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Conserved domains on  [gi|753980065|ref|WP_041667923|]
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MULTISPECIES: NAD(P)/FAD-dependent oxidoreductase [Streptomyces]

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 ...
1-503 1.09e-127

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


:

Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 381.89  E-value: 1.09e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065   1 MPDAVVIGAGPNGLVAANLLADAGWSVEVLEAQDEPGGAVRhdRGVDPDFTSDLFSSFYPLA-AASPVLAGLRLEREgLE 79
Cdd:COG1233    3 MYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRAR--TFERPGFRFDVGPSVLTMPgVLERLFRELGLEDY-LE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065  80 WSHAPKVLAHPLLDGRCAVLSRDPEETAASLEAFAPGDGAAWQELREVWERLRPDILDALF-TPFPPLRAGARLALRLRA 158
Cdd:COG1233   80 LVPLDPAYRVPFPDGRALDLPRDLERTAAELERLFPGDAEAYRRFLAELRRLYDALLEDLLyRPLLSLRDLLRPLALARL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065 159 AGGlrlartMVLPVRRLGEEEFRGEGGRLLLAGNALHADLAPESAGSggFGWLMSMLAQTYGFPVPTGGSGALTGALVRR 238
Cdd:COG1233  160 LRL------LLRSLRDLLRRYFKDPRLRALLAGQALYLGLSPDRTPA--LYALIAYLEYAGGVWYPKGGMGALADALARL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065 239 LARRGGSVRCGEQVTEVVVRGGRAVGVRTGSGEEVAArRAVLADVSAPALYGSLVAERHLPGRLLGDLKRFQWDFATFKV 318
Cdd:COG1233  232 AEELGGEIRTGAEVERILVEGGRATGVRLADGEEIRA-DAVVSNADPAHTYLRLLGEEALPARYRRRLERFRYSPSAFKL 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065 319 DWALNGPVpwacPEAAHAgTVHLAEGVDgltRFAAQIAMGRVPDRPFALFGQMTTTDPGRSPGGTESAWAYTHVPHrvrg 398
Cdd:COG1233  311 YLGLDGPL----PGLAHH-TIHLSEDYE---AAFDDIFRGRLPEDPSLYVSIPSLTDPSLAPEGKHTLWVLVPVPY---- 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065 399 dagdeGLSGSWDGREQEvMADRVEAQVERYAPGFRGLIRARRVLSPPTMESMDaNLHGGAINGGTTAMHQQLVFRPSPgt 478
Cdd:COG1233  379 -----GLEDAWDELKEE-YAERILARLERYAPGLRDRIVAREVLTPLDFERYL-NLVGGAIYGGAHTLDQSAFFRPSN-- 449
                        490       500
                 ....*....|....*....|....*
gi 753980065 479 grPETPVPGLYLASASAHPGGGVHG 503
Cdd:COG1233  450 --YRTPIPGLYLVGASTHPGGGVPG 472
 
Name Accession Description Interval E-value
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
1-503 1.09e-127

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 381.89  E-value: 1.09e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065   1 MPDAVVIGAGPNGLVAANLLADAGWSVEVLEAQDEPGGAVRhdRGVDPDFTSDLFSSFYPLA-AASPVLAGLRLEREgLE 79
Cdd:COG1233    3 MYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRAR--TFERPGFRFDVGPSVLTMPgVLERLFRELGLEDY-LE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065  80 WSHAPKVLAHPLLDGRCAVLSRDPEETAASLEAFAPGDGAAWQELREVWERLRPDILDALF-TPFPPLRAGARLALRLRA 158
Cdd:COG1233   80 LVPLDPAYRVPFPDGRALDLPRDLERTAAELERLFPGDAEAYRRFLAELRRLYDALLEDLLyRPLLSLRDLLRPLALARL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065 159 AGGlrlartMVLPVRRLGEEEFRGEGGRLLLAGNALHADLAPESAGSggFGWLMSMLAQTYGFPVPTGGSGALTGALVRR 238
Cdd:COG1233  160 LRL------LLRSLRDLLRRYFKDPRLRALLAGQALYLGLSPDRTPA--LYALIAYLEYAGGVWYPKGGMGALADALARL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065 239 LARRGGSVRCGEQVTEVVVRGGRAVGVRTGSGEEVAArRAVLADVSAPALYGSLVAERHLPGRLLGDLKRFQWDFATFKV 318
Cdd:COG1233  232 AEELGGEIRTGAEVERILVEGGRATGVRLADGEEIRA-DAVVSNADPAHTYLRLLGEEALPARYRRRLERFRYSPSAFKL 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065 319 DWALNGPVpwacPEAAHAgTVHLAEGVDgltRFAAQIAMGRVPDRPFALFGQMTTTDPGRSPGGTESAWAYTHVPHrvrg 398
Cdd:COG1233  311 YLGLDGPL----PGLAHH-TIHLSEDYE---AAFDDIFRGRLPEDPSLYVSIPSLTDPSLAPEGKHTLWVLVPVPY---- 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065 399 dagdeGLSGSWDGREQEvMADRVEAQVERYAPGFRGLIRARRVLSPPTMESMDaNLHGGAINGGTTAMHQQLVFRPSPgt 478
Cdd:COG1233  379 -----GLEDAWDELKEE-YAERILARLERYAPGLRDRIVAREVLTPLDFERYL-NLVGGAIYGGAHTLDQSAFFRPSN-- 449
                        490       500
                 ....*....|....*....|....*
gi 753980065 479 grPETPVPGLYLASASAHPGGGVHG 503
Cdd:COG1233  450 --YRTPIPGLYLVGASTHPGGGVPG 472
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
4-503 7.51e-28

