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Conserved domains on  [gi|2217279057|ref|XP_047281838|]
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pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 isoform X2 [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

CATH:  3.50.50.60
EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0009055|GO:0016117|GO:0016116
SCOP:  4000128|3000055

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 ...
 35-618 2.81e-118

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


:

Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 360.70  E-value: 2.81e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057  35 YDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAVTEEiIPGFKFSRASYLLSLLRP--QIYTDLELKKHgLRLH 112
Cdd:COG1233     4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTFE-RPGFRFDVGPSVLTMPGVleRLFRELGLEDY-LELV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 113 LRNPySFTPMLEEGagskvpRCLLLGTDMAENQKQIAQFSQKDAQVFPKYEEFMHRLA-LAIDPLLDaapvdmaafqhgs 191
Cdd:COG1233    82 PLDP-AYRVPFPDG------RALDLPRDLERTAAELERLFPGDAEAYRRFLAELRRLYdALLEDLLY------------- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 192 llqrmRSLSTLKPLLKAgrilgAQLPRYYEVLTAPITKVLDQWFESEPLKATLATdavIGAMTSPHTPGSGYVLLHHVMG 271
Cdd:COG1233   142 -----RPLLSLRDLLRP-----LALARLLRLLLRSLRDLLRRYFKDPRLRALLAG---QALYLGLSPDRTPALYALIAYL 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 272 gleGMQGAWGYVQGGMGALSDAIASSATTHGASIFTEKTVAKVQVnSEGCVQGVVLEDGTEVRSKMVLSNTSPQITFLKL 351
Cdd:COG1233   209 ---EYAGGVWYPKGGMGALADALARLAEELGGEIRTGAEVERILV-EGGRATGVRLADGEEIRADAVVSNADPAHTYLRL 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 352 TPqdeedfrrerlrdlpeqrkkaaslgpwtseafhgafsfQEWLPEEFLERISQLDTRSPVTKINVAVDR-LPSflaapn 430
Cdd:COG1233   285 LG--------------------------------------EEALPARYRRRLERFRYSPSAFKLYLGLDGpLPG------ 320

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 431 aprgqpLPHHQcsIHLNcEDtllLHQAFEDAMDGLPSHRPVIELCIPSSLDPTLAPPGCHVVSLFTQyMPYTLagGKAWD 510
Cdd:COG1233   321 ------LAHHT--IHLS-ED---YEAAFDDIFRGRLPEDPSLYVSIPSLTDPSLAPEGKHTLWVLVP-VPYGL--EDAWD 385

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 511 EqERDAYADRVFDCIEVYAPGFKDSVVGRDILTPPDLERIFGLPGGNIFHCAMSLDQLYFARPvplhSGYRCPLQGLYLC 590
Cdd:COG1233   386 E-LKEEYAERILARLERYAPGLRDRIVAREVLTPLDFERYLNLVGGAIYGGAHTLDQSAFFRP----SNYRTPIPGLYLV 460

                         570       580       590
                  ....*....|....*....|....*....|
gi 2217279057 591 GSGAHPGGGVMGAA--GRNAAHVAFRDLKS 618
Cdd:COG1233   461 GASTHPGGGVPGVLisGRLAARRILKDLKR 490
 
Name Accession Description Interval E-value
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 35-618 2.81e-118

