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Conserved domains on  [gi|817033869|sp|X2L4E2|]
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RecName: Full=L-amino acid oxidase; Short=Bpic-LAAO; Short=LAO; Flags: Precursor

Protein Classification

flavin monoamine oxidase family protein( domain architecture ID 11440890)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
38-494 9.65e-124

Monoamine oxidase [Amino acid transport and metabolism];


:

Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 368.48  E-value: 9.65e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869  38 LSTTSNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTYRNEKEGWYANLGPMRLPEKHRIVREYIKKFD 117
Cdd:COG1231    1 MSRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGLYAELGAMRIPPSHTNLLALARELG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 118 LRLNEFSQENENAWYFLQNIKKRVREVNKDPGVLeypvkpsevgksagqlyEESLRKAVEELRR--TNCSYMLNKYDTYS 195
Cdd:COG1231   81 LPLEPFPNENGNALLYLGGKRVRAGEIAADLRGV-----------------AELLAKLLRALAAalDPWAHPAAELDRES 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 196 TKEYLLKEGnLSPGAVDMIGDLLNEDSG---YYVSFIESLKHDDIFAYEKRFDEIVGGMDKLPTSMYQAIQEKVHLNARV 272
Cdd:COG1231  144 LAEWLRRNG-ASPSARRLLGLLGAGEYGadpDELSLLDLLRYAASAGGGAQQFRIVGGMDQLPRALAAELGDRIRLGAPV 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 273 IEIQQDVKEVTVTYQTSQketlSVTADYVIVCTTSRAARRITFEPPLPPKKAHALLSVHYRSGTKIFLTCTKKFWEDDGI 352
Cdd:COG1231  223 TRIRQDGDGVTVTTDDGG----TVRADAVIVTVPPSVLRRIEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEEDGL 298

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 353 HGGKSTTDLPSRFIYYPNHNFPNGVGVIIAYGIGDDANYFQALDFEDCGDIVINDLSLIHQLPKEEIQAicrpSMIQRWS 432
Cdd:COG1231  299 YGGISLTDLPIRQTWYPSNGPDGGAGVLLGYVGGDDARALAALSPEERVAAALEQLARIFGVYAAEPVD----YVSTDWG 374

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 817033869 433 LDNYAMGGITTFTPYHFQHFSEALTAPVDRIYFAGEYTAQA-HGWIDSTIKSGLRAATDVNRA 494
Cdd:COG1231  375 RDPWSRGAYAAAPPGQLTAAGPALAEPDGRIHFAGEHTSDEwPGWVEGALESGERAAAEILAR 437
 
Name Accession Description Interval E-value
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
38-494 9.65e-124

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 368.48  E-value: 9.65e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869  38 LSTTSNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTYRNEKEGWYANLGPMRLPEKHRIVREYIKKFD 117
Cdd:COG1231    1 MSRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGLYAELGAMRIPPSHTNLLALARELG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 118 LRLNEFSQENENAWYFLQNIKKRVREVNKDPGVLeypvkpsevgksagqlyEESLRKAVEELRR--TNCSYMLNKYDTYS 195
Cdd:COG1231   81 LPLEPFPNENGNALLYLGGKRVRAGEIAADLRGV-----------------AELLAKLLRALAAalDPWAHPAAELDRES 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 196 TKEYLLKEGnLSPGAVDMIGDLLNEDSG---YYVSFIESLKHDDIFAYEKRFDEIVGGMDKLPTSMYQAIQEKVHLNARV 272
Cdd:COG1231  144 LAEWLRRNG-ASPSARRLLGLLGAGEYGadpDELSLLDLLRYAASAGGGAQQFRIVGGMDQLPRALAAELGDRIRLGAPV 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 273 IEIQQDVKEVTVTYQTSQketlSVTADYVIVCTTSRAARRITFEPPLPPKKAHALLSVHYRSGTKIFLTCTKKFWEDDGI 352
Cdd:COG1231  223 TRIRQDGDGVTVTTDDGG----TVRADAVIVTVPPSVLRRIEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEEDGL 298

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 353 HGGKSTTDLPSRFIYYPNHNFPNGVGVIIAYGIGDDANYFQALDFEDCGDIVINDLSLIHQLPKEEIQAicrpSMIQRWS 432
Cdd:COG1231  299 YGGISLTDLPIRQTWYPSNGPDGGAGVLLGYVGGDDARALAALSPEERVAAALEQLARIFGVYAAEPVD----YVSTDWG 374

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 817033869 433 LDNYAMGGITTFTPYHFQHFSEALTAPVDRIYFAGEYTAQA-HGWIDSTIKSGLRAATDVNRA 494
Cdd:COG1231  375 RDPWSRGAYAAAPPGQLTAAGPALAEPDGRIHFAGEHTSDEwPGWVEGALESGERAAAEILAR 437
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 54-492 9.89e-85

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: 268.59  E-value: 9.89e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869   54 MSGLSAAYVLANAGHQVTVLEASERAGGRVKTYRneKEGWYANLGPMRLPEKHRIVREYIKKFDL----RLNEFSQENEN 129
Cdd:pfam01593   1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVR--DDGFLIELGAMWFHGAQPPLLALLKELGLedrlVLPDPAPFYTV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869  130 AWYFLQNIKKRVREVNKDPGVLEYPVKPSEVgksagqlyEESLRKAVEELRRTNCSYMLNkyDTYSTKEYLLKEGNLSPG 209
Cdd:pfam01593  79 LFAGGRRYPGDFRRVPAGWEGLLEFGRLLSI--------PEKLRLGLAALASDALDEFDL--DDFSLAESLLFLGRRGPG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869  210 AVDMIGDL--------LNEDSGYYVSFIESL----KHDDIFAYEKRFDEIV---GGMDKLPTSMYQAI-QEKVHLNARVI 273
Cdd:pfam01593 149 DVEVWDRLidpelfaaLPFASGAFAGDPSELsaglALPLLWALLGEGGSLLlprGGLGALPDALAAQLlGGDVRLNTRVR 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869  274 EIQQDVKEVTVTYQTSQketlSVTADYVIVCTTSRAARRITFEPPLPPKKAHALLSVHYRSGTKIFLTCTKKFWEDDGIH 353
Cdd:pfam01593 229 SIDREGDGVTVTLTDGE----VIEADAVIVTVPLGVLKRILFTPPLPPEKARAIRNLGYGPVNKVHLEFDRKFWPDLGLL 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869  354 G--GKSTTDLPSRFIY--YPNHNFPNGVGVIIAY-GIGDDANYFQALDFEDCGDIVINDLSLIHQLPKEEIQAICRPsmi 428
Cdd:pfam01593 305 GllSELLTGLGTAFSWltFPNRAPPGKGLLLLVYvGPGDRARELEGLSDEELLQAVLRDLRKLFGEEAPEPLRVLVS--- 381

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 817033869  429 qRWSLDNYAMGGITTFTPYHFQHFSEALTAPVD-RIYFAGEYTAQAH-GWIDSTIKSGLRAATDVN 492
Cdd:pfam01593 382 -DWHTDPWPRGSYSLPQYGPGHDDYRPLARTPDpGLFFAGEHTSTGYpGTVEGAIESGRRAARAVL 446
PLN02676 PLN02676
polyamine oxidase
 46-490 2.67e-17

