|
Name |
Accession |
Description |
Interval |
E-value |
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
247-523 |
3.14e-117 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 349.03 E-value: 3.14e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 247 DLAIIGGGPAGMSAGIYAKRSGLSCIILEKQGVGGQVALTPKVENYPGFTN-IQGFELVEILGSHAREY-TDIQqFAEVK 324
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATTKEIENYPGFPEgISGPELAERLREQAERFgAEIL-LEEVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 325 DVKY-GPRIEITTDE-KNYRAKGVLLATGVNVRMLGVPGEDKFYGHGVSYCATCDGNFYKGGKAVIVGGGNTALTDALHL 402
Cdd:COG0492 81 SVDKdDGPFRVTTDDgTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 403 KHLGIETTIVHRGDKFRAEKVLQDSV-NREGINIIWNSQVTEIIGEDQVESARIVN-KDGTETILDTDVVFVAIGHTANT 480
Cdd:COG0492 161 TKFASKVTLIHRRDELRASKILVERLrANPKIEVLWNTEVTEIEGDGRVEGVTLKNvKTGEEKELEVDGVFVAIGLKPNT 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 242124088 481 ELAEKLGCELRPDGFIKVDPTQRTSVERVYAAGDVTGG-VRQII 523
Cdd:COG0492 241 ELLKGLGLELDEDGYIVVDEDMETSVPGVFAAGDVRDYkYRQAA 284
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
247-523 |
8.22e-100 |
|
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070). [Energy metabolism, Electron transport]
Pssm-ID: 273540 [Multi-domain] Cd Length: 299 Bit Score: 304.16 E-value: 8.22e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 247 DLAIIGGGPAGMSAGIYAKRSGLSCIILEKQGVGGQVALTPKVENYPGFTN-IQGFELVEILGSHAREYTDIQQFAEVKD 325
Cdd:TIGR01292 1 DVIIIGAGPAGLTAAIYAARANLKPLLIEGMEPGGQLTTTTEVENYPGFPEgISGPELMEKMKEQAVKFGAEIIYEEVIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 326 VKYG--PRIEITTDEKNYRAKGVLLATGVNVRMLGVPGEDKFYGHGVSYCATCDGNFYKGGKAVIVGGGNTALTDALHLK 403
Cdd:TIGR01292 81 VDKSdrPFKVYTGDGKEYTAKAVIIATGASARKLGIPGEDEFWGRGVSYCATCDGPFFKNKEVAVVGGGDSAIEEALYLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 404 HLGIETTIVHRGDKFRAEKVLQDSV-NREGINIIWNSQVTEIIGEDQVESARIVN-KDGTETILDTDVVFVAIGHTANTE 481
Cdd:TIGR01292 161 RIAKKVTLVHRRDKFRAEKILLDRLkKNPKIEFLWNSTVEEIVGDNKVEGVKIKNtVTGEEEELEVDGVFIAIGHEPNTE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 242124088 482 LAEKLgCELRPDGFIKVDPTQRTSVERVYAAGDVTG-GVRQII 523
Cdd:TIGR01292 241 LLKGL-LELDENGYIVTDEGMRTSVPGVFAAGDVRDkGYRQAV 282
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
19-542 |
7.23e-60 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 206.55 E-value: 7.23e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 19 REYLEKLfaefKRTVTIEVYTAEGEH-REYNDFTLNICrafnVISDKIELREyavdsemgkNRNIIATPTVLISPDEYD- 96
Cdd:PRK15317 11 KQYLELL----ERPIELVASLDDSEKsAELKELLEEIA----SLSDKITVEE---------DSLDVRKPSFSITRPGEDt 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 97 -IRFLGAPAGEEGRALVEALNLASKGADGISESTKEILEPLEEDRLVKIFASPTCPYCPG--QAINAFkaAVARPdKISA 173
Cdd:PRK15317 74 gVRFAGIPMGHEFTSLVLALLQVGGHPPKLDQEVIEQIKALDGDFHFETYVSLSCHNCPDvvQALNLM--AVLNP-NITH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 174 WNISTLDNENMAHEYKVGSVPhtdindTVTFTGlepeEKF----MlqllflkPLEEVVE------EQRAAKAETTEDtVY 243
Cdd:PRK15317 151 TMIDGALFQDEVEARNIMAVP------TVFLNG----EEFgqgrM-------TLEEILAkldtgaAARAAEELNAKD-PY 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 244 edvDLAIIGGGPAGMSAGIYAKRSGLSC-IILEKqgVGGQVALTPKVENYPGFTNIQGFELVEILGSHAREYT-DI---Q 318
Cdd:PRK15317 213 ---DVLVVGGGPAGAAAAIYAARKGIRTgIVAER--FGGQVLDTMGIENFISVPETEGPKLAAALEEHVKEYDvDImnlQ 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 319 QFAEVKDVKYGPRIEITTDEKnYRAKGVLLATGVNVRMLGVPGEDKFYGHGVSYCATCDGNFYKGGKAVIVGGGNTALTD 398
Cdd:PRK15317 288 RASKLEPAAGLIEVELANGAV-LKAKTVILATGARWRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEA 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 399 ALHL----KHLgietTIVHRGDKFRAEKVLQDSVN-REGINIIWNSQVTEIIGE-DQVESarIVNKD---GTETILDTDV 469
Cdd:PRK15317 367 AIDLagivKHV----TVLEFAPELKADQVLQDKLRsLPNVTIITNAQTTEVTGDgDKVTG--LTYKDrttGEEHHLELEG 440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 242124088 470 VFVAIGHTANTELAEKLgCELRPDGFIKVDPTQRTSVERVYAAGDVTGGV-RQIITATGQGAAAALTAFDDFTR 542
Cdd:PRK15317 441 VFVQIGLVPNTEWLKGT-VELNRRGEIIVDARGATSVPGVFAAGDCTTVPyKQIIIAMGEGAKAALSAFDYLIR 513
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
247-519 |
1.73e-56 |
|
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: 191.38 E-value: 1.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 247 DLAIIGGGPAGMSAGIYAKRSGLS--CIILEKQGVGGQVALTPKVENYPGFTNI--QGFELVEILGSHAREYT-DIQQFA 321
Cdd:pfam07992 2 DVVVIGGGPAGLAAALTLAQLGGKvtLIEDEGTCPYGGCVLSKALLGAAEAPEIasLWADLYKRKEEVVKKLNnGIEVLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 322 --EVKDVKYGPRI-----EITTDEKNYRAKGVLLATGVNVRMLGVPGEDKFYGHGVSYCATCDGNFYK--GGKAVIVGGG 392
Cdd:pfam07992 82 gtEVVSIDPGAKKvvleeLVDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKllPKRVVVVGGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 393 NTALTDALHLKHLGIETTIVHRGDKF------RAEKVLQDSVNREGINIIWNSQVTEIIGEDQVesarIVNKDGTETILD 466
Cdd:pfam07992 162 YIGVELAAALAKLGKEVTLIEALDRLlrafdeEISAALEKALEKNGVEVRLGTSVKEIIGDGDG----VEVILKDGTEID 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 242124088 467 TDVVFVAIGHTANTELAEKLGCELRPDGFIKVDPTQRTSVERVYAAGDVTGGV 519
Cdd:pfam07992 238 ADLVVVAIGRRPNTELLEAAGLELDERGGIVVDEYLRTSVPGIYAAGDCRVGG 290
|
|
| AhpF_homolog |
TIGR03143 |
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase ... |
247-523 |
2.31e-56 |
|
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase homologs is found adjacent to alkylhydroperoxide reductase C subunit predominantly in cases where there is only one C subunit in the genome and that genome is lacking the F subunit partner (also a thioredcxin reductase homolog) that is usually found (TIGR03140).