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: 116.61  E-value: 7.51e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065    4 AVVIGAGPNGLVAANLLADAGWSVEVLEAQDEPGG--AVRHDRG----------VDPDFTSDLFSsfyplaaaspvLAGL 71
Cdd:TIGR02734   1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGraGVLEDDGfrfdtgptviTMPEALEELFA-----------LAGR 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065   72 RLEREglewshAPKVLAHPLL-----DGRCAVLSRDPEETAASLEAFAPGDGAAWQELREVWERL-RPDILDALFTPFPP 145
Cdd:TIGR02734  70 DLADY------VELVPLDPFYrlcweDGSQLDVDNDQEELEAQIARFNPGDVAGYRRFLDYAERVyREGYRKLGYVPFLS 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065  146 LRAGARLALRLRAagglrlartMVLPVRRLGEEEFRGEGGRLL---LAGNALHADLAPESAGSggFGWLMSMLAQTYGFP 222
Cdd:TIGR02734 144 PRDLLRADAPQLL---------ALLAWRSLYSKVARFFSDERLrqaFSFHALFLGGNPFRTPS--IYALISALEREWGVW 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065  223 VPTGGSGALTGALVRRLARRGGSVRCGEQVTEVVVRGGRAVGVRTGSGEEVAARRAVL-ADVsaPALYGSLVAERHLPGR 301
Cdd:TIGR02734 213 FPRGGTGALVAAMAKLAEDLGGELRLNAEVIRIETEGGRATAVHLADGERLDADAVVSnADL--HHTYRRLLPNHPRRRY 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065  302 LLGDLKRFQWDFATFKVDWALNGpVPWACPEAAHAgTVHLAEGVDGLtrFAAQIAMGRVPDRPFALFGQMTTTDPGRSPG 381
Cdd:TIGR02734 291 PAARLSRKRPSPSLFVLYFGLLG-VDGHWPQLAHH-TLCFGPRYKEL--FDEIFRKGRLAEDPSLYLHRPTVTDPSLAPP 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065  382 GTESAWAYTHVPHRVRGDagdeglsGSWDgREQEVMADRVEAQVE-RYAPGFRGLIRARRVLSPPTMESMDANLHGGAIN 460
Cdd:TIGR02734 367 GCESLYVLAPVPHLGTAD-------VDWS-VEGPRYRDRILAYLEeRAIPGLRDRIVVERTFTPADFRDRYNAWLGSAFS 438
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 753980065  461 GGTTAMhQQLVFRPSpgtGRPETpVPGLYLASASAHPGGGVHG 503
Cdd:TIGR02734 439 LEHTLT-QSAWFRPH---NRDRK-IDNLYLVGAGTHPGAGVPG 476
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
13-301 1.74e-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: 63.28  E-value: 1.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065   13 GLVAANLLADAGWSVEVLEAQDEPGGAVRHDRgvDPDFTSDLFSSFYPlAAASPVLAglRLEREGLEwshapKVLAHPLL 92
Cdd:pfam01593   3 GLAAARELLRAGHDVTVLEARDRVGGRIRTVR--DDGFLIELGAMWFH-GAQPPLLA--LLKELGLE-----DRLVLPDP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065   93 DGRCAVLSRDPEEtaaSLEAFAPGDGAAWQELREVWERLRPDILDALFTPFPPLRAGARLALRLRAAGGLRLARTMVLPV 172
Cdd:pfam01593  73 APFYTVLFAGGRR---YPGDFRRVPAGWEGLLEFGRLLSIPEKLRLGLAALASDALDEFDLDDFSLAESLLFLGRRGPGD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065  173 RRLGEEEFRGEGGRLLLAGNALHAdLAPESAGSGGFGWLMSMLAQTYGFP-VPTGGSgaltGALVRRLAR--RGGSVRCG 249
Cdd:pfam01593 150 VEVWDRLIDPELFAALPFASGAFA-GDPSELSAGLALPLLWALLGEGGSLlLPRGGL----GALPDALAAqlLGGDVRLN 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 753980065  250 EQVTEvVVRGGRAVGVRTGSGEEVAARRAVLAdVSAPALYGSLVAERHLPGR 301
Cdd:pfam01593 225 TRVRS-IDREGDGVTVTLTDGEVIEADAVIVT-VPLGVLKRILFTPPLPPEK 274
PRK07208 PRK07208
hypothetical protein; Provisional
1-38 8.29e-06

