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Conserved domains on  [gi|157817668|ref|NP_001100152|]
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L-amino acid oxidase 1 precursor [Rattus norvegicus]

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

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];
51-504 4.32e-120

Monoamine oxidase [Amino acid transport and metabolism];


:

Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 360.01  E-value: 4.32e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  51 LHTSPSSKRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRVVTLRNKEEGWHFELGPMRIPESHRIIHTYIQKFG 130
Cdd:COG1231    1 MSRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGLYAELGAMRIPPSHTNLLALARELG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 131 LKLNNFTQHDNNTWYLLRGHRYRASEVKANPEILGyplrpseknkTAEDLFYQAITKvKASNCSQLLSLYDSYSTKAYLL 210
Cdd:COG1231   81 LPLEPFPNENGNALLYLGGKRVRAGEIAADLRGVA----------ELLAKLLRALAA-ALDPWAHPAAELDRESLAEWLR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 211 KEGmLSRGAVEMIGDMMNEN--AGFYR-SLLESLRIANIFTKNDQFTEITGGFDQLPNSLNDSLkPGTIHLGSKVERVVG 287
Cdd:COG1231  150 RNG-ASPSARRLLGLLGAGEygADPDElSLLDLLRYAASAGGGAQQFRIVGGMDQLPRALAAEL-GDRIRLGAPVTRIRQ 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 288 NESKVEVLYRTDGptsalyNLTADYVIISASAKATRLIAFQPPLSPEKIRALRSVHYNSATKVIFVCNERFWEKDGIHGG 367
Cdd:COG1231  228 DGDGVTVTTDDGG------TVRADAVIVTVPPSVLRRIEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEEDGLYGG 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 368 YSITDRPSRFIYYPSYSRPSSKGILLaSFTMDDDSFFFTALKPNQVVDIILDDLAAVHLIPKEELKRmcpkSEVKHWSLD 447
Cdd:COG1231  302 ISLTDLPIRQTWYPSNGPDGGAGVLL-GYVGGDDARALAALSPEERVAAALEQLARIFGVYAAEPVD----YVSTDWGRD 376
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157817668 448 PFTIGSYAEFTPYQFLDDLKQLSQTEGRIYFAGEHTSLP-HAWIETAIKSGIRAAKNI 504
Cdd:COG1231  377 PWSRGAYAAAPPGQLTAAGPALAEPDGRIHFAGEHTSDEwPGWVEGALESGERAAAEI 434
 
Name Accession Description Interval E-value
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
51-504 4.32e-120

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 360.01  E-value: 4.32e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  51 LHTSPSSKRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRVVTLRNKEEGWHFELGPMRIPESHRIIHTYIQKFG 130
Cdd:COG1231    1 MSRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGLYAELGAMRIPPSHTNLLALARELG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 131 LKLNNFTQHDNNTWYLLRGHRYRASEVKANPEILGyplrpseknkTAEDLFYQAITKvKASNCSQLLSLYDSYSTKAYLL 210
Cdd:COG1231   81 LPLEPFPNENGNALLYLGGKRVRAGEIAADLRGVA----------ELLAKLLRALAA-ALDPWAHPAAELDRESLAEWLR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 211 KEGmLSRGAVEMIGDMMNEN--AGFYR-SLLESLRIANIFTKNDQFTEITGGFDQLPNSLNDSLkPGTIHLGSKVERVVG 287
Cdd:COG1231  150 RNG-ASPSARRLLGLLGAGEygADPDElSLLDLLRYAASAGGGAQQFRIVGGMDQLPRALAAEL-GDRIRLGAPVTRIRQ 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 288 NESKVEVLYRTDGptsalyNLTADYVIISASAKATRLIAFQPPLSPEKIRALRSVHYNSATKVIFVCNERFWEKDGIHGG 367
Cdd:COG1231  228 DGDGVTVTTDDGG------TVRADAVIVTVPPSVLRRIEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEEDGLYGG 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 368 YSITDRPSRFIYYPSYSRPSSKGILLaSFTMDDDSFFFTALKPNQVVDIILDDLAAVHLIPKEELKRmcpkSEVKHWSLD 447
Cdd:COG1231  302 ISLTDLPIRQTWYPSNGPDGGAGVLL-GYVGGDDARALAALSPEERVAAALEQLARIFGVYAAEPVD----YVSTDWGRD 376
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157817668 448 PFTIGSYAEFTPYQFLDDLKQLSQTEGRIYFAGEHTSLP-HAWIETAIKSGIRAAKNI 504
Cdd:COG1231  377 PWSRGAYAAAPPGQLTAAGPALAEPDGRIHFAGEHTSDEwPGWVEGALESGERAAAEI 434
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
67-504 1.05e-80

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: 258.58  E-value: 1.05e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668   67 MAGLVAAKLLQDAGHEVTILEASNHIGGRVVTLRnkEEGWHFELGPMRIPESHRIIHTYIQKFGLK----LNNFTQHDNN 142
Cdd:pfam01593   1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVR--DDGFLIELGAMWFHGAQPPLLALLKELGLEdrlvLPDPAPFYTV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  143 TWYLLRGHRYRASEVKANPEIL---GYPLRPSEKNKTAEDLFYQAITKVKAsncsqllslYDSYSTKAYLLKEGMLSRGA 219
Cdd:pfam01593  79 LFAGGRRYPGDFRRVPAGWEGLlefGRLLSIPEKLRLGLAALASDALDEFD---------LDDFSLAESLLFLGRRGPGD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  220 VEMIGDMMNENA--------GFYRSLLESLRIANIFTKNDQFTE-------ITGGFDQLPNSLNDSLKPGTIHLGSKVER 284
Cdd:pfam01593 150 VEVWDRLIDPELfaalpfasGAFAGDPSELSAGLALPLLWALLGeggslllPRGGLGALPDALAAQLLGGDVRLNTRVRS 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  285 VVGNESKVEVLYrTDGPTsalynLTADYVIISASAKATRLIAFQPPLSPEKIRALRSVHYNSATKVIFVCNERFWEKDGI 364
Cdd:pfam01593 230 IDREGDGVTVTL-TDGEV-----IEADAVIVTVPLGVLKRILFTPPLPPEKARAIRNLGYGPVNKVHLEFDRKFWPDLGL 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  365 HG--GYSITDRPSRFIYYPSYSR-PSSKGILLASFTMDDDSF-FFTALKPNQVVDIILDDLAAVHLIPKEELKRMCpkse 440
Cdd:pfam01593 304 LGllSELLTGLGTAFSWLTFPNRaPPGKGLLLLVYVGPGDRArELEGLSDEELLQAVLRDLRKLFGEEAPEPLRVL---- 379
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157817668  441 VKHWSLDPFTIGSYAEFTPYQFLDDLKQLSQT-EGRIYFAGEHTSLPH-AWIETAIKSGIRAAKNI 504
Cdd:pfam01593 380 VSDWHTDPWPRGSYSLPQYGPGHDDYRPLARTpDPGLFFAGEHTSTGYpGTVEGAIESGRRAARAV 445
PLN02676 PLN02676
polyamine oxidase
42-517 2.58e-20