Pssm-ID: 132187 [Multi-domain] Cd Length: 555 Bit Score: 198.08 E-value: 2.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 247 DLAIIGGGPAGMSAGIYAKRSGLSCIILEKQGVGGQVALTPKVENYPGFTNIQGFELVEILGSHAREYTDIQQFAEVKDV 326
Cdd:TIGR03143 6 DLIIIGGGPAGLSAGIYAGRAKLDTLIIEKDDFGGQITITSEVVNYPGILNTTGPELMQEMRQQAQDFGVKFLQAEVLDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 327 KYGPRI-EITTDEKNYRAKGVLLATGVNVRMLGVPGEDKFYGHGVSYCATCDGNFYKGGKAVIVGGGNTALTDALHLKHL 405
Cdd:TIGR03143 86 DFDGDIkTIKTARGDYKTLAVLIATGASPRKLGFPGEEEFTGRGVAYCATCDGEFFTGMDVFVIGGGFAAAEEAVFLTRY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 406 GIETTIVHRGDKFRAEKVLQDSV-NREGINIIWNSQVTEIIGEDQVESARIVN-KDGTETILDTDV------VFVAIGHT 477
Cdd:TIGR03143 166 ASKVTVIVREPDFTCAKLIAEKVkNHPKIEVKFNTELKEATGDDGLRYAKFVNnVTGEITEYKAPKdagtfgVFVFVGYA 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 242124088 478 ANTELAEKLgCELRPDGFIKVDPTQRTSVERVYAAGDV-TGGVRQII 523
Cdd:TIGR03143 246 PSSELFKGV-VELDKRGYIPTNEDMETNVPGVYAAGDLrPKELRQVV 291
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
248-523 |
2.30e-47 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 167.93 E-value: 2.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 248 LAIIGGGPAGMSAGIYAKRSGLSCIILEKQGVGGQVALTPKVENYPGFTN-IQGFELVEILGSHAREYTDIQQFAEVKDV 326
Cdd:PRK10262 9 LLILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNdLTGPLLMERMHEHATKFETEIIFDHINKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 327 KYGPR-IEITTDEKNYRAKGVLLATGVNVRMLGVPGEDKFYGHGVSYCATCDGNFYKGGKAVIVGGGNTALTDALHLKHL 405
Cdd:PRK10262 89 DLQNRpFRLTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 406 GIETTIVHRGDKFRAEKV----LQDSVNREGINIIWNSQVTEIIGEDQ-VESARIVNKDGTETILDTDV--VFVAIGHTA 478
Cdd:PRK10262 169 ASEVHLIHRRDGFRAEKIlikrLMDKVENGNIILHTNRTLEEVTGDQMgVTGVRLRDTQNSDNIESLDVagLFVAIGHSP 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 242124088 479 NTELAE-KLGCElrpDGFIKVDP-----TQRTSVERVYAAGDVTGGV-RQII 523
Cdd:PRK10262 249 NTAIFEgQLELE---NGYIKVQSgihgnATQTSIPGVFAAGDVMDHIyRQAI 297
|
|
| GlrX_arch |
TIGR02187 |
Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal ... |
14-214 |
1.04e-36 |
|
Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal domain with homology to bacterial and eukaryotic glutaredoxins, including a CPYC motif. There is an N-terminal domain which has even more distant homology to glutaredoxins. The name "glutaredoxin" may be inappropriate in the sense of working in tandem with glutathione and glutathione reductase which may not be present in the archaea. The overall domain structure appears to be related to bacterial alkylhydroperoxide reductases, but the homology may be distant enough that the function of this family is wholly different.
Pssm-ID: 274021 [Multi-domain] Cd Length: 215 Bit Score: 135.65 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 14 IPEESREYLEKLF-AEFKRTVTIEVYTAEG-EHREYNDFTLNICRAFNVISDKIELREYAVDSEMGKNR----NIIATPT 87
Cdd:TIGR02187 1 LSEEDREILKELFlKELKNPVEIVVFTDNDkEGCQYCKETEQLLEELSEVSPKLKLEIYDFDTPEDKEEaekyGVERVPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 88 VLISPD--EYDIRFLGAPAGEEGRALVEALNLASKGADGISESTKEILEPLEEDRLVKIFASPTCPYCPGQAINAFKAAV 165
Cdd:TIGR02187 81 TIILEEgkDGGIRYTGIPAGYEFAALIEDIVRVSQGEPGLSEKTVELLQSLDEPVRIEVFVTPTCPYCPYAVLMAHKFAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 242124088 166 ARPdKISAWNISTLDNENMAHEYKVGSVPHTDIN-DTVTFTGLEPEEKFM 214
Cdd:TIGR02187 161 AND-KILGEMIEANENPDLAEKYGVMSVPKIVINkGVEEFVGAYPEEQFL 209
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
347-517 |
1.11e-33 |
|
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: 130.32 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 347 LLATGVNVRMLGVPGEDkfyGHGVSYCATCDG--------NFYKGGKAVIVGGGNTALTDALHLKHLGIETTIVHRGD-- 416
Cdd:COG0446 83 VLATGARPRPPPIPGLD---LPGVFTLRTLDDadalrealKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPrl 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 417 --KFRAE--KVLQDSVNREGINIIWNSQVTEIIGEDQVesaRIVNKDGTEtiLDTDVVFVAIGHTANTELAEKLGCELRP 492
Cdd:COG0446 160 lgVLDPEmaALLEEELREHGVELRLGETVVAIDGDDKV---AVTLTDGEE--IPADLVVVAPGVRPNTELAKDAGLALGE 234
|
170 180
....*....|....*....|....*
gi 242124088 493 DGFIKVDPTQRTSVERVYAAGDVTG 517
Cdd:COG0446 235 RGWIKVDETLQTSDPDVYAAGDCAE 259
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
244-518 |
1.40e-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: 130.21 E-value: 1.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 244 EDVDLAIIGGGPAGMSAGIYAKRSGLSCIILEKQGVGG---QVALTPK------VENYPGFTNIQGF----ELVEI---- 306
Cdd:COG1249 2 KDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGtclNVGCIPSkallhaAEVAHEARHAAEFgisaGAPSVdwaa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 307 LGSHAREYTD-----------------IQQFAEVKDVKygpRIEITTDEKnYRAKGVLLATGVNVRMLGVPGEDKFYGHg 369
Cdd:COG1249 82 LMARKDKVVDrlrggveellkkngvdvIRGRARFVDPH---TVEVTGGET-LTADHIVIATGSRPRVPPIPGLDEVRVL- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 370 vsycaTCDGNF---YKGGKAVIVGGGNTALTDALHLKHLGIETTIVHRGDKF-RAE-----KVLQDSVNREGINIIWNSQ 440
Cdd:COG1249 157 -----TSDEALeleELPKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLlPGEdpeisEALEKALEKEGIDILTGAK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 441 VTEI-IGEDQVEsARIVNKDGTETIlDTDVVFVAIGHTANTEL--AEKLGCELRPDGFIKVDPTQRTSVERVYAAGDVTG 517
Cdd:COG1249 232 VTSVeKTGDGVT-VTLEDGGGEEAV-EADKVLVATGRRPNTDGlgLEAAGVELDERGGIKVDEYLRTSVPGIYAIGDVTG 309
|
.
