|
Name |
Accession |
Description |
Interval |
E-value |
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
6-408 |
6.53e-131 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 382.18 E-value: 6.53e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 6 PYLIAGGGHAARRAAETLRERDPAARIVMIGAEPELPYDRPVLSKeaLVGGDAGERRAFVRDAAWYRERDIELRLGVRVE 85
Cdd:COG1251 3 RIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSK--VLAGETDEEDLLLRPADFYEENGIDLRLGTRVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 86 AIERGARRVRLSDGARLGYARLLIATGSRVRRFAGPVDAGVHVHYVRTLADTRALRAALAPGKRVAVLGGGFIGLEVAAS 165
Cdd:COG1251 81 AIDRAARTVTLADGETLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 166 AVRLGCRATVVDPAPRLLQRGMPEAVGAFALALHARHGVDVRLGALPERIRRAANGAAVVETSAGGIVADVVVAGIGVVP 245
Cdd:COG1251 161 LRKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRLADGEELPADLVVVAIGVRP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 246 NVELAQAAGLDVDDGVCVDEMCRTADPAIFAAGEVTRHFNPLVGRaLRIESWQIAENQPAVAAANMLGAAETYAQW-PWL 324
Cdd:COG1251 241 NTELARAAGLAVDRGIVVDDYLRTSDPDIYAAGDCAEHPGPVYGR-RVLELVAPAYEQARVAAANLAGGPAAYEGSvPST 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 325 WSDQYDCNLQTLGLFGGERTLVLRGSPERDRaFCVFALNARReLAAVAAVNAGREIAVCRRLMTAGVALDPARLADPSDA 404
Cdd:COG1251 320 KLKVFGVDVASAGDAEGDEEVVVRGDPARGV-YKKLVLRDGR-LVGAVLVGDTSDAGALRQLIKNGRPLPPRALLDAALP 397
|
....
gi 516493774 405 LRAM 408
Cdd:COG1251 398 LKEL 401
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
25-337 |
5.46e-90 |
|
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: 274.77 E-value: 5.46e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 25 ERDPAARIVMIGAEPELPYDRPVLSKeaLVGGDAGERRA-FVRDAAWYRERDIELRLGVRVEAIERGARRVRLSDGARLG 103
Cdd:COG0446 1 RLGPDAEITVIEKGPHHSYQPCGLPY--YVGGGIKDPEDlLVRTPESFERKGIDVRTGTEVTAIDPEAKTVTLRDGETLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 104 YARLLIATGSRVRRFAGPVDAGVHVHYVRTLADTRALRAALA--PGKRVAVLGGGFIGLEVAASAVRLGCRATVVDPAPR 181
Cdd:COG0446 79 YDKLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALREALKefKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 182 LLQRGMPEaVGAFALALHARHGVDVRLGALPERIRrAANGAAVVETSAGGIVADVVVAGIGVVPNVELAQAAGLDVDD-- 259
Cdd:COG0446 159 LLGVLDPE-MAALLEEELREHGVELRLGETVVAID-GDDKVAVTLTDGEEIPADLVVVAPGVRPNTELAKDAGLALGErg 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516493774 260 GVCVDEMCRTADPAIFAAGEVTRHFNPLVGRALRIESWQIAENQPAVAAANMLGAAETYAQWPWLWSDQYDCNLQTLG 337
Cdd:COG0446 237 WIKVDETLQTSDPDVYAAGDCAEVPHPVTGKTVYIPLASAANKQGRVAAENILGGPAPFPGLGTFISKVFDLCIASTG 314
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
7-400 |
3.11e-83 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 260.24 E-value: 3.11e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 7 YLIAGGGHAARRAAETLRERDPAARIVMIGAEPELPYDRPVLSKEALVggDAGERRAFVRDAAWYRERDIELRLGVRVEA 86
Cdd:PRK09754 6 IIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLL--EDSPQLQQVLPANWWQENNVHLHSGVTIKT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 87 IERGARRVRLSDGARLGYARLLIATGSRVRRFAGPVDAGVHVHYVRTLADTRALRAALAPGKRVAVLGGGFIGLEVAASA 166
Cdd:PRK09754 84 LGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAASA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 167 VRLGCRATVVDPAPRLLQRGMPEAVGAFALALHARHGVDVRLGAlpeRIRRAANGAAVVETSAGG--IVADVVVAGIGVV 244
Cdd:PRK09754 164 TQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNN---AIEHVVDGEKVELTLQSGetLQADVVIYGIGIS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 245 PNVELAQAAGLDVDDGVCVDEMCRTADPAIFAAGEVTRHFNPlVGRALRIESWQIAENQPAVAAANMLGAAETYAQWPWL 324
Cdd:PRK09754 241 ANDQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAITRLD-NGALHRCESWENANNQAQIAAAAMLGLPLPLLPPPWF 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516493774 325 WSDQYDCNLQTLGLFGGERTLVlRGSPERDRAFcVFALNARRELAAVaAVNAGREIAVCRRLMTAGVALDPARLAD 400
Cdd:PRK09754 320 WSDQYSDNLQFIGDMRGDDWLC-RGNPETQKAI-WFNLQNGVLIGAV-TLNQGREIRPIRKWIQSGKTFDAKLLID 392
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
7-303 |
1.81e-64 |
|
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: 208.71 E-value: 1.81e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 7 YLIAGGGHAARRAAETLRERDpaARIVMIGAEPELPYDRPVLSKEAL-VGGDAGERRAFVRDAAWYRE------RDIELR 79
Cdd:pfam07992 3 VVVIGGGPAGLAAALTLAQLG--GKVTLIEDEGTCPYGGCVLSKALLgAAEAPEIASLWADLYKRKEEvvkklnNGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 80 LGVRVEAIERGARRVRLS-----DGARLGYARLLIATGSRVRRFAGPVDAGVHVHYVRTLADTRALRAALAPgKRVAVLG 154