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 48.35  E-value: 8.29e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 753980065   1 MPDAVVIGAGPNGLVAANLLADAGWSVEVLEAQDEPGG 38
Cdd:PRK07208   4 KKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGG 41
 
Name Accession Description Interval E-value
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
1-503 1.09e-127

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 381.89  E-value: 1.09e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065   1 MPDAVVIGAGPNGLVAANLLADAGWSVEVLEAQDEPGGAVRhdRGVDPDFTSDLFSSFYPLA-AASPVLAGLRLEREgLE 79
Cdd:COG1233    3 MYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRAR--TFERPGFRFDVGPSVLTMPgVLERLFRELGLEDY-LE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065  80 WSHAPKVLAHPLLDGRCAVLSRDPEETAASLEAFAPGDGAAWQELREVWERLRPDILDALF-TPFPPLRAGARLALRLRA 158
Cdd:COG1233   80 LVPLDPAYRVPFPDGRALDLPRDLERTAAELERLFPGDAEAYRRFLAELRRLYDALLEDLLyRPLLSLRDLLRPLALARL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065 159 AGGlrlartMVLPVRRLGEEEFRGEGGRLLLAGNALHADLAPESAGSggFGWLMSMLAQTYGFPVPTGGSGALTGALVRR 238
Cdd:COG1233  160 LRL------LLRSLRDLLRRYFKDPRLRALLAGQALYLGLSPDRTPA--LYALIAYLEYAGGVWYPKGGMGALADALARL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065 239 LARRGGSVRCGEQVTEVVVRGGRAVGVRTGSGEEVAArRAVLADVSAPALYGSLVAERHLPGRLLGDLKRFQWDFATFKV 318
Cdd:COG1233  232 AEELGGEIRTGAEVERILVEGGRATGVRLADGEEIRA-DAVVSNADPAHTYLRLLGEEALPARYRRRLERFRYSPSAFKL 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065 319 DWALNGPVpwacPEAAHAgTVHLAEGVDgltRFAAQIAMGRVPDRPFALFGQMTTTDPGRSPGGTESAWAYTHVPHrvrg 398
Cdd:COG1233  311 YLGLDGPL----PGLAHH-TIHLSEDYE---AAFDDIFRGRLPEDPSLYVSIPSLTDPSLAPEGKHTLWVLVPVPY---- 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065 399 dagdeGLSGSWDGREQEvMADRVEAQVERYAPGFRGLIRARRVLSPPTMESMDaNLHGGAINGGTTAMHQQLVFRPSPgt 478
Cdd:COG1233  379 -----GLEDAWDELKEE-YAERILARLERYAPGLRDRIVAREVLTPLDFERYL-NLVGGAIYGGAHTLDQSAFFRPSN-- 449
                        490       500
                 ....*....|....*....|....*
gi 753980065 479 grPETPVPGLYLASASAHPGGGVHG 503
Cdd:COG1233  450 --YRTPIPGLYLVGASTHPGGGVPG 472
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
4-503 7.51e-28

