSFQPTVVSLVHGYLNSSYFGFPDPKLFPFAN 358
Cdd:pfam07156 161 LYEVTYKTESGTHSDLYDIVVIATPLH--RKMSNITFDNFSPPIPEFPGPYQHTVATLVHGRLNPSYFGLPDPSLFPLAT 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788  359 ILTTDFPS-FFCSLDNICPVNISASFRRKQPQEAAVWRVQSPKPLFRTELKTLFRSYYSVQTAEWQAHPLYGSRRTLPKF 437
Cdd:pfam07156 239 ILTTDNPSlFINSISSVSPVNISDNPRRKPPKEAAVWKIFSPEPLSKEQLKSLFSSYDSVQEKDWLAYPHYSPPETFPPF 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 197245788  438 ALHDQLFYLNALEWAASSVEVAAVAAKNVALLAYNRWYQDLDKIDQ 483
Cdd:pfam07156 319 ILHDGLYYLNGIEWAASAMEMSAIAAKNVALLAYHRWYGNTDKIDQ 364
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 28-305 7.44e-10

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 61.00  E-value: 7.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788  28 KIAVIGAGIGGSAVAHFLQQHfgpRVQIVVYEKG-TVGGRLATISVNKQNYESGAASFHSLSLHMQDFVKLLGLRQRREV 106
Cdd:COG1232    3 RVAVIGGGIAGLTAAYRLAKA---GHEVTVLEASdRVGGLIRTVEVDGFRIDRGPHSFLTRDPEVLELLRELGLGDELVW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788 107 V--GRSAIF-GGEHFVLEETDWYLL--NLFRLW--WYYGISFLRLQMWVEEVM--EKFMRiykyqahgyafsgteellYS 177
Cdd:COG1232   80 PntRKSYIYyGGKLHPLPQGPLALLrsPLLSLAgkLRALLELLAPRRPPGEDEslAEFVR------------------RR 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788 178 LGEatfvnmtqrsvaesllqvGVTQRFIDDVVSAVlrasYGQSAS-------MPAFAGAM----SL----------AGAQ 236
Cdd:COG1232  142 FGR------------------EVYERLVEPLLEGV----YAGDPDelsadwaFPRLKRLElehgSLikgalalrkgAKAG 199

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 197245788 237 GNLWSVEGGNKLVCSGLLKLAKATVIH--ATVTSVTLHSTEgkalYQVgyETDKGNSSDfYDIVVIATPLH 305
Cdd:COG1232  200 EVFGYLRGGLGTLVEALAEALEAGEIRlgTRVTAIEREGGG----WRV--TTSDGETIE-ADAVVSATPAP 263
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
31-96 1.80e-09

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 53.69  E-value: 1.80e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 197245788   31 VIGAGIGGSAVAHFLQQHfgpRVQIVVYEKGT-VGGRLATISVNKQNYESGAASFHSLS-LHMQDFVK 96
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKR---GFRVLVLEKRDrLGGNAYSYRVPGYVFDYGAHIFHGSDePNVRDLLD 65
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
28-124 3.45e-09

Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 58.35  E-value: 3.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788  28 KIAVIGAGIGGSAVAHFLQQHfGPRVQivVYEKGT-VGGRLATISVNKQNYESGAASFHSLSLHMQDFVKLLglrQRREV 106
Cdd:COG3380    5 DIAIIGAGIAGLAAARALQDA-GHEVT--VFEKSRgVGGRMATRRLDGGRFDHGAQYFTARDPRFQALVEEW---LAAGL 78

                         90       100
                 ....*....|....*....|..
gi 197245788 107 V----GRSAIFGGEHFVLEETD 124
Cdd:COG3380   79 VapwtFDFVVLDADGLVSPRDD 100
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
 28-113 6.96e-07

