|
Name |
Accession |
Description |
Interval |
E-value |
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
1-481 |
0e+00 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 752.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 1 MGEFKGFMKYDKQYLGELSLVDRLKHHKAYQQRFTKEDASIQGARCMDCGTPFCQTGqqygretigCPIGNYIPEWNDLV 80
Cdd:PRK12810 1 MGKPTGFLEYDRVDPKKRPVAERIKDFKEFYEPFSEEQAKIQAARCMDCGIPFCHWG---------CPVHNYIPEWNDLV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 81 YHQDFKTAYERLSETNNFPDFTGRVCPAPCESACVMKINRESIAIKGIERTIIDEAFENGWVAPKVPSRRRDEKVAIVGS 160
Cdd:PRK12810 72 YRGRWEEAAERLHQTNNFPEFTGRVCPAPCEGACTLNINFGPVTIKNIERYIIDKAFEEGWVKPDPPVKRTGKKVAVVGS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 161 GPAGLTAAEELNLLGYQVTIYERARESGGLLMYGIPNMKLDKDVVRRRIKLMEEAGITFINGVEVGVDIDKATLESEYDA 240
Cdd:PRK12810 152 GPAGLAAADQLARAGHKVTVFERADRIGGLLRYGIPDFKLEKEVIDRRIELMEAEGIEFRTNVEVGKDITAEELLAEYDA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 241 IILCTGAQKGRDLPLEGRMGDGIHFAMDYLTEQTQLLNGEIDDITITAKDKNVIIIGAGDTGADCVATALRENCKSIVQF 320
Cdd:PRK12810 232 VFLGTGAYKPRDLGIPGRDLDGVHFAMDFLIQNTRRVLGDETEPFISAKGKHVVVIGGGDTGMDCVGTAIRQGAKSVTQR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 321 NKYTKLPEAItfTENASWPLAMPVFKMDYAHQEYeakfgkEPRAYGVQTMRYDVDDkGHIRGLYTQILEQGENGMVMKEG 400
Cdd:PRK12810 312 DIMPMPPSRR--NKNNPWPYWPMKLEVSNAHEEG------VEREFNVQTKEFEGEN-GKVTGVKVVRTELGEGDFEPVEG 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 401 PERFWPADLVLLSIGFEGTEPTVPNAFNIKTD-RNRIVADDTNYQTNNEKVFAAGDARRGQSLVVWAIKEGRGVAKAVDQ 479
Cdd:PRK12810 383 SEFVLPADLVLLAMGFTGPEAGLLAQFGVELDeRGRVAAPDNAYQTSNPKVFAAGDMRRGQSLVVWAIAEGRQAARAIDA 462
|
..
gi 446425735 480 YL 481
Cdd:PRK12810 463 YL 464
|
|
| GOGAT_sm_gam |
TIGR01317 |
glutamate synthases, NADH/NADPH, small subunit; This model represents one of three built for ... |
6-481 |
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: 605.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 6 GFMKYDKQYLGELSLVDRLKHHKAYQQRFTKEDASIQGARCMDCGTPFCQTgqqygreTIGCPIGNYIPEWNDLVYHQDF 85
Cdd:TIGR01317 4 GFLEYKRRKPTERDPRTRLKDWKEFTNPFDKESAKYQAARCMDCGTPFCHN-------DSGCPLNNLIPEFNDLVFRGRW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 86 KTAYERLSETNNFPDFTGRVCPAPCESACVMKINRESIAIKGIERTIIDEAFENGWVAPKVPSRRRDEKVAIVGSGPAGL 165
Cdd:TIGR01317 77 KEALDRLHATNNFPEFTGRVCPAPCEGACTLGISEDPVGIKSIERIIIDKGFQEGWVQPRPPSKRTGKKVAVVGSGPAGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 166 TAAEELNLLGYQVTIYERARESGGLLMYGIPNMKLDKDVVRRRIKLMEEAGITFINGVEVGVDIDKATLESEYDAIILCT 245
Cdd:TIGR01317 157 AAADQLNRAGHTVTVFEREDRCGGLLMYGIPNMKLDKAIVDRRIDLLSAEGIDFVTNTEIGVDISADELKEQFDAVVLAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 246 GAQKGRDLPLEGRMGDGIHFAMDYLTEQTQLLNGE--IDDITITAKDKNVIIIGAGDTGADCVATALRENCKSIVQFNKY 323
Cdd:TIGR01317 237 GATKPRDLPIPGRELKGIHYAMEFLPSATKALLGKdfKDIIFIKAKGKKVVVIGGGDTGADCVGTSLRHGAASVHQFEIM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 324 TKLPEAitFTENASWPLAMPVFKMDYAHQEYEAKFGKEPRAYGVQTMRYDVDDKGHIRGLYTQILE-----QGENGMVMK 398
Cdd:TIGR01317 317 PKPPEA--RAKDNPWPEWPRVYRVDYAHEEAAAHYGRDPREYSILTKEFIGDDEGKVTALRTVRVEwkksqDGKWQFVEI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 399 EGPERFWPADLVLLSIGFEGTEPTVPNAFNI-KTDRNRIVADDTNYQTNNEKVFAAGDARRGQSLVVWAIKEGRGVAKAV 477
Cdd:TIGR01317 395 PGSEEVFEADLVLLAMGFVGPEQILLDDFGVkKTRRGNISAGYDDYSTSIPGVFAAGDCRRGQSLIVWAINEGRKAAAAV 474
|
....
gi 446425735 478 DQYL 481
Cdd:TIGR01317 475 DRYL 478
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
23-480 |
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: 553.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 23 RLKHHKAYQQRFTKEDASIQGARCMDCGTPFCQTGqqygretigCPIGNYIPEWNDLVYHQDFKTAYERLSETNNFPDFT 102
Cdd:COG0493 1 RIKDFREVYPGLSEEEAIEQAARCLDCGDPPCQTG---------CPVGNDIPEWIRLIAEGDYEEALELIHETNPFPEVC 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 103 GRVCPAPCESACVMKINRESIAIKGIERTIIDEAFENGWVAPKVPSRRRDEKVAIVGSGPAGLTAAEELNLLGYQVTIYE 182
Cdd:COG0493 72 GRVCPAPCEGACVRGIVDEPVAIGALERFIADKAFEEGWVKPPPPAPRTGKKVAVVGSGPAGLAAAYQLARAGHEVTVFE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 183 RARESGGLLMYGIPNMKLDKDVVRRRIKLMEEAGITFINGVEVGVDIDKATLESEYDAIILCTGAQKGRDLPLEGRMGDG 262
Cdd:COG0493 152 ALDKPGGLLRYGIPEFRLPKDVLDREIELIEALGVEFRTNVEVGKDITLDELLEEFDAVFLATGAGKPRDLGIPGEDLKG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 263 IHFAMDYLTEQtqllNGEIDDITITAKDKNVIIIGAGDTGADCVATALRENCKSIVQFNKYTKlpeaitftENaswplaM 342
Cdd:COG0493 232 VHSAMDFLTAV----NLGEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTR--------EE------M 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 343 P--VFKMDYAHQEyeakfGKEpRAYGVQTMRYDVDDKGHIRGL---YTQILEQGENG---MVMKEGPERFWPADLVLLSI 414
Cdd:COG0493 294 PasKEEVEEALEE-----GVE-FLFLVAPVEIIGDENGRVTGLecvRMELGEPDESGrrrPVPIEGSEFTLPADLVILAI 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446425735 415 GFEGTEPTVPNAFNIKTD-RNRIVADDTNYQTNNEKVFAAGDARRGQSLVVWAIKEGRGVAKAVDQY 480
Cdd:COG0493 368 GQTPDPSGLEEELGLELDkRGTIVVDEETYQTSLPGVFAGGDAVRGPSLVVWAIAEGRKAARAIDRY 434
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
5-484 |
2.78e-130 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 385.30 E-value: 2.78e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 5 KGFMKYDKQYLGELSLVDRLKHHKAYQQRFTKEDASIQGARCMDCGTPFCQTGqqygretigCPIGNYIPEWNDLVYHQD 84
Cdd:PRK11749 1 LKFLTTPRIPMPRQDAEERAQNFDEVAPGYTPEEAIEEASRCLQCKDAPCVKA---------CPVSIDIPEFIRLIAEGN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 85 FKTAYERLSETNNFPDFTGRVCPAP--CESACVMKINRESIAIKGIERTIIDEAFENGWVAPKVPsRRRDEKVAIVGSGP 162
Cdd:PRK11749 72 LKGAAETILETNPLPAVCGRVCPQErlCEGACVRGKKGEPVAIGRLERYITDWAMETGWVLFKRA-PKTGKKVAVIGAGP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 163 AGLTAAEELNLLGYQVTIYERARESGGLLMYGIPNMKLDKDVVRRRIKLMEEAGITFINGVEVGVDIDKATLESEYDAII 242
Cdd:PRK11749 151 AGLTAAHRLARKGYDVTIFEARDKAGGLLRYGIPEFRLPKDIVDREVERLLKLGVEIRTNTEVGRDITLDELRAGYDAVF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 243 LCTGAQKGRDLPLEGRMGDGIHFAMDYLTEQTQLlngeiDDITITAKDKNVIIIGAGDTGADCVATALRENCKS--IVqf 320
Cdd:PRK11749 231 IGTGAGLPRFLGIPGENLGGVYSAVDFLTRVNQA-----VADYDLPVGKRVVVIGGGNTAMDAARTAKRLGAESvtIV-- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 321 nkYTKLPEAITftenASWplampvFKMDYAHQEyeakfgkeprayGV------QTMRYDVDDKGH--IRGLYTQILEQGE 392
Cdd:PRK11749 304 --YRRGREEMP----ASE------EEVEHAKEE------------GVefewlaAPVEILGDEGRVtgVEFVRMELGEPDA 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 393 NG--MVMKEGPERFWPADLVLLSIGFEGTEPTVPNAFNIKTDRNR-IVADDTNYQTNNEKVFAAGDARRGQSLVVWAIKE 469
