|
Name |
Accession |
Description |
Interval |
E-value |
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
1-374 |
2.90e-109 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 326.33 E-value: 2.90e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 1 MHPIVIIGSGMAGYAVAREFRKLNPEQELLMLCADDATNYAKPTLSNAFVANKAPEQIALGDtEKMATQLKMQIATHTWV 80
Cdd:COG1251 1 KMRIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVLAGETDEEDLLLRP-ADFYEENGIDLRLGTRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 81 KEIHTEQQQLTViKDGaeSTQPYSQLVLAVGANPIRLAIAGDGSTDIQVVNNLDDYKTFRAKLekRADKRVVILGAGLIG 160
Cdd:COG1251 80 TAIDRAARTVTL-ADG--ETLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAAL--APGKRVVVIGGGLIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 161 CEFANDLQHTGHQATVIDLANQPLGRLLPAHVSSAFKENLEATGIHFVLGTTVEKVSKIENGdYVVTLANGQSLVADVVL 240
Cdd:COG1251 155 LEAAAALRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRV-TGVRLADGEELPADLVV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 241 SAIGLQPNISLAKEAGIQTSRGILTNAQLETNQPHIYAVGDCAEVNG-----LLLPYVMPIMQQARALAKTLNGETTAVH 315
Cdd:COG1251 234 VAIGVRPNTELARAAGLAVDRGIVVDDYLRTSDPDIYAAGDCAEHPGpvygrRVLELVAPAYEQARVAAANLAGGPAAYE 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 498012108 316 YPAMPVAVKTPAAPLTVLPAPIDAEVNWETEELDDGMIAKALDSQGTLRGFVLLGATAA 374
Cdd:COG1251 314 GSVPSTKLKVFGVDVASAGDAEGDEEVVVRGDPARGVYKKLVLRDGRLVGAVLVGDTSD 372
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
1-367 |
2.07e-107 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 320.71 E-value: 2.07e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 1 MHPIVIIGSGMAGYAVAREFRKLNPEQELLMLCADDATNYAKPTLSNAFVANKAPEQIALGDTEKMATQLKMQIATHTWV 80
Cdd:PRK04965 2 SNGIVIIGSGFAARQLVKNIRKQDAHIPITLITADSGDEYNKPDLSHVFSQGQRADDLTRQSAGEFAEQFNLRLFPHTWV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 81 KEIHTEQQQLTVikdgAESTQPYSQLVLAVGANPIRLAIAGDGStdIQVVNNLDDYKTFRAKLekRADKRVVILGAGLIG 160
Cdd:PRK04965 82 TDIDAEAQVVKS----QGNQWQYDKLVLATGASAFVPPIPGREL--MLTLNSQQEYRAAETQL--RDAQRVLVVGGGLIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 161 CEFANDLQHTGHQATVIDLANQPLGRLLPAHVSSAFKENLEATGIHFVLGTTVEKVSKIENGdYVVTLANGQSLVADVVL 240
Cdd:PRK04965 154 TELAMDLCRAGKAVTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLEKTDSG-IRATLDSGRSIEVDAVI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 241 SAIGLQPNISLAKEAGIQTSRGILTNAQLETNQPHIYAVGDCAEVNGLLLPYVMPIMQQARALAKTLNGETTAVHYPAMP 320
Cdd:PRK04965 233 AAAGLRPNTALARRAGLAVNRGIVVDSYLQTSAPDIYALGDCAEINGQVLPFLQPIQLSAMALAKNLLGQNTPLKLPAML 312
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 498012108 321 VAVKTPAAPLTVLPAPIDAEVNWETEELDDGMIAKALDSQGTLRGFV 367
Cdd:PRK04965 313 VKVKTPELPLQLAGETQRQDLRWQINAESQGMVAKGVDEAGQLRAFV 359
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
22-323 |
4.18e-58 |
|
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: 191.95 E-value: 4.18e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 22 KLNPEQELLMLCADDATNYAKPTLSNAFVAN-KAPEQIALGDTEKMAtQLKMQIATHTWVKEIHTEQQQLTViKDGaeST 100
Cdd:COG0446 1 RLGPDAEITVIEKGPHHSYQPCGLPYYVGGGiKDPEDLLVRTPESFE-RKGIDVRTGTEVTAIDPEAKTVTL-RDG--ET 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 101 QPYSQLVLAVGANPIRLAIAGDGSTDIQVVNNLDDYKTFRAKLEKRADKRVVILGAGLIGCEFANDLQHTGHQATVIDLA 180
Cdd:COG0446 77 LSYDKLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALREALKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 181 NQPLGRLLPAhVSSAFKENLEATGIHFVLGTTVEKVskIENGDYVVTLANGQSLVADVVLSAIGLQPNISLAKEAGIQT- 259
Cdd:COG0446 157 PRLLGVLDPE-MAALLEEELREHGVELRLGETVVAI--DGDDKVAVTLTDGEEIPADLVVVAPGVRPNTELAKDAGLALg 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498012108 260 -SRGILTNAQLETNQPHIYAVGDCAEVNGLL------LPYVMPIMQQARALAKTLNGETTAvhYPAMPVAV 323
Cdd:COG0446 234 eRGWIKVDETLQTSDPDVYAAGDCAEVPHPVtgktvyIPLASAANKQGRVAAENILGGPAP--FPGLGTFI 302
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
4-378 |
3.22e-51 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 183.11 E-value: 3.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 4 IVIIGSGMAGYAVAREFRKLNPEQ-ELLMLCADDATNYAKPTLSNAFVANKAPEQIALGDtEKMATQLKMQIATHTWVKE 82
Cdd:TIGR02374 1 LVLVGNGMAGHRCIEEVLKLNRHMfEITIFGEEPHPNYNRILLSSVLQGEADLDDITLNS-KDWYEKHGITLYTGETVIQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 83 IHTEQQQltVIKDgAESTQPYSQLVLAVGANPIRLAIAGDGSTDIQVVNNLDDYKTFRAkLEKRADKRVVIlGAGLIGCE 162
Cdd:TIGR02374 80 IDTDQKQ--VITD-AGRTLSYDKLILATGSYPFILPIPGADKKGVYVFRTIEDLDAIMA-MAQRFKKAAVI-GGGLLGLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 163 FANDLQHTGHQATVIDLANQPLGRLLPAHVSSAFKENLEATGIHFVLGTTVEKVSKIENGDyVVTLANGQSLVADVVLSA 242