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 51.39  E-value: 6.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788  28 KIAVIGAGIGGSAVAHFLQQHFgPRVQIVVYEKGT-VGGRLATISVNKQNYESGAASFHSLSLHMQDFVKLLGL--RQRR 104
Cdd:PRK11883   2 KVAIIGGGITGLSAAYRLHKKG-PDADITLLEASDrLGGKIQTVRKDGFPIELGPESFLARKPSAPALVKELGLedELVA 80


                 ....*....
gi 197245788 105 EVVGRSAIF 113
Cdd:PRK11883  81 NTTGQSYIY 89
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
 28-100 6.48e-06

protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 213540 [Multi-domain]  Cd Length: 462  Bit Score: 48.68  E-value: 6.48e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 197245788   28 KIAVIGAGIGGSAVAHFL-QQHFGPRVQIVVYEKGT-VGGRLATISVNKQNYESGAASFHSLSLHMQDFVKLLGL 100
Cdd:TIGR00562   4 HVVIIGGGISGLCAAYYLeKEIPELPVELTLVEASDrVGGKIQTVKEDGYLIERGPDSFLERKKSAPDLVKDLGL 78
 
Name Accession Description Interval E-value
Prenylcys_lyase pfam07156
Prenylcysteine lyase; This family contains prenylcysteine lyases (EC:1.8.3.5) that are ...
 120-483 0e+00

Prenylcysteine lyase; This family contains prenylcysteine lyases (EC:1.8.3.5) that are approximately 500 residues long. Prenylcysteine lyase is a FAD-dependent thioether oxidase that degrades a variety of prenylcysteines, producing free cysteine, an isoprenoid aldehyde and hydrogen peroxide as products of the reaction. It has been noted that this enzyme has considerable homology with ClP55, a 55 kDa protein that is associated with chloride ion pumps.


Pssm-ID: 462104 [Multi-domain]  Cd Length: 364  Bit Score: 556.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788  120 LEETDWYLLNLFRLWWYYGISFLRLQMWVEEVMEKFMRIYKYQAHGYAFSGTEELLYSLGEATFVNMTQRSVAESLLQVG 199
Cdd:pfam07156   1 FEESSWSWINLAKLLWRYGFSPLRMQMWVEDILDKFMRIYEYQAHGYAFSSVEELLHALGGDGFLNLTNQTLEEALLKAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788  200 VTQRFIDDVVSAVLRASYGQSASMPAFAGAMSLAGAQGNLWSVEGGNKLVCSGLLKLAKATVIHATVTSVTL-HSTEGKA 278
Cdd:pfam07156  81 FSQLFINEIVQAVTRVNYGQSVNINGFVGAVSLAGAQSGLWAVEGGNKLVCSGLLKASKANLINGTVTSIELkQSGGSTS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788  279 LYQVGYETDKGNSSDFYDIVVIATPLHldNSSSNITFEGFTPPIDDIQGSFQPTVVSLVHGYLNSSYFGFPDPKLFPFAN 358
Cdd:pfam07156 161 LYEVTYKTESGTHSDLYDIVVIATPLH--RKMSNITFDNFSPPIPEFPGPYQHTVATLVHGRLNPSYFGLPDPSLFPLAT 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788  359 ILTTDFPS-FFCSLDNICPVNISASFRRKQPQEAAVWRVQSPKPLFRTELKTLFRSYYSVQTAEWQAHPLYGSRRTLPKF 437
Cdd:pfam07156 239 ILTTDNPSlFINSISSVSPVNISDNPRRKPPKEAAVWKIFSPEPLSKEQLKSLFSSYDSVQEKDWLAYPHYSPPETFPPF 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 197245788  438 ALHDQLFYLNALEWAASSVEVAAVAAKNVALLAYNRWYQDLDKIDQ 483
Cdd:pfam07156 319 ILHDGLYYLNGIEWAASAMEMSAIAAKNVALLAYHRWYGNTDKIDQ 364
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 28-305 7.44e-10