polyamine oxidase


Pssm-ID: 215362 [Multi-domain]  Cd Length: 487  Bit Score: 93.63  E-value: 2.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  42 ALLLIAQNGLHTSPSSKRIVVVGAGMAGLVAAKLLQDAGHE-VTILEASNHIGGRVvtlrNKEE--GWHFELGPMRI--- 115
Cdd:PLN02676  11 LAVHLFAVAAMDAKPSPSVIIVGAGMSGISAAKTLSEAGIEdILILEATDRIGGRM----RKANfaGVSVELGANWVegv 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 116 --PESHRIIhTYIQKFGLK--LNNFTQHDNNTwYLLRGHRYRASEVKAnpeilgyplrpSEKNKTAEDLFYQAITKVKAS 191
Cdd:PLN02676  87 ggPESNPIW-ELANKLKLRtfYSDFDNLSSNI-YKQDGGLYPKKVVQK-----------SMKVADASDEFGENLSISLSA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 192 NCSQLLSLYDSYSTKAYLLKEgmlsrgAVEMIGDMMN---ENAGFYR--SLLESLRIANI--FTKNDQFTEITGGFDQLP 264
Cdd:PLN02676 154 KKAVDISILTAQRLFGQVPKT------PLEMVIDYYNydyEFAEPPRvtSLKNTEPNPTFvdFGEDEYFVADPRGYESLV 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 265 NSLND---SLKPGTIH----LGSKVERVVgNESKVEVLYRT-DGPTsalYNltADYVIISASAKA--TRLIAFQPPLSPE 334
Cdd:PLN02676 228 YYLAEqflSTKSGKITdprlKLNKVVREI-SYSKNGVTVKTeDGSV---YR--AKYVIVSVSLGVlqSDLIKFKPPLPDW 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 335 KIRALRSVHYNSATKVIFVCNERFW-------------EKDGihggysitdrpsrfiYYPSYSR-----PSSKgILLASF 396
Cdd:PLN02676 302 KIEAIYQFDMAVYTKIFLKFPYKFWpsgpgtefflyahERRG---------------YYPFWQHleneyPGSN-VLFVTV 365
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 397 TmDDDSFFFTALKPNQVvdiilddLAAVHlipkEELKRM----CPKSE---VKHWSLDPFTIGSYAEF----TPYQFldd 465
Cdd:PLN02676 366 T-DEESRRIEQQPDSET-------KAEIM----EVLRKMfgpnIPEATdilVPRWWSNRFFKGSYSNWpigvSRYEF--- 430
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157817668 466 lKQLSQTEGRIYFAGEHTSLPH-AWIETAIKSGIRAAKNIQDTVDKEATQGQV 517
Cdd:PLN02676 431 -DQIRAPVGRVYFTGEHTSEKYnGYVHGAYLAGIDTANDLLECIKKKKCRKNV 482
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
58-503 3.16e-09

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: 59.08  E-value: 3.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668   58 KRIVVVGAGMAGLVAA----KLLQDAGHEVTILEASNHIGGRVVTLrnKEEGWHFELGPMRIPESHRIIHTYIQKFGLKl 133
Cdd:TIGR00562   3 KHVVIIGGGISGLCAAyyleKEIPELPVELTLVEASDRVGGKIQTV--KEDGYLIERGPDSFLERKKSAPDLVKDLGLE- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  134 nNFTQHDNNTWYLLRGHRYRASEVKANP-EILGYPLRP-SEKNKTAEDLFYQA--------------------ITKVKAS 191
Cdd:TIGR00562  80 -HVLVSDATGQRYVLVNRGKLMPVPTKIaPFVKTGLFSlGGKLRAGMDFIRPAspgkdesveefvrrrfgdevVENLIEP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  192 NCS-------QLLSLYDSYStKAYLLKEGMLSrgaveMIGDMMNENAGFYRSLLESLriANIFTKNdqFTEITGGFDQLP 264
Cdd:TIGR00562 159 LLSgiyagdpSKLSLKSTFP-KFYQTEQKHGS-----LILGMKKTRNLPQGSGLQLT--AKKQGQD--FQTLATGLETLP 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  265 NSLNDSLKPGTIHLGSKVERVVgNESKVEVLYRTDGPTsalynLTADYVIISASA-KATRLIafqPPLSPEKIRALRSVH 343
Cdd:TIGR00562 229 EEIEKRLKLTKVYKGTKVTKLS-HRGSNYTLELDNGVT-----VETDSVVVTAPHkAAAGLL---SELSNSASSHLDKIH 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  344 YNSatkvIFVCNERFWEK--DGIHGGYS-ITDRPSRF-----IY----YPSYSRPSSkgILLASFT--MDDDSFFftALK 409
Cdd:TIGR00562 300 SPP----VANVNLGFPEGsvDGELEGFGfLISRSSKFailgcIFtsklFPNRAPPGK--TLLTAYIggATDESIV--DLS 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  410 PNQVVDIILDDLAAVHLIPKEELkrmcpKSEVKHW--SLDPFTIGSyaeftpYQFLDDLKQLSQTegriyfAGEHTSLPH 487
Cdd:TIGR00562 372 ENEIINIVLRDLKKVLNINNEPE-----MLCVTRWhrAIPQYHVGH------DQRLKEARELLES------AYPGVFLTG 434
                         490
                  ....*....|....*..
gi 157817668  488 AWIE-TAIKSGIRAAKN 503
Cdd:TIGR00562 435 NSFEgVGIPDCIDQGKA 451
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
59-99 2.01e-03

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: 38.64  E-value: 2.01e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 157817668    59 RIVVVGAGMAGLVAAKLLQDAGHEVTIL--------EASNHIGGRVVTL 99
Cdd:smart01002  22 KVVVIGAGVVGLGAAATAKGLGAEVTVLdvrparlrQLESLLGARFTTL 70
 
Name Accession Description Interval E-value
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
51-504 4.32e-120

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 360.01  E-value: 4.32e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  51 LHTSPSSKRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRVVTLRNKEEGWHFELGPMRIPESHRIIHTYIQKFG 130
Cdd:COG1231    1 MSRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGLYAELGAMRIPPSHTNLLALARELG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 131 LKLNNFTQHDNNTWYLLRGHRYRASEVKANPEILGyplrpseknkTAEDLFYQAITKvKASNCSQLLSLYDSYSTKAYLL 210
Cdd:COG1231   81 LPLEPFPNENGNALLYLGGKRVRAGEIAADLRGVA----------ELLAKLLRALAA-ALDPWAHPAAELDRESLAEWLR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 211 KEGmLSRGAVEMIGDMMNEN--AGFYR-SLLESLRIANIFTKNDQFTEITGGFDQLPNSLNDSLkPGTIHLGSKVERVVG 287
Cdd:COG1231  150 RNG-ASPSARRLLGLLGAGEygADPDElSLLDLLRYAASAGGGAQQFRIVGGMDQLPRALAAEL-GDRIRLGAPVTRIRQ 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 288 NESKVEVLYRTDGptsalyNLTADYVIISASAKATRLIAFQPPLSPEKIRALRSVHYNSATKVIFVCNERFWEKDGIHGG 367
Cdd:COG1231  228 DGDGVTVTTDDGG------TVRADAVIVTVPPSVLRRIEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEEDGLYGG 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 368 YSITDRPSRFIYYPSYSRPSSKGILLaSFTMDDDSFFFTALKPNQVVDIILDDLAAVHLIPKEELKRmcpkSEVKHWSLD 447
Cdd:COG1231  302 ISLTDLPIRQTWYPSNGPDGGAGVLL-GYVGGDDARALAALSPEERVAAALEQLARIFGVYAAEPVD----YVSTDWGRD 376
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157817668 448 PFTIGSYAEFTPYQFLDDLKQLSQTEGRIYFAGEHTSLP-HAWIETAIKSGIRAAKNI 504
Cdd:COG1231  377 PWSRGAYAAAPPGQLTAAGPALAEPDGRIHFAGEHTSDEwPGWVEGALESGERAAAEI 434
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
67-504 1.05e-80