Cdd:PRK11749 360 SGrrRVPIEGSEFTLPADLVIKAIGQTPNPLILSTTPGLELNRWGtIIADDETGRTSLPGVFAGGDIVTGAATVVWAVGD 439
|
490
....*....|....*
gi 446425735 470 GRGVAKAVDQYLASK 484
Cdd:PRK11749 440 GKDAAEAIHEYLEGA 454
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
51-482 |
5.22e-81 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 261.73 E-value: 5.22e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 51 TPFCQTGqqygretigCPIGNYIPEWNDLVYHQDFKTAYERLSETNNFPDFTGRVCPAPCESACvmkiNR----ESIAIK 126
Cdd:PRK12771 46 TPPCNAA---------CPAGEDIRGWLALVRGGDYEYAWRRLTKDNPFPAVMGRVCYHPCESGC----NRgqvdDAVGIN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 127 GIERTIIDEAFENGWVAPKvPSRRRDEKVAIVGSGPAGLTAAEELNLLGYQVTIYERARESGGLLMYGIPNMKLDKDVVR 206
Cdd:PRK12771 113 AVERFLGDYAIANGWKFPA-PAPDTGKRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRYGIPAYRLPREVLD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 207 RRIKLMEEAGITFINGVEVGVDIDKATLESEYDAIILCTGAQKGRDLPLEGRMGDGIHFAMDYLteqTQLLNGEIDDIti 286
Cdd:PRK12771 192 AEIQRILDLGVEVRLGVRVGEDITLEQLEGEFDAVFVAIGAQLGKRLPIPGEDAAGVLDAVDFL---RAVGEGEPPFL-- 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 287 takDKNVIIIGAGDTGADCVATALRENCKSIVqfnkytklpeaITFtenaswplAMPVFKMDYAHQEYEakfgkEPRAYG 366
Cdd:PRK12771 267 ---GKRVVVIGGGNTAMDAARTARRLGAEEVT-----------IVY--------RRTREDMPAHDEEIE-----EALREG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 367 VQTM------RYDVDDKGHIRGLYTQ--ILEQGENGM-VMKEGPERFWPADLVLLSIG----FEGTEptvpNAFNIKTDR 433
Cdd:PRK12771 320 VEINwlrtpvEIEGDENGATGLRVITveKMELDEDGRpSPVTGEEETLEADLVVLAIGqdidSAGLE----SVPGVEVGR 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 446425735 434 NRIVADDTNYQTNNEKVFAAGDARRGQSLVVWAIKEGRGVAKAVDQYLA 482
Cdd:PRK12771 396 GVVQVDPNFMMTGRPGVFAGGDMVPGPRTVTTAIGHGKKAARNIDAFLG 444
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
18-484 |
4.47e-76 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 251.20 E-value: 4.47e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 18 LSLVDRLKHHKAYQQRFTKEDASIQGARCMDCGT-PFCQTGqqygretigCPIGNYIPEWNDLVYHQDFKTAYERLSETN 96
Cdd:PRK12769 199 LAIEARKTGFDEIYLPFRADQAQREASRCLKCGEhSICEWT---------CPLHNHIPQWIELVKAGNIDAAVELSHQTN 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 97 NFPDFTGRVCPAP--CESACVMKINRESIAIKGIERTIIDEAFENGWVAPKVPSRRRDEKVAIVGSGPAGLTAAEELNLL 174
Cdd:PRK12769 270 SLPEITGRVCPQDrlCEGACTLRDEYGAVTIGNIERYISDQALAKGWRPDLSQVTKSDKRVAIIGAGPAGLACADVLARN 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 175 GYQVTIYERARESGGLLMYGIPNMKLDKDVVRRRIKLMEEAGITFINGVEVGVDIDKATLESEYDAIILCTGAQKGRDLP 254
Cdd:PRK12769 350 GVAVTVYDRHPEIGGLLTFGIPAFKLDKSLLARRREIFSAMGIEFELNCEVGKDISLESLLEDYDAVFVGVGTYRSMKAG 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 255 LEGRMGDGIHFAMDYL---TEQTQLLNGEIDDITITAKDKNVIIIGAGDTGADCVATALRENCKSIVqfNKYTKlPEAit 331
Cdd:PRK12769 430 LPNEDAPGVYDALPFLianTKQVMGLEELPEEPFINTAGLNVVVLGGGDTAMDCVRTALRHGASNVT--CAYRR-DEA-- 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 332 ftenaswplAMPVFKMdyahqeyEAKFGKEPRA---YGVQTMRYDVDDKGH---IRGLYTQILE---QGENGMVMKEGPE 402
Cdd:PRK12769 505 ---------NMPGSKK-------EVKNAREEGAnfeFNVQPVALELNEQGHvcgIRFLRTRLGEpdaQGRRRPVPIPGSE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 403 RFWPADLVLLSIGFEGTEPTVPNAFNIKTDR-NRIVADDTN---YQTNNEKVFAAGDARRGQSLVVWAIKEGRGVAKAVD 478
Cdd:PRK12769 569 FVMPADAVIMAFGFNPHGMPWLESHGVTVDKwGRIIADVESqyrYQTSNPKIFAGGDAVRGADLVVTAMAEGRHAAQGII 648
|
....*.
gi 446425735 479 QYLASK 484
Cdd:PRK12769 649 DWLGVK 654
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
34-484 |
1.30e-75 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 244.93 E-value: 1.30e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 34 FTKEDASIQGARCMDCGTPFCQTGqqygretigCPIGNYIPEWNDLVYHQDFKTAYERLSETNNFPDFTGRVCP--APCE 111
Cdd:PRK12831 30 YNEEEAVKEASRCLQCKKPKCVKG---------CPVSINIPGFISKLKEGDFEEAAKIIAKYNALPAVCGRVCPqeSQCE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 112 SACVMKINRESIAIKGIERTIIDEAFENGwVAPKVPSRRRDEKVAIVGSGPAGLTAAEELNLLGYQVTIYERARESGGLL 191
Cdd:PRK12831 101 GKCVLGIKGEPVAIGKLERFVADWARENG-IDLSETEEKKGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGGVL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 192 MYGIPNMKLDKD-VVRRRIKLMEEAGITFINGVEVG--VDIDKATLESEYDAIILCTGAQKGRDLPLEGRMGDGIHFAMD 268
Cdd:PRK12831 180 VYGIPEFRLPKEtVVKKEIENIKKLGVKIETNVVVGktVTIDELLEEEGFDAVFIGSGAGLPKFMGIPGENLNGVFSANE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 269 YLTeQTQLLNGEIDDI-TITAKDKNVIIIGAGDTGADCVATALRENCKSIVQFNKytklpeaitfTENaswplAMPVFKM 347
Cdd:PRK12831 260 FLT-RVNLMKAYKPEYdTPIKVGKKVAVVGGGNVAMDAARTALRLGAEVHIVYRR----------SEE-----ELPARVE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 348 DYAHQEYEA-KFgkeprAYGVQTMRYDVDDKGHIRGLYTQILEQGE------NGMVMKEGPERFWPADLVLLSIGfEGTE 420
Cdd:PRK12831 324 EVHHAKEEGvIF-----DLLTNPVEILGDENGWVKGMKCIKMELGEpdasgrRRPVEIEGSEFVLEVDTVIMSLG-TSPN 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446425735 421 PTVPNAF-NIKTDRNR-IVADDTNYQTNNEKVFAAGDARRGQSLVVWAIKEGRGVAKAVDQYLASK 484
Cdd:PRK12831 398 PLISSTTkGLKINKRGcIVADEETGLTSKEGVFAGGDAVTGAATVILAMGAGKKAAKAIDEYLSKK 463
|
|
| gltA |
TIGR01316 |
glutamate synthase (NADPH), homotetrameric; This protein is homologous to the small subunit of ... |
22-481 |
7.88e-65 |
|
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: 216.27 E-value: 7.88e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 22 DRLKHHKAYQQRFTKEDASIQGARCMDCGtpfcqtgQQYGRETIGCPIGNYIPEWNDLVYHQDFKTAYERLSETNNFPDF 101
Cdd:TIGR01316 4 ERSKLFQEAALGYTEQLALVEAQRCLNCK-------DATKPCIKGCPVHVPIPEFIAKIQEGDFKGAVDIIKTTSLLPAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 102 TGRVCPAP--CESACVMKINRES----IAIKGIERTIIDEAFENGW--VAPKVPSRRRdeKVAIVGSGPAGLTAAEELNL 173
Cdd:TIGR01316 77 CGRVCPQErqCEGQCTVGKMFKDvgkpVSIGALERFVADWERQHGIetEPEKAPSTHK--KVAVIGAGPAGLACASELAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 174 LGYQVTIYERARESGGLLMYGIPNMKLDKDVVRRRIKLMEEAGITFINGVEVGVDIDKATLESEYDAIILCTGAQKGRDL 253
Cdd:TIGR01316 155 AGHSVTVFEALHKPGGVVTYGIPEFRLPKEIVVTEIKTLKKLGVTFRMNFLVGKTATLEELFSQYDAVFIGTGAGLPKLM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 254 PLEGRMGDGIHFAMDYLTEQTQLLNGEIDDI-TITAKDKNVIIIGAGDTGADCVATALRENCKSIVQfnkYTKLPEAITF 332
Cdd:TIGR01316 235 NIPGEELCGVYSANDFLTRANLMKAYEFPHAdTPVYAGKSVVVIGGGNTAVDSARTALRLGAEVHCL---YRRTREDMTA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 333 TENaswplampvfkmDYAHQEYEA-KFgkeprAYGVQTMRYDVDDKGHIRGL---YTQILEQGENG---MVMKEGPERFW 405
Cdd:TIGR01316 312 RVE------------EIAHAEEEGvKF-----HFLCQPVEIIGDEEGNVRAVkfrKMDCQEQIDSGerrFLPCGDAECKL 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446425735 406 PADLVLLSIGfEGTEPTVPNAFNIKTDRNRIVADDTNYQTNNEKVFAAGDARRGQSLVVWAIKEGRGVAKAVDQYL 481