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 61.00  E-value: 7.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788  28 KIAVIGAGIGGSAVAHFLQQHfgpRVQIVVYEKG-TVGGRLATISVNKQNYESGAASFHSLSLHMQDFVKLLGLRQRREV 106
Cdd:COG1232    3 RVAVIGGGIAGLTAAYRLAKA---GHEVTVLEASdRVGGLIRTVEVDGFRIDRGPHSFLTRDPEVLELLRELGLGDELVW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788 107 V--GRSAIF-GGEHFVLEETDWYLL--NLFRLW--WYYGISFLRLQMWVEEVM--EKFMRiykyqahgyafsgteellYS 177
Cdd:COG1232   80 PntRKSYIYyGGKLHPLPQGPLALLrsPLLSLAgkLRALLELLAPRRPPGEDEslAEFVR------------------RR 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788 178 LGEatfvnmtqrsvaesllqvGVTQRFIDDVVSAVlrasYGQSAS-------MPAFAGAM----SL----------AGAQ 236
Cdd:COG1232  142 FGR------------------EVYERLVEPLLEGV----YAGDPDelsadwaFPRLKRLElehgSLikgalalrkgAKAG 199

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 197245788 237 GNLWSVEGGNKLVCSGLLKLAKATVIH--ATVTSVTLHSTEgkalYQVgyETDKGNSSDfYDIVVIATPLH 305
Cdd:COG1232  200 EVFGYLRGGLGTLVEALAEALEAGEIRlgTRVTAIEREGGG----WRV--TTSDGETIE-ADAVVSATPAP 263
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
31-96 1.80e-09

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 53.69  E-value: 1.80e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 197245788   31 VIGAGIGGSAVAHFLQQHfgpRVQIVVYEKGT-VGGRLATISVNKQNYESGAASFHSLS-LHMQDFVK 96
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKR---GFRVLVLEKRDrLGGNAYSYRVPGYVFDYGAHIFHGSDePNVRDLLD 65
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
28-124 3.45e-09

Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 58.35  E-value: 3.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788  28 KIAVIGAGIGGSAVAHFLQQHfGPRVQivVYEKGT-VGGRLATISVNKQNYESGAASFHSLSLHMQDFVKLLglrQRREV 106
Cdd:COG3380    5 DIAIIGAGIAGLAAARALQDA-GHEVT--VFEKSRgVGGRMATRRLDGGRFDHGAQYFTARDPRFQALVEEW---LAAGL 78

                         90       100
                 ....*....|....*....|..
gi 197245788 107 V----GRSAIFGGEHFVLEETD 124
Cdd:COG3380   79 VapwtFDFVVLDADGLVSPRDD 100
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 28-306 1.34e-07

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 54.09  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788  28 KIAVIGAGIGGSAVAHFLQQHfGPRVqiVVYEK-GTVGGRLATISVNKQNYESGaASFHSLSLHMQDFVKLLGLRQRREV 106
Cdd:COG1233    5 DVVVIGAGIGGLAAAALLARA-GYRV--TVLEKnDTPGGRARTFERPGFRFDVG-PSVLTMPGVLERLFRELGLEDYLEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788 107 VGRSAIF-----GGEHFVLEETDWYLLNLFRlwwyyGIS------FLRLQMWVEEVMEKFMRIYKYQahgyAFSGTEELL 175
Cdd:COG1233   81 VPLDPAYrvpfpDGRALDLPRDLERTAAELE-----RLFpgdaeaYRRFLAELRRLYDALLEDLLYR----PLLSLRDLL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788 176 YSLGEATFVNMTQRSVAESLlqvgvTQRFIDDVVSAVLRAS---YGQSA-SMPAFAGAMSLAGAQGNLWSVEGGNKLVCS 251
Cdd:COG1233  152 RPLALARLLRLLLRSLRDLL-----RRYFKDPRLRALLAGQalyLGLSPdRTPALYALIAYLEYAGGVWYPKGGMGALAD 226