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: 258.58  E-value: 1.05e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668   67 MAGLVAAKLLQDAGHEVTILEASNHIGGRVVTLRnkEEGWHFELGPMRIPESHRIIHTYIQKFGLK----LNNFTQHDNN 142
Cdd:pfam01593   1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVR--DDGFLIELGAMWFHGAQPPLLALLKELGLEdrlvLPDPAPFYTV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  143 TWYLLRGHRYRASEVKANPEIL---GYPLRPSEKNKTAEDLFYQAITKVKAsncsqllslYDSYSTKAYLLKEGMLSRGA 219
Cdd:pfam01593  79 LFAGGRRYPGDFRRVPAGWEGLlefGRLLSIPEKLRLGLAALASDALDEFD---------LDDFSLAESLLFLGRRGPGD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  220 VEMIGDMMNENA--------GFYRSLLESLRIANIFTKNDQFTE-------ITGGFDQLPNSLNDSLKPGTIHLGSKVER 284
Cdd:pfam01593 150 VEVWDRLIDPELfaalpfasGAFAGDPSELSAGLALPLLWALLGeggslllPRGGLGALPDALAAQLLGGDVRLNTRVRS 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  285 VVGNESKVEVLYrTDGPTsalynLTADYVIISASAKATRLIAFQPPLSPEKIRALRSVHYNSATKVIFVCNERFWEKDGI 364
Cdd:pfam01593 230 IDREGDGVTVTL-TDGEV-----IEADAVIVTVPLGVLKRILFTPPLPPEKARAIRNLGYGPVNKVHLEFDRKFWPDLGL 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  365 HG--GYSITDRPSRFIYYPSYSR-PSSKGILLASFTMDDDSF-FFTALKPNQVVDIILDDLAAVHLIPKEELKRMCpkse 440
Cdd:pfam01593 304 LGllSELLTGLGTAFSWLTFPNRaPPGKGLLLLVYVGPGDRArELEGLSDEELLQAVLRDLRKLFGEEAPEPLRVL---- 379
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157817668  441 VKHWSLDPFTIGSYAEFTPYQFLDDLKQLSQT-EGRIYFAGEHTSLPH-AWIETAIKSGIRAAKNI 504
Cdd:pfam01593 380 VSDWHTDPWPRGSYSLPQYGPGHDDYRPLARTpDPGLFFAGEHTSTGYpGTVEGAIESGRRAARAV 445
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
57-508 4.32e-31

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: 125.33  E-value: 4.32e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  57 SKRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRVVTLRnkEEGWHFELGPMRIPESHRIIHTYIQKFGLKlNNF 136
Cdd:COG1232    1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRTVE--VDGFRIDRGPHSFLTRDPEVLELLRELGLG-DEL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 137 TQHDN-NTWYLLRGHRYRASevKANPEILGYPL-----------------RPSEKNKTAEDLFYQA-------------I 185
Cdd:COG1232   78 VWPNTrKSYIYYGGKLHPLP--QGPLALLRSPLlslagklrallellaprRPPGEDESLAEFVRRRfgrevyerlveplL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 186 TKVKASNCSQLlslydsySTKAyllkegmlsrgAVEMIGDMMNEnagfYRSLLES-LRIANIFTKNDQFTEITGGFDQLP 264
Cdd:COG1232  156 EGVYAGDPDEL-------SADW-----------AFPRLKRLELE----HGSLIKGaLALRKGAKAGEVFGYLRGGLGTLV 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 265 NSLNDSLKPGTIHLGSKVERVVGNESKVEVLYRtDGPTsalynLTADYVIISASAKAT-RLIafqPPLSPEKIRALRSVH 343
Cdd:COG1232  214 EALAEALEAGEIRLGTRVTAIEREGGGWRVTTS-DGET-----IEADAVVSATPAPALaRLL---APLPPEVAAALAGIP 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 344 YNSATKVIFVCNERFWeKDGIHGGYSITDRPSRFIY---YPS----YSRPSSKGILLAS-FTMDDDSFFftALKPNQVVD 415
Cdd:COG1232  285 YASVAVVALGFDRPDL-PPPDGFGWLVPRDEGVPILavtFSSnkwpHRAPDGKVLLRLEvGGAGDPELW--QLSDEELVA 361
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 416 IILDDLAAVHLIPKEELkrmcpKSEVKHWsldpftIGSYAEFTP--YQFLDDLKQLSQTEGRIYFAG---EHTSLPHawi 490
Cdd:COG1232  362 LALADLRKLLGIDAEPV-----DTRVVRW------PKAYPQYTVghLERVAAIREALAALPGLYLAGrayDGVGLPD--- 427
                        490
                 ....*....|....*...
gi 157817668 491 etAIKSGIRAAKNIQDTV 508
Cdd:COG1232  428 --CIRSGREAAERILAEL 443
PLN02676 PLN02676
polyamine oxidase
42-517 2.58e-20

polyamine oxidase


Pssm-ID: 215362 [Multi-domain]  Cd Length: 487  Bit Score: 93.63  E-value: 2.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  42 ALLLIAQNGLHTSPSSKRIVVVGAGMAGLVAAKLLQDAGHE-VTILEASNHIGGRVvtlrNKEE--GWHFELGPMRI--- 115
Cdd:PLN02676  11 LAVHLFAVAAMDAKPSPSVIIVGAGMSGISAAKTLSEAGIEdILILEATDRIGGRM----RKANfaGVSVELGANWVegv 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 116 --PESHRIIhTYIQKFGLK--LNNFTQHDNNTwYLLRGHRYRASEVKAnpeilgyplrpSEKNKTAEDLFYQAITKVKAS 191
Cdd:PLN02676  87 ggPESNPIW-ELANKLKLRtfYSDFDNLSSNI-YKQDGGLYPKKVVQK-----------SMKVADASDEFGENLSISLSA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 192 NCSQLLSLYDSYSTKAYLLKEgmlsrgAVEMIGDMMN---ENAGFYR--SLLESLRIANI--FTKNDQFTEITGGFDQLP 264
Cdd:PLN02676 154 KKAVDISILTAQRLFGQVPKT------PLEMVIDYYNydyEFAEPPRvtSLKNTEPNPTFvdFGEDEYFVADPRGYESLV 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 265 NSLND---SLKPGTIH----LGSKVERVVgNESKVEVLYRT-DGPTsalYNltADYVIISASAKA--TRLIAFQPPLSPE 334
Cdd:PLN02676 228 YYLAEqflSTKSGKITdprlKLNKVVREI-SYSKNGVTVKTeDGSV---YR--AKYVIVSVSLGVlqSDLIKFKPPLPDW 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 335 KIRALRSVHYNSATKVIFVCNERFW-------------EKDGihggysitdrpsrfiYYPSYSR-----PSSKgILLASF 396
Cdd:PLN02676 302 KIEAIYQFDMAVYTKIFLKFPYKFWpsgpgtefflyahERRG---------------YYPFWQHleneyPGSN-VLFVTV 365
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 397 TmDDDSFFFTALKPNQVvdiilddLAAVHlipkEELKRM----CPKSE---VKHWSLDPFTIGSYAEF----TPYQFldd 465
Cdd:PLN02676 366 T-DEESRRIEQQPDSET-------KAEIM----EVLRKMfgpnIPEATdilVPRWWSNRFFKGSYSNWpigvSRYEF--- 430
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157817668 466 lKQLSQTEGRIYFAGEHTSLPH-AWIETAIKSGIRAAKNIQDTVDKEATQGQV 517
Cdd:PLN02676 431 -DQIRAPVGRVYFTGEHTSEKYnGYVHGAYLAGIDTANDLLECIKKKKCRKNV 482
PLN03000 PLN03000
amine oxidase
53-504 4.08e-18