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: 116.61  E-value: 7.51e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065    4 AVVIGAGPNGLVAANLLADAGWSVEVLEAQDEPGG--AVRHDRG----------VDPDFTSDLFSsfyplaaaspvLAGL 71
Cdd:TIGR02734   1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGraGVLEDDGfrfdtgptviTMPEALEELFA-----------LAGR 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065   72 RLEREglewshAPKVLAHPLL-----DGRCAVLSRDPEETAASLEAFAPGDGAAWQELREVWERL-RPDILDALFTPFPP 145
Cdd:TIGR02734  70 DLADY------VELVPLDPFYrlcweDGSQLDVDNDQEELEAQIARFNPGDVAGYRRFLDYAERVyREGYRKLGYVPFLS 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065  146 LRAGARLALRLRAagglrlartMVLPVRRLGEEEFRGEGGRLL---LAGNALHADLAPESAGSggFGWLMSMLAQTYGFP 222
Cdd:TIGR02734 144 PRDLLRADAPQLL---------ALLAWRSLYSKVARFFSDERLrqaFSFHALFLGGNPFRTPS--IYALISALEREWGVW 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065  223 VPTGGSGALTGALVRRLARRGGSVRCGEQVTEVVVRGGRAVGVRTGSGEEVAARRAVL-ADVsaPALYGSLVAERHLPGR 301
Cdd:TIGR02734 213 FPRGGTGALVAAMAKLAEDLGGELRLNAEVIRIETEGGRATAVHLADGERLDADAVVSnADL--HHTYRRLLPNHPRRRY 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065  302 LLGDLKRFQWDFATFKVDWALNGpVPWACPEAAHAgTVHLAEGVDGLtrFAAQIAMGRVPDRPFALFGQMTTTDPGRSPG 381
Cdd:TIGR02734 291 PAARLSRKRPSPSLFVLYFGLLG-VDGHWPQLAHH-TLCFGPRYKEL--FDEIFRKGRLAEDPSLYLHRPTVTDPSLAPP 366
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065  382 GTESAWAYTHVPHRVRGDagdeglsGSWDgREQEVMADRVEAQVE-RYAPGFRGLIRARRVLSPPTMESMDANLHGGAIN 460
Cdd:TIGR02734 367 GCESLYVLAPVPHLGTAD-------VDWS-VEGPRYRDRILAYLEeRAIPGLRDRIVVERTFTPADFRDRYNAWLGSAFS 438
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 753980065  461 GGTTAMhQQLVFRPSpgtGRPETpVPGLYLASASAHPGGGVHG 503
Cdd:TIGR02734 439 LEHTLT-QSAWFRPH---NRDRK-IDNLYLVGAGTHPGAGVPG 476
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
1-281 2.46e-13

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 71.88  E-value: 2.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065   1 MPDAVVIGAGPNGLVAANLLADAGWSVEVLEAQDEPGGAVRHDRGVDPDFTSDLFSSFYPlaAASPVLAGLrLEREGLEW 80
Cdd:COG1231    7 GKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGLYAELGAMRIP--PSHTNLLAL-ARELGLPL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065  81 SHAPKVLAHPLLDGRCAVLSRDPEEtaasleafapgdgAAWQELREVWERLRPDILDALftpfpplragarlalRLRAAG 160
Cdd:COG1231   84 EPFPNENGNALLYLGGKRVRAGEIA-------------ADLRGVAELLAKLLRALAAAL---------------DPWAHP 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065 161 GLRLARTMVLPVRRLGEEEFRGEGGRLLLAGNALHADLAPESAgsggFGWLMSMLAQTYGFP--VPTGGSGALTGALVRR 238
Cdd:COG1231  136 AAELDRESLAEWLRRNGASPSARRLLGLLGAGEYGADPDELSL----LDLLRYAASAGGGAQqfRIVGGMDQLPRALAAE 211
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 753980065 239 LarrGGSVRCGEQVTEvVVRGGRAVGVRTGSGEEVAARRAVLA 281
Cdd:COG1231  212 L---GDRIRLGAPVTR-IRQDGDGVTVTTDDGGTVRADAVIVT 250
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
13-301 1.74e-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: 63.28  E-value: 1.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065   13 GLVAANLLADAGWSVEVLEAQDEPGGAVRHDRgvDPDFTSDLFSSFYPlAAASPVLAglRLEREGLEwshapKVLAHPLL 92
Cdd:pfam01593   3 GLAAARELLRAGHDVTVLEARDRVGGRIRTVR--DDGFLIELGAMWFH-GAQPPLLA--LLKELGLE-----DRLVLPDP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065   93 DGRCAVLSRDPEEtaaSLEAFAPGDGAAWQELREVWERLRPDILDALFTPFPPLRAGARLALRLRAAGGLRLARTMVLPV 172
Cdd:pfam01593  73 APFYTVLFAGGRR---YPGDFRRVPAGWEGLLEFGRLLSIPEKLRLGLAALASDALDEFDLDDFSLAESLLFLGRRGPGD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065  173 RRLGEEEFRGEGGRLLLAGNALHAdLAPESAGSGGFGWLMSMLAQTYGFP-VPTGGSgaltGALVRRLAR--RGGSVRCG 249
Cdd:pfam01593 150 VEVWDRLIDPELFAALPFASGAFA-GDPSELSAGLALPLLWALLGEGGSLlLPRGGL----GALPDALAAqlLGGDVRLN 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 753980065  250 EQVTEvVVRGGRAVGVRTGSGEEVAARRAVLAdVSAPALYGSLVAERHLPGR 301
Cdd:pfam01593 225 TRVRS-IDREGDGVTVTLTDGEVIEADAVIVT-VPLGVLKRILFTPPLPPEK 274
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
1-288 1.57e-07

