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Conserved domains on  [gi|1120505585|ref|WP_073366007|]
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glutamate synthase subunit beta [Rhodococcus jostii]

Protein Classification

glutamate synthase subunit beta( domain architecture ID 11486208)

beta subunit of the glutamate synthase that catalyzes the formation of L-glutamate from 2-oxoglutarate and L-glutamine, as part of the L-glutamate biosynthesis GLT pathway

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
gltD PRK12810
glutamate synthase subunit beta; Reviewed
1-472 0e+00

glutamate synthase subunit beta; Reviewed


:

Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 905.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585   1 MGDPSGFLKHtSRELPVRRPVPLRLLDWNEVYEEFSSDTLKTQASRCMDCGIPFCHNGCPLGNLIPEWNDLVYKDRWHDG 80
Cdd:PRK12810    1 MGKPTGFLEY-DRVDPKKRPVAERIKDFKEFYEPFSEEQAKIQAARCMDCGIPFCHWGCPVHNYIPEWNDLVYRGRWEEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  81 IERLHATNNFPEFTGRLCPAPCEASCVLGINQDPVTIKQVEVELIDRAFDEGWVKPVHPTRSTGKKVAVVGSGPAGLAAA 160
Cdd:PRK12810   80 AERLHQTNNFPEFTGRVCPAPCEGACTLNINFGPVTIKNIERYIIDKAFEEGWVKPDPPVKRTGKKVAVVGSGPAGLAAA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 161 QQLTRAGHMVTVFERADRIGGLLRYGIPEFKMEKRHIDRRLDQMNSEGTVFKTGVNVGVDITADALREQFDAVVLAGGAT 240
Cdd:PRK12810  160 DQLARAGHKVTVFERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKDITAEELLAEYDAVFLGTGAY 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 241 EARDLPIPGRELDGIHQAMEFLPIANRVQLGDLEEPTITAEGKKVVIIGGGDTGADCLGTSHRQGAESVHQFEIMPRPPE 320
Cdd:PRK12810  240 KPRDLGIPGRDLDGVHFAMDFLIQNTRRVLGDETEPFISAKGKHVVVIGGGDTGMDCVGTAIRQGAKSVTQRDIMPMPPS 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 321 TRAEHTPWPTYPLMYRVASAHEEGGERLFSVNTERFVGADGKVTALKAHEVEMKSGRFEKVEGSDFELEADLVLLAMGFV 400
Cdd:PRK12810  320 RRNKNNPWPYWPMKLEVSNAHEEGVEREFNVQTKEFEGENGKVTGVKVVRTELGEGDFEPVEGSEFVLPADLVLLAMGFT 399
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1120505585 401 GPEkPGLLTDLGVDLNERGNVARS-AKWATNVDGVFVAGDMGRGQSLIVWAIAEGRSAAAAVDAYLEGESALP 472
Cdd:PRK12810  400 GPE-AGLLAQFGVELDERGRVAAPdNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAIDAYLMGSTALP 471
 
Name Accession Description Interval E-value
gltD PRK12810
glutamate synthase subunit beta; Reviewed
1-472 0e+00

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 905.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585   1 MGDPSGFLKHtSRELPVRRPVPLRLLDWNEVYEEFSSDTLKTQASRCMDCGIPFCHNGCPLGNLIPEWNDLVYKDRWHDG 80
Cdd:PRK12810    1 MGKPTGFLEY-DRVDPKKRPVAERIKDFKEFYEPFSEEQAKIQAARCMDCGIPFCHWGCPVHNYIPEWNDLVYRGRWEEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  81 IERLHATNNFPEFTGRLCPAPCEASCVLGINQDPVTIKQVEVELIDRAFDEGWVKPVHPTRSTGKKVAVVGSGPAGLAAA 160
Cdd:PRK12810   80 AERLHQTNNFPEFTGRVCPAPCEGACTLNINFGPVTIKNIERYIIDKAFEEGWVKPDPPVKRTGKKVAVVGSGPAGLAAA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 161 QQLTRAGHMVTVFERADRIGGLLRYGIPEFKMEKRHIDRRLDQMNSEGTVFKTGVNVGVDITADALREQFDAVVLAGGAT 240
Cdd:PRK12810  160 DQLARAGHKVTVFERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKDITAEELLAEYDAVFLGTGAY 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 241 EARDLPIPGRELDGIHQAMEFLPIANRVQLGDLEEPTITAEGKKVVIIGGGDTGADCLGTSHRQGAESVHQFEIMPRPPE 320
Cdd:PRK12810  240 KPRDLGIPGRDLDGVHFAMDFLIQNTRRVLGDETEPFISAKGKHVVVIGGGDTGMDCVGTAIRQGAKSVTQRDIMPMPPS 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 321 TRAEHTPWPTYPLMYRVASAHEEGGERLFSVNTERFVGADGKVTALKAHEVEMKSGRFEKVEGSDFELEADLVLLAMGFV 400
Cdd:PRK12810  320 RRNKNNPWPYWPMKLEVSNAHEEGVEREFNVQTKEFEGENGKVTGVKVVRTELGEGDFEPVEGSEFVLPADLVLLAMGFT 399
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1120505585 401 GPEkPGLLTDLGVDLNERGNVARS-AKWATNVDGVFVAGDMGRGQSLIVWAIAEGRSAAAAVDAYLEGESALP 472
Cdd:PRK12810  400 GPE-AGLLAQFGVELDERGRVAAPdNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAIDAYLMGSTALP 471
GOGAT_sm_gam TIGR01317
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for ...
3-472 0e+00

glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for the NADPH-dependent or NADH-dependent glutamate synthase (EC 1.4.1.13 and 1.4.1.14, respectively) small subunit or homologous region. TIGR01316 describes a family in several archaeal and deeply branched bacterial lineages of a homotetrameric form for which there is no large subunit. Another model describes glutamate synthase small subunit from gamma and some alpha subdivision Proteobacteria plus paralogs of unknown function. This model describes the small subunit, or homologous region of longer forms proteins, of eukaryotes, Gram-positive bacteria, cyanobacteria, and some other lineages. All members with known function participate in NADH or NADPH-dependent reactions to interconvert between glutamine plus 2-oxoglutarate and two molecules of glutamate.


Pssm-ID: 162300 [Multi-domain]  Cd Length: 485  Bit Score: 773.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585   3 DPSGFLKHTSRELPVRRPVpLRLLDWNEVYEEFSSDTLKTQASRCMDCGIPFCHN--GCPLGNLIPEWNDLVYKDRWHDG 80
Cdd:TIGR01317   1 KPTGFLEYKRRKPTERDPR-TRLKDWKEFTNPFDKESAKYQAARCMDCGTPFCHNdsGCPLNNLIPEFNDLVFRGRWKEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  81 IERLHATNNFPEFTGRLCPAPCEASCVLGINQDPVTIKQVEVELIDRAFDEGWVKPVHPTRSTGKKVAVVGSGPAGLAAA 160
Cdd:TIGR01317  80 LDRLHATNNFPEFTGRVCPAPCEGACTLGISEDPVGIKSIERIIIDKGFQEGWVQPRPPSKRTGKKVAVVGSGPAGLAAA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 161 QQLTRAGHMVTVFERADRIGGLLRYGIPEFKMEKRHIDRRLDQMNSEGTVFKTGVNVGVDITADALREQFDAVVLAGGAT 240
Cdd:TIGR01317 160 DQLNRAGHTVTVFEREDRCGGLLMYGIPNMKLDKAIVDRRIDLLSAEGIDFVTNTEIGVDISADELKEQFDAVVLAGGAT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 241 EARDLPIPGRELDGIHQAMEFLPIANRVQLGD--LEEPTITAEGKKVVIIGGGDTGADCLGTSHRQGAESVHQFEIMPRP 318
Cdd:TIGR01317 240 KPRDLPIPGRELKGIHYAMEFLPSATKALLGKdfKDIIFIKAKGKKVVVIGGGDTGADCVGTSLRHGAASVHQFEIMPKP 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 319 PETRAEHTPWPTYPLMYRVASAHEEGGE------RLFSVNTERFVGAD-GKVTALKAHEVEMK---SGR--FEKVEGSDF 386
Cdd:TIGR01317 320 PEARAKDNPWPEWPRVYRVDYAHEEAAAhygrdpREYSILTKEFIGDDeGKVTALRTVRVEWKksqDGKwqFVEIPGSEE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 387 ELEADLVLLAMGFVGPEKPgLLTDLGVDLNERGNVARS-AKWATNVDGVFVAGDMGRGQSLIVWAIAEGRSAAAAVDAYL 465
Cdd:TIGR01317 400 VFEADLVLLAMGFVGPEQI-LLDDFGVKKTRRGNISAGyDDYSTSIPGVFAAGDCRRGQSLIVWAINEGRKAAAAVDRYL 478

                  ....*..
gi 1120505585 466 EGESALP 472
Cdd:TIGR01317 479 MGSSVLP 485
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
24-464 0e+00

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: 646.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  24 RLLDWNEVYEEFSSDTLKTQASRCMDCGIPFCHNGCPLGNLIPEWNDLVYKDRWHDGIERLHATNNFPEFTGRLCPAPCE 103
Cdd:COG0493     1 RIKDFREVYPGLSEEEAIEQAARCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCPAPCE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 104 ASCVLGINQDPVTIKQVEVELIDRAFDEGWVKPVHPTRSTGKKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGGLL 183
Cdd:COG0493    81 GACVRGIVDEPVAIGALERFIADKAFEEGWVKPPPPAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGGLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 184 RYGIPEFKMEKRHIDRRLDQMNSEGTVFKTGVNVGVDITADALREQFDAVVLAGGATEARDLPIPGRELDGIHQAMEFLP 263
Cdd:COG0493   161 RYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAVFLATGAGKPRDLGIPGEDLKGVHSAMDFLT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 264 IANRVQLGDleepTITAEGKKVVIIGGGDTGADCLGTSHRQGAESVHQFEIMPRppetraEHTPwptyPLMYRVASAHEE 343
Cdd:COG0493   241 AVNLGEAPD----TILAVGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTR------EEMP----ASKEEVEEALEE 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 344 GGERLFSVNTERFVG-ADGKVTALKAHEVEM----KSGR--FEKVEGSDFELEADLVLLAMGFVGPEkPGLLTDLGVDLN 416
Cdd:COG0493   307 GVEFLFLVAPVEIIGdENGRVTGLECVRMELgepdESGRrrPVPIEGSEFTLPADLVILAIGQTPDP-SGLEEELGLELD 385
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1120505585 417 ERGNVARSAK-WATNVDGVFVAGDMGRGQSLIVWAIAEGRSAAAAVDAY 464
Cdd:COG0493   386 KRGTIVVDEEtYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDRY 434
Fer4_20 pfam14691
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ...
24-133 5.11e-30

Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme dihydroprymidine dehydrogenase binds FAD. Dihydroprymidine dehydrogenase catalyzes the first and rate-limiting step of pyrimidine degradation by converting pyrimidines to the corresponding 5,6- dihydro compounds. This domain carries two Fe4-S4 clusters.