amine oxidase


Pssm-ID: 178578 [Multi-domain]  Cd Length: 881  Bit Score: 87.77  E-value: 4.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  53 TSPSSKRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRVVT--LRNKEEGWHFELGPMRIPESHriihtyiqkfG 130
Cdd:PLN03000 180 AQSSKSSVVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGGRVYTkkMEANRVGAAADLGGSVLTGTL----------G 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 131 LKLNNFTQHDNNTWYLLRGH--RYRASevkanpeilGYPLRPSEKNKTAEDlFYQAITKVkasncSQLLSLYDSYSTKAY 208
Cdd:PLN03000 250 NPLGIIARQLGSSLYKVRDKcpLYRVD---------GKPVDPDVDLKVEVA-FNQLLDKA-----SKLRQLMGDVSMDVS 314
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 209 LlkeGMLSRGAVEMIGDMMN-ENAGFYRSLLESLRIAN----------IFTKNDQFTE------ITGGFDQLPNSLNDSL 271
Cdd:PLN03000 315 L---GAALETFRQVSGNDVAtEEMGLFNWHLANLEYANaglvsklslaFWDQDDPYDMggdhcfLPGGNGRLVQALAENV 391
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 272 ------KPGTIHLGSK-VERVVGNESKVEVLYRTDGPTSALYNLTadyviisasakatrlIAFQPPLSPEKIRALRSVHY 344
Cdd:PLN03000 392 pilyekTVQTIRYGSNgVKVIAGNQVYEGDMVLCTVPLGVLKNGS---------------IKFVPELPQRKLDCIKRLGF 456
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 345 NSATKVIFVCNERFWEKDGIHGGYsITDRPSR----FIYYpSYSrPSSKGILLASFTMDDDSFFFTALKPNQVVDIILDD 420
Cdd:PLN03000 457 GLLNKVAMLFPYVFWSTDLDTFGH-LTEDPNYrgefFLFY-SYA-PVAGGPLLIALVAGEAAHKFETMPPTDAVTRVLHI 533
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 421 LAAVH----LIPKEELKRMCPKsevkhWSLDPFTIGSYAEFTPYQFLDDLKQLSQT--EGRIYFAGEHTSLPH-AWIETA 493
Cdd:PLN03000 534 LRGIYepqgINVPDPLQTVCTR-----WGGDPFSLGSYSNVAVGASGDDYDILAESvgDGRLFFAGEATTRRYpATMHGA 608
                        490
                 ....*....|.
gi 157817668 494 IKSGIRAAKNI 504
Cdd:PLN03000 609 FVTGLREAANM 619
PLN02268 PLN02268
probable polyamine oxidase
60-508 3.29e-17

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 83.97  E-value: 3.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  60 IVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRVVTlrNKEEGWHFELGPMRIPE--SHRIIHTYIQKFGLKLNNfT 137
Cdd:PLN02268   3 VIVIGGGIAGIAAARALHDASFKVTLLESRDRIGGRVHT--DYSFGFPVDMGASWLHGvcNENPLAPLIGRLGLPLYR-T 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 138 QHDNNTWYllrghryrasevkaNPEILGYPLRPSEKNKTAEDLFYQ----------AITKVKASNCSQlLSLYDSYSTka 207
Cdd:PLN02268  80 SGDNSVLY--------------DHDLESYALFDMDGNQVPQELVTKvgetferileETEKVRDEHEED-MSLLQAISI-- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 208 yllkegMLSRGAVEMIGDMMNENAGFYRSLLESLRIA---NIFTKN-DQFTEITG-------GFDQLPNSLNDSLKpgtI 276
Cdd:PLN02268 143 ------VLERHPELRLEGLAHEVLQWYLCRMEGWFAAdadTISLKSwDQEELLEGghglmvrGYDPVINTLAKGLD---I 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 277 HLGSKVERVVGNESKVEVLYRtDGPTsalynLTADYVIISASA---KAtRLIAFQPPLSPEKIRALRSVHYNSATKVIFV 353
Cdd:PLN02268 214 RLNHRVTKIVRRYNGVKVTVE-DGTT-----FVADAAIIAVPLgvlKA-NIIKFEPELPEWKEEAISDLGVGIENKIALH 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 354 CNERFWEKDGIHGGYSITDRP-SRFI-YYPSYSRPSSKGILLASFTMDDDSffftalkpnqvvdiiLDDLAAVHLIpKEE 431
Cdd:PLN02268 287 FDSVFWPNVEFLGVVAPTSYGcSYFLnLHKATGHPVLVYMPAGRLARDIEK---------------LSDEAAANFA-MSQ 350
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 432 LKRMCP------KSEVKHWSLDPFTIGSYAeFTPYQFLDDL-KQLSQTEGRIYFAGEHTSLPH-AWIETAIKSGIRAAKN 503
Cdd:PLN02268 351 LKKMLPdatepvQYLVSRWGSDPNSLGCYS-YDLVGKPHDLyERLRAPVDNLFFAGEATSSDFpGSVHGAYSTGVMAAEE 429

                 ....*
gi 157817668 504 IQDTV 508
Cdd:PLN02268 430 CRMRL 434
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
56-111 2.52e-15

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


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 77.23  E-value: 2.52e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157817668  56 SSKRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRVVTLRNkeEGWHFELG 111
Cdd:COG3380    2 SMPDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGGRMATRRL--DGGRFDHG 55
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
56-112 2.63e-15

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 78.35  E-value: 2.63e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157817668  56 SSKRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRVVTLrnKEEGWHFELGP 112
Cdd:COG1233    2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTF--ERPGFRFDVGP 56
PLN02328 PLN02328
lysine-specific histone demethylase 1 homolog
47-512 6.98e-14

lysine-specific histone demethylase 1 homolog


Pssm-ID: 215187 [Multi-domain]  Cd Length: 808  Bit Score: 74.64  E-value: 6.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  47 AQNGLHTSPSSKRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRVVTLRNKEEGWHFEL---GPMRIPESHRIIH 123
Cdd:PLN02328 228 AQLRSFEGVEPANVVVVGAGLAGLVAARQLLSMGFKVVVLEGRARPGGRVKTMKMKGDGVVAAAdlgGSVLTGINGNPLG 307
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 124 TYIQKFGLKLNNFtqHDNNTWYLLRGhRYRASEVKANPEIlgyplrpsEKNKTAEDL--FYQAITKVKASNCSQLLSLYD 201
Cdd:PLN02328 308 VLARQLGLPLHKV--RDICPLYLPDG-KAVDAEIDSKIEA--------SFNKLLDRVckLRQAMIEEVKSVDVNLGTALE 376
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 202 SYStKAYLLKEGMLSRGAVEM-IGDMMNENAgfyrSLLESLRIAnIFTKNDQFTE------ITGGFDQLPNSLNDSLKpg 274
Cdd:PLN02328 377 AFR-HVYKVAEDPQERMLLNWhLANLEYANA----SLMSNLSMA-YWDQDDPYEMggdhcfIPGGNDTFVRELAKDLP-- 448
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 275 tIHLGSKVErvvgneskvEVLYRTDGptsalynltadyVIISASAKATR----------------LIAFQPPLSPEKIRA 338
Cdd:PLN02328 449 -IFYERTVE---------SIRYGVDG------------VIVYAGGQEFHgdmvlctvplgvlkkgSIEFYPELPQRKKDA 506
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 339 LRSVHYNSATKV--IFVCNerFWEKDGIHGGYSITDRPSR---FIYYpSYSRPSSkGILLASFTMDDDSFFFTALKPNQV 413
Cdd:PLN02328 507 IQRLGYGLLNKValLFPYN--FWGGEIDTFGHLTEDPSMRgefFLFY-SYSSVSG-GPLLIALVAGDAAVKFETLSPVES 582
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 414 VDIILDDLAAVH----LIPKEELKRMCPKsevkhWSLDPFTIGSYAEFTPYQFLDDLKQLSQT--EGRIYFAGEHTSLPH 487
Cdd:PLN02328 583 VKRVLQILRGIFhpkgIVVPDPVQAVCTR-----WGKDCFTYGSYSYVAVGSSGDDYDILAESvgDGRVFFAGEATNKQY 657
                        490       500
                 ....*....|....*....|....*.
gi 157817668 488 -AWIETAIKSGIRAAKNIQDTVDKEA 512
Cdd:PLN02328 658 pATMHGAFLSGMREAANILRVARRRS 683
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
62-125 1.54e-13

