|
Name |
Accession |
Description |
Interval |
E-value |
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
29-351 |
1.44e-107 |
|
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: 321.38 E-value: 1.44e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 29 EIVVFDQNSNISFLGCGMALWIGEQIAGPEGLFYSDKEELESLGAKVYMESPVQSIDYDAKTVTaLVDGKnhVETYDKLI 108
Cdd:COG0446 7 EITVIEKGPHHSYQPCGLPYYVGGGIKDPEDLLVRTPESFERKGIDVRTGTEVTAIDPEAKTVT-LRDGE--TLSYDKLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 109 FATGSQPILPPIKGAEikegslefeatLENLQFVKLYQNSADVIAKLENKDIKRVAVVGAGYIGVELAEAFQRKGKEVVL 188
Cdd:COG0446 84 LATGARPRPPPIPGLD-----------LPGVFTLRTLDDADALREALKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 189 IDVVDTCLAGYyDRDLTDLMAKNMEEHGIQLAFGETVKEVAGNGKVEKIITDKNEYDVDMVILAVGFRPNTTLGNG-KID 267
Cdd:COG0446 153 VERAPRLLGVL-DPEMAALLEEELREHGVELRLGETVVAIDGDDKVAVTLTDGEEIPADLVVVAPGVRPNTELAKDaGLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 268 LFRNGAFLVNKRQETSIPGVYAIGDCATIYDNATRDTNYIALASNAVRTGIVAAHNACGTDLEGIGvQGSNGISIYGLHM 347
Cdd:COG0446 232 LGERGWIKVDETLQTSDPDVYAAGDCAEVPHPVTGKTVYIPLASAANKQGRVAAENILGGPAPFPG-LGTFISKVFDLCI 310
|
....
gi 489079851 348 VSTG 351
Cdd:COG0446 311 ASTG 314
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
3-455 |
1.33e-99 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 305.43 E-value: 1.33e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 3 KIVVVGANHAGT-ACIKTMLTNYGDanEIVVFDQNSNISFLGCGMALWIGEQIAGPEGLFYSDKEELESLGAKVYMESPV 81
Cdd:PRK09564 2 KIIIIGGTAAGMsAAAKAKRLNKEL--EITVYEKTDIVSFGACGLPYFVGGFFDDPNTMIARTPEEFIKSGIDVKTEHEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 82 QSIDYDAKTVTA--LVDGKNHVETYDKLIFATGSQPILPPIKGAEikegslefeatLENLQFVKLYQNSADVIAKLENKD 159
Cdd:PRK09564 80 VKVDAKNKTITVknLKTGSIFNDTYDKLMIATGARPIIPPIKNIN-----------LENVYTLKSMEDGLALKELLKDEE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 160 IKRVAVVGAGYIGVELAEAFQRKGKEVVLIDVVDTCLAGYYDRDLTDLMAKNMEEHGIQLAFGETVKEVAGNGKVEKIIT 239
Cdd:PRK09564 149 IKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVVT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 240 DKNEYDVDMVILAVGFRPNTT-LGNGKIDLFRNGAFLVNKRQETSIPGVYAIGDCATIYDNATRDTNYIALASNAVRTGI 318
Cdd:PRK09564 229 DKGEYEADVVIVATGVKPNTEfLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDCATIYNIVSNKNVYVPLATTANKLGR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 319 VAAHNACGTDLEGIGVQGSNGISIYGLHMVSTGLTLEKAKRLGFDAAVTEYTDnqkpefIEHGNF-----PVTIKIVYDK 393
Cdd:PRK09564 309 MVGENLAGRHVSFKGTLGSACIKVLDLEAARTGLTEEEAKKLGIDYKTVFIKD------KNHTNYypgqeDLYVKLIYEA 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489079851 394 DSRRILGAQMAAREDVSMGIHMFSLAIQEGVTIEKLALTDIFFLPHFNKPYNYITMAALGAK 455
Cdd:PRK09564 383 DTKVILGGQIIGKKGAVLRIDALAVAIYAKLTTQELGMMDFCYAPPFARTWDALNVAGNVAK 444
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
3-317 |
3.93e-66 |
|
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: 214.10 E-value: 3.93e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 3 KIVVVGANHAGTACIKTMLTNYGdanEIVVFDQNSNISFLGCGMALWIGEQIAGPEGL-----FYSDKEEL---ESLGAK 74
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGG---KVTLIEDEGTCPYGGCVLSKALLGAAEAPEIAslwadLYKRKEEVvkkLNNGIE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 75 VYMESPVQSIDYDAKTVT--ALVDGKNHVETYDKLIFATGSQPILPPIKGAEikegslefeatlENLQFVKLYQNSADVI 152
Cdd:pfam07992 79 VLLGTEVVSIDPGAKKVVleELVDGDGETITYDRLVIATGARPRLPPIPGVE------------LNVGFLVRTLDSAEAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 153 aKLENKDiKRVAVVGAGYIGVELAEAFQRKGKEVVLIDVVDTCLAGyYDRDLTDLMAKNMEEHGIQLAFGETVKEVAGNG 232
Cdd:pfam07992 147 -RLKLLP-KRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRLLRA-FDEEISAALEKALEKNGVEVRLGTSVKEIIGDG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 233 K-VEKIITDKNEYDVDMVILAVGFRPNTTL-GNGKIDLFRNGAFLVNKRQETSIPGVYAIGDCatiydnatrDTNYIALA 310
Cdd:pfam07992 224 DgVEVILKDGTEIDADLVVVAIGRRPNTELlEAAGLELDERGGIVVDEYLRTSVPGIYAAGDC---------RVGGPELA 294
|
....*..
gi 489079851 311 SNAVRTG 317
Cdd:pfam07992 295 QNAVAQG 301
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
1-403 |
6.52e-64 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 211.54 E-value: 6.52e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 1 MSKIVVVGANHAGTACIKTmLTNYGDANEIVVFDQNS-------NISflgcgmalwigEQIAG---PEGLFYSDKEELES 70
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEE-LRKLDPDGEITVIGAEPhppynrpPLS-----------KVLAGetdEEDLLLRPADFYEE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 71 LGAKVYMESPVQSIDYDAKTVTaLVDGKnhVETYDKLIFATGSQPILPPIKGAEikegslefeatLENLQFVKLYQNSAD 150
Cdd:COG1251 69 NGIDLRLGTRVTAIDRAARTVT-LADGE--TLPYDKLVLATGSRPRVPPIPGAD-----------LPGVFTLRTLDDADA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 151 VIAKLENKdiKRVAVVGAGYIGVELAEAFQRKGKEVVLIDVVDTCLAGYYDRDLTDLMAKNMEEHGIQLAFGETVKEVAG 230
Cdd:COG1251 135 LRAALAPG--KRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 231 NGKVEKIIT-DKNEYDVDMVILAVGFRPNTTLGNG-KIDLfrNGAFLVNKRQETSIPGVYAIGDCATiYDNATRDTNYIA 308
Cdd:COG1251 213 DDRVTGVRLaDGEELPADLVVVAIGVRPNTELARAaGLAV--DRGIVVDDYLRTSDPDIYAAGDCAE-HPGPVYGRRVLE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 309 LASNAVRTGIVAAHNACGTDLEGIGVQGSNGISIYGLHMVSTGLTLEkakrlgfDAAVTEYTDNQKPEFiehgnfpvtIK 388
Cdd:COG1251 290 LVAPAYEQARVAAANLAGGPAAYEGSVPSTKLKVFGVDVASAGDAEG-------DEEVVVRGDPARGVY---------KK 353
|
410
....*....|....*
gi 489079851 389 IVYDKDsrRILGAQM 403
Cdd:COG1251 354 LVLRDG--RLVGAVL 366
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
87-432 |
2.04e-50 |
|
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: 177.20 E-value: 2.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 87 DAKTVTalVDGKNHVETyDKLIFATGSQPILPPIKGaeIKEgslefeatlenlqfvKLYQNSADViakLENKDI-KRVAV 165
Cdd:COG1249 117 DPHTVE--VTGGETLTA-DHIVIATGSRPRVPPIPG--LDE---------------VRVLTSDEA---LELEELpKSLVV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 166 VGAGYIGVELAEAFQRKGKEVVLIDVVDTCLAGyYDRDLTDLMAKNMEEHGIQLAFGETVKEVAGNGKVEKIITDKNE-- 243
Cdd:COG1249 174 IGGGYIGLEFAQIFARLGSEVTLVERGDRLLPG-EDPEISEALEKALEKEGIDILTGAKVTSVEKTGDGVTVTLEDGGge 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 244 --YDVDMVILAVGFRPNTT---LGNGKIDLFRNGAFLVNKRQETSIPGVYAIGDCatiydnatrdTNYIALASNAVRTGI 318
Cdd:COG1249 253 eaVEADKVLVATGRRPNTDglgLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDV----------TGGPQLAHVASAEGR 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 319 VAAHNACG----------------TDLEgigvqgsngisiyglhMVSTGLTLEKAKRLGFDAAVTE--YTDNQKpeFIEH 380
Cdd:COG1249 323 VAAENILGkkprpvdyraipsvvfTDPE----------------IASVGLTEEEAREAGIDVKVGKfpFAANGR--ALAL 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 489079851 381 GNFPVTIKIVYDKDSRRILGAQMAArEDVSMGIHMFSLAIQEGVTIEKLALT 432
Cdd:COG1249 385 GETEGFVKLIADAETGRILGAHIVG-PHAGELIHEAALAMEMGLTVEDLADT 435
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
1-455 |
7.32e-50 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 175.36 E-value: 7.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 1 MSKIVVVGANhAGTACIKTMLTNYGDANEIVVFDQNSNISFLGCGMALWIGEQIAGPEGL-------FYSDKEelesLGA 73
Cdd:PRK13512 1 MPKIIVVGAV-AGGATCASQIRRLDKESDIIIFEKDRDMSFANCALPYYIGEVVEDRKYAlaytpekFYDRKQ----ITV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 74 KVYMEspVQSIDYDAKTVTALVDGKNHV--ETYDKLIFATGSQPILPPIkgaeikEGSLEFeaTLENLQfvklyqnSADV 151
Cdd:PRK13512 76 KTYHE--VIAINDERQTVTVLNRKTNEQfeESYDKLILSPGASANSLGF------ESDITF--TLRNLE-------DTDA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 152 IAK-LENKDIKRVAVVGAGYIGVELAEAFQRKGKEVVLIDVVDTCLAgYYDRDLTDLMAKNMEEHGIQLAFGETVKEVAG 230
Cdd:PRK13512 139 IDQfIKANQVDKALVVGAGYISLEVLENLYERGLHPTLIHRSDKINK-LMDADMNQPILDELDKREIPYRLNEEIDAING 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 231 N------GKVEkiitdkneyDVDMVILAVGFRPNTT-LGNGKIDLFRNGAFLVNKRQETSIPGVYAIGDCATIYDNATRD 303
Cdd:PRK13512 218 NevtfksGKVE---------HYDMIIEGVGTHPNSKfIESSNIKLDDKGFIPVNDKFETNVPNIYAIGDIITSHYRHVDL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 304 TNYIALASNAVRTGIVAAHNACGTDLEGI-GVQGSNGISIYGLHMVSTGLTLEKAKRlgFDAAVTEYTDNQKPEFIEhGN 382
Cdd:PRK13512 289 PASVPLAWGAHRAASIVAEQIAGNDTIEFkGFLGNNIVKFFDYTFASVGVKPNELKQ--FDYKMVEVTQGAHANYYP-GN 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489079851 383 FPVTIKIVYDKDSRRILGAQMAAREDVSMGIHMFSLAIQEGVTIEKLALTDIFFLPHFNKPYNYITMAALGAK 455
Cdd:PRK13512 366 SPLHLRVYYDTSNRKILRAAAVGKEGADKRIDVLSMAMMNQLTVDELTEFEVAYAPPYSHPKDLINMIGYKAK 438
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
87-432 |
1.24e-41 |
|
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.
