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Conserved domains on  [gi|23821023|ref|NP_690863|]
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L-amino-acid oxidase isoform 1 precursor [Homo sapiens]

Protein Classification

flavin monoamine oxidase family protein( domain architecture ID 11440890)

flavin monoamine oxidase family protein catalyzes the FAD-dependent oxidative deamination of biogenic and xenobiotic amines

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
53-507 7.03e-106

Monoamine oxidase [Amino acid transport and metabolism];


:

Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 325.34  E-value: 7.03e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  53 LNRTLKPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQNTGWIGELGAMRMPSSHRILHKLCQGLG 132
Cdd:COG1231   1 MSRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGLYAELGAMRIPPSHTNLLALARELG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023 133 LNLTKFTQYDKNTWtevhevklrnYVVEKVPeklgyaLRPQEKGHSPEDIYQmALNQALKDLKAL--GCRKAMKKFERHT 210
Cdd:COG1231  81 LPLEPFPNENGNAL----------LYLGGKR------VRAGEIAADLRGVAE-LLAKLLRALAAAldPWAHPAAELDRES 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023 211 LLEYL--LGEGNLSRPAVQLLGDVMSEDGFFYLSFAEALRAHSCLSDRLQYSRIVGGWDLLPRALLSSLSGLVLLNAPVV 288
Cdd:COG1231 144 LAEWLrrNGASPSARRLLGLLGAGEYGADPDELSLLDLLRYAASAGGGAQQFRIVGGMDQLPRALAAELGDRIRLGAPVT 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023 289 AMTQGPHDVHVQietsppARNLKVLKADVVLLTASGPAVKRITFSPPLPRHMQEALRRLHYVPATKVFLSFRRPFWREEH 368
Cdd:COG1231 224 RIRQDGDGVTVT------TDDGGTVRADAVIVTVPPSVLRRIEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEEDG 297

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023 369 IEGGHSNTDRPSRMIFYP--PPREGALLLASYTWSDAAAAFAGLSREEALRLALDDVAALHGPVVRQLwdGTGVVKRWAE 446
Cdd:COG1231 298 LYGGISLTDLPIRQTWYPsnGPDGGAGVLLGYVGGDDARALAALSPEERVAAALEQLARIFGVYAAEP--VDYVSTDWGR 375

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23821023 447 DQHSQGGFVVQPPALWQTEKDDWTVPYGRIYFAGEHTAYP-HGWVETAVKSALRAAIKINSR 507
Cdd:COG1231 376 DPWSRGAYAAAPPGQLTAAGPALAEPDGRIHFAGEHTSDEwPGWVEGALESGERAAAEILAR 437
 
Name Accession Description Interval E-value
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
53-507 7.03e-106

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 325.34  E-value: 7.03e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  53 LNRTLKPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQNTGWIGELGAMRMPSSHRILHKLCQGLG 132
Cdd:COG1231   1 MSRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGLYAELGAMRIPPSHTNLLALARELG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023 133 LNLTKFTQYDKNTWtevhevklrnYVVEKVPeklgyaLRPQEKGHSPEDIYQmALNQALKDLKAL--GCRKAMKKFERHT 210
Cdd:COG1231  81 LPLEPFPNENGNAL----------LYLGGKR------VRAGEIAADLRGVAE-LLAKLLRALAAAldPWAHPAAELDRES 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023 211 LLEYL--LGEGNLSRPAVQLLGDVMSEDGFFYLSFAEALRAHSCLSDRLQYSRIVGGWDLLPRALLSSLSGLVLLNAPVV 288
Cdd:COG1231 144 LAEWLrrNGASPSARRLLGLLGAGEYGADPDELSLLDLLRYAASAGGGAQQFRIVGGMDQLPRALAAELGDRIRLGAPVT 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023 289 AMTQGPHDVHVQietsppARNLKVLKADVVLLTASGPAVKRITFSPPLPRHMQEALRRLHYVPATKVFLSFRRPFWREEH 368
Cdd:COG1231 224 RIRQDGDGVTVT------TDDGGTVRADAVIVTVPPSVLRRIEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEEDG 297

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023 369 IEGGHSNTDRPSRMIFYP--PPREGALLLASYTWSDAAAAFAGLSREEALRLALDDVAALHGPVVRQLwdGTGVVKRWAE 446
Cdd:COG1231 298 LYGGISLTDLPIRQTWYPsnGPDGGAGVLLGYVGGDDARALAALSPEERVAAALEQLARIFGVYAAEP--VDYVSTDWGR 375

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23821023 447 DQHSQGGFVVQPPALWQTEKDDWTVPYGRIYFAGEHTAYP-HGWVETAVKSALRAAIKINSR 507
Cdd:COG1231 376 DPWSRGAYAAAPPGQLTAAGPALAEPDGRIHFAGEHTSDEwPGWVEGALESGERAAAEILAR 437
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 69-501 2.64e-75

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: 245.86  E-value: 2.64e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023    69 VAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQntGWIGELGAMRMPSSHRILHKLCQGLGLNlTKFTQYDKNTWTE 148
Cdd:pfam01593   1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVRDD--GFLIELGAMWFHGAQPPLLALLKELGLE-DRLVLPDPAPFYT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023   149 VHEVKLRNY--VVEKVPEKLGYALRPQEKGHSPEdiyqmALNQALKDLKALGCRKamKKFERHTLLEYLLGEGNLSRPAV 226
Cdd:pfam01593  78 VLFAGGRRYpgDFRRVPAGWEGLLEFGRLLSIPE-----KLRLGLAALASDALDE--FDLDDFSLAESLLFLGRRGPGDV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023   227 QLLGDVMSEDGFFYLSFA--------EALRAHSCLSDRLQYS-------RIVGGWDLLPRALLSSLSGLV-LLNAPVVAM 290
Cdd:pfam01593 151 EVWDRLIDPELFAALPFAsgafagdpSELSAGLALPLLWALLgeggsllLPRGGLGALPDALAAQLLGGDvRLNTRVRSI 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023   291 TQGPHDVHVQIETSpparnlKVLKADVVLLTASGPAVKRITFSPPLPRHMQEALRRLHYVPATKVFLSFRRPFWREE--H 368
Cdd:pfam01593 231 DREGDGVTVTLTDG------EVIEADAVIVTVPLGVLKRILFTPPLPPEKARAIRNLGYGPVNKVHLEFDRKFWPDLglL 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023   369 IEGGHSNTDRPSRMIFYP----PPREGALLLASYTW-SDAAAAFAGLSREEALRLALDDVAALHGPVVrqLWDGTGVVKR 443
Cdd:pfam01593 305 GLLSELLTGLGTAFSWLTfpnrAPPGKGLLLLVYVGpGDRARELEGLSDEELLQAVLRDLRKLFGEEA--PEPLRVLVSD 382