Cdd:TIGR02374 155 AAVGLQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKAD-RIRFKDGSSLEADLIVMA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 243 IGLQPNISLAKEAGIQTSRGILTNAQLETNQPHIYAVGDCAEVNGLLLPYVMPIMQQARALAKTLNGETTAvHYPAMPVA 322
Cdd:TIGR02374 234 AGIRPNDELAVSAGIKVNRGIIVNDSMQTSDPDIYAVGECAEHNGRVYGLVAPLYEQAKVLADHICGVECE-EYEGSDLS 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498012108 323 VKTPAAPLTVLPAPiDAEVNWETEEL-----DDGMIAKALDSQGTLRGFVLLGATAAKQRL 378
Cdd:TIGR02374 313 AKLKLLGVDVWSAG-DAQETERTTSIkiydeQKGIYKKLVLSDDKLLGAVLFGDTSDYGRL 372
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
2-282 |
5.49e-46 |
|
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: 159.79 E-value: 5.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 2 HPIVIIGSGMAGYAVAREFRKLNPEqeLLMLCADDATNYAKPTLSNAFVANKAPEQIALGD----------TEKMATQLK 71
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGK--VTLIEDEGTCPYGGCVLSKALLGAAEAPEIASLWadlykrkeevVKKLNNGIE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 72 MQIATHtwVKEIHTEQQQLTVIK--DGAESTQPYSQLVLAVGANPIRLAIAGDGSTDIQVVNNLDDYKTFRAKLekrADK 149
Cdd:pfam07992 79 VLLGTE--VVSIDPGAKKVVLEElvDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKL---LPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 150 RVVILGAGLIGCEFANDLQHTGHQATVIDLANQpLGRLLPAHVSSAFKENLEATGIHFVLGTTVEKVSKiENGDYVVTLA 229
Cdd:pfam07992 154 RVVVVGGGYIGVELAAALAKLGKEVTLIEALDR-LLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIG-DGDGVEVILK 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 498012108 230 NGQSLVADVVLSAIGLQPNISLAKEAGIQTSR--GILTNAQLETNQPHIYAVGDC 282
Cdd:pfam07992 232 DGTEIDADLVVVAIGRRPNTELLEAAGLELDErgGIVVDEYLRTSVPGIYAAGDC 286
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
107-323 |
8.97e-32 |
|
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: 124.81 E-value: 8.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 107 VLAVGANPIRLAIAG-DG-----STDIqvvnnLDdyktfrakLEKRAdKRVVILGAGLIGCEFANDLQHTGHQATVIDLA 180
Cdd:COG1249 135 VIATGSRPRVPPIPGlDEvrvltSDEA-----LE--------LEELP-KSLVVIGGGYIGLEFAQIFARLGSEVTLVERG 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 181 NQPLGRLLPAhVSSAFKENLEATGIHFVLGTTVEKVSKIENGdYVVTLANGQSLV---ADVVLSAIGLQPNISL--AKEA 255
Cdd:COG1249 201 DRLLPGEDPE-ISEALEKALEKEGIDILTGAKVTSVEKTGDG-VTVTLEDGGGEEaveADKVLVATGRRPNTDGlgLEAA 278
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498012108 256 GIQTSR--GILTNAQLETNQPHIYAVGDCaeVNGLLLPYVMpiMQQARALAKTLNGETTA-VHYPAMPVAV 323
Cdd:COG1249 279 GVELDErgGIKVDEYLRTSVPGIYAIGDV--TGGPQLAHVA--SAEGRVAAENILGKKPRpVDYRAIPSVV 345
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
4-290 |
8.26e-31 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 122.07 E-value: 8.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 4 IVIIGSGMAGYAVAREFRKLNPEQELLMLCADDATNYAKPTL----------SNAFVAnKAPEQialgdTEKMATQLKmq 73
Cdd:PRK09564 3 IIIIGGTAAGMSAAAKAKRLNKELEITVYEKTDIVSFGACGLpyfvggffddPNTMIA-RTPEE-----FIKSGIDVK-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 74 iaTHTWVKEIHTEQQQLTV--IKDGAESTQPYSQLVLAVGANPIRLAIAGDGSTDIQVVNNLDDYKTFRAKLEKRADKRV 151
Cdd:PRK09564 75 --TEHEVVKVDAKNKTITVknLKTGSIFNDTYDKLMIATGARPIIPPIKNINLENVYTLKSMEDGLALKELLKDEEIKNI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 152 VILGAGLIGCEFANDLQHTGHQATVIDLANQPLGRLLPAHVSSAFKENLEATGIHFVLGTTVEKVSKIENGDYVVTlaNG 231
Cdd:PRK09564 153 VIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVVT--DK 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498012108 232 QSLVADVVLSAIGLQPNISLAKEAGIQTSR--GILTNAQLETNQPHIYAVGDCAEVNGLLL 290
Cdd:PRK09564 231 GEYEADVVIVATGVKPNTEFLEDTGLKTLKngAIIVDEYGETSIENIYAAGDCATIYNIVS 291
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
1-307 |
2.78e-30 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 119.85 E-value: 2.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 1 MHPIVIIGSGMAGYAVAREFRK-LNPEQELLMLcadDATNYA--KPTLSNAFVANKAPEQIALgDTEKMA--TQLKMQIA 75
Cdd:COG1252 1 MKRIVIVGGGFAGLEAARRLRKkLGGDAEVTLI---DPNPYHlfQPLLPEVAAGTLSPDDIAI-PLRELLrrAGVRFIQG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 76 ThtwVKEIHTEQQQLTViKDGaeSTQPYSQLVLAVGANPIRLAIAGDGStDIQVVNNLDDYKTFRAKLEKRADK------ 149
Cdd:COG1252 77 E---VTGIDPEARTVTL-ADG--RTLSYDYLVIATGSVTNFFGIPGLAE-HALPLKTLEDALALRERLLAAFERaerrrl 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 150 -RVVILGAGLIGCEFANDLQHTGHQA-------------TVIDLANQPLGRlLPAHVSSAFKENLEATGIHFVLGTTVEK 215
Cdd:COG1252 150 lTIVVVGGGPTGVELAGELAELLRKLlrypgidpdkvriTLVEAGPRILPG-LGEKLSEAAEKELEKRGVEVHTGTRVTE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 216 VSkiENGdyvVTLANGQSLVADVVLSAIGLQPNiSLAKEAGIQTSRG--ILTNAQLET-NQPHIYAVGDCAEV---NGLL 289
Cdd:COG1252 229 VD--ADG---VTLEDGEEIPADTVIWAAGVKAP-PLLADLGLPTDRRgrVLVDPTLQVpGHPNVFAIGDCAAVpdpDGKP 302
|
330
....*....|....*....