Pssm-ID: 434132 [Multi-domain]  Cd Length: 113  Bit Score: 113.02  E-value: 5.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  24 RLLDWNEVYEEFSSDTLKTQASRCMDCGIPFCHNGCPLGNLIPEWNDLVYKDRWHDGIERLHATNNFPEFTGRLCPA--P 101
Cdd:pfam14691   1 RIKNFEEVALGYTEEEAIAEASRCLQCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQerQ 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1120505585 102 CEASCVLGI-NQDPVTIKQVEVELIDRAFDEGW 133
Cdd:pfam14691  81 CEGACVLGKkGFEPVAIGRLERFAADWARENGI 113
 
Name Accession Description Interval E-value
gltD PRK12810
glutamate synthase subunit beta; Reviewed
1-472 0e+00

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 905.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585   1 MGDPSGFLKHtSRELPVRRPVPLRLLDWNEVYEEFSSDTLKTQASRCMDCGIPFCHNGCPLGNLIPEWNDLVYKDRWHDG 80
Cdd:PRK12810    1 MGKPTGFLEY-DRVDPKKRPVAERIKDFKEFYEPFSEEQAKIQAARCMDCGIPFCHWGCPVHNYIPEWNDLVYRGRWEEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  81 IERLHATNNFPEFTGRLCPAPCEASCVLGINQDPVTIKQVEVELIDRAFDEGWVKPVHPTRSTGKKVAVVGSGPAGLAAA 160
Cdd:PRK12810   80 AERLHQTNNFPEFTGRVCPAPCEGACTLNINFGPVTIKNIERYIIDKAFEEGWVKPDPPVKRTGKKVAVVGSGPAGLAAA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 161 QQLTRAGHMVTVFERADRIGGLLRYGIPEFKMEKRHIDRRLDQMNSEGTVFKTGVNVGVDITADALREQFDAVVLAGGAT 240
Cdd:PRK12810  160 DQLARAGHKVTVFERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKDITAEELLAEYDAVFLGTGAY 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 241 EARDLPIPGRELDGIHQAMEFLPIANRVQLGDLEEPTITAEGKKVVIIGGGDTGADCLGTSHRQGAESVHQFEIMPRPPE 320
Cdd:PRK12810  240 KPRDLGIPGRDLDGVHFAMDFLIQNTRRVLGDETEPFISAKGKHVVVIGGGDTGMDCVGTAIRQGAKSVTQRDIMPMPPS 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 321 TRAEHTPWPTYPLMYRVASAHEEGGERLFSVNTERFVGADGKVTALKAHEVEMKSGRFEKVEGSDFELEADLVLLAMGFV 400
Cdd:PRK12810  320 RRNKNNPWPYWPMKLEVSNAHEEGVEREFNVQTKEFEGENGKVTGVKVVRTELGEGDFEPVEGSEFVLPADLVLLAMGFT 399
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1120505585 401 GPEkPGLLTDLGVDLNERGNVARS-AKWATNVDGVFVAGDMGRGQSLIVWAIAEGRSAAAAVDAYLEGESALP 472
Cdd:PRK12810  400 GPE-AGLLAQFGVELDERGRVAAPdNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAIDAYLMGSTALP 471
GOGAT_sm_gam TIGR01317
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for ...
3-472 0e+00

glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for the NADPH-dependent or NADH-dependent glutamate synthase (EC 1.4.1.13 and 1.4.1.14, respectively) small subunit or homologous region. TIGR01316 describes a family in several archaeal and deeply branched bacterial lineages of a homotetrameric form for which there is no large subunit. Another model describes glutamate synthase small subunit from gamma and some alpha subdivision Proteobacteria plus paralogs of unknown function. This model describes the small subunit, or homologous region of longer forms proteins, of eukaryotes, Gram-positive bacteria, cyanobacteria, and some other lineages. All members with known function participate in NADH or NADPH-dependent reactions to interconvert between glutamine plus 2-oxoglutarate and two molecules of glutamate.


Pssm-ID: 162300 [Multi-domain]  Cd Length: 485  Bit Score: 773.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585   3 DPSGFLKHTSRELPVRRPVpLRLLDWNEVYEEFSSDTLKTQASRCMDCGIPFCHN--GCPLGNLIPEWNDLVYKDRWHDG 80
Cdd:TIGR01317   1 KPTGFLEYKRRKPTERDPR-TRLKDWKEFTNPFDKESAKYQAARCMDCGTPFCHNdsGCPLNNLIPEFNDLVFRGRWKEA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  81 IERLHATNNFPEFTGRLCPAPCEASCVLGINQDPVTIKQVEVELIDRAFDEGWVKPVHPTRSTGKKVAVVGSGPAGLAAA 160
Cdd:TIGR01317  80 LDRLHATNNFPEFTGRVCPAPCEGACTLGISEDPVGIKSIERIIIDKGFQEGWVQPRPPSKRTGKKVAVVGSGPAGLAAA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 161 QQLTRAGHMVTVFERADRIGGLLRYGIPEFKMEKRHIDRRLDQMNSEGTVFKTGVNVGVDITADALREQFDAVVLAGGAT 240
Cdd:TIGR01317 160 DQLNRAGHTVTVFEREDRCGGLLMYGIPNMKLDKAIVDRRIDLLSAEGIDFVTNTEIGVDISADELKEQFDAVVLAGGAT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 241 EARDLPIPGRELDGIHQAMEFLPIANRVQLGD--LEEPTITAEGKKVVIIGGGDTGADCLGTSHRQGAESVHQFEIMPRP 318
Cdd:TIGR01317 240 KPRDLPIPGRELKGIHYAMEFLPSATKALLGKdfKDIIFIKAKGKKVVVIGGGDTGADCVGTSLRHGAASVHQFEIMPKP 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 319 PETRAEHTPWPTYPLMYRVASAHEEGGE------RLFSVNTERFVGAD-GKVTALKAHEVEMK---SGR--FEKVEGSDF 386
Cdd:TIGR01317 320 PEARAKDNPWPEWPRVYRVDYAHEEAAAhygrdpREYSILTKEFIGDDeGKVTALRTVRVEWKksqDGKwqFVEIPGSEE 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 387 ELEADLVLLAMGFVGPEKPgLLTDLGVDLNERGNVARS-AKWATNVDGVFVAGDMGRGQSLIVWAIAEGRSAAAAVDAYL 465
Cdd:TIGR01317 400 VFEADLVLLAMGFVGPEQI-LLDDFGVKKTRRGNISAGyDDYSTSIPGVFAAGDCRRGQSLIVWAINEGRKAAAAVDRYL 478

                  ....*..
gi 1120505585 466 EGESALP 472
Cdd:TIGR01317 479 MGSSVLP 485
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
24-464 0e+00

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: 646.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  24 RLLDWNEVYEEFSSDTLKTQASRCMDCGIPFCHNGCPLGNLIPEWNDLVYKDRWHDGIERLHATNNFPEFTGRLCPAPCE 103
Cdd:COG0493     1 RIKDFREVYPGLSEEEAIEQAARCLDCGDPPCQTGCPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVCGRVCPAPCE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 104 ASCVLGINQDPVTIKQVEVELIDRAFDEGWVKPVHPTRSTGKKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGGLL 183
Cdd:COG0493    81 GACVRGIVDEPVAIGALERFIADKAFEEGWVKPPPPAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGGLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 184 RYGIPEFKMEKRHIDRRLDQMNSEGTVFKTGVNVGVDITADALREQFDAVVLAGGATEARDLPIPGRELDGIHQAMEFLP 263
Cdd:COG0493   161 RYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAVFLATGAGKPRDLGIPGEDLKGVHSAMDFLT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 264 IANRVQLGDleepTITAEGKKVVIIGGGDTGADCLGTSHRQGAESVHQFEIMPRppetraEHTPwptyPLMYRVASAHEE 343
Cdd:COG0493   241 AVNLGEAPD----TILAVGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTR------EEMP----ASKEEVEEALEE 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 344 GGERLFSVNTERFVG-ADGKVTALKAHEVEM----KSGR--FEKVEGSDFELEADLVLLAMGFVGPEkPGLLTDLGVDLN 416
Cdd:COG0493   307 GVEFLFLVAPVEIIGdENGRVTGLECVRMELgepdESGRrrPVPIEGSEFTLPADLVILAIGQTPDP-SGLEEELGLELD 385
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1120505585 417 ERGNVARSAK-WATNVDGVFVAGDMGRGQSLIVWAIAEGRSAAAAVDAY 464
Cdd:COG0493   386 KRGTIVVDEEtYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDRY 434
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
9-470 5.79e-166

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 476.21  E-value: 5.79e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585   9 KHTSRELPVRRPVPLRLLDWNEVYEEFSSDTLKTQASRCMDCGIPFCHNGCPLGNLIPEWNDLVYKDRWHDGIERLHATN 88
Cdd:PRK11749    4 LTTPRIPMPRQDAEERAQNFDEVAPGYTPEEAIEEASRCLQCKDAPCVKACPVSIDIPEFIRLIAEGNLKGAAETILETN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  89 NFPEFTGRLCPAP--CEASCVLGINQDPVTIKQVEVELIDRAFDEGWVKPVhPTRSTGKKVAVVGSGPAGLAAAQQLTRA 166
Cdd:PRK11749   84 PLPAVCGRVCPQErlCEGACVRGKKGEPVAIGRLERYITDWAMETGWVLFK-RAPKTGKKVAVIGAGPAGLTAAHRLARK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 167 GHMVTVFERADRIGGLLRYGIPEFKMEKRHIDRRLDQMNSEGTVFKTGVNVGVDITADALREQFDAVVLAGGATEARDLP 246
Cdd:PRK11749  163 GYDVTIFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRDITLDELRAGYDAVFIGTGAGLPRFLG 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 247 IPGRELDGIHQAMEFLPIANRVqlgdlEEPTITAEGKKVVIIGGGDTGADCLGTSHRQGAESVHqfeIMPRppETRAEht 326
Cdd:PRK11749  243 IPGENLGGVYSAVDFLTRVNQA-----VADYDLPVGKRVVVIGGGNTAMDAARTAKRLGAESVT---IVYR--RGREE-- 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 327 pwptyplM----YRVASAHEEGGERLFSVNTERFVGADGKVTALKAHEVEM----KSGR-FEKVEGSDFELEADLVLLAM 397
Cdd:PRK11749  311 -------MpaseEEVEHAKEEGVEFEWLAAPVEILGDEGRVTGVEFVRMELgepdASGRrRVPIEGSEFTLPADLVIKAI 383
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1120505585 398 GFvGPEKPGLLTDLGVDLNERGNVARS-AKWATNVDGVFVAGDMGRGQSLIVWAIAEGRSAAAAVDAYLEGESA 470
Cdd:PRK11749  384 GQ-TPNPLILSTTPGLELNRWGTIIADdETGRTSLPGVFAGGDIVTGAATVVWAVGDGKDAAEAIHEYLEGAAS 456
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
53-483 1.09e-88

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 281.76  E-value: 1.09e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  53 PFCHNGCPLGNLIPEWNDLVYKDRWHDGIERLHATNNFPEFTGRLCPAPCEASCVLGINQDPVTIKQVEVELIDRAFDEG 132
Cdd:PRK12771   47 PPCNAACPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHPCESGCNRGQVDDAVGINAVERFLGDYAIANG 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 133 WVKPVhPTRSTGKKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGGLLRYGIPEFKMEKRHIDRRLDQMNSEGTVFK 212
Cdd:PRK12771  127 WKFPA-PAPDTGKRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRYGIPAYRLPREVLDAEIQRILDLGVEVR 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 213 TGVNVGVDITADALREQFDAVVLAGGATEARDLPIPGRELDGIHQAMEFLPianrvQLGDLEEPTItaeGKKVVIIGGGD 292
Cdd:PRK12771  206 LGVRVGEDITLEQLEGEFDAVFVAIGAQLGKRLPIPGEDAAGVLDAVDFLR-----AVGEGEPPFL---GKRVVVIGGGN 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 293 TGADCLGTSHRQGAESV-------------HQFEIMprppetraehtpwptyplmyrvaSAHEEGGERLFSVNTERFVGA 359
Cdd:PRK12771  278 TAMDAARTARRLGAEEVtivyrrtredmpaHDEEIE-----------------------EALREGVEINWLRTPVEIEGD 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 360 DGKVTALKAHEVEMK----SGRFEKVEGSDFELEADLVLLAMG----FVGPEK-PGLLTDLG---VDLNERgnvarsakw 427
Cdd:PRK12771  335 ENGATGLRVITVEKMeldeDGRPSPVTGEEETLEADLVVLAIGqdidSAGLESvPGVEVGRGvvqVDPNFM--------- 405
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1120505585 428 ATNVDGVFVAGDMGRGQSLIVWAIAEGRSAAAAVDAYLEGESALPSPIATTTAPQR 483
Cdd:PRK12771  406 MTGRPGVFAGGDMVPGPRTVTTAIGHGKKAARNIDAFLGGEPYEHRPKREIVKFDK 461
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
13-465 4.85e-88