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23821023   444 WAEDQHSQGGFVVQPPALWQTEKDDWTVP-YGRIYFAGEHTA--YPHGwVETAVKSALRAA 501
Cdd:pfam01593 383 WHTDPWPRGSYSLPQYGPGHDDYRPLARTpDPGLFFAGEHTStgYPGT-VEGAIESGRRAA 442
PLN02676 PLN02676
polyamine oxidase
 61-488 6.83e-19

polyamine oxidase


Pssm-ID: 215362 [Multi-domain]  Cd Length: 487  Bit Score: 89.77  E-value: 6.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023   61 RVIVVGAGVAGLVAAKVLSDAGHK-VTILEADNRIGGRIftYRDQNTGWIGELGAMRMpsshrilhklcqgLGLNLTKft 139
Cdd:PLN02676  28 SVIIVGAGMSGISAAKTLSEAGIEdILILEATDRIGGRM--RKANFAGVSVELGANWV-------------EGVGGPE-- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  140 qydKN-TWTEVHEVKLRNYVVEKvpEKLGYALRPQEKGHSPEDIYQMALNQAlkdlkalgcrKAMKKF-ERHTLLEYLLG 217
Cdd:PLN02676  91 ---SNpIWELANKLKLRTFYSDF--DNLSSNIYKQDGGLYPKKVVQKSMKVA----------DASDEFgENLSISLSAKK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  218 EGNLSRPAVQLLGDV-------MSEDGFFY-LSFAEALRAHSC------------------LSDRLQYSRIVG--GWDLL 269
Cdd:PLN02676 156 AVDISILTAQRLFGQvpktpleMVIDYYNYdYEFAEPPRVTSLkntepnptfvdfgedeyfVADPRGYESLVYylAEQFL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  270 PRALLSSLSGLVLLNAPVVAMTQGPHDVHVQIETSpparnlKVLKADVVLLTASGPAVKR--ITFSPPLPRHMQEALRRL 347
Cdd:PLN02676 236 STKSGKITDPRLKLNKVVREISYSKNGVTVKTEDG------SVYRAKYVIVSVSLGVLQSdlIKFKPPLPDWKIEAIYQF 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  348 HYVPATKVFLSFRRPFWREEhiegghsntdrPSRMIF-YPPPREGalllaSYT-WSDAAAAFAG-------LSREEALRL 418
Cdd:PLN02676 310 DMAVYTKIFLKFPYKFWPSG-----------PGTEFFlYAHERRG-----YYPfWQHLENEYPGsnvlfvtVTDEESRRI 373

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  419 -ALDD---VAALHGpVVRQLW-----DGTGV-VKRWAEDQHSQGGFVVQPPALWQTEKDDWTVPYGRIYFAGEHTA---- 484
Cdd:PLN02676 374 eQQPDsetKAEIME-VLRKMFgpnipEATDIlVPRWWSNRFFKGSYSNWPIGVSRYEFDQIRAPVGRVYFTGEHTSekyn 452


                 ....*
gi 23821023  485 -YPHG 488
Cdd:PLN02676 453 gYVHG 457
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
 62-104 2.24e-07

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: 53.43  E-value: 2.24e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 23821023    62 VIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQ 104
Cdd:TIGR02734   1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGRAGVLEDD 43
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 56-100 2.06e-05

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 44.81  E-value: 2.06e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 23821023     56 TLKPQRVIVVGAGVAGLVAAKVLSDAGHKVTIL--------EADNRIGGRIFT 100
Cdd:smart01002  17 GVPPAKVVVIGAGVVGLGAAATAKGLGAEVTVLdvrparlrQLESLLGARFTT 69
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 59-100 1.43e-04

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 44.32  E-value: 1.43e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 23821023  59 PQRVIVVGAGVAGLVAAKVLSDAGHKVTIL--------EADNRIGGRIFT 100
Cdd:cd05305 168 PAKVVILGAGVVGENAARVALGLGAEVTVLdinlerlrYLDDIFGGRVTT 217
 
Name Accession Description Interval E-value
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
53-507 7.03e-106

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 325.34  E-value: 7.03e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  53 LNRTLKPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQNTGWIGELGAMRMPSSHRILHKLCQGLG 132
Cdd:COG1231   1 MSRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGLYAELGAMRIPPSHTNLLALARELG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023 133 LNLTKFTQYDKNTWtevhevklrnYVVEKVPeklgyaLRPQEKGHSPEDIYQmALNQALKDLKAL--GCRKAMKKFERHT 210
Cdd:COG1231  81 LPLEPFPNENGNAL----------LYLGGKR------VRAGEIAADLRGVAE-LLAKLLRALAAAldPWAHPAAELDRES 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023 211 LLEYL--LGEGNLSRPAVQLLGDVMSEDGFFYLSFAEALRAHSCLSDRLQYSRIVGGWDLLPRALLSSLSGLVLLNAPVV 288
Cdd:COG1231 144 LAEWLrrNGASPSARRLLGLLGAGEYGADPDELSLLDLLRYAASAGGGAQQFRIVGGMDQLPRALAAELGDRIRLGAPVT 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023 289 AMTQGPHDVHVQietsppARNLKVLKADVVLLTASGPAVKRITFSPPLPRHMQEALRRLHYVPATKVFLSFRRPFWREEH 368
Cdd:COG1231 224 RIRQDGDGVTVT------TDDGGTVRADAVIVTVPPSVLRRIEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEEDG 297

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023 369 IEGGHSNTDRPSRMIFYP--PPREGALLLASYTWSDAAAAFAGLSREEALRLALDDVAALHGPVVRQLwdGTGVVKRWAE 446
Cdd:COG1231 298 LYGGISLTDLPIRQTWYPsnGPDGGAGVLLGYVGGDDARALAALSPEERVAAALEQLARIFGVYAAEP--VDYVSTDWGR 375

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23821023 447 DQHSQGGFVVQPPALWQTEKDDWTVPYGRIYFAGEHTAYP-HGWVETAVKSALRAAIKINSR 507
Cdd:COG1231 376 DPWSRGAYAAAPPGQLTAAGPALAEPDGRIHFAGEHTSDEwPGWVEGALESGERAAAEILAR 437
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 69-501 2.64e-75