Cdd:TIGR01316 375 EADAVIVAIG-NGSNPIMAETTRLKTSERGTIVVDEDQRTSIPGVFAGGDIILGAATVIRAMGQGKRAAKSINEYL 449
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
34-484 |
9.00e-64 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 220.38 E-value: 9.00e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 34 FTKEDASIQGARCMDCGTPFCQTGqqygretigCPIGNYIPEWNDLVYHQDFKTAYERLSETNNFPDFTGRVCP--APCE 111
Cdd:PRK12778 319 LTKEQAMTEAKRCLDCKNPGCVEG---------CPVGIDIPRFIKNIERGNFLEAAKILKETSALPAVCGRVCPqeKQCE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 112 SACV-MKINRESIAIKGIERTIIDEAFENGWVAPKVPSRRRDEKVAIVGSGPAGLTAAEELNLLGYQVTIYERARESGGL 190
Cdd:PRK12778 390 SKCIhGKMGEEAVAIGYLERFVADYERESGNISVPEVAEKNGKKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGGV 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 191 LMYGIPNMKLDKDVVRRRIKLMEEAGITFINGVEVGVDIDKATLESE-YDAIILCTGAQKGRDLPLEGRMGDGIHFAMDY 269
Cdd:PRK12778 470 LKYGIPEFRLPKKIVDVEIENLKKLGVKFETDVIVGKTITIEELEEEgFKGIFIASGAGLPNFMNIPGENSNGVMSSNEY 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 270 LTeQTQLLNGEIDDI-TITAKDKNVIIIGAGDTGADCVATALRENCKSIVQFnkYTKLPEaitftenaswplAMPVFKMD 348
Cdd:PRK12778 550 LT-RVNLMDAASPDSdTPIKFGKKVAVVGGGNTAMDSARTAKRLGAERVTIV--YRRSEE------------EMPARLEE 614
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 349 YAHQEYEakfgkeprayGVQTM------RYDVDDKGHIRGLYTQILEQGE---NGM---VMKEGPERFWPADLVLLSIGF 416
Cdd:PRK12778 615 VKHAKEE----------GIEFLtlhnpiEYLADEKGWVKQVVLQKMELGEpdaSGRrrpVAIPGSTFTVDVDLVIVSVGV 684
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446425735 417 EgTEPTVPNAF-NIKTDRNRIVADDTNYQTNNEKVFAAGDARRGQSLVVWAIKEGRGVAKAVDQYLASK 484
Cdd:PRK12778 685 S-PNPLVPSSIpGLELNRKGTIVVDEEMQSSIPGIYAGGDIVRGGATVILAMGDGKRAAAAIDEYLSSK 752
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
17-475 |
3.68e-63 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 216.43 E-value: 3.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 17 ELSLVDRLKHHKAYQQRFTKEDASIQGARCMDCGtpfcqtgqQYGRETIGCPIGNYIPEWNDLVYHQDFKTAYERLSETN 96
Cdd:PRK12809 181 KISASERKTHFGEIYCGLDPQQATYESDRCVYCA--------EKANCNWHCPLHNAIPDYIRLVQEGKIIEAAELCHQTS 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 97 NFPDFTGRVCPAP--CESACVMKINRESIAIKGIERTIIDEAFENGW---VAPKVPsrrRDEKVAIVGSGPAGLTAAEEL 171
Cdd:PRK12809 253 SLPEICGRVCPQDrlCEGACTLKDHSGAVSIGNLERYITDTALAMGWrpdVSKVVP---RSEKVAVIGAGPAGLGCADIL 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 172 NLLGYQVTIYERARESGGLLMYGIPNMKLDKDVVRRRIKLMEEAGITFINGVEVGVDIDKATLESEYDAIILCTGAQKGR 251
Cdd:PRK12809 330 ARAGVQVDVFDRHPEIGGMLTFGIPPFKLDKTVLSQRREIFTAMGIDFHLNCEIGRDITFSDLTSEYDAVFIGVGTYGMM 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 252 DLPLEGRMGDGIHFAMDYLTEQTQLLNG--EIDDITITA-KDKNVIIIGAGDTGADCVATALRENCKSIVQFNKYTKlpe 328
Cdd:PRK12809 410 RADLPHEDAPGVIQALPFLTAHTRQLMGlpESEEYPLTDvEGKRVVVLGGGDTTMDCLRTSIRLNAASVTCAYRRDE--- 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 329 aitftenaswpLAMPVFKMDYAHQEYEA-KFgkeprAYGVQTMRYDVDDKGHIRG---LYTQILEQGENGMVMKE---GP 401
Cdd:PRK12809 487 -----------VSMPGSRKEVVNAREEGvEF-----QFNVQPQYIACDEDGRLTAvglIRTAMGEPGPDGRRRPRpvaGS 550
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446425735 402 ERFWPADLVLLSIGFEGTEPTVPNAFNIKTDR-NRIVADDTNY---QTNNEKVFAAGDARRGQSLVVWAIKEGRGVAK 475
Cdd:PRK12809 551 EFELPADVLIMAFGFQAHAMPWLQGSGIKLDKwGLIQTGDVGYlptQTHLKKVFAGGDAVHGADLVVTAMAAGRQAAR 628
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
23-484 |
4.59e-55 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 193.83 E-value: 4.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 23 RLKHHKAYQQRFTKEDASIQGARCMDCGtpFCqtgqqygreTIGCPIGNYIPEWNDLVYHQDFKTAYERLSETNNFPDFT 102
Cdd:PRK13984 164 RVKSFIEIVKGYSKEQAMQEAARCVECG--IC---------TDTCPAHMDIPQYIKAIYKDDLEEGLRWLYKTNPLSMVC 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 103 GRVCPAPCESACVMKINRESIAIKGIERTIIDEAFENGWvaPKV---PSRRRDEKVAIVGSGPAGLTAAEELNLLGYQVT 179
Cdd:PRK13984 233 GRVCTHKCETVCSIGHRGEPIAIRWLKRYIVDNVPVEKY--SEIlddEPEKKNKKVAIVGSGPAGLSAAYFLATMGYEVT 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 180 IYERARESGGLLMYGIPNMKLDKDVVRRRIKLMEEAGITFINGVEVGVDIDKATLESEYDAIILCTGAQKGRDLPLEGRM 259
Cdd:PRK13984 311 VYESLSKPGGVMRYGIPSYRLPDEALDKDIAFIEALGVKIHLNTRVGKDIPLEELREKHDAVFLSTGFTLGRSTRIPGTD 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 260 GDGIHFAMDYLTEQTQLLNGEIDDITITakdKNVIIIGAGDTGADCVATALRencksiVQFNKYTKLPEAITFTENASwp 339
Cdd:PRK13984 391 HPDVIQALPLLREIRDYLRGEGPKPKIP---RSLVVIGGGNVAMDIARSMAR------LQKMEYGEVNVKVTSLERTF-- 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 340 LAMPVfKMDYAHQEYEAKFGKEPrAYGVQTMrydVDDKGHIRGLYTQIL-----EQGENGMVMKEGPERFWPADLVLLSI 414
Cdd:PRK13984 460 EEMPA-DMEEIEEGLEEGVVIYP-GWGPMEV---VIENDKVKGVKFKKCvevfdEEGRFNPKFDESDQIIVEADMVVEAI 534
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446425735 415 GFEGTEPTVPNAF--NIKTDRNRIVADDTNyQTNNEKVFAAGDARRGQSlVVWAIKEGRGVAKAVDQYLASK 484
Cdd:PRK13984 535 GQAPDYSYLPEELksKLEFVRGRILTNEYG-QTSIPWLFAGGDIVHGPD-IIHGVADGYWAAEGIDMYLRKQ 604
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
46-484 |
9.36e-52 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 185.70 E-value: 9.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 46 CMDCGTPfCQTGqqygretigCPIGNYIPEWNDLVYHQDFKTAYERLSETNNFPDFTGRVCPAPCESACVMKINRESIAI 125
Cdd:PRK12814 97 CGDCLGP-CELA---------CPAGCNIPGFIAAIARGDDREAIRIIKETIPLPGILGRICPAPCEEACRRHGVDEPVSI 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 126 KGIERTIIDEAFENGwvAPKVPSRRRD--EKVAIVGSGPAGLTAAEELNLLGYQVTIYERARESGGLLMYGIPNMKLDKD 203
Cdd:PRK12814 167 CALKRYAADRDMESA--ERYIPERAPKsgKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYGIPRFRLPES 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 204 VVRRRIKLMEEAGITFINGVEVGVDIDKATLESEYDAIILCTGAQKGRDLPLEGRMGDGIHFAMDYLTeqtqllngEIDD 283
Cdd:PRK12814 245 VIDADIAPLRAMGAEFRFNTVFGRDITLEELQKEFDAVLLAVGAQKASKMGIPGEELPGVISGIDFLR--------NVAL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 284 ITITAKDKNVIIIGAGDTGADCVATALRENCKSIVQFNKYTK-------------LPEAITFTenaswPLAMPVfkmdya 350
Cdd:PRK12814 317 GTALHPGKKVVVIGGGNTAIDAARTALRLGAESVTILYRRTReempanraeieeaLAEGVSLR-----ELAAPV------ 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 351 hqeyeakfgkeprayGVQTMrydvDDKGHIRGLYTQILEQGENGM---VMKEGPERFWPADLVLLSIGFEgTEPTVPNAF 427
Cdd:PRK12814 386 ---------------SIERS----EGGLELTAIKMQQGEPDESGRrrpVPVEGSEFTLQADTVISAIGQQ-VDPPIAEAA 445
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 446425735 428 NIKTDRN-RIVADDTNYQTNNEKVFAAGDARRGQSLVVWAIKEGRGVAKAVDQYLASK 484