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 360.70  E-value: 2.81e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057  35 YDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAVTEEiIPGFKFSRASYLLSLLRP--QIYTDLELKKHgLRLH 112
Cdd:COG1233     4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTFE-RPGFRFDVGPSVLTMPGVleRLFRELGLEDY-LELV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 113 LRNPySFTPMLEEGagskvpRCLLLGTDMAENQKQIAQFSQKDAQVFPKYEEFMHRLA-LAIDPLLDaapvdmaafqhgs 191
Cdd:COG1233    82 PLDP-AYRVPFPDG------RALDLPRDLERTAAELERLFPGDAEAYRRFLAELRRLYdALLEDLLY------------- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 192 llqrmRSLSTLKPLLKAgrilgAQLPRYYEVLTAPITKVLDQWFESEPLKATLATdavIGAMTSPHTPGSGYVLLHHVMG 271
Cdd:COG1233   142 -----RPLLSLRDLLRP-----LALARLLRLLLRSLRDLLRRYFKDPRLRALLAG---QALYLGLSPDRTPALYALIAYL 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 272 gleGMQGAWGYVQGGMGALSDAIASSATTHGASIFTEKTVAKVQVnSEGCVQGVVLEDGTEVRSKMVLSNTSPQITFLKL 351
Cdd:COG1233   209 ---EYAGGVWYPKGGMGALADALARLAEELGGEIRTGAEVERILV-EGGRATGVRLADGEEIRADAVVSNADPAHTYLRL 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 352 TPqdeedfrrerlrdlpeqrkkaaslgpwtseafhgafsfQEWLPEEFLERISQLDTRSPVTKINVAVDR-LPSflaapn 430
Cdd:COG1233   285 LG--------------------------------------EEALPARYRRRLERFRYSPSAFKLYLGLDGpLPG------ 320

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 431 aprgqpLPHHQcsIHLNcEDtllLHQAFEDAMDGLPSHRPVIELCIPSSLDPTLAPPGCHVVSLFTQyMPYTLagGKAWD 510
Cdd:COG1233   321 ------LAHHT--IHLS-ED---YEAAFDDIFRGRLPEDPSLYVSIPSLTDPSLAPEGKHTLWVLVP-VPYGL--EDAWD 385

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 511 EqERDAYADRVFDCIEVYAPGFKDSVVGRDILTPPDLERIFGLPGGNIFHCAMSLDQLYFARPvplhSGYRCPLQGLYLC 590
Cdd:COG1233   386 E-LKEEYAERILARLERYAPGLRDRIVAREVLTPLDFERYLNLVGGAIYGGAHTLDQSAFFRP----SNYRTPIPGLYLV 460

                         570       580       590
                  ....*....|....*....|....*....|
gi 2217279057 591 GSGAHPGGGVMGAA--GRNAAHVAFRDLKS 618
Cdd:COG1233   461 GASTHPGGGVPGVLisGRLAARRILKDLKR 490
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
 37-618 6.19e-31

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: 126.62  E-value: 6.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057  37 AVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAVTEEiIPGFKFSrasyllslLRPQIYTDLELKKHGLRL---HL 113
Cdd:TIGR02734   1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGRAGVLE-DDGFRFD--------TGPTVITMPEALEELFALagrDL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 114 RNPYSFTPM-------LEEGAGSKVPrclllgTDMAENQKQIAQFSQKDAQVFPKYEEFMHRL-ALAIDPLLDAAPVDMA 185
Cdd:TIGR02734  72 ADYVELVPLdpfyrlcWEDGSQLDVD------NDQEELEAQIARFNPGDVAGYRRFLDYAERVyREGYRKLGYVPFLSPR 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 186 AFQHGSLLQRMRSLSTlkpllkagRILGAQLPRYyevltapitkvldqwFESEPLKATLATDAV-IGamTSPHTPGSGYV 264
Cdd:TIGR02734 146 DLLRADAPQLLALLAW--------RSLYSKVARF---------------FSDERLRQAFSFHALfLG--GNPFRTPSIYA 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 265 LLHHvmggLEGMQGAWgYVQGGMGALSDAIASSATTHGASIFTEKTVAKVQVnSEGCVQGVVLEDGTEVRSKMVLSNTSP 344
Cdd:TIGR02734 201 LISA----LEREWGVW-FPRGGTGALVAAMAKLAEDLGGELRLNAEVIRIET-EGGRATAVHLADGERLDADAVVSNADL 274

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 345 QITFLKLtpqdeedfrrerLRDLPEQRKKAASLGPwtseafhgafsfQEWLPEEFLERISQLDTRSPVTKinvavdrlps 424
Cdd:TIGR02734 275 HHTYRRL------------LPNHPRRRYPAARLSR------------KRPSPSLFVLYFGLLGVDGHWPQ---------- 320

