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Conserved domains on  [gi|1678214323|ref|NP_001352330|]
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protoporphyrinogen oxidase isoform 4 [Homo sapiens]

Protein Classification

protoporphyrinogen/coproporphyrinogen oxidase( domain architecture ID 11440906)

protoporphyrinogen/coproporphyrinogen oxidase is a FAD-dependent enzyme that catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX or the oxidation of coproporphyrinogen III to coproporphyrin III, respectively

CATH:  3.50.50.60|3.50.50.60|1.10.3110.10|3.90.660.20
EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0009055|GO:0006779|GO:0071949
PubMed:  10944103
SCOP:  4000128|3000055|4000128

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 1-311 7.55e-55

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: 184.27  E-value: 7.55e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323   1 MDSLCRGVFAGNSRELSIRSCFPSLFQAEQTHRSillglllgagrtpqpdsaLIRQALAERWSQ------WSLRGGLEML 74
Cdd:COG1232   151 VEPLLEGVYAGDPDELSADWAFPRLKRLELEHGS------------------LIKGALALRKGAkagevfGYLRGGLGTL 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323  75 PQALETHLtsRGVSVLRGQPVCGLSlQAEGRWKVSLRD-SSLEADHVISAIPASVLSELLPAEAAPLARALSAITAVSVA 153
Cdd:COG1232   213 VEALAEAL--EAGEIRLGTRVTAIE-REGGGWRVTTSDgETIEADAVVSATPAPALARLLAPLPPEVAAALAGIPYASVA 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323 154 VVNLQYQGAHL-PVQGFGHLVPSSEDPGVLGIVYDSVAFPEQdgSPPGLR-VTVMLGGSWLQTLEAsgcvLSQELFQQRA 231
Cdd:COG1232   290 VVALGFDRPDLpPPDGFGWLVPRDEGVPILAVTFSSNKWPHR--APDGKVlLRLEVGGAGDPELWQ----LSDEELVALA 363

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323 232 QEAAATQLGLKEMPSHCLVHLHKNCIPQYTLGHWQKLESARQFLTAHRlPLTLAGASYEGVAVNDCIESGRQAAVSVLGT 311
Cdd:COG1232   364 LADLRKLLGIDAEPVDTRVVRWPKAYPQYTVGHLERVAAIREALAALP-GLYLAGRAYDGVGLPDCIRSGREAAERILAE 442
 
Name Accession Description Interval E-value
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 1-311 7.55e-55

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: 184.27  E-value: 7.55e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323   1 MDSLCRGVFAGNSRELSIRSCFPSLFQAEQTHRSillglllgagrtpqpdsaLIRQALAERWSQ------WSLRGGLEML 74
Cdd:COG1232   151 VEPLLEGVYAGDPDELSADWAFPRLKRLELEHGS------------------LIKGALALRKGAkagevfGYLRGGLGTL 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323  75 PQALETHLtsRGVSVLRGQPVCGLSlQAEGRWKVSLRD-SSLEADHVISAIPASVLSELLPAEAAPLARALSAITAVSVA 153
Cdd:COG1232   213 VEALAEAL--EAGEIRLGTRVTAIE-REGGGWRVTTSDgETIEADAVVSATPAPALARLLAPLPPEVAAALAGIPYASVA 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323 154 VVNLQYQGAHL-PVQGFGHLVPSSEDPGVLGIVYDSVAFPEQdgSPPGLR-VTVMLGGSWLQTLEAsgcvLSQELFQQRA 231
Cdd:COG1232   290 VVALGFDRPDLpPPDGFGWLVPRDEGVPILAVTFSSNKWPHR--APDGKVlLRLEVGGAGDPELWQ----LSDEELVALA 363

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323 232 QEAAATQLGLKEMPSHCLVHLHKNCIPQYTLGHWQKLESARQFLTAHRlPLTLAGASYEGVAVNDCIESGRQAAVSVLGT 311
Cdd:COG1232   364 LADLRKLLGIDAEPVDTRVVRWPKAYPQYTVGHLERVAAIREALAALP-GLYLAGRAYDGVGLPDCIRSGREAAERILAE 442
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
 4-309 5.94e-46