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 65.25  E-value: 1.54e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157817668   62 VVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRVVTLRNKeeGWHFELGPmripeshRIIHTY 125
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYSYRVP--GYVFDYGA-------HIFHGS 55
PLN02568 PLN02568
polyamine oxidase
59-501 3.61e-13

polyamine oxidase


Pssm-ID: 215308 [Multi-domain]  Cd Length: 539  Bit Score: 71.78  E-value: 3.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  59 RIVVVGAGMAGLVAAKLLQDAGH-----EVTILEASNHIGGRVVTlrNKEEGWHFELGPMRIpesHRIIHTYIQKFGLKL 133
Cdd:PLN02568   7 RIVIIGAGMAGLTAANKLYTSSAandmfELTVVEGGDRIGGRINT--SEFGGERIEMGATWI---HGIGGSPVYKIAQEA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 134 NNFtqHDNNTWYLLRGHRYRASEVKANpeilGYPLRPSEKNKTAEdLFYQ----AITKVKASNCSQLLSLYDSYSTKAYL 209
Cdd:PLN02568  82 GSL--ESDEPWECMDGFPDRPKTVAEG----GFEVDPSIVESIST-LFRGlmddAQGKLIEPSEVDEVDFVKLAAKAARV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 210 LKEG-------MLSRGAVEMIGDMMNEN-----AGFYRSLLESlriaNIFT--KNDQFT--------------------- 254
Cdd:PLN02568 155 CESGgggsvgsFLRRGLDAYWDSVSADEqikgyGGWSRKLLEE----AIFTmhENTQRTytsaddlstldlaaeseyrmf 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 255 ---EIT--GGFDQLPNSLNDSLKPGTIHLGSKVERVVGNESKVEvLYRTDGPTsalynLTADYVIISAS---AKA---TR 323
Cdd:PLN02568 231 pgeEITiaKGYLSVIEALASVLPPGTIQLGRKVTRIEWQDEPVK-LHFADGST-----MTADHVIVTVSlgvLKAgigED 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 324 LIAFQPPLSPEKIRALRSVHYNSATKVIFVCNERFWEKDGIHGGYSI-------TDRPSRFIYYPSYSR------PSSKG 390
Cdd:PLN02568 305 SGLFSPPLPDFKTDAISRLGFGVVNKLFVELSPRPDGSPEDVAKFPFlqmafhrSDSEARHDKIPWWMRrtasicPIHKN 384
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 391 --ILLASFTmDDDSFFFTALKPNQVVDIILDDLAAvhLIPKEELKRMCP------------------KSEVKH--WSLDP 448
Cdd:PLN02568 385 ssVLLSWFA-GKEALELEKLSDEEIIRGVQTTLSS--FLKRRVAGLGSQshplcnggassndgsrwkFVKVLKskWGTDP 461
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157817668 449 FTIGSY---------------AEftPYQFLDDLKQLSQTEGRIYFAGE-----HTSLPHAwietAIKSGIRAA 501
Cdd:PLN02568 462 LFLGSYsyvavgssgddldrmAE--PLPRISDHDQAGGPPLQLLFAGEathrtHYSTTHG----AYFSGLREA 528
PRK07233 PRK07233
hypothetical protein; Provisional
59-416 2.13e-12

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 69.15  E-value: 2.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  59 RIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRVVTLRnkEEGW------HFelgpmrIPESHRIIHTYIQKFGL- 131
Cdd:PRK07233   1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAASFE--FGGLpierfyHH------IFKSDEALLELLDELGLe 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 132 -KLnNFTQHDNNTWYllRGHRYRASevkaNP-EILGYP-LRPSEKNKTAedLFYQAITKVKAsncsqlLSLYDSYSTKAY 208
Cdd:PRK07233  73 dKL-RWRETKTGYYV--DGKLYPLG----TPlELLRFPhLSLIDKFRLG--LLTLLARRIKD------WRALDKVPAEEW 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 209 LLKEgmLSRGAVEMigdmmnenagFYRSLLES---------------LRIANI-FTKNDQFTE----ITGGFDQLPNSLN 268
Cdd:PRK07233 138 LRRW--SGEGVYEV----------FWEPLLESkfgdyaddvsaawlwSRIKRRgNRRYSLFGEklgyLEGGFATLIDALA 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 269 DSL--KPGTIHLGSKVERVVGNESKVEVLyRTDGPTsalynLTADYVIISASAKATRLIAfqPPLSPEKIRALRSVHYNS 346
Cdd:PRK07233 206 EAIeaRGGEIRLGTPVTSVVIDGGGVTGV-EVDGEE-----EDFDAVISTAPPPILARLV--PDLPADVLARLRRIDYQG 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 347 ATKVIFVCNER----FW---EKDGI----------------HGGYSItdrpsrfIYYPSYSRPSSKGillasFTMDDDSF 403
Cdd:PRK07233 278 VVCMVLKLRRPltdyYWlniNDPGApfggviehtnlvpperYGGEHL-------VYLPKYLPGDHPL-----WQMSDEEL 345
                        410       420
                 ....*....|....*....|...
gi 157817668 404 ----------FFTALKPNQVVDI 416
Cdd:PRK07233 346 ldrflsylrkMFPDFDRDDVRAV 368
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
57-507 3.31e-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: 68.34  E-value: 3.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  57 SKRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRVVTLRNKEEGWHFELGPMRIPESHRIIHTYIQKFGLkLNNF 136
Cdd:COG3349    3 PPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGGRARSFPDPDTGLPIDNGQHVLLGCYRNTLDLLRRIGA-ADNL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 137 TQHDNNTWYLLRGhryRASEVKANP---------EILGYP-LRPSEKNKTAEDLFyqaitkvkaSNCSQLLSLYDSYSTK 206
Cdd:COG3349   82 VGPEPLQFPLPGG---RRWTLRAPRlpaplhllrALLRAPgLSLADRLALLRLLT---------ACRERRWRELDDISVA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 207 AYLLKEGMlsrgavemigdmmneNAGFYRSLLESLRIANIFTKNDQ--------------FTEITGGFDQLPN-SLNDSL 271
Cdd:COG3349  150 DWLRRHGQ---------------SPRLIRRLWEPLLLAALNTPPEQasarlaltvlretlLAGPAASDLLVPRgPLSELF 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 272 -KP---------GTIHLGSKVERVVGNESKVEVLYRTDGPTsalynLTADYVIISASAK-ATRLIAFQPPL-SPEKIRAL 339
Cdd:COG3349  215 vDPalayleargGEVRLGTRVRALEFDGGRVTGLVLADGET-----VPADAVVLAVPPEvAARLLPELARLpELGLLAPL 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 340 RSVHYNSAtkvifvcneRFW---EKDGIHGGYS-ITDRPSRFIYYPSYSRPSSKGILLASFTMDDDsffFTALKPNQVVD 415
Cdd:COG3349  290 EYSPIVNV---------HLWldrPVTLGPPPFAgLVGSTSQWVFDRGAGDGGQGGVLSVVISAADR---LLDLSREELAA 357
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 416 IILDDLAAvhLIPKEELKRMCPKSEVK-HWSLDPFTIGSYAeFTPYQflddlkqlsQTEGR-IYFAGE--HTSLPhAWIE 491
Cdd:COG3349  358 EVWAELAA--LLPAAREALPVWSRVVReKRATFAATPGSDR-LRPGA---------RTPIPnLFLAGDwtATGLP-ATME 424
                        490
                 ....*....|....*.
gi 157817668 492 TAIKSGIRAAKNIQDT 507
Cdd:COG3349  425 GAVRSGRRAANAILAR 440
PLN02976 PLN02976
amine oxidase
58-100 1.72e-10