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: 245.86  E-value: 2.64e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023    69 VAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQntGWIGELGAMRMPSSHRILHKLCQGLGLNlTKFTQYDKNTWTE 148
Cdd:pfam01593   1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVRDD--GFLIELGAMWFHGAQPPLLALLKELGLE-DRLVLPDPAPFYT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023   149 VHEVKLRNY--VVEKVPEKLGYALRPQEKGHSPEdiyqmALNQALKDLKALGCRKamKKFERHTLLEYLLGEGNLSRPAV 226
Cdd:pfam01593  78 VLFAGGRRYpgDFRRVPAGWEGLLEFGRLLSIPE-----KLRLGLAALASDALDE--FDLDDFSLAESLLFLGRRGPGDV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023   227 QLLGDVMSEDGFFYLSFA--------EALRAHSCLSDRLQYS-------RIVGGWDLLPRALLSSLSGLV-LLNAPVVAM 290
Cdd:pfam01593 151 EVWDRLIDPELFAALPFAsgafagdpSELSAGLALPLLWALLgeggsllLPRGGLGALPDALAAQLLGGDvRLNTRVRSI 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023   291 TQGPHDVHVQIETSpparnlKVLKADVVLLTASGPAVKRITFSPPLPRHMQEALRRLHYVPATKVFLSFRRPFWREE--H 368
Cdd:pfam01593 231 DREGDGVTVTLTDG------EVIEADAVIVTVPLGVLKRILFTPPLPPEKARAIRNLGYGPVNKVHLEFDRKFWPDLglL 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023   369 IEGGHSNTDRPSRMIFYP----PPREGALLLASYTW-SDAAAAFAGLSREEALRLALDDVAALHGPVVrqLWDGTGVVKR 443
Cdd:pfam01593 305 GLLSELLTGLGTAFSWLTfpnrAPPGKGLLLLVYVGpGDRARELEGLSDEELLQAVLRDLRKLFGEEA--PEPLRVLVSD 382

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23821023   444 WAEDQHSQGGFVVQPPALWQTEKDDWTVP-YGRIYFAGEHTA--YPHGwVETAVKSALRAA 501
Cdd:pfam01593 383 WHTDPWPRGSYSLPQYGPGHDDYRPLARTpDPGLFFAGEHTStgYPGT-VEGAIESGRRAA 442
PLN02676 PLN02676
polyamine oxidase
 61-488 6.83e-19

polyamine oxidase


Pssm-ID: 215362 [Multi-domain]  Cd Length: 487  Bit Score: 89.77  E-value: 6.83e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023   61 RVIVVGAGVAGLVAAKVLSDAGHK-VTILEADNRIGGRIftYRDQNTGWIGELGAMRMpsshrilhklcqgLGLNLTKft 139
Cdd:PLN02676  28 SVIIVGAGMSGISAAKTLSEAGIEdILILEATDRIGGRM--RKANFAGVSVELGANWV-------------EGVGGPE-- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  140 qydKN-TWTEVHEVKLRNYVVEKvpEKLGYALRPQEKGHSPEDIYQMALNQAlkdlkalgcrKAMKKF-ERHTLLEYLLG 217
Cdd:PLN02676  91 ---SNpIWELANKLKLRTFYSDF--DNLSSNIYKQDGGLYPKKVVQKSMKVA----------DASDEFgENLSISLSAKK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  218 EGNLSRPAVQLLGDV-------MSEDGFFY-LSFAEALRAHSC------------------LSDRLQYSRIVG--GWDLL 269
Cdd:PLN02676 156 AVDISILTAQRLFGQvpktpleMVIDYYNYdYEFAEPPRVTSLkntepnptfvdfgedeyfVADPRGYESLVYylAEQFL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  270 PRALLSSLSGLVLLNAPVVAMTQGPHDVHVQIETSpparnlKVLKADVVLLTASGPAVKR--ITFSPPLPRHMQEALRRL 347
Cdd:PLN02676 236 STKSGKITDPRLKLNKVVREISYSKNGVTVKTEDG------SVYRAKYVIVSVSLGVLQSdlIKFKPPLPDWKIEAIYQF 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  348 HYVPATKVFLSFRRPFWREEhiegghsntdrPSRMIF-YPPPREGalllaSYT-WSDAAAAFAG-------LSREEALRL 418
Cdd:PLN02676 310 DMAVYTKIFLKFPYKFWPSG-----------PGTEFFlYAHERRG-----YYPfWQHLENEYPGsnvlfvtVTDEESRRI 373

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  419 -ALDD---VAALHGpVVRQLW-----DGTGV-VKRWAEDQHSQGGFVVQPPALWQTEKDDWTVPYGRIYFAGEHTA---- 484
Cdd:PLN02676 374 eQQPDsetKAEIME-VLRKMFgpnipEATDIlVPRWWSNRFFKGSYSNWPIGVSRYEFDQIRAPVGRVYFTGEHTSekyn 452


                 ....*
gi 23821023  485 -YPHG 488
Cdd:PLN02676 453 gYVHG 457
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 59-507 4.18e-18

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: 86.81  E-value: 4.18e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  59 PQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQntGWIGELGAMRMPSSHRILHKLCQGLGL--NLT 136
Cdd:COG1232   1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRTVEVD--GFRIDRGPHSFLTRDPEVLELLRELGLgdELV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023 137 -------------KFTQYDKNTWTEVHEVKLRnyvvekVPEKLGYA---LRPQEKGHSPEDIYQMALNQ----ALK---- 192
Cdd:COG1232  79 wpntrksyiyyggKLHPLPQGPLALLRSPLLS------LAGKLRALlelLAPRRPPGEDESLAEFVRRRfgreVYErlve 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023 193 ---------DLKALGCRKAMKKferhtLLEYLLGEGNLSRPAVQLLGDVMSEDGFFYL-----SFAEALRahsclsDRLQ 258
Cdd:COG1232 153 pllegvyagDPDELSADWAFPR-----LKRLELEHGSLIKGALALRKGAKAGEVFGYLrgglgTLVEALA------EALE 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023 259 YSRIVggwdllprallsslsglvlLNAPVVAMTQGPHDVHVQIETSpparnlKVLKADVVLLTASGPAVKRITfsPPLPR 338
Cdd:COG1232 222 AGEIR-------------------LGTRVTAIEREGGGWRVTTSDG------ETIEADAVVSATPAPALARLL--APLPP 274

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023 339 HMQEALRRLHYVPATKVFLSFRRPFWREEHIEGG--HSNTDRP-SRMIFYP---PPR--EGALLLASYTWSDAAAAFAGL 410
Cdd:COG1232 275 EVAAALAGIPYASVAVVALGFDRPDLPPPDGFGWlvPRDEGVPiLAVTFSSnkwPHRapDGKVLLRLEVGGAGDPELWQL 354