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 282.79  E-value: 4.85e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  13 RELPVRRPVPLRLLDWNEVYEEFSSDTLKTQASRCMDCGI-PFCHNGCPLGNLIPEWNDLVYKDRWHDGIERLHATNNFP 91
Cdd:PRK12769  193 RGEPDKLAIEARKTGFDEIYLPFRADQAQREASRCLKCGEhSICEWTCPLHNHIPQWIELVKAGNIDAAVELSHQTNSLP 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  92 EFTGRLCPAP--CEASCVLGINQDPVTIKQVEVELIDRAFDEGWVKPVHPTRSTGKKVAVVGSGPAGLAAAQQLTRAGHM 169
Cdd:PRK12769  273 EITGRVCPQDrlCEGACTLRDEYGAVTIGNIERYISDQALAKGWRPDLSQVTKSDKRVAIIGAGPAGLACADVLARNGVA 352
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 170 VTVFERADRIGGLLRYGIPEFKMEKRHIDRRLDQMNSEGTVFKTGVNVGVDITADALREQFDAVVLAGGATEARDLPIPG 249
Cdd:PRK12769  353 VTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFELNCEVGKDISLESLLEDYDAVFVGVGTYRSMKAGLPN 432
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 250 RELDGIHQAMEFLpIANRVQLGDLE----EPTITAEGKKVVIIGGGDTGADCLGTSHRQGAESVhqfeimprppeTRAEH 325
Cdd:PRK12769  433 EDAPGVYDALPFL-IANTKQVMGLEelpeEPFINTAGLNVVVLGGGDTAMDCVRTALRHGASNV-----------TCAYR 500
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 326 TPWPTYPLMYR-VASAHEEGGERLFSVN-TERFVGADGKVTALKAHEVEM----KSGRFEK--VEGSDFELEADLVLLAM 397
Cdd:PRK12769  501 RDEANMPGSKKeVKNAREEGANFEFNVQpVALELNEQGHVCGIRFLRTRLgepdAQGRRRPvpIPGSEFVMPADAVIMAF 580
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1120505585 398 GFvGPEKPGLLTDLGVDLNERGNVARSA----KWATNVDGVFVAGDMGRGQSLIVWAIAEGRSAAAAVDAYL 465
Cdd:PRK12769  581 GF-NPHGMPWLESHGVTVDKWGRIIADVesqyRYQTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGIIDWL 651
PRK12831 PRK12831
putative oxidoreductase; Provisional
16-469 2.66e-85

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 269.97  E-value: 2.66e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  16 PVR-RPVPLRLLDWNEVYEEFSSDTLKTQASRCMDCGIPFCHNGCPLGNLIPEWNDLVYKDRWHDGIERLHATNNFPEFT 94
Cdd:PRK12831   10 PVReQDPEVRATNFEEVCLGYNEEEAVKEASRCLQCKKPKCVKGCPVSINIPGFISKLKEGDFEEAAKIIAKYNALPAVC 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  95 GRLCP--APCEASCVLGINQDPVTIKQVEVELIDRAFDEGwVKPVHPTRSTGKKVAVVGSGPAGLAAAQQLTRAGHMVTV 172
Cdd:PRK12831   90 GRVCPqeSQCEGKCVLGIKGEPVAIGKLERFVADWARENG-IDLSETEEKKGKKVAVIGSGPAGLTCAGDLAKMGYDVTI 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 173 FERADRIGGLLRYGIPEFKMEKRHI-DRRLDQMNSEGTVFKTGVNVGVDITADALREQ--FDAVVLAGGATEARDLPIPG 249
Cdd:PRK12831  169 FEALHEPGGVLVYGIPEFRLPKETVvKKEIENIKKLGVKIETNVVVGKTVTIDELLEEegFDAVFIGSGAGLPKFMGIPG 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 250 RELDGIHQAMEFLpiaNRVQLGDLEEP---TITAEGKKVVIIGGGDTGADCLGTSHRQGAEsVHqfeIMPRPPE----TR 322
Cdd:PRK12831  249 ENLNGVFSANEFL---TRVNLMKAYKPeydTPIKVGKKVAVVGGGNVAMDAARTALRLGAE-VH---IVYRRSEeelpAR 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 323 AEhtpwptyplmyRVASAHEEGGERLFSVNTERFVG-ADGKVTALKAHEVEMK----SGRFEKV--EGSDFELEADLVLL 395
Cdd:PRK12831  322 VE-----------EVHHAKEEGVIFDLLTNPVEILGdENGWVKGMKCIKMELGepdaSGRRRPVeiEGSEFVLEVDTVIM 390
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1120505585 396 AMGfVGPEKPGLLTDLGVDLNERGN-VARSAKWATNVDGVFVAGDMGRGQSLIVWAIAEGRSAAAAVDAYLEGES 469
Cdd:PRK12831  391 SLG-TSPNPLISSTTKGLKINKRGCiVADEETGLTSKEGVFAGGDAVTGAATVILAMGAGKKAAKAIDEYLSKKW 464
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
42-468 6.62e-78

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 258.13  E-value: 6.62e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  42 TQASRCMDCGIPFCHNGCPLGNLIPEWNDLVYKDRWHDGIERLHATNNFPEFTGRLCP--APCEASCVLGI-NQDPVTIK 118
Cdd:PRK12778  326 TEAKRCLDCKNPGCVEGCPVGIDIPRFIKNIERGNFLEAAKILKETSALPAVCGRVCPqeKQCESKCIHGKmGEEAVAIG 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 119 QVEVELIDRAFDEGWVKPVHPTRSTGKKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGGLLRYGIPEFKMEKRHID 198
Cdd:PRK12778  406 YLERFVADYERESGNISVPEVAEKNGKKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGGVLKYGIPEFRLPKKIVD 485
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 199 RRLDQMNSEGTVFKTGVNVGVDITADALREQ-FDAVVLAGGATEARDLPIPGRELDGIHQAMEFLpiaNRVQLGDLEEP- 276
Cdd:PRK12778  486 VEIENLKKLGVKFETDVIVGKTITIEELEEEgFKGIFIASGAGLPNFMNIPGENSNGVMSSNEYL---TRVNLMDAASPd 562
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 277 --TITAEGKKVVIIGGGDTGADCLGTSHRQGAESV-----HQFEIMPrppeTRAEhtpwptyplmyRVASAHEEGGERLF 349
Cdd:PRK12778  563 sdTPIKFGKKVAVVGGGNTAMDSARTAKRLGAERVtivyrRSEEEMP----ARLE-----------EVKHAKEEGIEFLT 627
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 350 SVNTERFVG-ADGKVTALKAHEVEM----KSGRFEKV--EGSDFELEADLVLLAMGfVGPEKPGLLTDLGVDLNERGNVA 422
Cdd:PRK12778  628 LHNPIEYLAdEKGWVKQVVLQKMELgepdASGRRRPVaiPGSTFTVDVDLVIVSVG-VSPNPLVPSSIPGLELNRKGTIV 706
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1120505585 423 RSAKWATNVDGVFVAGDMGRGQSLIVWAIAEGRSAAAAVDAYLEGE 468
Cdd:PRK12778  707 VDEEMQSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYLSSK 752
gltA TIGR01316
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of ...
20-465 6.51e-76

glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of NADPH and NADH forms of glutamate synthase as found in eukaryotes and some bacteria. This protein is found in numerous species having no homolog of the glutamate synthase large subunit. The prototype of the family, from Pyrococcus sp. KOD1, was shown to be active as a homotetramer and to require NADPH. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 130383 [Multi-domain]  Cd Length: 449  Bit Score: 245.16  E-value: 6.51e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  20 PVPLRLLDWNEVYEEFSSDTLKTQASRCMDCGIPF--CHNGCPLGNLIPEWNDLVYKDRWHDGIERLHATNNFPEFTGRL 97
Cdd:TIGR01316   1 PPEERSKLFQEAALGYTEQLALVEAQRCLNCKDATkpCIKGCPVHVPIPEFIAKIQEGDFKGAVDIIKTTSLLPAICGRV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  98 CPAP--CEASCVLGINQ----DPVTIKQVEVELIDRAFDEGWVKPVHPTRSTGKKVAVVGSGPAGLAAAQQLTRAGHMVT 171
Cdd:TIGR01316  81 CPQErqCEGQCTVGKMFkdvgKPVSIGALERFVADWERQHGIETEPEKAPSTHKKVAVIGAGPAGLACASELAKAGHSVT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 172 VFERADRIGGLLRYGIPEFKMEKRHIDRRLDQMNSEGTVFKTGVNVGVDITADALREQFDAVVLAGGATEARDLPIPGRE 251
Cdd:TIGR01316 161 VFEALHKPGGVVTYGIPEFRLPKEIVVTEIKTLKKLGVTFRMNFLVGKTATLEELFSQYDAVFIGTGAGLPKLMNIPGEE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 252 LDGIHQAMEFLPIANRVQLGDL-EEPTITAEGKKVVIIGGGDTGADCLGTSHRQGAEsVHqfeIMPRppETRAEHTpwpt 330
Cdd:TIGR01316 241 LCGVYSANDFLTRANLMKAYEFpHADTPVYAGKSVVVIGGGNTAVDSARTALRLGAE-VH---CLYR--RTREDMT---- 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 331 yPLMYRVASAHEEGGERLFSVNTERFVG-ADGKVTALK------AHEVEMKSGRFEKVEGSDFELEADLVLLAMGfVGPe 403
Cdd:TIGR01316 311 -ARVEEIAHAEEEGVKFHFLCQPVEIIGdEEGNVRAVKfrkmdcQEQIDSGERRFLPCGDAECKLEADAVIVAIG-NGS- 387
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1120505585 404 KPGLLTDLGVDLNERGNVARSAKWATNVDGVFVAGDMGRGQSLIVWAIAEGRSAAAAVDAYL 465
Cdd:TIGR01316 388 NPIMAETTRLKTSERGTIVVDEDQRTSIPGVFAGGDIILGAATVIRAMGQGKRAAKSINEYL 449
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
30-458 3.52e-72

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 240.70  E-value: 3.52e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  30 EVYEEFSSDTLKTQASRCMDCG-IPFCHNGCPLGNLIPEWNDLVYKDRWHDGIERLHATNNFPEFTGRLCPAP--CEASC 106
Cdd:PRK12809  193 EIYCGLDPQQATYESDRCVYCAeKANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTSSLPEICGRVCPQDrlCEGAC 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 107 VLGINQDPVTIKQVEVELIDRAFDEGWVKPVHPTRSTGKKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGGLLRYG 186
Cdd:PRK12809  273 TLKDHSGAVSIGNLERYITDTALAMGWRPDVSKVVPRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTFG 352
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 187 IPEFKMEKRHIDRRLDQMNSEGTVFKTGVNVGVDITADALREQFDAVVLAGGATEARDLPIPGRELDGIHQAMEFLpIAN 266
Cdd:PRK12809  353 IPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVFIGVGTYGMMRADLPHEDAPGVIQALPFL-TAH 431
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 267 RVQLGDLEE----PTITAEGKKVVIIGGGDTGADCLGTSHRQGAESV----HQFEImpRPPETRAEhtpwptyplmyrVA 338
Cdd:PRK12809  432 TRQLMGLPEseeyPLTDVEGKRVVVLGGGDTTMDCLRTSIRLNAASVtcayRRDEV--SMPGSRKE------------VV 497
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 339 SAHEEGGERLFSVNTERFV-GADGKVTALKAHEVEMKSG------RFEKVEGSDFELEADLVLLAMGFVGPEKPgLLTDL 411
Cdd:PRK12809  498 NAREEGVEFQFNVQPQYIAcDEDGRLTAVGLIRTAMGEPgpdgrrRPRPVAGSEFELPADVLIMAFGFQAHAMP-WLQGS 576
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1120505585 412 GVDLNERGNVARSAK----WATNVDGVFVAGDMGRGQSLIVWAIAEGRSAA 458
Cdd:PRK12809  577 GIKLDKWGLIQTGDVgylpTQTHLKKVFAGGDAVHGADLVVTAMAAGRQAA 627
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
44-481 6.43e-69