amine oxidase


Pssm-ID: 215527 [Multi-domain]  Cd Length: 1713  Bit Score: 64.12  E-value: 1.72e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 157817668   58 KRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRVVTLR 100
Cdd:PLN02976  694 KKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGRVYTDR 736
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
58-112 3.92e-10

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 61.79  E-value: 3.92e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157817668  58 KRIVVVGAGMAGLVAAKLLQDAG--HEVTILEASNHIGGRVVTLRnkEEGWHFELGP 112
Cdd:PRK11883   1 KKVAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKIQTVR--KDGFPIELGP 55
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
58-503 3.16e-09

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: 59.08  E-value: 3.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668   58 KRIVVVGAGMAGLVAA----KLLQDAGHEVTILEASNHIGGRVVTLrnKEEGWHFELGPMRIPESHRIIHTYIQKFGLKl 133
Cdd:TIGR00562   3 KHVVIIGGGISGLCAAyyleKEIPELPVELTLVEASDRVGGKIQTV--KEDGYLIERGPDSFLERKKSAPDLVKDLGLE- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  134 nNFTQHDNNTWYLLRGHRYRASEVKANP-EILGYPLRP-SEKNKTAEDLFYQA--------------------ITKVKAS 191
Cdd:TIGR00562  80 -HVLVSDATGQRYVLVNRGKLMPVPTKIaPFVKTGLFSlGGKLRAGMDFIRPAspgkdesveefvrrrfgdevVENLIEP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  192 NCS-------QLLSLYDSYStKAYLLKEGMLSrgaveMIGDMMNENAGFYRSLLESLriANIFTKNdqFTEITGGFDQLP 264
Cdd:TIGR00562 159 LLSgiyagdpSKLSLKSTFP-KFYQTEQKHGS-----LILGMKKTRNLPQGSGLQLT--AKKQGQD--FQTLATGLETLP 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  265 NSLNDSLKPGTIHLGSKVERVVgNESKVEVLYRTDGPTsalynLTADYVIISASA-KATRLIafqPPLSPEKIRALRSVH 343
Cdd:TIGR00562 229 EEIEKRLKLTKVYKGTKVTKLS-HRGSNYTLELDNGVT-----VETDSVVVTAPHkAAAGLL---SELSNSASSHLDKIH 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  344 YNSatkvIFVCNERFWEK--DGIHGGYS-ITDRPSRF-----IY----YPSYSRPSSkgILLASFT--MDDDSFFftALK 409
Cdd:TIGR00562 300 SPP----VANVNLGFPEGsvDGELEGFGfLISRSSKFailgcIFtsklFPNRAPPGK--TLLTAYIggATDESIV--DLS 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  410 PNQVVDIILDDLAAVHLIPKEELkrmcpKSEVKHW--SLDPFTIGSyaeftpYQFLDDLKQLSQTegriyfAGEHTSLPH 487
Cdd:TIGR00562 372 ENEIINIVLRDLKKVLNINNEPE-----MLCVTRWhrAIPQYHVGH------DQRLKEARELLES------AYPGVFLTG 434
                         490
                  ....*....|....*..
gi 157817668  488 AWIE-TAIKSGIRAAKN 503
Cdd:TIGR00562 435 NSFEgVGIPDCIDQGKA 451
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
52-100 4.75e-09

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 58.72  E-value: 4.75e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 157817668  52 HTSPSSKRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRVVTLR 100
Cdd:COG1148  135 IKVPVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQLH 183
PRK07208 PRK07208
hypothetical protein; Provisional
55-114 5.03e-09

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 58.36  E-value: 5.03e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  55 PSSKRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRVVTLRNKeeGWHFELGPMR 114
Cdd:PRK07208   2 TNKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGISRTVTYK--GNRFDIGGHR 59
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
56-94 9.77e-09

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


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 57.43  E-value: 9.77e-09
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 157817668  56 SSKRIVVVGAGMAGLVAAKLLQDAgHEVTILEASNHIGG 94
Cdd:COG2907    2 ARMRIAVIGSGISGLTAAWLLSRR-HDVTLFEANDRLGG 39
PLN02529 PLN02529
lysine-specific histone demethylase 1
51-504 1.17e-08

lysine-specific histone demethylase 1


Pssm-ID: 178144 [Multi-domain]  Cd Length: 738  Bit Score: 57.59  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  51 LHTSP-----SSKRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRVVTLRNKEEGWH--FELGPMRIPeshriih 123
Cdd:PLN02529 149 SFASPipeegTEGSVIIVGAGLAGLAAARQLLSFGFKVVVLEGRNRPGGRVYTQKMGRKGQFaaVDLGGSVIT------- 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 124 tyiqkfGLklnnftqHDNNTWYLLRG-----HRYRASEVKANPEilGYPLrPSEKNKTAEDLFYQAITKV---------- 188
Cdd:PLN02529 222 ------GI-------HANPLGVLARQlsiplHKVRDNCPLYKPD--GALV-DKEIDSNIEFIFNKLLDKVtelrqimggf 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 189 --KASNCSQLLSLYDSYSTKAYLLKEGMLSRGavemIGDMMNENAGFYRSLleslrIANIFTKNDQFTE------ITGGF 260
Cdd:PLN02529 286 anDISLGSVLERLRQLYGVARSTEERQLLDWH----LANLEYANAGCLSDL-----SAAYWDQDDPYEMggdhcfLAGGN 356
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 261 DQLPNSLNDSLKpgtIHLGSKVERVVGNESKVEVLyrtdgptSALYNLTADYVI--ISASAKATRLIAFQPPLSPEKIRA 338
Cdd:PLN02529 357 WRLINALCEGVP---IFYGKTVDTIKYGNDGVEVI-------AGSQVFQADMVLctVPLGVLKKRTIRFEPELPRRKLAA 426
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 339 LRSVHYNSATKVIFVCNERFWEKD----GIHGGYSItDRPSRFIYYPSYSrpSSKGILLASFTMDDDSFFFTALKPNQVV 414
Cdd:PLN02529 427 IDRLGFGLLNKVAMVFPSVFWGEEldtfGCLNESSN-KRGEFFLFYGYHT--VSGGPALVALVAGEAAQRFENTDPSTLL 503
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668 415 DIILDDLAAVHlIPK-----EELKRMCPKsevkhWSLDPFTIGSYAEFTPYQFLDDLKQLSQT-EGRIYFAGEHTSLPH- 487
Cdd:PLN02529 504 HRVLSVLRGIY-NPKginvpDPIQTICTR-----WGSDPLSYGSYSHVRVQSSGSDYDILAESvSGRLFFAGEATTRQYp 577
                        490
                 ....*....|....*..
gi 157817668 488 AWIETAIKSGIRAAKNI 504
Cdd:PLN02529 578 ATMHGAFLSGLREASRI 594
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
60-112 1.47e-08

