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Conserved domains on  [gi|227500024|ref|NP_598653|]
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L-amino acid oxidase 1 precursor [Mus musculus]

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];
51-512 2.23e-126

Monoamine oxidase [Amino acid transport and metabolism];


:

Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 376.18  E-value: 2.23e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  51 LHTSPLSKRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGGRVVTLRNKEEGWYLELGPMRIPESHKLIHTYVQKLG 130
Cdd:COG1231    1 MSRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGLYAELGAMRIPPSHTNLLALARELG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 131 LKLNKFHQYDSNTWYLLNGQRYRASEVMANPGILGyplrpseknktvtDLFYQAITKIKphRKTSNCSQLLSLYDSYSTK 210
Cdd:COG1231   81 LPLEPFPNENGNALLYLGGKRVRAGEIAADLRGVA-------------ELLAKLLRALA--AALDPWAHPAAELDRESLA 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 211 AYLMKEGtLSKGAIEMIGDIMNENAG---YYKSLLESLRIASIFSKSDQFSEITGGFDQLPNGLSASLkPGTIRLGSKVE 287
Cdd:COG1231  146 EWLRRNG-ASPSARRLLGLLGAGEYGadpDELSLLDLLRYAASAGGGAQQFRIVGGMDQLPRALAAEL-GDRIRLGAPVT 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 288 RVVRDGPKVKVMYRTDGptsalhKLTADYAIITASAKATRLITFQPPLSREKTHALRSVHYTSATKVVLVCNERFWEQDG 367
Cdd:COG1231  224 RIRQDGDGVTVTTDDGG------TVRADAVIVTVPPSVLRRIEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEEDG 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 368 IRGGYSITDRPSRFIYYPSHSLPGGKGVLLaSFTVGDDSSFFAALKPNQVVDVVLDDLAAVHRIPKEELKRmcpkSAIKH 447
Cdd:COG1231  298 LYGGISLTDLPIRQTWYPSNGPDGGAGVLL-GYVGGDDARALAALSPEERVAAALEQLARIFGVYAAEPVD----YVSTD 372
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227500024 448 WSLDPLTIGAFTEFTPYQFVDYSKQLSQPEGRIYFAGEHTCLP-HSWIDTAIKSGIRASCNIQAAV 512
Cdd:COG1231  373 WGRDPWSRGAYAAAPPGQLTAAGPALAEPDGRIHFAGEHTSDEwPGWVEGALESGERAAAEILARL 438
 
Name Accession Description Interval E-value
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
51-512 2.23e-126

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 376.18  E-value: 2.23e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  51 LHTSPLSKRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGGRVVTLRNKEEGWYLELGPMRIPESHKLIHTYVQKLG 130
Cdd:COG1231    1 MSRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGLYAELGAMRIPPSHTNLLALARELG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 131 LKLNKFHQYDSNTWYLLNGQRYRASEVMANPGILGyplrpseknktvtDLFYQAITKIKphRKTSNCSQLLSLYDSYSTK 210
Cdd:COG1231   81 LPLEPFPNENGNALLYLGGKRVRAGEIAADLRGVA-------------ELLAKLLRALA--AALDPWAHPAAELDRESLA 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 211 AYLMKEGtLSKGAIEMIGDIMNENAG---YYKSLLESLRIASIFSKSDQFSEITGGFDQLPNGLSASLkPGTIRLGSKVE 287
Cdd:COG1231  146 EWLRRNG-ASPSARRLLGLLGAGEYGadpDELSLLDLLRYAASAGGGAQQFRIVGGMDQLPRALAAEL-GDRIRLGAPVT 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 288 RVVRDGPKVKVMYRTDGptsalhKLTADYAIITASAKATRLITFQPPLSREKTHALRSVHYTSATKVVLVCNERFWEQDG 367
Cdd:COG1231  224 RIRQDGDGVTVTTDDGG------TVRADAVIVTVPPSVLRRIEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEEDG 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 368 IRGGYSITDRPSRFIYYPSHSLPGGKGVLLaSFTVGDDSSFFAALKPNQVVDVVLDDLAAVHRIPKEELKRmcpkSAIKH 447
Cdd:COG1231  298 LYGGISLTDLPIRQTWYPSNGPDGGAGVLL-GYVGGDDARALAALSPEERVAAALEQLARIFGVYAAEPVD----YVSTD 372
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227500024 448 WSLDPLTIGAFTEFTPYQFVDYSKQLSQPEGRIYFAGEHTCLP-HSWIDTAIKSGIRASCNIQAAV 512
Cdd:COG1231  373 WGRDPWSRGAYAAAPPGQLTAAGPALAEPDGRIHFAGEHTSDEwPGWVEGALESGERAAAEILARL 438
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
67-508 2.50e-77

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: 250.10  E-value: 2.50e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024   67 MAGLVAAKTLQDAGHEVTILEASNHIGGRVVTLRnkEEGWYLELGPMRIPESHKLIHTYVQKLGLKLNKFHQyDSNTWYL 146
Cdd:pfam01593   1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVR--DDGFLIELGAMWFHGAQPPLLALLKELGLEDRLVLP-DPAPFYT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  147 L---NGQRYRAsEVMANPGIL------GYPLRPSEKNKTVTDLFYQAITKIKPhrktsncsqllslYDSYSTKAYLMKEG 217
Cdd:pfam01593  78 VlfaGGRRYPG-DFRRVPAGWegllefGRLLSIPEKLRLGLAALASDALDEFD-------------LDDFSLAESLLFLG 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  218 TLSKGAIEMIGDIMNENA--------GYYKSLLESLRIASIFSKSDQFSE-------ITGGFDQLPNGLSASLKPGTIRL 282
Cdd:pfam01593 144 RRGPGDVEVWDRLIDPELfaalpfasGAFAGDPSELSAGLALPLLWALLGeggslllPRGGLGALPDALAAQLLGGDVRL 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  283 GSKVERVVRDGPKVKVMYrTDGptsalHKLTADYAIITASAKATRLITFQPPLSREKTHALRSVHYTSATKVVLVCNERF 362
Cdd:pfam01593 224 NTRVRSIDREGDGVTVTL-TDG-----EVIEADAVIVTVPLGVLKRILFTPPLPPEKARAIRNLGYGPVNKVHLEFDRKF 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  363 WEQDGIRG--GYSITDRPSRFIY--YPSHSLPGGKGVLLASFTVGDDSSFFAALKPNQVVDVVLDDLAAVHRIPKEELKR 438
Cdd:pfam01593 298 WPDLGLLGllSELLTGLGTAFSWltFPNRAPPGKGLLLLVYVGPGDRARELEGLSDEELLQAVLRDLRKLFGEEAPEPLR 377
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227500024  439 MCpksaIKHWSLDPLTIGAFTEFTPYQF-VDYSKQLSQPEGRIYFAGEHTC--LPHSwIDTAIKSGIRASCNI 508
Cdd:pfam01593 378 VL----VSDWHTDPWPRGSYSLPQYGPGhDDYRPLARTPDPGLFFAGEHTStgYPGT-VEGAIESGRRAARAV 445
PLN02676 PLN02676
polyamine oxidase
44-520 9.08e-20