polyamine oxidase


Pssm-ID: 215362 [Multi-domain]  Cd Length: 487  Bit Score: 84.38  E-value: 2.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869  46 RVVIVGAGMSGLSAAYVLANAGHQ-VTVLEASERAGGRVKT-----YRNE-KEGWYANLGpmrlPEKHRIVREYIKKFDL 118
Cdd:PLN02676  28 SVIIVGAGMSGISAAKTLSEAGIEdILILEATDRIGGRMRKanfagVSVElGANWVEGVG----GPESNPIWELANKLKL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 119 R--LNEFSqeneNAWYflqNIKKRvrevnkDPGVleYPvkPSEVGKSAGQLYEESlrKAVEELRRTNCSymlNKYDTYST 196
Cdd:PLN02676 104 RtfYSDFD----NLSS---NIYKQ------DGGL--YP--KKVVQKSMKVADASD--EFGENLSISLSA---KKAVDISI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 197 KEYLLKEGNLSPGAVDMIGDLLNEDsgyyVSFIE-----SLKH-----------DDIF--AYEKRFDEIVGGMDK--LPT 256
Cdd:PLN02676 162 LTAQRLFGQVPKTPLEMVIDYYNYD----YEFAEpprvtSLKNtepnptfvdfgEDEYfvADPRGYESLVYYLAEqfLST 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 257 SMYQAIQEKVHLNARVIEIQQDVKEVTV------TYQtsqketlsvtADYVIVcTTSRAARR---ITFEPPLPPKKAHAL 327
Cdd:PLN02676 238 KSGKITDPRLKLNKVVREISYSKNGVTVktedgsVYR----------AKYVIV-SVSLGVLQsdlIKFKPPLPDWKIEAI 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 328 LSVHYRSGTKIFLTCTKKFWEDdgihgGKSTTDL---PSRFIYYP-----NHNFPnGVGVIIAygigddanyfqaldfed 399
Cdd:PLN02676 307 YQFDMAVYTKIFLKFPYKFWPS-----GPGTEFFlyaHERRGYYPfwqhlENEYP-GSNVLFV----------------- 363

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 400 cgdIVINDLS-LIHQLPKEEIQA-------------ICRPS--MIQRWSLDNYAMGGITTFTPYHFQHFSEALTAPVDRI 463
Cdd:PLN02676 364 ---TVTDEESrRIEQQPDSETKAeimevlrkmfgpnIPEATdiLVPRWWSNRFFKGSYSNWPIGVSRYEFDQIRAPVGRV 440

                        490       500
                 ....*....|....*....|....*...
gi 817033869 464 YFAGEYTAQAH-GWIDSTIKSGLRAATD 490
Cdd:PLN02676 441 YFTGEHTSEKYnGYVHGAYLAGIDTAND 468
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
 47-99 4.42e-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: 55.36  E-value: 4.42e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 817033869   47 VVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRvkTYRNEKEGWYANLGP 99
Cdd:TIGR02734   1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGR--AGVLEDDGFRFDTGP 51
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 44-85 3.91e-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: 40.95  E-value: 3.91e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 817033869    44 PKRVVIVGAGMSGLSAAYVLANAGHQVTVL--------EASERAGGRVKT 85
Cdd:smart01002  20 PAKVVVIGAGVVGLGAAATAKGLGAEVTVLdvrparlrQLESLLGARFTT 69
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 44-85 2.89e-03

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: 39.70  E-value: 2.89e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 817033869  44 PKRVVIVGAGMSGLSAAYVLANAGHQVTVLEAS--------ERAGGRVKT 85
Cdd:cd05305  168 PAKVVILGAGVVGENAARVALGLGAEVTVLDINlerlryldDIFGGRVTT 217
 
Name Accession Description Interval E-value
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
38-494 9.65e-124

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 368.48  E-value: 9.65e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869  38 LSTTSNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTYRNEKEGWYANLGPMRLPEKHRIVREYIKKFD 117
Cdd:COG1231    1 MSRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGRVWTLRFGDDGLYAELGAMRIPPSHTNLLALARELG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 118 LRLNEFSQENENAWYFLQNIKKRVREVNKDPGVLeypvkpsevgksagqlyEESLRKAVEELRR--TNCSYMLNKYDTYS 195
Cdd:COG1231   81 LPLEPFPNENGNALLYLGGKRVRAGEIAADLRGV-----------------AELLAKLLRALAAalDPWAHPAAELDRES 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 196 TKEYLLKEGnLSPGAVDMIGDLLNEDSG---YYVSFIESLKHDDIFAYEKRFDEIVGGMDKLPTSMYQAIQEKVHLNARV 272
Cdd:COG1231  144 LAEWLRRNG-ASPSARRLLGLLGAGEYGadpDELSLLDLLRYAASAGGGAQQFRIVGGMDQLPRALAAELGDRIRLGAPV 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 273 IEIQQDVKEVTVTYQTSQketlSVTADYVIVCTTSRAARRITFEPPLPPKKAHALLSVHYRSGTKIFLTCTKKFWEDDGI 352
Cdd:COG1231  223 TRIRQDGDGVTVTTDDGG----TVRADAVIVTVPPSVLRRIEFDPPLPAAKRAAIQRLPYGAAIKVFLQFDRPFWEEDGL 298

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 353 HGGKSTTDLPSRFIYYPNHNFPNGVGVIIAYGIGDDANYFQALDFEDCGDIVINDLSLIHQLPKEEIQAicrpSMIQRWS 432
Cdd:COG1231  299 YGGISLTDLPIRQTWYPSNGPDGGAGVLLGYVGGDDARALAALSPEERVAAALEQLARIFGVYAAEPVD----YVSTDWG 374

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 817033869 433 LDNYAMGGITTFTPYHFQHFSEALTAPVDRIYFAGEYTAQA-HGWIDSTIKSGLRAATDVNRA 494
Cdd:COG1231  375 RDPWSRGAYAAAPPGQLTAAGPALAEPDGRIHFAGEHTSDEwPGWVEGALESGERAAAEILAR 437
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 54-492 9.89e-85

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: 268.59  E-value: 9.89e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869   54 MSGLSAAYVLANAGHQVTVLEASERAGGRVKTYRneKEGWYANLGPMRLPEKHRIVREYIKKFDL----RLNEFSQENEN 129
Cdd:pfam01593   1 LAGLAAARELLRAGHDVTVLEARDRVGGRIRTVR--DDGFLIELGAMWFHGAQPPLLALLKELGLedrlVLPDPAPFYTV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869  130 AWYFLQNIKKRVREVNKDPGVLEYPVKPSEVgksagqlyEESLRKAVEELRRTNCSYMLNkyDTYSTKEYLLKEGNLSPG 209
Cdd:pfam01593  79 LFAGGRRYPGDFRRVPAGWEGLLEFGRLLSI--------PEKLRLGLAALASDALDEFDL--DDFSLAESLLFLGRRGPG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869  210 AVDMIGDL--------LNEDSGYYVSFIESL----KHDDIFAYEKRFDEIV---GGMDKLPTSMYQAI-QEKVHLNARVI 273
Cdd:pfam01593 149 DVEVWDRLidpelfaaLPFASGAFAGDPSELsaglALPLLWALLGEGGSLLlprGGLGALPDALAAQLlGGDVRLNTRVR 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869  274 EIQQDVKEVTVTYQTSQketlSVTADYVIVCTTSRAARRITFEPPLPPKKAHALLSVHYRSGTKIFLTCTKKFWEDDGIH 353
Cdd:pfam01593 229 SIDREGDGVTVTLTDGE----VIEADAVIVTVPLGVLKRILFTPPLPPEKARAIRNLGYGPVNKVHLEFDRKFWPDLGLL 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869  354 G--GKSTTDLPSRFIY--YPNHNFPNGVGVIIAY-GIGDDANYFQALDFEDCGDIVINDLSLIHQLPKEEIQAICRPsmi 428
Cdd:pfam01593 305 GllSELLTGLGTAFSWltFPNRAPPGKGLLLLVYvGPGDRARELEGLSDEELLQAVLRDLRKLFGEEAPEPLRVLVS--- 381

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 817033869  429 qRWSLDNYAMGGITTFTPYHFQHFSEALTAPVD-RIYFAGEYTAQAH-GWIDSTIKSGLRAATDVN 492
Cdd:pfam01593 382 -DWHTDPWPRGSYSLPQYGPGHDDYRPLARTPDpGLFFAGEHTSTGYpGTVEGAIESGRRAARAVL 446
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 44-491 6.24e-23