Cdd:pfam07992 81 LGTEVVSIDPGAKKVVLEelvdgDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLLP-KRVVVVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 155 GGFIGLEVAASAVRLGCRATVVDPAPRLLqRGMPEAVGAFALALHARHGVDVRLGALPERIRRAANGAAVVETSAGGIVA 234
Cdd:pfam07992 160 GGYIGVELAAALAKLGKEVTLIEALDRLL-RAFDEEISAALEKALEKNGVEVRLGTSVKEIIGDGDGVEVILKDGTEIDA 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516493774 235 DVVVAGIGVVPNVELAQAAGLDVDD--GVCVDEMCRTADPAIFAAGEVTRHfnplvgralRIESWQIAENQ 303
Cdd:pfam07992 239 DLVVVAIGRRPNTELLEAAGLELDErgGIVVDEYLRTSVPGIYAAGDCRVG---------GPELAQNAVAQ 300
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
9-289 |
3.55e-40 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 152.29 E-value: 3.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 9 IAGGGHAARRAAETLRERDPAA-RIVMIGAEPELPYDRPVLSKeaLVGGDAGERRAFVRDAAWYRERDIELRLGVRVEAI 87
Cdd:TIGR02374 3 LVGNGMAGHRCIEEVLKLNRHMfEITIFGEEPHPNYNRILLSS--VLQGEADLDDITLNSKDWYEKHGITLYTGETVIQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 88 ERGARRVRLSDGARLGYARLLIATGSR--VRRFAGPVDAGVHVHyvRTLADTRALRAALAPGKRVAVLGGGFIGLEVAAS 165
Cdd:TIGR02374 81 DTDQKQVITDAGRTLSYDKLILATGSYpfILPIPGADKKGVYVF--RTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAAVG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 166 AVRLGCRATVVDPAPRLLQRGMPEAVGAFALALHARHGVDVRLGALPERIRRAANGAAVVETSAGGIVADVVVAGIGVVP 245
Cdd:TIGR02374 159 LQNLGMDVSVIHHAPGLMAKQLDQTAGRLLQRELEQKGLTFLLEKDTVEIVGATKADRIRFKDGSSLEADLIVMAAGIRP 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 516493774 246 NVELAQAAGLDVDDGVCVDEMCRTADPAIFAAGEVTRHFNPLVG 289
Cdd:TIGR02374 239 NDELAVSAGIKVNRGIIVNDSMQTSDPDIYAVGECAEHNGRVYG 282
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
1-278 |
1.66e-36 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 136.97 E-value: 1.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 1 MStaDPYLIAGGGHAARRAAETLRERDPAARIVMIGAEPELPYDRP----VLSK----EALVGGDAGErrafvrdaaWYR 72
Cdd:PRK04965 1 MS--NGIVIIGSGFAARQLVKNIRKQDAHIPITLITADSGDEYNKPdlshVFSQgqraDDLTRQSAGE---------FAE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 73 ERDIELRLGVRVEAIERGARRVrLSDGARLGYARLLIATGSRVrrFAGPVDAGVHVHYVRTLADTRALRAALAPGKRVAV 152
Cdd:PRK04965 70 QFNLRLFPHTWVTDIDAEAQVV-KSQGNQWQYDKLVLATGASA--FVPPIPGRELMLTLNSQQEYRAAETQLRDAQRVLV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 153 LGGGFIGLEVAASAVRLGCRATVVDPAPRLLQRGMPEAVgafALALH---ARHGVDVRLGALPERIRRAANGAAVVETSA 229
Cdd:PRK04965 147 VGGGLIGTELAMDLCRAGKAVTLVDNAASLLASLMPPEV---SSRLQhrlTEMGVHLLLKSQLQGLEKTDSGIRATLDSG 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 516493774 230 GGIVADVVVAGIGVVPNVELAQAAGLDVDDGVCVDEMCRTADPAIFAAG 278
Cdd:PRK04965 224 RSIEVDAVIAAAGLRPNTALARRAGLAVNRGIVVDSYLQTSAPDIYALG 272
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
90-313 |
8.45e-29 |
|
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: 117.11 E-value: 8.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 90 GARRVRLSDGARLGYARLLIATGSRVRRFAGPVDAGVHVHyvrtlaDTR-ALRAALAPgKRVAVLGGGFIGLEVAASAVR 168
Cdd:COG1249 117 DPHTVEVTGGETLTADHIVIATGSRPRVPPIPGLDEVRVL------TSDeALELEELP-KSLVVIGGGYIGLEFAQIFAR 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 169 LGCRATVVDPAPRLLqRGMPEAVGAFALALHARHGVDVRLGALPERIRRAANGAAVVETSAGG---IVADVVVAGIGVVP 245
Cdd:COG1249 190 LGSEVTLVERGDRLL-PGEDPEISEALEKALEKEGIDILTGAKVTSVEKTGDGVTVTLEDGGGeeaVEADKVLVATGRRP 268
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516493774 246 NVEL--AQAAGLDVDD--GVCVDEMCRTADPAIFAAGEVTRHFnPLVgralrieswQIAENQPAVAAANMLG 313
Cdd:COG1249 269 NTDGlgLEAAGVELDErgGIKVDEYLRTSVPGIYAIGDVTGGP-QLA---------HVASAEGRVAAENILG 330
|
|
| Reductase_C |
pfam14759 |
Reductase C-terminal; This domain occurs at the C-terminus of various reductase enzymes, ... |
323-407 |
3.58e-26 |
|
Reductase C-terminal; This domain occurs at the C-terminus of various reductase enzymes, including putidaredoxin reductase, ferredoxin reductase, 3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component, benzene 1,2-dioxygenase system ferredoxin--NAD(+) reductase subunit, rhodocoxin reductase, biphenyl dioxygenase system ferredoxin--NAD(+) reductase component, rubredoxin-NAD(+) reductase and toluene 1,2-dioxygenase system ferredoxin--NAD(+) reductase component. In putidaredoxin reductase this domain is involved in dimerization. In the FAD-containing NADH-ferredoxin reductase (BphA4) it is responsible for interaction with the Rieske-type [2Fe-2S] ferredoxin (BphA3).