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: 53.68  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065   1 MPDAVVIGAGPNGLVAANLLADAGWSVEVLEAQDEPGGAVRHDR--GVDPDFTSDLFSSFYPLAAAspVLAGLRLEREgL 78
Cdd:COG1232    1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRTVEvdGFRIDRGPHSFLTRDPEVLE--LLRELGLGDE-L 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065  79 EWSHAPK------------------VLAHPLLD----GRCA---VLSRDPEETAASLEAFapgdgaawqeLR-----EVW 128
Cdd:COG1232   78 VWPNTRKsyiyyggklhplpqgplaLLRSPLLSlagkLRALlelLAPRRPPGEDESLAEF----------VRrrfgrEVY 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065 129 ERL-----------RPDILDALFTpFPplragarlalrlraagglrlartmvlpvrRLGEEEFRGEGgrllLAGNALhaD 197
Cdd:COG1232  148 ERLvepllegvyagDPDELSADWA-FP-----------------------------RLKRLELEHGS----LIKGAL--A 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065 198 LAPESAGSGGFGwlmsmlaqtYgfpvPTGGSGALTGALVRRLARrgGSVRCGEQVTEVVVRGGRaVGVRTGSGEEVAARR 277
Cdd:COG1232  192 LRKGAKAGEVFG---------Y----LRGGLGTLVEALAEALEA--GEIRLGTRVTAIEREGGG-WRVTTSDGETIEADA 255
                        330
                 ....*....|.
gi 753980065 278 AVLAdVSAPAL 288
Cdd:COG1232  256 VVSA-TPAPAL 265
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
1-492 2.20e-07

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: 53.32  E-value: 2.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065   1 MPDAVVIGAGPNGLVAANLLADAGWSVEVLEAQDEPGGAVR----HDRGVDPDFTSDLFSSFYP----LAAASPVLAGLR 72
Cdd:COG3349    3 PPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGGRARsfpdPDTGLPIDNGQHVLLGCYRntldLLRRIGAADNLV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065  73 LERE-------GLEWSHAPKVLAHPL--LDG--RCAVLSrdPEETAASLEAFAPGDGAAWQELRE--VWERLR-----PD 134
Cdd:COG3349   83 GPEPlqfplpgGRRWTLRAPRLPAPLhlLRAllRAPGLS--LADRLALLRLLTACRERRWRELDDisVADWLRrhgqsPR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065 135 ILDALFTPfpplragarlalrlraagglrlartmvlpvrrlgeeefrgeggrLLLAgnALHADLAPESAGSGGFGWLMSM 214
Cdd:COG3349  161 LIRRLWEP--------------------------------------------LLLA--ALNTPPEQASARLALTVLRETL 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065 215 LAQTYGFP--VPTGG-SGALTGALVRRLARRGGSVRCGEQVTEVVVRGGRAVGVRTGSGEEVAARRAVLAdVSAPALygs 291
Cdd:COG3349  195 LAGPAASDllVPRGPlSELFVDPALAYLEARGGEVRLGTRVRALEFDGGRVTGLVLADGETVPADAVVLA-VPPEVA--- 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065 292 lvaerhlpGRLLGDLKRFQW--DFATFKVDWALNgpvpwacpeaahagtVHLaegvdgltRFAAQIAMGRVPdrPFALFg 369
Cdd:COG3349  271 --------ARLLPELARLPElgLLAPLEYSPIVN---------------VHL--------WLDRPVTLGPPP--FAGLV- 316
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065 370 qmtttdpgrspgGTESAWAYThvphRVRGDAGDEGL-------SGSWDGREQEVMADRVEAQVERYAPGFRG-LIRARRV 441
Cdd:COG3349  317 ------------GSTSQWVFD----RGAGDGGQGGVlsvvisaADRLLDLSREELAAEVWAELAALLPAAREaLPVWSRV 380
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 753980065 442 LSpptmesmdanlhggainggttamHQQLVFRPSPGTGR----PETPVPGLYLAS 492
Cdd:COG3349  381 VR-----------------------EKRATFAATPGSDRlrpgARTPIPNLFLAG 412
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
6-50 9.30e-07

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: 51.29  E-value: 9.30e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 753980065   6 VIGAGPNGLVAANLLADAGWSVEVLEAQDEPGGAVRHdrGVdPDF 50
Cdd:COG0493  126 VVGSGPAGLAAAYQLARAGHEVTVFEALDKPGGLLRY--GI-PEF 167
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
6-45 2.14e-06