Cdd:PRK12814 446 GIGTSRNgTVKVDPETLQTSVAGVFAGGDCVTGADIAINAVEQGKRAAHAIDLFLNGK 503
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
17-481 |
2.42e-49 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 181.68 E-value: 2.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 17 ELSLVDRLKHHKAYQQRFTKEDASIQGARCMDCGTPFCqtgqqygreTIGCPIGNYIPEWNDLVYHQDFKTAYERLSETN 96
Cdd:PRK12775 304 ERDAVERARNFKEVNLGYSLEDALQEAERCIQCAKPTC---------IAGCPVQIDIPVFIRHVVVRDFDGALEVIYEAS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 97 NFPDFTGRVCP--APCESACVMKINRESIAIKGIERTIIDEAfengwVAPKVPSRRRDE---KVAIVGSGPAGLTAAEEL 171
Cdd:PRK12775 375 IFPSICGRVCPqeTQCEAQCIIAKKHESVGIGRLERFVGDNA-----RAKPVKPPRFSKklgKVAICGSGPAGLAAAADL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 172 NLLGYQVTIYERARESGGLLMYGIPNMKLDKDVVRRRIKLMEEAGITFINGVEVG--VDIDKATLESEYDAIILCTGAQK 249
Cdd:PRK12775 450 VKYGVDVTVYEALHVVGGVLQYGIPSFRLPRDIIDREVQRLVDIGVKIETNKVIGktFTVPQLMNDKGFDAVFLGVGAGA 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 250 GRDLPLEGRMGDGIHFAMDYLTeQTQLLNGEI---DDITITAkDKNVIIIGAGDTGADCVATALRencksivqfnkytkl 326
Cdd:PRK12775 530 PTFLGIPGEFAGQVYSANEFLT-RVNLMGGDKfpfLDTPISL-GKSVVVIGAGNTAMDCLRVAKR--------------- 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 327 peaitftenaswpLAMPVFKMDYAHQEYEA-------KFGKEPrayGVQ------TMRYDVDDKGHIRGLYTQILEQGEN 393
Cdd:PRK12775 593 -------------LGAPTVRCVYRRSEAEAparieeiRHAKEE---GIDffflhsPVEIYVDAEGSVRGMKVEEMELGEP 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 394 GMVMKEGP---ERF--WPADLVLLSIGFEG----TEPTVPNAFNiktDRNRIVADDTNYQ----TNNEKVFAAGDARRGQ 460
Cdd:PRK12775 657 DEKGRRKPmptGEFkdLECDTVIYALGTKAnpiiTQSTPGLALN---KWGNIAADDGKLEstqsTNLPGVFAGGDIVTGG 733
|
490 500
....*....|....*....|.
gi 446425735 461 SLVVWAIKEGRGVAKAVDQYL 481
Cdd:PRK12775 734 ATVILAMGAGRRAARSIATYL 754
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
145-484 |
4.18e-44 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 158.61 E-value: 4.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 145 KVPSRRRDEKVAIVGSGPAGLTAAEELNLLGYQVTIYERARESGGLLMYGIPNMKLDKDVVRRRIKLMEEAGITFINGVE 224
Cdd:PRK12770 11 KEKPPPTGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLMLFGIPEFRIPIERVREGVKELEEAGVVFHTRTK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 225 VGVDI------------DKATLE---SEYDAIILCTGAQKGRDLPLEGRMGDGIHFAMDYL-----TEQTQLLNGEIDDI 284
Cdd:PRK12770 91 VCCGEplheeegdefveRIVSLEelvKKYDAVLIATGTWKSRKLGIPGEDLPGVYSALEYLfriraAKLGYLPWEKVPPV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 285 titaKDKNVIIIGAGDTGADCVATALRENCKSIVQFNKYTkLPEA------ITFTENAS---WPLAMPVfkmdyahqeye 355
Cdd:PRK12770 171 ----EGKKVVVVGAGLTAVDAALEAVLLGAEKVYLAYRRT-INEApagkyeIERLIARGvefLELVTPV----------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 356 AKFGKEprayGVQTMRYdvddkghIRGLYTQILEQGENGMVMKEGPERFWPADLVLLSIGFEGTEPTVPNAFNIKTDRNR 435
Cdd:PRK12770 235 RIIGEG----RVEGVEL-------AKMRLGEPDESGRPRPVPIPGSEFVLEADTVVFAIGEIPTPPFAKECLGIELNRKG 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 446425735 436 IVADDTNYQTNNEKVFAAGDARRGQSLVVWAIKEGRGVAKAVDQYLASK 484
Cdd:PRK12770 304 EIVVDEKHMTSREGVFAAGDVVTGPSKIGKAIKSGLRAAQSIHEWLDLK 352
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
66-477 |
4.99e-31 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 127.26 E-value: 4.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 66 GCPIGNYIPEWNDLVYHQDFKTAYERLSETNNFPDFTGRVCPAP--CESACVMkiNRESIAIKGIE----------RTII 133
Cdd:PRK12779 213 GCPVKIHIPEMLDLLGNGKHREALELIESCNPLPNVTGRVCPQElqCQGVCTH--TKRPIEIGQLEwylpqheklvNPNA 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 134 DEAFE---NGWVAPKVPSrrrdekVAIVGSGPAGLTAAEELNLLGYQVTIYERARESGGLLMYGIPNMKLDK---DVVRR 207
Cdd:PRK12779 291 NERFAgriSPWAAAVKPP------IAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVLRYGIPEFRLPNqliDDVVE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 208 RIKLMeeaGITFINGVEVGvdiDKATLESEYDA----IILCTGAQKGRDLPLEGRMGDGIHFAMDYLTeQTQLLNGEIDD 283
Cdd:PRK12779 365 KIKLL---GGRFVKNFVVG---KTATLEDLKAAgfwkIFVGTGAGLPTFMNVPGEHLLGVMSANEFLT-RVNLMRGLDDD 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 284 ITI---TAKDKNVIIIGAGDTGADCVATALRENCKSIVQFNKytklpeaiTFTEnaswplaMPVFKMDYAHQEYEAKFGK 360
Cdd:PRK12779 438 YETplpEVKGKEVFVIGGGNTAMDAARTAKRLGGNVTIVYRR--------TKSE-------MPARVEELHHALEEGINLA 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 361 EPRAygvqTMRYDVDDKGH-IRGLYTQILEQGENGMVMKEGP------ERFwPADLVLLSIGfEGTEPTVPNAF-NIKTD 432
Cdd:PRK12779 503 VLRA----PREFIGDDHTHfVTHALLDVNELGEPDKSGRRSPkptgeiERV-PVDLVIMALG-NTANPIMKDAEpGLKTN 576
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 446425735 433 R-NRIVADDTNYQTNNEKVFAAGDARRGQSLVVWAIKEGRGVAKAV 477
Cdd:PRK12779 577 KwGTIEVEKGSQRTSIKGVYSGGDAARGGSTAIRAAGDGQAAAKEI 622
|
|
| Fer4_20 |
pfam14691 |
Dihydroprymidine dehydrogenase domain II, 4Fe-4S cluster; Domain II of the enzyme ... |
34-141 |
4.20e-28 |
|
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: 107.63 E-value: 4.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 34 FTKEDASIQGARCMDCGTPFCQTGqqygretigCPIGNYIPEWNDLVYHQDFKTAYERLSETNNFPDFTGRVCPA--PCE 111
Cdd:pfam14691 12 YTEEEAIAEASRCLQCKDPPCVKG---------CPVHIDIPEFIKLIAEGNFEGAARIILETNPLPAICGRVCPQerQCE 82
|
90 100 110
....*....|....*....|....*....|.
gi 446425735 112 SACVM-KINRESIAIKGIERTIIDEAFENGW 141
Cdd:pfam14691 83 GACVLgKKGFEPVAIGRLERFAADWARENGI 113
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
154-470 |
1.50e-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: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 154 KVAIVGSGPAGLTAAEELNLLGYQVTIYERARE---SGGLLMYGIPNMKLDKDVVRRRIKLME---------EAGITFIN 221
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKVTLIEDEGTcpyGGCVLSKALLGAAEAPEIASLWADLYKrkeevvkklNNGIEVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 222 GVEV-GVDIDKATLES-----------EYDAIILCTGAqKGRDLPLEGrMGDGIHFAMDYLtEQTQLLNgeidditITAK 289
Cdd:pfam07992 82 GTEVvSIDPGAKKVVLeelvdgdgetiTYDRLVIATGA-RPRLPPIPG-VELNVGFLVRTL-DSAEALR-------LKLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 290 DKNVIIIGAGDTGADCVATALRENCKsivqfnkytklpeaITFTENASWPLAMpvfkMDYAHQEYEAkfgKEPRAYGVQT 369
Cdd:pfam07992 152 PKRVVVVGGGYIGVELAAALAKLGKE--------------VTLIEALDRLLRA----FDEEISAALE---KALEKNGVEV 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 370 M------RYDVDDKGhirglYTQILEQGengmvmkegpERFwPADLVLLSIGFegtEPTVPNAFNIK---TDRNRIVADD 440
Cdd:pfam07992 211 RlgtsvkEIIGDGDG-----VEVILKDG----------TEI-DADLVVVAIGR---RPNTELLEAAGlelDERGGIVVDE 271
|
330 340 350
....*....|....*....|....*....|.