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 425 flaapnaprgqpLPHHqcSIHLNCEDTLLLHQAFEdamDGLPSHRPVIELCIPSSLDPTLAPPGCHvvslfTQYM----P 500
Cdd:TIGR02734 321 ------------LAHH--TLCFGPRYKELFDEIFR---KGRLAEDPSLYLHRPTVTDPSLAPPGCE-----SLYVlapvP 378

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 501 YTLAGGKAWDeQERDAYADRVFDCIEVYA-PGFKDSVVGRDILTPPDLERIFGLPGGNIFHCAMSLDQLYFARPVPLHSG 579
Cdd:TIGR02734 379 HLGTADVDWS-VEGPRYRDRILAYLEERAiPGLRDRIVVERTFTPADFRDRYNAWLGSAFSLEHTLTQSAWFRPHNRDRK 457

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 2217279057 580 yrcpLQGLYLCGSGAHPGGGVMG--AAGRNAAHVAFRDLKS 618
Cdd:TIGR02734 458 ----IDNLYLVGAGTHPGAGVPGvlGSAKATAKLMLGDLAP 494
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 46-609 1.43e-10

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: 63.66  E-value: 1.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057  46 GLVAAAYLQRLGVNTAVFERRHVIGGAAVTEEiIPGFKFSRASYLLSLLRPQIYTdlELKKHGLRLHLRNPYSFTPMLEE 125
Cdd:pfam01593   3 GLAAARELLRAGHDVTVLEARDRVGGRIRTVR-DDGFLIELGAMWFHGAQPPLLA--LLKELGLEDRLVLPDPAPFYTVL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 126 GAGSKVPRCLLlgtdmaenqkqiaQFSQKDAQVFPKYEEFMH---RLALAIDPLLdAAPVDMAAFQHGSLLQRMRSLStl 202
Cdd:pfam01593  80 FAGGRRYPGDF-------------RRVPAGWEGLLEFGRLLSipeKLRLGLAALA-SDALDEFDLDDFSLAESLLFLG-- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 203 kpllkaGRILGAQlpryyevltapitKVLDQWFESEPLKATLATDAVIGAMTSPHTPGSGYVLLHHVMGGLEGMQGAwgy 282
Cdd:pfam01593 144 ------RRGPGDV-------------EVWDRLIDPELFAALPFASGAFAGDPSELSAGLALPLLWALLGEGGSLLLP--- 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 283 vQGGMGALSDAIASSAttHGASIFTEKTVAKVQVNSEGCvqGVVLEDGTEVRSKMVLSntspqitflkltpqdeedfrre 362
Cdd:pfam01593 202 -RGGLGALPDALAAQL--LGGDVRLNTRVRSIDREGDGV--TVTLTDGEVIEADAVIV---------------------- 254

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 363 rlrdlpeqrkkAASLGPWtseafhGAFSFQEWLPEEFLERISQLDTRsPVTKINVAVDRlpsflaapnaprgQPLPHHQC 442
Cdd:pfam01593 255 -----------TVPLGVL------KRILFTPPLPPEKARAIRNLGYG-PVNKVHLEFDR-------------KFWPDLGL 303

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 443 SiHLNCEDTLLLHQAFEdamdglpshrpvielcipSSLDPTLAPPGCHVVslftqYMPYTLAGGKAWDEQE--RDAYADR 520
Cdd:pfam01593 304 L-GLLSELLTGLGTAFS------------------WLTFPNRAPPGKGLL-----LLVYVGPGDRARELEGlsDEELLQA 359

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 521 VFDCIEvyapgfkdSVVGRDILTPPDLERiFGLPGGNIFHCAMSLDQlYFARPVPLHSGYRCPLQGLYLCGSGAHPG--G 598
Cdd:pfam01593 360 VLRDLR--------KLFGEEAPEPLRVLV-SDWHTDPWPRGSYSLPQ-YGPGHDDYRPLARTPDPGLFFAGEHTSTGypG 429

                         570
                  ....*....|...
gi 2217279057 599 GVMGA--AGRNAA 609
Cdd:pfam01593 430 TVEGAieSGRRAA 442
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 39-83 2.48e-06