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: 56.90  E-value: 1.47e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157817668   60 IVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRVVTLRnkEEGWHFELGP 112
Cdd:TIGR02734   1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGRAGVLE--DDGFRFDTGP 51
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
53-94 1.64e-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: 56.79  E-value: 1.64e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 157817668  53 TSPSSKRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGG 94
Cdd:COG2072    2 AATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGG 43
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
55-99 3.14e-08

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: 55.33  E-value: 3.14e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 157817668  55 PSSKRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHI--GGRVVTL 99
Cdd:COG0654    1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPrpDGRGIAL 47
PLN02487 PLN02487
zeta-carotene desaturase
59-111 5.57e-08

zeta-carotene desaturase


Pssm-ID: 215268 [Multi-domain]  Cd Length: 569  Bit Score: 55.19  E-value: 5.57e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157817668  59 RIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRVVTLRNKeEGWHFELG 111
Cdd:PLN02487  77 KVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGGKVGSFVDK-NGNHIEMG 128
PLN02612 PLN02612
phytoene desaturase
41-111 6.26e-08

phytoene desaturase


Pssm-ID: 215330 [Multi-domain]  Cd Length: 567  Bit Score: 55.23  E-value: 6.26e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157817668  41 EALLLIAQngLHTSPS-SK--RIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRVVTLRNKEEGWhFELG 111
Cdd:PLN02612  76 EAAALSAS--FRSAPRpAKplKVVIAGAGLAGLSTAKYLADAGHKPILLEARDVLGGKVAAWKDEDGDW-YETG 146
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
39-97 3.42e-07

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 52.45  E-value: 3.42e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157817668  39 DYEALLLIAQNGlhtspssKRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRVV 97
Cdd:COG1251  131 DADALRAALAPG-------KRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQL 182
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
55-94 3.92e-07

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


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 52.44  E-value: 3.92e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 157817668  55 PSSKRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGG 94
Cdd:COG0493  119 RTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG 158
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
55-94 8.93e-07

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 51.33  E-value: 8.93e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 157817668  55 PSSKRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGG 94
Cdd:PRK11749 138 KTGKKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG 177
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
54-94 1.40e-06

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 51.03  E-value: 1.40e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 157817668  54 SPSSKRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGG 94
Cdd:PRK12771 134 PDTGKRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGG 174
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
56-94 2.67e-06

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 50.11  E-value: 2.67e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 157817668  56 SSKRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGG 94
Cdd:PRK12814 192 SGKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGG 230
gltD PRK12810
glutamate synthase subunit beta; Reviewed
52-94 2.97e-06

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 49.78  E-value: 2.97e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 157817668  52 HTSPSSKRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGG 94
Cdd:PRK12810 138 PVKRTGKKVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGG 180
PRK07236 PRK07236
hypothetical protein; Provisional
53-100 4.89e-06

hypothetical protein; Provisional


Pssm-ID: 235980 [Multi-domain]  Cd Length: 386  Bit Score: 48.76  E-value: 4.89e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 157817668  53 TSPSSKRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHI----GGRVVTLR 100
Cdd:PRK07236   2 THMSGPRAVVIGGSLGGLFAALLLRRAGWDVDVFERSPTEldgrGAGIVLQP 53
PRK06753 PRK06753
hypothetical protein; Provisional
59-146 7.55e-06

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 48.15  E-value: 7.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668  59 RIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIggrvvtlrnKEEGWHFELGP--MRIPESHRIIHTyIQKFGLKLNNF 136
Cdd:PRK06753   2 KIAIIGAGIGGLTAAALLQEQGHEVKVFEKNESV---------KEVGAGIGIGDnvIKKLGNHDLAKG-IKNAGQILSTM 71
                         90
                 ....*....|
gi 157817668 137 TQHDNNTWYL 146
Cdd:PRK06753  72 NLLDDKGTLL 81
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
60-94 1.10e-05

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 47.87  E-value: 1.10e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 157817668  60 IVVVGAGMAGLVAAKLLQDAGHEVTIL--EASNHIGG 94
Cdd:COG3573    8 VIVVGAGLAGLVAAAELADAGRRVLLLdqEPEANLGG 44
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
57-94 1.41e-05

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 47.21  E-value: 1.41e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 157817668  57 SKRIVVVGAGMAGLVAAKLLQDAGHEVTILEAsNHIGG 94
Cdd:COG0665    2 TADVVVIGGGIAGLSTAYHLARRGLDVTVLER-GRPGS 38
PLN02576 PLN02576
protoporphyrinogen oxidase
50-112 1.66e-05

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 47.31  E-value: 1.66e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157817668  50 GLHTSPSSKRIVVVGAGMAGLVAA-KLLQDAGHEVTILEASNHIGGRVVTlrNKEEGWHFELGP 112
Cdd:PLN02576   5 EGSAAASSKDVAVVGAGVSGLAAAyALASKHGVNVLVTEARDRVGGNITS--VSEDGFIWEEGP 66
PRK12834 PRK12834
putative FAD-binding dehydrogenase; Reviewed
60-94 1.98e-05

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 183782 [Multi-domain]  Cd Length: 549  Bit Score: 47.20  E-value: 1.98e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 157817668  60 IVVVGAGMAGLVAAKLLQDAGHEVTIL--EASNHIGG 94
Cdd:PRK12834   7 VIVVGAGLAGLVAAAELADAGKRVLLLdqENEANLGG 43
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
59-111 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: 42.58  E-value: 2.23e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157817668   59 RIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIG-------GRVVTLRNKEEGWHFELG 111
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLpgfdpeiAKILQEKLEKNGIEFLLN 60
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
58-91 2.82e-05

NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 46.28  E-value: 2.82e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 157817668  58 KRIVVVGAGMAGLVAAKLLQD---AGHEVTILEASNH 91
Cdd:COG1252    2 KRIVIVGGGFAGLEAARRLRKklgGDAEVTLIDPNPY 38
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
59-94 3.73e-05

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: 45.85  E-value: 3.73e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 157817668   59 RIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGG 94
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGS 36
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
65-98 6.90e-05

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 44.57  E-value: 6.90e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 157817668  65 AGMAGLVAAKLLQDAGHEVTILEASNHIGGRVVT 98
Cdd:COG0644    1 AGPAGSAAARRLARAGLSVLLLEKGSFPGDKICG 34
PLN02172 PLN02172
flavin-containing monooxygenase FMO GS-OX
56-126 8.95e-05

flavin-containing monooxygenase FMO GS-OX


Pssm-ID: 215116 [Multi-domain]  Cd Length: 461  Bit Score: 44.85  E-value: 8.95e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157817668  56 SSKRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRVVTLRNKEEgwhfelGPMRIPESHRIIHTYI 126
Cdd:PLN02172   9 NSQHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGLWVYTPKSES------DPLSLDPTRSIVHSSV 73
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
58-88 1.53e-04