Pssm-ID: 434185 [Multi-domain] Cd Length: 83 Bit Score: 100.72 E-value: 3.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 323 WLWSDQYDCNLQTLGLFGGERTLVLRGSPErDRAFCVFALNARReLAAVAAVNAGREIAVCRRLMTAGVALDPARLADPS 402
Cdd:pfam14759 1 WFWSDQYDLKLQIAGLPTGADEVVLRGDPE-DGAFSVFYLRDGR-LVAVDAVNRPRDFMAARRLIARGASVDPAALADPA 78
|
....*
gi 516493774 403 DALRA 407
Cdd:pfam14759 79 VDLKA 83
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
8-310 |
1.32e-25 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 107.14 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 8 LIAGGGHAARRAAETLRER-DPAARIVMIGAEPELPYdRPVLSkEALVGG-DAGERRAFVRDAAwyRERDIELRLGvRVE 85
Cdd:COG1252 5 VIVGGGFAGLEAARRLRKKlGGDAEVTLIDPNPYHLF-QPLLP-EVAAGTlSPDDIAIPLRELL--RRAGVRFIQG-EVT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 86 AIERGARRVRLSDGARLGYARLLIATGSRVRRFAGPvDAGVHVHYVRTLADTRALRAAL---------APGKRVAVLGGG 156
Cdd:COG1252 80 GIDPEARTVTLADGRTLSYDYLVIATGSVTNFFGIP-GLAEHALPLKTLEDALALRERLlaaferaerRRLLTIVVVGGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 157 FIGLEVA---ASAVRLGCRA----------TVVDPAPRLLQrGMPEAVGAFALALHARHGVDVRLGALPERIRraangAA 223
Cdd:COG1252 159 PTGVELAgelAELLRKLLRYpgidpdkvriTLVEAGPRILP-GLGEKLSEAAEKELEKRGVEVHTGTRVTEVD-----AD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 224 VVETSAGG-IVADVVVAGIGVVPNvELAQAAGLDVDDG--VCVDEMCRTAD-PAIFAAGEV----TRHFNPLVGRAlrie 295
Cdd:COG1252 233 GVTLEDGEeIPADTVIWAAGVKAP-PLLADLGLPTDRRgrVLVDPTLQVPGhPNVFAIGDCaavpDPDGKPVPKTA---- 307
|
330
....*....|....*
gi 516493774 296 swQIAENQPAVAAAN 310
Cdd:COG1252 308 --QAAVQQAKVLAKN 320
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
8-279 |
3.55e-23 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 100.89 E-value: 3.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 8 LIAGGGHAARRAAETLRERDPAARIVM--------IGAePELPYdrpvlskeaLVGG---DAGERRAFVRDAAwyRERDI 76
Cdd:PRK09564 4 IIIGGTAAGMSAAAKAKRLNKELEITVyektdivsFGA-CGLPY---------FVGGffdDPNTMIARTPEEF--IKSGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 77 ELRLGVRVEAIERGARRVRLSDGAR-----LGYARLLIATGSR--VRRFAGpVDAGvHVHYVRTLADTRALRAALAPG-- 147
Cdd:PRK09564 72 DVKTEHEVVKVDAKNKTITVKNLKTgsifnDTYDKLMIATGARpiIPPIKN-INLE-NVYTLKSMEDGLALKELLKDEei 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 148 KRVAVLGGGFIGLEVAASAVRLGCRATVVDPAPRLLQRGM-PEAVGAFALALHaRHGVDVRLGALPERIRRAANGAAVVe 226
Cdd:PRK09564 150 KNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPDSFdKEITDVMEEELR-ENGVELHLNEFVKSLIGEDKVEGVV- 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 516493774 227 TSAGGIVADVVVAGIGVVPNVELAQAAGLD-VDDG-VCVDEMCRTADPAIFAAGE 279
Cdd:PRK09564 228 TDKGEYEADVVIVATGVKPNTEFLEDTGLKtLKNGaIIVDEYGETSIENIYAAGD 282
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
90-280 |
9.22e-22 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 96.81 E-value: 9.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 90 GARRVRLsDGARLGYARLLIATGSRVrrfAGPVDAGVHVhyVRTLADTRALRAALAPgKRVAVLGGGFIGLEVAASAVRL 169
Cdd:PRK06370 121 SPNTVRV-GGETLRAKRIFINTGARA---AIPPIPGLDE--VGYLTNETIFSLDELP-EHLVIIGGGYIGLEFAQMFRRF 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 170 GCRATVVDPAPRLLQRGMPEAVGAFALALhARHGVDVRLGALPERIRRAANGAAVVETSAGG---IVADVVVAGIGVVPN 246
Cdd:PRK06370 194 GSEVTVIERGPRLLPREDEDVAAAVREIL-EREGIDVRLNAECIRVERDGDGIAVGLDCNGGapeITGSHILVAVGRVPN 272
|
170 180 190
....*....|....*....|....*....|....*...
gi 516493774 247 VE-LA-QAAGLDVDD--GVCVDEMCRTADPAIFAAGEV 280
Cdd:PRK06370 273 TDdLGlEAAGVETDArgYIKVDDQLRTTNPGIYAAGDC 310
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
9-279 |
1.55e-21 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 97.11 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 9 IAGGGHAARRAAETLRERDPAAR--IVMIGAEPELPYDRPVLSkeALVGGDAGERRAFVRDAaWYRERDIELRLGVRVEA 86
Cdd:PRK14989 8 IIGNGMVGHRFIEDLLDKADAANfdITVFCEEPRIAYDRVHLS--SYFSHHTAEELSLVREG-FYEKHGIKVLVGERAIT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 87 IERGARRVRLSDGARLGYARLLIATGSR--VRRFAGPVDAGVHVHyvRTLADTRALRAALAPGKRVAVLGGGFIGLEVAA 164
Cdd:PRK14989 85 INRQEKVIHSSAGRTVFYDKLIMATGSYpwIPPIKGSETQDCFVY--RTIEDLNAIEACARRSKRGAVVGGGLLGLEAAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 165 SAVRLGCRATVVDPAPRLLQRGMPEAVGAFALALHARHGVDVRLGALPERIRRAANGAAVVETSAGG--IVADVVVAGIG 242
Cdd:PRK14989 163 ALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSKNTLEIVQEGVEARKTMRFADGseLEVDFIVFSTG 242
|
250 260 270
....*....|....*....|....*....|....*....
gi 516493774 243 VVPNVELAQAAGLDVDD--GVCVDEMCRTADPAIFAAGE 279
Cdd:PRK14989 243 IRPQDKLATQCGLAVAPrgGIVINDSCQTSDPDIYAIGE 281
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
106-281 |
1.58e-19 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 90.24 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 106 RLLIATGSRVRRFAGpVDAGVHVHYVRTladtralRAALAP---GKRVAVLGGGFIGLEVAASAVRLGCRATVVDPAPRL 182
Cdd:PRK06292 133 NIVIATGSRVPPIPG-VWLILGDRLLTS-------DDAFELdklPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRI 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 183 LqRGMPEAVGAFALALHARHgVDVRLGALPERIRRAANGAAVVETSAGG---IVADVVVAGIGVVPNVEL--AQAAGLDV 257
Cdd:PRK06292 205 L-PLEDPEVSKQAQKILSKE-FKIKLGAKVTSVEKSGDEKVEELEKGGKtetIEADYVLVATGRRPNTDGlgLENTGIEL 282
|
170 180
....*....|....*....|....*.
gi 516493774 258 DDG--VCVDEMCRTADPAIFAAGEVT 281
Cdd:PRK06292 283 DERgrPVVDEHTQTSVPGIYAAGDVN 308
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
90-280 |
3.62e-19 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 88.86 E-value: 3.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 90 GARRVRLSDGARLGYARLLIATGSRVRRFAGPVDAGVHVHYVRTLadtraLRAALAPgKRVAVLGGGFIGLEVAASAVRL 169
Cdd:PRK07846 115 GPKTLRTGDGEEITADQVVIAAGSRPVIPPVIADSGVRYHTSDTI-----MRLPELP-ESLVIVGGGFIAAEFAHVFSAL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 170 GCRATVVDPAPRLLqRGMPEAVGAfALALHARHGVDVRLGALPERIRRAANGAAVVETSAGGIVADVVVAGIGVVPNVEL 249
Cdd:PRK07846 189 GVRVTVVNRSGRLL-RHLDDDISE-RFTELASKRWDVRLGRNVVGVSQDGSGVTLRLDDGSTVEADVLLVATGRVPNGDL 266
|
170 180 190
....*....|....*....|....*....|....*
gi 516493774 250 --AQAAGLDVDDG--VCVDEMCRTADPAIFAAGEV 280
Cdd:PRK07846 267 ldAAAAGVDVDEDgrVVVDEYQRTSAEGVFALGDV 301
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
109-282 |
4.29e-18 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 85.75 E-value: 4.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 109 IATGSRVRRFAG-PVDagvhvhYVRTLADTRALRAALAPgKRVAVLGGGFIGLEVAASAVRLGCRATVVDPAPRLLqrGM 187
Cdd:PRK06327 151 IATGSEPRHLPGvPFD------NKIILDNTGALNFTEVP-KKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFL--AA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 188 P-EAVGAFALALHARHGVDVRLGALPERIRRAANGAAVVETSAGG----IVADVVVAGIGVVPNVE--LAQAAGLDVDDG 260
Cdd:PRK06327 222 AdEQVAKEAAKAFTKQGLDIHLGVKIGEIKTGGKGVSVAYTDADGeaqtLEVDKLIVSIGRVPNTDglGLEAVGLKLDER 301
|
170 180
....*....|....*....|....