gi 446425735 441 tNYQTNNEKVFAAGDARRGQ-SLVVWAIKEG 470
Cdd:pfam07992 272 -YLRTSVPGIYAAGDCRVGGpELAQNAVAQG 301
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
154-484 |
1.38e-21 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 94.80 E-value: 1.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 154 KVAIVGSGPAGLTAAEELNLLGYQVTIYERaRESGGLLM--------YGIPNMKLDKDVVRRRIKLMEEAGITFINGVEV 225
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLAttkeienyPGFPEGISGPELAERLREQAERFGAEILLEEVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 226 GVDID----KATLES--EY--DAIILCTGAQKgRDLPLEG---RMGDGIHFAmdyLTEQTQLLngeiddititaKDKNVI 294
Cdd:COG0492 81 SVDKDdgpfRVTTDDgtEYeaKAVIIATGAGP-RKLGLPGeeeFEGRGVSYC---ATCDGFFF-----------RGKDVV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 295 IIGAGDTGADcVATALRENCKSIVQFNKYTKLpeaitfteNASWPLAMPVFkmdyAHQEYEAKFGKEPRAygvqtmrydV 374
Cdd:COG0492 146 VVGGGDSALE-EALYLTKFASKVTLIHRRDEL--------RASKILVERLR----ANPKIEVLWNTEVTE---------I 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 375 DDKGHIRGLytqILEQGengmvmKEGPERFWPADLVLLSIGFEG-TEPtVPNAFNIKTDRNRIVADDTnYQTNNEKVFAA 453
Cdd:COG0492 204 EGDGRVEGV---TLKNV------KTGEEKELEVDGVFVAIGLKPnTEL-LKGLGLELDEDGYIVVDED-METSVPGVFAA 272
|
330 340 350
....*....|....*....|....*....|..
gi 446425735 454 GDARRGQS-LVVWAIKEGRGVAKAVDQYLASK 484
Cdd:COG0492 273 GDVRDYKYrQAATAAGEGAIAALSAARYLEPL 304
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
153-455 |
1.67e-16 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 81.34 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 153 EKVAIVGSGPAGLTAAEELNLLGYQVTI----------YERAresggLLMYGIPNMKLDKDVVRRRIKLMEEAGITFING 222
Cdd:COG1251 2 MRIVIIGAGMAGVRAAEELRKLDPDGEItvigaephppYNRP-----PLSKVLAGETDEEDLLLRPADFYEENGIDLRLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 223 VEVgVDIDKA----TLES----EYDAIILCTGAqKGRDLPLEGRMGDGIHFamdylteqtqlLNGeIDD----ITITAKD 290
Cdd:COG1251 77 TRV-TAIDRAartvTLADgetlPYDKLVLATGS-RPRVPPIPGADLPGVFT-----------LRT-LDDadalRAALAPG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 291 KNVIIIGAGDTGADcVATALRENCKsivqfnkytklpeAITFTENASWPLA--MPVFKMDYAHQEYEAKfGKEPRaYGVQ 368
Cdd:COG1251 143 KRVVVIGGGLIGLE-AAAALRKRGL-------------EVTVVERAPRLLPrqLDEEAGALLQRLLEAL-GVEVR-LGTG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 369 TMRYDVDDKGHirglytqileqgenGMVMKEGpeRFWPADLVLLSIGfegtepTVPN-----AFNIKTDRnRIVADDTnY 443
Cdd:COG1251 207 VTEIEGDDRVT--------------GVRLADG--EELPADLVVVAIG------VRPNtelarAAGLAVDR-GIVVDDY-L 262
|
330
....*....|..
gi 446425735 444 QTNNEKVFAAGD 455
Cdd:COG1251 263 RTSDPDIYAAGD 274
|
|
| PLN02852 |
PLN02852 |
ferredoxin-NADP+ reductase |
130-311 |
1.90e-15 |
|
ferredoxin-NADP+ reductase
Pssm-ID: 215457 Cd Length: 491 Bit Score: 78.58 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 130 RTIIDEAFENGWVAPKVPSRRRdekVAIVGSGPAGLTAAEELnLLGYQ---VTIYERARESGGLLMYGI-PNMKLDKDVV 205
Cdd:PLN02852 7 RTWLSRALSFSNSSSSTSEPLH---VCVVGSGPAGFYTADKL-LKAHDgarVDIIERLPTPFGLVRSGVaPDHPETKNVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 206 RRRIKLMEEAGITFINGVEVGVDIDKATLESEYDAIILCTGAQKGRDLPLEGRMGDGIHFAmdylTEQTQLLNGEID--D 283
Cdd:PLN02852 83 NQFSRVATDDRVSFFGNVTLGRDVSLSELRDLYHVVVLAYGAESDRRLGIPGEDLPGVLSA----REFVWWYNGHPDcvH 158
|
170 180
....*....|....*....|....*....
gi 446425735 284 ITITAK-DKNVIIIGAGDTGADCVATALR 311
Cdd:PLN02852 159 LPPDLKsSDTAVVLGQGNVALDCARILLR 187
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
154-476 |
3.31e-12 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 67.85 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 154 KVAIVGSGPAGLTAAEEL-NLL--GYQVTIYERARE---SGGLlmYGIPNMKLDKDVVRRRI-KLMEEAGITFINGVEVG 226
Cdd:COG1252 3 RIVIVGGGFAGLEAARRLrKKLggDAEVTLIDPNPYhlfQPLL--PEVAAGTLSPDDIAIPLrELLRRAGVRFIQGEVTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 227 VDID--KATLES----EYDAIILCTGAQKgRDLPLEGrMGDGIHFAmdYLTEQTQLLNGEIDDITITAKDK---NVIIIG 297
Cdd:COG1252 81 IDPEarTVTLADgrtlSYDYLVIATGSVT-NFFGIPG-LAEHALPL--KTLEDALALRERLLAAFERAERRrllTIVVVG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 298 AGDTG---ADCVATALRENCksivqfnKYTKLPEA---ITFTENASWPLAMpvfkmdyahqeyeakFGKEPRAYGVQTMR 371
Cdd:COG1252 157 GGPTGvelAGELAELLRKLL-------RYPGIDPDkvrITLVEAGPRILPG---------------LGEKLSEAAEKELE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 372 ydvdDKG-HIRgLYTQILEQGENGMVMKEGpeRFWPADLVLLSIGFEGtePTVPNAFNIKTDR-NRIVADDTNYQTNNEK 449
Cdd:COG1252 215 ----KRGvEVH-TGTRVTEVDADGVTLEDG--EEIPADTVIWAAGVKA--PPLLADLGLPTDRrGRVLVDPTLQVPGHPN 285
|
330 340
....*....|....*....|....*..
gi 446425735 450 VFAAGDArrgqSLVVWAikEGRGVAKA 476
Cdd:COG1252 286 VFAIGDC----AAVPDP--DGKPVPKT 306
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
177-456 |
8.66e-12 |
|
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: 65.99 E-value: 8.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 177 QVTIYERARE-----SGGLLMYGIPNMKLDkDVVRRRIKLMEEAGITFINGVEVgVDIDKA----TLES----EYDAIIL 243
Cdd:COG0446 7 EITVIEKGPHhsyqpCGLPYYVGGGIKDPE-DLLVRTPESFERKGIDVRTGTEV-TAIDPEaktvTLRDgetlSYDKLVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 244 CTGAQKgRDLPLEGRMGDGIHFAMDYltEQTQLLNGEIDDititAKDKNVIIIGAGDTGADcVATALRENCKSivqfnky 323
Cdd:COG0446 85 ATGARP-RPPPIPGLDLPGVFTLRTL--DDADALREALKE----FKGKRAVVIGGGPIGLE-LAEALRKRGLK------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 324 tklpeaITFTENASWPLAMPVFKM-DYAHQEYEAKfGKEPRaYGVQTMRYDVDDKGHIRglytqiLEQGENgmvmkegpe 402
Cdd:COG0446 150 ------VTLVERAPRLLGVLDPEMaALLEEELREH-GVELR-LGETVVAIDGDDKVAVT------LTDGEE--------- 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 403 rfWPADLVLLSIGFegteptVPN-----AFNIKTDRNR-IVADDTnYQTNNEKVFAAGDA 456
Cdd:COG0446 207 --IPADLVVVAPGV------RPNtelakDAGLALGERGwIKVDET-LQTSDPDVYAAGDC 257
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
155-475 |
3.67e-10 |
|
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: 62.03 E-value: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 155 VAIVGSGPAGLTAAEELNLLGYQVTI---------------------------YERARESGGllmYGI--PNMKLD-KDV 204
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALvekgrlggtclnvgcipskallhaaevAHEARHAAE---FGIsaGAPSVDwAAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 205 VRRR-----------IKLMEEAGITFING---------VEVGvdiDKATLESeyDAIILCTGAqKGRDLPLEGRMGDGIH 264
Cdd:COG1249 83 MARKdkvvdrlrggvEELLKKNGVDVIRGrarfvdphtVEVT---GGETLTA--DHIVIATGS-RPRVPPIPGLDEVRVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 265 -----FAMDYLTeqtqllngeiddititakdKNVIIIGAGDTGADcVATALRE-NCK-SIVQFNkytklpeaitftenas 337
Cdd:COG1249 157 tsdeaLELEELP-------------------KSLVVIGGGYIGLE-FAQIFARlGSEvTLVERG---------------- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 338 wPLAMPVFKMDYAhQEYEAKFGKEprayGVqtmrydvddkgHIRgLYTQI--LEQGENGMVMK---EGPERFWPADLVLL 412
Cdd:COG1249 201 -DRLLPGEDPEIS-EALEKALEKE----GI-----------DIL-TGAKVtsVEKTGDGVTVTledGGGEEAVEADKVLV 262
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446425735 413 SIGFegteptVPN-------AFNIKTD-RNRIVADDTnYQTNNEKVFAAGDARRGQSLVVWAIKEGRGVAK 475
Cdd:COG1249 263 ATGR------RPNtdglgleAAGVELDeRGGIKVDEY-LRTSVPGIYAIGDVTGGPQLAHVASAEGRVAAE 326
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
153-246 |
1.04e-09 |
|
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: 59.82 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 153 EKVAIVGSGPAGLTAAEELNLLGYQVTIYERAresGGLLmygipnMKLDKDVVRRRIKLMEEAGITFINGVEV----GVD 228
Cdd:COG0446 125 KRAVVIGGGPIGLELAEALRKRGLKVTLVERA---PRLL------GVLDPEMAALLEEELREHGVELRLGETVvaidGDD 195
|
90 100
....*....|....*....|..