polyamine oxidase


Pssm-ID: 215362 [Multi-domain]  Cd Length: 487  Bit Score: 92.09  E-value: 9.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  44 LLIAQNGLHTSPLSKRVVVVGAGMAGLVAAKTLQDAGHE-VTILEASNHIGGRVvtlrNKEE--GWYLELGPMRI----- 115
Cdd:PLN02676  13 VHLFAVAAMDAKPSPSVIIVGAGMSGISAAKTLSEAGIEdILILEATDRIGGRM----RKANfaGVSVELGANWVegvgg 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 116 PESHKlIHTYVQKLGLK--LNKFHQYDSNTwYLLNGQRYrasevmanpgilgyplrpseKNKTVTDLFYQAITKIKphrK 193
Cdd:PLN02676  89 PESNP-IWELANKLKLRtfYSDFDNLSSNI-YKQDGGLY--------------------PKKVVQKSMKVADASDE---F 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 194 TSNCSQLLSLYDSYSTKAYLMK--EGTLSKGAIEMIGDIMNenagYYKSLLESLRIASI-----------FSKSDQFSEI 260
Cdd:PLN02676 144 GENLSISLSAKKAVDISILTAQrlFGQVPKTPLEMVIDYYN----YDYEFAEPPRVTSLkntepnptfvdFGEDEYFVAD 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 261 TGGFDQLPNGLSA---SLKPGTI---RLgsKVERVVR------DGPKVKVmyrTDGPTsalhkLTADYAIITASAKA--T 326
Cdd:PLN02676 220 PRGYESLVYYLAEqflSTKSGKItdpRL--KLNKVVReisyskNGVTVKT---EDGSV-----YRAKYVIVSVSLGVlqS 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 327 RLITFQPPLSREKTHALRSVHYTSATKVVLVCNERFWEQ----------DGIRGGYSITDRPSRfiYYPshslpgGKGVL 396
Cdd:PLN02676 290 DLIKFKPPLPDWKIEAIYQFDMAVYTKIFLKFPYKFWPSgpgtefflyaHERRGYYPFWQHLEN--EYP------GSNVL 361
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 397 LASFTvGDDSSFFAALKPNQV---VDVVLDDLAAVHrIPKEElKRMCPKsaikhWSLDPLTIGAFTEF----TPYQFvdy 469
Cdd:PLN02676 362 FVTVT-DEESRRIEQQPDSETkaeIMEVLRKMFGPN-IPEAT-DILVPR-----WWSNRFFKGSYSNWpigvSRYEF--- 430
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 227500024 470 sKQLSQPEGRIYFAGEHTCLPHS-WIDTAIKSGIRASCNIQAAVDKEATRGH 520
Cdd:PLN02676 431 -DQIRAPVGRVYFTGEHTSEKYNgYVHGAYLAGIDTANDLLECIKKKKCRKN 481
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
58-437 2.98e-13

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: 71.79  E-value: 2.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024   58 KRVVVVGAGMAGLVAA----KTLQDAGHEVTILEASNHIGGRVVTLrnKEEGWYLELGPMRIPESHKLIHTYVQKLGLKl 133
Cdd:TIGR00562   3 KHVVIIGGGISGLCAAyyleKEIPELPVELTLVEASDRVGGKIQTV--KEDGYLIERGPDSFLERKKSAPDLVKDLGLE- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  134 nkfHQYDSNTwyllNGQRYraseVMANPG-ILGYPLRPSEKNKtvTDLF------YQAITKIKPHRKTSNCS-------Q 199
Cdd:TIGR00562  80 ---HVLVSDA----TGQRY----VLVNRGkLMPVPTKIAPFVK--TGLFslggklRAGMDFIRPASPGKDESveefvrrR 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  200 LLSLYDSYSTKAYL--MKEGTLSKGAIEMIGDIMNENAGYYKSLLESLRIASIFSKSDQFSEITGGFDQLPNGLSASLK- 276
Cdd:TIGR00562 147 FGDEVVENLIEPLLsgIYAGDPSKLSLKSTFPKFYQTEQKHGSLILGMKKTRNLPQGSGLQLTAKKQGQDFQTLATGLEt 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  277 -PGTIRLGSKVERVVRDGPKVKVMYRTDGPTSALH---KLTADYAIITASA-KATRLItfqPPLSREKTHALRSVHYTSA 351
Cdd:TIGR00562 227 lPEEIEKRLKLTKVYKGTKVTKLSHRGSNYTLELDngvTVETDSVVVTAPHkAAAGLL---SELSNSASSHLDKIHSPPV 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  352 TKVVLVCNERFWEQDGIRGGYSITdRPSRF-----IYYPS---HSLPGGKgVLLASFTVGDDSSFFAALKPNQVVDVVLD 423
Cdd:TIGR00562 304 ANVNLGFPEGSVDGELEGFGFLIS-RSSKFailgcIFTSKlfpNRAPPGK-TLLTAYIGGATDESIVDLSENEIINIVLR 381
                         410
                  ....*....|....
gi 227500024  424 DLAAVHRIPKEELK 437
Cdd:TIGR00562 382 DLKKVLNINNEPEM 395
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
59-99 1.88e-04

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: 41.72  E-value: 1.88e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 227500024    59 RVVVVGAGMAGLVAAKTLQDAGHEVTIL--------EASNHIGGRVVTL 99
Cdd:smart01002  22 KVVVIGAGVVGLGAAATAKGLGAEVTVLdvrparlrQLESLLGARFTTL 70
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
59-99 8.16e-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: 41.62  E-value: 8.16e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 227500024  59 RVVVVGAGMAGLVAAKTLQDAGHEVTILEAS--------NHIGGRVVTL 99
Cdd:cd05305  170 KVVILGAGVVGENAARVALGLGAEVTVLDINlerlryldDIFGGRVTTL 218
 
Name Accession Description Interval E-value
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
51-512 2.23e-126

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 376.18  E-value: 2.23e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  51 LHTSPLSKRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGGRVVTLRNKEEGWYLELGPMRIPESHKLIHTYVQKLG 130
Cdd:COG1231    1 MSRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGLYAELGAMRIPPSHTNLLALARELG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 131 LKLNKFHQYDSNTWYLLNGQRYRASEVMANPGILGyplrpseknktvtDLFYQAITKIKphRKTSNCSQLLSLYDSYSTK 210
Cdd:COG1231   81 LPLEPFPNENGNALLYLGGKRVRAGEIAADLRGVA-------------ELLAKLLRALA--AALDPWAHPAAELDRESLA 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 211 AYLMKEGtLSKGAIEMIGDIMNENAG---YYKSLLESLRIASIFSKSDQFSEITGGFDQLPNGLSASLkPGTIRLGSKVE 287
Cdd:COG1231  146 EWLRRNG-ASPSARRLLGLLGAGEYGadpDELSLLDLLRYAASAGGGAQQFRIVGGMDQLPRALAAEL-GDRIRLGAPVT 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 288 RVVRDGPKVKVMYRTDGptsalhKLTADYAIITASAKATRLITFQPPLSREKTHALRSVHYTSATKVVLVCNERFWEQDG 367
Cdd:COG1231  224 RIRQDGDGVTVTTDDGG------TVRADAVIVTVPPSVLRRIEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEEDG 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 368 IRGGYSITDRPSRFIYYPSHSLPGGKGVLLaSFTVGDDSSFFAALKPNQVVDVVLDDLAAVHRIPKEELKRmcpkSAIKH 447
Cdd:COG1231  298 LYGGISLTDLPIRQTWYPSNGPDGGAGVLL-GYVGGDDARALAALSPEERVAAALEQLARIFGVYAAEPVD----YVSTD 372
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 227500024 448 WSLDPLTIGAFTEFTPYQFVDYSKQLSQPEGRIYFAGEHTCLP-HSWIDTAIKSGIRASCNIQAAV 512
Cdd:COG1231  373 WGRDPWSRGAYAAAPPGQLTAAGPALAEPDGRIHFAGEHTSDEwPGWVEGALESGERAAAEILARL 438
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
67-508 2.50e-77