gi 516493774 261 --VCVDEMCRTADPAIFAAGEVTR 282
Cdd:PRK06327 302 gfIPVDDHCRTNVPNVYAIGDVVR 325
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
149-225 |
2.16e-14 |
|
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: 68.00 E-value: 2.16e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516493774 149 RVAVLGGGFIGLEVAASAVRLGCRATVVDPAPRLLqRGMPEAVGAFALALHARHGVDVRLGALPERIRRAANGAAVV 225
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLL-PGFDPEIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVV 76
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
93-281 |
2.52e-14 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 74.41 E-value: 2.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 93 RVRLSDGARLGYAR-LLIATGSRVRRFAG-PVDAgvhvhyvRTLAD-TRALRAALAPgKRVAVLGGGFIGLEVaASAVR- 168
Cdd:PRK06416 123 RVMTEDGEQTYTAKnIILATGSRPRELPGiEIDG-------RVIWTsDEALNLDEVP-KSLVVIGGGYIGVEF-ASAYAs 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 169 LGCRATVVDPAPRLLQRGMPEAVGAFALALHARhGVDVRLGALPERIRRAANGaAVVETSAGGIV----ADVVVAGIGVV 244
Cdd:PRK06416 194 LGAEVTIVEALPRILPGEDKEISKLAERALKKR-GIKIKTGAKAKKVEQTDDG-VTVTLEDGGKEetleADYVLVAVGRR 271
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 516493774 245 PNVE---LAQaAGLDVDDG-VCVDEMCRTADPAIFAAGEVT 281
Cdd:PRK06416 272 PNTEnlgLEE-LGVKTDRGfIEVDEQLRTNVPNIYAIGDIV 311
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
75-283 |
9.87e-14 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 71.30 E-value: 9.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 75 DIELRLGvRVEAIER--GARRVRLSDGARLgYAR-LLIATGSRVRR--FAGPVDA-GVHVHYVRTlADtralrAALAPGK 148
Cdd:COG0492 71 GAEILLE-EVTSVDKddGPFRVTTDDGTEY-EAKaVIIATGAGPRKlgLPGEEEFeGRGVSYCAT-CD-----GFFFRGK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 149 RVAVLGGGFIGLEVA------ASAVRLGCRATVVDPAPRLLQRgmpeavgafalaLHARHGVDVRLGALPERIR--RAAN 220
Cdd:COG0492 143 DVVVVGGGDSALEEAlyltkfASKVTLIHRRDELRASKILVER------------LRANPKIEVLWNTEVTEIEgdGRVE 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516493774 221 GAAVVETSAGG---IVADVVVAGIGVVPNVELAQAAGLDVDDG--VCVDEMCRTADPAIFAAGEVTRH 283
Cdd:COG0492 211 GVTLKNVKTGEekeLEVDGVFVAIGLKPNTELLKGLGLELDEDgyIVVDEDMETSVPGVFAAGDVRDY 278
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
93-280 |
5.30e-13 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 70.19 E-value: 5.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 93 RVRLSDGA--RLGYARLLIATGSRVRRfagpvDAGVHVHYVRTLADTRALRAALAPgKRVAVLGGGFIGLEVAASAVRLG 170
Cdd:PRK05249 125 EVECPDGEveTLTADKIVIATGSRPYR-----PPDVDFDHPRIYDSDSILSLDHLP-RSLIIYGAGVIGCEYASIFAALG 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 171 CRATVVDPAPRLLQRGMPEAVGAFALALHARhGVDVRLGALPERIRRAANGAAVVETSAGGIVADVVVAGIGVVPNVE-L 249
Cdd:PRK05249 199 VKVTLINTRDRLLSFLDDEISDALSYHLRDS-GVTIRHNEEVEKVEGGDDGVIVHLKSGKKIKADCLLYANGRTGNTDgL 277
|
170 180 190
....*....|....*....|....*....|....
gi 516493774 250 A-QAAGLDVDD-G-VCVDEMCRTADPAIFAAGEV 280
Cdd:PRK05249 278 NlENAGLEADSrGqLKVNENYQTAVPHIYAVGDV 311
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
107-281 |
1.39e-12 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 69.01 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 107 LLIATGSRVRRFAGP-VDAGVHVHyvrtlaDTRALRAALAPGKRVAVLGGGFIGLEVAASAVRLGCRATVVDPAPRLLQR 185
Cdd:PRK07251 122 IVINTGAVSNVLPIPgLADSKHVY------DSTGIQSLETLPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTILPR 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 186 GMPEaVGAFALALHARHGVDVRLGALPERIRRAAnGAAVVETSAGGIVADVVVAGIGVVPNVELAQAAGLDVD----DGV 261
Cdd:PRK07251 196 EEPS-VAALAKQYMEEDGITFLLNAHTTEVKNDG-DQVLVVTEDETYRFDALLYATGRKPNTEPLGLENTDIElterGAI 273
|
170 180
....*....|....*....|
gi 516493774 262 CVDEMCRTADPAIFAAGEVT 281
Cdd:PRK07251 274 KVDDYCQTSVPGVFAVGDVN 293
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
148-285 |
9.20e-12 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 66.33 E-value: 9.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 148 KRVAVLGGGFIGLEVAASAVRLGCRATVVDPAPRLLqRGMPEAVGAFALALHARHGVDVRLGALPERIRRAANGAAVVET 227
Cdd:PRK06116 168 KRVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPL-RGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEKNADGSLTLTL 246