Pssm-ID: 273568 [Multi-domain] Cd Length: 460 Bit Score: 153.95 E-value: 1.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 87 DAKTVtaLVDGKNHVETY--DKLIFATGSQPILPPikgaeikeGSLEFEatlenlqfVKLYQNSADVIAkLENKdIKRVA 164
Cdd:TIGR01350 115 DPGTV--SVTGENGEETLeaKNIIIATGSRPRSLP--------GPFDFD--------GKVVITSTGALN-LEEV-PESLV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 165 VVGAGYIGVELAEAFQRKGKEVVLIDVVDTCLAGYyDRDLTDLMAKNMEEHGIQLAFGETVKEVAGNGKVEKIITDKNE- 243
Cdd:TIGR01350 175 IIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGE-DAEVSKVLQKALKKKGVKILTNTKVTAVEKNDDQVTYENKGGEt 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 244 --YDVDMVILAVGFRPNTT-LGNGKIDLFRN--GAFLVNKRQETSIPGVYAIGDCatiydnatrdTNYIALASNAVRTGI 318
Cdd:TIGR01350 254 etLTGEKVLVAVGRKPNTEgLGLEKLGVELDerGRIVVDEYMRTNVPGIYAIGDV----------IGGPMLAHVASHEGI 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 319 VAAHNACGTDLEGIGVQGSNGIsIYGLHMVST-GLTLEKAKRLGFDAAVTEY---------TDNQKPEFiehgnfpvtIK 388
Cdd:TIGR01350 324 VAAENIAGKEPAHIDYDAVPSV-IYTDPEVASvGLTEEQAKEAGYDVKIGKFpfaangkalALGETDGF---------VK 393
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 489079851 389 IVYDKDSRRILGAQMAAREDVSMgIHMFSLAIQEGVTIEKLALT 432
Cdd:TIGR01350 394 IIADKKTGEILGAHIIGPHATEL-ISEAALAMELEGTVEELART 436
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
87-450 |
6.76e-37 |
|
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]
Pssm-ID: 273944 [Multi-domain] Cd Length: 463 Bit Score: 140.64 E-value: 6.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 87 DAKTVTalVDGKNHVETYDKLIFATGSQPILPPIKGaeIKEGSLefeatLENLQFVKLyqnsadviakleNKDIKRVAVV 166
Cdd:TIGR02053 114 DPKTVK--VDLGREVRGAKRFLIATGARPAIPPIPG--LKEAGY-----LTSEEALAL------------DRIPESLAVI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 167 GAGYIGVELAEAFQRKGKEVVLIDVVDTcLAGYYDRDLTDLMAKNMEEHGIQLAFGETVKEVAGNGKVEKIITDKN---- 242
Cdd:TIGR02053 173 GGGAIGVELAQAFARLGSEVTILQRSDR-LLPREEPEISAAVEEALAEEGIEVVTSAQVKAVSVRGGGKIITVEKPggqg 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 243 EYDVDMVILAVGFRPNTT---LGNGKIDLFRNGAFLVNKRQETSIPGVYAIGDCatiydnatrdTNYIALASNAVRTGIV 319
Cdd:TIGR02053 252 EVEADELLVATGRRPNTDglgLEKAGVKLDERGGILVDETLRTSNPGIYAAGDV----------TGGLQLEYVAAKEGVV 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 320 AAHNACGTDLEGIGVQGSNGISIYGLHMVSTGLTLEKAKRLGFDAAVTEYTDNQKPEFIEHGNFPVTIKIVYDKDSRRIL 399
Cdd:TIGR02053 322 AAENALGGANAKLDLLVIPRVVFTDPAVASVGLTEAEAQKAGIECDCRTLPLTNVPRARINRDTRGFIKLVAEPGTGKVL 401
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 489079851 400 GAQMAAREDVSMgIHMFSLAIQEGVTIEKLALTdifflphfnkPYNYITMA 450
Cdd:TIGR02053 402 GVQVVAPEAAEV-INEAALAIRAGMTVDDLIDT----------LHPFPTMA 441
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
87-430 |
1.27e-36 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 139.93 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 87 DAKTVTalVDGKnHVETyDKLIFATGSQpiLPPIKGAEIKEGslefeatlenlqfVKLYqNSADViakLENKDI-KRVAV 165
Cdd:PRK06292 118 DPNTVE--VNGE-RIEA-KNIVIATGSR--VPPIPGVWLILG-------------DRLL-TSDDA---FELDKLpKSLAV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 166 VGAGYIGVELAEAFQRKGKEVVLIDVVDTcLAGYYDRDLTDLMAKNMEEHgIQLAFGETVKEVAGNGKVEKIITDKN--- 242
Cdd:PRK06292 175 IGGGVIGLELGQALSRLGVKVTVFERGDR-ILPLEDPEVSKQAQKILSKE-FKIKLGAKVTSVEKSGDEKVEELEKGgkt 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 243 -EYDVDMVILAVGFRPNT-TLG--NGKIDLFRNGAFLVNKRQETSIPGVYAIGDCatiydnatrdTNYIALASNAVRTGI 318
Cdd:PRK06292 253 eTIEADYVLVATGRRPNTdGLGleNTGIELDERGRPVVDEHTQTSVPGIYAAGDV----------NGKPPLLHEAADEGR 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 319 VAAHNACGTDLEGIgvqgsNGISIYGL-----HMVSTGLTLEKAKRLGFDAAVTEY--TDNQKPEFI-EHGNFpvtIKIV 390
Cdd:PRK06292 323 IAAENAAGDVAGGV-----RYHPIPSVvftdpQIASVGLTEEELKAAGIDYVVGEVpfEAQGRARVMgKNDGF---VKVY 394
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 489079851 391 YDKDSRRILGAQMAArEDVSMGIHMFSLAIQEGVTIEKLA 430
Cdd:PRK06292 395 ADKKTGRLLGAHIIG-PDAEHLIHLLAWAMQQGLTVEDLL 433
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
79-296 |
9.94e-35 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 133.12 E-value: 9.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 79 SPVQSIDYDAKTVTAlvdgKNHVETYDKLIFATGSQPILPPIKGaeikegsLEFEATLENLQfvkLYQNSADVIAklenk 158
Cdd:PRK04965 79 TWVTDIDAEAQVVKS----QGNQWQYDKLVLATGASAFVPPIPG-------RELMLTLNSQQ---EYRAAETQLR----- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 159 DIKRVAVVGAGYIGVELAEAFQRKGKEVVLIDVVDTCLAGYYDRDLTDLMAKNMEEHGIQLAFGETVKEVAGNGKVEKII 238
Cdd:PRK04965 140 DAQRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSGIRAT 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489079851 239 TDKNE-YDVDMVILAVGFRPNTTLGNGKiDLFRNGAFLVNKRQETSIPGVYAIGDCATI 296
Cdd:PRK04965 220 LDSGRsIEVDAVIAAAGLRPNTALARRA-GLAVNRGIVVDSYLQTSAPDIYALGDCAEI 277
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
1-323 |
1.93e-34 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 132.56 E-value: 1.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 1 MSKIVVVGANHAGTACIKTMLTNYGDANEIVVFDQNSNISFLgcGMALWIgeqIAG---PEGLFYSDKEELESLGAKVYM 77
Cdd:COG1252 1 MKRIVIVGGGFAGLEAARRLRKKLGGDAEVTLIDPNPYHLFQ--PLLPEV---AAGtlsPDDIAIPLRELLRRAGVRFIQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 78 ESpVQSIDYDAKTVTaLVDGKNHveTYDKLIFATGSQPILPPIKGAEikEGSLEFEaTLEnlQFVKLYQNSADVIAKLEN 157
Cdd:COG1252 76 GE-VTGIDPEARTVT-LADGRTL--SYDYLVIATGSVTNFFGIPGLA--EHALPLK-TLE--DALALRERLLAAFERAER 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 158 KDIKRVAVVGAGYIGVELA----EAFQRKGK---------EVVLIDVVDTCLAGyYDRDLTDLMAKNMEEHGIQLAFGET 224
Cdd:COG1252 147 RRLLTIVVVGGGPTGVELAgelaELLRKLLRypgidpdkvRITLVEAGPRILPG-LGEKLSEAAEKELEKRGVEVHTGTR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 225 VKEVAGNGkVekIITDKNEYDVDMVILAVGFRPNTTLGNGKIDLFRNGAFLVNKRQET-SIPGVYAIGDCATIYDNAtrD 303
Cdd:COG1252 226 VTEVDADG-V--TLEDGEEIPADTVIWAAGVKAPPLLADLGLPTDRRGRVLVDPTLQVpGHPNVFAIGDCAAVPDPD--G 300
|
330 340
....*....|....*....|
gi 489079851 304 TNYIALASNAVRTGIVAAHN 323
Cdd:COG1252 301 KPVPKTAQAAVQQAKVLAKN 320
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
87-439 |
9.07e-32 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 126.41 E-value: 9.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 87 DAKTVTALVDGKNHVETYDKLIFATGSQPILPPikGAEIKEGSLE--FEATleNLQFVKlyqnsadviaklenkdiKRVA 164