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: 250.10  E-value: 2.50e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024   67 MAGLVAAKTLQDAGHEVTILEASNHIGGRVVTLRnkEEGWYLELGPMRIPESHKLIHTYVQKLGLKLNKFHQyDSNTWYL 146
Cdd:pfam01593   1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVR--DDGFLIELGAMWFHGAQPPLLALLKELGLEDRLVLP-DPAPFYT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  147 L---NGQRYRAsEVMANPGIL------GYPLRPSEKNKTVTDLFYQAITKIKPhrktsncsqllslYDSYSTKAYLMKEG 217
Cdd:pfam01593  78 VlfaGGRRYPG-DFRRVPAGWegllefGRLLSIPEKLRLGLAALASDALDEFD-------------LDDFSLAESLLFLG 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  218 TLSKGAIEMIGDIMNENA--------GYYKSLLESLRIASIFSKSDQFSE-------ITGGFDQLPNGLSASLKPGTIRL 282
Cdd:pfam01593 144 RRGPGDVEVWDRLIDPELfaalpfasGAFAGDPSELSAGLALPLLWALLGeggslllPRGGLGALPDALAAQLLGGDVRL 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  283 GSKVERVVRDGPKVKVMYrTDGptsalHKLTADYAIITASAKATRLITFQPPLSREKTHALRSVHYTSATKVVLVCNERF 362
Cdd:pfam01593 224 NTRVRSIDREGDGVTVTL-TDG-----EVIEADAVIVTVPLGVLKRILFTPPLPPEKARAIRNLGYGPVNKVHLEFDRKF 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  363 WEQDGIRG--GYSITDRPSRFIY--YPSHSLPGGKGVLLASFTVGDDSSFFAALKPNQVVDVVLDDLAAVHRIPKEELKR 438
Cdd:pfam01593 298 WPDLGLLGllSELLTGLGTAFSWltFPNRAPPGKGLLLLVYVGPGDRARELEGLSDEELLQAVLRDLRKLFGEEAPEPLR 377
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227500024  439 MCpksaIKHWSLDPLTIGAFTEFTPYQF-VDYSKQLSQPEGRIYFAGEHTC--LPHSwIDTAIKSGIRASCNI 508
Cdd:pfam01593 378 VL----VSDWHTDPWPRGSYSLPQYGPGhDDYRPLARTPDPGLFFAGEHTStgYPGT-VEGAIESGRRAARAV 445
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
57-436 1.15e-29

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: 121.09  E-value: 1.15e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  57 SKRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGGRVVTLRnkEEGWYLELGP----MRIPESHKLIHtyvqKLGLK 132
Cdd:COG1232    1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRTVE--VDGFRIDRGPhsflTRDPEVLELLR----ELGLG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 133 LNKFHQYDSNTWYLLNGQRYR----ASEVMANPGI---------LGY--PLRPSEKNKTVTDLFYQAITK------IKPh 191
Cdd:COG1232   75 DELVWPNTRKSYIYYGGKLHPlpqgPLALLRSPLLslagklralLELlaPRRPPGEDESLAEFVRRRFGRevyerlVEP- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 192 rktsncsqLLSLYdsYSTKAYlmkegTLSKGAI-EMIGDIMNEnagyYKSLLES-LRIASIFSKSDQFSEITGGFDQLPN 269
Cdd:COG1232  154 --------LLEGV--YAGDPD-----ELSADWAfPRLKRLELE----HGSLIKGaLALRKGAKAGEVFGYLRGGLGTLVE 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 270 GLSASLKPGTIRLGSKVERVVRDGPKVKVMYRtDGPTsalhkLTADYAIITASAKAT-RLItfqPPLSREKTHALRSVHY 348
Cdd:COG1232  215 ALAEALEAGEIRLGTRVTAIEREGGGWRVTTS-DGET-----IEADAVVSATPAPALaRLL---APLPPEVAAALAGIPY 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 349 TSATKVVLVCN-ERFWEQDGIrgGYSITDRPSRFIY---YPS----HSLPGGKGVLLAS-FTVGDDSsfFAALKPNQVVD 419
Cdd:COG1232  286 ASVAVVALGFDrPDLPPPDGF--GWLVPRDEGVPILavtFSSnkwpHRAPDGKVLLRLEvGGAGDPE--LWQLSDEELVA 361
                        410
                 ....*....|....*..
gi 227500024 420 VVLDDLAAVHRIPKEEL 436
Cdd:COG1232  362 LALADLRKLLGIDAEPV 378
PLN02676 PLN02676
polyamine oxidase
44-520 9.08e-20

polyamine oxidase


Pssm-ID: 215362 [Multi-domain]  Cd Length: 487  Bit Score: 92.09  E-value: 9.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  44 LLIAQNGLHTSPLSKRVVVVGAGMAGLVAAKTLQDAGHE-VTILEASNHIGGRVvtlrNKEE--GWYLELGPMRI----- 115
Cdd:PLN02676  13 VHLFAVAAMDAKPSPSVIIVGAGMSGISAAKTLSEAGIEdILILEATDRIGGRM----RKANfaGVSVELGANWVegvgg 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 116 PESHKlIHTYVQKLGLK--LNKFHQYDSNTwYLLNGQRYrasevmanpgilgyplrpseKNKTVTDLFYQAITKIKphrK 193
Cdd:PLN02676  89 PESNP-IWELANKLKLRtfYSDFDNLSSNI-YKQDGGLY--------------------PKKVVQKSMKVADASDE---F 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 194 TSNCSQLLSLYDSYSTKAYLMK--EGTLSKGAIEMIGDIMNenagYYKSLLESLRIASI-----------FSKSDQFSEI 260
Cdd:PLN02676 144 GENLSISLSAKKAVDISILTAQrlFGQVPKTPLEMVIDYYN----YDYEFAEPPRVTSLkntepnptfvdFGEDEYFVAD 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 261 TGGFDQLPNGLSA---SLKPGTI---RLgsKVERVVR------DGPKVKVmyrTDGPTsalhkLTADYAIITASAKA--T 326
Cdd:PLN02676 220 PRGYESLVYYLAEqflSTKSGKItdpRL--KLNKVVReisyskNGVTVKT---EDGSV-----YRAKYVIVSVSLGVlqS 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 327 RLITFQPPLSREKTHALRSVHYTSATKVVLVCNERFWEQ----------DGIRGGYSITDRPSRfiYYPshslpgGKGVL 396
Cdd:PLN02676 290 DLIKFKPPLPDWKIEAIYQFDMAVYTKIFLKFPYKFWPSgpgtefflyaHERRGYYPFWQHLEN--EYP------GSNVL 361
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 397 LASFTvGDDSSFFAALKPNQV---VDVVLDDLAAVHrIPKEElKRMCPKsaikhWSLDPLTIGAFTEF----TPYQFvdy 469
Cdd:PLN02676 362 FVTVT-DEESRRIEQQPDSETkaeIMEVLRKMFGPN-IPEAT-DILVPR-----WWSNRFFKGSYSNWpigvSRYEF--- 430
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 227500024 470 sKQLSQPEGRIYFAGEHTCLPHS-WIDTAIKSGIRASCNIQAAVDKEATRGH 520
Cdd:PLN02676 431 -DQIRAPVGRVYFTGEHTSEKYNgYVHGAYLAGIDTANDLLECIKKKKCRKN 481
PLN02268 PLN02268
probable polyamine oxidase
60-509 1.44e-19

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 91.29  E-value: 1.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  60 VVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGGRVVTlrNKEEGWYLELGPMRIPE--SHKLIHTYVQKLGLKLNKF- 136
Cdd:PLN02268   3 VIVIGGGIAGIAAARALHDASFKVTLLESRDRIGGRVHT--DYSFGFPVDMGASWLHGvcNENPLAPLIGRLGLPLYRTs 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 137 --------HQYDSNTWYLLNGQRYrasevmanpgilgyplrPSEKNKTVTDLFYQAITKIKPHRKTSncSQLLSLYDSYS 208
Cdd:PLN02268  81 gdnsvlydHDLESYALFDMDGNQV-----------------PQELVTKVGETFERILEETEKVRDEH--EEDMSLLQAIS 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 209 T----KAYLMKEGtlskgaiemigdIMNENAGYYKSLLESLRIA---SIFSKS-DQFSEITG-------GFDQLPNGLSA 273
Cdd:PLN02268 142 IvlerHPELRLEG------------LAHEVLQWYLCRMEGWFAAdadTISLKSwDQEELLEGghglmvrGYDPVINTLAK 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 274 SLKpgtIRLGSKVERVVRDGPKVKVMYRtDGPTsalhkLTADYAIITASA---KAtRLITFQPPLSREKTHALRSVHYTS 350
Cdd:PLN02268 210 GLD---IRLNHRVTKIVRRYNGVKVTVE-DGTT-----FVADAAIIAVPLgvlKA-NIIKFEPELPEWKEEAISDLGVGI 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 351 ATKVVLVCNERFWEQDGIRGGYSITDRPSRfiYYPSHSLPGGKGVLLasftvgddssFFAALKPNQVVDVVLDDLAAVHR 430
Cdd:PLN02268 280 ENKIALHFDSVFWPNVEFLGVVAPTSYGCS--YFLNLHKATGHPVLV----------YMPAGRLARDIEKLSDEAAANFA 347
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 431 IpkEELKRMCP------KSAIKHWSLDPLTIGAFTeftpYQFV----DYSKQLSQPEGRIYFAGEHTCLPHSW-IDTAIK 499
Cdd:PLN02268 348 M--SQLKKMLPdatepvQYLVSRWGSDPNSLGCYS----YDLVgkphDLYERLRAPVDNLFFAGEATSSDFPGsVHGAYS 421
                        490
                 ....*....|
gi 227500024 500 SGIRASCNIQ 509
Cdd:PLN02268 422 TGVMAAEECR 431
PLN02568 PLN02568
polyamine oxidase
59-503 3.13e-16