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 50.18  E-value: 2.48e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2217279057  39 VIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGaaVTEEIIPGFK 83
Cdd:PRK11749  145 VIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG--LLRYGIPEFR 187
 
Name Accession Description Interval E-value
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 35-618 2.81e-118

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 360.70  E-value: 2.81e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057  35 YDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAVTEEiIPGFKFSRASYLLSLLRP--QIYTDLELKKHgLRLH 112
Cdd:COG1233     4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTFE-RPGFRFDVGPSVLTMPGVleRLFRELGLEDY-LELV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 113 LRNPySFTPMLEEGagskvpRCLLLGTDMAENQKQIAQFSQKDAQVFPKYEEFMHRLA-LAIDPLLDaapvdmaafqhgs 191
Cdd:COG1233    82 PLDP-AYRVPFPDG------RALDLPRDLERTAAELERLFPGDAEAYRRFLAELRRLYdALLEDLLY------------- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 192 llqrmRSLSTLKPLLKAgrilgAQLPRYYEVLTAPITKVLDQWFESEPLKATLATdavIGAMTSPHTPGSGYVLLHHVMG 271
Cdd:COG1233   142 -----RPLLSLRDLLRP-----LALARLLRLLLRSLRDLLRRYFKDPRLRALLAG---QALYLGLSPDRTPALYALIAYL 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 272 gleGMQGAWGYVQGGMGALSDAIASSATTHGASIFTEKTVAKVQVnSEGCVQGVVLEDGTEVRSKMVLSNTSPQITFLKL 351
Cdd:COG1233   209 ---EYAGGVWYPKGGMGALADALARLAEELGGEIRTGAEVERILV-EGGRATGVRLADGEEIRADAVVSNADPAHTYLRL 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 352 TPqdeedfrrerlrdlpeqrkkaaslgpwtseafhgafsfQEWLPEEFLERISQLDTRSPVTKINVAVDR-LPSflaapn 430
Cdd:COG1233   285 LG--------------------------------------EEALPARYRRRLERFRYSPSAFKLYLGLDGpLPG------ 320

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 431 aprgqpLPHHQcsIHLNcEDtllLHQAFEDAMDGLPSHRPVIELCIPSSLDPTLAPPGCHVVSLFTQyMPYTLagGKAWD 510
Cdd:COG1233   321 ------LAHHT--IHLS-ED---YEAAFDDIFRGRLPEDPSLYVSIPSLTDPSLAPEGKHTLWVLVP-VPYGL--EDAWD 385

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 511 EqERDAYADRVFDCIEVYAPGFKDSVVGRDILTPPDLERIFGLPGGNIFHCAMSLDQLYFARPvplhSGYRCPLQGLYLC 590
Cdd:COG1233   386 E-LKEEYAERILARLERYAPGLRDRIVAREVLTPLDFERYLNLVGGAIYGGAHTLDQSAFFRP----SNYRTPIPGLYLV 460

                         570       580       590
                  ....*....|....*....|....*....|
gi 2217279057 591 GSGAHPGGGVMGAA--GRNAAHVAFRDLKS 618
Cdd:COG1233   461 GASTHPGGGVPGVLisGRLAARRILKDLKR 490
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
 37-618 6.19e-31