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023 411 SREEALRLALDDVAALHGPVVRQLWdgtGVVKRW------AEDQHSQggfvvqppalWQTEKDDWTVPYGRIYFAGehtA 484
Cdd:COG1232 355 SDEELVALALADLRKLLGIDAEPVD---TRVVRWpkaypqYTVGHLE----------RVAAIREALAALPGLYLAG---R 418

                       490       500
                ....*....|....*....|....
gi 23821023 485 YPHG-WVETAVKSALRAAIKINSR 507
Cdd:COG1232 419 AYDGvGLPDCIRSGREAAERILAE 442
PLN02328 PLN02328
lysine-specific histone demethylase 1 homolog
 46-504 1.83e-16

lysine-specific histone demethylase 1 homolog


Pssm-ID: 215187 [Multi-domain]  Cd Length: 808  Bit Score: 83.12  E-value: 1.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023   46 LKVVTWGLNRTLKPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQNTGWIG--ELGA--------- 114
Cdd:PLN02328 225 IKEAQLRSFEGVEPANVVVVGAGLAGLVAARQLLSMGFKVVVLEGRARPGGRVKTMKMKGDGVVAaaDLGGsvltgingn 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  115 --------MRMPsshriLHKLCQGLGLNLTKFTQYDKNTWTEVHE---------VKLRNYVVEKVPE---KLGYALRPQE 174
Cdd:PLN02328 305 plgvlarqLGLP-----LHKVRDICPLYLPDGKAVDAEIDSKIEAsfnklldrvCKLRQAMIEEVKSvdvNLGTALEAFR 379

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  175 KGHS-PED-IYQMALNQALKDLKalgcrkamkkFERHTLLeyllgeGNLSRPavqllgdVMSEDGFFYLSfaealrAHSC 252
Cdd:PLN02328 380 HVYKvAEDpQERMLLNWHLANLE----------YANASLM------SNLSMA-------YWDQDDPYEMG------GDHC 430

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  253 LsdrlqysrIVGGWDLLPRALLSslsglvllNAP------VVAMTQGPHDVHVQIETspparnlKVLKADVVLLTASGPA 326
Cdd:PLN02328 431 F--------IPGGNDTFVRELAK--------DLPifyertVESIRYGVDGVIVYAGG-------QEFHGDMVLCTVPLGV 487

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  327 VKR--ITFSPPLPRHMQEALRRLHYVPATKVFLSFRRPFWREEHIEGGHSNTDRPSR---MIFYP-PPREGALLLASYTW 400
Cdd:PLN02328 488 LKKgsIEFYPELPQRKKDAIQRLGYGLLNKVALLFPYNFWGGEIDTFGHLTEDPSMRgefFLFYSySSVSGGPLLIALVA 567

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  401 SDAAAAFAGLSREEALRLALDDVAALHGPVVRQLWDGT-GVVKRWAEDQHSQGGFVVQPPAlwqTEKDDW-----TVPYG 474
Cdd:PLN02328 568 GDAAVKFETLSPVESVKRVLQILRGIFHPKGIVVPDPVqAVCTRWGKDCFTYGSYSYVAVG---SSGDDYdilaeSVGDG 644

                        490       500       510
                 ....*....|....*....|....*....|....*
gi 23821023  475 RIYFAGEHT--AYP---HGwvetAVKSALRAAIKI 504
Cdd:PLN02328 645 RVFFAGEATnkQYPatmHG----AFLSGMREAANI 675
PLN03000 PLN03000
amine oxidase
 60-507 7.22e-16

amine oxidase


Pssm-ID: 178578 [Multi-domain]  Cd Length: 881  Bit Score: 81.22  E-value: 7.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023   60 QRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQ--NTGWIGELGAMRMPSSH-RILHKLCQGLGLNLT 136
Cdd:PLN03000 185 SSVVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGGRVYTKKMEanRVGAAADLGGSVLTGTLgNPLGIIARQLGSSLY 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  137 KftqydkntwtevhevklrnyVVEKVPeklgyALRPQEKGHSPE-DI-YQMALNQALKdlKALGCRKAMKKFERHTLLey 214
Cdd:PLN03000 265 K--------------------VRDKCP-----LYRVDGKPVDPDvDLkVEVAFNQLLD--KASKLRQLMGDVSMDVSL-- 315

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  215 llgeGNLSRPAVQLLGDVMS--EDGFFYLSFAEALRAHSCLSDRLQysriVGGWD------------LLPrALLSSLSGL 280
Cdd:PLN03000 316 ----GAALETFRQVSGNDVAteEMGLFNWHLANLEYANAGLVSKLS----LAFWDqddpydmggdhcFLP-GGNGRLVQA 386

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  281 VLLNAPVV------AMTQGPHDVHVQietsppARNlKVLKADVVLLTASGPAVKR--ITFSPPLPRHMQEALRRLHYVPA 352
Cdd:PLN03000 387 LAENVPILyektvqTIRYGSNGVKVI------AGN-QVYEGDMVLCTVPLGVLKNgsIKFVPELPQRKLDCIKRLGFGLL 459

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  353 TKVFLSFRRPFWREEHIEGGHSnTDRPSR----MIFYP-PPREGALLLASYTWSDAAAAFAGLSREEALRLALDDVAALH 427
Cdd:PLN03000 460 NKVAMLFPYVFWSTDLDTFGHL-TEDPNYrgefFLFYSyAPVAGGPLLIALVAGEAAHKFETMPPTDAVTRVLHILRGIY 538

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  428 GPVVRQLWDGTGVV-KRWAEDQHSQGGFvvqPPALWQTEKDDW-----TVPYGRIYFAGEHTA--YP---HGWVETAVKS 496
Cdd:PLN03000 539 EPQGINVPDPLQTVcTRWGGDPFSLGSY---SNVAVGASGDDYdilaeSVGDGRLFFAGEATTrrYPatmHGAFVTGLRE 615

                        490
                 ....*....|.
gi 23821023  497 ALRAAIKINSR 507
Cdd:PLN03000 616 AANMAQSAKAR 626
PLN02268 PLN02268
probable polyamine oxidase
 62-501 1.97e-13