gi 446425735 229 IDKATLES----EYDAIILCTG 246
Cdd:COG0446 196 KVAVTLTDgeeiPADLVVVAPG 217
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
154-202 |
1.10e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 57.20 E-value: 1.10e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 446425735 154 KVAIVGSGPAGLTAAEELNLLGYQVTIYERARESGGLL-MYGIPNMKLDK 202
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGLAaSFEFGGLPIER 50
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
154-190 |
4.50e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 55.28 E-value: 4.50e-08
10 20 30
....*....|....*....|....*....|....*..
gi 446425735 154 KVAIVGSGPAGLTAAEELNLLGYQVTIYERARESGGL 190
Cdd:PRK07208 6 SVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGI 42
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
154-191 |
6.63e-08 |
|
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: 54.84 E-value: 6.63e-08
10 20 30
....*....|....*....|....*....|....*...
gi 446425735 154 KVAIVGSGPAGLTAAEELNLLGYQVTIYERARESGGLL 191
Cdd:COG1232 3 RVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLI 40
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
154-225 |
9.40e-08 |
|
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: 49.51 E-value: 9.40e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446425735 154 KVAIVGSGPAGLTAAEELNLLGYQVTIYERAREsggllmygiPNMKLDKDVVRRRIKLMEEAGITFINGVEV 225
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDR---------LLPGFDPEIAKILQEKLEKNGIEFLLNTTV 63
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
154-189 |
1.31e-07 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 53.34 E-value: 1.31e-07
10 20 30
....*....|....*....|....*....|....*.
gi 446425735 154 KVAIVGSGPAGLTAAEELNLLGYQVTIYERARESGG 189
Cdd:COG3380 5 DIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGG 40
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
149-189 |
1.64e-07 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 53.39 E-value: 1.64e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 446425735 149 RRRDEKVAIVGSGPAGLTAAEELNLLGYQVTIYErARE-SGG 189
Cdd:COG1231 4 RARGKDVVIVGAGLAGLAAARELRKAGLDVTVLE-ARDrVGG 44
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
154-483 |
2.20e-07 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 53.33 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 154 KVAIVGSGPAGLTAAEELNLLGYQVTIYERARESGGL---LMYGIPNMKLDKDVVRRRIKLMEE-AGITFINGVEVgVDI 229
Cdd:COG1148 142 RALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGRaaqLHKTFPGLDCPQCILEPLIAEVEAnPNITVYTGAEV-EEV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 230 D------KATLES--------EYDAIILCTGAQkgrdlplegrmgdgiHFAMDYLTEqtqLLNGEIDDItITA------- 288
Cdd:COG1148 221 SgyvgnfTVTIKKgpreeieiEVGAIVLATGFK---------------PYDPTKLGE---YGYGKYPNV-ITNlelerll 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 289 ------------KDKNVIIIgagdtgaDCV----ATALRENCKSI-----VQFNKYTK--LPEAITFtenaswplampVF 345
Cdd:COG1148 282 aagkilrpsdgkEPKSVAFI-------QCVgsrdEENGLPYCSRVccmyaLKQALYLKekNPDADVY-----------IF 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 346 KMDY-AHQEYEaKFGKEPRAYGVQTMRYDVDDKghIRGLYTQILEQGEN---GMVMKEgperfwPADLVLLSIGFEGTEP 421
Cdd:COG1148 344 YRDIrTYGKYE-EFYRRAREDGVRFIRGRVAEI--EEDEGGKLVVTVEDtllGEPVEI------EADLVVLATGMVPSED 414
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446425735 422 TVPNA--FNIKTDRNRIVADD----TNYQTNNEKVFAAGDArRGQSLVVWAIKEGRGVAKAVDQYLAS 483
Cdd:COG1148 415 NEELAklLKLPLDQDGFFLEAhpklRPVETATDGIFLAGAA-HGPKDIPESIAQATAAAARAIQLLSK 481
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
157-201 |
4.02e-07 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 47.14 E-value: 4.02e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 446425735 157 IVGSGPAGLTAAEELNLLGYQVTIYERARESGGLLM-YGIPNMKLD 201
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNAYsYRVPGYVFD 46
|
|
| mnmC |
PRK01747 |
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ... |
141-219 |
4.37e-07 |
|
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: 52.54 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 141 WVAPKVPSRRRDekVAIVGSGPAGLTAAEELNLLGYQVTIYER----ARE-SG---GLLMygiPNMKLDKDVV------- 205
Cdd:PRK01747 251 WFARPGSPKARD--AAIIGGGIAGAALALALARRGWQVTLYEAdeapAQGaSGnrqGALY---PLLSKDDNALsrffraa 325
|
90
....*....|....*...
gi 446425735 206 ----RRRIKLMEEAGITF 219
Cdd:PRK01747 326 flfaRRFYDALPAAGVAF 343
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
151-246 |
6.53e-07 |
|
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: 51.16 E-value: 6.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 151 RDEKVAIVGSGPAGLTAAEELNLLGYQVTIYERAREsggllmygiPNMKLDKDVVRRRIKLMEEAGITFINGVEV-GVDI 229
Cdd:pfam07992 151 LPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDR---------LLRAFDEEISAALEKALEKNGVEVRLGTSVkEIIG 221
|
90 100
....*....|....*....|....*
gi 446425735 230 DKATLES--------EYDAIILCTG 246
Cdd:pfam07992 222 DGDGVEVilkdgteiDADLVVVAIG 246
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
154-189 |
8.41e-07 |
|
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: 51.39 E-value: 8.41e-07
10 20 30
....*....|....*....|....*....|....*.
gi 446425735 154 KVAIVGSGPAGLTAAEELNLLGYQVTIYERARESGG 189
Cdd:COG3349 5 RVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
|
|
| PTZ00188 |
PTZ00188 |
adrenodoxin reductase; Provisional |
154-304 |
1.38e-06 |
|
adrenodoxin reductase; Provisional
Pssm-ID: 240308 Cd Length: 506 Bit Score: 50.65 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 154 KVAIVGSGPAGLTAAEE-LNLLGYQVTIYERARESGGLLMYGI-PNMKLDKDVVRRRIKLMEEAGITFINGVEVGVDIDK 231
Cdd:PTZ00188 41 KVGIIGAGPSALYCCKHlLKHERVKVDIFEKLPNPYGLIRYGVaPDHIHVKNTYKTFDPVFLSPNYRFFGNVHVGVDLKM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 232 ATLESEYDAIILCTGA--------QKGRDLPLEG-----RMGDGIHFAMDYLteqtQLLNGEIDDITITAKDK------- 291
Cdd:PTZ00188 121 EELRNHYNCVIFCCGAsevsipigQQDEDKAVSGgetnpRKQNGIFHARDLI----YFYNNMYNDVRCKAVDNylnsfen 196
|
170
....*....|....*
gi 446425735 292 --NVIIIGAGDTGAD 304
Cdd:PTZ00188 197 ftTSIIIGNGNVSLD 211
|
|
| glucose_DH |
cd08230 |
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ... |
122-247 |
1.91e-06 |
|
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain dehydrogenase/zinc-dependent alcohol dehydrogenase-like family, catalyzes the NADP(+)-dependent oxidation of glucose to gluconate, the first step in the Entner-Doudoroff pathway, an alternative to or substitute for glycolysis or the pentose phosphate pathway. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossman fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.