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: 101.06  E-value: 6.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869  44 PKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTYRneKEGWYANLGPMRLPEKHRIVREYIKKFDLRlNEF 123
Cdd:COG1232    1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIRTVE--VDGFRIDRGPHSFLTRDPEVLELLRELGLG-DEL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 124 -SQENENAWYFLQNikkRVREVNKDPG----------------VLEY--PVKPSEVGKSAGQLYEESL-RKAVEELRRTn 183
Cdd:COG1232   78 vWPNTRKSYIYYGG---KLHPLPQGPLallrspllslagklraLLELlaPRRPPGEDESLAEFVRRRFgREVYERLVEP- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 184 csYMLNKY----DTYST-------KEYLLKEGNLSPGAVDMIGDllNEDSGyyvsfieslkhddIFAYekrfdeIVGGMD 252
Cdd:COG1232  154 --LLEGVYagdpDELSAdwafprlKRLELEHGSLIKGALALRKG--AKAGE-------------VFGY------LRGGLG 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 253 KLPTSMYQAIQE-KVHLNARVIEIQQDVKEVTVTyqTSQKETlsVTADYVIVCTTSRAARRITfePPLPPKKAHALLSVH 331
Cdd:COG1232  211 TLVEALAEALEAgEIRLGTRVTAIEREGGGWRVT--TSDGET--IEADAVVSATPAPALARLL--APLPPEVAAALAGIP 284

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 332 YRSgtkiFLTCT-----KKFWEDDG----IHggkSTTDLP-SRFIYYPN---HNFPNGVGVIIAY--GIGDDANYfqALD 396
Cdd:COG1232  285 YAS----VAVVAlgfdrPDLPPPDGfgwlVP---RDEGVPiLAVTFSSNkwpHRAPDGKVLLRLEvgGAGDPELW--QLS 355

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 397 FEDCGDIVINDLSLIHQLPKEEIQAIcrpsmIQRWSldnyamGGITTFTPYHFQHFSEALT--APVDRIYFAGeytAQAH 474
Cdd:COG1232  356 DEELVALALADLRKLLGIDAEPVDTR-----VVRWP------KAYPQYTVGHLERVAAIREalAALPGLYLAG---RAYD 421

                        490
                 ....*....|....*...
gi 817033869 475 G-WIDSTIKSGLRAATDV 491
Cdd:COG1232  422 GvGLPDCIRSGREAAERI 439
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 45-346 2.11e-17

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 84.52  E-value: 2.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869  45 KRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTYrnEKEGWYANLGP------------------------M 100
Cdd:COG1233    4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRARTF--ERPGFRFDVGPsvltmpgvlerlfrelgledylelV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 101 RLPEKHRIVREYIKKFDL---------RLNEFSQENENAWY-FLQNIKKRVREVNKDpgVLEYPVKP------SEVGKSA 164
Cdd:COG1233   82 PLDPAYRVPFPDGRALDLprdlertaaELERLFPGDAEAYRrFLAELRRLYDALLED--LLYRPLLSlrdllrPLALARL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 165 GQLYEESLRKAV------EELRRtncsyMLNKYDTYStkeyllkeG---NLSPGAVDMIGDLLNEDSGYYVsfieslkhd 235
Cdd:COG1233  160 LRLLLRSLRDLLrryfkdPRLRA-----LLAGQALYL--------GlspDRTPALYALIAYLEYAGGVWYP--------- 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 236 difayekrfdeiVGGMDKLPTSMYQAIQE---KVHLNARVIEIQQDVKEVT-VTYQTSQKetlsVTADYVIVCTTSRAA- 310
Cdd:COG1233  218 ------------KGGMGALADALARLAEElggEIRTGAEVERILVEGGRATgVRLADGEE----IRADAVVSNADPAHTy 281

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 817033869 311 RRITFEPPLPPKKAHALLSVHYRSGT-KIFLTCTKKF 346
Cdd:COG1233  282 LRLLGEEALPARYRRRLERFRYSPSAfKLYLGLDGPL 318
PLN02676 PLN02676
polyamine oxidase
 46-490 2.67e-17

polyamine oxidase


Pssm-ID: 215362 [Multi-domain]  Cd Length: 487  Bit Score: 84.38  E-value: 2.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869  46 RVVIVGAGMSGLSAAYVLANAGHQ-VTVLEASERAGGRVKT-----YRNE-KEGWYANLGpmrlPEKHRIVREYIKKFDL 118
Cdd:PLN02676  28 SVIIVGAGMSGISAAKTLSEAGIEdILILEATDRIGGRMRKanfagVSVElGANWVEGVG----GPESNPIWELANKLKL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 119 R--LNEFSqeneNAWYflqNIKKRvrevnkDPGVleYPvkPSEVGKSAGQLYEESlrKAVEELRRTNCSymlNKYDTYST 196
Cdd:PLN02676 104 RtfYSDFD----NLSS---NIYKQ------DGGL--YP--KKVVQKSMKVADASD--EFGENLSISLSA---KKAVDISI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 197 KEYLLKEGNLSPGAVDMIGDLLNEDsgyyVSFIE-----SLKH-----------DDIF--AYEKRFDEIVGGMDK--LPT 256
Cdd:PLN02676 162 LTAQRLFGQVPKTPLEMVIDYYNYD----YEFAEpprvtSLKNtepnptfvdfgEDEYfvADPRGYESLVYYLAEqfLST 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 257 SMYQAIQEKVHLNARVIEIQQDVKEVTV------TYQtsqketlsvtADYVIVcTTSRAARR---ITFEPPLPPKKAHAL 327
Cdd:PLN02676 238 KSGKITDPRLKLNKVVREISYSKNGVTVktedgsVYR----------AKYVIV-SVSLGVLQsdlIKFKPPLPDWKIEAI 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 328 LSVHYRSGTKIFLTCTKKFWEDdgihgGKSTTDL---PSRFIYYP-----NHNFPnGVGVIIAygigddanyfqaldfed 399
Cdd:PLN02676 307 YQFDMAVYTKIFLKFPYKFWPS-----GPGTEFFlyaHERRGYYPfwqhlENEYP-GSNVLFV----------------- 363

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 400 cgdIVINDLS-LIHQLPKEEIQA-------------ICRPS--MIQRWSLDNYAMGGITTFTPYHFQHFSEALTAPVDRI 463
Cdd:PLN02676 364 ---TVTDEESrRIEQQPDSETKAeimevlrkmfgpnIPEATdiLVPRWWSNRFFKGSYSNWPIGVSRYEFDQIRAPVGRV 440

                        490       500
                 ....*....|....*....|....*...
gi 817033869 464 YFAGEYTAQAH-GWIDSTIKSGLRAATD 490
Cdd:PLN02676 441 YFTGEHTSEKYnGYVHGAYLAGIDTAND 468
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 44-92 5.55e-16

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: 79.90  E-value: 5.55e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 817033869  44 PKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTYRNEKEG 92
Cdd:COG3349    3 PPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGGRARSFPDPDTG 51
PLN02268 PLN02268
probable polyamine oxidase
 47-493 8.38e-16

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 79.35  E-value: 8.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869  47 VVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTyrNEKEGWYANLGPMRLpekHRIVRE-----YIKKFDLRLN 121
Cdd:PLN02268   3 VIVIGGGIAGIAAARALHDASFKVTLLESRDRIGGRVHT--DYSFGFPVDMGASWL---HGVCNEnplapLIGRLGLPLY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 122 EFSQENenawyflqnikkrvrEVNKDPGVLEYPV-------KPSEVGKSAGQLYEESLrKAVEELRRTNCSYMlNKYDTY 194
Cdd:PLN02268  78 RTSGDN---------------SVLYDHDLESYALfdmdgnqVPQELVTKVGETFERIL-EETEKVRDEHEEDM-SLLQAI 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 195 ST----KEYLLKEGnlspgavdmigdLLNEDSGYYVSFIE----------SLKHDDifayEKRFDE-----IVGGMDKLP 255
Cdd:PLN02268 141 SIvlerHPELRLEG------------LAHEVLQWYLCRMEgwfaadadtiSLKSWD----QEELLEgghglMVRGYDPVI 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 256 TSMYQAIQekVHLNARVIEIQQDVKEVTVTYQTSQketlSVTADYVIVCTT--SRAARRITFEPPLPPKKAHALLSVHYR 333
Cdd:PLN02268 205 NTLAKGLD--IRLNHRVTKIVRRYNGVKVTVEDGT----TFVADAAIIAVPlgVLKANIIKFEPELPEWKEEAISDLGVG 278