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: 43.85  E-value: 1.53e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 157817668   58 KRIVVVGAGMAGLVAAKLLQDAGHEVTILEA 88
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIED 31
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
49-92 2.16e-04

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: 43.46  E-value: 2.16e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 157817668   49 NGLHTSPSSKRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHI 92
Cdd:pfam07992 144 EALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRL 187
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
58-96 4.14e-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: 42.49  E-value: 4.14e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 157817668  58 KRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRV 96
Cdd:COG0446  125 KRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGVL 163
BetA COG2303
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ...
61-109 4.39e-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: 42.89  E-value: 4.39e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157817668  61 VVVGAGMAG-LVAAKLLQDAGHEVTILEAsnhiGGR------------VVTLRNKEEGWHFE 109
Cdd:COG2303    8 VIVGAGSAGcVLANRLSEDAGLRVLLLEA----GGRdddplirmpagyAKLLGNPRYDWRYE 65
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
60-94 5.20e-04

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


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 42.51  E-value: 5.20e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 157817668  60 IVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGG 94
Cdd:COG1053    6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
PRK13984 PRK13984
putative oxidoreductase; Provisional
55-94 1.21e-03

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 41.68  E-value: 1.21e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 157817668  55 PSSKRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGG 94
Cdd:PRK13984 281 KKNKKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGG 320
YhiN COG2081
Predicted flavoprotein YhiN [General function prediction only];
61-93 1.48e-03

Predicted flavoprotein YhiN [General function prediction only];


Pssm-ID: 441684 [Multi-domain]  Cd Length: 402  Bit Score: 40.80  E-value: 1.48e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 157817668  61 VVVGAGMAGLVAAKLLQDAGHEVTILEASNHIG 93
Cdd:COG2081    1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVG 33
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
60-94 1.68e-03

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


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 40.73  E-value: 1.68e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 157817668   60 IVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGG 94
Cdd:pfam00890   2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGG 36
PRK12779 PRK12779
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ...
60-94 1.73e-03

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


Pssm-ID: 183740 [Multi-domain]  Cd Length: 944  Bit Score: 41.36  E-value: 1.73e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 157817668  60 IVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGG 94
Cdd:PRK12779 309 IAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGG 343
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
39-94 1.76e-03

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 41.27  E-value: 1.76e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157817668  39 DYEAllliaQNGLHTSPSS-----KRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGG 94
Cdd:PRK12778 413 DYER-----ESGNISVPEVaekngKKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGG 468
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
57-88 1.95e-03

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 40.51  E-value: 1.95e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 157817668  57 SKRIVVVGAGMAGLVAAKLL--QDAGHEVTILEA 88
Cdd:COG1251    1 KMRIVIIGAGMAGVRAAEELrkLDPDGEITVIGA 34
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
60-86 2.00e-03

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 40.60  E-value: 2.00e-03
                         10        20
                 ....*....|....*....|....*..
gi 157817668  60 IVVVGAGMAGLVAAKLLQDAGHEVTIL 86
Cdd:PRK05329   5 VLVIGGGLAGLTAALAAAEAGKRVALV 31
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
59-99 2.01e-03

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: 38.64  E-value: 2.01e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 157817668    59 RIVVVGAGMAGLVAAKLLQDAGHEVTIL--------EASNHIGGRVVTL 99
Cdd:smart01002  22 KVVVIGAGVVGLGAAATAKGLGAEVTVLdvrparlrQLESLLGARFTTL 70
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
54-116 2.30e-03

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 40.36  E-value: 2.30e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157817668  54 SPSSKRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRVVtlrnkeegwhFELGPMRIP 116
Cdd:PRK12770  15 PPTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLML----------FGIPEFRIP 67
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
59-86 2.53e-03

Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 441497 [Multi-domain]  Cd Length: 305  Bit Score: 39.84  E-value: 2.53e-03
                         10        20
                 ....*....|....*....|....*....
gi 157817668  59 RIVVVGAG-MAGLVAAKLLQdAGHEVTIL 86
Cdd:COG1893    2 KIAILGAGaIGGLLGARLAR-AGHDVTLV 29
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
52-88 2.77e-03

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


Pssm-ID: 234978 [Multi-domain]  Cd Length: 662  Bit Score: 40.21  E-value: 2.77e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 157817668  52 HTSPSSKRIVVVGAGMAGLVAAKLLQDAGHEVTILEA 88
Cdd:PRK01747 255 PGSPKARDAAIIGGGIAGAALALALARRGWQVTLYEA 291
FMO-like pfam00743
Flavin-binding monooxygenase-like; This family includes FMO proteins, cyclohexanone ...
58-105 3.38e-03

Flavin-binding monooxygenase-like; This family includes FMO proteins, cyclohexanone mono-oxygenase and a number of different mono-oxygenases.


Pssm-ID: 395602 [Multi-domain]  Cd Length: 531  Bit Score: 40.15  E-value: 3.38e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 157817668   58 KRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRVVTLRNKEEG 105
Cdd:pfam00743   2 KKVAVIGAGVSGLASIKCCLEEGLEPTCFERSDDIGGLWRFTENVEEG 49
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
50-87 3.78e-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: 39.28  E-value: 3.78e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 157817668  50 GLHTSPSSKRIVVVGAGMAGLVAAKLLQDAGHEVTILE 87
Cdd:COG0569   88 ERGIKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVID 125
PRK12831 PRK12831
putative oxidoreductase; Provisional
58-97 3.80e-03

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 39.62  E-value: 3.80e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 157817668  58 KRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRVV 97
Cdd:PRK12831 141 KKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGGVLV 180
HI0933_like pfam03486
HI0933-like protein;
58-93 3.96e-03

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 39.49  E-value: 3.96e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 157817668   58 KRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHIG 93
Cdd:pfam03486   1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
58-103 4.84e-03

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 39.52  E-value: 4.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 157817668   58 KRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNhigGRVVTLRNKE 103
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQ---EKVDKLNKGK 43
PRK06847 PRK06847
hypothetical protein; Provisional
55-88 7.50e-03

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 38.70  E-value: 7.50e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 157817668  55 PSSKRIVVVGAGMAGLVAAKLLQDAGHEVTILEA 88
Cdd:PRK06847   2 AAVKKVLIVGGGIGGLSAAIALRRAGIAVDLVEI 35
PRK07588 PRK07588
FAD-binding domain;
58-97 8.39e-03

FAD-binding domain;


Pssm-ID: 169028 [Multi-domain]  Cd Length: 391  Bit Score: 38.56  E-value: 8.39e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 157817668  58 KRIVVVGAGMAGLVAAKLLQDAGHEVTILEASNHI--GGRVV 97
Cdd:PRK07588   1 MKVAISGAGIAGPTLAYWLRRYGHEPTLIERAPELrtGGYMV 42
PRK10157 PRK10157
putative oxidoreductase FixC; Provisional
61-98 8.41e-03

putative oxidoreductase FixC; Provisional


Pssm-ID: 182273 [Multi-domain]  Cd Length: 428  Bit Score: 38.74  E-value: 8.41e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 157817668  61 VVVGAGMAGLVAAKLLQDAGHEVTILEASNHIGGRVVT 98
Cdd:PRK10157   9 IIVGAGLAGSVAALVLAREGAQVLVIERGNSAGAKNVT 46
 
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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