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: 126.62  E-value: 6.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057  37 AVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAVTEEiIPGFKFSrasyllslLRPQIYTDLELKKHGLRL---HL 113
Cdd:TIGR02734   1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGRAGVLE-DDGFRFD--------TGPTVITMPEALEELFALagrDL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 114 RNPYSFTPM-------LEEGAGSKVPrclllgTDMAENQKQIAQFSQKDAQVFPKYEEFMHRL-ALAIDPLLDAAPVDMA 185
Cdd:TIGR02734  72 ADYVELVPLdpfyrlcWEDGSQLDVD------NDQEELEAQIARFNPGDVAGYRRFLDYAERVyREGYRKLGYVPFLSPR 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 186 AFQHGSLLQRMRSLSTlkpllkagRILGAQLPRYyevltapitkvldqwFESEPLKATLATDAV-IGamTSPHTPGSGYV 264
Cdd:TIGR02734 146 DLLRADAPQLLALLAW--------RSLYSKVARF---------------FSDERLRQAFSFHALfLG--GNPFRTPSIYA 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 265 LLHHvmggLEGMQGAWgYVQGGMGALSDAIASSATTHGASIFTEKTVAKVQVnSEGCVQGVVLEDGTEVRSKMVLSNTSP 344
Cdd:TIGR02734 201 LISA----LEREWGVW-FPRGGTGALVAAMAKLAEDLGGELRLNAEVIRIET-EGGRATAVHLADGERLDADAVVSNADL 274

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 345 QITFLKLtpqdeedfrrerLRDLPEQRKKAASLGPwtseafhgafsfQEWLPEEFLERISQLDTRSPVTKinvavdrlps 424
Cdd:TIGR02734 275 HHTYRRL------------LPNHPRRRYPAARLSR------------KRPSPSLFVLYFGLLGVDGHWPQ---------- 320

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 425 flaapnaprgqpLPHHqcSIHLNCEDTLLLHQAFEdamDGLPSHRPVIELCIPSSLDPTLAPPGCHvvslfTQYM----P 500
Cdd:TIGR02734 321 ------------LAHH--TLCFGPRYKELFDEIFR---KGRLAEDPSLYLHRPTVTDPSLAPPGCE-----SLYVlapvP 378

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 501 YTLAGGKAWDeQERDAYADRVFDCIEVYA-PGFKDSVVGRDILTPPDLERIFGLPGGNIFHCAMSLDQLYFARPVPLHSG 579
Cdd:TIGR02734 379 HLGTADVDWS-VEGPRYRDRILAYLEERAiPGLRDRIVVERTFTPADFRDRYNAWLGSAFSLEHTLTQSAWFRPHNRDRK 457

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 2217279057 580 yrcpLQGLYLCGSGAHPGGGVMG--AAGRNAAHVAFRDLKS 618
Cdd:TIGR02734 458 ----IDNLYLVGAGTHPGAGVPGvlGSAKATAKLMLGDLAP 494
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 46-609 1.43e-10

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: 63.66  E-value: 1.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057  46 GLVAAAYLQRLGVNTAVFERRHVIGGAAVTEEiIPGFKFSRASYLLSLLRPQIYTdlELKKHGLRLHLRNPYSFTPMLEE 125
Cdd:pfam01593   3 GLAAARELLRAGHDVTVLEARDRVGGRIRTVR-DDGFLIELGAMWFHGAQPPLLA--LLKELGLEDRLVLPDPAPFYTVL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 126 GAGSKVPRCLLlgtdmaenqkqiaQFSQKDAQVFPKYEEFMH---RLALAIDPLLdAAPVDMAAFQHGSLLQRMRSLStl 202
Cdd:pfam01593  80 FAGGRRYPGDF-------------RRVPAGWEGLLEFGRLLSipeKLRLGLAALA-SDALDEFDLDDFSLAESLLFLG-- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 203 kpllkaGRILGAQlpryyevltapitKVLDQWFESEPLKATLATDAVIGAMTSPHTPGSGYVLLHHVMGGLEGMQGAwgy 282
Cdd:pfam01593 144 ------RRGPGDV-------------EVWDRLIDPELFAALPFASGAFAGDPSELSAGLALPLLWALLGEGGSLLLP--- 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 283 vQGGMGALSDAIASSAttHGASIFTEKTVAKVQVNSEGCvqGVVLEDGTEVRSKMVLSntspqitflkltpqdeedfrre 362
Cdd:pfam01593 202 -RGGLGALPDALAAQL--LGGDVRLNTRVRSIDREGDGV--TVTLTDGEVIEADAVIV---------------------- 254