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: 161.54  E-value: 5.94e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323   4 LCRGVFAGNSRELSIRSCFPSLFQAEQTHRSILLGLLLgagRTPQPdSALIRQALAERWSQW--SLRGGLEMLPQALETH 81
Cdd:TIGR00562 159 LLSGIYAGDPSKLSLKSTFPKFYQTEQKHGSLILGMKK---TRNLP-QGSGLQLTAKKQGQDfqTLATGLETLPEEIEKR 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323  82 LtsRGVSVLRGQPVCGLSLQAEGRWKVSLRDSSLEADHVISAIPASVLSELLPAEAAPLARALSAITAVSVAVVNLQY-- 159
Cdd:TIGR00562 235 L--KLTKVYKGTKVTKLSHRGSNYTLELDNGVTVETDSVVVTAPHKAAAGLLSELSNSASSHLDKIHSPPVANVNLGFpe 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323 160 ---QGAHlpvQGFGHLVPSSEDPGVLGIVYDSVAFPEQdgSPPG-LRVTVMLGGSwlqtLEASGCVLSQELFQQRAQEAA 235
Cdd:TIGR00562 313 gsvDGEL---EGFGFLISRSSKFAILGCIFTSKLFPNR--APPGkTLLTAYIGGA----TDESIVDLSENEIINIVLRDL 383

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678214323 236 ATQLGLKEMPSHCLVHLHKNCIPQYTLGHWQKLESARQFLTAHRLPLTLAGASYEGVAVNDCIESGRQAAVSVL 309
Cdd:TIGR00562 384 KKVLNINNEPEMLCVTRWHRAIPQYHVGHDQRLKEARELLESAYPGVFLTGNSFEGVGIPDCIDQGKAAASDVL 457
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
 2-310 2.19e-34

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 129.97  E-value: 2.19e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323   2 DSLCRGVFAGNSRELSIRSCFPSLFQAEQTHRSIllglLLGAGRTPQPDSALIRQALAerwsqwSLRGGLEMLPQALETH 81
Cdd:PRK11883  161 EPLLSGIYAGDIDTLSLRATFPQLAQAEDKYGSL----LRGMRKALPKEKKKTKGVFG------TLKGGLQSLIEALEEK 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323  82 LtsRGVSVLRGQPVCGLSLQAEGrWKVSLRDSS-LEADHVISAIPASVLSELLPAEAAplARALSAITAVSVAVVNLQYQ 160
Cdd:PRK11883  231 L--PAGTIHKGTPVTKIDKSGDG-YEIVLSNGGeIEADAVIVAVPHPVLPSLFVAPPA--FALFKTIPSTSVATVALAFP 305

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323 161 GAHLPV-QGFGHLVPSSEDPGVLGIVYDSVAFPEQdgSPPG---LRVTVmlgGSWLQTLEASgcvLSQELFQQRAQEAAA 236
Cdd:PRK11883  306 ESATNLpDGTGFLVARNSDYTITACTWTSKKWPHT--TPEGkvlLRLYV---GRPGDEAVVD---ATDEELVAFVLADLS 377

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678214323 237 TQLGLKEMPSHCLVHLHKNCIPQYTLGHWQKLESARQFLtAHRLPLTLAGASYEGVAVNDCIESGRQAAVSVLG 310
Cdd:PRK11883  378 KVMGITGDPEFTIVQRWKEAMPQYGVGHIERVAELRAGL-PHYPGLYVAGASFEGVGLPDCIAQAKRAAARLLA 450
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 1-309 2.31e-28

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: 113.74  E-value: 2.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323   1 MDSLCRGVFAGNSRELSIRSCFPSLFQAEQTHRSIllglllgagrtpqpdsalirqalaerwsqWSLRGGLEMLPQALET 80
Cdd:pfam01593 164 ALPFASGAFAGDPSELSAGLALPLLWALLGEGGSL-----------------------------LLPRGGLGALPDALAA 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323  81 HLtsRGVSVLRGQPVCGLSLQAEGRwKVSLRD-SSLEADHVISAIPASVLS--ELLPAEAAPLARALSAITAVSVAVVNL 157
Cdd:pfam01593 215 QL--LGGDVRLNTRVRSIDREGDGV-TVTLTDgEVIEADAVIVTVPLGVLKriLFTPPLPPEKARAIRNLGYGPVNKVHL 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323 158 QYQGAHLPVQgfGHLVPSSEDPGVLGIVYDSVAFPEQDGSPPGLRVTVMLG-GSWLQTLEAsgcvLSQELFQQRAQEAAA 236
Cdd:pfam01593 292 EFDRKFWPDL--GLLGLLSELLTGLGTAFSWLTFPNRAPPGKGLLLLVYVGpGDRARELEG----LSDEELLQAVLRDLR 365