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 231.93  E-value: 6.43e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  44 ASRCMDCGIPfCHNGCPLGNLIPEWNDLVYKDRWHDGIERLHATNNFPEFTGRLCPAPCEASCVLGINQDPVTIKQVEVE 123
Cdd:PRK12814   94 EQHCGDCLGP-CELACPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAPCEEACRRHGVDEPVSICALKRY 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 124 LIDR--AFDEGWVKPVHPtrSTGKKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGGLLRYGIPEFKMEKRHIDRRL 201
Cdd:PRK12814  173 AADRdmESAERYIPERAP--KSGKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYGIPRFRLPESVIDADI 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 202 DQMNSEGTVFKTGVNVGVDITADALREQFDAVVLAGGATEARDLPIPGRELDGIHQAMEFLpiaNRVQLGDLEEPtitae 281
Cdd:PRK12814  251 APLRAMGAEFRFNTVFGRDITLEELQKEFDAVLLAVGAQKASKMGIPGEELPGVISGIDFL---RNVALGTALHP----- 322
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 282 GKKVVIIGGGDTGADCLGTSHRQGAESVhqfEIMPRP-----PETRAEhtpwptyplmyrVASAHEEGGE-RLFSVNTER 355
Cdd:PRK12814  323 GKKVVVIGGGNTAIDAARTALRLGAESV---TILYRRtreemPANRAE------------IEEALAEGVSlRELAAPVSI 387
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 356 FVGADG-KVTALKAHEVEM-KSGRFEKV--EGSDFELEADLVLLAMG-FVGPEkpgLLTDLGVDLNERGNVA-RSAKWAT 429
Cdd:PRK12814  388 ERSEGGlELTAIKMQQGEPdESGRRRPVpvEGSEFTLQADTVISAIGqQVDPP---IAEAAGIGTSRNGTVKvDPETLQT 464
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1120505585 430 NVDGVFVAGDMGRGQSLIVWAIAEGRSAAAAVDAYLEGEsalpsPIATTTAP 481
Cdd:PRK12814  465 SVAGVFAGGDCVTGADIAINAVEQGKRAAHAIDLFLNGK-----PVTAPVQP 511
PRK12775 PRK12775
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ...
15-472 1.63e-64

putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional


Pssm-ID: 183738 [Multi-domain]  Cd Length: 1006  Bit Score: 225.21  E-value: 1.63e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585   15 LPVRRPVPLR-----LLDWNEVYEEFSSDTLKTQASRCMDCGIPFCHNGCPLGNLIPEW-NDLVYKDrWHDGIERLHATN 88
Cdd:PRK12775   296 VPHQTPMPERdaverARNFKEVNLGYSLEDALQEAERCIQCAKPTCIAGCPVQIDIPVFiRHVVVRD-FDGALEVIYEAS 374
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585   89 NFPEFTGRLCP--APCEASCVLGINQDPVTIKQVEVELIDRAfdegWVKPVHPTRSTGK--KVAVVGSGPAGLAAAQQLT 164
Cdd:PRK12775   375 IFPSICGRVCPqeTQCEAQCIIAKKHESVGIGRLERFVGDNA----RAKPVKPPRFSKKlgKVAICGSGPAGLAAAADLV 450
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  165 RAGHMVTVFERADRIGGLLRYGIPEFKMEKRHIDRRLDQMNSEGTVFKTGVNVGVDITADALREQ--FDAVVLAGGATEA 242
Cdd:PRK12775   451 KYGVDVTVYEALHVVGGVLQYGIPSFRLPRDIIDREVQRLVDIGVKIETNKVIGKTFTVPQLMNDkgFDAVFLGVGAGAP 530
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  243 RDLPIPGRELDGIHQAMEFLpiaNRVQL--GD----LEEPtiTAEGKKVVIIGGGDTGADCLGTSHRQGAESVhqfEIMP 316
Cdd:PRK12775   531 TFLGIPGEFAGQVYSANEFL---TRVNLmgGDkfpfLDTP--ISLGKSVVVIGAGNTAMDCLRVAKRLGAPTV---RCVY 602
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  317 RPPETRAEHTpwptyplMYRVASAHEEGGERLF-SVNTERFVGADGKVTALKAHEVEM----KSGRFEKVEGSDF-ELEA 390
Cdd:PRK12775   603 RRSEAEAPAR-------IEEIRHAKEEGIDFFFlHSPVEIYVDAEGSVRGMKVEEMELgepdEKGRRKPMPTGEFkDLEC 675
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  391 DLVLLAMG-----FVGPEKPGLltdlgvDLNERGNVA-----RSAKWATNVDGVFVAGDMGRGQSLIVWAIAEGRSAAAA 460
Cdd:PRK12775   676 DTVIYALGtkanpIITQSTPGL------ALNKWGNIAaddgkLESTQSTNLPGVFAGGDIVTGGATVILAMGAGRRAARS 749
                          490
                   ....*....|..
gi 1120505585  461 VDAYLEGESALP 472
Cdd:PRK12775   750 IATYLRLGKKWP 761
PRK13984 PRK13984
putative oxidoreductase; Provisional
11-468 3.29e-59

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 205.00  E-value: 3.29e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  11 TSRELPVRR------PVPLRLLDWNEVYEEFSSDTLKTQASRCMDCGIpfCHNGCPLGNLIPEWNDLVYKDRWHDGIERL 84
Cdd:PRK13984  145 NSELLDLERvemeeiPPEERVKSFIEIVKGYSKEQAMQEAARCVECGI--CTDTCPAHMDIPQYIKAIYKDDLEEGLRWL 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  85 HATNNFPEFTGRLCPAPCEASCVLGINQDPVTIKQVEVELIDRAFDEGWVKPV-HPTRSTGKKVAVVGSGPAGLAAAQQL 163
Cdd:PRK13984  223 YKTNPLSMVCGRVCTHKCETVCSIGHRGEPIAIRWLKRYIVDNVPVEKYSEILdDEPEKKNKKVAIVGSGPAGLSAAYFL 302
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 164 TRAGHMVTVFERADRIGGLLRYGIPEFKMEKRHIDRRLDQMNSEGTVFKTGVNVGVDITADALREQFDAVVLAGGATEAR 243
Cdd:PRK13984  303 ATMGYEVTVYESLSKPGGVMRYGIPSYRLPDEALDKDIAFIEALGVKIHLNTRVGKDIPLEELREKHDAVFLSTGFTLGR 382
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 244 DLPIPGRELDGIHQAMEFLPIANRVQLGDLEEPTITaegKKVVIIGGGDTGADCLGTSHRQGAESVHQFEIMPRPPETRA 323
Cdd:PRK13984  383 STRIPGTDHPDVIQALPLLREIRDYLRGEGPKPKIP---RSLVVIGGGNVAMDIARSMARLQKMEYGEVNVKVTSLERTF 459
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 324 EHTPWPtyplMYRVASAHEEGGERLFSVNTERFVGADGKVTAL---KAHEVEMKSGRFEKV--EGSDFELEADLVLLAMG 398
Cdd:PRK13984  460 EEMPAD----MEEIEEGLEEGVVIYPGWGPMEVVIENDKVKGVkfkKCVEVFDEEGRFNPKfdESDQIIVEADMVVEAIG 535
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1120505585 399 fVGPEKPGLLTDLGVDLN-ERGNVARSAKWATNVDGVFVAGDMGRGQSlIVWAIAEGRSAAAAVDAYLEGE 468
Cdd:PRK13984  536 -QAPDYSYLPEELKSKLEfVRGRILTNEYGQTSIPWLFAGGDIVHGPD-IIHGVADGYWAAEGIDMYLRKQ 604
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
139-468 4.46e-52

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 179.80  E-value: 4.46e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 139 PTRSTGKKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGGLLRYGIPEFKMEKRHIDRRLDQMNSEGTVFKTGVNVG 218
Cdd:PRK12770   13 KPPPTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVVFHTRTKVC 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 219 VD---------------ITADALREQFDAVVLAGGATEARDLPIPGRELDGIHQAMEFLPIANRVQLGDLEEPTIT-AEG 282
Cdd:PRK12770   93 CGeplheeegdefveriVSLEELVKKYDAVLIATGTWKSRKLGIPGEDLPGVYSALEYLFRIRAAKLGYLPWEKVPpVEG 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 283 KKVVIIGGGDTGADCLGTSHRQGAESVhqfEIMPRppETRAEhtpwpTYPLMYRVASAHEEGGERLFSVNTERFVGaDGK 362
Cdd:PRK12770  173 KKVVVVGAGLTAVDAALEAVLLGAEKV---YLAYR--RTINE-----APAGKYEIERLIARGVEFLELVTPVRIIG-EGR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 363 VTALKAHEVEM----KSGRF--EKVEGSDFELEADLVLLAMGFVgPEKPGLLTDLGVDLNERGNVARSAKWATNVDGVFV 436
Cdd:PRK12770  242 VEGVELAKMRLgepdESGRPrpVPIPGSEFVLEADTVVFAIGEI-PTPPFAKECLGIELNRKGEIVVDEKHMTSREGVFA 320
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1120505585 437 AGDMGRGQSLIVWAIAEGRSAAAAVDAYLEGE 468
Cdd:PRK12770  321 AGDVVTGPSKIGKAIKSGLRAAQSIHEWLDLK 352
PRK12779 PRK12779
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ...
58-458 1.29e-39

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


Pssm-ID: 183740 [Multi-domain]  Cd Length: 944  Bit Score: 153.06  E-value: 1.29e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  58 GCPLGNLIPEWNDLVYKDRWHDGIERLHATNNFPEFTGRLCPAPCEASCVLGINQDPVTIKQVEVELIDRafdEGWVKPV 137
Cdd:PRK12779  213 GCPVKIHIPEMLDLLGNGKHREALELIESCNPLPNVTGRVCPQELQCQGVCTHTKRPIEIGQLEWYLPQH---EKLVNPN 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 138 HPTRSTGK----------KVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGGLLRYGIPEFKMEKRHIDRRLDQMNSE 207
Cdd:PRK12779  290 ANERFAGRispwaaavkpPIAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVLRYGIPEFRLPNQLIDDVVEKIKLL 369
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 208 GTVFKTGVNVGVDITADAL-REQFDAVVLAGGATEARDLPIPGRELDGIHQAMEFLPIANRVQ--LGDLEEPTITAEGKK 284
Cdd:PRK12779  370 GGRFVKNFVVGKTATLEDLkAAGFWKIFVGTGAGLPTFMNVPGEHLLGVMSANEFLTRVNLMRglDDDYETPLPEVKGKE 449
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 285 VVIIGGGDTGADCLGTSHRQGAesvhQFEIMPRppETRAEhtpwptypLMYRVASAH---EEGGERLFSVNTERFVGaDG 361
Cdd:PRK12779  450 VFVIGGGNTAMDAARTAKRLGG----NVTIVYR--RTKSE--------MPARVEELHhalEEGINLAVLRAPREFIG-DD 514
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 362 K---VTALKAHEVEM----KSGRFE-KVEGSDFELEADLVLLAMG-----FVGPEKPGLLTD-LGVDLNERGNvarsakW 427
Cdd:PRK12779  515 HthfVTHALLDVNELgepdKSGRRSpKPTGEIERVPVDLVIMALGntanpIMKDAEPGLKTNkWGTIEVEKGS------Q 588
                         410       420       430
                  ....*....|....*....|....*....|.
gi 1120505585 428 ATNVDGVFVAGDMGRGQSLIVWAIAEGRSAA 458
Cdd:PRK12779  589 RTSIKGVYSGGDAARGGSTAIRAAGDGQAAA 619
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
146-467 5.64e-31

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 121.38  E-value: 5.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 146 KVAVVGSGPAGLAAAQQLTRAGHMVTVFERaDRIGGLLR--------YGIPEFKMEKRHIDRRLDQMNSEGTVFKTGVNV 217
Cdd:COG0492     2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLAttkeienyPGFPEGISGPELAERLREQAERFGAEILLEEVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 218 GVD--------ITADALREQFDAVVLAGGATEaRDLPIPG-RELD--GIH-----QAMEFlpianrvqlgdleeptitaE 281
Cdd:COG0492    81 SVDkddgpfrvTTDDGTEYEAKAVIIATGAGP-RKLGLPGeEEFEgrGVSycatcDGFFF-------------------R 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 282 GKKVVIIGGGDTGAD---CLgtshRQGAESVHqfeIMPRPPETRAEHtpwptyplmYRVASAHEEGG-ERLFSVNTERFV 357
Cdd:COG0492   141 GKDVVVVGGGDSALEealYL----TKFASKVT---LIHRRDELRASK---------ILVERLRANPKiEVLWNTEVTEIE 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 358 GaDGKVTAlkaheVEMKSGRfekvEGSDFELEADLVLLAMGFVgPEKpGLLTDLGVDLNERGNVARSAKWATNVDGVFVA 437
Cdd:COG0492   205 G-DGRVEG-----VTLKNVK----TGEEKELEVDGVFVAIGLK-PNT-ELLKGLGLELDEDGYIVVDEDMETSVPGVFAA 272
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1120505585 438 GDMgRGQS--LIVWAIAEGRSAAAAVDAYLEG 467
Cdd:COG0492   273 GDV-RDYKyrQAATAAGEGAIAALSAARYLEP 303
Fer4_20 pfam14691
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ...
24-133 5.11e-30

Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme dihydroprymidine dehydrogenase binds FAD. Dihydroprymidine dehydrogenase catalyzes the first and rate-limiting step of pyrimidine degradation by converting pyrimidines to the corresponding 5,6- dihydro compounds. This domain carries two Fe4-S4 clusters.


