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Conserved domains on  [gi|384381477|ref|NP_001244947|]
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L-amino-acid oxidase isoform 2 precursor [Homo sapiens]

Protein Classification

flavin monoamine oxidase family protein( domain architecture ID 11440890)

flavin monoamine oxidase family protein functions as an oxidoreductase that catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant

CATH:  3.50.50.60|1.10.405.10
EC:  1.-.-.-
Gene Ontology:  GO:0000166|GO:0016491
SCOP:  4000128

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];
75-529 2.61e-106

Monoamine oxidase [Amino acid transport and metabolism];


:

Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 326.88  E-value: 2.61e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477  75 LNRTLKPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQNTGWIGELGAMRMPSSHRILHKLCQGLG 154
Cdd:COG1231    1 MSRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGLYAELGAMRIPPSHTNLLALARELG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 155 LNLTKFTQYDKNTWtevhevklrnYVVEKVPeklgyaLRPQEKGHSPEDIYQmALNQALKDLKAL--GCRKAMKKFERHT 232
Cdd:COG1231   81 LPLEPFPNENGNAL----------LYLGGKR------VRAGEIAADLRGVAE-LLAKLLRALAAAldPWAHPAAELDRES 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 233 LLEYL--LGEGNLSRPAVQLLGDVMSEDGFFYLSFAEALRAHSCLSDRLQYSRIVGGWDLLPRALLSSLSGLVLLNAPVV 310
Cdd:COG1231  144 LAEWLrrNGASPSARRLLGLLGAGEYGADPDELSLLDLLRYAASAGGGAQQFRIVGGMDQLPRALAAELGDRIRLGAPVT 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 311 AMTQGPHDVHVQietsppARNLKVLKADVVLLTASGPAVKRITFSPPLPRHMQEALRRLHYVPATKVFLSFRRPFWREEH 390
Cdd:COG1231  224 RIRQDGDGVTVT------TDDGGTVRADAVIVTVPPSVLRRIEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEEDG 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 391 IEGGHSNTDRPSRMIFYP--PPREGALLLASYTWSDAAAAFAGLSREEALRLALDDVAALHGPVVRQLwdGTGVVKRWAE 468
Cdd:COG1231  298 LYGGISLTDLPIRQTWYPsnGPDGGAGVLLGYVGGDDARALAALSPEERVAAALEQLARIFGVYAAEP--VDYVSTDWGR 375

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384381477 469 DQHSQGGFVVQPPALWQTEKDDWTVPYGRIYFAGEHTAYP-HGWVETAVKSALRAAIKINSR 529
Cdd:COG1231  376 DPWSRGAYAAAPPGQLTAAGPALAEPDGRIHFAGEHTSDEwPGWVEGALESGERAAAEILAR 437
 
Name Accession Description Interval E-value
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
75-529 2.61e-106

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 326.88  E-value: 2.61e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477  75 LNRTLKPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQNTGWIGELGAMRMPSSHRILHKLCQGLG 154
Cdd:COG1231    1 MSRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGLYAELGAMRIPPSHTNLLALARELG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 155 LNLTKFTQYDKNTWtevhevklrnYVVEKVPeklgyaLRPQEKGHSPEDIYQmALNQALKDLKAL--GCRKAMKKFERHT 232
Cdd:COG1231   81 LPLEPFPNENGNAL----------LYLGGKR------VRAGEIAADLRGVAE-LLAKLLRALAAAldPWAHPAAELDRES 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 233 LLEYL--LGEGNLSRPAVQLLGDVMSEDGFFYLSFAEALRAHSCLSDRLQYSRIVGGWDLLPRALLSSLSGLVLLNAPVV 310
Cdd:COG1231  144 LAEWLrrNGASPSARRLLGLLGAGEYGADPDELSLLDLLRYAASAGGGAQQFRIVGGMDQLPRALAAELGDRIRLGAPVT 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 311 AMTQGPHDVHVQietsppARNLKVLKADVVLLTASGPAVKRITFSPPLPRHMQEALRRLHYVPATKVFLSFRRPFWREEH 390
Cdd:COG1231  224 RIRQDGDGVTVT------TDDGGTVRADAVIVTVPPSVLRRIEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEEDG 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 391 IEGGHSNTDRPSRMIFYP--PPREGALLLASYTWSDAAAAFAGLSREEALRLALDDVAALHGPVVRQLwdGTGVVKRWAE 468
Cdd:COG1231  298 LYGGISLTDLPIRQTWYPsnGPDGGAGVLLGYVGGDDARALAALSPEERVAAALEQLARIFGVYAAEP--VDYVSTDWGR 375

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384381477 469 DQHSQGGFVVQPPALWQTEKDDWTVPYGRIYFAGEHTAYP-HGWVETAVKSALRAAIKINSR 529
Cdd:COG1231  376 DPWSRGAYAAAPPGQLTAAGPALAEPDGRIHFAGEHTSDEwPGWVEGALESGERAAAEILAR 437
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 91-523 8.98e-76

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: 247.79  E-value: 8.98e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477   91 VAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQntGWIGELGAMRMPSSHRILHKLCQGLGLNlTKFTQYDKNTWTE 170
Cdd:pfam01593   1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVRDD--GFLIELGAMWFHGAQPPLLALLKELGLE-DRLVLPDPAPFYT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477  171 VHEVKLRNY--VVEKVPEKLGYALRPQEKGHSPEdiyqmALNQALKDLKALGCRKamKKFERHTLLEYLLGEGNLSRPAV 248
Cdd:pfam01593  78 VLFAGGRRYpgDFRRVPAGWEGLLEFGRLLSIPE-----KLRLGLAALASDALDE--FDLDDFSLAESLLFLGRRGPGDV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477  249 QLLGDVMSEDGFFYLSFA--------EALRAHSCLSDRLQYS-------RIVGGWDLLPRALLSSLSGLV-LLNAPVVAM 312
Cdd:pfam01593 151 EVWDRLIDPELFAALPFAsgafagdpSELSAGLALPLLWALLgeggsllLPRGGLGALPDALAAQLLGGDvRLNTRVRSI 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477  313 TQGPHDVHVQIETSpparnlKVLKADVVLLTASGPAVKRITFSPPLPRHMQEALRRLHYVPATKVFLSFRRPFWREE--H 390
Cdd:pfam01593 231 DREGDGVTVTLTDG------EVIEADAVIVTVPLGVLKRILFTPPLPPEKARAIRNLGYGPVNKVHLEFDRKFWPDLglL 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477  391 IEGGHSNTDRPSRMIFYP----PPREGALLLASYTW-SDAAAAFAGLSREEALRLALDDVAALHGPVVrqLWDGTGVVKR 465
Cdd:pfam01593 305 GLLSELLTGLGTAFSWLTfpnrAPPGKGLLLLVYVGpGDRARELEGLSDEELLQAVLRDLRKLFGEEA--PEPLRVLVSD 382