Pssm-ID: 176192 [Multi-domain] Cd Length: 355 Bit Score: 49.91 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 122 SIAIKGIErtiidEAFENGWVAPKVPSRRrdekVAIVGSGPAGLTAAEELNLLGYQVTIYERaRESGGLlmygipnmkld 201
Cdd:cd08230 152 SVVEKAIE-----QAEAVQKRLPTWNPRR----ALVLGAGPIGLLAALLLRLRGFEVYVLNR-RDPPDP----------- 210
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 446425735 202 kdvvrrRIKLMEEAGITFINGVEVGVDIDKATLesEYDAIILCTGA 247
Cdd:cd08230 211 ------KADIVEELGATYVNSSKTPVAEVKLVG--EFDLIIEATGV 248
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
151-189 |
2.89e-06 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 49.46 E-value: 2.89e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 446425735 151 RDEKVAIVGSGPAGLTAAeelNLL---GYQVTIYERARESGG 189
Cdd:COG1233 2 MMYDVVVIGAGIGGLAAA---ALLaraGYRVTVLEKNDTPGG 40
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
154-186 |
3.05e-06 |
|
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: 49.17 E-value: 3.05e-06
10 20 30
....*....|....*....|....*....|...
gi 446425735 154 KVAIVGSGPAGLTAAEELNLLGYQVTIYERARE 186
Cdd:COG0654 5 DVLIVGGGPAGLALALALARAGIRVTVVERAPP 37
|
|
| PLN02172 |
PLN02172 |
flavin-containing monooxygenase FMO GS-OX |
142-193 |
1.68e-05 |
|
flavin-containing monooxygenase FMO GS-OX
Pssm-ID: 215116 [Multi-domain] Cd Length: 461 Bit Score: 47.16 E-value: 1.68e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 446425735 142 VAPkVPSRRRDEKVAIVGSGPAGLTAAEELNLLGYQVTIYERARESGGLLMY 193
Cdd:PLN02172 1 MAP-AQNPINSQHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGLWVY 51
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
147-306 |
1.92e-05 |
|
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: 46.78 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 147 PSRRRDEKVAIVGSGPAGLTAAEELNLLGYQVTIYERARESGG---------------LLMYGIPNMKL--------DKD 203
Cdd:COG2072 1 TAATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGtwrdnrypglrldtpSHLYSLPFFPNwsddpdfpTGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 204 VVR-------RRIKLMEEagITFinGVEV-GVDIDKA----TLESE------YDAIILCTGA-QKGRDLPLEGRM---GD 261
Cdd:COG2072 81 EILayleayaDKFGLRRP--IRF--GTEVtSARWDEAdgrwTVTTDdgetltARFVVVATGPlSRPKIPDIPGLEdfaGE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446425735 262 GIHFAmDYlTEQTQLlngeiddititaKDKNVIIIGAGDTGADCV 306
Cdd:COG2072 157 QLHSA-DW-RNPVDL------------AGKRVLVVGTGASAVQIA 187
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
155-456 |
4.24e-05 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 45.94 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 155 VAIVGSGPAGLTAAEELNLLGYQVTI---------------------------YERARESGGllmYGI--PNMKLD-KDV 204
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGKKVALiekgplggtclnvgcipskaliaaaeaFHEAKHAEE---FGIhaDGPKIDfKKV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 205 VRR------------RIKLMEEAGITFINGVEVGVD-----IDKATLESEYdaIILCTGAqkgRDLPLEGrmgdgihfam 267
Cdd:PRK06292 83 MARvrrerdrfvggvVEGLEKKPKIDKIKGTARFVDpntveVNGERIEAKN--IVIATGS---RVPPIPG---------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 268 dylteqtqLLNGEIDDItITAKD--------KNVIIIGAGDTGADcVATAL-RENCK-SIVQFNKyTKLPEaitftenas 337
Cdd:PRK06292 148 --------VWLILGDRL-LTSDDafeldklpKSLAVIGGGVIGLE-LGQALsRLGVKvTVFERGD-RILPL--------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 338 wplampvfkMDYAHQEY-EAKFGKEpraygvqtMRYDVDDKghirglyTQILEQGENGMV---MKEGPERFWPADLVLLS 413
Cdd:PRK06292 208 ---------EDPEVSKQaQKILSKE--------FKIKLGAK-------VTSVEKSGDEKVeelEKGGKTETIEADYVLVA 263
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 446425735 414 IGfegTEPTVPN----AFNIKTD-RNRIVADDTnYQTNNEKVFAAGDA 456
Cdd:PRK06292 264 TG---RRPNTDGlgleNTGIELDeRGRPVVDEH-TQTSVPGIYAAGDV 307
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
154-215 |
5.99e-05 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 45.08 E-value: 5.99e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 154 KVAIVGSGPAGLTAAEELNLLGYQVTIYERARE--------SGGLLMYGIPNMKLdkdvvRRRIKLMEEA 215
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDpgsgasgrNAGLIHPGLRYLEP-----SELARLALEA 65
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
145-188 |
6.91e-05 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 45.63 E-value: 6.91e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 446425735 145 KVPSRRRDEK-VAIVGSGPAGLTAAEELNLLGYQVTIYE-RARESG 188
Cdd:PLN02976 685 CVLCDSVDRKkIIVVGAGPAGLTAARHLQRQGFSVTVLEaRSRIGG 730
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
154-215 |
1.05e-04 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 44.51 E-value: 1.05e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446425735 154 KVAIVGSGPAGLTAAEELNLLGYQVTIYER---ARES----GGLLMYGipnmkLDKDVVRRRIKLMEEA 215
Cdd:COG0665 4 DVVVIGGGIAGLSTAYHLARRGLDVTVLERgrpGSGAsgrnAGQLRPG-----LAALADRALVRLAREA 67
|
|
| PLN00093 |
PLN00093 |
geranylgeranyl diphosphate reductase; Provisional |
143-238 |
1.95e-04 |
|
geranylgeranyl diphosphate reductase; Provisional
Pssm-ID: 177713 [Multi-domain] Cd Length: 450 Bit Score: 43.59 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 143 APKVPSRRRdEKVAIVGSGPAGLTAAEELNLLGYQVTIYER----ARESGG---LLMYGipNMKLDKDVVRRRIKLMEea 215
Cdd:PLN00093 31 ASKKLSGRK-LRVAVIGGGPAGACAAETLAKGGIETFLIERkldnAKPCGGaipLCMVG--EFDLPLDIIDRKVTKMK-- 105
|
90 100
....*....|....*....|...
gi 446425735 216 gitFINGVEVGVDIDKATLESEY 238
Cdd:PLN00093 106 ---MISPSNVAVDIGKTLKPHEY 125
|
|
| PLN03000 |
PLN03000 |
amine oxidase |
145-189 |
2.03e-04 |
|
amine oxidase
Pssm-ID: 178578 [Multi-domain] Cd Length: 881 Bit Score: 43.86 E-value: 2.03e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 446425735 145 KVPSRRRDEKVAIVGSGPAGLTAAEELNLLGYQVTIYERARESGG 189
Cdd:PLN03000 177 KFPAQSSKSSVVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGG 221
|
|
| COG2509 |
COG2509 |
FAD-dependent dehydrogenase [General function prediction only]; |
128-183 |
2.48e-04 |
|
FAD-dependent dehydrogenase [General function prediction only];
Pssm-ID: 441999 [Multi-domain] Cd Length: 466 Bit Score: 43.56 E-value: 2.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 446425735 128 IERTIIDEAFENGWVAPKVPSRRRDEKVAIVGSGPAGLTAAEELNLLGYQVTIYER 183
Cdd:COG2509 6 LKLPLDDEEALKAAIAKKLGIPSLKYDVVIVGAGPAGLFAALELAEAGLKPLVLER 61
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
161-228 |
3.08e-04 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 42.65 E-value: 3.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446425735 161 GPAGLTAAEELNLLGYQVTIYERARE------SGGLLMYGIPNMKL--DKDVVRRRIKlmeEAGITFINGVEVGVD 228
Cdd:COG0644 2 GPAGSAAARRLARAGLSVLLLEKGSFpgdkicGGGLLPRALEELEPlgLDEPLERPVR---GARFYSPGGKSVELP 74
|
|
| Ppro0129 |
COG2907 |
Predicted flavin-containing amine oxidase [General function prediction only]; |
154-189 |
3.96e-04 |
|
Predicted flavin-containing amine oxidase [General function prediction only];
Pssm-ID: 442151 [Multi-domain] Cd Length: 423 Bit Score: 42.80 E-value: 3.96e-04
10 20 30
....*....|....*....|....*....|....*.
gi 446425735 154 KVAIVGSGPAGLTAAEELNLLgYQVTIYERARESGG 189
Cdd:COG2907 5 RIAVIGSGISGLTAAWLLSRR-HDVTLFEANDRLGG 39
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
152-183 |
4.45e-04 |
|
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: 42.31 E-value: 4.45e-04
10 20 30
....*....|....*....|....*....|..
gi 446425735 152 DEKVAIVGSGPAGLTAAEELNLLGYQVTIYER 183
Cdd:pfam01494 1 ETDVLIVGGGPAGLMLALLLARAGVRVVLVER 32
|
|
| PRK12409 |
PRK12409 |
D-amino acid dehydrogenase small subunit; Provisional |
154-185 |
5.09e-04 |
|
D-amino acid dehydrogenase small subunit; Provisional
Pssm-ID: 237093 [Multi-domain] Cd Length: 410 Bit Score: 42.32 E-value: 5.09e-04
10 20 30
....*....|....*....|....*....|..
gi 446425735 154 KVAIVGSGPAGLTAAEELNLLGYQVTIYERAR 185
Cdd:PRK12409 3 HIAVIGAGITGVTTAYALAQRGYQVTVFDRHR 34
|
|
| PRK06753 |
PRK06753 |
hypothetical protein; Provisional |
154-186 |
7.23e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 168661 [Multi-domain] Cd Length: 373 Bit Score: 41.98 E-value: 7.23e-04
10 20 30
....*....|....*....|....*....|...