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516493774 228 SAGG-IVADVVVAGIGVVPNVE---LaQAAGLDVDDG--VCVDEMCRTADPAIFAAGEVTRHFN 285
Cdd:PRK06116 247 EDGEtLTVDCLIWAIGREPNTDglgL-ENAGVKLNEKgyIIVDEYQNTNVPGIYAVGDVTGRVE 309
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
94-285 |
1.07e-11 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 66.38 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 94 VRLSDGARLGYA--RLLIATGSRVRRFAGPVdagvhvhyvRTLADT--RALRAALAPgKRVAVLGGGFIGLEVAASAVRL 169
Cdd:PLN02507 156 VTQLDGTKLRYTakHILIATGSRAQRPNIPG---------KELAITsdEALSLEELP-KRAVVLGGGYIAVEFASIWRGM 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 170 GCRATVVDPAPRLLqRGMPEAVGAF-ALALHARhGVDVRLGALPERIRRAANGAAVVETSAGGIVADVVVAGIGVVPNVE 248
Cdd:PLN02507 226 GATVDLFFRKELPL-RGFDDEMRAVvARNLEGR-GINLHPRTNLTQLTKTEGGIKVITDHGEEFVADVVLFATGRAPNTK 303
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 516493774 249 LA--QAAGLDVDD--GVCVDEMCRTADPAIFAAGEVTRHFN 285
Cdd:PLN02507 304 RLnlEAVGVELDKagAVKVDEYSRTNIPSIWAIGDVTNRIN 344
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
108-282 |
6.32e-10 |
|
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: 60.53 E-value: 6.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 108 LIATGSRVRRF---AGPVDAGVH--VHYVRTLADTRALRAALAPGKRVAVLGGGFIGLEVAASAVRLGCR-ATVVDPAPR 181
Cdd:COG0493 211 FLATGAGKPRDlgiPGEDLKGVHsaMDFLTAVNLGEAPDTILAVGKRVVVIGGGNTAMDCARTALRLGAEsVTIVYRRTR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 182 llqRGMPEAVGAFALALHarHGVDVRLGALPERIRRAANGAAV---------VETSAGG-------------IVADVVVA 239
Cdd:COG0493 291 ---EEMPASKEEVEEALE--EGVEFLFLVAPVEIIGDENGRVTglecvrmelGEPDESGrrrpvpiegseftLPADLVIL 365
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 516493774 240 GIGVVPNVE-LAQAAGLDVDDG--VCVDEMC-RTADPAIFAAGEVTR 282
Cdd:COG0493 366 AIGQTPDPSgLEEELGLELDKRgtIVVDEETyQTSLPGVFAGGDAVR 412
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
139-279 |
2.47e-09 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 58.97 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 139 ALRAALAPGKRVAVLGGGFIGLEVAASAVRLGcrATVVDPAPRLLQRGMPEAVGAFALALHarHGVDVRLGALPERIRRA 218
Cdd:PRK12814 315 ALGTALHPGKKVVVIGGGNTAIDAARTALRLG--AESVTILYRRTREEMPANRAEIEEALA--EGVSLRELAAPVSIERS 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 219 ANGAAV--------------------VETSAGGIVADVVVAGIGVVPNVELAQAAGLDVDDGVCV---DEMCRTADPAIF 275
Cdd:PRK12814 391 EGGLELtaikmqqgepdesgrrrpvpVEGSEFTLQADTVISAIGQQVDPPIAEAAGIGTSRNGTVkvdPETLQTSVAGVF 470
|
....
gi 516493774 276 AAGE 279
Cdd:PRK12814 471 AGGD 474
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
37-281 |
3.84e-09 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 58.10 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 37 AEPELPYDRPVLSKEALVGgdagerraFVRDAAWYRERD---IELRLGvRVEAIERGARRVRLSDGAR-LGYARLLIATG 112
Cdd:PRK08010 58 AQQHTDFVRAIQRKNEVVN--------FLRNKNFHNLADmpnIDVIDG-QAEFINNHSLRVHRPEGNLeIHGEKIFINTG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 113 SRVRRFAGP---VDAGVHvhyvrtlADTRALRAALAPGkRVAVLGGGFIGLEVAASAVRLGCRATVVDPAPRLLQRGMPE 189
Cdd:PRK08010 129 AQTVVPPIPgitTTPGVY-------DSTGLLNLKELPG-HLGILGGGYIGVEFASMFANFGSKVTILEAASLFLPREDRD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 190 AVGAFALALHARhGVDVRLGALPERIrRAANGAAVVETSAGGIVADVVVAGIGVVPNVE--LAQAAGLDVDD--GVCVDE 265
Cdd:PRK08010 201 IADNIATILRDQ-GVDIILNAHVERI-SHHENQVQVHSEHAQLAVDALLIASGRQPATAslHPENAGIAVNErgAIVVDK 278
|
250
....*....|....*.
gi 516493774 266 MCRTADPAIFAAGEVT 281
Cdd:PRK08010 279 YLHTTADNIWAMGDVT 294
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
101-281 |
7.08e-09 |
|
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: 57.68 E-value: 7.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 101 RLGYARLLIATGSRVRRFAGPVDAgvhvhyvRTLADTRALRAALAPgKRVAVLGGGFIGLEVAASAVRLGCRATVVDPAP 180
Cdd:TIGR01423 149 RLQAEHILLATGSWPQMLGIPGIE-------HCISSNEAFYLDEPP-RRVLTVGGGFISVEFAGIFNAYKPRGGKVTLCY 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 181 R--LLQRGMPEAVGAFALALHARHGVDVRLGALPERIRRAANGAAVVETSAGGIV-ADVVVAGIGVVPNVELAQ--AAGL 255
Cdd:TIGR01423 221 RnnMILRGFDSTLRKELTKQLRANGINIMTNENPAKVTLNADGSKHVTFESGKTLdVDVVMMAIGRVPRTQTLQldKVGV 300
|
170 180
....*....|....*....|....*...