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 72.41  E-value: 1.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023   62 VIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTyrDQNTGWIGELGA--MRMPSSHRILHKLCQGLGLNLTK-- 137
Cdd:PLN02268   3 VIVIGGGIAGIAAARALHDASFKVTLLESRDRIGGRVHT--DYSFGFPVDMGAswLHGVCNENPLAPLIGRLGLPLYRts 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  138 -------------FTQYDKntwtevHEVKLRNYVVEKVPEKLGYALRPQEK--GHSPEDiyqMALNQALKDLkalgcrka 202
Cdd:PLN02268  81 gdnsvlydhdlesYALFDM------DGNQVPQELVTKVGETFERILEETEKvrDEHEED---MSLLQAISIV-------- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  203 mkkFERHTLLEYllgEGnlsrPAVQLLGdvmsedgfFYLSFAEALRAHSclSDRL------QYSRIVGGWDLL-----PR 271
Cdd:PLN02268 144 ---LERHPELRL---EG----LAHEVLQ--------WYLCRMEGWFAAD--ADTIslkswdQEELLEGGHGLMvrgydPV 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  272 ALLSSLSGLVLLNAPVVAMTQGPHDVHVQIEtspparNLKVLKADVVLLTASGPAVK--RITFSPPLPRHMQEALRRLHY 349
Cdd:PLN02268 204 INTLAKGLDIRLNHRVTKIVRRYNGVKVTVE------DGTTFVADAAIIAVPLGVLKanIIKFEPELPEWKEEAISDLGV 277

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  350 VPATKVFLSFRRPFWREEHIEGG--------------HSNTDRPsrMIFYPPPreGALLLASYTWSD-AAAAFAGLSREE 414
Cdd:PLN02268 278 GIENKIALHFDSVFWPNVEFLGVvaptsygcsyflnlHKATGHP--VLVYMPA--GRLARDIEKLSDeAAANFAMSQLKK 353

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  415 ALRLALDDVAALhgpvvrqlwdgtgvVKRWAEDQHSQGGF----VVQPPALWqtekDDWTVPYGRIYFAGEHTAYPH-GW 489
Cdd:PLN02268 354 MLPDATEPVQYL--------------VSRWGSDPNSLGCYsydlVGKPHDLY----ERLRAPVDNLFFAGEATSSDFpGS 415

                        490
                 ....*....|..
gi 23821023  490 VETAVKSALRAA 501
Cdd:PLN02268 416 VHGAYSTGVMAA 427
PLN02529 PLN02529
lysine-specific histone demethylase 1
 62-508 4.03e-13

lysine-specific histone demethylase 1


Pssm-ID: 178144 [Multi-domain]  Cd Length: 738  Bit Score: 72.23  E-value: 4.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023   62 VIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTyrdQNTGWIGELGAMRMPSS-----HR------------IL 124
Cdd:PLN02529 163 VIIVGAGLAGLAAARQLLSFGFKVVVLEGRNRPGGRVYT---QKMGRKGQFAAVDLGGSvitgiHAnplgvlarqlsiPL 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  125 HKLCQGLGLNLTKFTQYDKNTWTEVHEVklRNYVVEKVPEklgyaLRpQEKGHSPEDIYQMALNQALKDLKALGcrkamK 204
Cdd:PLN02529 240 HKVRDNCPLYKPDGALVDKEIDSNIEFI--FNKLLDKVTE-----LR-QIMGGFANDISLGSVLERLRQLYGVA-----R 306

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  205 KFERHTLLEYLLGegNLSRPAVQLLGDVMS-----EDGFfylsfaEALRAHSCLSDrlqysrivGGWDLLpraLLSSLSG 279
Cdd:PLN02529 307 STEERQLLDWHLA--NLEYANAGCLSDLSAaywdqDDPY------EMGGDHCFLAG--------GNWRLI---NALCEGV 367

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  280 LVLLNAPVVAMTQGPHDVHVqIETSpparnlKVLKADVVLLTASGPAVKR--ITFSPPLPRHMQEALRRLHYVPATKVFL 357
Cdd:PLN02529 368 PIFYGKTVDTIKYGNDGVEV-IAGS------QVFQADMVLCTVPLGVLKKrtIRFEPELPRRKLAAIDRLGFGLLNKVAM 440

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  358 SFRRPFWREEHIEGGHSNTDRPSRMIFYpppregaLLLASYTWSDAAAAFAGLSREEALRLALDDVAA-LHG--PVVRQL 434
Cdd:PLN02529 441 VFPSVFWGEELDTFGCLNESSNKRGEFF-------LFYGYHTVSGGPALVALVAGEAAQRFENTDPSTlLHRvlSVLRGI 513

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  435 WDGTGVV---------KRWAEDQHSQGGFvvqPPALWQTEKDDWTV----PYGRIYFAGEHTA--YP---HGwvetAVKS 496
Cdd:PLN02529 514 YNPKGINvpdpiqticTRWGSDPLSYGSY---SHVRVQSSGSDYDIlaesVSGRLFFAGEATTrqYPatmHG----AFLS 586

                        490       500
                 ....*....|....*....|.
gi 23821023  497 ALRAAIKI---------NSRK 508
Cdd:PLN02529 587 GLREASRIlhvarsqqsNSRK 607
PLN02976 PLN02976
amine oxidase
 60-504 2.26e-12

amine oxidase


Pssm-ID: 215527 [Multi-domain]  Cd Length: 1713  Bit Score: 70.28  E-value: 2.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023    60 QRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQ-----------NTGWIGELGAMRM--PSShrilhK 126
Cdd:PLN02976  694 KKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGRVYTDRSSlsvpvdlgasiITGVEADVATERRpdPSS-----L 768

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023   127 LCQGLGLNLTKFTQ----YDKNTW----TEVHEVKLRNY------VVEKVPEK------------LGYALRPQEKGHSPE 180
Cdd:PLN02976  769 ICAQLGLELTVLNSdcplYDVVTGekvpADLDEALEAEYnsllddMVLLVAQKgehamkmsledgLEYALKRRRMPRPGV 848

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023   181 DIYQMALNQALKDL---KALG-----CRKAMKK-----FERHTL------LEY----LLGEgnLSRPavqllgdVMSEDG 237
Cdd:PLN02976  849 DIDETELGNAADDLydsASTGvdgghCEKESKEdvlspLERRVMnwhfahLEYgcaaLLKE--VSLP-------YWNQDD 919

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023   238 fFYLSFAEalrAHsCLsdrlqysrIVGGWDLLPRAllSSLSGLVLLNAPVVAMTQGPHDV--------HVQIETSpparN 309
Cdd:PLN02976  920 -VYGGFGG---AH-CM--------IKGGYSNVVES--LAEGLDIHLNHVVTDVSYGSKDAgasgssrkKVKVSTS----N 980

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023   310 LKVLKADVVLLTASGPAVK--RITFSPPLPRHMQEALRRLHYVPATKVFLSFRRPFWREEHIEGGHSNTDRPSR----MI 383
Cdd:PLN02976  981 GSEFLGDAVLITVPLGCLKaeTIKFSPPLPDWKYSSIQRLGFGVLNKVVLEFPEVFWDDSVDYFGATAEETDLRgqcfMF 1060