gi 498012108 290 LPYV-MPIMQQARALAKTL 307
Cdd:COG1252 303 VPKTaQAAVQQAKVLAKNI 321
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
4-329 |
6.51e-30 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 118.87 E-value: 6.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 4 IVIIGSGMAGYAVAREFRKLNPEQELLMLCADDATNYAKPTLSNAFVANKAPeqialgdtekmatQLKMQIATHTWV-KE 82
Cdd:PRK09754 6 IIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSP-------------QLQQVLPANWWQeNN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 83 IHTEQQQL--TVIKDGAE------STQPYSQLVLAVGANPIRLAIAGDGSTDIQVVNNLDDYKTFRAKLEKraDKRVVIL 154
Cdd:PRK09754 73 VHLHSGVTikTLGRDTRElvltngESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQP--ERSVVIV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 155 GAGLIGCEFANDLQHTGHQATVIDLANQPLGRLLPAHVSSAFKENLEATGIHFVLGTTVEKVSKIEngDYVVTLANGQSL 234
Cdd:PRK09754 151 GAGTIGLELAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGE--KVELTLQSGETL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 235 VADVVLSAIGLQPNISLAKEAGIQTSRGILTNAQLETNQPHIYAVGDCA---EVNGLLlpyvmpimqQARALAKTLNGET 311
Cdd:PRK09754 229 QADVVIYGIGISANDQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAitrLDNGAL---------HRCESWENANNQA 299
|
330
....*....|....*...
gi 498012108 312 TAVHYPAMPVAVKTPAAP 329
Cdd:PRK09754 300 QIAAAAMLGLPLPLLPPP 317
|
|
| Rbx_binding |
pfam18113 |
Rubredoxin binding C-terminal domain; This is the C-terminal domain found in rubredoxin ... |
313-382 |
4.86e-25 |
|
Rubredoxin binding C-terminal domain; This is the C-terminal domain found in rubredoxin reductase (RdxR) present in Pseudomonas aeruginosa. RdxR are important in prokaryotes as they allow for the metabolism of inert n-alkanes and RdxR is also crucial for archaea and anaerobic bacteria in the response to oxidative stress. This domain is known to recognize and bind to rubredoxin.
Pssm-ID: 436282 Cd Length: 71 Bit Score: 96.93 E-value: 4.86e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 313 AVHYPAMPVAVKTPAAPLTVLPAPIDAEVNWETEELDDGMIAKALDSQGTLRGFVLLGAtAAKQRLALTK 382
Cdd:pfam18113 1 AVVYPAMPVIVKTPACPLVVAPPAVGAEGEWQIEGDGEGLTARFYDADGQLLGFALTGE-AVAQRMALLK 69
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
149-323 |
5.03e-25 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 106.01 E-value: 5.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 149 KRVVILGAGLIGCEFANDLQHTGHQATVIDLANQPLGRLLPAhVSSAFKENLEATGIHFVLGTTVEKVSKIENGDYVVTL 228
Cdd:PRK06116 168 KRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPLRGFDPD-IRETLVEEMEKKGIRLHTNAVPKAVEKNADGSLTLTL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 229 ANGQSLVADVVLSAIGLQPN---ISLAKeAGIQT-SRG-ILTNAQLETNQPHIYAVGDCAevNGLLLPYVMpiMQQARAL 303
Cdd:PRK06116 247 EDGETLTVDCLIWAIGREPNtdgLGLEN-AGVKLnEKGyIIVDEYQNTNVPGIYAVGDVT--GRVELTPVA--IAAGRRL 321
|
170 180
....*....|....*....|..
gi 498012108 304 AKTL--NGETTAVHYPAMPVAV 323
Cdd:PRK06116 322 SERLfnNKPDEKLDYSNIPTVV 343
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
87-320 |
8.22e-25 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 105.23 E-value: 8.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 87 QQQLTVIKDGAESTQPYSQLVLAVGANPIRL-AIAGDGstdiQVVNNLDDyktfrA-KLEkRADKRVVILGAGLIGCEFA 164
Cdd:PRK06416 119 PNTVRVMTEDGEQTYTAKNIILATGSRPRELpGIEIDG----RVIWTSDE-----AlNLD-EVPKSLVVIGGGYIGVEFA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 165 NDLQHTGHQATVIDLanqpLGRLLP---AHVSSAFKENLEATGIHFVLGTTVEKVSKIENGdYVVTLANG---QSLVADV 238
Cdd:PRK06416 189 SAYASLGAEVTIVEA----LPRILPgedKEISKLAERALKKRGIKIKTGAKAKKVEQTDDG-VTVTLEDGgkeETLEADY 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 239 VLSAIGLQPNIS---LAkEAGIQTSRG-ILTNAQLETNQPHIYAVGDCaeVNGLLLPYVMpiMQQARALAKTLNGETTAV 314
Cdd:PRK06416 264 VLVAVGRRPNTEnlgLE-ELGVKTDRGfIEVDEQLRTNVPNIYAIGDI--VGGPMLAHKA--SAEGIIAAEAIAGNPHPI 338
|
....*.