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 45.21  E-value: 2.14e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 753980065    6 VIGAGPNGLVAANLLADAGWSVEVLEAQDEPGGA--------VRHDRG 45
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNaysyrvpgYVFDYG 48
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
1-47 7.94e-06

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: 48.01  E-value: 7.94e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 753980065   1 MPDAVVIGAGPNGLVAANLLADAGWSVEVLEAQDEPGGAVR----HDRGVD 47
Cdd:COG0654    3 RTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRgialSPRSLE 53
PRK07208 PRK07208
hypothetical protein; Provisional
1-38 8.29e-06

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 48.35  E-value: 8.29e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 753980065   1 MPDAVVIGAGPNGLVAANLLADAGWSVEVLEAQDEPGG 38
Cdd:PRK07208   4 KKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGG 41
PLN02976 PLN02976
amine oxidase
5-44 1.30e-05

amine oxidase


Pssm-ID: 215527 [Multi-domain]  Cd Length: 1713  Bit Score: 48.33  E-value: 1.30e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 753980065    5 VVIGAGPNGLVAANLLADAGWSVEVLEAQDEPGGAVRHDR 44
Cdd:PLN02976  697 IVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGRVYTDR 736
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
1-44 1.71e-05

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: 47.16  E-value: 1.71e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 753980065   1 MPDAVVIGAGPNGLVAANLLADAGWSVEVLEAQDEPGGAVRHDR 44
Cdd:COG2072    6 HVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGTWRDNR 49
PRK07233 PRK07233
hypothetical protein; Provisional
5-48 2.00e-05

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 47.19  E-value: 2.00e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 753980065   5 VVIGAGPNGLVAANLLADAGWSVEVLEAQDEPGG-AVRHDRGVDP 48
Cdd:PRK07233   3 AIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGlAASFEFGGLP 47
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
6-38 2.18e-05

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 47.10  E-value: 2.18e-05
                         10        20        30
                 ....*....|....*....|....*....|...
gi 753980065   6 VIGAGPNGLVAANLLADAGWSVEVLEAQDEPGG 38
Cdd:PRK11749 145 VIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG 177
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
3-36 2.44e-05

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


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 46.82  E-value: 2.44e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 753980065   3 DAVVIGAGPNGLVAANLLADAGWSVEVLEAQDEP 36
Cdd:PRK06183  12 DVVIVGAGPVGLTLANLLGQYGVRVLVLERWPTL 45
PRK13984 PRK13984
putative oxidoreductase; Provisional
6-42 3.69e-05

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 46.30  E-value: 3.69e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 753980065   6 VIGAGPNGLVAANLLADAGWSVEVLEAQDEPGGAVRH 42
Cdd:PRK13984 288 IVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMRY 324
PLN02268 PLN02268
probable polyamine oxidase
2-75 4.75e-05

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 45.83  E-value: 4.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065   2 PDAVVIGAGPNGLVAANLLADAGWSVEVLEAQDEPGGAVRHDRGVdpDFTSDLFSSFY-------PLAAASPVLaGLRLE 74
Cdd:PLN02268   1 PSVIVIGGGIAGIAAARALHDASFKVTLLESRDRIGGRVHTDYSF--GFPVDMGASWLhgvcnenPLAPLIGRL-GLPLY 77

                 .
gi 753980065  75 R 75
Cdd:PLN02268  78 R 78
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
229-281 5.05e-05

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 45.67  E-value: 5.05e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 753980065 229 GALTGALVRRLARRGGSVRCGEQVTEVVVRGGRAVGVRTGSGeEVAARRAVLA 281
Cdd:COG0665  151 AKLVRALARAARAAGVRIREGTPVTGLEREGGRVTGVRTERG-TVRADAVVLA 202
PLN02328 PLN02328
lysine-specific histone demethylase 1 homolog
2-41 5.92e-05

lysine-specific histone demethylase 1 homolog


Pssm-ID: 215187 [Multi-domain]  Cd Length: 808  Bit Score: 46.14  E-value: 5.92e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 753980065   2 PDAVVIGAGPNGLVAANLLADAGWSVEVLEAQDEPGGAVR 41
Cdd:PLN02328 239 ANVVVVGAGLAGLVAARQLLSMGFKVVVLEGRARPGGRVK 278
PRK07233 PRK07233
hypothetical protein; Provisional
226-309 9.09e-05

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 44.88  E-value: 9.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065 226 GGSGALTGALVRRLARRGGSVRCGEQVTEVVVRGGRAVGVRTgSGEEVAARRAVLAdvSAPALYGSLVAerHLPGRLLGD 305
Cdd:PRK07233 195 GGFATLIDALAEAIEARGGEIRLGTPVTSVVIDGGGVTGVEV-DGEEEDFDAVIST--APPPILARLVP--DLPADVLAR 269