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 363 rlrdlpeqrkkAASLGPWtseafhGAFSFQEWLPEEFLERISQLDTRsPVTKINVAVDRlpsflaapnaprgQPLPHHQC 442
Cdd:pfam01593 255 -----------TVPLGVL------KRILFTPPLPPEKARAIRNLGYG-PVNKVHLEFDR-------------KFWPDLGL 303

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 443 SiHLNCEDTLLLHQAFEdamdglpshrpvielcipSSLDPTLAPPGCHVVslftqYMPYTLAGGKAWDEQE--RDAYADR 520
Cdd:pfam01593 304 L-GLLSELLTGLGTAFS------------------WLTFPNRAPPGKGLL-----LLVYVGPGDRARELEGlsDEELLQA 359

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 521 VFDCIEvyapgfkdSVVGRDILTPPDLERiFGLPGGNIFHCAMSLDQlYFARPVPLHSGYRCPLQGLYLCGSGAHPG--G 598
Cdd:pfam01593 360 VLRDLR--------KLFGEEAPEPLRVLV-SDWHTDPWPRGSYSLPQ-YGPGHDDYRPLARTPDPGLFFAGEHTSTGypG 429

                         570
                  ....*....|...
gi 2217279057 599 GVMGA--AGRNAA 609
Cdd:pfam01593 430 TVEGAieSGRRAA 442
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
39-99 5.67e-10

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 55.62  E-value: 5.67e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217279057  39 VIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAVTEEiIPGFKFSR-ASYLLSLLRPQIY 99
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYSYR-VPGYVFDYgAHIFHGSDEPNVR 61
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 33-72 3.25e-08

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: 56.02  E-value: 3.25e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2217279057  33 PEYDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGA 72
Cdd:COG2072     5 EHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGT 44
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 39-86 2.00e-06

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 50.52  E-value: 2.00e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2217279057  39 VIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGaaVTEEIIPGFKFSR 86
Cdd:COG0493   126 VVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG--LLRYGIPEFRLPK 171
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 39-83 2.48e-06

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 50.18  E-value: 2.48e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2217279057  39 VIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGaaVTEEIIPGFK 83
Cdd:PRK11749  145 VIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG--LLRYGIPEFR 187
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
35-82 2.64e-06

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 49.73  E-value: 2.64e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2217279057  35 YDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHViGG-AAVTEEI--IPGF 82
Cdd:COG0492     1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEP-GGqLATTKEIenYPGF 50
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 35-78 3.20e-06

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: 49.83  E-value: 3.20e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2217279057  35 YDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAVTEEI 78
Cdd:COG1232     2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRTVEV 45
PRK06370 PRK06370
FAD-containing oxidoreductase;
33-74 4.81e-06

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 49.43  E-value: 4.81e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2217279057  33 PEYDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHViGGAAV 74
Cdd:PRK06370    4 QRYDAIVIGAGQAGPPLAARAAGLGMKVALIERGLL-GGTCV 44
PRK07233 PRK07233
hypothetical protein; Provisional
 38-370 5.21e-06

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 49.11  E-value: 5.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057  38 VVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAVTeeiipgFKFSrasyllsllrpqiytDLELKK---HglrlHLR 114
Cdd:PRK07233    3 AIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAAS------FEFG---------------GLPIERfyhH----IFK 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 115 NPYSFTPMLEE-GAGSKVprcLLLGTDMAenqkqiaQFSQKDaqvfpkyeefMHRLAlaidplldaAPVDMAAFQHGSLL 193
Cdd:PRK07233   58 SDEALLELLDElGLEDKL---RWRETKTG-------YYVDGK----------LYPLG---------TPLELLRFPHLSLI 108

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 194 QRMR-SLSTL--------KPLLKAG------RILGaqlPRYYEVLTAPItkvldqwFESeplKATLATDAV--------I 250
Cdd:PRK07233  109 DKFRlGLLTLlarrikdwRALDKVPaeewlrRWSG---EGVYEVFWEPL-------LES---KFGDYADDVsaawlwsrI 175