gi 446425735 154 KVAIVGSGPAGLTAAEELNLLGYQVTIYERARE 186
Cdd:PRK06753 2 KIAIIGAGIGGLTAAALLQEQGHEVKVFEKNES 34
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
153-246 |
7.76e-04 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 41.66 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 153 EKVAIVGSGPAGLTAAEELNLLGYQVTIYERAreSGGLLMYGIPNMKLDKDvvrrrikLMEEAGITFINGV---EVGVDI 229
Cdd:PRK07251 158 ERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAA--STILPREEPSVAALAKQ-------YMEEDGITFLLNAhttEVKNDG 228
|
90 100
....*....|....*....|..
gi 446425735 230 DKATLESE-----YDAIILCTG 246
Cdd:PRK07251 229 DQVLVVTEdetyrFDALLYATG 250
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
123-246 |
8.47e-04 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 41.70 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 123 IAIKGIER----TII--DEAFEngWvaPKVPsrrrdEKVAIVGSGPAGLTAAEELNLLGYQVTIYERareSGGLLmygiP 196
Cdd:PRK06292 143 PPIPGVWLilgdRLLtsDDAFE--L--DKLP-----KSLAVIGGGVIGLELGQALSRLGVKVTVFER---GDRIL----P 206
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446425735 197 NMklDKDVVR-------RRIKLMEEAGITFI----NGVEVGVDIDKATLESEYDAIILCTG 246
Cdd:PRK06292 207 LE--DPEVSKqaqkilsKEFKIKLGAKVTSVeksgDEKVEELEKGGKTETIEADYVLVATG 265
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
122-256 |
9.35e-04 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 41.27 E-value: 9.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 122 SIAIKGIERTI-----IDEAFENGwvapkvpSRRRDEKVAIVGSGPAG----LTAAEELN-LLGY--------QVTIYER 183
Cdd:COG1252 121 ALPLKTLEDALalrerLLAAFERA-------ERRRLLTIVVVGGGPTGvelaGELAELLRkLLRYpgidpdkvRITLVEA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 184 AREsggLLmygiPNMklDKDVVRRRIKLMEEAGITFINGVEV-GVDIDKATLES----EYDAIILCTGAqKG----RDLP 254
Cdd:COG1252 194 GPR---IL----PGL--GEKLSEAAEKELEKRGVEVHTGTRVtEVDADGVTLEDgeeiPADTVIWAAGV-KAppllADLG 263
|
..
gi 446425735 255 LE 256
Cdd:COG1252 264 LP 265
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
150-246 |
1.21e-03 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 41.28 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 150 RRDEKVAIVGSGPAGLTAAEELNLLGYQVTIYERAresgGLLMygiPNMkLDK---DVVRRRIklmEEAGITFINGVEV- 225
Cdd:COG1251 140 APGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERA----PRLL---PRQ-LDEeagALLQRLL---EALGVEVRLGTGVt 208
|
90 100
....*....|....*....|....*....
gi 446425735 226 ---GVD-IDKATLES----EYDAIILCTG 246
Cdd:COG1251 209 eieGDDrVTGVRLADgeelPADLVVVAIG 237
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
144-246 |
1.24e-03 |
|
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.
Pssm-ID: 273624 [Multi-domain] Cd Length: 484 Bit Score: 41.38 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 144 PKVPSrrrdeKVAIVGSGPAGLTAAEELNLLGYQVTIYERAresggllmygIPNMKLDKDVVRRRIKLMEEAGITFINGV 223
Cdd:TIGR01438 177 PYCPG-----KTLVVGASYVALECAGFLAGIGLDVTVMVRS----------ILLRGFDQDCANKVGEHMEEHGVKFKRQF 241
|
90 100 110
....*....|....*....|....*....|....*
gi 446425735 224 EV----GVDIDK--------ATLESEYDAIILCTG 246
Cdd:TIGR01438 242 VPikveQIEAKVlveftdstNGIEEEYDTVLLAIG 276
|
|
| PRK11883 |
PRK11883 |
protoporphyrinogen oxidase; Reviewed |
154-191 |
1.86e-03 |
|
protoporphyrinogen oxidase; Reviewed
Pssm-ID: 237009 [Multi-domain] Cd Length: 451 Bit Score: 40.60 E-value: 1.86e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 446425735 154 KVAIVGSGPAGLTAAEELNLLG--YQVTIYERARESGGLL 191
Cdd:PRK11883 2 KVAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKI 41
|
|
| PLN02487 |
PLN02487 |
zeta-carotene desaturase |
138-189 |
1.87e-03 |
|
zeta-carotene desaturase
Pssm-ID: 215268 [Multi-domain] Cd Length: 569 Bit Score: 40.94 E-value: 1.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 446425735 138 ENGWVAPKVPSRRRDE-KVAIVGSGPAGLTAAEELNLLGYQVTIYERARESGG 189
Cdd:PLN02487 60 PKGLFPPEPEAYKGPKlKVAIIGAGLAGMSTAVELLDQGHEVDIYESRPFIGG 112
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
154-246 |
2.00e-03 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 40.58 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 154 KVAIVGSGPAGLTAAEELNLLGYQVTIYERAresggllmygIPNMKLDKDVVRRRIKLMEEAGITFINGV---------- 223
Cdd:PTZ00052 184 KTLIVGASYIGLETAGFLNELGFDVTVAVRS----------IPLRGFDRQCSEKVVEYMKEQGTLFLEGVvpiniekmdd 253
|
90 100
....*....|....*....|...
gi 446425735 224 EVGVDIDKATLEsEYDAIILCTG 246
Cdd:PTZ00052 254 KIKVLFSDGTTE-LFDTVLYATG 275
|
|
| Thi4 |
pfam01946 |
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme. |
155-225 |
2.91e-03 |
|
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
Pssm-ID: 460393 Cd Length: 232 Bit Score: 39.38 E-value: 2.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446425735 155 VAIVGSGPAGLTAAEEL-NLLGYQVTIYERARESGGLLMYGipNMKLDKDVVRRRIKL-MEEAGITFI---NGVEV 225
Cdd:pfam01946 20 VVIVGAGSSGLTAAYYLaKNRGLKVAIIERSVSPGGGAWLG--GQLFSAMVVRKPAHLfLDEFGIPYEdegDYVVV 93
|
|
| Ala_dh_like |
cd01620 |
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ... |
149-223 |
3.12e-03 |
|
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such as the hexameric L-alanine dehydrogenase of Phormidium lapideum, contain 2 Rossmann fold-like domains linked by an alpha helical region. Related proteins include Saccharopine Dehydrogenase (SDH), bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme, N(5)-(carboxyethyl)ornithine synthase, and Rubrum transdehydrogenase. Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyrucate to L-alanine via reductive amination. Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matirx side. DI contains 2 domains with Rossmann folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with one dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than classical Rossmann domains.
Pssm-ID: 240621 [Multi-domain] Cd Length: 317 Bit Score: 39.70 E-value: 3.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446425735 149 RRRDEKVAIVGSGPAGLTAAEELNLLGYQVTIYER--ARESGGLLMYGIPNMKLDKDVVrrrIKLMEEAGItFINGV 223
Cdd:cd01620 159 GVPPAKVLIIGAGVVGLGAAKIAKKLGANVLVYDIkeEKLKGVETLGGSRLRYSQKEEL---EKELKQTDI-LINAI 231
|
|
| PRK08401 |
PRK08401 |
L-aspartate oxidase; Provisional |
152-225 |
3.53e-03 |
|
L-aspartate oxidase; Provisional
Pssm-ID: 236259 [Multi-domain] Cd Length: 466 Bit Score: 39.78 E-value: 3.53e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446425735 152 DEKVAIVGSGPAGLTAAEELNLLGYQVTIY-ERARESGGLL-MYGIPNMKLDKDVVRRRIKLMEEAGiTFINGVEV 225
Cdd:PRK08401 1 MMKVGIVGGGLAGLTAAISLAKKGFDVTIIgPGIKKSNSYLaQAGIAFPILEGDSIRAHVLDTIRAG-KYINDEEV 75
|
|
| MDR_like |
cd08242 |
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
150-250 |
4.08e-03 |
|
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family, including threonine dehydrogenase. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.
Pssm-ID: 176204 [Multi-domain] Cd Length: 319 Bit Score: 39.15 E-value: 4.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446425735 150 RRDEKVAIVGSGPAGLTAAEELNLLGYQVTIYERAREsggllmygipnmkldkdvvrrRIKLMEEAGITFINGVEVGvdi 229
Cdd:cd08242 154 TPGDKVAVLGDGKLGLLIAQVLALTGPDVVLVGRHSE---------------------KLALARRLGVETVLPDEAE--- 209
|
90 100
....*....|....*....|.
gi 446425735 230 dkaTLESEYDAIILCTGAQKG 250
Cdd:cd08242 210 ---SEGGGFDVVVEATGSPSG 227
|
|
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
155-185 |
4.73e-03 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 39.50 E-value: 4.73e-03
10 20 30
....*....|....*....|....*....|....
gi 446425735 155 VAIVGSGPAGLTAAeelNLL---GYQVTIYERAR 185
Cdd:PRK06183 13 VVIVGAGPVGLTLA---NLLgqyGVRVLVLERWP 43
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
155-198 |
7.52e-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: 38.81 E-value: 7.52e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 446425735 155 VAIVGSGPAGLTAAEELNLLGYQVTIYER--------ARESGGLLMYGIPNM 198
Cdd:pfam00890 2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKgqpfggatAWSSGGIDALGNPPQ 53
|
|
| |
