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Conserved domains on  [gi|2462521546|ref|XP_054222973|]
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pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 isoform X14 [Homo sapiens]

Protein Classification

phytoene desaturase family protein( domain architecture ID 11440907)

phytoene desaturase family protein is an NAD(P)/FAD-dependent oxidoreductase that catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant; similar to phytoene desaturase, which converts phytoene into 3,4-didehydrolycopene via several intermediates by introducing up to five double bonds into phytoene

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
6-311 1.02e-85

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


:

Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 265.56  E-value: 1.02e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521546   6 GMQGAWGYVQGGMGALSDAIASSATTHGASIFTEKTVAKVQVnSEGCVQGVVLEDGTEVRSKMVLSNTSPQITFLKLTPQ 85
Cdd:COG1233   209 EYAGGVWYPKGGMGALADALARLAEELGGEIRTGAEVERILV-EGGRATGVRLADGEEIRADAVVSNADPAHTYLRLLGE 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521546  86 EWLPEEFLERISQLDTRSPVTKINVAVDR-LPSflaapnaprgqpLPHHQcsIHLNcEDtllLHQAFEDAMDGLPSHRPV 164
Cdd:COG1233   288 EALPARYRRRLERFRYSPSAFKLYLGLDGpLPG------------LAHHT--IHLS-ED---YEAAFDDIFRGRLPEDPS 349
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521546 165 IELCIPSSLDPTLAPPGCHVVSLFTQyMPYTLagGKAWDEqERDAYADRVFDCIEVYAPGFKDSVVGRDILTPPDLERIF 244
Cdd:COG1233   350 LYVSIPSLTDPSLAPEGKHTLWVLVP-VPYGL--EDAWDE-LKEEYAERILARLERYAPGLRDRIVAREVLTPLDFERYL 425
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521546 245 GLPGGNIFHCAMSLDQLYFARPvplhSGYRCPLQGLYLCGSGAHPGGGVMGAA--GRNAAHVAFRDLKS 311
Cdd:COG1233   426 NLVGGAIYGGAHTLDQSAFFRP----SNYRTPIPGLYLVGASTHPGGGVPGVLisGRLAARRILKDLKR 490
 
Name Accession Description Interval E-value
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
6-311 1.02e-85

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 265.56  E-value: 1.02e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521546   6 GMQGAWGYVQGGMGALSDAIASSATTHGASIFTEKTVAKVQVnSEGCVQGVVLEDGTEVRSKMVLSNTSPQITFLKLTPQ 85
Cdd:COG1233   209 EYAGGVWYPKGGMGALADALARLAEELGGEIRTGAEVERILV-EGGRATGVRLADGEEIRADAVVSNADPAHTYLRLLGE 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521546  86 EWLPEEFLERISQLDTRSPVTKINVAVDR-LPSflaapnaprgqpLPHHQcsIHLNcEDtllLHQAFEDAMDGLPSHRPV 164
Cdd:COG1233   288 EALPARYRRRLERFRYSPSAFKLYLGLDGpLPG------------LAHHT--IHLS-ED---YEAAFDDIFRGRLPEDPS 349
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521546 165 IELCIPSSLDPTLAPPGCHVVSLFTQyMPYTLagGKAWDEqERDAYADRVFDCIEVYAPGFKDSVVGRDILTPPDLERIF 244
Cdd:COG1233   350 LYVSIPSLTDPSLAPEGKHTLWVLVP-VPYGL--EDAWDE-LKEEYAERILARLERYAPGLRDRIVAREVLTPLDFERYL 425
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521546 245 GLPGGNIFHCAMSLDQLYFARPvplhSGYRCPLQGLYLCGSGAHPGGGVMGAA--GRNAAHVAFRDLKS 311
Cdd:COG1233   426 NLVGGAIYGGAHTLDQSAFFRP----SNYRTPIPGLYLVGASTHPGGGVPGVLisGRLAARRILKDLKR 490
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
1-311 1.42e-19

phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two symmetrical pairs of) sites. This is achieved by two enzymes (crtP and crtQ) in cyanobacteria (Gloeobacter being an exception) and plants, but by a single enzyme in most other bacteria and in fungi. This single enzyme is called the bacterial-type phytoene desaturase, or CrtI. Most members of this family, part of the larger pfam01593, which also contains amino oxidases, are CrtI itself; it is likely that all members act on either phytoene or on related compounds such as dehydrosqualene, for carotenoid biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 274273 [Multi-domain]  Cd Length: 495  Bit Score: 88.87  E-value: 1.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521546   1 MGGLEGMQGAWgYVQGGMGALSDAIASSATTHGASIFTEKTVAKVQVnSEGCVQGVVLEDGTEVRSKMVLSNTSPQITFL 80
Cdd:TIGR02734 202 ISALEREWGVW-FPRGGTGALVAAMAKLAEDLGGELRLNAEVIRIET-EGGRATAVHLADGERLDADAVVSNADLHHTYR 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521546  81 KLTPQewlPEEFLERISQLDTRSPVtkiNVAVdrLPSFLAAPNAPRGQPLPHHqcSIHLNCEDTLLLHQAFEDamdGLPS 160
Cdd:TIGR02734 280 RLLPN---HPRRRYPAARLSRKRPS---PSLF--VLYFGLLGVDGHWPQLAHH--TLCFGPRYKELFDEIFRK---GRLA 346
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521546 161 HRPVIELCIPSSLDPTLAPPGCHvvslfTQYM----PYTLAGGKAWDeQERDAYADRVFDCIEVYA-PGFKDSVVGRDIL 235
Cdd:TIGR02734 347 EDPSLYLHRPTVTDPSLAPPGCE-----SLYVlapvPHLGTADVDWS-VEGPRYRDRILAYLEERAiPGLRDRIVVERTF 420
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521546 236 TPPDLERIFGLPGGNIFHCAMSLDQLYFARPVPLHSGyrcpLQGLYLCGSGAHPGGGVMG--AAGRNAAHVAFRDLKS 311
Cdd:TIGR02734 421 TPADFRDRYNAWLGSAFSLEHTLTQSAWFRPHNRDRK----IDNLYLVGAGTHPGAGVPGvlGSAKATAKLMLGDLAP 494
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
13-302 1.19e-08

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: 55.96  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521546  13 YVQGGMGALSDAIASSAttHGASIFTEKTVAKVQVNSEGCvqGVVLEDGTEVRSKMVLSnTSPQITFLKLTPQEWLPEEF 92
Cdd:pfam01593 200 LPRGGLGALPDALAAQL--LGGDVRLNTRVRSIDREGDGV--TVTLTDGEVIEADAVIV-TVPLGVLKRILFTPPLPPEK 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521546  93 LERISQLDTRsPVTKINVAVDRlpsflaapnaprgQPLPHHQCSiHLNCEDTLLLHQAFEdamdglpshrpvielcipSS 172
Cdd:pfam01593 275 ARAIRNLGYG-PVNKVHLEFDR-------------KFWPDLGLL-GLLSELLTGLGTAFS------------------WL 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521546 173 LDPTLAPPGCHVVslftqYMPYTLAGGKAWDEQE--RDAYADRVFDCIEvyapgfkdSVVGRDILTPPDLERiFGLPGGN 250
Cdd:pfam01593 322 TFPNRAPPGKGLL-----LLVYVGPGDRARELEGlsDEELLQAVLRDLR--------KLFGEEAPEPLRVLV-SDWHTDP 387
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521546 251 IFHCAMSLDQlYFARPVPLHSGYRCPLQGLYLCGSGAHPG--GGVMGA--AGRNAA 302
Cdd:pfam01593 388 WPRGSYSLPQ-YGPGHDDYRPLARTPDPGLFFAGEHTSTGypGTVEGAieSGRRAA 442
PRK07233 PRK07233
hypothetical protein; Provisional
12-120 4.84e-07

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 50.66  E-value: 4.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521546  12 GYVQGGMGALSDAIASSATTHGASIFTEKTVAKVQVNsEGCVQGVVLeDGTEVRSKMVLSNTSPQItFLKLTPQewLPEE 91
Cdd:PRK07233  191 GYLEGGFATLIDALAEAIEARGGEIRLGTPVTSVVID-GGGVTGVEV-DGEEEDFDAVISTAPPPI-LARLVPD--LPAD 265
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462521546  92 FLERISQLD----------TRSPVTKI---NVAVDRLPsFLA 120
Cdd:PRK07233  266 VLARLRRIDyqgvvcmvlkLRRPLTDYywlNINDPGAP-FGG 306
 
Name Accession Description Interval E-value
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
6-311 1.02e-85

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 265.56  E-value: 1.02e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521546   6 GMQGAWGYVQGGMGALSDAIASSATTHGASIFTEKTVAKVQVnSEGCVQGVVLEDGTEVRSKMVLSNTSPQITFLKLTPQ 85
Cdd:COG1233   209 EYAGGVWYPKGGMGALADALARLAEELGGEIRTGAEVERILV-EGGRATGVRLADGEEIRADAVVSNADPAHTYLRLLGE 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521546  86 EWLPEEFLERISQLDTRSPVTKINVAVDR-LPSflaapnaprgqpLPHHQcsIHLNcEDtllLHQAFEDAMDGLPSHRPV 164
Cdd:COG1233   288 EALPARYRRRLERFRYSPSAFKLYLGLDGpLPG------------LAHHT--IHLS-ED---YEAAFDDIFRGRLPEDPS 349
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521546 165 IELCIPSSLDPTLAPPGCHVVSLFTQyMPYTLagGKAWDEqERDAYADRVFDCIEVYAPGFKDSVVGRDILTPPDLERIF 244
Cdd:COG1233   350 LYVSIPSLTDPSLAPEGKHTLWVLVP-VPYGL--EDAWDE-LKEEYAERILARLERYAPGLRDRIVAREVLTPLDFERYL 425
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462521546 245 GLPGGNIFHCAMSLDQLYFARPvplhSGYRCPLQGLYLCGSGAHPGGGVMGAA--GRNAAHVAFRDLKS 311
Cdd:COG1233   426 NLVGGAIYGGAHTLDQSAFFRP----SNYRTPIPGLYLVGASTHPGGGVPGVLisGRLAARRILKDLKR 490
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
1-311 1.42e-19

phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two symmetrical pairs of) sites. This is achieved by two enzymes (crtP and crtQ) in cyanobacteria (Gloeobacter being an exception) and plants, but by a single enzyme in most other bacteria and in fungi. This single enzyme is called the bacterial-type phytoene desaturase, or CrtI. Most members of this family, part of the larger pfam01593, which also contains amino oxidases, are CrtI itself; it is likely that all members act on either phytoene or on related compounds such as dehydrosqualene, for carotenoid biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 274273 [Multi-domain]  Cd Length: 495  Bit Score: 88.87  E-value: 1.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521546   1 MGGLEGMQGAWgYVQGGMGALSDAIASSATTHGASIFTEKTVAKVQVnSEGCVQGVVLEDGTEVRSKMVLSNTSPQITFL 80
Cdd:TIGR02734 202 ISALEREWGVW-FPRGGTGALVAAMAKLAEDLGGELRLNAEVIRIET-EGGRATAVHLADGERLDADAVVSNADLHHTYR 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521546  81 KLTPQewlPEEFLERISQLDTRSPVtkiNVAVdrLPSFLAAPNAPRGQPLPHHqcSIHLNCEDTLLLHQAFEDamdGLPS 160
Cdd:TIGR02734 280 RLLPN---HPRRRYPAARLSRKRPS---PSLF--VLYFGLLGVDGHWPQLAHH--TLCFGPRYKELFDEIFRK---GRLA 346
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521546 161 HRPVIELCIPSSLDPTLAPPGCHvvslfTQYM----PYTLAGGKAWDeQERDAYADRVFDCIEVYA-PGFKDSVVGRDIL 235
Cdd:TIGR02734 347 EDPSLYLHRPTVTDPSLAPPGCE-----SLYVlapvPHLGTADVDWS-VEGPRYRDRILAYLEERAiPGLRDRIVVERTF 420
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462521546 236 TPPDLERIFGLPGGNIFHCAMSLDQLYFARPVPLHSGyrcpLQGLYLCGSGAHPGGGVMG--AAGRNAAHVAFRDLKS 311
Cdd:TIGR02734 421 TPADFRDRYNAWLGSAFSLEHTLTQSAWFRPHNRDRK----IDNLYLVGAGTHPGAGVPGvlGSAKATAKLMLGDLAP 494
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
13-302 1.19e-08

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: 55.96  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521546  13 YVQGGMGALSDAIASSAttHGASIFTEKTVAKVQVNSEGCvqGVVLEDGTEVRSKMVLSnTSPQITFLKLTPQEWLPEEF 92
Cdd:pfam01593 200 LPRGGLGALPDALAAQL--LGGDVRLNTRVRSIDREGDGV--TVTLTDGEVIEADAVIV-TVPLGVLKRILFTPPLPPEK 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521546  93 LERISQLDTRsPVTKINVAVDRlpsflaapnaprgQPLPHHQCSiHLNCEDTLLLHQAFEdamdglpshrpvielcipSS 172
Cdd:pfam01593 275 ARAIRNLGYG-PVNKVHLEFDR-------------KFWPDLGLL-GLLSELLTGLGTAFS------------------WL 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521546 173 LDPTLAPPGCHVVslftqYMPYTLAGGKAWDEQE--RDAYADRVFDCIEvyapgfkdSVVGRDILTPPDLERiFGLPGGN 250
Cdd:pfam01593 322 TFPNRAPPGKGLL-----LLVYVGPGDRARELEGlsDEELLQAVLRDLR--------KLFGEEAPEPLRVLV-SDWHTDP 387
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462521546 251 IFHCAMSLDQlYFARPVPLHSGYRCPLQGLYLCGSGAHPG--GGVMGA--AGRNAA 302
Cdd:pfam01593 388 WPRGSYSLPQ-YGPGHDDYRPLARTPDPGLFFAGEHTSTGypGTVEGAieSGRRAA 442
PRK07233 PRK07233
hypothetical protein; Provisional
12-120 4.84e-07

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 50.66  E-value: 4.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462521546  12 GYVQGGMGALSDAIASSATTHGASIFTEKTVAKVQVNsEGCVQGVVLeDGTEVRSKMVLSNTSPQItFLKLTPQewLPEE 91
Cdd:PRK07233  191 GYLEGGFATLIDALAEAIEARGGEIRLGTPVTSVVID-GGGVTGVEV-DGEEEDFDAVISTAPPPI-LARLVPD--LPAD 265
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462521546  92 FLERISQLD----------TRSPVTKI---NVAVDRLPsFLA 120
Cdd:PRK07233  266 VLARLRRIDyqgvvcmvlkLRRPLTDYywlNINDPGAP-FGG 306
 
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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