Cdd:PRK06416 118 DPNTVRVMTEDGEQTYTAKNIILATGSRPRELP--GIEIDGRVIWtsDEAL--NLDEVP-----------------KSLV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 165 VVGAGYIGVELAEAFQRKGKEVVLIDVVDTCLAGyYDRDLTDLMAKNMEEHGIQLAFGETVKEV-----------AGNGK 233
Cdd:PRK06416 177 VIGGGYIGVEFASAYASLGAEVTIVEALPRILPG-EDKEISKLAERALKKRGIKIKTGAKAKKVeqtddgvtvtlEDGGK 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 234 VEKIitdkneyDVDMVILAVGFRPNTT-LG--NGKIDLFRnGAFLVNKRQETSIPGVYAIGDCATiydnatrdtnYIALA 310
Cdd:PRK06416 256 EETL-------EADYVLVAVGRRPNTEnLGleELGVKTDR-GFIEVDEQLRTNVPNIYAIGDIVG----------GPMLA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 311 SNAVRTGIVAAHNACGTDLEgigvqgsngISIYGLHMV--------STGLTLEKAKRLGFDAAVTEYtdnqkpEFIehGN 382
Cdd:PRK06416 318 HKASAEGIIAAEAIAGNPHP---------IDYRGIPAVtythpevaSVGLTEAKAKEEGFDVKVVKF------PFA--GN 380
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489079851 383 -----------FpvtIKIVYDKDSRRILGAQMAAREdVSMGIHMFSLAIQEGVTIEKLALTdIFflPH 439
Cdd:PRK06416 381 gkalalgetdgF---VKLIFDKKDGEVLGAHMVGAR-ASELIQEAQLAINWEATPEDLALT-IH--PH 441
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
4-296 |
1.12e-31 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 128.41 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 4 IVVVGANHAGTACIKTMLTNYGDANEIVVFDQNSNISFLGCGMAL-----WIGEQIAGPEGLFYSDKeeleslGAKVYME 78
Cdd:TIGR02374 1 LVLVGNGMAGHRCIEEVLKLNRHMFEITIFGEEPHPNYNRILLSSvlqgeADLDDITLNSKDWYEKH------GITLYTG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 79 SPVQSIDYDAKTVtalVDGKNHVETYDKLIFATGSQPILPPIKGAEiKEGSLEFEaTLENLQFVklyQNSAdviaklenK 158
Cdd:TIGR02374 75 ETVIQIDTDQKQV---ITDAGRTLSYDKLILATGSYPFILPIPGAD-KKGVYVFR-TIEDLDAI---MAMA--------Q 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 159 DIKRVAVVGAGYIGVELAEAFQRKGKEVVLIDVVDTCLAGYYDRDLTDLMAKNMEEHGIQLAFGETVKEVAGNGKVEKI- 237
Cdd:TIGR02374 139 RFKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIr 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 238 ITDKNEYDVDMVILAVGFRPNTTLG-NGKIDLfrNGAFLVNKRQETSIPGVYAIGDCATI 296
Cdd:TIGR02374 219 FKDGSSLEADLIVMAAGIRPNDELAvSAGIKV--NRGIIVNDSMQTSDPDIYAVGECAEH 276
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
87-293 |
1.19e-30 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 122.96 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 87 DAKTVTalVDGKNHveTYDKLIFATGSQPILPPIKGAEIKEGSLEFEAtLENLQfvklyqnsadviaklenkdiKRVAVV 166
Cdd:PRK06116 119 DAHTVE--VNGERY--TADHILIATGGRPSIPDIPGAEYGITSDGFFA-LEELP--------------------KRVAVV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 167 GAGYIGVELAEAFQRKGKEVVLIDVVDTCLAGyYDRDLTDLMAKNMEEHGIQLAFGETVKEVA--GNGKVEKIITDKNEY 244
Cdd:PRK06116 174 GAGYIAVEFAGVLNGLGSETHLFVRGDAPLRG-FDPDIRETLVEEMEKKGIRLHTNAVPKAVEknADGSLTLTLEDGETL 252
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489079851 245 DVDMVILAVGFRPNTT---LGNGKIDLFRNGAFLVNKRQETSIPGVYAIGDC 293
Cdd:PRK06116 253 TVDCLIWAIGREPNTDglgLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDV 304
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
52-324 |
1.20e-29 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 117.53 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 52 EQIAGPEglfYSDK--EELESLGAKVYMESpVQSIDYDAKTVTALVDGKNHVETyDKLIFATGSQPILPPIKGAEikegs 129
Cdd:COG0492 52 EGISGPE---LAERlrEQAERFGAEILLEE-VTSVDKDDGPFRVTTDDGTEYEA-KAVIIATGAGPRKLGLPGEE----- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 130 lEFE-------ATLENLQFVKlyqnsadviaklenkdiKRVAVVGAGYIGVELAEAFQRKGKEVVLIdvvdtclagyYDR 202
Cdd:COG0492 122 -EFEgrgvsycATCDGFFFRG-----------------KDVVVVGGGDSALEEALYLTKFASKVTLI----------HRR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 203 D---LTDLMAKNMEEH-GIQLAFGETVKEVAGNGKVEKIITDKN------EYDVDMVILAVGFRPNTTLGNGK-IDLFRN 271
Cdd:COG0492 174 DelrASKILVERLRANpKIEVLWNTEVTEIEGDGRVEGVTLKNVktgeekELEVDGVFVAIGLKPNTELLKGLgLELDED 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 489079851 272 GAFLVNKRQETSIPGVYAIGDCAtiydnatrdTNYIALASNAVRTGIVAAHNA 324
Cdd:COG0492 254 GYIVVDEDMETSVPGVFAAGDVR---------DYKYRQAATAAGEGAIAALSA 297
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
87-430 |
3.57e-27 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 113.37 E-value: 3.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 87 DAKTVTalVDGKnhVETYDKLIFATGSQPILPPIKG-AEIKegslefeatlenlqfvklYQNSADVIAkLENKDiKRVAV 165
Cdd:PRK06370 121 SPNTVR--VGGE--TLRAKRIFINTGARAAIPPIPGlDEVG------------------YLTNETIFS-LDELP-EHLVI 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 166 VGAGYIGVELAEAFQRKGKEVVLIDVVDTcLAGYYDRDLTDLMAKNMEEHGIQLAFGETVKEVA--GNGKVEKIITDKNE 243
Cdd:PRK06370 177 IGGGYIGLEFAQMFRRFGSEVTVIERGPR-LLPREDEDVAAAVREILEREGIDVRLNAECIRVErdGDGIAVGLDCNGGA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 244 YDV--DMVILAVGFRPNTT-LGNGK--IDLFRNGAFLVNKRQETSIPGVYAIGDC------ATIYDNATRdtnyialasn 312
Cdd:PRK06370 256 PEItgSHILVAVGRVPNTDdLGLEAagVETDARGYIKVDDQLRTTNPGIYAAGDCngrgafTHTAYNDAR---------- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 313 avrtgIVAAhNAcgtdLEGIGVQGSNGISIYGLH----MVSTGLTLEKAKRLGFDAAVTEYTDNQKPEFIEHGNFPVTIK 388
Cdd:PRK06370 326 -----IVAA-NL----LDGGRRKVSDRIVPYATYtdppLARVGMTEAEARKSGRRVLVGTRPMTRVGRAVEKGETQGFMK 395
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 489079851 389 IVYDKDSRRILGAQMAAREDVSMgIHMFSLAIQEGVTIEKLA 430
Cdd:PRK06370 396 VVVDADTDRILGATILGVHGDEM-IHEILDAMYAGAPYTTLS 436
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
87-449 |
2.85e-21 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 96.37 E-value: 2.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 87 DAKTVT-ALVDGKNHVETYDKLIFATGSQPILPPIKGaeIKEGSlefeatlenlqfvklYQNSADViakLENKDI-KRVA 164
Cdd:PRK13748 215 DDQTLIvRLNDGGERVVAFDRCLIATGASPAVPPIPG--LKETP---------------YWTSTEA---LVSDTIpERLA 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 165 VVGAGYIGVELAEAFQRKGKEVvlidvvdTCLAG---YYDRD--LTDLMAKNMEEHGIQLAFGETVKEVAGNGKVEKIIT 239
Cdd:PRK13748 275 VIGSSVVALELAQAFARLGSKV-------TILARstlFFREDpaIGEAVTAAFRAEGIEVLEHTQASQVAHVDGEFVLTT 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 240 DKNEYDVDMVILAVGFRPNT---TLGNGKIDLFRNGAFLVNKRQETSIPGVYAIGDCatiydnatrdTN-----YIALAS 311
Cdd:PRK13748 348 GHGELRADKLLVATGRAPNTrslALDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDC----------TDqpqfvYVAAAA 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 312 navrtGIVAAHNACGTDLEgIGVQGSNGISIYGLHMVSTGLTLEKAKRLGFDAAVTEYTDNQKPEFIehGNFPVT--IKI 389