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323 237 TQLG--LKEMPSHCLVHLHKNCIPQYTLGHWQKLESARQFLTAHRLP---LTLAGAS----YEGVaVNDCIESGRQAAVS 307
Cdd:pfam01593 366 KLFGeeAPEPLRVLVSDWHTDPWPRGSYSLPQYGPGHDDYRPLARTPdpgLFFAGEHtstgYPGT-VEGAIESGRRAARA 444


                  ..
gi 1678214323 308 VL 309
Cdd:pfam01593 445 VL 446
 
Name Accession Description Interval E-value
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 1-311 7.55e-55

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: 184.27  E-value: 7.55e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323   1 MDSLCRGVFAGNSRELSIRSCFPSLFQAEQTHRSillglllgagrtpqpdsaLIRQALAERWSQ------WSLRGGLEML 74
Cdd:COG1232   151 VEPLLEGVYAGDPDELSADWAFPRLKRLELEHGS------------------LIKGALALRKGAkagevfGYLRGGLGTL 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323  75 PQALETHLtsRGVSVLRGQPVCGLSlQAEGRWKVSLRD-SSLEADHVISAIPASVLSELLPAEAAPLARALSAITAVSVA 153
Cdd:COG1232   213 VEALAEAL--EAGEIRLGTRVTAIE-REGGGWRVTTSDgETIEADAVVSATPAPALARLLAPLPPEVAAALAGIPYASVA 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323 154 VVNLQYQGAHL-PVQGFGHLVPSSEDPGVLGIVYDSVAFPEQdgSPPGLR-VTVMLGGSWLQTLEAsgcvLSQELFQQRA 231
Cdd:COG1232   290 VVALGFDRPDLpPPDGFGWLVPRDEGVPILAVTFSSNKWPHR--APDGKVlLRLEVGGAGDPELWQ----LSDEELVALA 363

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323 232 QEAAATQLGLKEMPSHCLVHLHKNCIPQYTLGHWQKLESARQFLTAHRlPLTLAGASYEGVAVNDCIESGRQAAVSVLGT 311
Cdd:COG1232   364 LADLRKLLGIDAEPVDTRVVRWPKAYPQYTVGHLERVAAIREALAALP-GLYLAGRAYDGVGLPDCIRSGREAAERILAE 442
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
 4-309 5.94e-46

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: 161.54  E-value: 5.94e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323   4 LCRGVFAGNSRELSIRSCFPSLFQAEQTHRSILLGLLLgagRTPQPdSALIRQALAERWSQW--SLRGGLEMLPQALETH 81
Cdd:TIGR00562 159 LLSGIYAGDPSKLSLKSTFPKFYQTEQKHGSLILGMKK---TRNLP-QGSGLQLTAKKQGQDfqTLATGLETLPEEIEKR 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323  82 LtsRGVSVLRGQPVCGLSLQAEGRWKVSLRDSSLEADHVISAIPASVLSELLPAEAAPLARALSAITAVSVAVVNLQY-- 159
Cdd:TIGR00562 235 L--KLTKVYKGTKVTKLSHRGSNYTLELDNGVTVETDSVVVTAPHKAAAGLLSELSNSASSHLDKIHSPPVANVNLGFpe 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323 160 ---QGAHlpvQGFGHLVPSSEDPGVLGIVYDSVAFPEQdgSPPG-LRVTVMLGGSwlqtLEASGCVLSQELFQQRAQEAA 235
Cdd:TIGR00562 313 gsvDGEL---EGFGFLISRSSKFAILGCIFTSKLFPNR--APPGkTLLTAYIGGA----TDESIVDLSENEIINIVLRDL 383