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 197245788 252 GLLKLAKAT--VIH--ATVTSVTLHSteGKAlyqVGYETDKGnsSDFY-DIVVI-ATPLHL 306
Cdd:COG1233  227 ALARLAEELggEIRtgAEVERILVEG--GRA---TGVRLADG--EEIRaDAVVSnADPAHT 280
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
28-306 3.45e-07

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 52.62  E-value: 3.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788  28 KIAVIGAGIGGSAVAHFLQQHfGPRVqiVVYEKGT-VGGRLATISVNKQNY--ESGAASFHSLSLHMQDFVKLLGL--RQ 102
Cdd:COG1231    9 DVVIVGAGLAGLAAARELRKA-GLDV--TVLEARDrVGGRVWTLRFGDDGLyaELGAMRIPPSHTNLLALARELGLplEP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788 103 RREVVGRSAI-FGGEHFVLEETDWYLLNLFRLWWyygisflrlqmWVEEVMEKFMRIYKYQAHGYafsgteellyslgea 181
Cdd:COG1231   86 FPNENGNALLyLGGKRVRAGEIAADLRGVAELLA-----------KLLRALAAALDPWAHPAAEL--------------- 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788 182 tfvnmTQRSVAESLLQVGVTQRFIdDVVSAVLRASYGQSA---SMPAFAGAMSLAGAQGNLWSVEGGNKLVCSGLLKLAK 258
Cdd:COG1231  140 -----DRESLAEWLRRNGASPSAR-RLLGLLGAGEYGADPdelSLLDLLRYAASAGGGAQQFRIVGGMDQLPRALAAELG 213

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 197245788 259 ATVIHAT-VTS-------VTLHSTEGKALYqvgyetdkgnssdfYDIVVIATPLHL 306
Cdd:COG1231  214 DRIRLGApVTRirqdgdgVTVTTDDGGTVR--------------ADAVIVTVPPSV 255
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
 28-113 6.96e-07

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 51.39  E-value: 6.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788  28 KIAVIGAGIGGSAVAHFLQQHFgPRVQIVVYEKGT-VGGRLATISVNKQNYESGAASFHSLSLHMQDFVKLLGL--RQRR 104
Cdd:PRK11883   2 KVAIIGGGITGLSAAYRLHKKG-PDADITLLEASDrLGGKIQTVRKDGFPIELGPESFLARKPSAPALVKELGLedELVA 80


                 ....*....
gi 197245788 105 EVVGRSAIF 113
Cdd:PRK11883  81 NTTGQSYIY 89
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 36-372 2.57e-06

Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.


Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 49.80  E-value: 2.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788   36 IGGSAVAHFLQQHfGPRVqiVVYE-KGTVGGRLATISVNKQNYESGAASFHSLSLHMQDFVKLLGLrQRREVVGRSAIFg 114
Cdd:pfam01593   1 LAGLAAARELLRA-GHDV--TVLEaRDRVGGRIRTVRDDGFLIELGAMWFHGAQPPLLALLKELGL-EDRLVLPDPAPF- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788  115 gehfvleetdwyllnlFRLWWYYGISFLRLQMWVEEVMEKFMRIYKYQAHGYAFSGTEELLYSLGEATFVNMTqRSVAES 194
Cdd:pfam01593  76 ----------------YTVLFAGGRRYPGDFRRVPAGWEGLLEFGRLLSIPEKLRLGLAALASDALDEFDLDD-FSLAES 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788  195 LLQVG--------VTQRFIDD-------VVSAVLRASYGQSASMPAFAGAMSLAGAQGNLWSVEGGNKLVCSGLLKLAKA 259
Cdd:pfam01593 139 LLFLGrrgpgdveVWDRLIDPelfaalpFASGAFAGDPSELSAGLALPLLWALLGEGGSLLLPRGGLGALPDALAAQLLG 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788  260 TVIH--ATVTSVTLHSTEGKALYQVGyetdkgnSSDFYDIVVIATPLhldnssSNITFEGFTPPIDD-----IQGSFQPT 332
Cdd:pfam01593 219 GDVRlnTRVRSIDREGDGVTVTLTDG-------EVIEADAVIVTVPL------GVLKRILFTPPLPPekaraIRNLGYGP 285