Cdd:PRK13748 418 -----GTRAAINMTGGDAA-LDLTAMPAVVFTDPQVATVGYSEAEAHHDGIETDSRTLTLDNVPRAL--ANFDTRgfIKL 489
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 390 VYDKDSRRILGAQMAAREDVSMgIHMFSLAIQEGVTIEKLAltDIFFlPhfnkpynYITM 449
Cdd:PRK13748 490 VIEEGSGRLIGVQAVAPEAGEL-IQTAALAIRNRMTVQELA--DQLF-P-------YLTM 538
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
86-448 |
3.33e-20 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 92.50 E-value: 3.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 86 YDAKT------VTALVDGKNHVE-TYDKLIFATGSQPILPPIKGaeIKEGSLEFEATlenlqfvklyqnsadVIAKLENK 158
Cdd:PRK07251 94 YDAEAhfvsnkVIEVQAGDEKIElTAETIVINTGAVSNVLPIPG--LADSKHVYDST---------------GIQSLETL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 159 DiKRVAVVGAGYIGVELAEAFQRKGKEVVLIDVVDTCLaGYYDRDLTDLMAKNMEEHGIQLAFGETVKEVAGNGKVEKII 238
Cdd:PRK07251 157 P-ERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTIL-PREEPSVAALAKQYMEEDGITFLLNAHTTEVKNDGDQVLVV 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 239 TDKNEYDVDMVILAVGFRPNTT---LGNGKIDLFRNGAFLVNKRQETSIPGVYAIGDCatiydNATRDTNYIALASNAVR 315
Cdd:PRK07251 235 TEDETYRFDALLYATGRKPNTEplgLENTDIELTERGAIKVDDYCQTSVPGVFAVGDV-----NGGPQFTYISLDDFRIV 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 316 TGIVAahnacGTDLEGIGVQGSNGISIYGLHMVST-GLTLEKAKRLGFDAAVTEYTDNQKPEFIEHGNFPVTIKIVYDKD 394
Cdd:PRK07251 310 FGYLT-----GDGSYTLEDRGNVPTTMFITPPLSQvGLTEKEAKEAGLPYAVKELLVAAMPRAHVNNDLRGAFKVVVNTE 384
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 489079851 395 SRRILGAQmaaredvsmgihMFSLAIQEGVTIEKLALTDifflphfNKPYNYIT 448
Cdd:PRK07251 385 TKEILGAT------------LFGEGSQEIINLITMAMDN-------KIPYTYFK 419
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
69-295 |
9.04e-20 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 92.49 E-value: 9.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 69 ESLGAKVYMESPVQSIDYDAKTVTAlvdGKNHVETYDKLIFATGSQPILPPIKGAEIKEGSLefEATLENLqfvklyqNS 148
Cdd:PRK14989 70 EKHGIKVLVGERAITINRQEKVIHS---SAGRTVFYDKLIMATGSYPWIPPIKGSETQDCFV--YRTIEDL-------NA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 149 ADVIAKLEnkdiKRVAVVGAGYIGVELAEAFQRKGKEVVLIDVVDTCLAGYYDRDLTDLMAKNMEEHGIQLAFGETVKEV 228
Cdd:PRK14989 138 IEACARRS----KRGAVVGGGLLGLEAAGALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEI 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489079851 229 AGNGKVEK---IITDKNEYDVDMVILAVGFRPNTTLGNG-KIDLFRNGAFLVNKRQETSIPGVYAIGDCAT 295
Cdd:PRK14989 214 VQEGVEARktmRFADGSELEVDFIVFSTGIRPQDKLATQcGLAVAPRGGIVINDSCQTSDPDIYAIGECAS 284
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
95-430 |
9.81e-19 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 88.44 E-value: 9.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 95 VDGKNHVE-TYDKLIFATGSQPI-LP--PIKGAEI--KEGSLEFEATlenlqfvklyqnsadviaklenkdIKRVAVVGA 168
Cdd:PRK06327 136 VTGEDETViTAKHVIIATGSEPRhLPgvPFDNKIIldNTGALNFTEV------------------------PKKLAVIGA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 169 GYIGVELAEAFQRKGKEVVLIDVVDTCLAGyYDRDLTDLMAKNMEEHGIQLAFGETVKEVAGNGK-VEKIITDKN----E 243
Cdd:PRK06327 192 GVIGLELGSVWRRLGAEVTILEALPAFLAA-ADEQVAKEAAKAFTKQGLDIHLGVKIGEIKTGGKgVSVAYTDADgeaqT 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 244 YDVDMVILAVGFRPNTT-LGNGKIDLFRN--GAFLVNKRQETSIPGVYAIGDCatiydnatrdTNYIALASNAVRTGIVA 320
Cdd:PRK06327 271 LEVDKLIVSIGRVPNTDgLGLEAVGLKLDerGFIPVDDHCRTNVPNVYAIGDV----------VRGPMLAHKAEEEGVAV 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 321 AHNACGTDlegiGVQGSNGIS--IYGLHMVST-GLTLEKAKRLGFDAAVTEYTDNQKPEFIEHGNFPVTIKIVYDKDSRR 397
Cdd:PRK06327 341 AERIAGQK----GHIDYNTIPwvIYTSPEIAWvGKTEQQLKAEGVEYKAGKFPFMANGRALAMGEPDGFVKIIADAKTDE 416
|
330 340 350
....*....|....*....|....*....|...
gi 489079851 398 ILGAQMAAREdVSMGIHMFSLAIQEGVTIEKLA 430
Cdd:PRK06327 417 ILGVHVIGPN-ASELIAEAVVAMEFKASSEDIA 448
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
162-239 |
1.54e-17 |
|
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: 76.86 E-value: 1.54e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489079851 162 RVAVVGAGYIGVELAEAFQRKGKEVVLIDVVDTCLAGyYDRDLTDLMAKNMEEHGIQLAFGETVKEVAGNGKVEKIIT 239
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLPG-FDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVL 77
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
96-403 |
3.19e-17 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 83.71 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 96 DGKNHVETYDKLIFATGSQPILPPIKGAEIKEGSLEfEATLENLQfvklyqnsadviaklenkdiKRVAVVGAGYIGVEL 175
Cdd:PLN02507 160 DGTKLRYTAKHILIATGSRAQRPNIPGKELAITSDE-ALSLEELP--------------------KRAVVLGGGYIAVEF 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 176 AEAFQRKGKEVVLIDVVDTCLAGyYDRDLTDLMAKNMEEHGIQLAFGETVKEVAGNGKVEKIITDK-NEYDVDMVILAVG 254
Cdd:PLN02507 219 ASIWRGMGATVDLFFRKELPLRG-FDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGGIKVITDHgEEFVADVVLFATG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 255 FRPNTT---LGNGKIDLFRNGAFLVNKRQETSIPGVYAIGDCatiydnatrdTNYIALASNAVRTGIVAAHNACG----- 326
Cdd:PLN02507 298 RAPNTKrlnLEAVGVELDKAGAVKVDEYSRTNIPSIWAIGDV----------TNRINLTPVALMEGTCFAKTVFGgqptk 367
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489079851 327 TDLEGIgvqGSNGISIYGLHMVstGLTLEKA-KRLGFDAAVTEYTDNQKPEFIEHGNFPVTIKIVYDKDSRRILGAQM 403
Cdd:PLN02507 368 PDYENV---ACAVFCIPPLSVV--GLSEEEAvEQAKGDILVFTSSFNPMKNTISGRQEKTVMKLIVDAETDKVLGASM 440
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
76-299 |
2.23e-16 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 81.59 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 76 YMESPVQSIDYDAKTVTALVDGKnhVETYDKLIFATGSQPILPPIKGAEIkegslefeaTLENLQFVKLyqnsadviakl 155
Cdd:PTZ00058 177 ADESDDDEVTIVSAGVSQLDDGQ--VIEGKNILIAVGNKPIFPDVKGKEF---------TISSDDFFKI----------- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 156 enKDIKRVAVVGAGYIGVELAEAFQRKGKEVVLIdVVDTCLAGYYDRDLTDLMAKNMEEHGIQLAFGETVKEVAgngKVE 235
Cdd:PTZ00058 235 --KEAKRIGIAGSGYIAVELINVVNRLGAESYIF-ARGNRLLRKFDETIINELENDMKKNNINIITHANVEEIE---KVK 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489079851 236 K-----IITDKNEYD-VDMVILAVGFRPNTTLGN--GKIDLFRNGAFLVNKRQETSIPGVYAIGDCATIYDN 299
Cdd:PTZ00058 309 EknltiYLSDGRKYEhFDYVIYCVGRSPNTEDLNlkALNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKKN 380
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
105-311 |
6.85e-15 |
|
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.