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678214323 236 ATQLGLKEMPSHCLVHLHKNCIPQYTLGHWQKLESARQFLTAHRLPLTLAGASYEGVAVNDCIESGRQAAVSVL 309
Cdd:TIGR00562 384 KKVLNINNEPEMLCVTRWHRAIPQYHVGHDQRLKEARELLESAYPGVFLTGNSFEGVGIPDCIDQGKAAASDVL 457
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
 2-310 2.19e-34

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 129.97  E-value: 2.19e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323   2 DSLCRGVFAGNSRELSIRSCFPSLFQAEQTHRSIllglLLGAGRTPQPDSALIRQALAerwsqwSLRGGLEMLPQALETH 81
Cdd:PRK11883  161 EPLLSGIYAGDIDTLSLRATFPQLAQAEDKYGSL----LRGMRKALPKEKKKTKGVFG------TLKGGLQSLIEALEEK 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323  82 LtsRGVSVLRGQPVCGLSLQAEGrWKVSLRDSS-LEADHVISAIPASVLSELLPAEAAplARALSAITAVSVAVVNLQYQ 160
Cdd:PRK11883  231 L--PAGTIHKGTPVTKIDKSGDG-YEIVLSNGGeIEADAVIVAVPHPVLPSLFVAPPA--FALFKTIPSTSVATVALAFP 305

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323 161 GAHLPV-QGFGHLVPSSEDPGVLGIVYDSVAFPEQdgSPPG---LRVTVmlgGSWLQTLEASgcvLSQELFQQRAQEAAA 236
Cdd:PRK11883  306 ESATNLpDGTGFLVARNSDYTITACTWTSKKWPHT--TPEGkvlLRLYV---GRPGDEAVVD---ATDEELVAFVLADLS 377

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1678214323 237 TQLGLKEMPSHCLVHLHKNCIPQYTLGHWQKLESARQFLtAHRLPLTLAGASYEGVAVNDCIESGRQAAVSVLG 310
Cdd:PRK11883  378 KVMGITGDPEFTIVQRWKEAMPQYGVGHIERVAELRAGL-PHYPGLYVAGASFEGVGLPDCIAQAKRAAARLLA 450
PLN02576 PLN02576
protoporphyrinogen oxidase
 2-309 1.92e-31

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 122.81  E-value: 1.92e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323   2 DSLCRGVFAGNSRELSIRSCFPSLFQAEQTHRSI-----LLGLLLGAGRTPQP-DSALIRQalaERWSQWSLRGGLEMLP 75
Cdd:PLN02576  166 DPFVSGVYAGDPSSLSMKAAFPKLWNLEKRGGSIiggaiKAIQEAKKNPKPEPrDPRLPKP---KGQTVGSFRGGLQTLP 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323  76 QALETHLTSRGVSVlrGQPVCGLSLQAEGRWKVSLRD----SSLEADHVISAIPASVLSELLPAEAAPLARALSAITAVS 151
Cdd:PLN02576  243 DALAKRLGKDKVKL--NWKVLSLSKNDDGGYSLTYDTpegkVNVTAKAVVMTAPLYVVSEMLRPKSPAAADALPEFYYPP 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323 152 VAVVNLQY--------QGAHLPVQGFGHLVPSSEDPGVLGIVYDSVAFPeqDGSPPGLRV-TVMLGGSWLQTL-EASgcv 221
Cdd:PLN02576  321 VAAVTTSYpkeavkreRLIDGPLEGFGQLHPRKQGVKTLGTIYSSSLFP--DRAPEGRVLlLNYIGGSRNTGIaSAS--- 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323 222 lSQELFQqrAQEAAATQLGLKEMPSHCLVHLHK---NCIPQYTLGHWQKLESARQFLTAHRLP-LTLAGASYEGVAVNDC 297
Cdd:PLN02576  396 -EEELVE--AVDRDLRKLLLKPGAPPPKVVGVRvwpKAIPQYLLGHLDVLEAAEKMEKDLGLPgLFLGGNYRGGVALGKC 472

                         330
                  ....*....|..
gi 1678214323 298 IESGRQAAVSVL 309
Cdd:PLN02576  473 VESGYEAADLVI 484
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 1-309 2.31e-28