gi 242124088 518 G 518
Cdd:COG1249 310 G 310
|
|
| AhpF |
COG3634 |
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms]; |
12-218 |
1.39e-30 |
|
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];
Pssm-ID: 442851 [Multi-domain] Cd Length: 200 Bit Score: 118.31 E-value: 1.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 12 NFIPEESREYLEKLFAEFKRTVTIEVYTaegEHREYNDFTLNICRAFNVISDKIELREYAVDsemgknrNIIATPTVLIS 91
Cdd:COG3634 2 AMLDDELKAQLKEYLEKLKNPVELVLFL---DDCEKSEELRELLEEIASLSDKISLEVYDKD-------DVERAPSFAIL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 92 PDEYD--IRFLGAPAGEEGRALVEALNLASKGADGISESTKEILEPLEEDRLVKIFASPTCPYCPG--QAINAFkaAVAR 167
Cdd:COG3634 72 RDGEDtgIRFAGIPSGHEFTSLVLALLQVSGHPPKLSEETIEQIKALDGPVHFEVFVSLSCPNCPDvvQALNLM--AVLN 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 242124088 168 PdKISAWNISTLDNENMAHEYKVGSVPHTDINDTVTFTGLEPEEKFMLQLL 218
Cdd:COG3634 150 P-NITHEMIDGAEFPDEAEKYGVMSVPTVVLNGEVFFVGRMPEEEILEKLD 199
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
347-516 |
5.70e-29 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 118.71 E-value: 5.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 347 LLATGVNVRMLGVPGEDKfygHGVSYCATCD------GNFYKGGKAVIVGGGNTALTDALHLKHLGIETTIVHRGDKF-- 418
Cdd:COG1251 103 VLATGSRPRVPPIPGADL---PGVFTLRTLDdadalrAALAPGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLlp 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 419 -----RAEKVLQDSVNREGINIIWNSQVTEIIGEDQVESARIvnKDGTEtiLDTDVVFVAIGHTANTELAEklGCELRPD 493
Cdd:COG1251 180 rqldeEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTGVRL--ADGEE--LPADLVVVAIGVRPNTELAR--AAGLAVD 253
|
170 180
....*....|....*....|...
gi 242124088 494 GFIKVDPTQRTSVERVYAAGDVT 516
Cdd:COG1251 254 RGIVVDDYLRTSDPDIYAAGDCA 276
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
249-518 |
1.97e-28 |
|
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: 117.93 E-value: 1.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 249 AIIGGGPAGMSAGIYAKRSGLSCIILEKQGVGGQVaLTpkvenYpGftnIQGFELV-EILgshAREytdIQQFAE--VKd 325
Cdd:COG0493 125 AVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGGL-LR-----Y-G---IPEFRLPkDVL---DRE---IELIEAlgVE- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 326 VKYGPRI--EITTDE--KNYRAkgVLLATGV-NVRMLGVPGEDKfygHGVsYCAT-----------CDGNFYKGGKAVIV 389
Cdd:COG0493 188 FRTNVEVgkDITLDEllEEFDA--VFLATGAgKPRDLGIPGEDL---KGV-HSAMdfltavnlgeaPDTILAVGKRVVVI 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 390 GGGNTAlTDALH-LKHLGIET-TIVHRGDK----FRAEKVlqDSVNREGINIIWNSQVTEIIGED--QVES--------- 452
Cdd:COG0493 262 GGGNTA-MDCARtALRLGAESvTIVYRRTReempASKEEV--EEALEEGVEFLFLVAPVEIIGDEngRVTGlecvrmelg 338
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242124088 453 -------ARIVNKDGTETILDTDVVFVAIGHTANTE-LAEKLGCELRPDGFIKVDP-TQRTSVERVYAAGDVTGG 518
Cdd:COG0493 339 epdesgrRRPVPIEGSEFTLPADLVILAIGQTPDPSgLEEELGLELDKRGTIVVDEeTYQTSLPGVFAGGDAVRG 413
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
247-518 |
1.56e-26 |
|
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.
Pssm-ID: 273568 [Multi-domain] Cd Length: 460 Bit Score: 112.74 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 247 DLAIIGGGPAGMSAGIYAKRSGLSCIILEKQGVGGqVALtpkveNY---PGFTNIQGFELVEILGsHAREY--------T 315
Cdd:TIGR01350 3 DVIVIGGGPGGYVAAIRAAQLGLKVALVEKEYLGG-TCL-----NVgciPTKALLHSAEVYDEIK-HAKDLgievenvsV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 316 DIQQFAEVKD---------VKY-----------------GPR-IEITT--DEKNYRAKGVLLATGVNVRMLgvPGEDKFY 366
Cdd:TIGR01350 76 DWEKMQKRKNkvvkklvggVSGllkknkvtvikgeakflDPGtVSVTGenGEETLEAKNIIIATGSRPRSL--PGPFDFD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 367 GHGVsycATCDGNFY---KGGKAVIVGGGNTALTDALHLKHLGIETTIVHRGDK----FRAE--KVLQDSVNREGINIIW 437
Cdd:TIGR01350 154 GKVV---ITSTGALNleeVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRilpgEDAEvsKVLQKALKKKGVKILT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 438 NSQVTEIIGEDqvESARIVNKDGTETILDTDVVFVAIGHTANTELA--EKLGCELRPDGFIKVDPTQRTSVERVYAAGDV 515
Cdd:TIGR01350 231 NTKVTAVEKND--DQVTYENKGGETETLTGEKVLVAVGRKPNTEGLglEKLGVELDERGRIVVDEYMRTNVPGIYAIGDV 308
|
...