Pssm-ID: 434132 [Multi-domain]  Cd Length: 113  Bit Score: 113.02  E-value: 5.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  24 RLLDWNEVYEEFSSDTLKTQASRCMDCGIPFCHNGCPLGNLIPEWNDLVYKDRWHDGIERLHATNNFPEFTGRLCPA--P 101
Cdd:pfam14691   1 RIKNFEEVALGYTEEEAIAEASRCLQCKDPPCVKGCPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQerQ 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1120505585 102 CEASCVLGI-NQDPVTIKQVEVELIDRAFDEGW 133
Cdd:pfam14691  81 CEGACVLGKkGFEPVAIGRLERFAADWARENGI 113
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
145-454 1.81e-26

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: 108.94  E-value: 1.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 145 KKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRI---GGLLRYGI---PEFKMEKRHIDRRLDQMNSEGTVFKTGVNV- 217
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTCpygGCVLSKALlgaAEAPEIASLWADLYKRKEEVVKKLNNGIEVl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 218 ----GVDI-------------TADALREQFDAVVLAGGATeARDLPIPGRELDGIHqAMEFLPIANRVQLGDLEeptita 280
Cdd:pfam07992  81 lgteVVSIdpgakkvvleelvDGDGETITYDRLVIATGAR-PRLPPIPGVELNVGF-LVRTLDSAEALRLKLLP------ 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 281 egKKVVIIGGGDTGADCLGTSHRQGAEsVHQFEIMPRP-PETRAEHTPWptyplmyrVASAHEEGG-ERLFSVNTERFVG 358
Cdd:pfam07992 153 --KRVVVVGGGYIGVELAAALAKLGKE-VTLIEALDRLlRAFDEEISAA--------LEKALEKNGvEVRLGTSVKEIIG 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 359 ADGKVtalkahEVEMKSGRfekvegsdfELEADLVLLAMGFVGpeKPGLLTDLGVDLNERGNVARSAKWATNVDGVFVAG 438
Cdd:pfam07992 222 DGDGV------EVILKDGT---------EIDADLVVVAIGRRP--NTELLEAAGLELDERGGIVVDEYLRTSVPGIYAAG 284
                         330
                  ....*....|....*..
gi 1120505585 439 DMGRGQ-SLIVWAIAEG 454
Cdd:pfam07992 285 DCRVGGpELAQNAVAQG 301
PLN02852 PLN02852
ferredoxin-NADP+ reductase
141-448 1.22e-20

ferredoxin-NADP+ reductase


Pssm-ID: 215457  Cd Length: 491  Bit Score: 94.38  E-value: 1.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 141 RSTGKKVAVVGSGPAGLAAAQQLTRA--GHMVTVFERADRIGGLLRYGI----PEFKMEKRHIDRRLDqmnSEGTVFKTG 214
Cdd:PLN02852   23 TSEPLHVCVVGSGPAGFYTADKLLKAhdGARVDIIERLPTPFGLVRSGVapdhPETKNVTNQFSRVAT---DDRVSFFGN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 215 VNVGVDITADALREQFDAVVLAGGATEARDLPIPGRELDGIHQAMEFLPIAN-----RVQLGDLeeptitAEGKKVVIIG 289
Cdd:PLN02852  100 VTLGRDVSLSELRDLYHVVVLAYGAESDRRLGIPGEDLPGVLSAREFVWWYNghpdcVHLPPDL------KSSDTAVVLG 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 290 GGDTGADC--------------------LGTSHRQGAESVHqfeIMPR---------PPETR--------------AEHT 326
Cdd:PLN02852  174 QGNVALDCarillrptdelastdiaehaLEALRGSSVRKVY---LVGRrgpvqaactAKELRellglknvrvrikeADLT 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 327 PWP--------------TYPLMYRVASAHEEGGER-------LFSVNTERFVGADGKVTALKAHEVEMK-------SGRF 378
Cdd:PLN02852  251 LSPedeeelkasrpkrrVYELLSKAAAAGKCAPSGgqrelhfVFFRNPTRFLDSGDGNGHVAGVKLERTvlegaagSGKQ 330
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1120505585 379 EKVEGSDFE-LEADLVLLAMGFVGPEKPGLLTD--LGVDLNERGNVARSAKWATNVDGVFVAGDMGRGQSLIV 448
Cdd:PLN02852  331 VAVGTGEFEdLPCGLVLKSIGYKSLPVDGLPFDhkRGVVPNVHGRVLSSASGADTEPGLYVVGWLKRGPTGII 403
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
145-460 1.34e-17

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 84.42  E-value: 1.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 145 KKVAVVGSGPAGLAAAQQLTRAGHM--VTVF--ERA---DRIggLLRYGIPEfKMEKRHIDRRLDQMNSEGTV-FKTGVN 216
Cdd:COG1251     2 MRIVIIGAGMAGVRAAEELRKLDPDgeITVIgaEPHppyNRP--PLSKVLAG-ETDEEDLLLRPADFYEENGIdLRLGTR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 217 V-GVD------ITADALREQFDAVVLAGGATeARDLPIPGRELDGIH--------QAMEflpianrvqlgdleepTITAE 281
Cdd:COG1251    79 VtAIDraartvTLADGETLPYDKLVLATGSR-PRVPPIPGADLPGVFtlrtlddaDALR----------------AALAP 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 282 GKKVVIIGGGDTGADCLGTSHRQGAEsVHQFEIMPRP-----PETRAEhtpwptyplmyRVASAHEEGG-ERLFSVNTER 355
Cdd:COG1251   142 GKRVVVIGGGLIGLEAAAALRKRGLE-VTVVERAPRLlprqlDEEAGA-----------LLQRLLEALGvEVRLGTGVTE 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 356 FVGaDGKVTAlkaheVEMKSGRfekvegsdfELEADLVLLAMGfVGP-----EKPGLLTDLGVDLNERGnvarsakwATN 430
Cdd:COG1251   210 IEG-DDRVTG-----VRLADGE---------ELPADLVVVAIG-VRPntelaRAAGLAVDRGIVVDDYL--------RTS 265
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1120505585 431 VDGVFVAGD--------MGRGQSLIVW-AIAEGRSAAAA 460
Cdd:COG1251   266 DPDIYAAGDcaehpgpvYGRRVLELVApAYEQARVAAAN 304
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
147-459 1.88e-16

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: 81.29  E-value: 1.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 147 VAVVGSGPAGLAAAQQLTRAGHMVTVFERaDRIGG------------LLR-------------YGI----PEFKMEK--R 195
Cdd:COG1249     6 LVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLGGtclnvgcipskaLLHaaevahearhaaeFGIsagaPSVDWAAlmA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 196 HIDRRLDQMNS--EGTVFKTGVNV--G---------VDITADalRE-QFDAVVLAGGATeARDLPIPGRELDGIHQAMEF 261
Cdd:COG1249    85 RKDKVVDRLRGgvEELLKKNGVDVirGrarfvdphtVEVTGG--ETlTADHIVIATGSR-PRVPPIPGLDEVRVLTSDEA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 262 LpianrvqlgDLEE-PtitaegKKVVIIGGGDTGADcLGTS-HRQGAEsVHQFEIMPRP-----PETRAEhtpwptypLM 334
Cdd:COG1249   162 L---------ELEElP------KSLVVIGGGYIGLE-FAQIfARLGSE-VTLVERGDRLlpgedPEISEA--------LE 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 335 YRVAsahEEGGERLFSVNTERFVGADGKVTalkaheVEMKSGRFEKVEgsdfelEADLVLLAMGFVgPEKPGL-LTDLGV 413
Cdd:COG1249   217 KALE---KEGIDILTGAKVTSVEKTGDGVT------VTLEDGGGEEAV------EADKVLVATGRR-PNTDGLgLEAAGV 280
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1120505585 414 DLNERGNVARSAKWATNVDGVFVAGDMGRGQSLIVWAIAEGRSAAA 459
Cdd:COG1249   281 ELDERGGIKVDEYLRTSVPGIYAIGDVTGGPQLAHVASAEGRVAAE 326
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
170-439 1.11e-14

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: 74.85  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 170 VTVFERADRIGGLlRYGIP------EFKMEKRHIdRRLDQMNSEGTVFKTGVNV-GVD------ITADALREQFDAVVLA 236
Cdd:COG0446     8 ITVIEKGPHHSYQ-PCGLPyyvgggIKDPEDLLV-RTPESFERKGIDVRTGTEVtAIDpeaktvTLRDGETLSYDKLVLA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 237 GGATEARdLPIPGRELDGIHqAMEFLPIANRvqlgdLEEPTITAEGKKVVIIGGGDTG---ADCLgtsHRQGAEsVHQFE 313
Cdd:COG0446    86 TGARPRP-PPIPGLDLPGVF-TLRTLDDADA-----LREALKEFKGKRAVVIGGGPIGlelAEAL---RKRGLK-VTLVE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 314 IMPRPPetraehtPWPTYPLMYRVASAHEEGG-ERLFSVNTERFVGaDGKVTalkaheVEMKSGRfekvegsdfELEADL 392
Cdd:COG0446   155 RAPRLL-------GVLDPEMAALLEEELREHGvELRLGETVVAIDG-DDKVA------VTLTDGE---------EIPADL 211
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1120505585 393 VLLAMGfVGPEkPGLLTDLGVDLNERGNVARSAKWATNVDGVFVAGD 439
Cdd:COG0446   212 VVVAPG-VRPN-TELAKDAGLALGERGWIKVDETLQTSDPDVYAAGD 256
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
139-399 2.43e-13

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: 71.43  E-value: 2.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 139 PTRSTGKKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGGL--------LR-------YGIPEFKMEK--------- 194
Cdd:COG2072     1 TAATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGTwrdnrypgLRldtpshlYSLPFFPNWSddpdfptgd 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 195 ------RHIDRRLD--------------QMNSEGTVFKTGVNVGVDITAdalreqfDAVVLAGGA-TEARDLPIPGRELD 253
Cdd:COG2072    81 eilaylEAYADKFGlrrpirfgtevtsaRWDEADGRWTVTTDDGETLTA-------RFVVVATGPlSRPKIPDIPGLEDF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 254 GIHQameFLPIA--NRVQLgdleeptitaEGKKVVIIGGGDTGADCLGTSHRQgAESVHQF-----EIMPRpPETRAEHT 326
Cdd:COG2072   154 AGEQ---LHSADwrNPVDL----------AGKRVLVVGTGASAVQIAPELARV-AAHVTVFqrtppWVLPR-PNYDPERG 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 327 PWPTYPLMYRVASAHEEGGERLFSVNTERFVG--ADGKVT------------------ALKAHEVEMKSGRFEKVEG--- 383
Cdd:COG2072   219 RPANYLGLEAPPALNRRDARAWLRRLLRAQVKdpELGLLTpdyppgckrpllstdyyeALRRGNVELVTGGIERITEdgv 298
                         330
                  ....*....|....*....
gi 1120505585 384 ---SDFELEADLVLLAMGF 399
Cdd:COG2072   299 vfaDGTEHEVDVIVWATGF 317
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
145-472 2.69e-13