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217279057 251 GAMTSPHTPGSGYVLlhhvmgglegmqgawGYVQGGMGALSDAIASSATTHGASIFTEKTVAKVQVNsEGCVQGVVLeDG 330
Cdd:PRK07233  176 KRRGNRRYSLFGEKL---------------GYLEGGFATLIDALAEAIEARGGEIRLGTPVTSVVID-GGGVTGVEV-DG 238

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 2217279057 331 TEVRSKMVLSNTSPQItFLKLTPQDEEDFrRERLRDLPEQ 370
Cdd:PRK07233  239 EEEDFDAVISTAPPPI-LARLVPDLPADV-LARLRRIDYQ 276
PRK12775 PRK12775
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ...
 23-86 1.07e-05

putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional


Pssm-ID: 183738 [Multi-domain]  Cd Length: 1006  Bit Score: 48.78  E-value: 1.07e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217279057   23 DNTEARGGLKPEYD-----AVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGaaVTEEIIPGFKFSR 86
Cdd:PRK12775   414 DNARAKPVKPPRFSkklgkVAICGSGPAGLAAAADLVKYGVDVTVYEALHVVGG--VLQYGIPSFRLPR 480
PLN02576 PLN02576
protoporphyrinogen oxidase
 23-71 1.17e-05

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 48.09  E-value: 1.17e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217279057  23 DNTEARGGLKPEYDAVVIGAGHNGLVAAAYLQ-RLGVNTAVFERRHVIGG 71
Cdd:PLN02576    1 SAIAEGSAAASSKDVAVVGAGVSGLAAAYALAsKHGVNVLVTEARDRVGG 50
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 27-83 2.55e-05

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 47.08  E-value: 2.55e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217279057  27 ARGGLKPEYDAV-------VIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGaaVTEEIIPGFK 83
Cdd:PRK12810  129 EEGWVKPDPPVKrtgkkvaVVGSGPAGLAAADQLARAGHKVTVFERADRIGG--LLRYGIPDFK 190
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 34-80 8.59e-05

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 45.46  E-value: 8.59e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2217279057  34 EYDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHViGGAAVTEEIIP 80
Cdd:COG1249     3 DYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRL-GGTCLNVGCIP 48
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 34-74 1.02e-04

Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 45.21  E-value: 1.02e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2217279057  34 EYDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAV 74
Cdd:COG1053     3 EYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGGHTA 43
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 36-73 1.52e-04

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: 44.31  E-value: 1.52e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2217279057  36 DAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAA 73
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSGA 38
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
34-74 1.80e-04

Si-specific NAD(P)(+) transhydrogenase;


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 44.38  E-value: 1.80e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2217279057  34 EYDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAV 74
Cdd:PRK05249    5 DYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGCT 45
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 33-66 2.51e-04

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: 43.39  E-value: 2.51e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2217279057  33 PEYDAVVIGAGHNGLVAAAYLQRLGVNTAVFERR 66
Cdd:COG0654     2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERA 35
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
34-72 2.98e-04

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 43.36  E-value: 2.98e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2217279057  34 EYDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGA 72
Cdd:COG0665     2 TADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGSGA 40
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
33-71 3.41e-04

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 43.37  E-value: 3.41e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2217279057  33 PEYDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGG 71
Cdd:COG1231     6 RGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGG 44
PLN02976 PLN02976
amine oxidase
 38-76 4.72e-04

amine oxidase


Pssm-ID: 215527 [Multi-domain]  Cd Length: 1713  Bit Score: 43.32  E-value: 4.72e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217279057   38 VVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAVTE 76
Cdd:PLN02976   697 IVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGRVYTD 735
Thi4 pfam01946
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
 34-73 5.42e-04

Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.