Pssm-ID: 200098 [Multi-domain] Cd Length: 486 Bit Score: 76.55 E-value: 6.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 105 DKLIFATGSQPILPPIKGAEIKEGSLEfeatlenlqfvKLYQNSADviaklenkdiKRVAVVGAGYIGVELA---EAFQR 181
Cdd:TIGR01423 153 EHILLATGSWPQMLGIPGIEHCISSNE-----------AFYLDEPP----------RRVLTVGGGFISVEFAgifNAYKP 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 182 KGKEVVLIDVVDTCLAGYyDRDLTDLMAKNMEEHGIQLAFGETVKEVAGNGKVEKIITDKN--EYDVDMVILAVGFRPNT 259
Cdd:TIGR01423 212 RGGKVTLCYRNNMILRGF-DSTLRKELTKQLRANGINIMTNENPAKVTLNADGSKHVTFESgkTLDVDVVMMAIGRVPRT 290
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489079851 260 ---TLGNGKIDLFRNGAFLVNKRQETSIPGVYAIGDCA------------------TIYDNATRDTNYIALAS 311
Cdd:TIGR01423 291 qtlQLDKVGVELTKKGAIQVDEFSRTNVPNIYAIGDVTdrvmltpvainegaafvdTVFGNKPRKTDHTRVAS 363
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
97-403 |
8.50e-15 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 76.21 E-value: 8.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 97 GKNHVETYDKLIFATGSQPILPPIKGAEIKEGSleFEATlenlQFVKLYQNSAdviaklenkdikRVAVVGAGYIGVELA 176
Cdd:PRK08010 113 EGNLEIHGEKIFINTGAQTVVPPIPGITTTPGV--YDST----GLLNLKELPG------------HLGILGGGYIGVEFA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 177 EAFQRKGKEVVLIDVVDTCLAgYYDRDLTDLMAKNMEEHGIQLAFGETVKEVAGNGKVEKIITDKNEYDVDMVILAVGFR 256
Cdd:PRK08010 175 SMFANFGSKVTILEAASLFLP-REDRDIADNIATILRDQGVDIILNAHVERISHHENQVQVHSEHAQLAVDALLIASGRQ 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 257 PNTT---LGNGKIDLFRNGAFLVNKRQETSIPGVYAIGDCatiydNATRDTNYIALAS-NAVRTGIVAAHNACGTDLEGI 332
Cdd:PRK08010 254 PATAslhPENAGIAVNERGAIVVDKYLHTTADNIWAMGDV-----TGGLQFTYISLDDyRIVRDELLGEGKRSTDDRKNV 328
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489079851 333 GvqgsngisiYGLHMV----STGLTLEKAKRLGFDAAVTEYTDNQKPEFIEHGNFPVTIKIVYDKDSRRILGAQM 403
Cdd:PRK08010 329 P---------YSVFMTpplsRVGMTEEQARESGADIQVVTLPVAAIPRARVMNDTRGVLKAIVDNKTQRILGASL 394
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
87-450 |
2.39e-14 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 74.81 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 87 DAKTVtALVDGKNHVETY--DKLIFATGSQPILPPikgaeikegSLEFEATlenlqfvKLYqNSaDVIAKLEnKDIKRVA 164
Cdd:PRK05249 120 DPHTV-EVECPDGEVETLtaDKIVIATGSRPYRPP---------DVDFDHP-------RIY-DS-DSILSLD-HLPRSLI 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 165 VVGAGYIGVELAEAFQRKGKEVVLIDVVDTCLAgYYDRDLTDLMAKNMEEHGIQLAFGETVKEVAG----------NGKv 234
Cdd:PRK05249 180 IYGAGVIGCEYASIFAALGVKVTLINTRDRLLS-FLDDEISDALSYHLRDSGVTIRHNEEVEKVEGgddgvivhlkSGK- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 235 eKIITdkneydvDMVILAVGFRPNT-TLGNGKIDLFRN--GAFLVNKRQETSIPGVYAIGDcaTIydnatrdtNYIALAS 311
Cdd:PRK05249 258 -KIKA-------DCLLYANGRTGNTdGLNLENAGLEADsrGQLKVNENYQTAVPHIYAVGD--VI--------GFPSLAS 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 312 NAVRTGIVAAHNACG-TDLEGIGVQgsnGISIYGLHMVST-GLTLE--KAKRLGFDAAVTEYTDNQKPEFI--EHGnfpv 385
Cdd:PRK05249 320 ASMDQGRIAAQHAVGeATAHLIEDI---PTGIYTIPEISSvGKTEQelTAAKVPYEVGRARFKELARAQIAgdNVG---- 392
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489079851 386 TIKIVYDKDSRRILGAQMAArEDVSMGIHMFSLAIQEGVTIEklaltdiFFLphfNKPYNYITMA 450
Cdd:PRK05249 393 MLKILFHRETLEILGVHCFG-ERATEIIHIGQAIMEQKGTIE-------YFV---NTTFNYPTMA 446
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
87-425 |
2.85e-14 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 74.91 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 87 DAKTVTalVDGKNHveTYDKLIFATGSQPILPPIKGAEikegslefeatlenlqfvklYQNSADVIAKLENKDiKRVAVV 166
Cdd:PLN02546 204 DPHTVD--VDGKLY--TARNILIAVGGRPFIPDIPGIE--------------------HAIDSDAALDLPSKP-EKIAIV 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 167 GAGYIGVELAEAFQRKGKEVVLIDVVDTCLAGYyDRDLTDLMAKNMEEHGIQLAFGETVKEV--AGNGKVEkIITDKNEY 244
Cdd:PLN02546 259 GGGYIALEFAGIFNGLKSDVHVFIRQKKVLRGF-DEEVRDFVAEQMSLRGIEFHTEESPQAIikSADGSLS-LKTNKGTV 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 245 D-VDMVILAVGFRPNTT---LGNGKIDLFRNGAFLVNKRQETSIPGVYAIGDCatiydnatrdTNYIALASNAVRTGIVA 320
Cdd:PLN02546 337 EgFSHVMFATGRKPNTKnlgLEEVGVKMDKNGAIEVDEYSRTSVPSIWAVGDV----------TDRINLTPVALMEGGAL 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 321 AHNACGT-----DLEGI--GVQGSNGISiyglhmvSTGLTLEKAKRLGFDAAVteYTDNQKPEFIEHGNFP--VTIKIVY 391
Cdd:PLN02546 407 AKTLFGNeptkpDYRAVpsAVFSQPPIG-------QVGLTEEQAIEEYGDVDV--FTANFRPLKATLSGLPdrVFMKLIV 477
|
330 340 350
....*....|....*....|....*....|....
gi 489079851 392 DKDSRRILGAQMAArEDVSMGIHMFSLAIQEGVT 425
Cdd:PLN02546 478 CAKTNKVLGVHMCG-EDAPEIIQGFAVAVKAGLT 510
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
97-401 |
2.94e-14 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 74.61 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 97 GKNHVETYDKLIFATGSQPILPPIkgaeIKEGSLEfeatlenlqfvklYQNSADV--IAKLEnkdiKRVAVVGAGYIGVE 174
Cdd:PRK07846 122 GDGEEITADQVVIAAGSRPVIPPV----IADSGVR-------------YHTSDTImrLPELP----ESLVIVGGGFIAAE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 175 LAEAFQRKGKEVVLIdVVDTCLAGYYDRDL----TDLMAKNMEEHGiqlafGETVKEVAGNGK-VEKIITDKNEYDVDMV 249
Cdd:PRK07846 181 FAHVFSALGVRVTVV-NRSGRLLRHLDDDIserfTELASKRWDVRL-----GRNVVGVSQDGSgVTLRLDDGSTVEADVL 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 250 ILAVGFRPNTTL---GNGKIDLFRNGAFLVNKRQETSIPGVYAIGDCATIYDnatrdtnyiaLASNAVRTGIVAAHN-AC 325
Cdd:PRK07846 255 LVATGRVPNGDLldaAAAGVDVDEDGRVVVDEYQRTSAEGVFALGDVSSPYQ----------LKHVANHEARVVQHNlLH 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 326 GTDLEGI-------GVQGSNGISiyglhmvSTGLTLEKAKRLGFD--AAVTEYTDnqkpefIEHG-------NFpvtIKI 389
Cdd:PRK07846 325 PDDLIASdhrfvpaAVFTHPQIA-------SVGLTENEARAAGLDitVKVQNYGD------VAYGwamedttGF---VKL 388
|
330
....*....|..
gi 489079851 390 VYDKDSRRILGA 401
Cdd:PRK07846 389 IADRDTGRLLGA 400
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
102-322 |
8.16e-13 |
|
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: 69.78 E-value: 8.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 102 ETYDKLIFATGSQ-PILPPIKGAEIK--EGSLEFeatlenlqfvkLYQNSADVIAKLENKDIKRVAVVGAGYIGVELAEA 178
Cdd:COG0493 205 EEFDAVFLATGAGkPRDLGIPGEDLKgvHSAMDF-----------LTAVNLGEAPDTILAVGKRVVVIGGGNTAMDCART 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 179 FQRKG-KEVVLIdvvdtclagyYDRDLTDLMAKNME-----EHGIQLAFGETVKEVAG--NGKVEKIITDKNE------- 243
Cdd:COG0493 274 ALRLGaESVTIV----------YRRTREEMPASKEEveealEEGVEFLFLVAPVEIIGdeNGRVTGLECVRMElgepdes 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 244 --------------YDVDMVILAVGFRPNTT--LGNGKIDLFRNGAFLVNKR-QETSIPGVYAIGDCATIYDNATRdtny 306
Cdd:COG0493 344 grrrpvpiegseftLPADLVILAIGQTPDPSglEEELGLELDKRGTIVVDEEtYQTSLPGVFAGGDAVRGPSLVVW---- 419
|
250
....*....|....*.
gi 489079851 307 ialasnAVRTGIVAAH 322
Cdd:COG0493 420 ------AIAEGRKAAR 429
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
66-295 |
7.97e-12 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 66.17 E-value: 7.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 66 EELESLGA------KVYMESPVQSIDYDAKtVTALVDGKNHVETYDKLIFATGS-QPILPPIKGAEIK--EGSLEFeatl 136
Cdd:PRK12770 76 KELEEAGVvfhtrtKVCCGEPLHEEEGDEF-VERIVSLEELVKKYDAVLIATGTwKSRKLGIPGEDLPgvYSALEY---- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 137 enLQFVKLYQnsadvIAKLENKDI-----KRVAVVGAGYIGVELA-EAFQRKGKEVVLIdvvdtclagyYDRDLTDLMA- 209
Cdd:PRK12770 151 --LFRIRAAK-----LGYLPWEKVppvegKKVVVVGAGLTAVDAAlEAVLLGAEKVYLA----------YRRTINEAPAg 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 210 ----KNMEEHGIQLAFGETVKEVAGNGKVEKI--------------------ITDKN-EYDVDMVILAVGFRPNTTLGNG 264
Cdd:PRK12770 214 kyeiERLIARGVEFLELVTPVRIIGEGRVEGVelakmrlgepdesgrprpvpIPGSEfVLEADTVVFAIGEIPTPPFAKE 293
|
250 260 270
....*....|....*....|....*....|...
gi 489079851 265 K--IDLFRNGAFLVNKRQETSIPGVYAIGDCAT 295
Cdd:PRK12770 294 ClgIELNRKGEIVVDEKHMTSREGVFAAGDVVT 326
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
87-294 |
1.35e-11 |
|
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: 66.41 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 87 DAKTVTA-LVDGKNHVETYDKLIFATGSQPILPPIKGAeikegslefeatlenlqfvKLYQNSADVIAKLEnKDIKRVAV 165
Cdd:TIGR01438 126 DKHRIKAtNKKGKEKIYSAERFLIATGERPRYPGIPGA-------------------KELCITSDDLFSLP-YCPGKTLV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 166 VGAGYIGVELAEAFQRKGKEVVLIdVVDTCLAGYyDRDLTDLMAKNMEEHGIQLAFGETVKEV-AGNGKVEKIITDKNEY 244
Cdd:TIGR01438 186 VGASYVALECAGFLAGIGLDVTVM-VRSILLRGF-DQDCANKVGEHMEEHGVKFKRQFVPIKVeQIEAKVLVEFTDSTNG 263
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489079851 245 DV---DMVILAVGFRPNT-TLG----NGKIDLfRNGAFLVNKRQETSIPGVYAIGDCA 294
Cdd:TIGR01438 264 IEeeyDTVLLAIGRDACTrKLNlenvGVKINK-KTGKIPADEEEQTNVPYIYAVGDIL 320
|
|
| Pyr_redox_dim |
pfam02852 |
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both ... |
349-440 |
5.90e-11 |
|
Pyridine nucleotide-disulphide oxidoreductase, dimerization domain; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.