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 71.32  E-value: 2.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 145 KKVAVVGSGPAGLAAAQQLTR---AGHMVTVFERADR--IGGLLrYGIPEFKMEKRHIDRRL-DQMNSEGTVFKTGVNVG 218
Cdd:COG1252     2 KRIVIVGGGFAGLEAARRLRKklgGDAEVTLIDPNPYhlFQPLL-PEVAAGTLSPDDIAIPLrELLRRAGVRFIQGEVTG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 219 VD------ITADALREQFDAVVLAGGATeARDLPIPGRE-----LDGIHQAMEflpIANRVQlgDLEEPTITAEGKKVVI 287
Cdd:COG1252    81 IDpeartvTLADGRTLSYDYLVIATGSV-TNFFGIPGLAehalpLKTLEDALA---LRERLL--AAFERAERRRLLTIVV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 288 IGGGDTGADCLGTSHRQGAESVHQFEIMPRPPEtraehtpwptyplMYRVasaheEGGERLFSVNTERFVGA-------- 359
Cdd:COG1252   155 VGGGPTGVELAGELAELLRKLLRYPGIDPDKVR-------------ITLV-----EAGPRILPGLGEKLSEAaekelekr 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 360 ------DGKVTALKAHEVEMKSGRfekvegsdfELEADLVLLAMGFVGPEkpgLLTDLGVDLNERGNVA-----RSakwa 428
Cdd:COG1252   217 gvevhtGTRVTEVDADGVTLEDGE---------EIPADTVIWAAGVKAPP---LLADLGLPTDRRGRVLvdptlQV---- 280
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1120505585 429 TNVDGVFVAGDM------------GRGQSlivwAIAEGRSAAAAVDAYLEGESALP 472
Cdd:COG1252   281 PGHPNVFAIGDCaavpdpdgkpvpKTAQA----AVQQAKVLAKNIAALLRGKPLKP 332
PRK07233 PRK07233
hypothetical protein; Provisional
146-194 1.52e-12

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 69.15  E-value: 1.52e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1120505585 146 KVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGGLL-RYGIPEFKMEK 194
Cdd:PRK07233    1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAaSFEFGGLPIER 50
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
135-475 1.64e-12

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 69.50  E-value: 1.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 135 KPVHPTR-STGKKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGGL---LRYGIPEFKMEKRHIDRRLDQMNSEG-- 208
Cdd:COG1148   130 EPLEPIKvPVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRaaqLHKTFPGLDCPQCILEPLIAEVEANPni 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 209 TVFK----TGVN--VG---VDITADALRE---QFDAVVLAGGATEARDLPIP----GReLDGIHQAMEFLPIANRvqlGD 272
Cdd:COG1148   210 TVYTgaevEEVSgyVGnftVTIKKGPREEieiEVGAIVLATGFKPYDPTKLGeygyGK-YPNVITNLELERLLAA---GK 285
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 273 LEEPTITAEGKKVVII---GGGDTGAD-------CLGTSHRQGAESVHQFeimprpPETRAEH------TPwPTYPLMYR 336
Cdd:COG1148   286 ILRPSDGKEPKSVAFIqcvGSRDEENGlpycsrvCCMYALKQALYLKEKN------PDADVYIfyrdirTY-GKYEEFYR 358
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 337 vaSAHEEGgerlfsVnteRFV---------GADGKVTaLKAHEVEMksgrfekveGSDFELEADLVLLAMGFVGPEKPGL 407
Cdd:COG1148   359 --RAREDG------V---RFIrgrvaeieeDEGGKLV-VTVEDTLL---------GEPVEIEADLVVLATGMVPSEDNEE 417
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1120505585 408 LTD-LGVDLNERGNVARS-AKWA---TNVDGVFVAGdMGRGQSLIVWAIAEGRSAAAAVDAYLEGESALPSPI 475
Cdd:COG1148   418 LAKlLKLPLDQDGFFLEAhPKLRpveTATDGIFLAG-AAHGPKDIPESIAQATAAAARAIQLLSKGELGVEPS 489
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
145-184 7.96e-12

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: 67.16  E-value: 7.96e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1120505585 145 KKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGGLLR 184
Cdd:COG1232     2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLIR 41
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
141-181 4.07e-11

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 64.94  E-value: 4.07e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1120505585 141 RSTGKKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGG 181
Cdd:COG1231     4 RARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGG 44
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
145-198 1.41e-10

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 63.33  E-value: 1.41e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1120505585 145 KKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGGLLRYgipeFKMEKRHID 198
Cdd:COG1233     4 YDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGGRART----FERPGFRFD 53
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
145-181 4.06e-10

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


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 61.05  E-value: 4.06e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1120505585 145 KKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGG 181
Cdd:COG3380     4 PDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGG 40
PRK07208 PRK07208
hypothetical protein; Provisional
145-184 1.47e-09

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 59.90  E-value: 1.47e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1120505585 145 KKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGGLLR 184
Cdd:PRK07208    5 KSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGISR 44
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
149-181 2.65e-09

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 53.30  E-value: 2.65e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1120505585 149 VVGSGPAGLAAAQQLTRAGHMVTVFERADRIGG 181
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGG 33
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
147-439 1.01e-08

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 57.49  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 147 VAVVGSGPAGLAAAQQLTRAGHMVTVFE------------------------------RADRIGglLRYGIPEF---KME 193
Cdd:PRK06292    6 VIVIGAGPAGYVAARRAAKLGKKVALIEkgplggtclnvgcipskaliaaaeafheakHAEEFG--IHADGPKIdfkKVM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 194 KR----------HIDRRLDQMNSEGTVFKTGVNVGVD-ITADALREQFDAVVLAGGAteaRDLPIPGREL---DGIhqam 259
Cdd:PRK06292   84 ARvrrerdrfvgGVVEGLEKKPKIDKIKGTARFVDPNtVEVNGERIEAKNIVIATGS---RVPPIPGVWLilgDRL---- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 260 eflpIANRvQLGDLEE-PtitaegKKVVIIGGGDTGADcLGTS-HRQGAEsVHQFEIMPR--P---PETRAEhtpwptyp 332
Cdd:PRK06292  157 ----LTSD-DAFELDKlP------KSLAVIGGGVIGLE-LGQAlSRLGVK-VTVFERGDRilPledPEVSKQ-------- 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 333 lmyrvasAHEEGGERL-FSVNTerfvgadgkvtalKAHEVEMKSGRFEKV---EGSDFELEADLVLLAMGFVgPEKPGL- 407
Cdd:PRK06292  216 -------AQKILSKEFkIKLGA-------------KVTSVEKSGDEKVEElekGGKTETIEADYVLVATGRR-PNTDGLg 274
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1120505585 408 LTDLGVDLNERGNVARSAKWATNVDGVFVAGD 439
Cdd:PRK06292  275 LENTGIELDERGRPVVDEHTQTSVPGIYAAGD 306
PTZ00188 PTZ00188
adrenodoxin reductase; Provisional
146-264 1.28e-08

adrenodoxin reductase; Provisional


Pssm-ID: 240308  Cd Length: 506  Bit Score: 57.20  E-value: 1.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 146 KVAVVGSGPAGLAAAQQLTRAGHM-VTVFERADRIGGLLRYGIPEFKMEKRHIDRRLDQ-MNSEGTVFKTGVNVGVDITA 223
Cdd:PTZ00188   41 KVGIIGAGPSALYCCKHLLKHERVkVDIFEKLPNPYGLIRYGVAPDHIHVKNTYKTFDPvFLSPNYRFFGNVHVGVDLKM 120
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1120505585 224 DALREQFDAVVLAGGATEArDLPIPGRELDGIHQAMEFLPI 264
Cdd:PTZ00188  121 EELRNHYNCVIFCCGASEV-SIPIGQQDEDKAVSGGETNPR 160
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
143-181 1.28e-08

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


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 57.05  E-value: 1.28e-08
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1120505585 143 TGKKVAVVGSGPAGLAAAQQLTRAgHMVTVFERADRIGG 181
Cdd:COG2907     2 ARMRIAVIGSGISGLTAAWLLSRR-HDVTLFEANDRLGG 39
PLN02172 PLN02172
flavin-containing monooxygenase FMO GS-OX
139-185 1.36e-08

flavin-containing monooxygenase FMO GS-OX


Pssm-ID: 215116 [Multi-domain]  Cd Length: 461  Bit Score: 56.79  E-value: 1.36e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1120505585 139 PTRSTGKKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGGLLRY 185
Cdd:PLN02172    5 QNPINSQHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGLWVY 51
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
143-255 2.21e-08

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: 55.59  E-value: 2.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 143 TGKKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIggLLRYGiPEF------KMEKRHIDRRLDQMNSEgtvFKTGVN 216
Cdd:COG0446   123 KGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRL--LGVLD-PEMaalleeELREHGVELRLGETVVA---IDGDDK 196
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1120505585 217 VGVdITADALREQFDAVVLAGGA---TE-ARDLPIPGRELDGI 255
Cdd:COG0446   197 VAV-TLTDGEEIPADLVVVAPGVrpnTElAKDAGLALGERGWI 238
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
143-184 2.21e-08

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: 56.40  E-value: 2.21e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1120505585 143 TGKKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGGLLR 184
Cdd:COG3349     2 MPPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGGRAR 43
PLN02976 PLN02976
amine oxidase
141-181 3.35e-08

amine oxidase


Pssm-ID: 215527 [Multi-domain]  Cd Length: 1713  Bit Score: 56.41  E-value: 3.35e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1120505585  141 RSTGKKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGG 181
Cdd:PLN02976   690 SVDRKKIIVVGAGPAGLTAARHLQRQGFSVTVLEARSRIGG 730
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
155-184 2.71e-07

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: 52.88  E-value: 2.71e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 1120505585 155 AGLAAAQQLTRAGHMVTVFERADRIGGLLR 184
Cdd:pfam01593   2 AGLAAARELLRAGHDVTVLEARDRVGGRIR 31
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
146-184 3.60e-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: 51.86  E-value: 3.60e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1120505585 146 KVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGGLLR 184
Cdd:COG0654     5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGR 43
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
147-181 4.40e-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: 4.40e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1120505585 147 VAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGG 181
Cdd:TIGR02734   1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGG 35
PRK07251 PRK07251
FAD-containing oxidoreductase;
149-443 6.58e-07

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 51.67  E-value: 6.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 149 VVGSGPAGLAAAQQLTRAGHMVTVFERADRIggllrYG--------IPEFKM---------------EKRHIDRRLDQMN 205
Cdd:PRK07251    8 VIGFGKAGKTLAAKLASAGKKVALVEESKAM-----YGgtcinigcIPTKTLlvaaeknlsfeqvmaTKNTVTSRLRGKN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 206 sEGTVFKTGVNV-----------GVDITADALREQFDA--VVLAGGATeARDLPIPGReLDGIH-------QAMEFLPia 265
Cdd:PRK07251   83 -YAMLAGSGVDLydaeahfvsnkVIEVQAGDEKIELTAetIVINTGAV-SNVLPIPGL-ADSKHvydstgiQSLETLP-- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 266 nrvqlgdleeptitaegKKVVIIGGGDTGADCLGTSHRQGAEsVHQFEIMPR--PpetRAEhtpwptyPLMYRVASAH-- 341
Cdd:PRK07251  158 -----------------ERLGIIGGGNIGLEFAGLYNKLGSK-VTVLDAASTilP---REE-------PSVAALAKQYme 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 342 EEGGERLFSVNTERfVGADGKVTALKAHEVEMksgRFekvegsdfeleaDLVLLAMGFVGPEKPGLLTDLGVDLNERGNV 421
Cdd:PRK07251  210 EDGITFLLNAHTTE-VKNDGDQVLVVTEDETY---RF------------DALLYATGRKPNTEPLGLENTDIELTERGAI 273
                         330       340
                  ....*....|....*....|..
gi 1120505585 422 ARSAKWATNVDGVFVAGDMGRG 443
Cdd:PRK07251  274 KVDDYCQTSVPGVFAVGDVNGG 295
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
143-240 1.36e-06

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


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 50.01  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 143 TGKKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGgllrygipeFKMEKRHIDRRLDQMNSEGTVFKTGVNV----- 217
Cdd:pfam07992 151 LPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLL---------RAFDEEISAALEKALEKNGVEVRLGTSVkeiig 221
                          90       100
                  ....*....|....*....|....*..
gi 1120505585 218 ---GVD-ITADALREQFDAVVLAGGAT 240
Cdd:pfam07992 222 dgdGVEvILKDGTEIDADLVVVAIGRR 248
PLN03000 PLN03000
amine oxidase
134-181 1.49e-06

amine oxidase


Pssm-ID: 178578 [Multi-domain]  Cd Length: 881  Bit Score: 50.79  E-value: 1.49e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1120505585 134 VKPVHPTRSTGKKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGG 181
Cdd:PLN03000  174 IKDKFPAQSSKSSVVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGG 221
PLN02576 PLN02576
protoporphyrinogen oxidase
144-184 1.76e-06