Pssm-ID: 460393  Cd Length: 232  Bit Score: 42.07  E-value: 5.42e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2217279057  34 EYDAVVIGAGHNGLVAAAYL-QRLGVNTAVFERRHVIGGAA 73
Cdd:pfam01946  17 ESDVVIVGAGSSGLTAAYYLaKNRGLKVAIIERSVSPGGGA 57
PRK10157 PRK10157
putative oxidoreductase FixC; Provisional
 35-82 9.60e-04

putative oxidoreductase FixC; Provisional


Pssm-ID: 182273 [Multi-domain]  Cd Length: 428  Bit Score: 41.82  E-value: 9.60e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2217279057  35 YDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAVT---------EEIIPGF 82
Cdd:PRK10157    6 FDAIIVGAGLAGSVAALVLAREGAQVLVIERGNSAGAKNVTggrlyahslEHIIPGF 62
PRK10015 PRK10015
oxidoreductase; Provisional
 34-82 1.35e-03

oxidoreductase; Provisional


Pssm-ID: 182194 [Multi-domain]  Cd Length: 429  Bit Score: 41.50  E-value: 1.35e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217279057  34 EYDAVVIGAGHNGLVAAAYLQRLGVNTAVFER------RHVIGG---AAVTEEIIPGF 82
Cdd:PRK10015    5 KFDAIVVGAGVAGSVAALVMARAGLDVLVIERgdsagcKNMTGGrlyAHTLEAIIPGF 62
GIDA pfam01134
Glucose inhibited division protein A;
36-63 2.49e-03

Glucose inhibited division protein A;


Pssm-ID: 250388 [Multi-domain]  Cd Length: 391  Bit Score: 40.61  E-value: 2.49e-03
                          10        20
                  ....*....|....*....|....*...
gi 2217279057  36 DAVVIGAGHNGLVAAAYLQRLGVNTAVF 63
Cdd:pfam01134   1 DVIVIGGGHAGCEAALAAARMGAKVLLI 28
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 34-71 2.72e-03

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 40.51  E-value: 2.72e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2217279057  34 EYDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHvIGG 71
Cdd:PRK06416    4 EYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEK-LGG 40
PRK07208 PRK07208
hypothetical protein; Provisional
 36-77 2.79e-03

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 40.64  E-value: 2.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2217279057  36 DAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAVTEE 77
Cdd:PRK07208    6 SVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGISRTVT 47
PRK06753 PRK06753
hypothetical protein; Provisional
 39-69 3.61e-03

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 40.06  E-value: 3.61e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2217279057  39 VIGAGHNGLVAAAYLQRLGVNTAVFERRHVI 69
Cdd:PRK06753    5 IIGAGIGGLTAAALLQEQGHEVKVFEKNESV 35
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 35-66 4.13e-03

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 39.61  E-value: 4.13e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2217279057  35 YDAVVIGAGHNGLVAAAYLQRLGVNTAVFERR 66
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDE 32
PRK12844 PRK12844
3-ketosteroid-delta-1-dehydrogenase; Reviewed
 34-72 4.87e-03

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 183787 [Multi-domain]  Cd Length: 557  Bit Score: 39.74  E-value: 4.87e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2217279057  34 EYDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGA 72
Cdd:PRK12844    6 TYDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGGS 44
PRK06481 PRK06481
flavocytochrome c;
31-71 5.24e-03

flavocytochrome c;


Pssm-ID: 180584 [Multi-domain]  Cd Length: 506  Bit Score: 39.82  E-value: 5.24e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2217279057  31 LKPEYDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGG 71
Cdd:PRK06481   58 LKDKYDIVIVGAGGAGMSAAIEAKDAGMNPVILEKMPVAGG 98
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 34-65 6.95e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 39.39  E-value: 6.95e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2217279057  34 EYDAVVIGAGHNGLVAAAYLQRLGVNTAVFER 65
Cdd:PRK06292    3 KYDVIVIGAGPAGYVAARRAAKLGKKVALIEK 34
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 37-113 7.25e-03

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 35.64  E-value: 7.25e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217279057  37 AVVIGAGHNGLVAAAYLQRLGVNTAVFERRhviggaavtEEIIPGFKFSRASYLLSllrpqiytdlELKKHGLRLHL 113
Cdd:pfam00070   2 VVVVGGGYIGLELAGALARLGSKVTVVERR---------DRLLPGFDPEIAKILQE----------KLEKNGIEFLL 59
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 36-74 7.62e-03

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 39.19  E-value: 7.62e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2217279057  36 DAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAV 74
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGATA 39
 
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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