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384381477  466 WAEDQHSQGGFVVQPPALWQTEKDDWTVP-YGRIYFAGEHTA--YPHGwVETAVKSALRAA 523
Cdd:pfam01593 383 WHTDPWPRGSYSLPQYGPGHDDYRPLARTpDPGLFFAGEHTStgYPGT-VEGAIESGRRAA 442
PLN02676 PLN02676
polyamine oxidase
 83-510 7.73e-19

polyamine oxidase


Pssm-ID: 215362 [Multi-domain]  Cd Length: 487  Bit Score: 89.77  E-value: 7.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477  83 RVIVVGAGVAGLVAAKVLSDAGHK-VTILEADNRIGGRIftYRDQNTGWIGELGAMRMpsshrilhklcqgLGLNLTKft 161
Cdd:PLN02676  28 SVIIVGAGMSGISAAKTLSEAGIEdILILEATDRIGGRM--RKANFAGVSVELGANWV-------------EGVGGPE-- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 162 qydKN-TWTEVHEVKLRNYVVEKvpEKLGYALRPQEKGHSPEDIYQMALNQAlkdlkalgcrKAMKKF-ERHTLLEYLLG 239
Cdd:PLN02676  91 ---SNpIWELANKLKLRTFYSDF--DNLSSNIYKQDGGLYPKKVVQKSMKVA----------DASDEFgENLSISLSAKK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 240 EGNLSRPAVQLLGDV-------MSEDGFFY-LSFAEALRAHSC------------------LSDRLQYSRIVG--GWDLL 291
Cdd:PLN02676 156 AVDISILTAQRLFGQvpktpleMVIDYYNYdYEFAEPPRVTSLkntepnptfvdfgedeyfVADPRGYESLVYylAEQFL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 292 PRALLSSLSGLVLLNAPVVAMTQGPHDVHVQIETSpparnlKVLKADVVLLTASGPAVKR--ITFSPPLPRHMQEALRRL 369
Cdd:PLN02676 236 STKSGKITDPRLKLNKVVREISYSKNGVTVKTEDG------SVYRAKYVIVSVSLGVLQSdlIKFKPPLPDWKIEAIYQF 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 370 HYVPATKVFLSFRRPFWREEhiegghsntdrPSRMIF-YPPPREGalllaSYT-WSDAAAAFAG-------LSREEALRL 440
Cdd:PLN02676 310 DMAVYTKIFLKFPYKFWPSG-----------PGTEFFlYAHERRG-----YYPfWQHLENEYPGsnvlfvtVTDEESRRI 373

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 441 -ALDD---VAALHGpVVRQLW-----DGTGV-VKRWAEDQHSQGGFVVQPPALWQTEKDDWTVPYGRIYFAGEHTA---- 506
Cdd:PLN02676 374 eQQPDsetKAEIME-VLRKMFgpnipEATDIlVPRWWSNRFFKGSYSNWPIGVSRYEFDQIRAPVGRVYFTGEHTSekyn 452


                 ....*
gi 384381477 507 -YPHG 510
Cdd:PLN02676 453 gYVHG 457
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
 84-126 2.03e-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: 53.82  E-value: 2.03e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 384381477   84 VIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQ 126
Cdd:TIGR02734   1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGRAGVLEDD 43
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 78-122 2.01e-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: 2.01e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 384381477    78 TLKPQRVIVVGAGVAGLVAAKVLSDAGHKVTIL--------EADNRIGGRIFT 122
Cdd:smart01002  17 GVPPAKVVVIGAGVVGLGAAATAKGLGAEVTVLdvrparlrQLESLLGARFTT 69
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 81-122 1.37e-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: 1.37e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 384381477  81 PQRVIVVGAGVAGLVAAKVLSDAGHKVTIL--------EADNRIGGRIFT 122
Cdd:cd05305  168 PAKVVILGAGVVGENAARVALGLGAEVTVLdinlerlrYLDDIFGGRVTT 217
 
Name Accession Description Interval E-value
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
75-529 2.61e-106

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 326.88  E-value: 2.61e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477  75 LNRTLKPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQNTGWIGELGAMRMPSSHRILHKLCQGLG 154
Cdd:COG1231    1 MSRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGLYAELGAMRIPPSHTNLLALARELG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 155 LNLTKFTQYDKNTWtevhevklrnYVVEKVPeklgyaLRPQEKGHSPEDIYQmALNQALKDLKAL--GCRKAMKKFERHT 232
Cdd:COG1231   81 LPLEPFPNENGNAL----------LYLGGKR------VRAGEIAADLRGVAE-LLAKLLRALAAAldPWAHPAAELDRES 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 233 LLEYL--LGEGNLSRPAVQLLGDVMSEDGFFYLSFAEALRAHSCLSDRLQYSRIVGGWDLLPRALLSSLSGLVLLNAPVV 310
Cdd:COG1231  144 LAEWLrrNGASPSARRLLGLLGAGEYGADPDELSLLDLLRYAASAGGGAQQFRIVGGMDQLPRALAAELGDRIRLGAPVT 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 311 AMTQGPHDVHVQietsppARNLKVLKADVVLLTASGPAVKRITFSPPLPRHMQEALRRLHYVPATKVFLSFRRPFWREEH 390
Cdd:COG1231  224 RIRQDGDGVTVT------TDDGGTVRADAVIVTVPPSVLRRIEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEEDG 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 391 IEGGHSNTDRPSRMIFYP--PPREGALLLASYTWSDAAAAFAGLSREEALRLALDDVAALHGPVVRQLwdGTGVVKRWAE 468
Cdd:COG1231  298 LYGGISLTDLPIRQTWYPsnGPDGGAGVLLGYVGGDDARALAALSPEERVAAALEQLARIFGVYAAEP--VDYVSTDWGR 375

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384381477 469 DQHSQGGFVVQPPALWQTEKDDWTVPYGRIYFAGEHTAYP-HGWVETAVKSALRAAIKINSR 529
Cdd:COG1231  376 DPWSRGAYAAAPPGQLTAAGPALAEPDGRIHFAGEHTSDEwPGWVEGALESGERAAAEILAR 437
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 91-523 8.98e-76