gi 516493774 256 DVDD--GVCVDEMCRTADPAIFAAGEVT 281
Cdd:TIGR01423 301 ELTKkgAIQVDEFSRTNVPNIYAIGDVT 328
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
94-281 |
1.03e-08 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 57.08 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 94 VRLSDGA--RLGYARLLIATGsrvrrfAGPVdagvhVHYVRTLADT------RALRAALAPgKRVAVLGGGFIGLEVAAS 165
Cdd:PRK13748 221 VRLNDGGerVVAFDRCLIATG------ASPA-----VPPIPGLKETpywtstEALVSDTIP-ERLAVIGSSVVALELAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 166 AVRLGCRATVVdPAPRLLQRGMPeAVGAFALALHARHGVDVRLGALPERIRRaANGAAVVETSAGGIVADVVVAGIGVVP 245
Cdd:PRK13748 289 FARLGSKVTIL-ARSTLFFREDP-AIGEAVTAAFRAEGIEVLEHTQASQVAH-VDGEFVLTTGHGELRADKLLVATGRAP 365
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 516493774 246 NV-ELA-QAAGLDVDDG--VCVDEMCRTADPAIFAAGEVT 281
Cdd:PRK13748 366 NTrSLAlDAAGVTVNAQgaIVIDQGMRTSVPHIYAAGDCT 405
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
104-293 |
4.74e-08 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 54.61 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 104 YARLLIATG---SRVRRFAGPVDAGVH--VHYvrtLADTRALRAALAP--------GKRVAVLGGGFIGLEVAASAVRLG 170
Cdd:PRK12770 119 YDAVLIATGtwkSRKLGIPGEDLPGVYsaLEY---LFRIRAAKLGYLPwekvppveGKKVVVVGAGLTAVDAALEAVLLG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 171 CRATVV------DPAP-------RLLQRG-------MPEAVgafaLALHARHGV---DVRLGALPERIRRAangAAVVET 227
Cdd:PRK12770 196 AEKVYLayrrtiNEAPagkyeieRLIARGveflelvTPVRI----IGEGRVEGVelaKMRLGEPDESGRPR---PVPIPG 268
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516493774 228 SAGGIVADVVVAGIGVVPNVELAQAA---GLDVDDGVCVDEMCRTADPAIFAAGEVTrHFNPLVGRALR 293
Cdd:PRK12770 269 SEFVLEADTVVFAIGEIPTPPFAKEClgiELNRKGEIVVDEKHMTSREGVFAAGDVV-TGPSKIGKAIK 336
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
104-302 |
1.34e-07 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 53.25 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 104 YARLLIATGSRVRRFAGPVDagvHVHYVRTLADTRALRAALA--PGKRVAVLGGGFIGLEVAASAVRLGCRATVV---DP 178
Cdd:PRK13512 106 YDKLILSPGASANSLGFESD---ITFTLRNLEDTDAIDQFIKanQVDKALVVGAGYISLEVLENLYERGLHPTLIhrsDK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 179 APRLLQRGMPEAVgafaLALHARHGVDVRLGalpERIRRaANGAAVVETSAGGIVADVVVAGIGVVPNVELAQAAGLDVD 258
Cdd:PRK13512 183 INKLMDADMNQPI----LDELDKREIPYRLN---EEIDA-INGNEVTFKSGKVEHYDMIIEGVGTHPNSKFIESSNIKLD 254
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 516493774 259 DG--VCVDEMCRTADPAIFAAGEVT----RHFN-----PLVGRALRIESwQIAEN 302
Cdd:PRK13512 255 DKgfIPVNDKFETNVPNIYAIGDIItshyRHVDlpasvPLAWGAHRAAS-IVAEQ 308
|
|
| Tdh |
COG1063 |
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ... |
139-228 |
1.37e-07 |
|
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440683 [Multi-domain] Cd Length: 341 Bit Score: 52.83 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 139 ALRAALAPGKRVAVLGGGFIGLEVAASAVRLGC-RATVVDPAP-RLlqrgmpeavgAFALALHARHGVDVRLGALPERIR 216
Cdd:COG1063 154 VERAGVKPGDTVLVIGAGPIGLLAALAARLAGAaRVIVVDRNPeRL----------ELARELGADAVVNPREEDLVEAVR 223
|
90
....*....|....*
gi 516493774 217 RAANGA---AVVETS 228
Cdd:COG1063 224 ELTGGRgadVVIEAV 238
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
72-282 |
3.23e-07 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 52.10 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 72 RERDIELRLGVRVEAIERGARRVRLSDgARLGYARLLIATG-SRVRRFAGPVDAGVHVHY-VRTLADTRALRAA--LAPG 147
Cdd:PRK11749 195 REVERLLKLGVEIRTNTEVGRDITLDE-LRAGYDAVFIGTGaGLPRFLGIPGENLGGVYSaVDFLTRVNQAVADydLPVG 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 148 KRVAVLGGGFIGLEVAASAVRLGCR-ATVVdpaprlLQRG---MPEAVGAFALAlhARHGVDVRLGALPERIRRAANGAA 223
Cdd:PRK11749 274 KRVVVIGGGNTAMDAARTAKRLGAEsVTIV------YRRGreeMPASEEEVEHA--KEEGVEFEWLAAPVEILGDEGRVT 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 224 --------------------VVETSAGGIVADVVVAGIGVVPN---VELAQAAGLDVDDGVCVDEM-CRTADPAIFAAGE 279
Cdd:PRK11749 346 gvefvrmelgepdasgrrrvPIEGSEFTLPADLVIKAIGQTPNpliLSTTPGLELNRWGTIIADDEtGRTSLPGVFAGGD 425
|
...
gi 516493774 280 VTR 282
Cdd:PRK11749 426 IVT 428
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
72-281 |
1.42e-06 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 50.16 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 72 RERDIELRLGVRVEAIERGAR--RVRLSDGARLGYARLLIATGSRVRRFAGPVDA-----GVhvhyvrtladtralraAL 144
Cdd:PRK15317 277 KEYDVDIMNLQRASKLEPAAGliEVELANGAVLKAKTVILATGARWRNMNVPGEDeyrnkGV----------------AY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 145 AP--------GKRVAVLGGGFIGLEVA---ASAVRlgcRATVVDPAPRL-----LQRgmpeavgafalALHARHGVDVRL 208
Cdd:PRK15317 341 CPhcdgplfkGKRVAVIGGGNSGVEAAidlAGIVK---HVTVLEFAPELkadqvLQD-----------KLRSLPNVTIIT 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 209 GALPERIRraANGAAVV----ETSAGGIVADVVVAG----IGVVPNVE-LAQAAGLDVDDGVCVDEMCRTADPAIFAAGE 279
Cdd:PRK15317 407 NAQTTEVT--GDGDKVTgltyKDRTTGEEHHLELEGvfvqIGLVPNTEwLKGTVELNRRGEIIVDARGATSVPGVFAAGD 484
|
..
gi 516493774 280 VT 281
Cdd:PRK15317 485 CT 486
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
148-285 |
2.88e-06 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 49.49 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 148 KRVAVLGGGFIGLEVAASAVRLGCRATVVDPAPRLLqRGMPEAVGAFALALHARHGVDVRLGALPERIRRAANGAAVVET 227
Cdd:PLN02546 253 EKIAIVGGGYIALEFAGIFNGLKSDVHVFIRQKKVL-RGFDEEVRDFVAEQMSLRGIEFHTEESPQAIIKSADGSLSLKT 331
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516493774 228 SAGGI--VADVVVAgIGVVPNVE-LA-QAAGLDVDD--GVCVDEMCRTADPAIFAAGEVTRHFN 285
Cdd:PLN02546 332 NKGTVegFSHVMFA-TGRKPNTKnLGlEEVGVKMDKngAIEVDEYSRTSVPSIWAVGDVTDRIN 394
|
|
| Zn_ADH7 |
cd08261 |
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ... |
141-221 |
5.55e-06 |
|
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.
Pssm-ID: 176222 [Multi-domain] Cd Length: 337 Bit Score: 47.95 E-value: 5.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 141 RAALAPGKRVAVLGGGFIGLEVAASAVRLGCRATVVDPAPRLLqrgmpeavgAFALALHARHGVDVRLGALPERIRRAAN 220
Cdd:cd08261 154 RAGVTAGDTVLVVGAGPIGLGVIQVAKARGARVIVVDIDDERL---------EFARELGADDTINVGDEDVAARLRELTD 224
|
.
gi 516493774 221 G 221
Cdd:cd08261 225 G 225
|
|
| MDR |
cd05188 |
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
138-253 |
6.15e-06 |
|
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.