Pssm-ID: 427019 [Multi-domain] Cd Length: 109 Bit Score: 59.10 E-value: 5.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 349 STGLTLEKAKRLGFDAAVTEYTDNQKPEFIEHGNFPVTIKIVYDKDSRRILGAQMAArEDVSMGIHMFSLAIQEGVTIEK 428
Cdd:pfam02852 13 SVGLTEEEAKEKGGEVKVGKFPFAANGRALAYGDTDGFVKLVADRETGKILGAHIVG-PNAGELIQEAALAIKMGATVED 91
|
90
....*....|..
gi 489079851 429 LALTdIFFLPHF 440
Cdd:pfam02852 92 LANT-IHIHPTL 102
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
161-295 |
7.22e-11 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 64.04 E-value: 7.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 161 KRVAVVGAGYIGVELAEAFQRKGKEVVlidvvdTCLagyYDRDLTDLMA-----KNMEEHGIQLAFGETVKEVAGNGKVE 235
Cdd:PRK11749 274 KRVVVIGGGNTAMDAARTAKRLGAESV------TIV---YRRGREEMPAseeevEHAKEEGVEFEWLAAPVEILGDEGRV 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 236 KIIT-DKNE--------------------YDVDMVILAVGFRPNTTLGNG--KIDLFRNGAFLVN-KRQETSIPGVYAIG 291
Cdd:PRK11749 345 TGVEfVRMElgepdasgrrrvpiegseftLPADLVIKAIGQTPNPLILSTtpGLELNRWGTIIADdETGRTSLPGVFAGG 424
|
....
gi 489079851 292 DCAT 295
Cdd:PRK11749 425 DIVT 428
|
|
| AhpF |
TIGR03140 |
alkyl hydroperoxide reductase subunit F; This enzyme is the partner of the peroxiredoxin ... |
161-296 |
1.21e-10 |
|
alkyl hydroperoxide reductase subunit F; This enzyme is the partner of the peroxiredoxin (alkyl hydroperoxide reductase) AhpC which contains the peroxide-reactive cysteine. AhpF contains the reductant (NAD(P)H) binding domain (pfam00070) and presumably acts to resolve the disulfide which forms after oxidation of the active site cysteine in AphC. This proteins contains two paired conserved cysteine motifs, CxxCP and CxHCDGP. [Cellular processes, Detoxification, Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 274444 [Multi-domain] Cd Length: 515 Bit Score: 63.54 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 161 KRVAVVGAGYIGVELAEAFQRKGKEVVLIDVVDTCLAgyyDRDLTDlmaKNMEEHGIQLAFGETVKEVAGNG-KVEKI-I 238
Cdd:TIGR03140 353 KDVAVIGGGNSGIEAAIDLAGIVRHVTVLEFADELKA---DKVLQD---KLKSLPNVDILTSAQTTEIVGDGdKVTGIrY 426
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489079851 239 TDKN-----EYDVDMVILAVGFRPNTTLGNGKIDLFRNGAFLVNKRQETSIPGVYAIGDCATI 296
Cdd:TIGR03140 427 QDRNsgeekQLDLDGVFVQIGLVPNTEWLKDAVELNRRGEIVIDERGRTSVPGIFAAGDVTTV 489
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
76-321 |
1.67e-10 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 62.86 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 76 YMESPVQSIDYDAKTVTALVDGKNHVET-------YDKLIFATGSQPILPPIKGAEikegslefeatlENLQFVK----- 143
Cdd:PTZ00318 79 YLRAVVYDVDFEEKRVKCGVVSKSNNANvntfsvpYDKLVVAHGARPNTFNIPGVE------------ERAFFLKevnha 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 144 ------LYQN----SADVIAKLENKDIKRVAVVGAGYIGVE----LAEAFQRKGK----------EVVLIDVVDTCLaGY 199
Cdd:PTZ00318 147 rgirkrIVQCieraSLPTTSVEERKRLLHFVVVGGGPTGVEfaaeLADFFRDDVRnlnpelveecKVTVLEAGSEVL-GS 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 200 YDRDLTDLMAKNMEEHGIQLAFGETVKEVAgngKVEKIITDKNEYDVDMVILAVGFRPNTTLGNGKIDLFRNGAFLVNKR 279
Cdd:PTZ00318 226 FDQALRKYGQRRLRRLGVDIRTKTAVKEVL---DKEVVLKDGEVIPTGLVVWSTGVGPGPLTKQLKVDKTSRGRISVDDH 302
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 489079851 280 -QETSIPGVYAIGDCATIYDNatrdtNYIALASNAVRTGIVAA 321
Cdd:PTZ00318 303 lRVKPIPNVFALGDCAANEER-----PLPTLAQVASQQGVYLA 340
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
162-326 |
2.63e-10 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 62.18 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 162 RVAVVGAGYIGVELAEAFQRKGKEVVLIDVVDTCLAGYyDRDLTDLMAKNMEEHGIQL---AFGETVkEVAGNGkVEKII 238
Cdd:PRK07845 179 HLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVLPGE-DADAAEVLEEVFARRGMTVlkrSRAESV-ERTGDG-VVVTL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 239 TDKNEYDVDMVILAVGFRPNTT---LGNGKIDLFRNGAFLVNKRQETSIPGVYAIGDCatiydnatrdTNYIALASNAVR 315
Cdd:PRK07845 256 TDGRTVEGSHALMAVGSVPNTAglgLEEAGVELTPSGHITVDRVSRTSVPGIYAAGDC----------TGVLPLASVAAM 325
|
170
....*....|.
gi 489079851 316 TGIVAAHNACG 326
Cdd:PRK07845 326 QGRIAMYHALG 336
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
4-326 |
1.34e-09 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 59.55 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 4 IVVVGANHAGTACIKTmLTNYGDANEIVVFDQNSNISFlgcgmalwigEQIAGPEGLFYSDKEELESL-GAKVYMES--- 79
Cdd:PRK09754 6 IIIVGGGQAAAMAAAS-LRQQGFTGELHLFSDERHLPY----------ERPPLSKSMLLEDSPQLQQVlPANWWQENnvh 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 80 -----PVQSIDYDAKTVTALVDGKNHvetYDKLIFATGSQPILPPIkgaeikegsleFEATLENLQFVKlyqnSADVIAK 154
Cdd:PRK09754 75 lhsgvTIKTLGRDTRELVLTNGESWH---WDQLFIATGAAARPLPL-----------LDALGERCFTLR----HAGDAAR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 155 LEN--KDIKRVAVVGAGYIGVELAEAFQRKGKEVVLIDVVDTCLAGYYDRDLTDLMAKNMEEHGIQLAFGETVKEVAGNG 232
Cdd:PRK09754 137 LREvlQPERSVVIVGAGTIGLELAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 233 KVEKIITDKNEYDVDMVILAVGFRPNTTLGNgKIDLFRNGAFLVNKRQETSIPGVYAIGD-CATIYDNAtrDTNYIALAS 311
Cdd:PRK09754 217 KVELTLQSGETLQADVVIYGIGISANDQLAR-EANLDTANGIVIDEACRTCDPAIFAGGDvAITRLDNG--ALHRCESWE 293
|
330
....*....|....*
gi 489079851 312 NAVRTGIVAAHNACG 326
Cdd:PRK09754 294 NANNQAQIAAAAMLG 308
|
|
| PTZ00153 |
PTZ00153 |
lipoamide dehydrogenase; Provisional |
107-439 |
2.39e-09 |
|
lipoamide dehydrogenase; Provisional
Pssm-ID: 173442 [Multi-domain] Cd Length: 659 Bit Score: 59.54 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 107 LIFATGSQPILPpiKGAEIKEGSLefeatlenlqfvklyqNSADVIAKLENKDiKRVAVVGAGYIGVELAEAFQRKGKEV 186
Cdd:PTZ00153 278 IIIATGSTPNIP--DNIEVDQKSV----------------FTSDTAVKLEGLQ-NYMGIVGMGIIGLEFMDIYTALGSEV 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 187 VLID-------VVDTCLAGYYDRDLtdLMAKNMEEHGIQLAfgETVKEVAGNGKVE---------------KIITDKNEY 244
Cdd:PTZ00153 339 VSFEyspqllpLLDADVAKYFERVF--LKSKPVRVHLNTLI--EYVRAGKGNQPVIighserqtgesdgpkKNMNDIKET 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 245 DVDMVILAVGFRPNTT-LGNGKIDLFRNGAFL-------VNKRQETSIPGVYAIGDC------------------ATIYD 298
Cdd:PTZ00153 415 YVDSCLVATGRKPNTNnLGLDKLKIQMKRGFVsvdehlrVLREDQEVYDNIFCIGDAngkqmlahtashqalkvvDWIEG 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 299 NATRDTNyIALASNAVRTGIVA-AHNACGT--DLEGIGVQGSNGISIYGLHMVSTGLTLEKAKRLGFDAAVTEYTDNQKP 375
Cdd:PTZ00153 495 KGKENVN-INVENWASKPIIYKnIPSVCYTtpELAFIGLTEKEAKELYPPDNVGVEISFYKANSKVLCENNISFPNNSKN 573
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489079851 376 EFIEHGNFPVT------IKIVYDKDSRRILGAQMaaredvsMGIHMfSLAIQEGVTI--EKLALTDIFFLPH 439
Cdd:PTZ00153 574 NSYNKGKYNTVdntegmVKIVYLKDTKEILGMFI-------VGSYA-SILIHEGVLAinLKLSVKDLAHMVH 637
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
161-295 |
5.53e-09 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 58.11 E-value: 5.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 161 KRVAVVGAGYIGVELAEAFQRKGKEVVLIdvvdtclagyYDRDLTDLMA-----KNMEEHGIQLAFGETVKEVAG--NGK 233
Cdd:PRK12831 282 KKVAVVGGGNVAMDAARTALRLGAEVHIV----------YRRSEEELPArveevHHAKEEGVIFDLLTNPVEILGdeNGW 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 234 VE------------------KIITDKNEY---DVDMVILAVGFRPN-----TTLGngkIDLFRNGAFLVNKRQ-ETSIPG 286
Cdd:PRK12831 352 VKgmkcikmelgepdasgrrRPVEIEGSEfvlEVDTVIMSLGTSPNplissTTKG---LKINKRGCIVADEETgLTSKEG 428
|
....*....