polyamine oxidase


Pssm-ID: 215308 [Multi-domain]  Cd Length: 539  Bit Score: 81.41  E-value: 3.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  59 RVVVVGAGMAGLVAAKTLQDAGH-----EVTILEASNHIGGRVVTlrNKEEGWYLELGPMRIpesHKLIHTYVQKLGLKL 133
Cdd:PLN02568   7 RIVIIGAGMAGLTAANKLYTSSAandmfELTVVEGGDRIGGRINT--SEFGGERIEMGATWI---HGIGGSPVYKIAQEA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 134 NKFHQydSNTWYLLNGQRYRASeVMANPGIL---------------------GYPLRPSEKNKTVTDLFYQAITKIKPHR 192
Cdd:PLN02568  82 GSLES--DEPWECMDGFPDRPK-TVAEGGFEvdpsivesistlfrglmddaqGKLIEPSEVDEVDFVKLAAKAARVCESG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 193 KTSNCSQLL-----SLYDSYSTKAYLMKEGTLSKGAIEMIGDIMNENAGY-YKSL--LESLRIASiFSKSDQFS--EIT- 261
Cdd:PLN02568 159 GGGSVGSFLrrgldAYWDSVSADEQIKGYGGWSRKLLEEAIFTMHENTQRtYTSAddLSTLDLAA-ESEYRMFPgeEITi 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 262 -GGFDQLPNGLSASLKPGTIRLGSKVERVVRDGPKVKVMYrTDGPTsalhkLTADYAIITAS---AKA---TRLITFQPP 334
Cdd:PLN02568 238 aKGYLSVIEALASVLPPGTIQLGRKVTRIEWQDEPVKLHF-ADGST-----MTADHVIVTVSlgvLKAgigEDSGLFSPP 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 335 LSREKTHALRSVHYTSATKVVLVCNERfweQDGIRGGYS-------ITDRP---SRFIYYP-----SHSL-P--GGKGVL 396
Cdd:PLN02568 312 LPDFKTDAISRLGFGVVNKLFVELSPR---PDGSPEDVAkfpflqmAFHRSdseARHDKIPwwmrrTASIcPihKNSSVL 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 397 LASFTvGDDSSFFAALKPNQVVDVVLDDLAAV--HRIPKEELKRMCP--------------KSAIKH--WSLDPLTIGAF 458
Cdd:PLN02568 389 LSWFA-GKEALELEKLSDEEIIRGVQTTLSSFlkRRVAGLGSQSHPLcnggassndgsrwkFVKVLKskWGTDPLFLGSY 467
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 227500024 459 TEFT-------------PYQFVDYSKQLSQPEGRIYFAGEHTCLPH-SWIDTAIKSGIR 503
Cdd:PLN02568 468 SYVAvgssgddldrmaePLPRISDHDQAGGPPLQLLFAGEATHRTHySTTHGAYFSGLR 526
PLN03000 PLN03000
amine oxidase
53-518 3.98e-16

amine oxidase


Pssm-ID: 178578 [Multi-domain]  Cd Length: 881  Bit Score: 81.60  E-value: 3.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  53 TSPLSKRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGGRVVT--LRNKEEGWYLELGPMRIPESH-KLIHTYVQKL 129
Cdd:PLN03000 180 AQSSKSSVVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGGRVYTkkMEANRVGAAADLGGSVLTGTLgNPLGIIARQL 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 130 GLKLNKFHqyDSNTWYLLNGQryrasevmanpgilgyPLRPSEKNKTVTDlFYQAITKIKPHRK-TSNCSQLLSLYDSYS 208
Cdd:PLN03000 260 GSSLYKVR--DKCPLYRVDGK----------------PVDPDVDLKVEVA-FNQLLDKASKLRQlMGDVSMDVSLGAALE 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 209 TkaylMKEGTLSKGAIEMIG-------DIMNENAGyyksLLESLRIAsiFSKSDQFSEITGGFDQLPNG---LSASLKPG 278
Cdd:PLN03000 321 T----FRQVSGNDVATEEMGlfnwhlaNLEYANAG----LVSKLSLA--FWDQDDPYDMGGDHCFLPGGngrLVQALAEN 390
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 279 TIRLGSKVERVVRDGPK-VKVmyrtdgpTSALHKLTADYAIITASAKATR--LITFQPPLSREKTHALRSVHYTSATKVV 355
Cdd:PLN03000 391 VPILYEKTVQTIRYGSNgVKV-------IAGNQVYEGDMVLCTVPLGVLKngSIKFVPELPQRKLDCIKRLGFGLLNKVA 463
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 356 LVCNERFWEQDGIRGGYsITDRPSR----FIYYPSHSLPGGKgvLLASFTVGDDSSFFAALKPNQVVDVVLDDLAAVHR- 430
Cdd:PLN03000 464 MLFPYVFWSTDLDTFGH-LTEDPNYrgefFLFYSYAPVAGGP--LLIALVAGEAAHKFETMPPTDAVTRVLHILRGIYEp 540
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 431 ----IPkEELKRMCPKsaikhWSLDPLTIGAFTEFTPYQFVDYSKQLSQP--EGRIYFAGEHTCLPH-SWIDTAIKSGIR 503
Cdd:PLN03000 541 qginVP-DPLQTVCTR-----WGGDPFSLGSYSNVAVGASGDDYDILAESvgDGRLFFAGEATTRRYpATMHGAFVTGLR 614
                        490
                 ....*....|....*
gi 227500024 504 ASCNIQAAVDKEATR 518
Cdd:PLN03000 615 EAANMAQSAKARGIR 629
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
57-428 1.80e-15

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: 78.74  E-value: 1.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  57 SKRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGGRVVTLRNKEEGWYLELGPmripesHKLI----HT--YVQKLG 130
Cdd:COG3349    3 PPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGGRARSFPDPDTGLPIDNGQ------HVLLgcyrNTldLLRRIG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 131 LkLNKFHQYDSNTWYLLNGQRYRASevmANPG---------ILGYP-LRPSEKNKTVtdlfyQAITKIKPHRktsncsql 200
Cdd:COG3349   77 A-ADNLVGPEPLQFPLPGGRRWTLR---APRLpaplhllraLLRAPgLSLADRLALL-----RLLTACRERR-------- 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 201 LSLYDSYSTKAYLMKEGtlskgaiemigdimnENAGYYKSLLESLRIASIFSKSDQ--------------FSEITGGFDQ 266
Cdd:COG3349  140 WRELDDISVADWLRRHG---------------QSPRLIRRLWEPLLLAALNTPPEQasarlaltvlretlLAGPAASDLL 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 267 LPNG-LSASL-KP---------GTIRLGSKVERVVRDGPKVKVMYRTDGPTsalhkLTADYAIITASAK-ATRLItfqPP 334
Cdd:COG3349  205 VPRGpLSELFvDPalayleargGEVRLGTRVRALEFDGGRVTGLVLADGET-----VPADAVVLAVPPEvAARLL---PE 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 335 LSREKTHALrsvhyTSATKVVLVCNERFWEQDGIRGG----YSITDRPSRFIYYPSHSLPGGKGVLLASFTVGDDssfFA 410
Cdd:COG3349  277 LARLPELGL-----LAPLEYSPIVNVHLWLDRPVTLGpppfAGLVGSTSQWVFDRGAGDGGQGGVLSVVISAADR---LL 348
                        410
                 ....*....|....*...
gi 227500024 411 ALKPNQVVDVVLDDLAAV 428
Cdd:COG3349  349 DLSREELAAEVWAELAAL 366
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
58-434 2.33e-15