gi 498012108 315 HYPAMP 320
Cdd:PRK06416 339 DYRGIP 344
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
1-284 |
1.11e-22 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 99.09 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 1 MHPIVIIGSGMAGYAVAREFRKLNPEQELLMLCADDATNYAK---PTLSNAFVANKapEQIALGDTEKMATQLKMQIATH 77
Cdd:PRK13512 1 MPKIIVVGAVAGGATCASQIRRLDKESDIIIFEKDRDMSFANcalPYYIGEVVEDR--KYALAYTPEKFYDRKQITVKTY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 78 TWVKEIHTEQQQLTVI--KDGAESTQPYSQLVLAVGANPIRLaiaGDGSTDIQVVNNLDDYKTFRAKLEKRADKRVVILG 155
Cdd:PRK13512 79 HEVIAINDERQTVTVLnrKTNEQFEESYDKLILSPGASANSL---GFESDITFTLRNLEDTDAIDQFIKANQVDKALVVG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 156 AGLIGCEFANDLQHTGHQATVIDLANQpLGRLLPAHVSSAFKENLEATGIHFVLGttvEKVSKIEngDYVVTLANGQSLV 235
Cdd:PRK13512 156 AGYISLEVLENLYERGLHPTLIHRSDK-INKLMDADMNQPILDELDKREIPYRLN---EEIDAIN--GNEVTFKSGKVEH 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 498012108 236 ADVVLSAIGLQPNISLAKEAGIQTSRG--ILTNAQLETNQPHIYAVGDCAE 284
Cdd:PRK13512 230 YDMIIEGVGTHPNSKFIESSNIKLDDKgfIPVNDKFETNVPNIYAIGDIIT 280
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
4-324 |
5.77e-22 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 97.88 E-value: 5.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 4 IVIIGSGMAGYAVAREF-RKLNPEQ-ELLMLCADDATNYAKPTLSNAFVANKApEQIAL---GDTEKMAtqLKMQIATHt 78
Cdd:PRK14989 6 LAIIGNGMVGHRFIEDLlDKADAANfDITVFCEEPRIAYDRVHLSSYFSHHTA-EELSLvreGFYEKHG--IKVLVGER- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 79 wVKEIHTEQQqltVIKDGAESTQPYSQLVLAVGANPIRLAIAGDGSTDIQVVNNLDDYKTFRAKleKRADKRVVILGAGL 158
Cdd:PRK14989 82 -AITINRQEK---VIHSSAGRTVFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEAC--ARRSKRGAVVGGGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 159 IGCEFANDLQHTGHQATVIDLANQPLGRLLPAHVSSAFKENLEATGIHFVLG-TTVEKVSKIENGDYVVTLANGQSLVAD 237
Cdd:PRK14989 156 LGLEAAGALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSkNTLEIVQEGVEARKTMRFADGSELEVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 238 VVLSAIGLQPNISLAKEAGIQTSR--GILTNAQLETNQPHIYAVGDCAEVNGLLLPYVMPIMQQARALAKTLNGETTAVH 315
Cdd:PRK14989 236 FIVFSTGIRPQDKLATQCGLAVAPrgGIVINDSCQTSDPDIYAIGECASWNNRVFGLVAPGYKMAQVAVDHLLGSENAFE 315
|
....*....
gi 498012108 316 YPAMPVAVK 324
Cdd:PRK14989 316 GADLSAKLK 324
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
149-281 |
6.09e-22 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 97.15 E-value: 6.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 149 KRVVILGAGLIGCEFANDLQHTGHQATVIDLANQPLGrLLPAHVSSAFKENLEATGIHFVLGTTVEKVSKIENGdYVVTL 228
Cdd:PRK05249 176 RSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLS-FLDDEISDALSYHLRDSGVTIRHNEEVEKVEGGDDG-VIVHL 253
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 498012108 229 ANGQSLVADVVLSAIGLQPNI-SLAKE-AGIQT-SRGILT-NAQLETNQPHIYAVGD 281
Cdd:PRK05249 254 KSGKKIKADCLLYANGRTGNTdGLNLEnAGLEAdSRGQLKvNENYQTAVPHIYAVGD 310
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
149-282 |
7.63e-22 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 96.81 E-value: 7.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 149 KRVVILGAGLIGCEFANDLQHTGHQATVIDLANQPLGRlLPAHVSSAFKENLEATGIHFVLGTTVEKVSKIENGDYVVTL 228
Cdd:PRK06370 172 EHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLLPR-EDEDVAAAVREILEREGIDVRLNAECIRVERDGDGIAVGLD 250
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498012108 229 ANG--QSLVADVVLSAIGLQPNIS---LAKeAGIQTSR--GILTNAQLETNQPHIYAVGDC 282
Cdd:PRK06370 251 CNGgaPEITGSHILVAVGRVPNTDdlgLEA-AGVETDArgYIKVDDQLRTTNPGIYAAGDC 310
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
149-323 |
2.08e-20 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 92.55 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 149 KRVVILGAGLIGCEFANDLQHTGHQATVIDLANQPLGRLLPAhVSSAFKENLEATgIHFVLGTTVEKVSKIENGDYVVTL 228
Cdd:PRK06292 170 KSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRILPLEDPE-VSKQAQKILSKE-FKIKLGAKVTSVEKSGDEKVEELE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 229 ANG--QSLVADVVLSAIGLQPNI-SLA-KEAGIQT-SRG-ILTNAQLETNQPHIYAVGDcaeVNGlllpyVMPIMQ---- 298
Cdd:PRK06292 248 KGGktETIEADYVLVATGRRPNTdGLGlENTGIELdERGrPVVDEHTQTSVPGIYAAGD---VNG-----KPPLLHeaad 319
|
170 180
....*....|....*....|....*.