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 334 SGTKIFLTCTKKFWEDDGIHGGKSTTdlPSRFIYYPNHNFPNGVGVIIAYGIGDDANYFQALDFEDCGDIVINDLSLIhq 413
Cdd:PLN02268 279 IENKIALHFDSVFWPNVEFLGVVAPT--SYGCSYFLNLHKATGHPVLVYMPAGRLARDIEKLSDEAAANFAMSQLKKM-- 354

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 414 LPK--EEIQaicrpSMIQRWSLDNYAMGGItTFTPYHFQH-FSEALTAPVDRIYFAGEYTAQAH-GWIDSTIKSGLRAAT 489
Cdd:PLN02268 355 LPDatEPVQ-----YLVSRWGSDPNSLGCY-SYDLVGKPHdLYERLRAPVDNLFFAGEATSSDFpGSVHGAYSTGVMAAE 428


                 ....
gi 817033869 490 DVNR 493
Cdd:PLN02268 429 ECRM 432
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
44-98 5.36e-14

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


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 72.99  E-value: 5.36e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 817033869  44 PKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTYRNekEGWYANLG 98
Cdd:COG3380    3 MPDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGGRMATRRL--DGGRFDHG 55
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
49-116 4.66e-13

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 64.09  E-value: 4.66e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869   49 IVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTYRNekEGWYANLGP--MRLPEKHRiVREYIKKF 116
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYSYRV--PGYVFDYGAhiFHGSDEPN-VRDLLDEL 67
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
 45-99 5.51e-12

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 67.57  E-value: 5.51e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 817033869  45 KRVVIVGAGMSGLSAAYVL--ANAGHQVTVLEASERAGGRVKTYRneKEGWYANLGP 99
Cdd:PRK11883   1 KKVAIIGGGITGLSAAYRLhkKGPDADITLLEASDRLGGKIQTVR--KDGFPIELGP 55
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 42-81 6.33e-12

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: 67.47  E-value: 6.33e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 817033869  42 SNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGG 81
Cdd:COG0493  119 RTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG 158
PLN03000 PLN03000
amine oxidase
 35-498 2.10e-11

amine oxidase


Pssm-ID: 178578 [Multi-domain]  Cd Length: 881  Bit Score: 66.58  E-value: 2.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869  35 KNGLSTTSNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTYRNE--KEGWYANLGPMRLPEKHRivrey 112
Cdd:PLN03000 175 KDKFPAQSSKSSVVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGGRVYTKKMEanRVGAAADLGGSVLTGTLG----- 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 113 ikkfdlrlNEFSQENENAWYFLQNIKK-----RVREVNKDPGV-LEYPVKPSEVGKSAGQL--------YEESLRKAVEE 178
Cdd:PLN03000 250 --------NPLGIIARQLGSSLYKVRDkcplyRVDGKPVDPDVdLKVEVAFNQLLDKASKLrqlmgdvsMDVSLGAALET 321

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 179 LRRTNCsymlnkyDTYSTKEYLLKE---GNLSPGAVDMIGDL----LNEDSGYyvsfieSLKHDDIFayekrfdeIVGGM 251
Cdd:PLN03000 322 FRQVSG-------NDVATEEMGLFNwhlANLEYANAGLVSKLslafWDQDDPY------DMGGDHCF--------LPGGN 380

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 252 DKLptsmYQAIQEKVHL----NARVIEIQQDVKEVTVTYQTSQKEtlsvtadyVIVCTTSRAARR---ITFEPPLPPKKA 324
Cdd:PLN03000 381 GRL----VQALAENVPIlyekTVQTIRYGSNGVKVIAGNQVYEGD--------MVLCTVPLGVLKngsIKFVPELPQRKL 448

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 325 HALLSVHYRSGTKIFLTCTKKFWEDDGIHGGKSTTDlPSR----FIYYPNHNFPNGvGVIIAYGIGDDANYFQALDFEDC 400
Cdd:PLN03000 449 DCIKRLGFGLLNKVAMLFPYVFWSTDLDTFGHLTED-PNYrgefFLFYSYAPVAGG-PLLIALVAGEAAHKFETMPPTDA 526

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 401 GDIVINDLSLIHqlpkeEIQAICRPSMIQ----RWSLDNYAMGGITTFTPYHFQHFSEALTAPV--DRIYFAGE-----Y 469
Cdd:PLN03000 527 VTRVLHILRGIY-----EPQGINVPDPLQtvctRWGGDPFSLGSYSNVAVGASGDDYDILAESVgdGRLFFAGEattrrY 601

                        490       500
                 ....*....|....*....|....*....
gi 817033869 470 TAQAHGwidsTIKSGLRAATDVNRASENK 498
Cdd:PLN03000 602 PATMHG----AFVTGLREAANMAQSAKAR 626
PLN02328 PLN02328
lysine-specific histone demethylase 1 homolog
 34-498 2.58e-11

lysine-specific histone demethylase 1 homolog


Pssm-ID: 215187 [Multi-domain]  Cd Length: 808  Bit Score: 66.17  E-value: 2.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869  34 AKNGLSTTSNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTYRNEKEG--WYANLG------------- 98
Cdd:PLN02328 228 AQLRSFEGVEPANVVVVGAGLAGLVAARQLLSMGFKVVVLEGRARPGGRVKTMKMKGDGvvAAADLGgsvltgingnplg 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869  99 -----------------PMRLPEKHRIVREYIKKFDLRLNEFSqenENAWYFLQNIKKRVREVNKDPG-VLEYPVKPSEV 160
Cdd:PLN02328 308 vlarqlglplhkvrdicPLYLPDGKAVDAEIDSKIEASFNKLL---DRVCKLRQAMIEEVKSVDVNLGtALEAFRHVYKV 384

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 161 GKSAGQLYeeSLRKAVEELRRTNCSYMLNKYDTYSTKEYLLKEGN---LSPGAVDmigdllnedsgyyvSFIESLKHDDI 237
Cdd:PLN02328 385 AEDPQERM--LLNWHLANLEYANASLMSNLSMAYWDQDDPYEMGGdhcFIPGGND--------------TFVRELAKDLP 448

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 238 FAYEKRFDEIVGGMDKLptSMYQAIQekvhlnarviEIQQDVKEVTVTYQTSQKETlsvtadyvivcttsraarrITFEP 317
Cdd:PLN02328 449 IFYERTVESIRYGVDGV--IVYAGGQ----------EFHGDMVLCTVPLGVLKKGS-------------------IEFYP 497

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 318 PLPPKKAHALLSVHYRSGTKIFLTCTKKFWEDDGIHGGKSTTDLPSR---FIYYpNHNFPNGVGVIIAYGIGDDANYFQA 394
Cdd:PLN02328 498 ELPQRKKDAIQRLGYGLLNKVALLFPYNFWGGEIDTFGHLTEDPSMRgefFLFY-SYSSVSGGPLLIALVAGDAAVKFET 576

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 395 LDFEDCGDIVINDLSLIHQlPK-----EEIQAICrpsmiQRWSLDNYAMGGITTFTPYHFQHFSEALTAPV--DRIYFAG 467
Cdd:PLN02328 577 LSPVESVKRVLQILRGIFH-PKgivvpDPVQAVC-----TRWGKDCFTYGSYSYVAVGSSGDDYDILAESVgdGRVFFAG 650

                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 817033869 468 E-----YTAQAHGwidsTIKSGLRAATDVNRASENK 498
Cdd:PLN02328 651 EatnkqYPATMHG----AFLSGMREAANILRVARRR 682
PRK07233 PRK07233
hypothetical protein; Provisional
 46-87 4.31e-11

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 64.91  E-value: 4.31e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 817033869  46 RVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTYR 87
Cdd:PRK07233   1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAASFE 42
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 22-86 4.82e-11