                 ....
gi 753980065 306 LKRF 309
Cdd:PRK07233 270 LRRI 273
gltD PRK12810
glutamate synthase subunit beta; Reviewed
6-38 1.03e-04

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 44.77  E-value: 1.03e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 753980065   6 VIGAGPNGLVAANLLADAGWSVEVLEAQDEPGG 38
Cdd:PRK12810 148 VVGSGPAGLAAADQLARAGHKVTVFERADRIGG 180
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
6-42 1.39e-04

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 44.48  E-value: 1.39e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 753980065   6 VIGAGPNGLVAANLLADAGWSVEVLEAQDEPGGAVRH 42
Cdd:PRK12771 142 VIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRY 178
PRK12831 PRK12831
putative oxidoreductase; Provisional
6-38 3.62e-04

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 43.08  E-value: 3.62e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 753980065   6 VIGAGPNGLVAANLLADAGWSVEVLEAQDEPGG 38
Cdd:PRK12831 145 VIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGG 177
HI0933_like pfam03486
HI0933-like protein;
2-37 4.07e-04

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 42.95  E-value: 4.07e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 753980065    2 PDAVVIGAGPNGLVAANLLADAGWSVEVLEAQDEPG 37
Cdd:pfam03486   1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
1-42 4.76e-04

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 42.92  E-value: 4.76e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 753980065   1 MPDAVVIGAGPNGLVAANLLADAGWSVEVLEAQDEPGGAVRH 42
Cdd:COG1148  140 NKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQ 181
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
6-50 5.97e-04

bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 42.81  E-value: 5.97e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 753980065   6 VIGAGPNGLVAANLLADAGWSVEVLEAQDEPGGAVRHdrGVdPDF 50
Cdd:PRK12778 436 VIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGGVLKY--GI-PEF 477
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
6-38 7.17e-04

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 41.90  E-value: 7.17e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 753980065   6 VIGAGPNGLVAANLLADAGWSVEVLEAQDEPGG 38
Cdd:PRK12770  23 IIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGG 55
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
3-37 8.97e-04

geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273936 [Multi-domain]  Cd Length: 295  Bit Score: 41.54  E-value: 8.97e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 753980065    3 DAVVIGAGPNGLVAANLLADAGWSVEVLEAQDEPG 37
Cdd:TIGR02032   2 DVVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPR 36
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
6-42 1.09e-03

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 41.64  E-value: 1.09e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 753980065   6 VIGAGPNGLVAANLLADAGWSVEVLEAQDEPGGAVRH 42
Cdd:PRK12814 198 IIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRY 234
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
3-142 1.27e-03

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


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 41.23  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065    3 DAVVIGAGPNGLVAANLLADAGWSVEVLEAQDEPGGAVRHDRG--VDPDFTSDLFSSFYPLAAASPVLAGLRLEREGLEW 80
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSGASGRNAglIHPGLRYLEPSELARLALEALDLWEELEEELGIDC 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 753980065   81 SHAPK---VLAHPLLDGRCAVLSRDPEETAASLEAFAPgdgaawQELREVWERLrPDILDALFTP 142
Cdd:pfam01266  81 GFRRCgvlVLARDEEEEALEKLLAALRRLGVPAELLDA------EELRELEPLL-PGLRGGLFYP 138
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
3-38 2.01e-03

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: 40.84  E-value: 2.01e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 753980065   3 DAVVIGAGPNGLVAANLLADAGWSVEVLEaQDEPGG 38
Cdd:COG1249    5 DLVVIGAGPGGYVAAIRAAQLGLKVALVE-KGRLGG 39
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
234-282 2.40e-03

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 39.95  E-value: 2.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 753980065 234 ALVRRLARRGGSVRCGEQVTEVVVRGGRAVgVRTGSGEEVAARRAVLAD 282
Cdd:COG0644   91 WLAEQAEEAGAEVRTGTRVTDVLRDDGRVV-VRTGDGEEIRADYVVDAD 138
PRK12779 PRK12779
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ...
2-42 2.78e-03

putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional


Pssm-ID: 183740 [Multi-domain]  Cd Length: 944  Bit Score: 40.59  E-value: 2.78e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 753980065   2 PDAVVIGAGPNGLVAANLLADAGWSVEVLEAQDEPGGAVRH 42
Cdd:PRK12779 307 PPIAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVLRY 347
PLN02676 PLN02676
polyamine oxidase
2-41 3.42e-03

polyamine oxidase


Pssm-ID: 215362 [Multi-domain]  Cd Length: 487  Bit Score: 40.08  E-value: 3.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 753980065   2 PDAVVIGAGPNGLVAANLLADAGWS-VEVLEAQDEPGGAVR 41
Cdd:PLN02676  27 PSVIIVGAGMSGISAAKTLSEAGIEdILILEATDRIGGRMR 67
PRK08274 PRK08274
FAD-dependent tricarballylate dehydrogenase TcuA;
226-281 3.69e-03