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 78.35  E-value: 2.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  58 KRVVVVGAGMAGLVAAKTLQDAG--HEVTILEASNHIGGRVVTLRnkEEGWYLELGP----MRIPESHKLIHtyvqKLGL 131
Cdd:PRK11883   1 KKVAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKIQTVR--KDGFPIELGPesflARKPSAPALVK----ELGL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 132 KlnkfHQYDSNT----WYLLNGQRYRASE--VManpGIlgyplrPSEKNKTVTDLFYQAITK--------IKPHRKTSNC 197
Cdd:PRK11883  75 E----DELVANTtgqsYIYVNGKLHPIPPgtVM---GI------PTSIAPFLFAGLVSPIGKlraaadlrPPRWKPGQDQ 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 198 S-----------QL-------------------LSLYDSYST-KAYLMKEGTLSKGAIEMIGDIMNENAGYYKSLleslr 246
Cdd:PRK11883 142 SvgaffrrrfgdEVvenliepllsgiyagdidtLSLRATFPQlAQAEDKYGSLLRGMRKALPKEKKKTKGVFGTL----- 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 247 iasifsksdqfseiTGGFDQLPNGLSASLKPGTIRLGSKVERVVRDGPKVKVMYrTDGPTsalhkLTADYAIITASAKAT 326
Cdd:PRK11883 217 --------------KGGLQSLIEALEEKLPAGTIHKGTPVTKIDKSGDGYEIVL-SNGGE-----IEADAVIVAVPHPVL 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 327 RLITFQPPlsreKTHALRSVHYTSATKVVLV---CNERFWEQDGI----RGGYSITDrpsrfIYYPS----HSLPGGKGV 395
Cdd:PRK11883 277 PSLFVAPP----AFALFKTIPSTSVATVALAfpeSATNLPDGTGFlvarNSDYTITA-----CTWTSkkwpHTTPEGKVL 347
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 227500024 396 LLASF-TVGDDSSffAALKPNQVVDVVLDDLAAVHRIPKE 434
Cdd:PRK11883 348 LRLYVgRPGDEAV--VDATDEELVAFVLADLSKVMGITGD 385
PLN02328 PLN02328
lysine-specific histone demethylase 1 homolog
60-516 5.18e-15

lysine-specific histone demethylase 1 homolog


Pssm-ID: 215187 [Multi-domain]  Cd Length: 808  Bit Score: 78.11  E-value: 5.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  60 VVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGGRVVTLRNKEEGWYLEL---GPMRIPESHKLIHTYVQKLGLKLNKF 136
Cdd:PLN02328 241 VVVVGAGLAGLVAARQLLSMGFKVVVLEGRARPGGRVKTMKMKGDGVVAAAdlgGSVLTGINGNPLGVLARQLGLPLHKV 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 137 HqyDSNTWYLLNGQRYRAS-----EVMANPgILGY--PLRPS--EKNKTVTDLFYQAITKIKPHRKTSNCSQLLSLYDSY 207
Cdd:PLN02328 321 R--DICPLYLPDGKAVDAEidskiEASFNK-LLDRvcKLRQAmiEEVKSVDVNLGTALEAFRHVYKVAEDPQERMLLNWH 397
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 208 stkaylmkegtlskgaiemIGDIMNENAgyykSLLESLRIAsIFSKSDQFSE------ITGGFDQLPNGLSASLKpgtIR 281
Cdd:PLN02328 398 -------------------LANLEYANA----SLMSNLSMA-YWDQDDPYEMggdhcfIPGGNDTFVRELAKDLP---IF 450
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 282 LGSKVERvVRDGPKVKVMYRTDgptsalHKLTADYAIITASAKATR--LITFQPPLSREKTHALRSVHYTSATKVVLVCN 359
Cdd:PLN02328 451 YERTVES-IRYGVDGVIVYAGG------QEFHGDMVLCTVPLGVLKkgSIEFYPELPQRKKDAIQRLGYGLLNKVALLFP 523
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 360 ERFWEQDGIRGGYSITDRPSR---FIYYPSHSLPGGKgvLLASFTVGDDSSFFAALKPNQVVDVVLDDLAAVHRiPK--- 433
Cdd:PLN02328 524 YNFWGGEIDTFGHLTEDPSMRgefFLFYSYSSVSGGP--LLIALVAGDAAVKFETLSPVESVKRVLQILRGIFH-PKgiv 600
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 434 --EELKRMCPKsaikhWSLDPLTIGAFTEFTPYQFVDYSKQLSQP--EGRIYFAGEHTCLPH-SWIDTAIKSGIRASCNI 508
Cdd:PLN02328 601 vpDPVQAVCTR-----WGKDCFTYGSYSYVAVGSSGDDYDILAESvgDGRVFFAGEATNKQYpATMHGAFLSGMREAANI 675

                 ....*...
gi 227500024 509 QAAVDKEA 516
Cdd:PLN02328 676 LRVARRRS 683
PRK07233 PRK07233
hypothetical protein; Provisional
59-363 1.56e-14

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 75.69  E-value: 1.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  59 RVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGGRVVTLRnkEEGWYLElgpmR----IPES-HKLIHtYVQKLGLKl 133
Cdd:PRK07233   1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAASFE--FGGLPIE----RfyhhIFKSdEALLE-LLDELGLE- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 134 NKFHQYDSNTWYLLNGQRYRasevMANP-GILGYP-LRPSEKNKtvTDLFYQAITKIKPHRKtsncsqllslYDSYSTKA 211
Cdd:PRK07233  73 DKLRWRETKTGYYVDGKLYP----LGTPlELLRFPhLSLIDKFR--LGLLTLLARRIKDWRA----------LDKVPAEE 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 212 YLmkegtlskgaIEMIGdimnENAgyYKSLLESL-------------------RIASI-FSKSDQFSE----ITGGFDQL 267
Cdd:PRK07233 137 WL----------RRWSG----EGV--YEVFWEPLleskfgdyaddvsaawlwsRIKRRgNRRYSLFGEklgyLEGGFATL 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 268 PNGLSASL--KPGTIRLGSKVERVVRDGPKVKVMyRTDGptsalHKLTADYAIITASAKATRLITfqPPLSREKTHALRS 345
Cdd:PRK07233 201 IDALAEAIeaRGGEIRLGTPVTSVVIDGGGVTGV-EVDG-----EEEDFDAVISTAPPPILARLV--PDLPADVLARLRR 272
                        330       340
                 ....*....|....*....|..
gi 227500024 346 VHYTSATKVVLVCNER----FW 363
Cdd:PRK07233 273 IDYQGVVCMVLKLRRPltdyYW 294
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
58-111 2.47e-14

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


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 74.14  E-value: 2.47e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 227500024  58 KRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGGRVVTLRNkeEGWYLELG 111
Cdd:COG3380    4 PDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGGRMATRRL--DGGRFDHG 55
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
57-428 9.27e-14