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 50.40  E-value: 1.76e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1120505585 144 GKKVAVVGSGPAGLAAAQQL-TRAGHMVTVFERADRIGGLLR 184
Cdd:PLN02576   12 SKDVAVVGAGVSGLAAAYALaSKHGVNVLVTEARDRVGGNIT 53
PRK06567 PRK06567
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Validated
58-262 1.81e-06

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


Pssm-ID: 235832 [Multi-domain]  Cd Length: 1028  Bit Score: 50.67  E-value: 1.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585   58 GCPLGNLIPEWNDLVYKDRWHDGIERLHATNNFPEFTG-RLCpAPCEASCVLGiNQDPVTIKQVEVELIDRAFD------ 130
Cdd:PRK06567   283 GCPLKQKISEMNYVKAQGFNLSALAIIVIDNPMVAATGhRIC-NDCSKACIYQ-KQDPVNIPLIESNILEETLKlpygle 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  131 -----EGWvKPVH-----PTRSTGKKVAVVGSGPAGLAAAQQLTRAGHMVTVF--------------------------- 173
Cdd:PRK06567   361 iylllTRW-NPLNiyaplPKEPTNYNILVTGLGPAGFSLSYYLLRSGHNVTAIdglkitllpfdvhkpikfwheyknlls 439
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585  174 ERADR-IGGLLRYGIpEFKMEKRHID--RRLDQMNSEgtvFK--TGVNVGVDITAD-ALREQFDAVVLAGGATEARDLPI 247
Cdd:PRK06567   440 ERMPRgFGGVAEYGI-TVRWDKNNLDilRLILERNNN---FKyyDGVALDFNITKEqAFDLGFDHIAFCIGAGQPKVLDI 515
                          250
                   ....*....|....*
gi 1120505585  248 PGRELDGIHQAMEFL 262
Cdd:PRK06567   516 ENFEAKGVKTASDFL 530
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
146-241 3.02e-06

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 49.32  E-value: 3.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 146 KVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIG--------GLLRYGI---PEFKMEK------RHIDRRLDQMNSEG 208
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGsgasgrnaGLIHPGLrylEPSELARlalealDLWEELEEELGIDC 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1120505585 209 TVFKTGV-NVGVDITADALREQFDAVVLAGGATE 241
Cdd:pfam01266  81 GFRRCGVlVLARDEEEEALEKLLAALRRLGVPAE 114
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
146-198 4.53e-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: 44.50  E-value: 4.53e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1120505585 146 KVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGGLLRYGIPEF---KMEKRHID 198
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPGFDPEIAKIlqeKLEKNGIE 56
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
145-184 6.24e-06

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 48.31  E-value: 6.24e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1120505585 145 KKVAVVGSGPAGLAAAQQLTRAG--HMVTVFERADRIGGLLR 184
Cdd:PRK11883    1 KKVAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKIQ 42
COG4716 COG4716
Myosin-crossreactive antigen (function unknown) [Function unknown];
131-183 1.17e-05

Myosin-crossreactive antigen (function unknown) [Function unknown];


Pssm-ID: 443751  Cd Length: 578  Bit Score: 47.90  E-value: 1.17e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1120505585 131 EGWVKPVHPTRSTGKKVAVVGSGPAGLAAAQQLTRAGHM----VTVFERADRIGGLL 183
Cdd:COG4716     9 EAFARPRKPEGVDDKSAYLVGSGLASLAAAAFLIRDGQMpgenIHILEELDLPGGSL 65
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
149-234 1.92e-05

Si-specific NAD(P)(+) transhydrogenase;


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 47.07  E-value: 1.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 149 VVGSGPAGLAAAQQLTRAGHMVTVFERADRIGGL-LRYG-IPefkmEK--RHIDRRLDQMNSEGTVFKTGVNvgVDITAD 224
Cdd:PRK05249   10 VIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGGGcTHTGtIP----SKalREAVLRLIGFNQNPLYSSYRVK--LRITFA 83
                          90
                  ....*....|
gi 1120505585 225 ALREQFDAVV 234
Cdd:PRK05249   84 DLLARADHVI 93
HI0933_like pfam03486
HI0933-like protein;
145-180 2.25e-05

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 46.81  E-value: 2.25e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1120505585 145 KKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIG 180
Cdd:pfam03486   1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
146-189 2.26e-05

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 46.44  E-value: 2.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1120505585 146 KVAVVGSGPAGLAAAQQLTRAGHMVTVFERAD-------RIGGLLRYGIPE 189
Cdd:COG0665     4 DVVVIGGGIAGLSTAYHLARRGLDVTVLERGRpgsgasgRNAGQLRPGLAA 54
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
153-242 4.17e-05

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 45.34  E-value: 4.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 153 GPAGLAAAQQLTRAGHMVTVFERADRI------GGLLRYGIPEFKM--EKRHIDRRLDQMnseGTVFKTGVNVGVDITAD 224
Cdd:COG0644     2 GPAGSAAARRLARAGLSVLLLEKGSFPgdkicgGGLLPRALEELEPlgLDEPLERPVRGA---RFYSPGGKSVELPPGRG 78
                          90       100
                  ....*....|....*....|..
gi 1120505585 225 A----LREQFDAvVLAGGATEA 242
Cdd:COG0644    79 GgyvvDRARFDR-WLAEQAEEA 99
PLN02268 PLN02268
probable polyamine oxidase
147-181 4.93e-05

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 45.45  E-value: 4.93e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1120505585 147 VAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGG 181
Cdd:PLN02268    3 VIVIGGGIAGIAAARALHDASFKVTLLESRDRIGG 37
FAD_oxidored pfam12831
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ...
147-183 8.62e-05

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


Pssm-ID: 432816 [Multi-domain]  Cd Length: 420  Bit Score: 44.91  E-value: 8.62e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1120505585 147 VAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGGLL 183
Cdd:pfam12831   2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGML 38
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
145-238 9.91e-05

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 44.78  E-value: 9.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 145 KKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGGLL-----RYGIPEFkmeKRHIDRRLDQMNSEGTVFKTGVNVGV 219
Cdd:PRK06292  170 KSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEdpevsKQAQKIL---SKEFKIKLGAKVTSVEKSGDEKVEEL 246
                          90
                  ....*....|....*....
gi 1120505585 220 DITADALREQFDAVVLAGG 238
Cdd:PRK06292  247 EKGGKTETIEADYVLVATG 265
PRK07588 PRK07588
FAD-binding domain;
145-186 1.54e-04

FAD-binding domain;


Pssm-ID: 169028 [Multi-domain]  Cd Length: 391  Bit Score: 43.96  E-value: 1.54e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1120505585 145 KKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRigglLRYG 186
Cdd:PRK07588    1 MKVAISGAGIAGPTLAYWLRRYGHEPTLIERAPE----LRTG 38
PRK06116 PRK06116
glutathione reductase; Validated
283-455 1.69e-04

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 43.99  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 283 KKVVIIGGGDTGADCLGTSHRQGAEsVHQFeimprppeTRAeHTPWPTYPLMYR---VASAHEEGGERLFSVNTERFV-G 358
Cdd:PRK06116  168 KRVAVVGAGYIAVEFAGVLNGLGSE-THLF--------VRG-DAPLRGFDPDIRetlVEEMEKKGIRLHTNAVPKAVEkN 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 359 ADGKVTalkaheVEMKSGRfekvegsdfELEADLVLLAMGFVgPEKPGL-LTDLGVDLNERGNVARSAKWATNVDGVFVA 437
Cdd:PRK06116  238 ADGSLT------LTLEDGE---------TLTVDCLIWAIGRE-PNTDGLgLENAGVKLNEKGYIIVDEYQNTNVPGIYAV 301
                         170
                  ....*....|....*...
gi 1120505585 438 GDMGRGQSLIVWAIAEGR 455
Cdd:PRK06116  302 GDVTGRVELTPVAIAAGR 319
carotene-cycl TIGR01790
lycopene cyclase family protein; This family includes lycopene beta and epsilion cyclases ...
147-191 1.77e-04

lycopene cyclase family protein; This family includes lycopene beta and epsilion cyclases (which form beta and delta carotene, respectively) from bacteria and plants as well as the plant capsanthin/capsorubin and neoxanthin cyclases which appear to have evolved from the plant lycopene cyclases. The plant lycopene epsilon cyclases also transform neurosporene to alpha zeacarotene.


Pssm-ID: 130850 [Multi-domain]  Cd Length: 388  Bit Score: 43.57  E-value: 1.77e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1120505585 147 VAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGGLLRYGI--PEFK 191
Cdd:TIGR01790   2 LAVIGGGPAGLAIALELARPGLRVQLIEPHPPIPGNHTYGVwdDDLS 48
PLN00093 PLN00093
geranylgeranyl diphosphate reductase; Provisional
146-205 2.01e-04

geranylgeranyl diphosphate reductase; Provisional


Pssm-ID: 177713 [Multi-domain]  Cd Length: 450  Bit Score: 43.59  E-value: 2.01e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1120505585 146 KVAVVGSGPAGLAAAQQLTRAGHMVTVFER----ADRIGGllryGIP-----EFKMEKRHIDRRLDQMN 205
Cdd:PLN00093   41 RVAVIGGGPAGACAAETLAKGGIETFLIERkldnAKPCGG----AIPlcmvgEFDLPLDIIDRKVTKMK 105
PRK13977 PRK13977
myosin-cross-reactive antigen; Provisional
131-181 2.23e-04

myosin-cross-reactive antigen; Provisional


Pssm-ID: 237575  Cd Length: 576  Bit Score: 43.66  E-value: 2.23e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1120505585 131 EGWVKPVHPTRSTGKKVAVVGSGPAGLAAAQQLTRAGHM----VTVFERADRIGG 181
Cdd:PRK13977    9 EAFARPRKPEGVDNKKAYIIGSGLASLAAAVFLIRDGQMpgenITILEELDVPGG 63
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
143-240 2.60e-04

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 43.21  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 143 TGKKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRI---------GGLLRygipefkmeKRHIDRrldqmnseGTVFKT 213
Cdd:COG1251   141 PGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLlprqldeeaGALLQ---------RLLEAL--------GVEVRL 203
                          90       100
                  ....*....|....*....|....*..
gi 1120505585 214 GVNVgVDITADalrEQFDAVVLAGGAT 240
Cdd:COG1251   204 GTGV-TEIEGD---DRVTGVRLADGEE 226
FMO-like pfam00743
Flavin-binding monooxygenase-like; This family includes FMO proteins, cyclohexanone ...
144-185 3.86e-04

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: 42.84  E-value: 3.86e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1120505585 144 GKKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGGLLRY 185
Cdd:pfam00743   1 AKKVAVIGAGVSGLASIKCCLEEGLEPTCFERSDDIGGLWRF 42
PRK08163 PRK08163
3-hydroxybenzoate 6-monooxygenase;
142-180 3.92e-04

3-hydroxybenzoate 6-monooxygenase;


Pssm-ID: 181262 [Multi-domain]  Cd Length: 396  Bit Score: 42.72  E-value: 3.92e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1120505585 142 STGKKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIG 180
Cdd:PRK08163    2 TKVTPVLIVGGGIGGLAAALALARQGIKVKLLEQAAEIG 40
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
147-182 4.25e-04

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 42.86  E-value: 4.25e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1120505585 147 VAVVGSGPAGLAAAQQLTRAGHMVTVFER--ADRIGGL 182
Cdd:COG3573     8 VIVVGAGLAGLVAAAELADAGRRVLLLDQepEANLGGQ 45
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
147-461 4.27e-04