gi 242124088 516 TGG 518
Cdd:TIGR01350 309 IGG 311
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
249-518 |
5.02e-26 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 111.04 E-value: 5.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 249 AIIGGGPAGMSAGIYAKRSGLSCIILEKQGVGGQVaLTpkvenYpGftnIQGFELV-EILgshAREytdIQQFAE--VKd 325
Cdd:PRK11749 144 AVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGGL-LR-----Y-G---IPEFRLPkDIV---DRE---VERLLKlgVE- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 326 VKYGPRI--EITTDE--KNYRAkgVLLATGV-NVRMLGVPGEDKfygHGVSYC---------ATCDGNFYKGGKAVIVGG 391
Cdd:PRK11749 207 IRTNTEVgrDITLDElrAGYDA--VFIGTGAgLPRFLGIPGENL---GGVYSAvdfltrvnqAVADYDLPVGKRVVVIGG 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 392 GNTALTDALHLKHLGIE-TTIVHRGDK--FRAEKVLQDSVNREGINIIWNSQVTEIIGEDQVESA--------------- 453
Cdd:PRK11749 282 GNTAMDAARTAKRLGAEsVTIVYRRGReeMPASEEEVEHAKEEGVEFEWLAAPVEILGDEGRVTGvefvrmelgepdasg 361
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 242124088 454 -RIVNKDGTETILDTDVVFVAIGHTANTELAEKL-GCELRPDGFIKVDP-TQRTSVERVYAAGDVTGG 518
Cdd:PRK11749 362 rRRVPIEGSEFTLPADLVIKAIGQTPNPLILSTTpGLELNRWGTIIADDeTGRTSLPGVFAGGDIVTG 429
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
244-518 |
1.23e-24 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 106.80 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 244 EDVDLAIIGGGPAGMSAGIYAKRSGLSCIILEKQGVGG-----------------QVALTpkVENYPGF---TNIQGFEL 303
Cdd:PRK06292 2 EKYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGtclnvgcipskaliaaaEAFHE--AKHAEEFgihADGPKIDF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 304 VEIL-----------GSHAREYTD------IQQFAEVKDVKygpRIEIttDEKNYRAKGVLLATGVnvRMLGVPGEDKFY 366
Cdd:PRK06292 80 KKVMarvrrerdrfvGGVVEGLEKkpkidkIKGTARFVDPN---TVEV--NGERIEAKNIVIATGS--RVPPIPGVWLIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 367 GHGVsycATCDGNF---YKGGKAVIVGGGNTALTDALHLKHLGIETTIVHRGDKF----------RAEKVLQDSvnregI 433
Cdd:PRK06292 153 GDRL---LTSDDAFeldKLPKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRIlpledpevskQAQKILSKE-----F 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 434 NIIWNSQVTEIiGEDQVESARIVNKDGTETILDTDVVFVAIGHTANTEL--AEKLGCELRPDGFIKVDPTQRTSVERVYA 511
Cdd:PRK06292 225 KIKLGAKVTSV-EKSGDEKVEELEKGGKTETIEADYVLVATGRRPNTDGlgLENTGIELDERGRPVVDEHTQTSVPGIYA 303
|
....*..
gi 242124088 512 AGDVTGG 518
Cdd:PRK06292 304 AGDVNGK 310
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
255-513 |
6.20e-24 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 101.92 E-value: 6.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 255 PAGMSAGIYAKRSGL-SCIILEKQ-------------------------GVGGQVALTPkvENYPGFTN----IQGFELV 304
Cdd:pfam13738 1 PAGIGCAIALKKAGLeDYLILEKGnignsfyrypthmtffspsftsngfGIPDLNAISP--GTSPAFTFnrehPSGNEYA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 305 EILgshaREYTD-----IQQFAEVKDVKYGPRI-EITTDEKNYRAKGVLLATGV--NVRMLGVPGedkfygHGVSYCATC 376
Cdd:pfam13738 79 EYL----RRVADhfelpINLFEEVTSVKKEDDGfVVTTSKGTYQARYVIIATGEfdFPNKLGVPE------LPKHYSYVK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 377 DGNFYKGGKAVIVGGGNTALTDALHLKHLGIETTIVHRGDKFRAEKV-------------LQDSVNREGINIIWNSQVTE 443
Cdd:pfam13738 149 DFHPYAGQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRDSdpsyslspdtlnrLEELVKNGKIKAHFNAEVKE 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242124088 444 IigEDQVESARIVNKDGTETILDTDVVFvAIGHTANTELAEKLGCELRPDGFIKVDP-TQRTSVERVYAAG 513
Cdd:pfam13738 229 I--TEVDVSYKVHTEDGRKVTSNDDPIL-ATGYHPDLSFLKKGLFELDEDGRPVLTEeTESTNVPGLFLAG 296
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
249-523 |
2.46e-22 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 100.72 E-value: 2.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 249 AIIGGGPAGMSAGIYAKRSGLSCIILEKQ-GVGGQValtpkveNYpgftNIQGFEL-VEILGshareyTDIQQFA----E 322
Cdd:PRK12771 141 AVIGGGPAGLSAAYHLRRMGHAVTIFEAGpKLGGMM-------RY----GIPAYRLpREVLD------AEIQRILdlgvE 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 323 VK-DVKYGPRIEITTDEKNYRAkgVLLATGVNV-RMLGVPGEDKfyGH---GVSYC-ATCDGNF-YKGGKAVIVGGGNTA 395
Cdd:PRK12771 204 VRlGVRVGEDITLEQLEGEFDA--VFVAIGAQLgKRLPIPGEDA--AGvldAVDFLrAVGEGEPpFLGKRVVVIGGGNTA 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 396 LTDALHLKHLGI-ETTIVHRGDK-----FRAEKvlqDSVNREGINIIWNSQVTEIIGEDQ---------------VESAR 454
Cdd:PRK12771 280 MDAARTARRLGAeEVTIVYRRTRedmpaHDEEI---EEALREGVEINWLRTPVEIEGDENgatglrvitvekmelDEDGR 356
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 455 IVNKDGTETILDTDVVFVAIGHTANTELAEKLGCELRPDGFIKVDPTQR-TSVERVYAAGDVTGGVRQII 523
Cdd:PRK12771 357 PSPVTGEEETLEADLVVLAIGQDIDSAGLESVPGVEVGRGVVQVDPNFMmTGRPGVFAGGDMVPGPRTVT 426
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
249-522 |
8.60e-22 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 96.98 E-value: 8.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 249 AIIGGGPAGMSAGIYAKRSGLSCIILEKQ-GVGGQVALTPKVENYPGFTNIQGFELVEILG----SHAREYTDIQQFAEV 323
Cdd:PRK12770 22 AIIGAGPAGLAAAGYLACLGYEVHVYDKLpEPGGLMLFGIPEFRIPIERVREGVKELEEAGvvfhTRTKVCCGEPLHEEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 324 KDVKYGPRIEITTDEKNYRAkgVLLATGV-NVRMLGVPGEDK----------FYGHGVSYCATCDGNFY--KGGKAVIVG 390