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: 113.74  E-value: 2.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323   1 MDSLCRGVFAGNSRELSIRSCFPSLFQAEQTHRSIllglllgagrtpqpdsalirqalaerwsqWSLRGGLEMLPQALET 80
Cdd:pfam01593 164 ALPFASGAFAGDPSELSAGLALPLLWALLGEGGSL-----------------------------LLPRGGLGALPDALAA 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323  81 HLtsRGVSVLRGQPVCGLSLQAEGRwKVSLRD-SSLEADHVISAIPASVLS--ELLPAEAAPLARALSAITAVSVAVVNL 157
Cdd:pfam01593 215 QL--LGGDVRLNTRVRSIDREGDGV-TVTLTDgEVIEADAVIVTVPLGVLKriLFTPPLPPEKARAIRNLGYGPVNKVHL 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323 158 QYQGAHLPVQgfGHLVPSSEDPGVLGIVYDSVAFPEQDGSPPGLRVTVMLG-GSWLQTLEAsgcvLSQELFQQRAQEAAA 236
Cdd:pfam01593 292 EFDRKFWPDL--GLLGLLSELLTGLGTAFSWLTFPNRAPPGKGLLLLVYVGpGDRARELEG----LSDEELLQAVLRDLR 365

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323 237 TQLG--LKEMPSHCLVHLHKNCIPQYTLGHWQKLESARQFLTAHRLP---LTLAGAS----YEGVaVNDCIESGRQAAVS 307
Cdd:pfam01593 366 KLFGeeAPEPLRVLVSDWHTDPWPRGSYSLPQYGPGHDDYRPLARTPdpgLFFAGEHtstgYPGT-VEGAIESGRRAARA 444


                  ..
gi 1678214323 308 VL 309
Cdd:pfam01593 445 VL 446
PRK12416 PRK12416
protoporphyrinogen oxidase; Provisional
 7-311 3.32e-15

protoporphyrinogen oxidase; Provisional


Pssm-ID: 183516  Cd Length: 463  Bit Score: 75.63  E-value: 3.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323   7 GVFAGNSRELSIRSCFPSLFQAEQTHRSILlglllgagrtpqpdsalirQALAERWSQW---------SLRGGLEMLPQA 77
Cdd:PRK12416  171 GVYSGKLNELTMASTLPYLLDYKNKYGSII-------------------KGFEENKKQFqsagnkkfvSFKGGLSTIIDR 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323  78 LETHLTSrgVSVLRGQPVCGLSLQAEgRWKVSLRD-SSLEADHVISAIPASVLSELLpaEAAPLARALSAITAVSVAVVN 156
Cdd:PRK12416  232 LEEVLTE--TVVKKGAVTTAVSKQGD-RYEISFANhESIQADYVVLAAPHDIAETLL--QSNELNEQFHTFKNSSLISIY 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323 157 LQYQ--GAHLPVQGFGHLVPSSEDPGVLGIVYDSVAFPEQDGSPPGL-RVTVMLGGSWLQTLEAsgcvLSQELFQQRAQE 233
Cdd:PRK12416  307 LGFDilDEQLPADGTGFIVTENSDLHCDACTWTSRKWKHTSGKQKLLvRMFYKSTNPVYETIKN----YSEEELVRVALY 382

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1678214323 234 AAATQLGLKEMPSHCLVHLHKNCIPQYTLGHWQKLESARQFLTAHRLPLTLAGASYEGVAVNDCIESGRQAAVSVLGT 311
Cdd:PRK12416  383 DIEKSLGIKGEPEVVEVTNWKDLMPKYHLEHNQAVQSLQEKMMNLYPNIYLAGASYYGVGIGACIGNGKNTANEIIAT 460
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 67-169 3.06e-10

Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];


Pssm-ID: 442577 [Multi-domain]  Cd Length: 445  Bit Score: 60.64  E-value: 3.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323  67 LRGGL-EMLPQALETHLTSRGVSVLRGQPVCGLSLQAEGRWKVSLRD-SSLEADHVISAIPASVLSELLPA-EAAPLARA 143
Cdd:COG3349   206 PRGPLsELFVDPALAYLEARGGEVRLGTRVRALEFDGGRVTGLVLADgETVPADAVVLAVPPEVAARLLPElARLPELGL 285