FAD-dependent tricarballylate dehydrogenase TcuA;


Pssm-ID: 236214 [Multi-domain]  Cd Length: 466  Bit Score: 39.86  E-value: 3.69e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065 226 GGSGALTGALVRRLARRGGSVRCGEQVTEVVVRGGRAVGVRTGSG----EEVAARRAVLA 281
Cdd:PRK08274 128 GGGKALVNALYRSAERLGVEIRYDAPVTALELDDGRFVGARAGSAaggaERIRAKAVVLA 187
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
3-42 3.74e-03

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 39.75  E-value: 3.74e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 753980065   3 DAVVIGAGPNGLVAANLLADAGWSVEVLEAQDEPGGAVRH 42
Cdd:PRK05249   7 DLVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGCTH 46
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
3-131 4.22e-03

bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;


Pssm-ID: 234978 [Multi-domain]  Cd Length: 662  Bit Score: 39.83  E-value: 4.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 753980065   3 DAVVIGAGPNGLVAANLLADAGWSVEVLEAQDEPG-GAVRHDRGVdpdftsdlfssFYPLAAASPVLAGlRLEREG---- 77
Cdd:PRK01747 262 DAAIIGGGIAGAALALALARRGWQVTLYEADEAPAqGASGNRQGA-----------LYPLLSKDDNALS-RFFRAAflfa 329
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 753980065  78 LEWSHAPKVLAHPLLDGRCAV--LSRDPEETA---ASLEAFAPGDGAAWQELREVWERL 131
Cdd:PRK01747 330 RRFYDALPAAGVAFDHDWCGVlqLAWDEKSAEkiaKMLALGLPAELARALDAEEAEELA 388
PRK12834 PRK12834
putative FAD-binding dehydrogenase; Reviewed
2-35 5.43e-03

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 183782 [Multi-domain]  Cd Length: 549  Bit Score: 39.50  E-value: 5.43e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 753980065   2 PDAVVIGAGPNGLVAANLLADAGWSVEVLEAQDE 35
Cdd:PRK12834   5 ADVIVVGAGLAGLVAAAELADAGKRVLLLDQENE 38
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
3-38 6.15e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 39.01  E-value: 6.15e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 753980065   3 DAVVIGAGPNGLVAANLLADAGWSVEVLEaQDEPGG 38
Cdd:PRK06292   5 DVIVIGAGPAGYVAARRAAKLGKKVALIE-KGPLGG 39
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
2-36 6.20e-03

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 39.39  E-value: 6.20e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 753980065   2 PDAVVIGAGPNGLVAANLLADAGWSVEVLEaQDEP 36
Cdd:COG3573    6 ADVIVVGAGLAGLVAAAELADAGRRVLLLD-QEPE 39
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
224-281 6.30e-03

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: 39.05  E-value: 6.30e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 753980065 224 PTGGSG-ALTGALVRRLARRGGSVRCGEQVTEVVVRGGRAVGV----RTGSGEEVAARRAVLA 281
Cdd:COG1053  128 AGDGTGhALLATLYQAALRLGVEIFTETEVLDLIVDDGRVVGVvardRTGEIVRIRAKAVVLA 190
PRK06370 PRK06370
FAD-containing oxidoreductase;
3-31 7.02e-03

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 39.03  E-value: 7.02e-03
                         10        20
                 ....*....|....*....|....*....
gi 753980065   3 DAVVIGAGPNGLVAANLLADAGWSVEVLE 31
Cdd:PRK06370   7 DAIVIGAGQAGPPLAARAAGLGMKVALIE 35
PLN02576 PLN02576
protoporphyrinogen oxidase
3-41 7.18e-03

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 38.84  E-value: 7.18e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 753980065   3 DAVVIGAGPNGLVAA-NLLADAGWSVEVLEAQDEPGGAVR 41
Cdd:PLN02576  14 DVAVVGAGVSGLAAAyALASKHGVNVLVTEARDRVGGNIT 53
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
3-38 7.73e-03

dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.


Pssm-ID: 273568 [Multi-domain]  Cd Length: 460  Bit Score: 38.78  E-value: 7.73e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 753980065    3 DAVVIGAGPNGLVAANLLADAGWSVEVLEaQDEPGG 38
Cdd:TIGR01350   3 DVIVIGGGPGGYVAAIRAAQLGLKVALVE-KEYLGG 37
 
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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