Cdd:PRK12770 102 GDEFVERIVSLEELVKKYDA--VLIATGTwKSRKLGIPGEDLpgvysaleylFRIRAAKLGYLPWEKVPpvEGKKVVVVG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 391 GGNTALTDALHLKHLGIET-TIVHR-------GDKFRAEKVLQdsvnrEGINIIWNSQVTEIIGEDQVESARIVNKD--- 459
Cdd:PRK12770 180 AGLTAVDAALEAVLLGAEKvYLAYRrtineapAGKYEIERLIA-----RGVEFLELVTPVRIIGEGRVEGVELAKMRlge 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 242124088 460 -------------GTETILDTDVVFVAIGHTANTELA-EKLGCELRPDGFIKVDPTQRTSVERVYAAGDVTGGVRQI 522
Cdd:PRK12770 255 pdesgrprpvpipGSEFVLEADTVVFAIGEIPTPPFAkECLGIELNRKGEIVVDEKHMTSREGVFAAGDVVTGPSKI 331
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
245-519 |
8.83e-22 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 98.30 E-value: 8.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 245 DVDLAIIGGGPAGMSAGIYAKRSGLSCIILEKQGVGG---QVALTPK------------VENY-PGFtniqGFELVE--- 305
Cdd:PRK06116 4 DYDLIVIGGGSGGIASANRAAMYGAKVALIEAKRLGGtcvNVGCVPKklmwygaqiaeaFHDYaPGY----GFDVTEnkf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 306 ---------------ILGSHAR-----EYTDIQQFAEVKDVKygpRIEITtDEKnYRAKGVLLATGVNVRMLGVPGEDkf 365
Cdd:PRK06116 80 dwaklianrdayidrLHGSYRNglennGVDLIEGFARFVDAH---TVEVN-GER-YTADHILIATGGRPSIPDIPGAE-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 366 yghgvsYCATCDGNFY-----KggKAVIVGGGNTALTDALHLKHLGIETTIVHRGDKF-RA-----EKVLQDSVNREGIN 434
Cdd:PRK06116 153 ------YGITSDGFFAleelpK--RVAVVGAGYIAVEFAGVLNGLGSETHLFVRGDAPlRGfdpdiRETLVEEMEKKGIR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 435 IIWNSQVTEIIGEDQvESARIVNKDGTEtiLDTDVVFVAIGHTANTE---LaEKLGCELRPDGFIKVDPTQRTSVERVYA 511
Cdd:PRK06116 225 LHTNAVPKAVEKNAD-GSLTLTLEDGET--LTVDCLIWAIGREPNTDglgL-ENAGVKLNEKGYIIVDEYQNTNVPGIYA 300
|
....*...
gi 242124088 512 AGDVTGGV 519
Cdd:PRK06116 301 VGDVTGRV 308
|
|
| MerA |
TIGR02053 |
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ... |
247-518 |
1.66e-19 |
|
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: 91.33 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 247 DLAIIGGGPAGMSAGIYAKRSGLSCIILEKQGVGGQ-----------------------------VALTPKVENYPGFTN 297
Cdd:TIGR02053 2 DLVIIGSGAAAFAAAIKAAELGASVAMVERGPLGGTcvnvgcvpskmllraaevahyarkppfggLAATVAVDFGELLEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 298 IQgfELVEILgsHAREYTDIqqfAEVKDVKY---------GPRIEITTDEKNYRAKGVLLATGVNVRMLGVPGEDKfygh 368
Cdd:TIGR02053 82 KR--EVVEEL--RHEKYEDV---LSSYGVDYlrgrarfkdPKTVKVDLGREVRGAKRFLIATGARPAIPPIPGLKE---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 369 gVSYCATCDgnFYKGGKA----VIVGGGNTALTDALHLKHLGIETTIVHRGDKF------RAEKVLQDSVNREGINIIWN 438
Cdd:TIGR02053 151 -AGYLTSEE--ALALDRIpeslAVIGGGAIGVELAQAFARLGSEVTILQRSDRLlpreepEISAAVEEALAEEGIEVVTS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 439 SQVTEIigEDQVESARIVN-KDGTETILDTDVVFVAIGHTANTELA--EKLGCELRPDGFIKVDPTQRTSVERVYAAGDV 515
Cdd:TIGR02053 228 AQVKAV--SVRGGGKIITVeKPGGQGEVEADELLVATGRRPNTDGLglEKAGVKLDERGGILVDETLRTSNPGIYAAGDV 305
|
...
gi 242124088 516 TGG 518
Cdd:TIGR02053 306 TGG 308
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
244-518 |
6.09e-18 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 86.52 E-value: 6.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 244 EDVDLAIIGGGPAGMSAGIYAKRSGLSCIILEKqgvggqvALTPKVENYPGFT--N---------IQGFELVEILGSH-- 310
Cdd:PRK06327 3 KQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEA-------WKNPKGKPALGGTclNvgcipskalLASSEEFENAGHHfa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 311 -----------------AREYTDIQQFAE--------------------VKDVKYGPRIEIT-TDEKNYRAKGVLLATGV 352
Cdd:PRK06327 76 dhgihvdgvkidvakmiARKDKVVKKMTGgieglfkknkitvlkgrgsfVGKTDAGYEIKVTgEDETVITAKHVIIATGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 353 NVRML-GVPgedkFYGHGVSyCATCDGNFYK-GGKAVIVGGGNTALTDALHLKHLGIETTIVHRGDKFRA------EKVL 424
Cdd:PRK06327 156 EPRHLpGVP----FDNKIIL-DNTGALNFTEvPKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAaadeqvAKEA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 425 QDSVNREGINIIWNSQVTEI-IGEDQVeSARIVNKDGTETILDTDVVFVAIGHTANTE--LAEKLGCELRPDGFIKVDPT 501
Cdd:PRK06327 231 AKAFTKQGLDIHLGVKIGEIkTGGKGV-SVAYTDADGEAQTLEVDKLIVSIGRVPNTDglGLEAVGLKLDERGFIPVDDH 309
|
330
....*....|....*..
gi 242124088 502 QRTSVERVYAAGDVTGG 518
Cdd:PRK06327 310 CRTNVPNVYAIGDVVRG 326
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
247-518 |
8.23e-16 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 79.86 E-value: 8.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 247 DLAIIGGGPAGMSAGIYAKRSGLSCIILEKQGVGG--------------------QVALTPKvenYPGFTN--------- 297
Cdd:PRK06370 7 DAIVIGAGQAGPPLAARAAGLGMKVALIERGLLGGtcvntgcvptktliasaraaHLARRAA---EYGVSVggpvsvdfk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 298 --------------------IQGFELVEILGSHAReytdiqqFAevkdvkyGPRiEITTDEKNYRAKGVLLATGVNVRML 357
Cdd:PRK06370 84 avmarkrrirarsrhgseqwLRGLEGVDVFRGHAR-------FE-------SPN-TVRVGGETLRAKRIFINTGARAAIP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 358 GVPGEDKfyghgVSYCaTCDGNFYKG---GKAVIVGGGNTALTDALHLKHLGIETTIVHRGDKF------RAEKVLQDSV 428
Cdd:PRK06370 149 PIPGLDE-----VGYL-TNETIFSLDelpEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLlpredeDVAAAVREIL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 429 NREGINIIWNSQVTEIigEDQVESARI-VNKDGTETILDTDVVFVAIGHTANTE-LA-EKLGCELRPDGFIKVDPTQRTS 505
Cdd:PRK06370 223 EREGIDVRLNAECIRV--ERDGDGIAVgLDCNGGAPEITGSHILVAVGRVPNTDdLGlEAAGVETDARGYIKVDDQLRTT 300
|
330
....*....|...