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 73.35  E-value: 9.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  57 SKRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGGRVVTLrnKEEGWYLELGPMRIPESHkLIHTYVQKLGLKLN-K 135
Cdd:COG1233    3 MYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTF--ERPGFRFDVGPSVLTMPG-VLERLFRELGLEDYlE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 136 FHQYDSNTWYLLNGQR----YRASEVMAN----------PGILGYpLRPSEK--NKTVTDLFYQAITKIKPHRKTSNCSQ 199
Cdd:COG1233   80 LVPLDPAYRVPFPDGRaldlPRDLERTAAelerlfpgdaEAYRRF-LAELRRlyDALLEDLLYRPLLSLRDLLRPLALAR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 200 LLSLYDSySTKAYLMKEgTLSKGAIEMigdiMNENAGYY-KSLLESLRIASIFSKSDQFSEI---TGGFDQLPNGLSASL 275
Cdd:COG1233  159 LLRLLLR-SLRDLLRRY-FKDPRLRAL----LAGQALYLgLSPDRTPALYALIAYLEYAGGVwypKGGMGALADALARLA 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 276 K--PGTIRLGSKVERVVRDGPKVKVMYRTDGptsalHKLTADYAIITASAKAT--RLITfQPPLSREKTHALRSVHYT-S 350
Cdd:COG1233  233 EelGGEIRTGAEVERILVEGGRATGVRLADG-----EEIRADAVVSNADPAHTylRLLG-EEALPARYRRRLERFRYSpS 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 351 ATKVVLVCNERF-------------WEQ--DGIRGGySITDRPSRFIYYPSH---SL-PGGKGVLLASFTVG-DDSSFFA 410
Cdd:COG1233  307 AFKLYLGLDGPLpglahhtihlsedYEAafDDIFRG-RLPEDPSLYVSIPSLtdpSLaPEGKHTLWVLVPVPyGLEDAWD 385
                        410
                 ....*....|....*...
gi 227500024 411 ALKPnQVVDVVLDDLAAV 428
Cdd:COG1233  386 ELKE-EYAERILARLERY 402
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
58-437 2.98e-13

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: 71.79  E-value: 2.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024   58 KRVVVVGAGMAGLVAA----KTLQDAGHEVTILEASNHIGGRVVTLrnKEEGWYLELGPMRIPESHKLIHTYVQKLGLKl 133
Cdd:TIGR00562   3 KHVVIIGGGISGLCAAyyleKEIPELPVELTLVEASDRVGGKIQTV--KEDGYLIERGPDSFLERKKSAPDLVKDLGLE- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  134 nkfHQYDSNTwyllNGQRYraseVMANPG-ILGYPLRPSEKNKtvTDLF------YQAITKIKPHRKTSNCS-------Q 199
Cdd:TIGR00562  80 ---HVLVSDA----TGQRY----VLVNRGkLMPVPTKIAPFVK--TGLFslggklRAGMDFIRPASPGKDESveefvrrR 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  200 LLSLYDSYSTKAYL--MKEGTLSKGAIEMIGDIMNENAGYYKSLLESLRIASIFSKSDQFSEITGGFDQLPNGLSASLK- 276
Cdd:TIGR00562 147 FGDEVVENLIEPLLsgIYAGDPSKLSLKSTFPKFYQTEQKHGSLILGMKKTRNLPQGSGLQLTAKKQGQDFQTLATGLEt 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  277 -PGTIRLGSKVERVVRDGPKVKVMYRTDGPTSALH---KLTADYAIITASA-KATRLItfqPPLSREKTHALRSVHYTSA 351
Cdd:TIGR00562 227 lPEEIEKRLKLTKVYKGTKVTKLSHRGSNYTLELDngvTVETDSVVVTAPHkAAAGLL---SELSNSASSHLDKIHSPPV 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  352 TKVVLVCNERFWEQDGIRGGYSITdRPSRF-----IYYPS---HSLPGGKgVLLASFTVGDDSSFFAALKPNQVVDVVLD 423
Cdd:TIGR00562 304 ANVNLGFPEGSVDGELEGFGFLIS-RSSKFailgcIFTSKlfpNRAPPGK-TLLTAYIGGATDESIVDLSENEIINIVLR 381
                         410
                  ....*....|....
gi 227500024  424 DLAAVHRIPKEELK 437
Cdd:TIGR00562 382 DLKKVLNINNEPEM 395
PLN02529 PLN02529
lysine-specific histone demethylase 1
51-511 1.02e-12

lysine-specific histone demethylase 1


Pssm-ID: 178144 [Multi-domain]  Cd Length: 738  Bit Score: 70.69  E-value: 1.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  51 LHTSPL-----SKRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGGRVVTLRNKEEGWY--LELGPMRIPESH-KLI 122
Cdd:PLN02529 149 SFASPIpeegtEGSVIIVGAGLAGLAAARQLLSFGFKVVVLEGRNRPGGRVYTQKMGRKGQFaaVDLGGSVITGIHaNPL 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 123 HTYVQKLGLKLNKFHQydsntwyllNGQRYRASEVMANPGIlgyplrpsekNKTVTDLFYQAITKIKPHRKT----SNCS 198
Cdd:PLN02529 229 GVLARQLSIPLHKVRD---------NCPLYKPDGALVDKEI----------DSNIEFIFNKLLDKVTELRQImggfANDI 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 199 QLLSLYDSYStKAYLMKEGTLSKGAIEM-IGDIMNENAGYYKSLleslrIASIFSKSDQFSE------ITGGFDQLPNGL 271
Cdd:PLN02529 290 SLGSVLERLR-QLYGVARSTEERQLLDWhLANLEYANAGCLSDL-----SAAYWDQDDPYEMggdhcfLAGGNWRLINAL 363
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 272 SASLKpgtIRLGSKVERVVRDGPKVKVMyrtdgptSALHKLTADYAIITA--SAKATRLITFQPPLSREKTHALRSVHYT 349
Cdd:PLN02529 364 CEGVP---IFYGKTVDTIKYGNDGVEVI-------AGSQVFQADMVLCTVplGVLKKRTIRFEPELPRRKLAAIDRLGFG 433
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 350 SATKVVLVCNERFWEQD----GIRGGYSItDRPSRFIYYPSHSLPGGKgvLLASFTVGDDSSFFAALKPNQVVDVVLDDL 425
Cdd:PLN02529 434 LLNKVAMVFPSVFWGEEldtfGCLNESSN-KRGEFFLFYGYHTVSGGP--ALVALVAGEAAQRFENTDPSTLLHRVLSVL 510
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024 426 AAVHRiPK-----EELKRMCPKsaikhWSLDPLTIGAFTEF-TPYQFVDYSKQLSQPEGRIYFAGEHTCLPH-SWIDTAI 498
Cdd:PLN02529 511 RGIYN-PKginvpDPIQTICTR-----WGSDPLSYGSYSHVrVQSSGSDYDILAESVSGRLFFAGEATTRQYpATMHGAF 584
                        490
                 ....*....|....
gi 227500024 499 KSGIR-ASCNIQAA 511
Cdd:PLN02529 585 LSGLReASRILHVA 598
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
62-112 6.04e-12

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 61.01  E-value: 6.04e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 227500024   62 VVGAGMAGLVAAKTLQDAGHEVTILEASNHIGGRVVTLRNKeeGWYLELGP 112
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYSYRVP--GYVFDYGA 49
PLN02976 PLN02976
amine oxidase
58-100 2.89e-10

amine oxidase


Pssm-ID: 215527 [Multi-domain]  Cd Length: 1713  Bit Score: 63.35  E-value: 2.89e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 227500024   58 KRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGGRVVTLR 100
Cdd:PLN02976  694 KKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGRVYTDR 736
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
52-125 3.56e-10

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 62.18  E-value: 3.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  52 HTSPLSKRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGGRVVTLRNKEEGwyLE-----LGPM--RIpESHKLIHT 124
Cdd:COG1148  135 IKVPVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQLHKTFPG--LDcpqciLEPLiaEV-EANPNITV 211

                 .
gi 227500024 125 Y 125
Cdd:COG1148  212 Y 212
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
59-94 2.35e-09

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: 59.49  E-value: 2.35e-09
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 227500024  59 RVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGG 94
Cdd:COG2072    8 DVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGG 43
PLN02612 PLN02612
phytoene desaturase
53-107 8.81e-09

phytoene desaturase


Pssm-ID: 215330 [Multi-domain]  Cd Length: 567  Bit Score: 57.93  E-value: 8.81e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 227500024  53 TSPLskRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGGRVVTLRNKEEGWY 107
Cdd:PLN02612  91 AKPL--KVVIAGAGLAGLSTAKYLADAGHKPILLEARDVLGGKVAAWKDEDGDWY 143
PRK07208 PRK07208
hypothetical protein; Provisional
55-114 1.32e-08