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 64.82  E-value: 4.82e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 817033869  22 FRETDYEEFLEIAKNGlsttsnpKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGrVKTY 86
Cdd:PRK11749 125 AMETGWVLFKRAPKTG-------KKVAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGG-LLRY 181
PLN02529 PLN02529
lysine-specific histone demethylase 1
 43-495 5.14e-11

lysine-specific histone demethylase 1


Pssm-ID: 178144 [Multi-domain]  Cd Length: 738  Bit Score: 65.30  E-value: 5.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869  43 NPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTYRNEKEGWYA--NLGPMRLPEKHR-----IVREY-IK 114
Cdd:PLN02529 159 TEGSVIIVGAGLAGLAAARQLLSFGFKVVVLEGRNRPGGRVYTQKMGRKGQFAavDLGGSVITGIHAnplgvLARQLsIP 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 115 KFDLRLNEFSQENENAwyflqnIKKRVREVNKDPGVLEYPVKPSEVGKSAGQLYEE-SLRKAVEELRRTncsYMLNKydt 193
Cdd:PLN02529 239 LHKVRDNCPLYKPDGA------LVDKEIDSNIEFIFNKLLDKVTELRQIMGGFANDiSLGSVLERLRQL---YGVAR--- 306

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 194 ySTKEYLLKEGNLSPGAVDMIGDLLNEDSGYYvsfieslKHDDifAYEKRFDE--IVGGMDKLPTSMYQAIQEKVHLNAR 271
Cdd:PLN02529 307 -STEERQLLDWHLANLEYANAGCLSDLSAAYW-------DQDD--PYEMGGDHcfLAGGNWRLINALCEGVPIFYGKTVD 376

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 272 VIEIQQDVKEVTVTYQTSQketlsvtADyVIVCTTSRAA---RRITFEPPLPPKKAHALLSVHYRSGTKIFLTCTKKFWE 348
Cdd:PLN02529 377 TIKYGNDGVEVIAGSQVFQ-------AD-MVLCTVPLGVlkkRTIRFEPELPRRKLAAIDRLGFGLLNKVAMVFPSVFWG 448

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 349 DDGIHGG---KSTTDLPSRFIYYPNHNFPNGvGVIIAYGIGDDANYFQALDFEDCGDIVINDLSLIHQlPK-----EEIQ 420
Cdd:PLN02529 449 EELDTFGclnESSNKRGEFFLFYGYHTVSGG-PALVALVAGEAAQRFENTDPSTLLHRVLSVLRGIYN-PKginvpDPIQ 526

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869 421 AICrpsmiQRWSLDNYAMGGITTFTPYHFQHFSEALTAPV-DRIYFAGE-----YTAQAHGwidsTIKSGLRAATDVNRA 494
Cdd:PLN02529 527 TIC-----TRWGSDPLSYGSYSHVRVQSSGSDYDILAESVsGRLFFAGEattrqYPATMHG----AFLSGLREASRILHV 597


                 .
gi 817033869 495 S 495
Cdd:PLN02529 598 A 598
PLN02612 PLN02612
phytoene desaturase
 28-94 4.23e-10

phytoene desaturase


Pssm-ID: 215330 [Multi-domain]  Cd Length: 567  Bit Score: 62.17  E-value: 4.23e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 817033869  28 EEFLEIAKngLSTT-------SNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTYRNEKEGWY 94
Cdd:PLN02612  72 VNFLEAAA--LSASfrsaprpAKPLKVVIAGAGLAGLSTAKYLADAGHKPILLEARDVLGGKVAAWKDEDGDWY 143
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 45-81 4.25e-10

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 61.81  E-value: 4.25e-10
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 817033869  45 KRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGG 81
Cdd:PRK12771 138 KRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGG 174
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 45-81 5.24e-10

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 61.33  E-value: 5.24e-10
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 817033869  45 KRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGG 81
Cdd:PRK12810 144 KKVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGG 180
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 39-119 8.22e-10

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: 60.65  E-value: 8.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869  39 STTSNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRvktyrnekegWYANL-------GPMRL--------- 102
Cdd:COG2072    1 TAATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGT----------WRDNRypglrldTPSHLyslpffpnw 70

                         90       100
                 ....*....|....*....|....*.
gi 817033869 103 ------PEKHRIV---REYIKKFDLR 119
Cdd:COG2072   71 sddpdfPTGDEILaylEAYADKFGLR 96
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 46-126 9.03e-10

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: 60.10  E-value: 9.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869   46 RVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVkTYRNEKeGWYANLGPMRLPEKHRIVREYIKKFDLRLNEFSQ 125
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGSGA-SGRNAG-LIHPGLRYLEPSELARLALEALDLWEELEEELGI 78


                  .
gi 817033869  126 E 126
Cdd:pfam01266  79 D 79
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
46-81 1.38e-09

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 59.92  E-value: 1.38e-09
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 817033869  46 RVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGG 81
Cdd:COG0665    4 DVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGSG 39
PLN02576 PLN02576
protoporphyrinogen oxidase
 34-89 1.54e-09

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 60.03  E-value: 1.54e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 817033869  34 AKNGLSTTSNPKRVVIVGAGMSGLSAAYVLA-NAGHQVTVLEASERAGGRVKTYRNE 89
Cdd:PLN02576   2 AIAEGSAAASSKDVAVVGAGVSGLAAAYALAsKHGVNVLVTEARDRVGGNITSVSED 58
PRK07208 PRK07208
hypothetical protein; Provisional
 42-101 1.70e-09

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 59.90  E-value: 1.70e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869  42 SNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTYRNekEGWYANLGPMR 101
Cdd:PRK07208   2 TNKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGISRTVTY--KGNRFDIGGHR 59
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 46-83 2.17e-09

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: 58.80  E-value: 2.17e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 817033869  46 RVVIVGAGMSGLSAAYVLANAGHQVTVLEAS--ERAGGRV 83
Cdd:COG0654    5 DVLIVGGGPAGLALALALARAGIRVTVVERAppPRPDGRG 44
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
44-81 3.05e-09

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


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 58.97  E-value: 3.05e-09
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 817033869  44 PKRVVIVGAGMSGLSAAYVLANAgHQVTVLEASERAGG 81
Cdd:COG2907    3 RMRIAVIGSGISGLTAAWLLSRR-HDVTLFEANDRLGG 39
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 45-81 3.51e-09

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 59.36  E-value: 3.51e-09
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 817033869  45 KRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGG 81
Cdd:PRK12814 194 KKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGG 230
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
26-83 1.55e-08

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 56.69  E-value: 1.55e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 817033869  26 DYEEFLEIAKNGlsttsnpKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRV 83
Cdd:COG1251  131 DADALRAALAPG-------KRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQ 181
PLN02976 PLN02976
amine oxidase
 35-87 3.54e-08

amine oxidase


Pssm-ID: 215527 [Multi-domain]  Cd Length: 1713  Bit Score: 56.41  E-value: 3.54e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 817033869   35 KNGLSTTSNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTYR 87
Cdd:PLN02976  684 HCVLCDSVDRKKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGGRVYTDR 736
PLN02568 PLN02568
polyamine oxidase
 46-85 4.03e-08

polyamine oxidase


Pssm-ID: 215308 [Multi-domain]  Cd Length: 539  Bit Score: 55.61  E-value: 4.03e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 817033869  46 RVVIVGAGMSGLSAAYVLANAGH-----QVTVLEASERAGGRVKT 85
Cdd:PLN02568   7 RIVIIGAGMAGLTAANKLYTSSAandmfELTVVEGGDRIGGRINT 51
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
 47-99 4.42e-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: 55.36  E-value: 4.42e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 817033869   47 VVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRvkTYRNEKEGWYANLGP 99
Cdd:TIGR02734   1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGGR--AGVLEDDGFRFDTGP 51
PRK13984 PRK13984
putative oxidoreductase; Provisional
 14-81 1.45e-07

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 54.00  E-value: 1.45e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 817033869  14 DRNPLEEcfretdYEEFLE---IAKNglsttsnpKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGG 81
Cdd:PRK13984 264 DNVPVEK------YSEILDdepEKKN--------KKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGG 320
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
 45-181 6.21e-07