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: 247.79  E-value: 8.98e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477   91 VAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQntGWIGELGAMRMPSSHRILHKLCQGLGLNlTKFTQYDKNTWTE 170
Cdd:pfam01593   1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVRDD--GFLIELGAMWFHGAQPPLLALLKELGLE-DRLVLPDPAPFYT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477  171 VHEVKLRNY--VVEKVPEKLGYALRPQEKGHSPEdiyqmALNQALKDLKALGCRKamKKFERHTLLEYLLGEGNLSRPAV 248
Cdd:pfam01593  78 VLFAGGRRYpgDFRRVPAGWEGLLEFGRLLSIPE-----KLRLGLAALASDALDE--FDLDDFSLAESLLFLGRRGPGDV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477  249 QLLGDVMSEDGFFYLSFA--------EALRAHSCLSDRLQYS-------RIVGGWDLLPRALLSSLSGLV-LLNAPVVAM 312
Cdd:pfam01593 151 EVWDRLIDPELFAALPFAsgafagdpSELSAGLALPLLWALLgeggsllLPRGGLGALPDALAAQLLGGDvRLNTRVRSI 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477  313 TQGPHDVHVQIETSpparnlKVLKADVVLLTASGPAVKRITFSPPLPRHMQEALRRLHYVPATKVFLSFRRPFWREE--H 390
Cdd:pfam01593 231 DREGDGVTVTLTDG------EVIEADAVIVTVPLGVLKRILFTPPLPPEKARAIRNLGYGPVNKVHLEFDRKFWPDLglL 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477  391 IEGGHSNTDRPSRMIFYP----PPREGALLLASYTW-SDAAAAFAGLSREEALRLALDDVAALHGPVVrqLWDGTGVVKR 465
Cdd:pfam01593 305 GLLSELLTGLGTAFSWLTfpnrAPPGKGLLLLVYVGpGDRARELEGLSDEELLQAVLRDLRKLFGEEA--PEPLRVLVSD 382

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 384381477  466 WAEDQHSQGGFVVQPPALWQTEKDDWTVP-YGRIYFAGEHTA--YPHGwVETAVKSALRAA 523
Cdd:pfam01593 383 WHTDPWPRGSYSLPQYGPGHDDYRPLARTpDPGLFFAGEHTStgYPGT-VEGAIESGRRAA 442
PLN02676 PLN02676
polyamine oxidase
 83-510 7.73e-19

polyamine oxidase


Pssm-ID: 215362 [Multi-domain]  Cd Length: 487  Bit Score: 89.77  E-value: 7.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477  83 RVIVVGAGVAGLVAAKVLSDAGHK-VTILEADNRIGGRIftYRDQNTGWIGELGAMRMpsshrilhklcqgLGLNLTKft 161
Cdd:PLN02676  28 SVIIVGAGMSGISAAKTLSEAGIEdILILEATDRIGGRM--RKANFAGVSVELGANWV-------------EGVGGPE-- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 162 qydKN-TWTEVHEVKLRNYVVEKvpEKLGYALRPQEKGHSPEDIYQMALNQAlkdlkalgcrKAMKKF-ERHTLLEYLLG 239
Cdd:PLN02676  91 ---SNpIWELANKLKLRTFYSDF--DNLSSNIYKQDGGLYPKKVVQKSMKVA----------DASDEFgENLSISLSAKK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 240 EGNLSRPAVQLLGDV-------MSEDGFFY-LSFAEALRAHSC------------------LSDRLQYSRIVG--GWDLL 291
Cdd:PLN02676 156 AVDISILTAQRLFGQvpktpleMVIDYYNYdYEFAEPPRVTSLkntepnptfvdfgedeyfVADPRGYESLVYylAEQFL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 292 PRALLSSLSGLVLLNAPVVAMTQGPHDVHVQIETSpparnlKVLKADVVLLTASGPAVKR--ITFSPPLPRHMQEALRRL 369
Cdd:PLN02676 236 STKSGKITDPRLKLNKVVREISYSKNGVTVKTEDG------SVYRAKYVIVSVSLGVLQSdlIKFKPPLPDWKIEAIYQF 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 370 HYVPATKVFLSFRRPFWREEhiegghsntdrPSRMIF-YPPPREGalllaSYT-WSDAAAAFAG-------LSREEALRL 440
Cdd:PLN02676 310 DMAVYTKIFLKFPYKFWPSG-----------PGTEFFlYAHERRG-----YYPfWQHLENEYPGsnvlfvtVTDEESRRI 373

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 441 -ALDD---VAALHGpVVRQLW-----DGTGV-VKRWAEDQHSQGGFVVQPPALWQTEKDDWTVPYGRIYFAGEHTA---- 506
Cdd:PLN02676 374 eQQPDsetKAEIME-VLRKMFgpnipEATDIlVPRWWSNRFFKGSYSNWPIGVSRYEFDQIRAPVGRVYFTGEHTSekyn 452


                 ....*
gi 384381477 507 -YPHG 510
Cdd:PLN02676 453 gYVHG 457
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 81-529 1.76e-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: 88.35  E-value: 1.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477  81 PQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQntGWIGELGAMRMPSSHRILHKLCQGLGL--NLT 158
Cdd:COG1232    1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRTVEVD--GFRIDRGPHSFLTRDPEVLELLRELGLgdELV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 159 -------------KFTQYDKNTWTEVHEVKLRnyvvekVPEKLGYA---LRPQEKGHSPEDIYQMALNQ----ALK---- 214
Cdd:COG1232   79 wpntrksyiyyggKLHPLPQGPLALLRSPLLS------LAGKLRALlelLAPRRPPGEDESLAEFVRRRfgreVYErlve 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 215 ---------DLKALGCRKAMKKferhtLLEYLLGEGNLSRPAVQLLGDVMSEDGFFYL-----SFAEALRahsclsDRLQ 280
Cdd:COG1232  153 pllegvyagDPDELSADWAFPR-----LKRLELEHGSLIKGALALRKGAKAGEVFGYLrgglgTLVEALA------EALE 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 281 YSRIVggwdllprallsslsglvlLNAPVVAMTQGPHDVHVQIETSpparnlKVLKADVVLLTASGPAVKRITfsPPLPR 360
Cdd:COG1232  222 AGEIR-------------------LGTRVTAIEREGGGWRVTTSDG------ETIEADAVVSATPAPALARLL--APLPP 274