                          90       100       110
                  ....*....|....*....|....*....|
gi 1678214323 144 LSAITAVSVAVVNLQYQG----AHLPVQGF 169
Cdd:COG3349   286 LAPLEYSPIVNVHLWLDRpvtlGPPPFAGL 315
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
33-159 2.10e-08

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 54.93  E-value: 2.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323  33 RSILLGLLLGAGRTPQPDSAL--IRQALAERWS--QWSLRGGLEMLPQALETHLTSRgvsVLRGQPVCGLSlQAEGRWKV 108
Cdd:COG1231   159 RLLGLLGAGEYGADPDELSLLdlLRYAASAGGGaqQFRIVGGMDQLPRALAAELGDR---IRLGAPVTRIR-QDGDGVTV 234

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1678214323 109 SLRD-SSLEADHVISAIPASVLS--ELLPAEAAPLARALSAITAVSVAVVNLQY 159
Cdd:COG1231   235 TTDDgGTVRADAVIVTVPPSVLRriEFDPPLPAAKRAAIQRLPYGAAIKVFLQF 288
PRK07233 PRK07233
hypothetical protein; Provisional
 67-155 4.66e-07

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 51.04  E-value: 4.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323  67 LRGGLEMLPQALETHLTSRGVSVLRGQPVCGLSLQAEGRWKVSLRDSSLEADHVISAIPASVLSELLPAEAAPLARALSA 146
Cdd:PRK07233  193 LEGGFATLIDALAEAIEARGGEIRLGTPVTSVVIDGGGVTGVEVDGEEEDFDAVISTAPPPILARLVPDLPADVLARLRR 272


                  ....*....
gi 1678214323 147 ITAVSVAVV 155
Cdd:PRK07233  273 IDYQGVVCM 281
PRK07208 PRK07208
hypothetical protein; Provisional
 73-146 1.72e-05

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 46.04  E-value: 1.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323  73 MLPQALETHLTSRGVSVLRGQPVCGLSLQAEGR-WKVSLRDS-----SLEADHVISAIPASVLSELLPAEAAPLARALSA 146
Cdd:PRK07208  219 QLWETAAEKLEALGGKVVLNAKVVGLHHDGDGRiAVVVVNDTdgteeTVTADQVISSMPLRELVAALDPPPPPEVRAAAA 298
HpnE TIGR03467
squalene-associated FAD-dependent desaturase; The sequences in this family are members of the ...
 82-173 2.50e-05

squalene-associated FAD-dependent desaturase; The sequences in this family are members of the pfam01593 superfamily of flavin-containing amine oxidases which include the phytoene desaturases. These sequences also include a FAD-dependent oxidoreductase domain, pfam01266. The genes of the family modeled here are generally in the same locus with genes involved in the biosynthesis and elaboration of squalene, the condensation product of the polyisoprenoid farnesyl pyrophosphate. This gene and its association with hopene biosynthesis in Zymomonas mobilis has been noted in the literature where the gene symbol hpnE was assigned. This gene is also found in contexts where the downstream conversion of squalene to hopenes is not evidence. The precise nature of the reaction catalyzed by this enzyme is unknown at this time.


Pssm-ID: 274593 [Multi-domain]  Cd Length: 419  Bit Score: 45.43  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678214323  82 LTSRGVSVLRGQPVCGLSLQAEG-RWKVSLRDSSLEADHVISAIPASVLSELLPAEAAPlaRALSAITAVSVAVVNLQYQ 160
Cdd:TIGR03467 207 LDSRGGEVRLGTRVRSIEANAGGiRALVRSGGETLPADAVVLAVPPRHAASLLPGEDLG--ALLTALGYSPITTVHLRLD 284

                          90
                  ....*....|...
gi 1678214323 161 GAhlPVQGFGHLV 173
Cdd:TIGR03467 285 RA--VRLPAPMVG 295
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
73-124 7.78e-03

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 37.59  E-value: 7.78e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1678214323  73 MLP----QALETHLTSRGVSVLRGQPVCGLSLQAEGrWKVSLRDS-SLEADHVISAI 124
Cdd:PRK04965  180 LMPpevsSRLQHRLTEMGVHLLLKSQLQGLEKTDSG-IRATLDSGrSIEVDAVIAAA 235
 
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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