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 57.21  E-value: 1.32e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  55 PLSKRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGGRVVTLRNKeeGWYLELGPMR 114
Cdd:PRK07208   2 TNKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGISRTVTYK--GNRFDIGGHR 59
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
39-97 3.33e-08

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 55.53  E-value: 3.33e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 227500024  39 DYEAFLLIAQNGlhtsplsKRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGGRVV 97
Cdd:COG1251  131 DADALRAALAPG-------KRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQL 182
PLN02487 PLN02487
zeta-carotene desaturase
59-111 1.21e-07

zeta-carotene desaturase


Pssm-ID: 215268 [Multi-domain]  Cd Length: 569  Bit Score: 54.42  E-value: 1.21e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 227500024  59 RVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGGRVVTLRNKeEGWYLELG 111
Cdd:PLN02487  77 KVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGGKVGSFVDK-NGNHIEMG 128
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
59-99 1.32e-07

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: 53.40  E-value: 1.32e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 227500024  59 RVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHI--GGRVVTL 99
Cdd:COG0654    5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPrpDGRGIAL 47
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
58-94 3.36e-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: 3.36e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 227500024  58 KRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGG 94
Cdd:COG0493  122 KKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG 158
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
57-94 3.83e-07

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


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 52.43  E-value: 3.83e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 227500024  57 SKRVVVVGAGMAGLVAAKTLQDAgHEVTILEASNHIGG 94
Cdd:COG2907    3 RMRIAVIGSGISGLTAAWLLSRR-HDVTLFEANDRLGG 39
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
60-112 4.44e-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: 52.28  E-value: 4.44e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 227500024   60 VVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGGRVVTLRnkEEGWYLELGP 112
Cdd:TIGR02734   1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGRAGVLE--DDGFRFDTGP 51
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
55-94 4.65e-07

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 52.10  E-value: 4.65e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 227500024  55 PLSKRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGG 94
Cdd:PRK11749 138 KTGKKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG 177
gltD PRK12810
glutamate synthase subunit beta; Reviewed
58-94 5.63e-07

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 52.09  E-value: 5.63e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 227500024  58 KRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGG 94
Cdd:PRK12810 144 KKVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGG 180
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
60-94 1.56e-06

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 50.56  E-value: 1.56e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 227500024  60 VVVVGAGMAGLVAAKTLQDAGHEVTIL--EASNHIGG 94
Cdd:COG3573    8 VIVVGAGLAGLVAAAELADAGRRVLLLdqEPEANLGG 44
PRK12834 PRK12834
putative FAD-binding dehydrogenase; Reviewed
60-94 2.41e-06

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 183782 [Multi-domain]  Cd Length: 549  Bit Score: 50.28  E-value: 2.41e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 227500024  60 VVVVGAGMAGLVAAKTLQDAGHEVTIL--EASNHIGG 94
Cdd:PRK12834   7 VIVVGAGLAGLVAAAELADAGKRVLLLdqENEANLGG 43
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
58-94 3.97e-06

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 49.49  E-value: 3.97e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 227500024  58 KRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGG 94
Cdd:PRK12771 138 KRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGG 174
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
58-94 4.65e-06

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 49.34  E-value: 4.65e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 227500024  58 KRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGG 94
Cdd:PRK12814 194 KKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGG 230
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
57-94 5.08e-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: 5.08e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 227500024  57 SKRVVVVGAGMAGLVAAKTLQDAGHEVTILEAsNHIGG 94
Cdd:COG0665    2 TADVVVIGGGIAGLSTAYHLARRGLDVTVLER-GRPGS 38
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
58-88 6.76e-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: 48.08  E-value: 6.76e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 227500024   58 KRVVVVGAGMAGLVAAKTLQDAGHEVTILEA 88
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIED 31
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
60-94 1.15e-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: 47.91  E-value: 1.15e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 227500024  60 VVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGG 94
Cdd:COG1053    6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
PLN02576 PLN02576
protoporphyrinogen oxidase
50-112 1.33e-05

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 47.70  E-value: 1.33e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 227500024  50 GLHTSPLSKRVVVVGAGMAGLVAAKTLQDA-GHEVTILEASNHIGGRVVTlrNKEEGWYLELGP 112
Cdd:PLN02576   5 EGSAAASSKDVAVVGAGVSGLAAAYALASKhGVNVLVTEARDRVGGNITS--VSEDGFIWEEGP 66
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
58-91 1.70e-05

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 47.05  E-value: 1.70e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 227500024  58 KRVVVVGAGMAGLVAAKTLQD---AGHEVTILEASNH 91
Cdd:COG1252    2 KRIVIVGGGFAGLEAARRLRKklgGDAEVTLIDPNPY 38
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
59-133 2.11e-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: 46.62  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024   59 RVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIG-------GRVVTlrnkeeGWYLELGPMRIP----ESHKLIHTYVQ 127
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGsgasgrnAGLIH------PGLRYLEPSELArlalEALDLWEELEE 74

                  ....*.
gi 227500024  128 KLGLKL 133
Cdd:pfam01266  75 ELGIDC 80
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
57-111 2.18e-05

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 46.67  E-value: 2.18e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227500024  57 SKRVVVVGAGMAGLVAAKTL--QDAGHEVTILEA-----------SNHIGGRV----VTLRnkEEGWYLELG 111
Cdd:COG1251    1 KMRIVIIGAGMAGVRAAEELrkLDPDGEITVIGAephppynrpplSKVLAGETdeedLLLR--PADFYEENG 70
PRK07236 PRK07236
hypothetical protein; Provisional
59-100 2.84e-05

hypothetical protein; Provisional


Pssm-ID: 235980 [Multi-domain]  Cd Length: 386  Bit Score: 46.45  E-value: 2.84e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 227500024  59 RVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHI----GGRVVTLR 100
Cdd:PRK07236   8 RAVVIGGSLGGLFAALLLRRAGWDVDVFERSPTEldgrGAGIVLQP 53
PLN02172 PLN02172
flavin-containing monooxygenase FMO GS-OX
57-94 4.47e-05

flavin-containing monooxygenase FMO GS-OX


Pssm-ID: 215116 [Multi-domain]  Cd Length: 461  Bit Score: 46.01  E-value: 4.47e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 227500024  57 SKRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGG 94
Cdd:PLN02172  10 SQHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGG 47
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
49-92 4.60e-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: 45.39  E-value: 4.60e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 227500024   49 NGLHTSPLSKRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHI 92
Cdd:pfam07992 144 EALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRL 187
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
58-96 5.87e-05

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: 45.19  E-value: 5.87e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 227500024  58 KRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGGRV 96
Cdd:COG0446  125 KRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGVL 163
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
60-94 6.13e-05

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: 45.36  E-value: 6.13e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 227500024   60 VVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGG 94
Cdd:pfam00890   2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGG 36
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
65-98 6.26e-05

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 44.96  E-value: 6.26e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 227500024  65 AGMAGLVAAKTLQDAGHEVTILEASNHIGGRVVT 98
Cdd:COG0644    1 AGPAGSAAARRLARAGLSVLLLEKGSFPGDKICG 34
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
59-92 7.22e-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: 41.42  E-value: 7.22e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 227500024   59 RVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHI 92
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRL 34
PRK06753 PRK06753
hypothetical protein; Provisional
59-146 1.04e-04

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 44.68  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227500024  59 RVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIggrvvtlrnKEEGWYLELGPMRIpesHKL----IHTYVQKLGLKLN 134
Cdd:PRK06753   2 KIAIIGAGIGGLTAAALLQEQGHEVKVFEKNESV---------KEVGAGIGIGDNVI---KKLgnhdLAKGIKNAGQILS 69
                         90
                 ....*....|..
gi 227500024 135 KFHQYDSNTWYL 146
Cdd:PRK06753  70 TMNLLDDKGTLL 81
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
59-99 1.88e-04