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 361 HMQEALRRLHYVPATKVFLSFRRPFWREEHIEGG--HSNTDRP-SRMIFYP---PPR--EGALLLASYTWSDAAAAFAGL 432
Cdd:COG1232  275 EVAAALAGIPYASVAVVALGFDRPDLPPPDGFGWlvPRDEGVPiLAVTFSSnkwPHRapDGKVLLRLEVGGAGDPELWQL 354

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 433 SREEALRLALDDVAALHGPVVRQLWdgtGVVKRW------AEDQHSQggfvvqppalWQTEKDDWTVPYGRIYFAGehtA 506
Cdd:COG1232  355 SDEELVALALADLRKLLGIDAEPVD---TRVVRWpkaypqYTVGHLE----------RVAAIREALAALPGLYLAG---R 418

                        490       500
                 ....*....|....*....|....
gi 384381477 507 YPHG-WVETAVKSALRAAIKINSR 529
Cdd:COG1232  419 AYDGvGLPDCIRSGREAAERILAE 442
PLN02328 PLN02328
lysine-specific histone demethylase 1 homolog
 68-526 2.04e-16

lysine-specific histone demethylase 1 homolog


Pssm-ID: 215187 [Multi-domain]  Cd Length: 808  Bit Score: 83.12  E-value: 2.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477  68 LKVVTWGLNRTLKPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQNTGWIG--ELGA--------- 136
Cdd:PLN02328 225 IKEAQLRSFEGVEPANVVVVGAGLAGLVAARQLLSMGFKVVVLEGRARPGGRVKTMKMKGDGVVAaaDLGGsvltgingn 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 137 --------MRMPsshriLHKLCQGLGLNLTKFTQYDKNTWTEVHE---------VKLRNYVVEKVPE---KLGYALRPQE 196
Cdd:PLN02328 305 plgvlarqLGLP-----LHKVRDICPLYLPDGKAVDAEIDSKIEAsfnklldrvCKLRQAMIEEVKSvdvNLGTALEAFR 379

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 197 KGHS-PED-IYQMALNQALKDLKalgcrkamkkFERHTLLeyllgeGNLSRPavqllgdVMSEDGFFYLSfaealrAHSC 274
Cdd:PLN02328 380 HVYKvAEDpQERMLLNWHLANLE----------YANASLM------SNLSMA-------YWDQDDPYEMG------GDHC 430

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 275 LsdrlqysrIVGGWDLLPRALLSslsglvllNAP------VVAMTQGPHDVHVQIETspparnlKVLKADVVLLTASGPA 348
Cdd:PLN02328 431 F--------IPGGNDTFVRELAK--------DLPifyertVESIRYGVDGVIVYAGG-------QEFHGDMVLCTVPLGV 487

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 349 VKR--ITFSPPLPRHMQEALRRLHYVPATKVFLSFRRPFWREEHIEGGHSNTDRPSR---MIFYP-PPREGALLLASYTW 422
Cdd:PLN02328 488 LKKgsIEFYPELPQRKKDAIQRLGYGLLNKVALLFPYNFWGGEIDTFGHLTEDPSMRgefFLFYSySSVSGGPLLIALVA 567

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 423 SDAAAAFAGLSREEALRLALDDVAALHGPVVRQLWDGT-GVVKRWAEDQHSQGGFVVQPPAlwqTEKDDW-----TVPYG 496
Cdd:PLN02328 568 GDAAVKFETLSPVESVKRVLQILRGIFHPKGIVVPDPVqAVCTRWGKDCFTYGSYSYVAVG---SSGDDYdilaeSVGDG 644

                        490       500       510
                 ....*....|....*....|....*....|....*
gi 384381477 497 RIYFAGEHT--AYP---HGwvetAVKSALRAAIKI 526
Cdd:PLN02328 645 RVFFAGEATnkQYPatmHG----AFLSGMREAANI 675
PLN03000 PLN03000
amine oxidase
 82-529 7.91e-16

amine oxidase


Pssm-ID: 178578 [Multi-domain]  Cd Length: 881  Bit Score: 81.22  E-value: 7.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477  82 QRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQ--NTGWIGELGAMRMPSSH-RILHKLCQGLGLNLT 158
Cdd:PLN03000 185 SSVVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGGRVYTKKMEanRVGAAADLGGSVLTGTLgNPLGIIARQLGSSLY 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 159 KftqydkntwtevhevklrnyVVEKVPeklgyALRPQEKGHSPE-DI-YQMALNQALKdlKALGCRKAMKKFERHTLLey 236
Cdd:PLN03000 265 K--------------------VRDKCP-----LYRVDGKPVDPDvDLkVEVAFNQLLD--KASKLRQLMGDVSMDVSL-- 315

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 237 llgeGNLSRPAVQLLGDVMS--EDGFFYLSFAEALRAHSCLSDRLQysriVGGWD------------LLPrALLSSLSGL 302
Cdd:PLN03000 316 ----GAALETFRQVSGNDVAteEMGLFNWHLANLEYANAGLVSKLS----LAFWDqddpydmggdhcFLP-GGNGRLVQA 386

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 303 VLLNAPVV------AMTQGPHDVHVQietsppARNlKVLKADVVLLTASGPAVKR--ITFSPPLPRHMQEALRRLHYVPA 374
Cdd:PLN03000 387 LAENVPILyektvqTIRYGSNGVKVI------AGN-QVYEGDMVLCTVPLGVLKNgsIKFVPELPQRKLDCIKRLGFGLL 459

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 375 TKVFLSFRRPFWREEHIEGGHSnTDRPSR----MIFYP-PPREGALLLASYTWSDAAAAFAGLSREEALRLALDDVAALH 449
Cdd:PLN03000 460 NKVAMLFPYVFWSTDLDTFGHL-TEDPNYrgefFLFYSyAPVAGGPLLIALVAGEAAHKFETMPPTDAVTRVLHILRGIY 538

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 450 GPVVRQLWDGTGVV-KRWAEDQHSQGGFvvqPPALWQTEKDDW-----TVPYGRIYFAGEHTA--YP---HGWVETAVKS 518
Cdd:PLN03000 539 EPQGINVPDPLQTVcTRWGGDPFSLGSY---SNVAVGASGDDYdilaeSVGDGRLFFAGEATTrrYPatmHGAFVTGLRE 615

                        490
                 ....*....|.
gi 384381477 519 ALRAAIKINSR 529
Cdd:PLN03000 616 AANMAQSAKAR 626
PLN02268 PLN02268
probable polyamine oxidase
 84-523 1.39e-13