gi 498012108 299 QARALAKT-LNGETTAVHYPAMPVAV 323
Cdd:PRK06292 320 EGRIAAENaAGDVAGGVRYHPIPSVV 345
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
86-287 |
4.61e-18 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 85.19 E-value: 4.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 86 EQQQLTvikdgAEStqpysqLVLAVGANPIRLAIAGDG-------STDIQvvnnlddyktfraKLEKRAdKRVVILGAGL 158
Cdd:PRK07251 113 EKIELT-----AET------IVINTGAVSNVLPIPGLAdskhvydSTGIQ-------------SLETLP-ERLGIIGGGN 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 159 IGCEFANDLQHTGHQATVIDLANQPLGRLLPAhVSSAFKENLEATGIHFVLGTTVEKVSKieNGDYVVTLANGQSLVADV 238
Cdd:PRK07251 168 IGLEFAGLYNKLGSKVTVLDAASTILPREEPS-VAALAKQYMEEDGITFLLNAHTTEVKN--DGDQVLVVTEDETYRFDA 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498012108 239 VLSAIGLQPNIS---LAKEAGIQTSRG-ILTNAQLETNQPHIYAVGDcaeVNG 287
Cdd:PRK07251 245 LLYATGRKPNTEplgLENTDIELTERGaIKVDDYCQTSVPGVFAVGD---VNG 294
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
91-379 |
2.83e-17 |
|
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: 83.24 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 91 TVIKDGAESTQPYSQLVLAVGANPIRLAIAGdgstdiqvVNNLDDYKTFRAKLEKRADKRVVILGAGLIGCEFANDLQHT 170
Cdd:TIGR02053 117 TVKVDLGREVRGAKRFLIATGARPAIPPIPG--------LKEAGYLTSEEALALDRIPESLAVIGGGAIGVELAQAFARL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 171 GHQATVIDLANQPLGRLLPAhVSSAFKENLEATGIHFVLGTTVEKVSKIENGDYVVTLANG--QSLVADVVLSAIGLQPN 248
Cdd:TIGR02053 189 GSEVTILQRSDRLLPREEPE-ISAAVEEALAEEGIEVVTSAQVKAVSVRGGGKIITVEKPGgqGEVEADELLVATGRRPN 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 249 I-SLAKE-AGIQTSR--GILTNAQLETNQPHIYAVGDCaeVNGLLLPYVMPiMQQARALAKTLNGETTAVHYPAMPVAVK 324
Cdd:TIGR02053 268 TdGLGLEkAGVKLDErgGILVDETLRTSNPGIYAAGDV--TGGLQLEYVAA-KEGVVAAENALGGANAKLDLLVIPRVVF 344
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 498012108 325 T-PAAP---LTVLPApIDAEVNWETEELDDGMIAKALDSQGTlRGFVLLGATAAKQRLA 379
Cdd:TIGR02053 345 TdPAVAsvgLTEAEA-QKAGIECDCRTLPLTNVPRARINRDT-RGFIKLVAEPGTGKVL 401
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
150-231 |
5.59e-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: 74.93 E-value: 5.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 150 RVVILGAGLIGCEFANDLQHTGHQATVIDLANQPLgRLLPAHVSSAFKENLEATGIHFVLGTTVEKVSKIENGDyVVTLA 229
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLL-PGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGV-VVVLT 78
|
..
gi 498012108 230 NG 231
Cdd:pfam00070 79 DG 80
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
149-320 |
5.33e-15 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 76.12 E-value: 5.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 149 KRVVILGAGLIGCEFANDLQHTGHQATVIDLanqpLGRLLPAHVSSAFKENLEA---TGIHFVLGTTVEKVSKIENG--- 222
Cdd:PRK06327 184 KKLAVIGAGVIGLELGSVWRRLGAEVTILEA----LPAFLAAADEQVAKEAAKAftkQGLDIHLGVKIGEIKTGGKGvsv 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 223 DYVVTLANGQSLVADVVLSAIGLQPNIS--LAKEAGIQ-TSRG-ILTNAQLETNQPHIYAVGDCaeVNGLLLPYVMpiMQ 298
Cdd:PRK06327 260 AYTDADGEAQTLEVDKLIVSIGRVPNTDglGLEAVGLKlDERGfIPVDDHCRTNVPNVYAIGDV--VRGPMLAHKA--EE 335
|
170 180
....*....|....*....|..
gi 498012108 299 QARALAKTLNGETTAVHYPAMP 320
Cdd:PRK06327 336 EGVAVAERIAGQKGHIDYNTIP 357
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
4-283 |
7.77e-15 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 74.39 E-value: 7.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 4 IVIIGSGMAGYAVARE--FRKLNPeqelLMLcaddatnyAKPTLSNAFVANKAPEQIaLGDTEK-----MATQLKMQIAT 76
Cdd:COG0492 3 VVIIGAGPAGLTAAIYaaRAGLKT----LVI--------EGGEPGGQLATTKEIENY-PGFPEGisgpeLAERLREQAER 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 77 H------TWVKEIHTEQQQLTVIKDGAESTQPYSqLVLAVGANPIRLAIAGdgstdiqvvnnLDDYKTF------RAKLE 144
Cdd:COG0492 70 FgaeillEEVTSVDKDDGPFRVTTDDGTEYEAKA-VIIATGAGPRKLGLPG-----------EEEFEGRgvsycaTCDGF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 145 KRADKRVVILGAGLIGCEFANDLQHTGHQATVIDLANQPlgRLLPAHVSSAFkenlEATGIHFVLGTTVEKVskieNGDY 224
Cdd:COG0492 138 FFRGKDVVVVGGGDSALEEALYLTKFASKVTLIHRRDEL--RASKILVERLR----ANPKIEVLWNTEVTEI----EGDG 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498012108 225 VVT---LANGQS-----LVADVVLSAIGLQPNISLAKEAGIQTSRG--ILTNAQLETNQPHIYAVGDCA 283
Cdd:COG0492 208 RVEgvtLKNVKTgeekeLEVDGVFVAIGLKPNTELLKGLGLELDEDgyIVVDEDMETSVPGVFAAGDVR 276
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
149-323 |
3.62e-13 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 70.61 E-value: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 149 KRVVILGAGLIGCEFANDLQHTGHQATVIDLANQPLgRLLPAHVSSAFKENLEATGIHFVLGTTVEKVSKIENGDYVVTl 228
Cdd:PLN02507 204 KRAVVLGGGYIAVEFASIWRGMGATVDLFFRKELPL-RGFDDEMRAVVARNLEGRGINLHPRTNLTQLTKTEGGIKVIT- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 229 ANGQSLVADVVLSAIGLQPNIS-LAKEA-GIQTSR--GILTNAQLETNQPHIYAVGDCAevNGLLLPYVMpiMQQARALA 304
Cdd:PLN02507 282 DHGEEFVADVVLFATGRAPNTKrLNLEAvGVELDKagAVKVDEYSRTNIPSIWAIGDVT--NRINLTPVA--LMEGTCFA 357
|
170 180
....*....|....*....|
gi 498012108 305 KT-LNGETTAVHYPAMPVAV 323
Cdd:PLN02507 358 KTvFGGQPTKPDYENVACAV 377
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
106-285 |
3.63e-12 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 67.72 E-value: 3.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 106 LVLAVGANPIRLAIAGdgstdIQVVNNLDDYktfrAKLEKraDKRVVILGAGLIGCEFANDLQHTGHQATVIDLANQPLg 185
Cdd:PTZ00058 206 ILIAVGNKPIFPDVKG-----KEFTISSDDF----FKIKE--AKRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLL- 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 186 RLLPAHVSSAFKENLEATGIHFVLGTTVEKVSKIENGDYVVTLANGQSLV-ADVVLSAIGLQPNISL--AKEAGIQTSRG 262
Cdd:PTZ00058 274 RKFDETIINELENDMKKNNINIITHANVEEIEKVKEKNLTIYLSDGRKYEhFDYVIYCVGRSPNTEDlnLKALNIKTPKG 353
|
170 180
....*....|....*....|....