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: 51.76  E-value: 6.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869   45 KRVVIVGAGMSGLSAAYVLA----NAGHQVTVLEASERAGGRVKTyrNEKEGWYANLGPMRLPEKHRIVREYIKkfDLRL 120
Cdd:TIGR00562   3 KHVVIIGGGISGLCAAYYLEkeipELPVELTLVEASDRVGGKIQT--VKEDGYLIERGPDSFLERKKSAPDLVK--DLGL 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 817033869  121 NEFSQENENAWYFLQNIKKRVREVnkdpgvleyPVKPSEVGKSAGQLYEESLRKAVEELRR 181
Cdd:TIGR00562  79 EHVLVSDATGQRYVLVNRGKLMPV---------PTKIAPFVKTGLFSLGGKLRAGMDFIRP 130
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 36-78 1.21e-06

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 50.39  E-value: 1.21e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 817033869   36 NGLSTTSNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASER 78
Cdd:pfam07992 144 EALRLKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDR 186
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 46-78 2.34e-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: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 45.27  E-value: 2.34e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 817033869   46 RVVIVGAGMSGLSAAYVLANAGHQVTVLEASER 78
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDR 33
PRK00711 PRK00711
D-amino acid dehydrogenase;
46-74 2.46e-06

D-amino acid dehydrogenase;


Pssm-ID: 234819 [Multi-domain]  Cd Length: 416  Bit Score: 49.80  E-value: 2.46e-06
                         10        20
                 ....*....|....*....|....*....
gi 817033869  46 RVVIVGAGMSGLSAAYVLANAGHQVTVLE 74
Cdd:PRK00711   2 RVVVLGSGVIGVTSAWYLAQAGHEVTVID 30
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
45-87 2.60e-06

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 49.86  E-value: 2.60e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 817033869  45 KRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTYR 87
Cdd:COG1148  141 KRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRAAQLH 183
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 47-81 2.65e-06

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: 49.59  E-value: 2.65e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 817033869   47 VVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGG 81
Cdd:pfam00890   2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGG 36
FadB COG1250
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ...
 45-86 5.84e-06

3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440862 [Multi-domain]  Cd Length: 281  Bit Score: 47.80  E-value: 5.84e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 817033869  45 KRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTY 86
Cdd:COG1250    3 KKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARAR 44
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
 42-81 6.69e-06

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 48.06  E-value: 6.69e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 817033869  42 SNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGG 81
Cdd:PRK12770  16 PTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGG 55
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
52-83 1.24e-05

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 46.88  E-value: 1.24e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 817033869  52 AGMSGLSAAYVLANAGHQVTVLEASERAGGRV 83
Cdd:COG0644    1 AGPAGSAAARRLARAGLSVLLLEKGSFPGDKI 32
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 47-81 1.61e-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: 47.14  E-value: 1.61e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 817033869  47 VVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGG 81
Cdd:COG1053    6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
PRK12831 PRK12831
putative oxidoreductase; Provisional
 41-115 2.25e-05

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 46.93  E-value: 2.25e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 817033869  41 TSNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGrVKTYrnekegwyaNLGPMRLPeKHRIVR---EYIKK 115
Cdd:PRK12831 137 EKKGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGG-VLVY---------GIPEFRLP-KETVVKkeiENIKK 203
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 47-85 2.32e-05

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: 46.16  E-value: 2.32e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 817033869   47 VVIVGAGMSGLSAAYVLANAGHQVTVLEasERAGGRVKT 85
Cdd:TIGR02032   3 VVVVGAGPAGASAAYRLADKGLRVLLLE--KKSFPRYKP 39
Thi4 pfam01946
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
 47-81 2.51e-05

Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.


Pssm-ID: 460393  Cd Length: 232  Bit Score: 45.54  E-value: 2.51e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 817033869   47 VVIVGAGMSGLSAAYVLA-NAGHQVTVLEASERAGG 81
Cdd:pfam01946  20 VVIVGAGSSGLTAAYYLAkNRGLKVAIIERSVSPGG 55
PTZ00306 PTZ00306
NADH-dependent fumarate reductase; Provisional
 42-81 2.65e-05

NADH-dependent fumarate reductase; Provisional


Pssm-ID: 140327 [Multi-domain]  Cd Length: 1167  Bit Score: 47.08  E-value: 2.65e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 817033869   42 SNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGG 81
Cdd:PTZ00306  407 SLPARVIVVGGGLAGCSAAIEAASCGAQVILLEKEAKLGG 446
PRK06847 PRK06847
hypothetical protein; Provisional
 41-75 5.48e-05

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 45.25  E-value: 5.48e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 817033869  41 TSNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEA 75
Cdd:PRK06847   1 MAAVKKVLIVGGGIGGLSAAIALRRAGIAVDLVEI 35
PLN02487 PLN02487
zeta-carotene desaturase
 44-98 5.97e-05

zeta-carotene desaturase


Pssm-ID: 215268 [Multi-domain]  Cd Length: 569  Bit Score: 45.56  E-value: 5.97e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 817033869  44 PK-RVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTYRnEKEGWYANLG 98
Cdd:PLN02487  74 PKlKVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGGKVGSFV-DKNGNHIEMG 128
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 26-86 6.67e-05

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 45.50  E-value: 6.67e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 817033869  26 DYEEflEIAKNGLSTT--SNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGrVKTY 86
Cdd:PRK12778 413 DYER--ESGNISVPEVaeKNGKKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGG-VLKY 472
PRK12409 PRK12409
D-amino acid dehydrogenase small subunit; Provisional
 45-74 8.24e-05

D-amino acid dehydrogenase small subunit; Provisional


Pssm-ID: 237093 [Multi-domain]  Cd Length: 410  Bit Score: 45.01  E-value: 8.24e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 817033869  45 KRVVIVGAGMSGLSAAYVLANAGHQVTVLE 74
Cdd:PRK12409   2 SHIAVIGAGITGVTTAYALAQRGYQVTVFD 31
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 43-83 9.56e-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: 44.42  E-value: 9.56e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 817033869  43 NPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRV 83
Cdd:COG0446  123 KGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLLGVL 163
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
47-85 1.19e-04

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 43.96  E-value: 1.19e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 817033869  47 VVIVGAGMSGLSAAYVLANAGHQVTVLEASErAGGRVKT 85
Cdd:COG0492    3 VVIIGAGPAGLTAAIYAARAGLKTLVIEGGE-PGGQLAT 40
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 45-75 1.87e-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: 1.87e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 817033869   45 KRVVIVGAGMSGLSAAYVLANAGHQVTVLEA 75
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIED 31
3HCDH_N pfam02737
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ...
 46-79 1.96e-04

3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.


Pssm-ID: 397037 [Multi-domain]  Cd Length: 180  Bit Score: 42.14  E-value: 1.96e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 817033869   46 RVVIVGAGMSGLSAAYVLANAGHQVTVLEASERA 79
Cdd:pfam02737   1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEA 34
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
 45-79 2.13e-04

UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440534 [Multi-domain]  Cd Length: 445  Bit Score: 43.53  E-value: 2.13e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 817033869  45 KRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERA 79
Cdd:COG0771    5 KKVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPAP 39
PRK07588 PRK07588
FAD-binding domain;
45-83 2.31e-04

FAD-binding domain;


Pssm-ID: 169028 [Multi-domain]  Cd Length: 391  Bit Score: 43.57  E-value: 2.31e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 817033869  45 KRVVIVGAGMSGLSAAYVLANAGHQVTVLE-ASE-RAGGRV 83
Cdd:PRK07588   1 MKVAISGAGIAGPTLAYWLRRYGHEPTLIErAPElRTGGYM 41
PRK12779 PRK12779
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ...
 47-84 2.74e-04

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


Pssm-ID: 183740 [Multi-domain]  Cd Length: 944  Bit Score: 43.67  E-value: 2.74e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 817033869  47 VVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVK 84
Cdd:PRK12779 309 IAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVLR 346
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 44-78 3.27e-04