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 73.18  E-value: 1.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477  84 VIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTyrDQNTGWIGELGA--MRMPSSHRILHKLCQGLGLNLTK-- 159
Cdd:PLN02268   3 VIVIGGGIAGIAAARALHDASFKVTLLESRDRIGGRVHT--DYSFGFPVDMGAswLHGVCNENPLAPLIGRLGLPLYRts 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 160 -------------FTQYDKntwtevHEVKLRNYVVEKVPEKLGYALRPQEK--GHSPEDiyqMALNQALKDLkalgcrka 224
Cdd:PLN02268  81 gdnsvlydhdlesYALFDM------DGNQVPQELVTKVGETFERILEETEKvrDEHEED---MSLLQAISIV-------- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 225 mkkFERHTLLEYllgEGnlsrPAVQLLGdvmsedgfFYLSFAEALRAHSclSDRL------QYSRIVGGWDLL-----PR 293
Cdd:PLN02268 144 ---LERHPELRL---EG----LAHEVLQ--------WYLCRMEGWFAAD--ADTIslkswdQEELLEGGHGLMvrgydPV 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 294 ALLSSLSGLVLLNAPVVAMTQGPHDVHVQIEtspparNLKVLKADVVLLTASGPAVK--RITFSPPLPRHMQEALRRLHY 371
Cdd:PLN02268 204 INTLAKGLDIRLNHRVTKIVRRYNGVKVTVE------DGTTFVADAAIIAVPLGVLKanIIKFEPELPEWKEEAISDLGV 277

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 372 VPATKVFLSFRRPFWREEHIEGG--------------HSNTDRPsrMIFYPPPreGALLLASYTWSD-AAAAFAGLSREE 436
Cdd:PLN02268 278 GIENKIALHFDSVFWPNVEFLGVvaptsygcsyflnlHKATGHP--VLVYMPA--GRLARDIEKLSDeAAANFAMSQLKK 353

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 437 ALRLALDDVAALhgpvvrqlwdgtgvVKRWAEDQHSQGGF----VVQPPALWqtekDDWTVPYGRIYFAGEHTAYPH-GW 511
Cdd:PLN02268 354 MLPDATEPVQYL--------------VSRWGSDPNSLGCYsydlVGKPHDLY----ERLRAPVDNLFFAGEATSSDFpGS 415

                        490
                 ....*....|..
gi 384381477 512 VETAVKSALRAA 523
Cdd:PLN02268 416 VHGAYSTGVMAA 427
PLN02529 PLN02529
lysine-specific histone demethylase 1
 84-536 4.21e-13

lysine-specific histone demethylase 1


Pssm-ID: 178144 [Multi-domain]  Cd Length: 738  Bit Score: 72.23  E-value: 4.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477  84 VIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTyrdQNTGWIGELGAMRMPSS-----HR------------IL 146
Cdd:PLN02529 163 VIIVGAGLAGLAAARQLLSFGFKVVVLEGRNRPGGRVYT---QKMGRKGQFAAVDLGGSvitgiHAnplgvlarqlsiPL 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 147 HKLCQGLGLNLTKFTQYDKNTWTEVHEVklRNYVVEKVPEklgyaLRpQEKGHSPEDIYQMALNQALKDLKALGcrkamK 226
Cdd:PLN02529 240 HKVRDNCPLYKPDGALVDKEIDSNIEFI--FNKLLDKVTE-----LR-QIMGGFANDISLGSVLERLRQLYGVA-----R 306

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 227 KFERHTLLEYLLGegNLSRPAVQLLGDVMS-----EDGFfylsfaEALRAHSCLSDrlqysrivGGWDLLpraLLSSLSG 301
Cdd:PLN02529 307 STEERQLLDWHLA--NLEYANAGCLSDLSAaywdqDDPY------EMGGDHCFLAG--------GNWRLI---NALCEGV 367

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 302 LVLLNAPVVAMTQGPHDVHVqIETSpparnlKVLKADVVLLTASGPAVKR--ITFSPPLPRHMQEALRRLHYVPATKVFL 379
Cdd:PLN02529 368 PIFYGKTVDTIKYGNDGVEV-IAGS------QVFQADMVLCTVPLGVLKKrtIRFEPELPRRKLAAIDRLGFGLLNKVAM 440

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 380 SFRRPFWREEHIEGGHSNTDRPSRMIFYpppregaLLLASYTWSDAAAAFAGLSREEALRLALDDVAA-LHG--PVVRQL 456
Cdd:PLN02529 441 VFPSVFWGEELDTFGCLNESSNKRGEFF-------LFYGYHTVSGGPALVALVAGEAAQRFENTDPSTlLHRvlSVLRGI 513

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477 457 WDGTGVV---------KRWAEDQHSQGGFvvqPPALWQTEKDDWTV----PYGRIYFAGEHTA--YP---HGwvetAVKS 518
Cdd:PLN02529 514 YNPKGINvpdpiqticTRWGSDPLSYGSY---SHVRVQSSGSDYDIlaesVSGRLFFAGEATTrqYPatmHG----AFLS 586

                        490       500       510
                 ....*....|....*....|....*....|...
gi 384381477 519 ALRAAIKI---------NSRK------GPASDT 536
Cdd:PLN02529 587 GLREASRIlhvarsqqsNSRKsmqrnsGVSNDV 619
PLN02976 PLN02976
amine oxidase
 82-526 2.53e-12

amine oxidase


Pssm-ID: 215527 [Multi-domain]  Cd Length: 1713  Bit Score: 70.28  E-value: 2.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477   82 QRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQ-----------NTGWIGELGAMRM--PSShrilhK 148
Cdd:PLN02976  694 KKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGRVYTDRSSlsvpvdlgasiITGVEADVATERRpdPSS-----L 768

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477  149 LCQGLGLNLTKFTQ----YDKNTW----TEVHEVKLRNY------VVEKVPEK------------LGYALRPQEKGHSPE 202
Cdd:PLN02976  769 ICAQLGLELTVLNSdcplYDVVTGekvpADLDEALEAEYnsllddMVLLVAQKgehamkmsledgLEYALKRRRMPRPGV 848

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477  203 DIYQMALNQALKDL---KALG-----CRKAMKK-----FERHTL------LEY----LLGEgnLSRPavqllgdVMSEDG 259
Cdd:PLN02976  849 DIDETELGNAADDLydsASTGvdgghCEKESKEdvlspLERRVMnwhfahLEYgcaaLLKE--VSLP-------YWNQDD 919

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477  260 fFYLSFAEalrAHsCLsdrlqysrIVGGWDLLPRAllSSLSGLVLLNAPVVAMTQGPHDV--------HVQIETSpparN 331
Cdd:PLN02976  920 -VYGGFGG---AH-CM--------IKGGYSNVVES--LAEGLDIHLNHVVTDVSYGSKDAgasgssrkKVKVSTS----N 980