gi 498012108 263 -ILTNAQLETNQPHIYAVGDCAEV 285
Cdd:PTZ00058 354 yIKVDDNQRTSVKHIYAVGDCCMV 377
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
86-281 |
4.71e-12 |
|
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: 67.31 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 86 EQQQLTVIKDGAESTQPYSQ------LVLAVGANPIRLAIAGDgstDIQVVNNLDDYktfrakLEKrADKRVVILGAGLI 159
Cdd:TIGR01423 129 EDKNVVLVRESADPKSAVKErlqaehILLATGSWPQMLGIPGI---EHCISSNEAFY------LDE-PPRRVLTVGGGFI 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 160 GCEFA---NDLQHTGHQATVIdLANQPLGRLLPAHVSSAFKENLEATGIHFVLGTTVEKVSKIENGDYVVTLANGQSLVA 236
Cdd:TIGR01423 199 SVEFAgifNAYKPRGGKVTLC-YRNNMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTLNADGSKHVTFESGKTLDV 277
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 498012108 237 DVVLSAIGLQP----------NISLAKEAGIQtsrgilTNAQLETNQPHIYAVGD 281
Cdd:TIGR01423 278 DVVMMAIGRVPrtqtlqldkvGVELTKKGAIQ------VDEFSRTNVPNIYAIGD 326
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
62-326 |
2.53e-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: 64.87 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 62 DTEKMATQLKMQIATHTWVKEIHTEQQQLTVI----------------KDGAESTQPYSQLVLAVGANPIRLAIAGDGST 125
Cdd:TIGR01438 87 DWKRLVEAVQNHIGSLNWGYRVALREKKVKYEnayaefvdkhrikatnKKGKEKIYSAERFLIATGERPRYPGIPGAKEL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 126 DIQVvnnlDDYKTFrakleKRADKRVVILGAGLIGCEFANDLQHTGHQATVidLANQPLGRLLPAHVSSAFKENLEATGI 205
Cdd:TIGR01438 167 CITS----DDLFSL-----PYCPGKTLVVGASYVALECAGFLAGIGLDVTV--MVRSILLRGFDQDCANKVGEHMEEHGV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 206 HFVLGTTVEKVSKIENgDYVVTLANGQSLVA---DVVLSAIGLQPNI-SLAKE-AGIQTSRG---ILTNAQLETNQPHIY 277
Cdd:TIGR01438 236 KFKRQFVPIKVEQIEA-KVLVEFTDSTNGIEeeyDTVLLAIGRDACTrKLNLEnVGVKINKKtgkIPADEEEQTNVPYIY 314
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 498012108 278 AVGDCAEVNGLLLPYVmpiMQQARALAKTL-NGETTAVHYPAMPVAVKTP 326
Cdd:TIGR01438 315 AVGDILEDKPELTPVA---IQAGRLLAQRLfKGSTVICDYENVPTTVFTP 361
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
88-378 |
2.07e-10 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 62.09 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 88 QQLTV-IKDGAESTQPYSQLVLAVGANPIRLAIAGDGSTDIqvvnnlddYKTFRAKLEKRADKRVVILGAGLIGCEFAND 166
Cdd:PRK13748 217 QTLIVrLNDGGERVVAFDRCLIATGASPAVPPIPGLKETPY--------WTSTEALVSDTIPERLAVIGSSVVALELAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 167 LQHTGHQATVidLA-NQPLGRLLPAhVSSAFKENLEATGIHFVLGTTVEKVSKiENGDYVVTLANGQsLVADVVLSAIGL 245
Cdd:PRK13748 289 FARLGSKVTI--LArSTLFFREDPA-IGEAVTAAFRAEGIEVLEHTQASQVAH-VDGEFVLTTGHGE-LRADKLLVATGR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 246 QPNI-SLAKEA-GIQTSRG--ILTNAQLETNQPHIYAVGDCAEvnglllpyvMPIMQQARALAKT-----LNGETTAVHY 316
Cdd:PRK13748 364 APNTrSLALDAaGVTVNAQgaIVIDQGMRTSVPHIYAAGDCTD---------QPQFVYVAAAAGTraainMTGGDAALDL 434
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498012108 317 PAMPVAVKTPAAPLTVLPAPIDA-----EVNWETEELDDgmIAKALDSQGTlRGFVLLGATAAKQRL 378
Cdd:PRK13748 435 TAMPAVVFTDPQVATVGYSEAEAhhdgiETDSRTLTLDN--VPRALANFDT-RGFIKLVIEEGSGRL 498
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
145-326 |
3.38e-10 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 61.38 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 145 KRADKRVVILGAGLIGCEFANDLQHTGHQATVIdLANQPLgRLLPAHVSSAFKENLEATGIHFVLGTTVEKVSKIENgDY 224
Cdd:PTZ00052 179 SKDPGKTLIVGASYIGLETAGFLNELGFDVTVA-VRSIPL-RGFDRQCSEKVVEYMKEQGTLFLEGVVPINIEKMDD-KI 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 225 VVTLANGQSLVADVVLSAIGLQPNISLAK--EAGIQTSRG---ILTNAQleTNQPHIYAVGDCAEVngllLPYVMPIMQQ 299
Cdd:PTZ00052 256 KVLFSDGTTELFDTVLYATGRKPDIKGLNlnAIGVHVNKSnkiIAPNDC--TNIPNIFAVGDVVEG----RPELTPVAIK 329
|
170 180
....*....|....*....|....*....