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 197245788  333 VVSLVHGYlnSSYFgFPDPKLFPFANILTTDFPSFFCSLD 372
Cdd:pfam01593 286 VNKVHLEF--DRKF-WPDLGLLGLLSELLTGLGTAFSWLT 322
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
 28-100 6.48e-06

protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 213540 [Multi-domain]  Cd Length: 462  Bit Score: 48.68  E-value: 6.48e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 197245788   28 KIAVIGAGIGGSAVAHFL-QQHFGPRVQIVVYEKGT-VGGRLATISVNKQNYESGAASFHSLSLHMQDFVKLLGL 100
Cdd:TIGR00562   4 HVVIIGGGISGLCAAYYLeKEIPELPVELTLVEASDrVGGKIQTVKEDGYLIERGPDSFLERKKSAPDLVKDLGL 78
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
28-72 8.88e-06

Predicted flavin-containing amine oxidase [General function prediction only];


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 47.80  E-value: 8.88e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 197245788  28 KIAVIGAGIGGSAVAHFLQQHFgprvQIVVYEKGT-VGGRLATISV 72
Cdd:COG2907    5 RIAVIGSGISGLTAAWLLSRRH----DVTLFEANDrLGGHTHTVDV 46
PLN02576 PLN02576
protoporphyrinogen oxidase
 30-84 1.43e-04

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 44.23  E-value: 1.43e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 197245788  30 AVIGAGIGGSAVAHFLQQHFGPRVqiVVYE-KGTVGGRLATISVNKQNYESGAASF 84
Cdd:PLN02576  16 AVVGAGVSGLAAAYALASKHGVNV--LVTEaRDRVGGNITSVSEDGFIWEEGPNSF 69
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
28-65 7.94e-04

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 41.81  E-value: 7.94e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 197245788  28 KIAVIGAGIGGSAVAHFLQQHfGprVQIVVYEKGTVGG 65
Cdd:COG0665    4 DVVVIGGGIAGLSTAYHLARR-G--LDVTVLERGRPGS 38
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 29-65 1.54e-03

Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];


Pssm-ID: 441675 [Multi-domain]  Cd Length: 414  Bit Score: 41.00  E-value: 1.54e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 197245788  29 IAVIGAGIGGSAVAHFLQQHfGPRVqiVVYEKGT-VGG 65
Cdd:COG2072    9 VVVIGAGQAGLAAAYHLRRA-GIDF--VVLEKADdVGG 43
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 28-128 2.23e-03

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 40.07  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 197245788   28 KIAVIGAGIGGSAVAHFLQQHfGPRVqiVVYEKGTVGGRlATISVNkqnyeSGAASFHSLSLHMQDFVKL--LGLRQRRE 105
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARR-GLSV--TLLERGDDPGS-GASGRN-----AGLIHPGLRYLEPSELARLalEALDLWEE 71

                          90       100
                  ....*....|....*....|...
gi 197245788  106 VVGRSAIfggeHFVLEETDWYLL 128
Cdd:pfam01266  72 LEEELGI----DCGFRRCGVLVL 90
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 28-60 3.25e-03

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: 39.54  E-value: 3.25e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 197245788  28 KIAVIGAGIGGSAVAHFLQQHFgprVQIVVYEK 60
Cdd:COG0654    5 DVLIVGGGPAGLALALALARAG---IRVTVVER 34
PRK07233 PRK07233
hypothetical protein; Provisional
 28-69 3.61e-03

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 39.87  E-value: 3.61e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 197245788  28 KIAVIGAGIGGSAVAHFLQQHfGPRVqiVVYEK-GTVGGRLAT 69
Cdd:PRK07233   1 KIAIVGGGIAGLAAAYRLAKR-GHEV--TVFEAdDQLGGLAAS 40
 
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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