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 42.83  E-value: 4.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 147 VAVVGSGPAGLAAAQQLTRAGHMVTVFERADrIGG------------LLR-------------YGI----PEFKMEK--R 195
Cdd:PRK06416    7 VIVIGAGPGGYVAAIRAAQLGLKVAIVEKEK-LGGtclnrgcipskaLLHaaeradearhsedFGIkaenVGIDFKKvqE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 196 HIDRRLDQMNS--EGTVFKTGVN-------------VGVDITADALREQFDAVVLAGGAteaRDLPIPGRELDG--IH-- 256
Cdd:PRK06416   86 WKNGVVNRLTGgvEGLLKKNKVDiirgeaklvdpntVRVMTEDGEQTYTAKNIILATGS---RPRELPGIEIDGrvIWts 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 257 -QAM--EFLPianrvqlgdleeptitaegKKVVIIGGGDTGADcLGTSHRQ-GAEsVHQFEIMPR--PPETRAehtpwpt 330
Cdd:PRK06416  163 dEALnlDEVP-------------------KSLVVIGGGYIGVE-FASAYASlGAE-VTIVEALPRilPGEDKE------- 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 331 yplMYRVAsaheeggERLFS-----VNTERFV-----GADG-KVTALKAHEVEmksgrfekvegsdfELEADLVLLAMGf 399
Cdd:PRK06416  215 ---ISKLA-------ERALKkrgikIKTGAKAkkveqTDDGvTVTLEDGGKEE--------------TLEADYVLVAVG- 269
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1120505585 400 VGPEKPGL-LTDLGVDLnERGNVARSAKWATNVDGVFVAGDMGRGQSLIVWAIAEGRSAAAAV 461
Cdd:PRK06416  270 RRPNTENLgLEELGVKT-DRGFIEVDEQLRTNVPNIYAIGDIVGGPMLAHKASAEGIIAAEAI 331
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
147-181 4.73e-04

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


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 42.51  E-value: 4.73e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1120505585 147 VAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGG 181
Cdd:COG1053     6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
PRK06753 PRK06753
hypothetical protein; Provisional
146-179 6.49e-04

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 41.98  E-value: 6.49e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1120505585 146 KVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRI 179
Cdd:PRK06753    2 KIAIIGAGIGGLTAAALLQEQGHEVKVFEKNESV 35
PRK08243 PRK08243
4-hydroxybenzoate 3-monooxygenase; Validated
146-240 7.83e-04

4-hydroxybenzoate 3-monooxygenase; Validated


Pssm-ID: 236198 [Multi-domain]  Cd Length: 392  Bit Score: 41.71  E-value: 7.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 146 KVAVVGSGPAGLAAAQQLTRAGHMVTVFERADR--IGGLLRYGIPEFK----MEKRHIDRRLDQmnsEGTvfktgVNVGV 219
Cdd:PRK08243    4 QVAIIGAGPAGLLLGQLLHLAGIDSVVLERRSReyVEGRIRAGVLEQGtvdlLREAGVGERMDR---EGL-----VHDGI 75
                          90       100
                  ....*....|....*....|.
gi 1120505585 220 DITADALREQFDAVVLAGGAT 240
Cdd:PRK08243   76 ELRFDGRRHRIDLTELTGGRA 96
PRK07251 PRK07251
FAD-containing oxidoreductase;
145-238 8.74e-04

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 41.66  E-value: 8.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 145 KKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIggLLRYGIPEFKMEKRHidrrldqMNSEGTVFKTGVNVG------ 218
Cdd:PRK07251  158 ERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTI--LPREEPSVAALAKQY-------MEEDGITFLLNAHTTevkndg 228
                          90       100
                  ....*....|....*....|..
gi 1120505585 219 --VDITADALREQFDAVVLAGG 238
Cdd:PRK07251  229 dqVLVVTEDETYRFDALLYATG 250
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
147-184 1.05e-03

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


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 41.43  E-value: 1.05e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1120505585 147 VAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGGLLR 184
Cdd:PRK06183   13 VVIVGAGPVGLTLANLLGQYGVRVLVLERWPTLYDLPR 50
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
147-181 1.15e-03

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


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 41.12  E-value: 1.15e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1120505585 147 VAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGG 181
Cdd:pfam00890   2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGG 36
PLN02487 PLN02487
zeta-carotene desaturase
135-181 1.18e-03

zeta-carotene desaturase


Pssm-ID: 215268 [Multi-domain]  Cd Length: 569  Bit Score: 41.32  E-value: 1.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1120505585 135 KPVHPtRSTGKKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGG 181
Cdd:PLN02487   67 EPEAY-KGPKLKVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGG 112
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
139-180 1.19e-03

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


Pssm-ID: 234978 [Multi-domain]  Cd Length: 662  Bit Score: 41.37  E-value: 1.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1120505585 139 PTRSTGKKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIG 180
Cdd:PRK01747  255 PGSPKARDAAIIGGGIAGAALALALARRGWQVTLYEADEAPA 296
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
145-474 1.24e-03

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 41.06  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 145 KKVAVVGSGPAGLAAA-----QQLTRAGHMVT-----VFERADRIGGLL-------RYGIPEFKMEKRHIDRRLDQmnse 207
Cdd:PRK09754    4 KTIIIVGGGQAAAMAAaslrqQGFTGELHLFSderhlPYERPPLSKSMLledspqlQQVLPANWWQENNVHLHSGV---- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 208 gTVFKTGVNVGVDITADALREQFDAVVLAGGAtEARDLPIpgreLDGIHQAMEFLPIANRVQlgDLEEptITAEGKKVVI 287
Cdd:PRK09754   80 -TIKTLGRDTRELVLTNGESWHWDQLFIATGA-AARPLPL----LDALGERCFTLRHAGDAA--RLRE--VLQPERSVVI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 288 IGGGDTGADCLGTSHRQGAeSVHQFE----IMPR--PPetraehtpwptyPLMYRVASAHEEGGERLFsVNTErfvgadg 361
Cdd:PRK09754  150 VGAGTIGLELAASATQRRC-KVTVIElaatVMGRnaPP------------PVQRYLLQRHQQAGVRIL-LNNA------- 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 362 KVTALKAHEVEMKSGRFEKVEGsdfeleaDLVLLAMGFVGPEK----PGLLTDLGVDLNERGNVARSAkwatnvdgVFVA 437
Cdd:PRK09754  209 IEHVVDGEKVELTLQSGETLQA-------DVVIYGIGISANDQlareANLDTANGIVIDEACRTCDPA--------IFAG 273
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1120505585 438 GDM-------GRGQSLIVWAIAEgRSAAAAVDAYLEGESALPSP 474
Cdd:PRK09754  274 GDVaitrldnGALHRCESWENAN-NQAQIAAAAMLGLPLPLLPP 316
YdhS COG4529
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
145-333 1.27e-03

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


Pssm-ID: 443597 [Multi-domain]  Cd Length: 466  Bit Score: 41.09  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 145 KKVAVVGSGPAGLAAAQQLTRAGHM---VTVFERADRIGGLLRYG--------------IPEFKMEKRH----------- 196
Cdd:COG4529     6 KRIAIIGGGASGTALAIHLLRRAPEplrITLFEPRPELGRGVAYStdspehllnvpagrMSAFPDDPDHflrwlrengar 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 197 ----------IDRRL------DQMNSEGTVFKTGVNV---------------GVDI-TADALREQFDAVVLAGGATEARD 244
Cdd:COG4529    86 aapaidpdafVPRRLfgeylrERLAEALARAPAGVRLrhiraevvdlerddgGYRVtLADGETLRADAVVLATGHPPPAP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 245 LPIPGRELDGIhqameflpIANRVQLGDLEEptiTAEGKKVVIIGGGDTGADCLGTSHRQGaesvHQFEIMP-----RPP 319
Cdd:COG4529   166 PPGLAAGSPRY--------IADPWPPGALAR---IPPDARVLIIGTGLTAIDVVLSLAARG----HRGPITAlsrrgLLP 230
                         250
                  ....*....|....
gi 1120505585 320 ETRAEHTPWPTYPL 333
Cdd:COG4529   231 RAHPPGAPLPLKFL 244
PLN02529 PLN02529
lysine-specific histone demethylase 1
139-181 1.66e-03

lysine-specific histone demethylase 1


Pssm-ID: 178144 [Multi-domain]  Cd Length: 738  Bit Score: 41.03  E-value: 1.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1120505585 139 PTRSTGKKVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGG 181
Cdd:PLN02529  155 PEEGTEGSVIIVGAGLAGLAAARQLLSFGFKVVVLEGRNRPGG 197
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
388-458 1.78e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 40.68  E-value: 1.78e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1120505585 388 LEADLVLLAMGFVgPEKPGLLTD-LGVDLNERGNVARSAKWATNVDGVFVAGDMGRGQSLIVWAIAEGRSAA 458
Cdd:PRK06327  271 LEVDKLIVSIGRV-PNTDGLGLEaVGLKLDERGFIPVDDHCRTNVPNVYAIGDVVRGPMLAHKAEEEGVAVA 341
PRK07236 PRK07236
hypothetical protein; Provisional
140-176 2.20e-03

hypothetical protein; Provisional


Pssm-ID: 235980 [Multi-domain]  Cd Length: 386  Bit Score: 40.29  E-value: 2.20e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1120505585 140 TRSTGKKVAVVGSGPAGLAAAQQLTRAGHMVTVFERA 176
Cdd:PRK07236    2 THMSGPRAVVIGGSLGGLFAALLLRRAGWDVDVFERS 38
PRK00711 PRK00711
D-amino acid dehydrogenase;
146-178 2.41e-03

D-amino acid dehydrogenase;


Pssm-ID: 234819 [Multi-domain]  Cd Length: 416  Bit Score: 40.17  E-value: 2.41e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1120505585 146 KVAVVGSGPAGLAAAQQLTRAGHMVTVFERADR 178
Cdd:PRK00711    2 RVVVLGSGVIGVTSAWYLAQAGHEVTVIDRQPG 34
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
145-181 2.50e-03

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: 40.20  E-value: 2.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1120505585 145 KKVAVVGSGPAGLAAAQQLTR----AGHMVTVFERADRIGG 181
Cdd:TIGR00562   3 KHVVIIGGGISGLCAAYYLEKeipeLPVELTLVEASDRVGG 43
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
146-175 3.18e-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: 39.62  E-value: 3.18e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1120505585 146 KVAVVGSGPAGLAAAQQLTRAGHMVTVFER 175
Cdd:pfam01494   3 DVLIVGGGPAGLMLALLLARAGVRVVLVER 32
PLN02328 PLN02328
lysine-specific histone demethylase 1 homolog
147-184 3.18e-03

lysine-specific histone demethylase 1 homolog


Pssm-ID: 215187 [Multi-domain]  Cd Length: 808  Bit Score: 39.98  E-value: 3.18e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1120505585 147 VAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIGGLLR 184
Cdd:PLN02328  241 VVVVGAGLAGLVAARQLLSMGFKVVVLEGRARPGGRVK 278
PRK09126 PRK09126
FAD-dependent hydroxylase;
147-176 4.45e-03

FAD-dependent hydroxylase;


Pssm-ID: 236385 [Multi-domain]  Cd Length: 392  Bit Score: 39.15  E-value: 4.45e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1120505585 147 VAVVGSGPAGLAAAQQLTRAGHMVTVFERA 176
Cdd:PRK09126    6 IVVVGAGPAGLSFARSLAGSGLKVTLIERQ 35
PLN02463 PLN02463
lycopene beta cyclase
139-172 4.56e-03

lycopene beta cyclase


Pssm-ID: 178082 [Multi-domain]  Cd Length: 447  Bit Score: 39.31  E-value: 4.56e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1120505585 139 PTRSTGKKVAVVGSGPAGLAAAQQLTRAGHMVTV 172
Cdd:PLN02463   23 PSKSRVVDLVVVGGGPAGLAVAQQVSEAGLSVCC 56
PRK08132 PRK08132
FAD-dependent oxidoreductase; Provisional
146-180 4.67e-03

FAD-dependent oxidoreductase; Provisional


Pssm-ID: 236158 [Multi-domain]  Cd Length: 547  Bit Score: 39.47  E-value: 4.67e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1120505585 146 KVAVVGSGPAGLAAAQQLTRAGHMVTVFERADRIG 180
Cdd:PRK08132   25 PVVVVGAGPVGLALAIDLAQQGVPVVLLDDDDTLS 59
PRK06370 PRK06370
FAD-containing oxidoreductase;
148-238 8.12e-03

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 38.64  E-value: 8.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120505585 148 AVVGSGPAGLAAAQQLTRAGHMVTVFERADRIggllrygIPEF----------KMEKRHIDRRLDQMNSEGTVFKTGVNV 217
Cdd:PRK06370  175 VIIGGGYIGLEFAQMFRRFGSEVTVIERGPRL-------LPREdedvaaavreILEREGIDVRLNAECIRVERDGDGIAV 247
                          90       100
                  ....*....|....*....|.
gi 1120505585 218 GVDITADALREQFDAVVLAGG 238
Cdd:PRK06370  248 GLDCNGGAPEITGSHILVAVG 268
 
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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