gi 498012108 300 A-RALAKTL-NGETTAVHYPAMPVAVKTP 326
Cdd:PTZ00052 330 AgILLARRLfKQSNEFIDYTFIPTTIFTP 358
|
|
| PTZ00318 |
PTZ00318 |
NADH dehydrogenase-like protein; Provisional |
4-310 |
4.54e-10 |
|
NADH dehydrogenase-like protein; Provisional
Pssm-ID: 185553 [Multi-domain] Cd Length: 424 Bit Score: 60.94 E-value: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 4 IVIIGSGMAGYAVARefrKLNPEqellmLCaddatNYAKPTLSNAFVANKAPEQIALGDTE--KMATQLKMQIATHTW-- 79
Cdd:PTZ00318 13 VVVLGTGWAGAYFVR---NLDPK-----KY-----NITVISPRNHMLFTPLLPQTTTGTLEfrSICEPVRPALAKLPNry 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 80 ----VKEIHTEQQQLTV-IKDGAES------TQPYSQLVLAVGANPIRLAIAGdgstdiqVVNN------LDDYKTFRAK 142
Cdd:PTZ00318 80 lravVYDVDFEEKRVKCgVVSKSNNanvntfSVPYDKLVVAHGARPNTFNIPG-------VEERafflkeVNHARGIRKR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 143 L---------------EKRADKRVVILGAGLIGCEFAndlqhtghqATVIDLANQPLGRLLP--------------AHVS 193
Cdd:PTZ00318 153 IvqcieraslpttsveERKRLLHFVVVGGGPTGVEFA---------AELADFFRDDVRNLNPelveeckvtvleagSEVL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 194 SAF--------KENLEATGIHFVLGTTVEKVSKiengDYVVTlANGQSLVADVVLSAIGLQPNiSLAKEAGI-QTSRG-I 263
Cdd:PTZ00318 224 GSFdqalrkygQRRLRRLGVDIRTKTAVKEVLD----KEVVL-KDGEVIPTGLVVWSTGVGPG-PLTKQLKVdKTSRGrI 297
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 498012108 264 LTNAQLET-NQPHIYAVGDCAEVNGLLLPYVMPIM-QQARALAKTLNGE 310
Cdd:PTZ00318 298 SVDDHLRVkPIPNVFALGDCAANEERPLPTLAQVAsQQGVYLAKEFNNE 346
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
149-281 |
3.88e-09 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 58.04 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 149 KRVVILGAGLIGCEFANDLQHTGHQATVIDLANQPLgRLLPAHVSSAFKEnLEATGIHFVLGTTVEKVSKIENGdYVVTL 228
Cdd:PRK07846 167 ESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLL-RHLDDDISERFTE-LASKRWDVRLGRNVVGVSQDGSG-VTLRL 243
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 498012108 229 ANGQSLVADVVLSAIGLQPNISL--AKEAGIQTSRG--ILTNAQLETNQPHIYAVGD 281
Cdd:PRK07846 244 DDGSTVEADVLLVATGRVPNGDLldAAAAGVDVDEDgrVVVDEYQRTSAEGVFALGD 300
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
150-293 |
8.49e-09 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 56.95 E-value: 8.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 150 RVVILGAGLIGCEFANDLQHTGHQATVIDLANQPLGRlLPAHVSSAFKENLEATGIHFVLGTTVEKVSKIENGDYVVTlA 229
Cdd:PRK08010 160 HLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPR-EDRDIADNIATILRDQGVDIILNAHVERISHHENQVQVHS-E 237
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498012108 230 NGQSLVaDVVLSAIGLQP-NISLAKE-AGIQTSR--GILTNAQLETNQPHIYAVGDCaeVNGLLLPYV 293
Cdd:PRK08010 238 HAQLAV-DALLIASGRQPaTASLHPEnAGIAVNErgAIVVDKYLHTTADNIWAMGDV--TGGLQFTYI 302
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
64-280 |
1.15e-07 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 53.00 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 64 EKMATQLKMQIATHTWVKEIHTEQQQLTVIKDGAESTQPYsqLVLAVG--ANPIRLaiagdGSTDIQVVN-NLDDYKTFr 140
Cdd:pfam13738 82 RRVADHFELPINLFEEVTSVKKEDDGFVVTTSKGTYQARY--VIIATGefDFPNKL-----GVPELPKHYsYVKDFHPY- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 141 aklekrADKRVVILGAGLIGCEFANDLQHTGHQATVIDlANQPLGRlLPAHVSSAFK-------ENLEATG---IHFvlG 210
Cdd:pfam13738 154 ------AGQKVVVIGGYNSAVDAALELVRKGARVTVLY-RGSEWED-RDSDPSYSLSpdtlnrlEELVKNGkikAHF--N 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498012108 211 TTVEKVSKIENGdYVVTLANGQSL-VADVVLSAIGLQPNISLAKEAGIQTSRG---ILTNAQLETNQPHIYAVG 280
Cdd:pfam13738 224 AEVKEITEVDVS-YKVHTEDGRKVtSNDDPILATGYHPDLSFLKKGLFELDEDgrpVLTEETESTNVPGLFLAG 296
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
150-351 |
5.20e-07 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 51.40 E-value: 5.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 150 RVVILGAGLIGCEFANDLQHTGHQATVI---DlanqplgRLLP---AHVSSAFKENLEATGIHFVLGTTVEKVSKIENGd 223
Cdd:PRK07845 179 HLIVVGSGVTGAEFASAYTELGVKVTLVssrD-------RVLPgedADAAEVLEEVFARRGMTVLKRSRAESVERTGDG- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 224 YVVTLANGQSLVADVVLSAIGLQPN---ISLAkEAGIQTSRG--ILTNAQLETNQPHIYAVGDCAEVngLLLPYVMPiMQ 298