gi 489079851 287 VYAIGDCAT 295
Cdd:PRK12831 429 VFAGGDAVT 437
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
87-321 |
1.85e-08 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 56.37 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 87 DAKTVTALVDGKNHVETYDKLIFATGSQPILPpikgaEIKEGSLEFEATLENLQFVKlyqnsadviaklenKDIKRVAVV 166
Cdd:PTZ00052 128 DEHTVSYGDNSQEETITAKYILIATGGRPSIP-----EDVPGAKEYSITSDDIFSLS--------------KDPGKTLIV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 167 GAGYIGVELAEAFQRKGKEVVlIDVVDTCLAGyYDRDLTDLMAKNMEEHGIQLAFGETVKEVA-GNGKVEKIITDKNEYD 245
Cdd:PTZ00052 189 GASYIGLETAGFLNELGFDVT-VAVRSIPLRG-FDRQCSEKVVEYMKEQGTLFLEGVVPINIEkMDDKIKVLFSDGTTEL 266
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489079851 246 VDMVILAVGFRPNT---TLGNGKIDLFRNGAFLVNKrQETSIPGVYAIGDCAtiydnatrdTNYIALASNAVRTGIVAA 321
Cdd:PTZ00052 267 FDTVLYATGRKPDIkglNLNAIGVHVNKSNKIIAPN-DCTNIPNIFAVGDVV---------EGRPELTPVAIKAGILLA 335
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
161-295 |
2.24e-08 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 56.67 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 161 KRVAVVGAGYIGVELAEAFQRKGKEVVLIdvvdtclagYYDRDLTDLMA-----KNMEEHGIQLAFGETVKEVAGN--GK 233
Cdd:PRK12778 571 KKVAVVGGGNTAMDSARTAKRLGAERVTI---------VYRRSEEEMPArleevKHAKEEGIEFLTLHNPIEYLADekGW 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 234 VEKIITDKNEY---------------------DVDMVILAVGFRPNTTLGNG--KIDLFRNGAFLVNKRQETSIPGVYAI 290
Cdd:PRK12778 642 VKQVVLQKMELgepdasgrrrpvaipgstftvDVDLVIVSVGVSPNPLVPSSipGLELNRKGTIVVDEEMQSSIPGIYAG 721
|
....*
gi 489079851 291 GDCAT 295
Cdd:PRK12778 722 GDIVR 726
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
161-295 |
5.70e-08 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 54.78 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 161 KRVAVVGAGYIGVE----LAeafqrkG--KEVVLIDVVDTCLAgyyDRDLTDLMAK--NMeehgiqlafgeTV------K 226
Cdd:PRK15317 352 KRVAVIGGGNSGVEaaidLA------GivKHVTVLEFAPELKA---DQVLQDKLRSlpNV-----------TIitnaqtT 411
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489079851 227 EVAGNG-KVEKII-TDKN-----EYDVDMVILAVGFRPNTTLGNGKIDLFRNGAFLVNKRQETSIPGVYAIGDCAT 295
Cdd:PRK15317 412 EVTGDGdKVTGLTyKDRTtgeehHLELEGVFVQIGLVPNTEWLKGTVELNRRGEIIVDARGATSVPGVFAAGDCTT 487
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
161-291 |
1.02e-06 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 50.30 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 161 KRVAVVGAGYIGVELAEAFQRKGKEVVLID----------VVDTCLAGYYDRDLTDLMAKNMeehgIQLAFGETVKEVAG 230
Cdd:pfam13738 156 QKVVVIGGYNSAVDAALELVRKGARVTVLYrgsewedrdsDPSYSLSPDTLNRLEELVKNGK----IKAHFNAEVKEITE 231
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489079851 231 NGKVEKIITDKNE----YDVdmVILAVGFRPNTT-LGNGKIDLFRNGAFLVNKR-QETSIPGVYAIG 291
Cdd:pfam13738 232 VDVSYKVHTEDGRkvtsNDD--PILATGYHPDLSfLKKGLFELDEDGRPVLTEEtESTNVPGLFLAG 296
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
81-259 |
6.38e-06 |
|
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: 48.32 E-value: 6.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 81 VQSIDYDAK----TVTaLVDGknHVETYDKLIFATG--SQPILPPIKGAEikegslEFEATlenlQF-VKLYQNSADvia 153
Cdd:COG2072 105 VTSARWDEAdgrwTVT-TDDG--ETLTARFVVVATGplSRPKIPDIPGLE------DFAGE----QLhSADWRNPVD--- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 154 kLENKdikRVAVVGAGYIGVELAEAFQRKGKEVVL----------------------IDVVDTCLAGYYDRDLTDLMAKN 211
Cdd:COG2072 169 -LAGK---RVLVVGTGASAVQIAPELARVAAHVTVfqrtppwvlprpnydpergrpaNYLGLEAPPALNRRDARAWLRRL 244
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489079851 212 MEE----------------HGIQLAFGETVKEVAGNGKVE------------KIIT-DKNEYDVDMVILAVGFRPNT 259
Cdd:COG2072 245 LRAqvkdpelglltpdyppGCKRPLLSTDYYEALRRGNVElvtggieritedGVVFaDGTEHEVDVIVWATGFRADL 321
|
|
| 3HCDH_N |
pfam02737 |
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda ... |
162-253 |
2.61e-05 |
|
3-hydroxyacyl-CoA dehydrogenase, NAD binding domain; This family also includes lambda crystallin.
Pssm-ID: 397037 [Multi-domain] Cd Length: 180 Bit Score: 44.84 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 162 RVAVVGAGYIGVELAEAFQRKGKEVVLIDVVDTCLAGYYDRdLTDLMAKNMEEHGIQlafGETVKEVAGNGkveKIITDK 241
Cdd:pfam02737 1 KVAVIGAGTMGAGIAQVFALAGLEVVLVDISEEALEKALER-IESSLERLVEKGRIT---EEEVDAALARI---SFTTDL 73
|
90
....*....|...
gi 489079851 242 NEY-DVDMVILAV 253
Cdd:pfam02737 74 AAAvDADLVIEAV 86
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
161-322 |
3.28e-05 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 46.26 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 161 KRVAVVGAGYIGVELAEAFQRKGKEVVLIdvvdtclagYYDRDLTDlMAKNMEEHGIQLAFGETVKEVA-------GNGK 233
Cdd:PRK12814 324 KKVVVIGGGNTAIDAARTALRLGAESVTI---------LYRRTREE-MPANRAEIEEALAEGVSLRELAapvsierSEGG 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 234 VE--KIITDKNEYD------------------VDMVILAVGFRPN-TTLGNGKIDLFRNGAFLVNKR-QETSIPGVYAIG 291
Cdd:PRK12814 394 LEltAIKMQQGEPDesgrrrpvpvegseftlqADTVISAIGQQVDpPIAEAAGIGTSRNGTVKVDPEtLQTSVAGVFAGG 473
|
170 180 190
....*....|....*....|....*....|.
gi 489079851 292 DCATIYDnatrdtnyiaLASNAVRTGIVAAH 322
Cdd:PRK12814 474 DCVTGAD----------IAINAVEQGKRAAH 494
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
210-293 |
3.49e-05 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 45.93 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 210 KNMEEHGIQLAFG-ETVKEVAGNGKVEKI---ITDKNE------------YDVDMVILAVGFRP--NTTLGNGKIDLFRN 271
Cdd:PRK12810 337 SNAHEEGVEREFNvQTKEFEGENGKVTGVkvvRTELGEgdfepvegsefvLPADLVLLAMGFTGpeAGLLAQFGVELDER 416
|
90 100
....*....|....*....|...
gi 489079851 272 GAFLVNKRQ-ETSIPGVYAIGDC 293
Cdd:PRK12810 417 GRVAAPDNAyQTSNPKVFAAGDM 439
|
|
| FadB |
COG1250 |
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ... |
159-193 |
9.47e-05 |
|
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA dehydrogenase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440862 [Multi-domain] Cd Length: 281 Bit Score: 43.95 E-value: 9.47e-05
10 20 30
....*....|....*....|....*....|....*
gi 489079851 159 DIKRVAVVGAGYIGVELAEAFQRKGKEVVLIDVVD 193
Cdd:COG1250 1 EIKKVAVIGAGTMGAGIAAVFANAGYEVVLLDISP 35
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
161-324 |
1.26e-04 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 43.90 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 161 KRVAVVGAGYIGVELAEAFQRKGKEVVLIDVVDTCLAgyyDRDLTDLMAKNMEEHGIQLAFGETVKEVAGN--GKVEKII 238
Cdd:PRK10262 147 QKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDGFRA---EKILIKRLMDKVENGNIILHTNRTLEEVTGDqmGVTGVRL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 239 TDKNEYD------VDMVILAVGFRPNTTLGNGKIDLfRNGAFLVN-----KRQETSIPGVYAIGDcatIYDNATRDtnyi 307
Cdd:PRK10262 224 RDTQNSDniesldVAGLFVAIGHSPNTAIFEGQLEL-ENGYIKVQsgihgNATQTSIPGVFAAGD---VMDHIYRQ---- 295
|
170
....*....|....*..
gi 489079851 308 alASNAVRTGIVAAHNA 324
Cdd:PRK10262 296 --AITSAGTGCMAALDA 310
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
161-293 |
1.32e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 44.37 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 161 KRVAVVGAGYIGVELAEAFQRKGK-EVVLIDVVDTCLAGYYDRdltdlMAKNMEEhgIQLAFGETVKEVAGNGKVEKII- 238
Cdd:PRK13984 419 RSLVVIGGGNVAMDIARSMARLQKmEYGEVNVKVTSLERTFEE-----MPADMEE--IEEGLEEGVVIYPGWGPMEVVIe 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 239 ----------------------------TDKNEYDVDMVILAVGFRPNTTL----GNGKIDLFRnGAFLVNKRQETSIPG 286
Cdd:PRK13984 492 ndkvkgvkfkkcvevfdeegrfnpkfdeSDQIIVEADMVVEAIGQAPDYSYlpeeLKSKLEFVR-GRILTNEYGQTSIPW 570
|
....*..
gi 489079851 287 VYAIGDC 293
Cdd:PRK13984 571 LFAGGDI 577
|
|
| NDP-sugDHase |
TIGR03026 |
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ... |
161-286 |
1.37e-04 |
|
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.