gi 242124088 506 VERVYAAGDVTGG 518
Cdd:PRK06370 301 NPGIYAAGDCNGR 313
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
250-514 |
4.03e-15 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 77.77 E-value: 4.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 250 IIGGGPAGMSAGIYAKR--SGLSCIILEKQG------------VGG-------QVALTPKVENYPGFTNIQGFELVEIlg 308
Cdd:PRK09564 5 IIGGTAAGMSAAAKAKRlnKELEITVYEKTDivsfgacglpyfVGGffddpntMIARTPEEFIKSGIDVKTEHEVVKV-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 309 shareytDIQ-QFAEVKDVKYGPRIEITTDEknyrakgVLLATGVNVRMLGVPGEDKfyghgvsycatcdGNFY-----K 382
Cdd:PRK09564 83 -------DAKnKTITVKNLKTGSIFNDTYDK-------LMIATGARPIIPPIKNINL-------------ENVYtlksmE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 383 GGKA-------------VIVGGGNTALTDALHLKHLGIETTIVHR-----GDKFRAE--KVLQDSVNREGINIIWNSQVT 442
Cdd:PRK09564 136 DGLAlkellkdeeikniVIIGAGFIGLEAVEAAKHLGKNVRIIQLedrilPDSFDKEitDVMEEELRENGVELHLNEFVK 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 242124088 443 EIIGEDQVEsarIVNKDGTEtiLDTDVVFVAIGHTANTELAEKLGCELRPDGFIKVDPTQRTSVERVYAAGD 514
Cdd:PRK09564 216 SLIGEDKVE---GVVTDKGE--YEADVVIVATGVKPNTEFLEDTGLKTLKNGAIIVDEYGETSIENIYAAGD 282
|
|
| Thioredoxin_3 |
pfam13192 |
Thioredoxin domain; |
147-218 |
5.42e-15 |
|
Thioredoxin domain;
Pssm-ID: 433026 [Multi-domain] Cd Length: 71 Bit Score: 69.94 E-value: 5.42e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 242124088 147 SPTCPYCPgQAINAFKAAVARPDkISAWNISTLDNENMAhEYKVGSVPHTDINDTVTFTGLEPEEKFMLQLL 218
Cdd:pfam13192 2 GPGCPKCP-QLEKAVKEAAAELG-IDAEVEKVTDFPEIA-KYGVMSTPALVINGKVVSSGKVPSEEEIRKLL 70
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
244-518 |
1.21e-14 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 76.34 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 244 EDVDLAIIGGGPAGMSAGIYAKRSGLSCIILEKQGVGGQV---------ALTPKVENYPGFTNIQGF----ELVEIlgsh 310
Cdd:PRK06416 3 FEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGTClnrgcipskALLHAAERADEARHSEDFgikaENVGI---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 311 arEYTDIQQFAE-------------VK----DVKYGP-------RIEITTD--EKNYRAKGVLLATGVNVRMLgvPGEdK 364
Cdd:PRK06416 79 --DFKKVQEWKNgvvnrltggveglLKknkvDIIRGEaklvdpnTVRVMTEdgEQTYTAKNIILATGSRPREL--PGI-E 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 365 FYGHGVSYcatcdgnfYKGG--------KAVIVGGG--NTALTDALHlkHLGIETTIVHRGDK----FRAE--KVLQDSV 428
Cdd:PRK06416 154 IDGRVIWT--------SDEAlnldevpkSLVVIGGGyiGVEFASAYA--SLGAEVTIVEALPRilpgEDKEisKLAERAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 429 NREGINIIWNSQVTEII-GEDQVESAriVNKDGTETILDTDVVFVAIGHTANTE---LaEKLGCEL-RpdGFIKVDPTQR 503
Cdd:PRK06416 224 KKRGIKIKTGAKAKKVEqTDDGVTVT--LEDGGKEETLEADYVLVAVGRRPNTEnlgL-EELGVKTdR--GFIEVDEQLR 298
|
330
....*....|....*
gi 242124088 504 TSVERVYAAGDVTGG 518
Cdd:PRK06416 299 TNVPNIYAIGDIVGG 313
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
348-515 |
1.31e-14 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 75.55 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 348 LATGVNVRMLGVPGEDKfygHGVSYC--------------ATCDGNFYKGGKAVIVGGGNT------ALTDALH--LKHL 405
Cdd:COG1252 103 IATGSVTNFFGIPGLAE---HALPLKtledalalrerllaAFERAERRRLLTIVVVGGGPTgvelagELAELLRklLRYP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 406 GIET-----TIVHRGDKF----------RAEKVLQdsvnREGINIIWNSQVTEIiGEDQVESarivnKDGTEtiLDTDVV 470
Cdd:COG1252 180 GIDPdkvriTLVEAGPRIlpglgeklseAAEKELE----KRGVEVHTGTRVTEV-DADGVTL-----EDGEE--IPADTV 247
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 242124088 471 FVAIGHTANtELAEKLGCELRPDGFIKVDPTQRT-SVERVYAAGDV 515
Cdd:COG1252 248 IWAAGVKAP-PLLADLGLPTDRRGRVLVDPTLQVpGHPNVFAIGDC 292
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
248-523 |
1.47e-14 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 76.70 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 248 LAIIGGGPAGMS-AGIYAKRsGLSCIILEK-QGVGGqvaltpkVENYpgftNIQGFELVEILGSHAREYTDIQQFAEVKD 325
Cdd:PRK12778 434 VAVIGSGPAGLSfAGDLAKR-GYDVTVFEAlHEIGG-------VLKY----GIPEFRLPKKIVDVEIENLKKLGVKFETD 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 326 VKYGPRIEITTDEKNyRAKGVLLATGVNV-RMLGVPGEDKfygHGV--------------SYCATCDGNFYKGGKAVIVG 390
Cdd:PRK12778 502 VIVGKTITIEELEEE-GFKGIFIASGAGLpNFMNIPGENS---NGVmssneyltrvnlmdAASPDSDTPIKFGKKVAVVG 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 391 GGNTALTDALHLKHLGIET-TIVHRGDK----FRAEKVlqDSVNREGINIIWNSQVTEIIGEDQ--VESARI-------- 455
Cdd:PRK12778 578 GGNTAMDSARTAKRLGAERvTIVYRRSEeempARLEEV--KHAKEEGIEFLTLHNPIEYLADEKgwVKQVVLqkmelgep 655
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 242124088 456 --------VNKDGTETILDTDVVFVAIGHTANTELAEKL-GCELRPDGFIKVDPTQRTSVERVYAAGD-VTGGVRQII 523
Cdd:PRK12778 656 dasgrrrpVAIPGSTFTVDVDLVIVSVGVSPNPLVPSSIpGLELNRKGTIVVDEEMQSSIPGIYAGGDiVRGGATVIL 733
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
248-517 |
1.58e-14 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 76.05 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 248 LAIIGGGPAGMSAGIYAKRSGLSCIILEKQGVGGQVALTPKVenyPGFTNIQGFELVEILGSHAREYTDIQQFAEVK--- 324
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIERDGLGGAAVLTDCV---PSKTLIATAEVRTELRRAAELGIRFIDDGEARvdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 325 -------------------------------------DVKYGP-RIEITTD---EKNYRAKGVLLATGVNVRMLgvPGed 363