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


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 43.15  E-value: 3.27e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 817033869  44 PKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASER 78
Cdd:COG1249  168 PKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDR 202
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 44-85 3.91e-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: 40.95  E-value: 3.91e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 817033869    44 PKRVVIVGAGMSGLSAAYVLANAGHQVTVL--------EASERAGGRVKT 85
Cdd:smart01002  20 PAKVVVIGAGVVGLGAAATAKGLGAEVTVLdvrparlrQLESLLGARFTT 69
PRK12834 PRK12834
putative FAD-binding dehydrogenase; Reviewed
 47-81 4.28e-04

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 183782 [Multi-domain]  Cd Length: 549  Bit Score: 42.96  E-value: 4.28e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 817033869  47 VVIVGAGMSGLSAAYVLANAGHQVTVLEASERA--GG 81
Cdd:PRK12834   7 VIVVGAGLAGLVAAAELADAGKRVLLLDQENEAnlGG 43
PRK07538 PRK07538
hypothetical protein; Provisional
 46-78 5.14e-04

hypothetical protein; Provisional


Pssm-ID: 236046 [Multi-domain]  Cd Length: 413  Bit Score: 42.58  E-value: 5.14e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 817033869  46 RVVIVGAGMSGLSAAYVLANAGHQVTVLEASER 78
Cdd:PRK07538   2 KVLIAGGGIGGLTLALTLHQRGIEVVVFEAAPE 34
PRK08163 PRK08163
3-hydroxybenzoate 6-monooxygenase;
42-80 5.66e-04

3-hydroxybenzoate 6-monooxygenase;


Pssm-ID: 181262 [Multi-domain]  Cd Length: 396  Bit Score: 42.33  E-value: 5.66e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 817033869  42 SNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAG 80
Cdd:PRK08163   2 TKVTPVLIVGGGIGGLAAALALARQGIKVKLLEQAAEIG 40
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
44-78 6.23e-04

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 42.04  E-value: 6.23e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 817033869  44 PKRVVIVGAGMSGLSAAYVLAN---AGHQVTVLEASER 78
Cdd:COG1252    1 MKRIVIVGGGFAGLEAARRLRKklgGDAEVTLIDPNPY 38
PRK06185 PRK06185
FAD-dependent oxidoreductase;
46-76 7.29e-04

FAD-dependent oxidoreductase;


Pssm-ID: 235729 [Multi-domain]  Cd Length: 407  Bit Score: 41.77  E-value: 7.29e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 817033869  46 RVVIVGAGMSGLSAAYVLANAGHQVTVLEAS 76
Cdd:PRK06185   8 DCCIVGGGPAGMMLGLLLARAGVDVTVLEKH 38
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 39-80 7.35e-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: 42.14  E-value: 7.35e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 817033869  39 STTSNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAG 80
Cdd:PRK01747 255 PGSPKARDAAIIGGGIAGAALALALARRGWQVTLYEADEAPA 296
PRK07236 PRK07236
hypothetical protein; Provisional
 40-83 7.57e-04

hypothetical protein; Provisional


Pssm-ID: 235980 [Multi-domain]  Cd Length: 386  Bit Score: 41.83  E-value: 7.57e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 817033869  40 TTSNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASE-----RAGGRV 83
Cdd:PRK07236   2 THMSGPRAVVIGGSLGGLFAALLLRRAGWDVDVFERSPteldgRGAGIV 50
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
47-74 8.62e-04

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


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 41.82  E-value: 8.62e-04
                         10        20
                 ....*....|....*....|....*...
gi 817033869  47 VVIVGAGMSGLSAAYVLANAGHQVTVLE 74
Cdd:PRK06183  13 VVIVGAGPVGLTLANLLGQYGVRVLVLE 40
PRK06753 PRK06753
hypothetical protein; Provisional
 46-123 9.62e-04

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 41.60  E-value: 9.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869  46 RVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAggrvktyrnEKEGWYANLGP--MRLPEKHRIVREyIKKFDLRLNEF 123
Cdd:PRK06753   2 KIAIIGAGIGGLTAAALLQEQGHEVKVFEKNESV---------KEVGAGIGIGDnvIKKLGNHDLAKG-IKNAGQILSTM 71
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 44-81 1.04e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 41.32  E-value: 1.04e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 817033869  44 PKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGG 81
Cdd:PRK06292 169 PKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILP 206
Ubi-OHases TIGR01988
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ...
 47-75 1.12e-03

Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a family of FAD-dependent hydroxylases (monooxygenases) which are all believed to act in the aerobic ubiquinone biosynthesis pathway. A separate set of hydroxylases, as yet undiscovered, are believed to be active under anaerobic conditions. In E. coli three enzyme activities have been described, UbiB (which acts first at position 6, see TIGR01982), UbiH (which acts at position 4) and UbiF (which acts at position 5). UbiH and UbiF are similar to one another and form the basis of this subfamily. Interestingly, E. coli contains another hydroxylase gene, called visC, that is highly similar to UbiF, adjacent to UbiH and, when mutated, results in a phenotype similar to that of UbiH (which has also been named visB). Several other species appear to have three homologs in this family, although they assort themselves differently on phylogenetic trees (e.g. Xylella and Mesorhizobium) making it difficult to ascribe a specific activity to each one. Eukaryotes appear to have only a single homolog in this subfamily (COQ6) which complements UbiH, but also possess a non-orthologous gene, COQ7 which complements UbiF. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273913 [Multi-domain]  Cd Length: 385  Bit Score: 41.42  E-value: 1.12e-03
                          10        20
                  ....*....|....*....|....*....
gi 817033869   47 VVIVGAGMSGLSAAYVLANAGHQVTVLEA 75
Cdd:TIGR01988   2 IVIVGGGMVGLALALALARSGLKVALIEA 30
YdhS COG4529
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
41-80 1.15e-03

Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];


Pssm-ID: 443597 [Multi-domain]  Cd Length: 466  Bit Score: 41.48  E-value: 1.15e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 817033869  41 TSNPKRVVIVGAGMSGLSAAYVLANAGH---QVTVLEASERAG 80
Cdd:COG4529    2 TGARKRIAIIGGGASGTALAIHLLRRAPeplRITLFEPRPELG 44
PRK05329 PRK05329
glycerol-3-phosphate dehydrogenase subunit GlpB;
47-73 1.43e-03

glycerol-3-phosphate dehydrogenase subunit GlpB;


Pssm-ID: 235412  Cd Length: 422  Bit Score: 40.99  E-value: 1.43e-03
                         10        20
                 ....*....|....*....|....*..
gi 817033869  47 VVIVGAGMSGLSAAYVLANAGHQVTVL 73
Cdd:PRK05329   5 VLVIGGGLAGLTAALAAAEAGKRVALV 31
PRK05335 PRK05335
tRNA (uracil-5-)-methyltransferase Gid; Reviewed
 45-74 1.45e-03

tRNA (uracil-5-)-methyltransferase Gid; Reviewed


Pssm-ID: 235416  Cd Length: 436  Bit Score: 40.90  E-value: 1.45e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 817033869  45 KRVVIVGAGMSGLSAAYVLANAGHQVTVLE 74
Cdd:PRK05335   3 KPVNVIGAGLAGSEAAWQLAKRGVPVELYE 32
ubiF PRK08020
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed
 40-74 1.58e-03

2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed


Pssm-ID: 181199 [Multi-domain]  Cd Length: 391  Bit Score: 40.74  E-value: 1.58e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 817033869  40 TTSNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLE 74
Cdd:PRK08020   1 MTNQPTDIAIVGGGMVGAALALGLAQHGFSVAVLE 35
PRK12843 PRK12843
FAD-dependent oxidoreductase;
47-81 2.11e-03

FAD-dependent oxidoreductase;


Pssm-ID: 237225 [Multi-domain]  Cd Length: 578  Bit Score: 40.49  E-value: 2.11e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 817033869  47 VVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGG 81
Cdd:PRK12843  19 VIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGG 53
PRK05868 PRK05868
FAD-binding protein;
45-130 2.16e-03

FAD-binding protein;