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023   384 FYPPPREGALLLASYTWSDAAAAFAGLSREEALRLALddvaalhgPVVRQLWDGT-------GVVKRWAEDQHSQGGF-V 455
Cdd:PLN02976 1061 WNVKKTVGAPVLIALVVGKAAIDGQSMSSSDHVNHAL--------MVLRKLFGEAlvpdpvaSVVTDWGRDPFSYGAYsY 1132

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 23821023   456 VQPPAlwqtEKDDWTVpYGR-----IYFAGEHTAYPH-GWVETAVKSALRAAIKI 504
Cdd:PLN02976 1133 VAIGA----SGEDYDI-LGRpvencLFFAGEATCKEHpDTVGGAMMSGLREAVRI 1182
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
64-105 3.69e-12

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 61.78  E-value: 3.69e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 23821023    64 VVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQN 105
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYSYRVPG 42
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 59-133 6.25e-12

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: 67.96  E-value: 6.25e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23821023  59 PQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQNTGWIGELGAMRMPSSHRILHKLCQGLGL 133
Cdd:COG3349   3 PPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGGRARSFPDPDTGLPIDNGQHVLLGCYRNTLDLLRRIGA 77
PLN02612 PLN02612
phytoene desaturase
 55-108 7.08e-10

phytoene desaturase


Pssm-ID: 215330 [Multi-domain]  Cd Length: 567  Bit Score: 61.78  E-value: 7.08e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 23821023   55 RTLKPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQNTGW 108
Cdd:PLN02612  89 RPAKPLKVVIAGAGLAGLSTAKYLADAGHKPILLEARDVLGGKVAAWKDEDGDW 142
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 58-97 1.57e-09

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 60.25  E-value: 1.57e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 23821023  58 KPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGR 97
Cdd:COG1233   2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGR 41
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
59-97 1.87e-09

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


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 59.51  E-value: 1.87e-09
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 23821023  59 PQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGR 97
Cdd:COG3380   3 MPDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGGR 41
PRK07233 PRK07233
hypothetical protein; Provisional
 61-96 2.00e-09

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 59.90  E-value: 2.00e-09
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 23821023   61 RVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 96
Cdd:PRK07233   1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGG 36
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 60-96 2.68e-08

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: 56.30  E-value: 2.68e-08
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 23821023  60 QRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 96
Cdd:COG0493 122 KKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG 158
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
58-96 2.86e-08

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


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 56.28  E-value: 2.86e-08
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 23821023  58 KPQRVIVVGAGVAGLVAAKVLSDAgHKVTILEADNRIGG 96
Cdd:COG2907   2 ARMRIAVIGSGISGLTAAWLLSRR-HDVTLFEANDRLGG 39
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 60-96 3.04e-08

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 56.33  E-value: 3.04e-08
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 23821023   60 QRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 96
Cdd:PRK12810 144 KKVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGG 180
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 61-101 3.24e-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: 3.24e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 23821023  61 RVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG--RIFTY 101
Cdd:COG2072   8 DVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGtwRDNRY 50
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
 61-132 9.24e-08

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 54.47  E-value: 9.24e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23821023   61 RVIVVGAGVAGLVAAKVLSDAG--HKVTILEADNRIGGRIFTYRDQntGWIGELGA----MRMPSSHRILHKLcqGLG 132
Cdd:PRK11883   2 KVAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKIQTVRKD--GFPIELGPesflARKPSAPALVKEL--GLE 75
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
60-97 1.30e-07

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 54.48  E-value: 1.30e-07
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 23821023  60 QRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGR 97
Cdd:COG1148 141 KRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGR 178
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
62-96 1.64e-07

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 54.03  E-value: 1.64e-07
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 23821023  62 VIVVGAGVAGLVAAKVLSDAGHKVTILEADN--RIGG 96
Cdd:COG3573   8 VIVVGAGLAGLVAAAELADAGRRVLLLDQEPeaNLGG 44
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
 62-104 2.24e-07

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: 53.43  E-value: 2.24e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 23821023    62 VIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQ 104
Cdd:TIGR02734   1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGRAGVLEDD 43
PLN02568 PLN02568
polyamine oxidase
 58-114 2.47e-07

polyamine oxidase


Pssm-ID: 215308 [Multi-domain]  Cd Length: 539  Bit Score: 53.29  E-value: 2.47e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23821023   58 KPqRVIVVGAGVAGLVAAKVLSDAGH-----KVTILEADNRIGGRIFTyrDQNTGWIGELGA 114
Cdd:PLN02568   5 KP-RIVIIGAGMAGLTAANKLYTSSAandmfELTVVEGGDRIGGRINT--SEFGGERIEMGA 63
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 60-96 4.43e-07

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 52.49  E-value: 4.43e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 23821023   60 QRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 96
Cdd:PRK11749 141 KKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG 177
PRK12834 PRK12834
putative FAD-binding dehydrogenase; Reviewed
 62-99 5.32e-07

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 183782 [Multi-domain]  Cd Length: 549  Bit Score: 52.59  E-value: 5.32e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 23821023   62 VIVVGAGVAGLVAAKVLSDAGHKVTILEADNR--IGGRIF 99
Cdd:PRK12834   7 VIVVGAGLAGLVAAAELADAGKRVLLLDQENEanLGGQAF 46
PLN02576 PLN02576
protoporphyrinogen oxidase
 61-128 6.99e-07

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 51.94  E-value: 6.99e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23821023   61 RVIVVGAGVAGLVAAKVL-SDAGHKVTILEADNRIGGRIFTYrdQNTGWIGELGAMRMPSSHRILHKLC 128
Cdd:PLN02576  14 DVAVVGAGVSGLAAAYALaSKHGVNVLVTEARDRVGGNITSV--SEDGFIWEEGPNSFQPSDPELTSAV 80
PRK07208 PRK07208
hypothetical protein; Provisional
 59-96 1.37e-06

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 51.04  E-value: 1.37e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 23821023   59 PQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 96
Cdd:PRK07208   4 KKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGG 41
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 61-135 1.52e-06

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: 50.47  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023    61 RVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIG----GRiftyrdqNTGWI----GELGAMRMPS----SHRILHKLC 128
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGsgasGR-------NAGLIhpglRYLEPSELARlaleALDLWEELE 73


                  ....*..
gi 23821023   129 QGLGLNL 135
Cdd:pfam01266  74 EELGIDC 80
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 52-94 1.78e-06

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: 50.01  E-value: 1.78e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 23821023    52 GLNRTLKPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRI 94
Cdd:pfam07992 145 ALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRL 187
PLN02487 PLN02487
zeta-carotene desaturase
 61-113 3.70e-06

zeta-carotene desaturase


Pssm-ID: 215268 [Multi-domain]  Cd Length: 569  Bit Score: 49.80  E-value: 3.70e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 23821023   61 RVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQNTGWIgELG 113
Cdd:PLN02487  77 KVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGGKVGSFVDKNGNHI-EMG 128
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
 62-114 4.69e-06