Pssm-ID: 176178 [Multi-domain] Cd Length: 271 Bit Score: 47.32 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 138 RALR--AALAPGKRVAVLGGGFIGLEVAASAVRLGCRATVVDPAPRLLqrgmpeavgAFALALHARHGVDVRLGALPERI 215
Cdd:cd05188 124 HALRraGVLKPGDTVLVLGAGGVGLLAAQLAKAAGARVIVTDRSDEKL---------ELAKELGADHVIDYKEEDLEEEL 194
|
90 100 110
....*....|....*....|....*....|....*...
gi 516493774 216 RRaangaavvetsAGGIVADVVVAGIGVVPNVELAQAA 253
Cdd:cd05188 195 RL-----------TGGGGADVVIDAVGGPETLAQALRL 221
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
106-280 |
8.14e-06 |
|
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: 47.92 E-value: 8.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 106 RLLIATGSRVRRFAGPVDAgvhvHYVRTLADTRALraALAPGKRVaVLGGGFIGLEVAASAVRLGCRATVVdpAPRLLQR 185
Cdd:TIGR01438 146 RFLIATGERPRYPGIPGAK----ELCITSDDLFSL--PYCPGKTL-VVGASYVALECAGFLAGIGLDVTVM--VRSILLR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 186 GMPEAVGAFALALHARHGVDVRLGALPERIRRAanGAAVVETSAG---GIVA--DVVVAGIGVVPNVELA--QAAGLDVD 258
Cdd:TIGR01438 217 GFDQDCANKVGEHMEEHGVKFKRQFVPIKVEQI--EAKVLVEFTDstnGIEEeyDTVLLAIGRDACTRKLnlENVGVKIN 294
|
170 180
....*....|....*....|....*
gi 516493774 259 DG---VCVDEMCRTADPAIFAAGEV 280
Cdd:TIGR01438 295 KKtgkIPADEEEQTNVPYIYAVGDI 319
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
33-278 |
1.40e-05 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 46.45 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 33 VMIGAEPELPYDRPVLSKEalvggdagerrafvrDAAWYRER-----DIELRLGVRVEAIERGAR--RVRLSDG---ARl 102
Cdd:pfam13738 57 ISPGTSPAFTFNREHPSGN---------------EYAEYLRRvadhfELPINLFEEVTSVKKEDDgfVVTTSKGtyqAR- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 103 gyaRLLIATGSRVR-RFAGPVDAGVHVHYVRTLADTRalraalapGKRVAVLGGGFIGLEVAASAVRLGCRATVVDP--- 178
Cdd:pfam13738 121 ---YVIIATGEFDFpNKLGVPELPKHYSYVKDFHPYA--------GQKVVVIGGYNSAVDAALELVRKGARVTVLYRgse 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 179 ------------APRLLQRgMPEAVGAFALALHARHGVdvrlgalpERIRRaANGAAVVETSAGG--IVADVVVAGIGVV 244
Cdd:pfam13738 190 wedrdsdpsyslSPDTLNR-LEELVKNGKIKAHFNAEV--------KEITE-VDVSYKVHTEDGRkvTSNDDPILATGYH 259
|
250 260 270
....*....|....*....|....*....|....*..
gi 516493774 245 PNVELAQAAGLDVDDG---VCVDEMCRTADPAIFAAG 278
Cdd:pfam13738 260 PDLSFLKKGLFELDEDgrpVLTEETESTNVPGLFLAG 296
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
148-279 |
1.56e-05 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 46.92 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 148 KRVAVLGGGFIGLEVAASAVRLGCRATVVDPAPRLLqRGMPEAVGAFALALHARHGVDVRLGALPERIRRAANGAAVVET 227
Cdd:PTZ00058 238 KRIGIAGSGYIAVELINVVNRLGAESYIFARGNRLL-RKFDETIINELENDMKKNNINIITHANVEEIEKVKEKNLTIYL 316
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 516493774 228 SAGG--IVADVVVAGIGVVPNVELAQAAGLDV---DDGVCVDEMCRTADPAIFAAGE 279
Cdd:PTZ00058 317 SDGRkyEHFDYVIYCVGRSPNTEDLNLKALNIktpKGYIKVDDNQRTSVKHIYAVGD 373
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
104-282 |
2.16e-05 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 46.31 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 104 YARLLIATGSRVRRfAGPVD----AGVH------VHYVRTLADTRALRAALAPGKRVAVLGGGFIGLEVAASAVRLGCRA 173
Cdd:PRK12810 229 YDAVFLGTGAYKPR-DLGIPgrdlDGVHfamdflIQNTRRVLGDETEPFISAKGKHVVVIGGGDTGMDCVGTAIRQGAKS 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 174 -TVVDPAPRL-LQRGMPEAVGAFALAL---HAR-HGVDVRLGALPERIrRAANGAA----VVETSAGG------------ 231
Cdd:PRK12810 308 vTQRDIMPMPpSRRNKNNPWPYWPMKLevsNAHeEGVEREFNVQTKEF-EGENGKVtgvkVVRTELGEgdfepvegsefv 386
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 516493774 232 IVADVVVAGIGVVPNVE-LAQAAGLDVDDG---VCVDEMCRTADPAIFAAGEVTR 282
Cdd:PRK12810 387 LPADLVLLAMGFTGPEAgLLAQFGVELDERgrvAAPDNAYQTSNPKVFAAGDMRR 441
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
147-282 |
1.62e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 43.85 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 147 GKRVAVLGGGFIGLEVAASAVRLGCRATVVdpaPRLLQRGMP---EAVGafalalHARH-GVDVRLGALPERIRRAANG- 221
Cdd:PRK12831 281 GKKVAVVGGGNVAMDAARTALRLGAEVHIV---YRRSEEELParvEEVH------HAKEeGVIFDLLTNPVEILGDENGw 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 222 ---------------------AAVVETSAGGIVADVVVAGIGVVPN-VELAQAAGLDVDDGVCV---DEMCRTADPAIFA 276
Cdd:PRK12831 352 vkgmkcikmelgepdasgrrrPVEIEGSEFVLEVDTVIMSLGTSPNpLISSTTKGLKINKRGCIvadEETGLTSKEGVFA 431
|
....*.
gi 516493774 277 AGEVTR 282
Cdd:PRK12831 432 GGDAVT 437
|
|
| 2-desacetyl-2-hydroxyethyl_bacteriochlorophyllide_ |
cd08255 |
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup ... |
140-231 |
1.82e-04 |
|
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide and other MDR family members; This subgroup of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family has members identified as 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase and alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.
Pssm-ID: 176217 [Multi-domain] Cd Length: 277 Bit Score: 43.03 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 140 LRAALAPGKRVAVLGGGFIGLEVAASAVRLGCRA-TVVDPAPRLLQR----GMPEAVGAFALALHARHGVDV------RL 208
Cdd:cd08255 91 RDAEPRLGERVAVVGLGLVGLLAAQLAKAAGAREvVGVDPDAARRELaealGPADPVAADTADEIGGRGADVvieasgSP 170
|
90 100
....*....|....*....|...
gi 516493774 209 GALPERIRRAANGAAVVETSAGG 231
Cdd:cd08255 171 SALETALRLLRDRGRVVLVGWYG 193
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
148-246 |
3.92e-04 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 42.43 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 148 KRVAVLGGGFIGLEVA---ASAVRLGCRATVVDPAPRLLQRGM-PE-AVG-------AFALALHAR-HGVDVRLGALpER 214
Cdd:COG1252 2 KRIVIVGGGFAGLEAArrlRKKLGGDAEVTLIDPNPYHLFQPLlPEvAAGtlspddiAIPLRELLRrAGVRFIQGEV-TG 80
|
90 100 110
....*....|....*....|....*....|...
gi 516493774 215 IRRAANgaaVVETSAGGIVA-DVVVAGIGVVPN 246
Cdd:COG1252 81 IDPEAR---TVTLADGRTLSyDYLVIATGSVTN 110
|
|
| Zn_ADH6 |
cd08260 |
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ... |
138-232 |
4.22e-04 |
|
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group has the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.