Cdd:PRK07845 81 pavnarvkalaaaqsadirarleregvrviagrgrliDPGLGPhRVKVTTAdggEETLDADVVLIATGASPRIL--PT-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 364 kfyghgvsycATCDGN-------FYKGG----KAVIVGGGNTALTDALHLKHLGIETTIVHRGDKF------RAEKVLQD 426
Cdd:PRK07845 157 ----------AEPDGEriltwrqLYDLDelpeHLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVlpgedaDAAEVLEE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 427 SVNREGINIIWNSQVteiigedqvESARIVNkDGTETIL-DTDVV-----FVAIGHTANTE---LaEKLGCELRPDGFIK 497
Cdd:PRK07845 227 VFARRGMTVLKRSRA---------ESVERTG-DGVVVTLtDGRTVegshaLMAVGSVPNTAglgL-EEAGVELTPSGHIT 295
|
330 340
....*....|....*....|
gi 242124088 498 VDPTQRTSVERVYAAGDVTG 517
Cdd:PRK07845 296 VDRVSRTSVPGIYAAGDCTG 315
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
245-522 |
2.60e-14 |
|
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: 75.27 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 245 DVDLAIIGGGPAGMSAGIYAKRSGLSCIILE---------KQGVGG---QVALTPK---------------VENYpGFTN 297
Cdd:TIGR01438 2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDfvtptplgtRWGIGGtcvNVGCIPKklmhqaallgqalkdSRNY-GWKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 298 IQGFE-----LVEILGSHAREYTDIQQFA-EVKDVKY--------GPRIEITTD----EKNYRAKGVLLATGVNVRMLGV 359
Cdd:TIGR01438 81 EETVKhdwkrLVEAVQNHIGSLNWGYRVAlREKKVKYenayaefvDKHRIKATNkkgkEKIYSAERFLIATGERPRYPGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 360 PGEDKfyghgvsYCATCDGNF---YKGGKAVIVGGGNTALTDALHLKHLGIETT-----IVHRG-DKFRAEKVLQdSVNR 430
Cdd:TIGR01438 161 PGAKE-------LCITSDDLFslpYCPGKTLVVGASYVALECAGFLAGIGLDVTvmvrsILLRGfDQDCANKVGE-HMEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 431 EGINIIwnSQVtEIIGEDQVESARIVNKDGTETIL--DTDVVFVAIGHTANTelaEKLGCEL------RPDGFIKVDPTQ 502
Cdd:TIGR01438 233 HGVKFK--RQF-VPIKVEQIEAKVLVEFTDSTNGIeeEYDTVLLAIGRDACT---RKLNLENvgvkinKKTGKIPADEEE 306
|
330 340
....*....|....*....|
gi 242124088 503 RTSVERVYAAGDVTGGVRQI 522
Cdd:TIGR01438 307 QTNVPYIYAVGDILEDKPEL 326
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
332-515 |
2.71e-14 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 76.02 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 332 IEITTDEKN--------YRAKGVLLATGVNVRMLGVPGEDKFYGHGVSYCATCD-----GNFYKggKAVIVGGGNTALTD 398
Cdd:TIGR02374 78 IQIDTDQKQvitdagrtLSYDKLILATGSYPFILPIPGADKKGVYVFRTIEDLDaimamAQRFK--KAAVIGGGLLGLEA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 399 ALHLKHLGIETTIVHRGDKFRAEKV-------LQDSVNREGINIIWNSQVTEIIGEDQVESARIvnKDGTEtiLDTDVVF 471
Cdd:TIGR02374 156 AVGLQNLGMDVSVIHHAPGLMAKQLdqtagrlLQRELEQKGLTFLLEKDTVEIVGATKADRIRF--KDGSS--LEADLIV 231
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 242124088 472 VAIGHTANTELAEKLGceLRPDGFIKVDPTQRTSVERVYAAGDV 515
Cdd:TIGR02374 232 MAAGIRPNDELAVSAG--IKVNRGIIVNDSMQTSDPDIYAVGEC 273
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
249-517 |
4.00e-14 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 75.15 E-value: 4.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 249 AIIGGGPAGMSAGIYAKRSGLSCIILEKQGVGGQVAltpkvenYPGftnIQGFELVE-ILGShareytDIQQFAEV-KDV 326
Cdd:PRK12814 197 AIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMM-------RYG---IPRFRLPEsVIDA------DIAPLRAMgAEF 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 327 KYGPRI--EITTDE--KNYRAkgVLLATGVN-VRMLGVPGEDKfYG--HGVSYCAT-CDGNFYKGGKAVIV-GGGNTALT 397
Cdd:PRK12814 261 RFNTVFgrDITLEElqKEFDA--VLLAVGAQkASKMGIPGEEL-PGviSGIDFLRNvALGTALHPGKKVVViGGGNTAID 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 398 DALHLKHLGIET-TIVHRgdKFRAEKvlqdSVNR--------EGINI-IWNSQV--------TEII------GE-DQVES 452
Cdd:PRK12814 338 AARTALRLGAESvTILYR--RTREEM----PANRaeieealaEGVSLrELAAPVsierseggLELTaikmqqGEpDESGR 411
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 242124088 453 ARIVNKDGTETILDTDVVFVAIGHTANTELAEKLGCELRPDGFIKVDP-TQRTSVERVYAAGD-VTG 517
Cdd:PRK12814 412 RRPVPVEGSEFTLQADTVISAIGQQVDPPIAEAAGIGTSRNGTVKVDPeTLQTSVAGVFAGGDcVTG 478
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
249-514 |
5.57e-14 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 74.43 E-value: 5.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 249 AIIGGGPAGMSAGIYAKRSGLSCIILEKQG-VGGqvALTpkvenYpGftnIQGFELvEilGSHAReyTDIQQFAE--VKd 325
Cdd:PRK12810 147 AVVGSGPAGLAAADQLARAGHKVTVFERADrIGG--LLR-----Y-G---IPDFKL-E--KEVID--RRIELMEAegIE- 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 326 VKYGPRI--EITTDE--KNYRAkgVLLATGV-NVRMLGVPGEDkfyGHGVsYCA---------TCDGNFYKG-----GKA 386
Cdd:PRK12810 210 FRTNVEVgkDITAEEllAEYDA--VFLGTGAyKPRDLGIPGRD---LDGV-HFAmdfliqntrRVLGDETEPfisakGKH 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 387 VIV-GGGNTAlTD---------ALHLKHLGIE----------TTIVHRGDKFRaekvlQDSVNREGINIIWNSQVTEIIG 446
Cdd:PRK12810 284 VVViGGGDTG-MDcvgtairqgAKSVTQRDIMpmppsrrnknNPWPYWPMKLE-----VSNAHEEGVEREFNVQTKEFEG 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 447 ED-QVESARIVN----------KDGTETILDTDVVFVAIGHT-ANTELAEKLGCELRPDGFIKVDPTQ-RTSVERVYAAG 513
Cdd:PRK12810 358 ENgKVTGVKVVRtelgegdfepVEGSEFVLPADLVLLAMGFTgPEAGLLAQFGVELDERGRVAAPDNAyQTSNPKVFAAG 437
|
.