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477  332 LKVLKADVVLLTASGPAVK--RITFSPPLPRHMQEALRRLHYVPATKVFLSFRRPFWREEHIEGGHSNTDRPSR----MI 405
Cdd:PLN02976  981 GSEFLGDAVLITVPLGCLKaeTIKFSPPLPDWKYSSIQRLGFGVLNKVVLEFPEVFWDDSVDYFGATAEETDLRgqcfMF 1060

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477  406 FYPPPREGALLLASYTWSDAAAAFAGLSREEALRLALddvaalhgPVVRQLWDGT-------GVVKRWAEDQHSQGGF-V 477
Cdd:PLN02976 1061 WNVKKTVGAPVLIALVVGKAAIDGQSMSSSDHVNHAL--------MVLRKLFGEAlvpdpvaSVVTDWGRDPFSYGAYsY 1132

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 384381477  478 VQPPAlwqtEKDDWTVpYGR-----IYFAGEHTAYPH-GWVETAVKSALRAAIKI 526
Cdd:PLN02976 1133 VAIGA----SGEDYDI-LGRpvencLFFAGEATCKEHpDTVGGAMMSGLREAVRI 1182
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
86-127 2.70e-12

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 62.16  E-value: 2.70e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 384381477   86 VVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQN 127
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYSYRVPG 42
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 81-155 5.36e-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: 5.36e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384381477  81 PQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQNTGWIGELGAMRMPSSHRILHKLCQGLGL 155
Cdd:COG3349    3 PPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGGRARSFPDPDTGLPIDNGQHVLLGCYRNTLDLLRRIGA 77
PLN02612 PLN02612
phytoene desaturase
 77-130 7.49e-10

phytoene desaturase


Pssm-ID: 215330 [Multi-domain]  Cd Length: 567  Bit Score: 61.78  E-value: 7.49e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 384381477  77 RTLKPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQNTGW 130
Cdd:PLN02612  89 RPAKPLKVVIAGAGLAGLSTAKYLADAGHKPILLEARDVLGGKVAAWKDEDGDW 142
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 80-119 1.41e-09

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 60.63  E-value: 1.41e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 384381477  80 KPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGR 119
Cdd:COG1233    2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGR 41
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
81-119 1.61e-09

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


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 59.51  E-value: 1.61e-09
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 384381477  81 PQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGR 119
Cdd:COG3380    3 MPDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGGR 41
PRK07233 PRK07233
hypothetical protein; Provisional
 83-118 1.72e-09

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 60.29  E-value: 1.72e-09
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 384381477  83 RVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 118
Cdd:PRK07233   1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGG 36
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
80-118 2.78e-08

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


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 56.28  E-value: 2.78e-08
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 384381477  80 KPQRVIVVGAGVAGLVAAKVLSDAgHKVTILEADNRIGG 118
Cdd:COG2907    2 ARMRIAVIGSGISGLTAAWLLSRR-HDVTLFEANDRLGG 39
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 82-118 2.92e-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: 2.92e-08
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 384381477  82 QRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 118
Cdd:COG0493  122 KKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG 158
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 83-123 2.98e-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: 2.98e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 384381477  83 RVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG--RIFTY 123
Cdd:COG2072    8 DVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGtwRDNRY 50
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 82-118 3.23e-08

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 56.33  E-value: 3.23e-08
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 384381477  82 QRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 118
Cdd:PRK12810 144 KKVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGG 180
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
 83-154 8.52e-08

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 54.85  E-value: 8.52e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384381477  83 RVIVVGAGVAGLVAAKVLSDAG--HKVTILEADNRIGGRIFTYRDQntGWIGELGA----MRMPSSHRILHKLcqGLG 154
Cdd:PRK11883   2 KVAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKIQTVRKD--GFPIELGPesflARKPSAPALVKEL--GLE 75
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
82-119 1.38e-07

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 54.48  E-value: 1.38e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 384381477  82 QRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGR 119
Cdd:COG1148  141 KRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGR 178
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
84-118 1.60e-07

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 54.03  E-value: 1.60e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 384381477  84 VIVVGAGVAGLVAAKVLSDAGHKVTILEADN--RIGG 118
Cdd:COG3573    8 VIVVGAGLAGLVAAAELADAGRRVLLLDQEPeaNLGG 44
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
 84-126 2.03e-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: 53.82  E-value: 2.03e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 384381477   84 VIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQ 126
Cdd:TIGR02734   1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGRAGVLEDD 43
PLN02568 PLN02568
polyamine oxidase
 80-136 2.38e-07

polyamine oxidase


Pssm-ID: 215308 [Multi-domain]  Cd Length: 539  Bit Score: 53.68  E-value: 2.38e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384381477  80 KPqRVIVVGAGVAGLVAAKVLSDAGH-----KVTILEADNRIGGRIFTyrDQNTGWIGELGA 136
Cdd:PLN02568   5 KP-RIVIIGAGMAGLTAANKLYTSSAandmfELTVVEGGDRIGGRINT--SEFGGERIEMGA 63
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 82-118 4.69e-07

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 52.49  E-value: 4.69e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 384381477  82 QRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 118
Cdd:PRK11749 141 KKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG 177
PRK12834 PRK12834
putative FAD-binding dehydrogenase; Reviewed
 84-121 5.03e-07

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 183782 [Multi-domain]  Cd Length: 549  Bit Score: 52.59  E-value: 5.03e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 384381477  84 VIVVGAGVAGLVAAKVLSDAGHKVTILEADNR--IGGRIF 121
Cdd:PRK12834   7 VIVVGAGLAGLVAAAELADAGKRVLLLDQENEanLGGQAF 46
PLN02576 PLN02576
protoporphyrinogen oxidase
 83-150 7.21e-07

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 51.94  E-value: 7.21e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 384381477  83 RVIVVGAGVAGLVAAKVL-SDAGHKVTILEADNRIGGRIFTYrdQNTGWIGELGAMRMPSSHRILHKLC 150
Cdd:PLN02576  14 DVAVVGAGVSGLAAAYALaSKHGVNVLVTEARDRVGGNITSV--SEDGFIWEEGPNSFQPSDPELTSAV 80
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 83-157 1.19e-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: 50.86  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477   83 RVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIG----GRiftyrdqNTGWI----GELGAMRMPS----SHRILHKLC 150
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGsgasGR-------NAGLIhpglRYLEPSELARlaleALDLWEELE 73