Cdd:PRK07845 251 VVVTLTDGRTVEGSHALMAVGSVPNtagLGLE-EAGVELTPSghITVDRVSRTSVPGIYAAGDCTGV--LPLASVAA-MQ 326
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498012108 299 QARALAKTLnGEttAVHypamPVAVKTPAAplTVLPAPIDAEVNWETEELDDG 351
Cdd:PRK07845 327 GRIAMYHAL-GE--AVS----PLRLKTVAS--NVFTRPEIATVGVSQAAIDSG 370
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
233-314 |
1.36e-06 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 50.50 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 233 SLVADVVLSAIGLQPNISLAKEAGIQTSRG--ILTNAQ-LETNQPHIYAVGDCAEVNGLLLPYVMPIMQQARALAKTLNG 309
Cdd:PRK12814 423 TLQADTVISAIGQQVDPPIAEAAGIGTSRNgtVKVDPEtLQTSVAGVFAGGDCVTGADIAINAVEQGKRAAHAIDLFLNG 502
|
....*
gi 498012108 310 ETTAV 314
Cdd:PRK12814 503 KPVTA 507
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
143-276 |
7.28e-06 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 48.19 E-value: 7.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 143 LEKRADKRVVILGAGLIGCEFANDLQHTGHQATVIDLANQPLGRL--------LPAHVSSAFKENLEATGIHFVLGTTVE 214
Cdd:PRK12814 188 RAPKSGKKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMrygiprfrLPESVIDADIAPLRAMGAEFRFNTVFG 267
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498012108 215 KvskiengDyvVTLANGQSLVaDVVLSAIGLQP----NISLAKEAGIQTSRGILTNAQLETnQPHI 276
Cdd:PRK12814 268 R-------D--ITLEELQKEF-DAVLLAVGAQKaskmGIPGEELPGVISGIDFLRNVALGT-ALHP 322
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
107-283 |
1.65e-04 |
|
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: 43.59 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 107 VLAVGA-NPIRLAIAGDGSTDI---------QVVNNLDDYKTFraklekrADKRVVILGAGLIgcefAND-----LQHTG 171
Cdd:COG0493 211 FLATGAgKPRDLGIPGEDLKGVhsamdfltaVNLGEAPDTILA-------VGKRVVVIGGGNT----AMDcartaLRLGA 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 172 HQATVI---DLANqplgrlLPAH---VSSAFKEnleatGIHFVLGTTVEKVSKIENG----------DYVVTLANG---- 231
Cdd:COG0493 280 ESVTIVyrrTREE------MPASkeeVEEALEE-----GVEFLFLVAPVEIIGDENGrvtglecvrmELGEPDESGrrrp 348
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498012108 232 -------QSLVADVVLSAIGLQPNIS-LAKEAGIQTSRG--ILTNAQ-LETNQPHIYAVGDCA 283
Cdd:COG0493 349 vpiegseFTLPADLVILAIGQTPDPSgLEEELGLELDKRgtIVVDEEtYQTSLPGVFAGGDAV 411
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
91-323 |
7.23e-04 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 41.79 E-value: 7.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 91 TVIKDGAESTQpySQLVLAVGANPIRLAIAGdgstdIQVVNNLDDYKTFRAKLEKradkrVVILGAGLIGCEFA---NDL 167
Cdd:PLN02546 207 TVDVDGKLYTA--RNILIAVGGRPFIPDIPG-----IEHAIDSDAALDLPSKPEK-----IAIVGGGYIALEFAgifNGL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 168 QHTGHqatvIDLANQPLGRLLPAHVSSAFKENLEATGIHFvlGTTVEKVSKIENGDYVVTLANGQSLVADV--VLSAIGL 245
Cdd:PLN02546 275 KSDVH----VFIRQKKVLRGFDEEVRDFVAEQMSLRGIEF--HTEESPQAIIKSADGSLSLKTNKGTVEGFshVMFATGR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 246 QPNislAKEAGIQT-------SRGILTNAQLETNQPHIYAVGDCAE-VNglLLPYVmpiMQQARALAKTLNG-ETTAVHY 316
Cdd:PLN02546 349 KPN---TKNLGLEEvgvkmdkNGAIEVDEYSRTSVPSIWAVGDVTDrIN--LTPVA---LMEGGALAKTLFGnEPTKPDY 420
|
....*..
gi 498012108 317 PAMPVAV 323
Cdd:PLN02546 421 RAVPSAV 427
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
107-282 |
7.26e-04 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 41.69 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 107 VLAVGA-NPIRLAIAG---DGSTD--------IQVVNNLDDYKTFRAKlekraDKRVVILGAGligcefanDlqhTG--- 171
Cdd:PRK12810 233 FLGTGAyKPRDLGIPGrdlDGVHFamdfliqnTRRVLGDETEPFISAK-----GKHVVVIGGG--------D---TGmdc 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498012108 172 ------HQA---TVIDLANQPLGRLLPAH----------VSSAFKE----------------NLEATGIHFVlgtTVE-- 214
Cdd:PRK12810 297 vgtairQGAksvTQRDIMPMPPSRRNKNNpwpywpmkleVSNAHEEgverefnvqtkefegeNGKVTGVKVV---RTElg 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498012108 215 --KVSKIENGDYVvtlangqsLVADVVLSAIGLQPNI-SLAKEAGIQT-SRGIL--TNAQLETNQPHIYAVGDC 282
Cdd:PRK12810 374 egDFEPVEGSEFV--------LPADLVLLAMGFTGPEaGLLAQFGVELdERGRVaaPDNAYQTSNPKVFAAGDM 439
|
|
| |