Pssm-ID: 180297 [Multi-domain]  Cd Length: 372  Bit Score: 40.35  E-value: 2.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869  45 KRVVIVGAGMSGLSAAYVLANAGHQVTVLEASE--RAGGRVKTYRNEKEGWYANLGPMRLPEKHRIVREYIKKFDLRLNE 122
Cdd:PRK05868   2 KTVVVSGASVAGTAAAYWLGRHGYSVTMVERHPglRPGGQAIDVRGPALDVLERMGLLAAAQEHKTRIRGASFVDRDGNE 81


                 ....*...
gi 817033869 123 FSQENENA 130
Cdd:PRK05868  82 LFRDTEST 89
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 44-85 2.89e-03

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: 39.70  E-value: 2.89e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 817033869  44 PKRVVIVGAGMSGLSAAYVLANAGHQVTVLEAS--------ERAGGRVKT 85
Cdd:cd05305  168 PAKVVILGAGVVGENAARVALGLGAEVTVLDINlerlryldDIFGGRVTT 217
PRK09126 PRK09126
FAD-dependent hydroxylase;
47-79 3.27e-03

FAD-dependent hydroxylase;


Pssm-ID: 236385 [Multi-domain]  Cd Length: 392  Bit Score: 39.92  E-value: 3.27e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 817033869  47 VVIVGAGMSGLSAAYVLANAGHQVTVLEASERA 79
Cdd:PRK09126   6 IVVVGAGPAGLSFARSLAGSGLKVTLIERQPLA 38
PRK09260 PRK09260
3-hydroxyacyl-CoA dehydrogenase;
45-79 3.33e-03

3-hydroxyacyl-CoA dehydrogenase;


Pssm-ID: 236434 [Multi-domain]  Cd Length: 288  Bit Score: 39.39  E-value: 3.33e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 817033869  45 KRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERA 79
Cdd:PRK09260   2 EKLVVVGAGVMGRGIAYVFAVSGFQTTLVDIKQEQ 36
PLN02661 PLN02661
Putative thiazole synthesis
 47-81 3.54e-03

Putative thiazole synthesis


Pssm-ID: 178267  Cd Length: 357  Bit Score: 39.81  E-value: 3.54e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 817033869  47 VVIVGAGMSGLSAAYVLANAGH-QVTVLEASERAGG 81
Cdd:PLN02661  95 VVIVGAGSAGLSCAYELSKNPNvKVAIIEQSVSPGG 130
PRK06129 PRK06129
3-hydroxyacyl-CoA dehydrogenase; Validated
 44-86 3.94e-03

3-hydroxyacyl-CoA dehydrogenase; Validated


Pssm-ID: 235706 [Multi-domain]  Cd Length: 308  Bit Score: 39.26  E-value: 3.94e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 817033869  44 PKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTY 86
Cdd:PRK06129   2 MGSVAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAAAAAPAY 44
TrmFO COG1206
Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and ...
 45-74 4.02e-03

Folate-dependent tRNA-U54 methylase TrmFO/GidA [Translation, ribosomal structure and biogenesis]; Folate-dependent tRNA-U54 methylase TrmFO/GidA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440819  Cd Length: 436  Bit Score: 39.66  E-value: 4.02e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 817033869  45 KRVVIVGAGMSGLSAAYVLANAGHQVTVLE 74
Cdd:COG1206    2 KPVTVIGGGLAGSEAAWQLAERGVPVRLYE 31
PRK10157 PRK10157
putative oxidoreductase FixC; Provisional
 48-82 4.40e-03

putative oxidoreductase FixC; Provisional


Pssm-ID: 182273 [Multi-domain]  Cd Length: 428  Bit Score: 39.51  E-value: 4.40e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 817033869  48 VIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGR 82
Cdd:PRK10157   9 IIVGAGLAGSVAALVLAREGAQVLVIERGNSAGAK 43
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
 25-73 4.56e-03

NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133443 [Multi-domain]  Cd Length: 155  Bit Score: 37.64  E-value: 4.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 817033869  25 TDYEEFLEIAKNGLSTTSNpKRVVIVGAGMSGLSAAYVLANAGHQ-VTVL 73
Cdd:cd01065    1 TDGLGFVRALEEAGIELKG-KKVLILGAGGAARAVAYALAELGAAkIVIV 49
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 47-74 5.09e-03

FAD binding domain; This domain is involved in FAD binding in a number of enzymes.


Pssm-ID: 396193 [Multi-domain]  Cd Length: 348  Bit Score: 39.23  E-value: 5.09e-03
                          10        20
                  ....*....|....*....|....*...
gi 817033869   47 VVIVGAGMSGLSAAYVLANAGHQVTVLE 74
Cdd:pfam01494   4 VLIVGGGPAGLMLALLLARAGVRVVLVE 31
Ald COG0686
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ...
 44-85 5.36e-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: 39.22  E-value: 5.36e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 817033869  44 PKRVVIVGAGMSGLSAAYVLANAGHQVTVL--------EASERAGGRVKT 85
Cdd:COG0686  168 PAKVVILGGGVVGTNAARMALGLGADVTVLdinldrlrRLDDIFGGRVTT 217
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 44-79 6.31e-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: 38.51  E-value: 6.31e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 817033869  44 PKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERA 79
Cdd:COG0569   95 KMHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPER 130
PRK14619 PRK14619
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
 41-72 6.83e-03

NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional


Pssm-ID: 237771 [Multi-domain]  Cd Length: 308  Bit Score: 38.43  E-value: 6.83e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 817033869  41 TSNPKRVVIVGAGMSGLSAAYVLANAGHQVTV 72
Cdd:PRK14619   1 TTQPKTIAILGAGAWGSTLAGLASANGHRVRV 32
PRK07045 PRK07045
putative monooxygenase; Reviewed
 41-79 6.90e-03

putative monooxygenase; Reviewed


Pssm-ID: 136171 [Multi-domain]  Cd Length: 388  Bit Score: 38.73  E-value: 6.90e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 817033869  41 TSNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLE--ASERA 79
Cdd:PRK07045   2 KNNPVDVLINGSGIAGVALAHLLGARGHSVTVVEraARNRA 42
PRK08132 PRK08132
FAD-dependent oxidoreductase; Provisional
 46-75 6.95e-03

FAD-dependent oxidoreductase; Provisional


Pssm-ID: 236158 [Multi-domain]  Cd Length: 547  Bit Score: 39.08  E-value: 6.95e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 817033869  46 RVVIVGAGMSGLSAAYVLANAGHQVTVLEA 75
Cdd:PRK08132  25 PVVVVGAGPVGLALAIDLAQQGVPVVLLDD 54
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
 47-81 7.06e-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: 38.74  E-value: 7.06e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 817033869   47 VVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGG 81
Cdd:pfam12831   2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGG 36
PRK07121 PRK07121
FAD-binding protein;
47-81 7.07e-03

FAD-binding protein;


Pssm-ID: 180854 [Multi-domain]  Cd Length: 492  Bit Score: 38.71  E-value: 7.07e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 817033869  47 VVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGG 81
Cdd:PRK07121  23 VVVVGFGAAGACAAIEAAAAGARVLVLERAAGAGG 57
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
 27-100 8.45e-03

Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain dehydrogenase/zinc-dependent alcohol dehydrogenase-like family, catalyzes the NADP(+)-dependent oxidation of glucose to gluconate, the first step in the Entner-Doudoroff pathway, an alternative to or substitute for glycolysis or the pentose phosphate pathway. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossman fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176192 [Multi-domain]  Cd Length: 355  Bit Score: 38.36  E-value: 8.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 817033869  27 YEEFLEIAKNglSTTSNPKRVVIVGAGMSGLSAAYVLANAGHQVTVL----------EASERAGGRVKTYRNEKEGWYAN 96
Cdd:cd08230  158 IEQAEAVQKR--LPTWNPRRALVLGAGPIGLLAALLLRLRGFEVYVLnrrdppdpkaDIVEELGATYVNSSKTPVAEVKL 235


                 ....
gi 817033869  97 LGPM 100
Cdd:cd08230  236 VGEF 239
 
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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