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


Pssm-ID: 213540 [Multi-domain]  Cd Length: 462  Bit Score: 49.06  E-value: 4.69e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 23821023    62 VIVVGAGVAGLVAAKVLS----DAGHKVTILEADNRIGGRIFTyRDQNtGWIGELGA 114
Cdd:TIGR00562   5 VVIIGGGISGLCAAYYLEkeipELPVELTLVEASDRVGGKIQT-VKED-GYLIERGP 59
HI0933_like pfam03486
HI0933-like protein;
61-98 6.97e-06

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 48.73  E-value: 6.97e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 23821023    61 RVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRI 98
Cdd:pfam03486   2 DVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGRKI 39
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
61-135 7.64e-06

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 48.36  E-value: 7.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023  61 RVIVVGAGVAGLVAAKVLSDAGHKVTILEADnRIG----GRiftyrdqNTGWI----GELGAMRM----PSSHRILHKLC 128
Cdd:COG0665   4 DVVVIGGGIAGLSTAYHLARRGLDVTVLERG-RPGsgasGR-------NAGQLrpglAALADRALvrlaREALDLWRELA 75


                ....*..
gi 23821023 129 QGLGLNL 135
Cdd:COG0665  76 AELGIDC 82
YhiN COG2081
Predicted flavoprotein YhiN [General function prediction only];
63-95 8.66e-06

Predicted flavoprotein YhiN [General function prediction only];


Pssm-ID: 441684 [Multi-domain]  Cd Length: 402  Bit Score: 48.12  E-value: 8.66e-06
                        10        20        30
                ....*....|....*....|....*....|...
gi 23821023  63 IVVGAGVAGLVAAKVLSDAGHKVTILEADNRIG 95
Cdd:COG2081   1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVG 33
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 61-113 1.39e-05

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 47.95  E-value: 1.39e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23821023   61 RVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG--R--IFTYR------DQNTGWIGELG 113
Cdd:PRK12771 139 RVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGmmRygIPAYRlprevlDAEIQRILDLG 201
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 56-100 2.06e-05

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 44.81  E-value: 2.06e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 23821023     56 TLKPQRVIVVGAGVAGLVAAKVLSDAGHKVTIL--------EADNRIGGRIFT 100
Cdd:smart01002  17 GVPPAKVVVIGAGVVGLGAAATAKGLGAEVTVLdvrparlrQLESLLGARFTT 69
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 61-94 2.14e-05

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: 42.96  E-value: 2.14e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 23821023    61 RVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRI 94
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRL 34
PTZ00367 PTZ00367
squalene epoxidase; Provisional
 53-96 2.47e-05

squalene epoxidase; Provisional


Pssm-ID: 240384 [Multi-domain]  Cd Length: 567  Bit Score: 47.15  E-value: 2.47e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23821023   53 LNRTL-----KPQR------VIVVGAGVAGLVAAKVLSDAGHKVTILEAD-----NRIGG 96
Cdd:PTZ00367  16 LNRILsrlrfKPARtnydydVIIVGGSIAGPVLAKALSKQGRKVLMLERDlfskpDRIVG 75
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 61-97 2.70e-05

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: 46.47  E-value: 2.70e-05
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 23821023  61 RVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGR 97
Cdd:COG0654   5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPD 41
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 62-96 2.99e-05

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: 46.75  E-value: 2.99e-05
                        10        20        30
                ....*....|....*....|....*....|....*
gi 23821023  62 VIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 96
Cdd:COG1053   6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 61-92 3.84e-05

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: 45.77  E-value: 3.84e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 23821023    61 RVIVVGAGVAGLVAAKVLSDAGHKVTILEADN 92
Cdd:pfam07992   2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEDEG 33
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
60-135 4.47e-05

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 45.90  E-value: 4.47e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23821023  60 QRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFtyrdqntgwiGELGAmrmpsshRILHKLCQGLGLNL 135
Cdd:COG1251 143 KRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQL----------DEEAG-------ALLQRLLEALGVEV 201
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 60-96 6.51e-05

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 45.87  E-value: 6.51e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 23821023   60 QRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 96
Cdd:PRK12814 194 KKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGG 230
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 59-100 1.43e-04

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 44.32  E-value: 1.43e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 23821023  59 PQRVIVVGAGVAGLVAAKVLSDAGHKVTIL--------EADNRIGGRIFT 100
Cdd:cd05305 168 PAKVVILGAGVVGENAARVALGLGAEVTVLdinlerlrYLDDIFGGRVTT 217
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 58-95 1.54e-04

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: 44.45  E-value: 1.54e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 23821023   58 KPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIG 95
Cdd:PRK01747 259 KARDAAIIGGGIAGAALALALARRGWQVTLYEADEAPA 296
PLN02172 PLN02172
flavin-containing monooxygenase FMO GS-OX
 60-96 1.58e-04

flavin-containing monooxygenase FMO GS-OX


Pssm-ID: 215116 [Multi-domain]  Cd Length: 461  Bit Score: 44.47  E-value: 1.58e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 23821023   60 QRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 96
Cdd:PLN02172  11 QHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGG 47
Ald COG0686
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ...
 58-100 1.73e-04

Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and metabolism]; Alanine dehydrogenase (includes sporulation protein SpoVN) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440450 [Multi-domain]  Cd Length: 372  Bit Score: 43.85  E-value: 1.73e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 23821023  58 KPQRVIVVGAGVAGLVAAKVLSDAGHKVTIL--------EADNRIGGRIFT 100
Cdd:COG0686 167 PPAKVVILGGGVVGTNAARMALGLGADVTVLdinldrlrRLDDIFGGRVTT 217
PRK13984 PRK13984
putative oxidoreductase; Provisional
 58-113 1.75e-04

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 44.37  E-value: 1.75e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23821023   58 KPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGR----IFTYR------DQNTGWIGELG 113
Cdd:PRK13984 282 KNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVmrygIPSYRlpdealDKDIAFIEALG 347
BetA COG2303
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ...
 62-97 1.90e-04

Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only]; Choline dehydrogenase or related flavoprotein is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 441878 [Multi-domain]  Cd Length: 531  Bit Score: 44.05  E-value: 1.90e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 23821023  62 VIVVGAGVAGLVAAKVLS-DAGHKVTILEAdnriGGR 97
Cdd:COG2303   7 YVIVGAGSAGCVLANRLSeDAGLRVLLLEA----GGR 39
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 62-96 2.00e-04