Pssm-ID: 274399 [Multi-domain] Cd Length: 409 Bit Score: 44.14 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 161 KRVAVVGAGYIGVELAEAFQRKGKEVVLIDV----VDTCLAG---YYDRDLTDLMAKNMEEHgiQLAFGETVKEVAGngk 233
Cdd:TIGR03026 1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIdqekVDKLNKGkspIYEPGLDELLAKALKAG--RLRATTDYEEAIR--- 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489079851 234 vekiitdkneyDVDMVILAVGFRPNTtlgNGKIDL-------------FRNGAFLVNKrqETSIPG 286
Cdd:TIGR03026 76 -----------DADVIIICVPTPLKE---DGSPDLsyvesaaetiakhLRKGATVVLE--STVPPG 125
|
|
| PRK06130 |
PRK06130 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
160-253 |
1.61e-04 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 235707 [Multi-domain] Cd Length: 311 Bit Score: 43.61 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 160 IKRVAVVGAGYIGVELAEAFQRKGKEVVLIDVVDTCLA---GYYDRDLTDLMAKnmeehGIQLAFGETVKEVAGNGKVEK 236
Cdd:PRK06130 4 IQNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALErarGVIERALGVYAPL-----GIASAGMGRIRMEAGLAAAVS 78
|
90
....*....|....*..
gi 489079851 237 iitdkneyDVDMVILAV 253
Cdd:PRK06130 79 --------GADLVIEAV 87
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
161-323 |
2.25e-04 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 43.71 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 161 KRVAVVGAGYIGVELAEAFQR-KGKEVVLIdvvdtclagyYDRDLTDLMAKNME-----EHGIQLAFGETVKEVAGNG-- 232
Cdd:PRK12771 268 KRVVVIGGGNTAMDAARTARRlGAEEVTIV----------YRRTREDMPAHDEEieealREGVEINWLRTPVEIEGDEng 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 233 -------KVEKIITDKN-----------EYDVDMVILAVG-------FR--PNTTLGNGKIDLFRNGAFlvnkrqeTSIP 285
Cdd:PRK12771 338 atglrviTVEKMELDEDgrpspvtgeeeTLEADLVVLAIGqdidsagLEsvPGVEVGRGVVQVDPNFMM-------TGRP 410
|
170 180 190
....*....|....*....|....*....|....*...
gi 489079851 286 GVYAIGDCATIYDNATRdtnyialasnAVRTGIVAAHN 323
Cdd:PRK12771 411 GVFAGGDMVPGPRTVTT----------AIGHGKKAARN 438
|
|
| UDPG_MGDP_dh_N |
pfam03721 |
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose ... |
161-213 |
3.38e-04 |
|
UDP-glucose/GDP-mannose dehydrogenase family, NAD binding domain; The UDP-glucose/GDP-mannose dehydrogenaseses are a small group of enzymes which possesses the ability to catalyze the NAD-dependent 2-fold oxidation of an alcohol to an acid without the release of an aldehyde intermediate.
Pssm-ID: 397677 [Multi-domain] Cd Length: 186 Bit Score: 41.46 E-value: 3.38e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 161 KRVAVVGAGYIGVELAEAFQRKGKEVVLIDV----VDTCLAG---YYDRDLTDLMAKNME 213
Cdd:pfam03721 1 MKISVIGLGYVGLPTAACLAEIGHDVIGVDIdeekVDKLNSGqipIYEPGLDELVKANVS 60
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
161-294 |
4.90e-04 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 42.51 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 161 KRVAVVGAGYIGVELAEAFQRKGKEVVLIdvvdtclagyYDRDLTDLMAKNMEEH-----GIQLAFGETVKEVAGNGK-- 233
Cdd:PRK12779 448 KEVFVIGGGNTAMDAARTAKRLGGNVTIV----------YRRTKSEMPARVEELHhaleeGINLAVLRAPREFIGDDHth 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 234 -VEKIITDKNEY--------------------DVDMVILAVGFRPNTTLGNGKIDLFRN--GAFLVNK-RQETSIPGVYA 289
Cdd:PRK12779 518 fVTHALLDVNELgepdksgrrspkptgeiervPVDLVIMALGNTANPIMKDAEPGLKTNkwGTIEVEKgSQRTSIKGVYS 597
|
....*
gi 489079851 290 IGDCA 294
Cdd:PRK12779 598 GGDAA 602
|
|
| MurD |
COG0771 |
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
161-223 |
5.23e-04 |
|
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440534 [Multi-domain] Cd Length: 445 Bit Score: 42.38 E-value: 5.23e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489079851 161 KRVAVVGAGYIGVELAEAFQRKGKEVVLIDvvdtclagyyDRDLTDLMAKNMEEHGIQLAFGE 223
Cdd:COG0771 5 KKVLVLGLGKSGLAAARLLAKLGAEVTVSD----------DRPAPELAAAELEAPGVEVVLGE 57
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
162-190 |
1.06e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 41.04 E-value: 1.06e-03
10 20
....*....|....*....|....*....
gi 489079851 162 RVAVVGAGYIGVELAEAFQRKGKEVVLID 190
Cdd:COG0665 4 DVVVIGGGIAGLSTAYHLARRGLDVTVLE 32
|
|
| PRK06035 |
PRK06035 |
3-hydroxyacyl-CoA dehydrogenase; Validated |
159-197 |
3.83e-03 |
|
3-hydroxyacyl-CoA dehydrogenase; Validated
Pssm-ID: 180361 [Multi-domain] Cd Length: 291 Bit Score: 39.09 E-value: 3.83e-03
10 20 30
....*....|....*....|....*....|....*....
gi 489079851 159 DIKRVAVVGAGYIGVELAEAFQRKGKEVVLIDVVDTCLA 197
Cdd:PRK06035 2 DIKVIGVVGSGVMGQGIAQVFARTGYDVTIVDVSEEILK 40
|
|
| wecC |
PRK11064 |
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional |
159-194 |
3.86e-03 |
|
UDP-N-acetyl-D-mannosamine dehydrogenase; Provisional
Pssm-ID: 182940 [Multi-domain] Cd Length: 415 Bit Score: 39.58 E-value: 3.86e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 489079851 159 DIKRVAVVGAGYIGVELAEAFQRKGKEVVLIDV----VDT 194
Cdd:PRK11064 2 SFETISVIGLGYIGLPTAAAFASRQKQVIGVDInqhaVDT 41
|
|
| PRK06129 |
PRK06129 |
3-hydroxyacyl-CoA dehydrogenase; Validated |
162-209 |
4.24e-03 |
|
3-hydroxyacyl-CoA dehydrogenase; Validated
Pssm-ID: 235706 [Multi-domain] Cd Length: 308 Bit Score: 38.87 E-value: 4.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 489079851 162 RVAVVGAGYIGVELAEAFQRKGKEVVLIDVVDTCLAG---YYDRDLTDLMA 209
Cdd:PRK06129 4 SVAIIGAGLIGRAWAIVFARAGHEVRLWDADPAAAAAapaYIAGRLEDLAA 54
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
161-190 |
4.49e-03 |
|
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 38.89 E-value: 4.49e-03
10 20 30
....*....|....*....|....*....|
gi 489079851 161 KRVAVVGAGYIGVELAEAFQRKGKEVVLID 190
Cdd:COG0569 96 MHVIIIGAGRVGRSLARELEEEGHDVVVID 125
|
|
| FlaA1 |
COG1086 |
NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular ... |
161-253 |
4.50e-03 |
|
NDP-sugar epimerase, includes UDP-GlcNAc-inverting 4,6-dehydratase FlaA1 and capsular polysaccharide biosynthesis protein EpsC [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440703 [Multi-domain] Cd Length: 121 Bit Score: 37.21 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079851 161 KRVAVVGAGYIGVELAEAFQRK---GKEVVlidvvdtclaGYYDRDLTDlmaKNMEEHGIQLAfgetvkevagnGKVEKI 237
Cdd:COG1086 22 RRVLIVGAGEAGRQLARALRRNpdlGYRVV----------GFVDDDPDK---RGRRIEGVPVL-----------GTLDDL 77
|
90
....*....|....*.
gi 489079851 238 ITDKNEYDVDMVILAV 253
Cdd:COG1086 78 PELVRRLGVDEVIIAL 93
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
66-120 |
8.12e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 38.35 E-value: 8.12e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 489079851 66 EELESLGAKVYMESPVQSIDYDAKTVTALVDGKNHVETyDKLIFATG--SQPILPPI 120
Cdd:COG0665 159 RAARAAGVRIREGTPVTGLEREGGRVTGVRTERGTVRA-DAVVLAAGawSARLLPML 214
|
|
| |