                  ....*..
gi 384381477  151 QGLGLNL 157
Cdd:pfam01266  74 EELGIDC 80
PRK07208 PRK07208
hypothetical protein; Provisional
 81-118 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 384381477  81 PQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 118
Cdd:PRK07208   4 KKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGG 41
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 74-116 1.62e-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: 1.62e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 384381477   74 GLNRTLKPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRI 116
Cdd:pfam07992 145 ALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRL 187
PLN02487 PLN02487
zeta-carotene desaturase
 83-135 3.91e-06

zeta-carotene desaturase


Pssm-ID: 215268 [Multi-domain]  Cd Length: 569  Bit Score: 49.80  E-value: 3.91e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 384381477  83 RVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQNTGWIgELG 135
Cdd:PLN02487  77 KVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGGKVGSFVDKNGNHI-EMG 128
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
 84-136 4.96e-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: 4.96e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 384381477   84 VIVVGAGVAGLVAAKVLS----DAGHKVTILEADNRIGGRIFTyRDQNtGWIGELGA 136
Cdd:TIGR00562   5 VVIIGGGISGLCAAYYLEkeipELPVELTLVEASDRVGGKIQT-VKED-GYLIERGP 59
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
83-157 6.52e-06

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 48.75  E-value: 6.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477  83 RVIVVGAGVAGLVAAKVLSDAGHKVTILEADnRIG----GRiftyrdqNTGWI----GELGAMRM----PSSHRILHKLC 150
Cdd:COG0665    4 DVVVIGGGIAGLSTAYHLARRGLDVTVLERG-RPGsgasGR-------NAGQLrpglAALADRALvrlaREALDLWRELA 75


                 ....*..
gi 384381477 151 QGLGLNL 157
Cdd:COG0665   76 AELGIDC 82
HI0933_like pfam03486
HI0933-like protein;
83-120 7.36e-06

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 48.73  E-value: 7.36e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 384381477   83 RVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRI 120
Cdd:pfam03486   2 DVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLGRKI 39
YhiN COG2081
Predicted flavoprotein YhiN [General function prediction only];
85-117 8.52e-06

Predicted flavoprotein YhiN [General function prediction only];


Pssm-ID: 441684 [Multi-domain]  Cd Length: 402  Bit Score: 48.51  E-value: 8.52e-06
                         10        20        30
                 ....*....|....*....|....*....|...
gi 384381477  85 IVVGAGVAGLVAAKVLSDAGHKVTILEADNRIG 117
Cdd:COG2081    1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVG 33
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 83-135 1.66e-05

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 47.56  E-value: 1.66e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384381477  83 RVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG--R--IFTYR------DQNTGWIGELG 135
Cdd:PRK12771 139 RVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGmmRygIPAYRlprevlDAEIQRILDLG 201
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 78-122 2.01e-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: 2.01e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 384381477    78 TLKPQRVIVVGAGVAGLVAAKVLSDAGHKVTIL--------EADNRIGGRIFT 122
Cdd:smart01002  17 GVPPAKVVVIGAGVVGLGAAATAKGLGAEVTVLdvrparlrQLESLLGARFTT 69
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 83-116 2.23e-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: 2.23e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 384381477   83 RVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRI 116
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRL 34
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 83-119 2.34e-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: 46.85  E-value: 2.34e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 384381477  83 RVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGR 119
Cdd:COG0654    5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPD 41
PTZ00367 PTZ00367
squalene epoxidase; Provisional
 75-118 2.61e-05

squalene epoxidase; Provisional


Pssm-ID: 240384 [Multi-domain]  Cd Length: 567  Bit Score: 47.15  E-value: 2.61e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381477  75 LNRTL-----KPQR------VIVVGAGVAGLVAAKVLSDAGHKVTILEAD-----NRIGG 118
Cdd:PTZ00367  16 LNRILsrlrfKPARtnydydVIIVGGSIAGPVLAKALSKQGRKVLMLERDlfskpDRIVG 75
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 84-118 2.89e-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: 2.89e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 384381477  84 VIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 118
Cdd:COG1053    6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 83-114 3.66e-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: 3.66e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 384381477   83 RVIVVGAGVAGLVAAKVLSDAGHKVTILEADN 114
Cdd:pfam07992   2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEDEG 33
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
82-157 3.89e-05

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 46.29  E-value: 3.89e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384381477  82 QRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFtyrdqntgwiGELGAmrmpsshRILHKLCQGLGLNL 157
Cdd:COG1251  143 KRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQL----------DEEAG-------ALLQRLLEALGVEV 201
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 82-118 6.87e-05

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 45.87  E-value: 6.87e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 384381477  82 QRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 118
Cdd:PRK12814 194 KKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGG 230
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 81-122 1.37e-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: 1.37e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 384381477  81 PQRVIVVGAGVAGLVAAKVLSDAGHKVTIL--------EADNRIGGRIFT 122
Cdd:cd05305  168 PAKVVILGAGVVGENAARVALGLGAEVTVLdinlerlrYLDDIFGGRVTT 217
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 80-117 1.49e-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: 44.84  E-value: 1.49e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 384381477  80 KPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIG 117
Cdd:PRK01747 259 KARDAAIIGGGIAGAALALALARRGWQVTLYEADEAPA 296
PLN02172 PLN02172
flavin-containing monooxygenase FMO GS-OX
 82-118 1.67e-04

flavin-containing monooxygenase FMO GS-OX


Pssm-ID: 215116 [Multi-domain]  Cd Length: 461  Bit Score: 44.47  E-value: 1.67e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 384381477  82 QRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 118
Cdd:PLN02172  11 QHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGG 47
Ald COG0686
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ...
 80-122 1.67e-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: 44.23  E-value: 1.67e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 384381477  80 KPQRVIVVGAGVAGLVAAKVLSDAGHKVTIL--------EADNRIGGRIFT 122
Cdd:COG0686  167 PPAKVVILGGGVVGTNAARMALGLGADVTVLdinldrlrRLDDIFGGRVTT 217
PRK13984 PRK13984
putative oxidoreductase; Provisional
 80-135 1.84e-04