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: 41.72  E-value: 1.88e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 227500024    59 RVVVVGAGMAGLVAAKTLQDAGHEVTIL--------EASNHIGGRVVTL 99
Cdd:smart01002  22 KVVVIGAGVVGLGAAATAKGLGAEVTVLdvrparlrQLESLLGARFTTL 70
HI0933_like pfam03486
HI0933-like protein;
58-93 2.03e-04

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 43.72  E-value: 2.03e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 227500024   58 KRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIG 93
Cdd:pfam03486   1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
60-86 2.54e-04

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 43.30  E-value: 2.54e-04
                         10        20
                 ....*....|....*....|....*..
gi 227500024  60 VVVVGAGMAGLVAAKTLQDAGHEVTIL 86
Cdd:PRK05329   5 VLVIGGGLAGLTAALAAAEAGKRVALV 31
YhiN COG2081
Predicted flavoprotein YhiN [General function prediction only];
61-93 2.57e-04

Predicted flavoprotein YhiN [General function prediction only];


Pssm-ID: 441684 [Multi-domain]  Cd Length: 402  Bit Score: 43.50  E-value: 2.57e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 227500024  61 VVVGAGMAGLVAAKTLQDAGHEVTILEASNHIG 93
Cdd:COG2081    1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVG 33
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
52-88 4.70e-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: 42.91  E-value: 4.70e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 227500024  52 HTSPLSKRVVVVGAGMAGLVAAKTLQDAGHEVTILEA 88
Cdd:PRK01747 255 PGSPKARDAAIIGGGIAGAALALALARRGWQVTLYEA 291
BetA COG2303
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ...
60-95 5.41e-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: 42.51  E-value: 5.41e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 227500024  60 VVVVGAGMAGLVAAKTL-QDAGHEVTILEAsnhiGGR 95
Cdd:COG2303    7 YVIVGAGSAGCVLANRLsEDAGLRVLLLEA----GGR 39
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
50-87 5.48e-04

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: 41.98  E-value: 5.48e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 227500024  50 GLHTSPLSKRVVVVGAGMAGLVAAKTLQDAGHEVTILE 87
Cdd:COG0569   88 ERGIKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVID 125
PRK12831 PRK12831
putative oxidoreductase; Provisional
58-97 6.83e-04

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 42.31  E-value: 6.83e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 227500024  58 KRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGGRVV 97
Cdd:PRK12831 141 KKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGGVLV 180
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
58-94 7.15e-04

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 42.42  E-value: 7.15e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 227500024  58 KRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGG 94
Cdd:PRK12778 432 KKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGG 468
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
59-99 8.16e-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: 41.62  E-value: 8.16e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 227500024  59 RVVVVGAGMAGLVAAKTLQDAGHEVTILEAS--------NHIGGRVVTL 99
Cdd:cd05305  170 KVVILGAGVVGENAARVALGLGAEVTVLDINlerlryldDIFGGRVTTL 218
PRK13984 PRK13984
putative oxidoreductase; Provisional
58-94 1.01e-03

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 41.68  E-value: 1.01e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 227500024  58 KRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGG 94
Cdd:PRK13984 284 KKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGG 320
FMO-like pfam00743
Flavin-binding monooxygenase-like; This family includes FMO proteins, cyclohexanone ...
58-105 1.50e-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: 41.30  E-value: 1.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 227500024   58 KRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGGRVVTLRNKEEG 105
Cdd:pfam00743   2 KKVAVIGAGVSGLASIKCCLEEGLEPTCFERSDDIGGLWRFTENVEEG 49
PRK07843 PRK07843
3-oxosteroid 1-dehydrogenase;
60-94 1.54e-03

3-oxosteroid 1-dehydrogenase;


Pssm-ID: 236111 [Multi-domain]  Cd Length: 557  Bit Score: 41.17  E-value: 1.54e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 227500024  60 VVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGG 94
Cdd:PRK07843  10 VVVVGSGAAGMVAALTAAHRGLSTVVVEKAPHYGG 44
Ald COG0686
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ...
59-99 3.11e-03

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: 39.99  E-value: 3.11e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 227500024  59 RVVVVGAGMAGLVAAKTLQDAGHEVTIL--------EASNHIGGRVVTL 99
Cdd:COG0686  170 KVVILGGGVVGTNAARMALGLGADVTVLdinldrlrRLDDIFGGRVTTL 218
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
60-94 3.79e-03

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


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 39.68  E-value: 3.79e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 227500024  60 VVVVGAGMAGLVAAKTLQDAGHEVTILEASnHIGG 94
Cdd:COG1249    6 LVVIGAGPGGYVAAIRAAQLGLKVALVEKG-RLGG 39
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
60-94 4.97e-03

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


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 39.51  E-value: 4.97e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 227500024   60 VVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGG 94
Cdd:pfam12831   2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGG 36
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
60-93 5.12e-03

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


Pssm-ID: 273936 [Multi-domain]  Cd Length: 295  Bit Score: 38.84  E-value: 5.12e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 227500024   60 VVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIG 93
Cdd:TIGR02032   3 VVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPR 36
PRK12844 PRK12844
3-ketosteroid-delta-1-dehydrogenase; Reviewed
60-94 5.54e-03

3-ketosteroid-delta-1-dehydrogenase; Reviewed


Pssm-ID: 183787 [Multi-domain]  Cd Length: 557  Bit Score: 39.35  E-value: 5.54e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 227500024  60 VVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGG 94
Cdd:PRK12844   9 VVVVGSGGGGMCAALAAADSGLEPLIVEKQDKVGG 43
PRK00711 PRK00711
D-amino acid dehydrogenase;
59-87 5.85e-03

D-amino acid dehydrogenase;


Pssm-ID: 234819 [Multi-domain]  Cd Length: 416  Bit Score: 39.01  E-value: 5.85e-03
                         10        20
                 ....*....|....*....|....*....
gi 227500024  59 RVVVVGAGMAGLVAAKTLQDAGHEVTILE 87
Cdd:PRK00711   2 RVVVLGSGVIGVTSAWYLAQAGHEVTVID 30
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
59-104 7.71e-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: 37.86  E-value: 7.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 227500024   59 RVVVVGAGMAGLVAAKTLQDAGHEVTIL--------EASNHIGGRVVTLRNKEE 104
Cdd:pfam01262  30 KVLVIGGGVAGLNAAATAKGLGAIVTILdvrparleQLESILGAKFVETLYSQA 83
PRK08163 PRK08163
3-hydroxybenzoate 6-monooxygenase;
59-112 8.97e-03

3-hydroxybenzoate 6-monooxygenase;


Pssm-ID: 181262 [Multi-domain]  Cd Length: 396  Bit Score: 38.48  E-value: 8.97e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 227500024  59 RVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHIGgrvvtlrnkEEGWYLELGP 112
Cdd:PRK08163   6 PVLIVGGGIGGLAAALALARQGIKVKLLEQAAEIG---------EIGAGIQLGP 50
PRK07588 PRK07588
FAD-binding domain;
58-97 9.09e-03

FAD-binding domain;


Pssm-ID: 169028 [Multi-domain]  Cd Length: 391  Bit Score: 38.56  E-value: 9.09e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 227500024  58 KRVVVVGAGMAGLVAAKTLQDAGHEVTILEASNHI--GGRVV 97
Cdd:PRK07588   1 MKVAISGAGIAGPTLAYWLRRYGHEPTLIERAPELrtGGYMV 42
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
59-86 9.12e-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: 38.30  E-value: 9.12e-03
                         10        20
                 ....*....|....*....|....*....
gi 227500024  59 RVVVVGAG-MAGLVAAKtLQDAGHEVTIL 86
Cdd:COG1893    2 KIAILGAGaIGGLLGAR-LARAGHDVTLV 29
PRK06847 PRK06847
hypothetical protein; Provisional
58-88 9.93e-03

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 38.32  E-value: 9.93e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 227500024  58 KRVVVVGAGMAGLVAAKTLQDAGHEVTILEA 88
Cdd:PRK06847   5 KKVLIVGGGIGGLSAAIALRRAGIAVDLVEI 35
 
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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