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: 43.82  E-value: 2.00e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 23821023    62 VIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 96
Cdd:pfam00890   2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGG 36
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 62-96 2.46e-04

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: 43.92  E-value: 2.46e-04
                        10        20        30
                ....*....|....*....|....*....|....*
gi 23821023  62 VIVVGAGVAGLVAAKVLSDAGHKVTILEADnRIGG 96
Cdd:COG1249   6 LVVIGAGPGGYVAAIRAAQLGLKVALVEKG-RLGG 39
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
67-98 2.69e-04

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 43.03  E-value: 2.69e-04
                        10        20        30
                ....*....|....*....|....*....|..
gi 23821023  67 AGVAGLVAAKVLSDAGHKVTILEADNRIGGRI 98
Cdd:COG0644   1 AGPAGSAAARRLARAGLSVLLLEKGSFPGDKI 32
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 55-98 3.22e-04

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 42.88  E-value: 3.22e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 23821023  55 RTLKPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRI 98
Cdd:COG0446 120 KEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGVL 163
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 59-97 4.51e-04

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: 42.77  E-value: 4.51e-04
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 23821023  59 PQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGR 97
Cdd:COG1249 168 PKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPG 206
PRK06753 PRK06753
hypothetical protein; Provisional
 61-94 5.76e-04

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 42.37  E-value: 5.76e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 23821023   61 RVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRI 94
Cdd:PRK06753   2 KIAIIGAGIGGLTAAALLQEQGHEVKVFEKNESV 35
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
 59-96 7.96e-04

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 42.46  E-value: 7.96e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 23821023    59 PQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 96
Cdd:PTZ00306  409 PARVIVVGGGLAGCSAAIEAASCGAQVILLEKEAKLGG 446
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
 58-89 1.36e-03

Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.


Pssm-ID: 426165 [Multi-domain]  Cd Length: 213  Bit Score: 40.17  E-value: 1.36e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 23821023    58 KPQRVIVVGAGVAGLVAAKVLSDAGHKVTILE 89
Cdd:pfam01262  27 APAKVLVIGGGVAGLNAAATAKGLGAIVTILD 58
PRK12831 PRK12831
putative oxidoreductase; Provisional
 58-96 1.65e-03

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 41.16  E-value: 1.65e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 23821023   58 KPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 96
Cdd:PRK12831 139 KGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGG 177
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 43-91 1.77e-03

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 40.44  E-value: 1.77e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 23821023  43 EQLLKVVTWGLNRTLKPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEAD 91
Cdd:COG0569  79 LEALRRRRMERGIKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVIDKD 127
PRK10015 PRK10015
oxidoreductase; Provisional
 63-101 1.83e-03

oxidoreductase; Provisional


Pssm-ID: 182194 [Multi-domain]  Cd Length: 429  Bit Score: 41.12  E-value: 1.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 23821023   63 IVVGAGVAGLVAAKVLSDAGHKVTILE------ADNRIGGRIFTY 101
Cdd:PRK10015   9 IVVGAGVAGSVAALVMARAGLDVLVIErgdsagCKNMTGGRLYAH 53
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 62-96 2.02e-03

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 40.90  E-value: 2.02e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 23821023   62 VIVVGAGVAGLVAAKVLSDAGHKVTILEADNrIGG 96
Cdd:PRK06416   7 VIVIGAGPGGYVAAIRAAQLGLKVAIVEKEK-LGG 40
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 59-96 2.29e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 40.55  E-value: 2.29e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 23821023   59 PQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 96
Cdd:PRK06292 169 PKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILP 206
PRK00711 PRK00711
D-amino acid dehydrogenase;
61-89 3.06e-03

D-amino acid dehydrogenase;


Pssm-ID: 234819 [Multi-domain]  Cd Length: 416  Bit Score: 40.17  E-value: 3.06e-03
                         10        20
                 ....*....|....*....|....*....
gi 23821023   61 RVIVVGAGVAGLVAAKVLSDAGHKVTILE 89
Cdd:PRK00711   2 RVVVLGSGVIGVTSAWYLAQAGHEVTVID 30
PRK06370 PRK06370
FAD-containing oxidoreductase;
63-96 3.36e-03

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 40.19  E-value: 3.36e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 23821023   63 IVVGAGVAGLVAAKVLSDAGHKVTILEaDNRIGG 96
Cdd:PRK06370   9 IVIGAGQAGPPLAARAAGLGMKVALIE-RGLLGG 41
PRK08163 PRK08163
3-hydroxybenzoate 6-monooxygenase;
58-95 3.83e-03

3-hydroxybenzoate 6-monooxygenase;


Pssm-ID: 181262 [Multi-domain]  Cd Length: 396  Bit Score: 40.02  E-value: 3.83e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 23821023   58 KPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIG 95
Cdd:PRK08163   3 KVTPVLIVGGGIGGLAAALALARQGIKVKLLEQAAEIG 40
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 62-96 4.49e-03

FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 39.51  E-value: 4.49e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 23821023    62 VIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 96
Cdd:pfam12831   2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGG 36
PRK12843 PRK12843
FAD-dependent oxidoreductase;
62-96 5.81e-03

FAD-dependent oxidoreductase;


Pssm-ID: 237225 [Multi-domain]  Cd Length: 578  Bit Score: 39.33  E-value: 5.81e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 23821023   62 VIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 96
Cdd:PRK12843  19 VIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGG 53
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
62-98 7.88e-03

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 38.56  E-value: 7.88e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 23821023  62 VIVVGAGVAGLVAAKVLSDAGHKVTILEADnRIGGRI 98
Cdd:COG0492   3 VVIIGAGPAGLTAAIYAARAGLKTLVIEGG-EPGGQL 38
PRK10157 PRK10157
putative oxidoreductase FixC; Provisional
 63-101 7.88e-03

putative oxidoreductase FixC; Provisional


Pssm-ID: 182273 [Multi-domain]  Cd Length: 428  Bit Score: 38.74  E-value: 7.88e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 23821023   63 IVVGAGVAGLVAAKVLSDAGHKVTILE------ADNRIGGRIFTY 101
Cdd:PRK10157   9 IIVGAGLAGSVAALVLAREGAQVLVIErgnsagAKNVTGGRLYAH 53
PntA COG3288
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
56-78 9.58e-03

NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];


Pssm-ID: 442518 [Multi-domain]  Cd Length: 359  Bit Score: 38.45  E-value: 9.58e-03
                        10        20
                ....*....|....*....|....*.
gi 23821023  56 TLKPQRVIVVGAGVAGLVA---AKVL 78
Cdd:COG3288 161 TIRPAGVLVVGAGVAGLQAiatAKRL 186
 
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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