Pssm-ID: 176221 [Multi-domain] Cd Length: 345 Bit Score: 42.20 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 138 RAL--RAALAPGKRVAVLGGGFIGLEVAASAVRLGCRATVVDPAPRLLQRGmpEAVGAFAlALHARHGVDVrlgalPERI 215
Cdd:cd08260 155 RALvhQARVKPGEWVAVHGCGGVGLSAVMIASALGARVIAVDIDDDKLELA--RELGAVA-TVNASEVEDV-----AAAV 226
|
90
....*....|....*..
gi 516493774 216 RRAANGAAVVETSAGGI 232
Cdd:cd08260 227 RDLTGGGAHVSVDALGI 243
|
|
| FadB |
COG1250 |
3-hydroxyacyl-CoA dehydrogenase [Lipid transport and metabolism]; 3-hydroxyacyl-CoA ... |
148-238 |
4.83e-04 |
|
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: 41.63 E-value: 4.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 148 KRVAVLGGGFIGLEVAASAVRLGCRATVVDPAPRLLQRGMPEAVGAFALALHARHGVDVRLGALPERIRRAANGAAVVEt 227
Cdd:COG1250 3 KKVAVIGAGTMGAGIAAVFANAGYEVVLLDISPEALERARARIAKLLDKLVKKGKLTEEEADAALARITPTTDLAALAD- 81
|
90
....*....|.
gi 516493774 228 saggivADVVV 238
Cdd:COG1250 82 ------ADLVI 86
|
|
| benzyl_alcohol_DH |
cd08278 |
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol ... |
146-242 |
5.39e-04 |
|
Benzyl alcohol dehydrogenase; Benzyl alcohol dehydrogenase is similar to liver alcohol dehydrogenase, but has some amino acid substitutions near the active site, which may determine the enzyme's specificity of oxidizing aromatic substrates. Also known as aryl-alcohol dehydrogenases, they catalyze the conversion of an aromatic alcohol + NAD+ to an aromatic aldehyde + NADH + H+. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.
Pssm-ID: 176239 [Multi-domain] Cd Length: 365 Bit Score: 41.72 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 146 PGKRVAVLGGGFIGLEVAASAVRLGCRATV-VDPAPRLLqrgmpeavgAFALALHARHGVDVRLGALPERIRRAANGAA- 223
Cdd:cd08278 186 PGSSIAVFGAGAVGLAAVMAAKIAGCTTIIaVDIVDSRL---------ELAKELGATHVINPKEEDLVAAIREITGGGVd 256
|
90 100
....*....|....*....|
gi 516493774 224 -VVETSAggiVADVVVAGIG 242
Cdd:cd08278 257 yALDTTG---VPAVIEQAVD 273
|
|
| AdhP |
COG1064 |
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ... |
138-228 |
8.27e-04 |
|
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism];
Pssm-ID: 440684 [Multi-domain] Cd Length: 332 Bit Score: 41.25 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 138 RALRAA-LAPGKRVAVLGGGFIGLEVAASAVRLGCRATVVDPAPRLLqrgmpeavgAFALALHARHGVDVRLGALPERIR 216
Cdd:COG1064 153 RALRRAgVGPGDRVAVIGAGGLGHLAVQIAKALGAEVIAVDRSPEKL---------ELARELGADHVVNSSDEDPVEAVR 223
|
90
....*....|..
gi 516493774 217 RAANGAAVVETS 228
Cdd:COG1064 224 ELTGADVVIDTV 235
|
|
| sugar_DH |
cd08236 |
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ... |
124-250 |
1.11e-03 |
|
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR), which includes zinc-dependent alcohol dehydrogenase and related proteins. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Related proteins include threonine dehydrogenase, formaldehyde dehydrogenase, and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex.
Pssm-ID: 176198 [Multi-domain] Cd Length: 343 Bit Score: 40.67 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 124 AGVHVHYVRtladtralRAALAPGKRVAVLGGGFIGLEVAASAVRLGC-RATVVDPAPRLLqrgmpeavgAFALALHARH 202
Cdd:cd08236 145 AAVALHAVR--------LAGITLGDTVVVIGAGTIGLLAIQWLKILGAkRVIAVDIDDEKL---------AVARELGADD 207
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 516493774 203 GVDVRLGALpERIRRAANGAAvvetsaggivADVVVAGIGVVPNVELA 250
Cdd:cd08236 208 TINPKEEDV-EKVRELTEGRG----------ADLVIEAAGSPATIEQA 244
|
|
| sorbitol_DH |
cd05285 |
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the ... |
141-238 |
2.04e-03 |
|
Sorbitol dehydrogenase; Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. Aldose reductase catalyzes the NADP(H)-dependent conversion of glucose to sorbital, and SDH uses NAD(H) in the conversion of sorbitol to fructose. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.
Pssm-ID: 176188 [Multi-domain] Cd Length: 343 Bit Score: 39.78 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 141 RAALAPGKRVAVLGGGFIGLEVAASAVRLGC-RATVVDPAPRLLQrgmpeavgaFALALHARHGVDVRLGALPERirraa 219
Cdd:cd05285 157 RAGVRPGDTVLVFGAGPIGLLTAAVAKAFGAtKVVVTDIDPSRLE---------FAKELGATHTVNVRTEDTPES----- 222
|
90
....*....|....*....
gi 516493774 220 ngAAVVETSAGGIVADVVV 238
Cdd:cd05285 223 --AEKIAELLGGKGPDVVI 239
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
147-280 |
5.10e-03 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 39.09 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 147 GKRVAVLGGGFIGLEVAASAVRLGC-RATVVDPAPRllqRGMP----EAVGAFalalhaRHGVDVRLGALPERIRRAANG 221
Cdd:PRK12771 267 GKRVVVIGGGNTAMDAARTARRLGAeEVTIVYRRTR---EDMPahdeEIEEAL------REGVEINWLRTPVEIEGDENG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516493774 222 AAVV--------ETSAGG-----------IVADVVVAGIGvvPNVELA---QAAGLDVDDG-VCVDEMCR-TADPAIFAA 277
Cdd:PRK12771 338 ATGLrvitvekmELDEDGrpspvtgeeetLEADLVVLAIG--QDIDSAgleSVPGVEVGRGvVQVDPNFMmTGRPGVFAG 415
|
...
gi 516493774 278 GEV 280
Cdd:PRK12771 416 GDM 418
|
|
| |