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 44.37  E-value: 1.84e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384381477  80 KPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGR----IFTYR------DQNTGWIGELG 135
Cdd:PRK13984 282 KNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVmrygIPSYRlpdealDKDIAFIEALG 347
BetA COG2303
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ...
 84-119 1.89e-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: 44.43  E-value: 1.89e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 384381477  84 VIVVGAGVAGLVAAKVLS-DAGHKVTILEAdnriGGR 119
Cdd:COG2303    7 YVIVGAGSAGCVLANRLSeDAGLRVLLLEA----GGR 39
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 84-118 1.96e-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: 44.20  E-value: 1.96e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 384381477   84 VIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 118
Cdd:pfam00890   2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGG 36
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 84-118 2.25e-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: 2.25e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 384381477  84 VIVVGAGVAGLVAAKVLSDAGHKVTILEADnRIGG 118
Cdd:COG1249    6 LVVIGAGPGGYVAAIRAAQLGLKVALVEKG-RLGG 39
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
89-120 2.48e-04

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 43.42  E-value: 2.48e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 384381477  89 AGVAGLVAAKVLSDAGHKVTILEADNRIGGRI 120
Cdd:COG0644    1 AGPAGSAAARRLARAGLSVLLLEKGSFPGDKI 32
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 77-120 3.16e-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: 43.26  E-value: 3.16e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 384381477  77 RTLKPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRI 120
Cdd:COG0446  120 KEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGVL 163
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 81-119 4.21e-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: 43.15  E-value: 4.21e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 384381477  81 PQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGR 119
Cdd:COG1249  168 PKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLLPG 206
PRK06753 PRK06753
hypothetical protein; Provisional
 83-116 6.06e-04

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 42.37  E-value: 6.06e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 384381477  83 RVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRI 116
Cdd:PRK06753   2 KIAIIGAGIGGLTAAALLQEQGHEVKVFEKNESV 35
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
 81-118 8.39e-04

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 42.46  E-value: 8.39e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 384381477   81 PQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 118
Cdd:PTZ00306  409 PARVIVVGGGLAGCSAAIEAASCGAQVILLEKEAKLGG 446
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
 80-111 1.30e-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: 40.56  E-value: 1.30e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 384381477   80 KPQRVIVVGAGVAGLVAAKVLSDAGHKVTILE 111
Cdd:pfam01262  27 APAKVLVIGGGVAGLNAAATAKGLGAIVTILD 58
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 65-113 1.70e-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: 40.82  E-value: 1.70e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 384381477  65 EQLLKVVTWGLNRTLKPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEAD 113
Cdd:COG0569   79 LEALRRRRMERGIKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVIDKD 127
PRK12831 PRK12831
putative oxidoreductase; Provisional
 80-118 1.74e-03

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 41.16  E-value: 1.74e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 384381477  80 KPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 118
Cdd:PRK12831 139 KGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGG 177
PRK10015 PRK10015
oxidoreductase; Provisional
 85-123 1.81e-03

oxidoreductase; Provisional


Pssm-ID: 182194 [Multi-domain]  Cd Length: 429  Bit Score: 41.12  E-value: 1.81e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 384381477  85 IVVGAGVAGLVAAKVLSDAGHKVTILE------ADNRIGGRIFTY 123
Cdd:PRK10015   9 IVVGAGVAGSVAALVMARAGLDVLVIErgdsagCKNMTGGRLYAH 53
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 81-118 2.11e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 40.93  E-value: 2.11e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 384381477  81 PQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 118
Cdd:PRK06292 169 PKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILP 206
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 84-118 2.13e-03

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 40.90  E-value: 2.13e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 384381477  84 VIVVGAGVAGLVAAKVLSDAGHKVTILEADNrIGG 118
Cdd:PRK06416   7 VIVIGAGPGGYVAAIRAAQLGLKVAIVEKEK-LGG 40
PRK00711 PRK00711
D-amino acid dehydrogenase;
83-111 2.95e-03

D-amino acid dehydrogenase;


Pssm-ID: 234819 [Multi-domain]  Cd Length: 416  Bit Score: 40.17  E-value: 2.95e-03
                         10        20
                 ....*....|....*....|....*....
gi 384381477  83 RVIVVGAGVAGLVAAKVLSDAGHKVTILE 111
Cdd:PRK00711   2 RVVVLGSGVIGVTSAWYLAQAGHEVTVID 30
PRK06370 PRK06370
FAD-containing oxidoreductase;
85-118 3.44e-03

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 40.19  E-value: 3.44e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 384381477  85 IVVGAGVAGLVAAKVLSDAGHKVTILEaDNRIGG 118
Cdd:PRK06370   9 IVIGAGQAGPPLAARAAGLGMKVALIE-RGLLGG 41
PRK08163 PRK08163
3-hydroxybenzoate 6-monooxygenase;
80-117 3.79e-03

3-hydroxybenzoate 6-monooxygenase;


Pssm-ID: 181262 [Multi-domain]  Cd Length: 396  Bit Score: 40.02  E-value: 3.79e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 384381477  80 KPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIG 117
Cdd:PRK08163   3 KVTPVLIVGGGIGGLAAALALARQGIKVKLLEQAAEIG 40
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 84-118 4.52e-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: 39.90  E-value: 4.52e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 384381477   84 VIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGG 118
Cdd:pfam12831   2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGG 36
PRK12843 PRK12843
FAD-dependent oxidoreductase;
84-131 5.90e-03

FAD-dependent oxidoreductase;


Pssm-ID: 237225 [Multi-domain]  Cd Length: 578  Bit Score: 39.72  E-value: 5.90e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 384381477  84 VIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRifTYRDQNTGWI 131
Cdd:PRK12843  19 VIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGGT--TATSAGTTWI 64
PRK10157 PRK10157
putative oxidoreductase FixC; Provisional
 85-123 7.80e-03

putative oxidoreductase FixC; Provisional


Pssm-ID: 182273 [Multi-domain]  Cd Length: 428  Bit Score: 39.12  E-value: 7.80e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 384381477  85 IVVGAGVAGLVAAKVLSDAGHKVTILE------ADNRIGGRIFTY 123
Cdd:PRK10157   9 IIVGAGLAGSVAALVLAREGAQVLVIErgnsagAKNVTGGRLYAH 53
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
84-120 7.99e-03

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 38.56  E-value: 7.99e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 384381477  84 VIVVGAGVAGLVAAKVLSDAGHKVTILEADnRIGGRI 120
Cdd:COG0492    3 VVIIGAGPAGLTAAIYAARAGLKTLVIEGG-EPGGQL 38
PntA COG3288
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
78-100 8.75e-03

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


Pssm-ID: 442518 [Multi-domain]  Cd Length: 359  Bit Score: 38.83  E-value: 8.75e-03
                         10        20
                 ....*....|....*....|....*.
gi 384381477  78 TLKPQRVIVVGAGVAGLVA---AKVL 100
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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