gi 242124088 514 D 514
Cdd:PRK12810 438 D 438
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
249-517 |
5.75e-14 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 74.28 E-value: 5.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 249 AIIGGGPAGMS-AGIYAKRsGLSCIILEkqgvggqvALtpkveNYPGFTNIQG---FELveilgshAREYTDIQQFAEVK 324
Cdd:PRK12831 144 AVIGSGPAGLTcAGDLAKM-GYDVTIFE--------AL-----HEPGGVLVYGipeFRL-------PKETVVKKEIENIK 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 325 dvKYGPRIE--------ITTDE--KNYRAKGVLLATGVNV-RMLGVPGEDkfyGHGV--------------SYCATCDGN 379
Cdd:PRK12831 203 --KLGVKIEtnvvvgktVTIDEllEEEGFDAVFIGSGAGLpKFMGIPGEN---LNGVfsanefltrvnlmkAYKPEYDTP 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 380 FYKGGKAVIVGGGNTALTDALHLKHLGIETTIVHRgdkfRAEKVLQDSVN------REGINIIWNSQVTEIIGE------ 447
Cdd:PRK12831 278 IKVGKKVAVVGGGNVAMDAARTALRLGAEVHIVYR----RSEEELPARVEevhhakEEGVIFDLLTNPVEILGDengwvk 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 448 ------------DQVESARIVNKDGTETILDTDVVFVAIGHTANTELAEKL-GCELRPDGFIKVDP-TQRTSVERVYAAG 513
Cdd:PRK12831 354 gmkcikmelgepDASGRRRPVEIEGSEFVLEVDTVIMSLGTSPNPLISSTTkGLKINKRGCIVADEeTGLTSKEGVFAGG 433
|
....*
gi 242124088 514 D-VTG 517
Cdd:PRK12831 434 DaVTG 438
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
204-517 |
6.84e-14 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 74.27 E-value: 6.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 204 FTGLEPEEKFMLQLLFLKPLEEvveEQRAAKAETTEDTVYedvDLAIIGGGPAGMSAGIYAKRSGLSCIILEKQGVGG-- 281
Cdd:PTZ00058 13 FALLNPSIKLIRSFSFYHNLEA---SSAPTHLKKKPRMVY---DLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGtc 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 282 -QVALTPK------------VEN--YPGFTNIQGFEL--------------------------VEILGSHAREYTDIQQF 320
Cdd:PTZ00058 87 vNVGCVPKkimfnaasihdiLENsrHYGFDTQFSFNLpllverrdkyirrlndiyrqnlkkdnVEYFEGKGSLLSENQVL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 321 AEVKDVKYGPRIEITTDEKNYRAKGVL------LATGVNVrMLGVPGEDKFYG-HGVSYCATCDGNFY--KGGKAVIVGG 391
Cdd:PTZ00058 167 IKKVSQVDGEADESDDDEVTIVSAGVSqlddgqVIEGKNI-LIAVGNKPIFPDvKGKEFTISSDDFFKikEAKRIGIAGS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 392 GNTALTDALHLKHLGIETTIVHRGDK-FRA--EKV---LQDSVNREGINIIWNSQVTEIIGEDQVESARIVNKDGTEtiL 465
Cdd:PTZ00058 246 GYIAVELINVVNRLGAESYIFARGNRlLRKfdETIineLENDMKKNNINIITHANVEEIEKVKEKNLTIYLSDGRKY--E 323
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 242124088 466 DTDVVFVAIGHTANTElaeKLGCE----LRPDGFIKVDPTQRTSVERVYAAGDVTG 517
Cdd:PTZ00058 324 HFDYVIYCVGRSPNTE---DLNLKalniKTPKGYIKVDDNQRTSVKHIYAVGDCCM 376
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
244-414 |
1.36e-13 |
|
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];
Pssm-ID: 441675 [Multi-domain] Cd Length: 414 Bit Score: 72.59 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 244 EDVDLAIIGGGPAGMSAGIYAKRSGLSCIILEK-QGVGGQ--------VAL-TPKVEN-YPGF---TNIQGF----ELVE 305
Cdd:COG2072 5 EHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKaDDVGGTwrdnrypgLRLdTPSHLYsLPFFpnwSDDPDFptgdEILA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 306 ILGSHAREYtDIQ---QF-AEVKDVKY---GPRIEITTDE-KNYRAKGVLLATGVNVR--MLGVPGEDKF---------Y 366
Cdd:COG2072 85 YLEAYADKF-GLRrpiRFgTEVTSARWdeaDGRWTVTTDDgETLTARFVVVATGPLSRpkIPDIPGLEDFageqlhsadW 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 242124088 367 GHGVSycatcdgnfYKGGKAVIVGGGNTALTDALHLKHLGIETTIVHR 414
Cdd:COG2072 164 RNPVD---------LAGKRVLVVGTGASAVQIAPELARVAAHVTVFQR 202
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
342-519 |
1.69e-13 |
|
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: 72.70 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 342 RAKGVLLATGVNVRMLGVPGEDkfyghgvsYCATCDGNFY---KGGKAVIVGGGNTALTDA---LHLKHLGIETTIVHRG 415
Cdd:TIGR01423 151 QAEHILLATGSWPQMLGIPGIE--------HCISSNEAFYldePPRRVLTVGGGFISVEFAgifNAYKPRGGKVTLCYRN 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 416 D--------KFRAEKVLQDSVNreGINIIWNSQVTEIIgedqvesariVNKDGTETI-------LDTDVVFVAIGHTANT 480
Cdd:TIGR01423 223 NmilrgfdsTLRKELTKQLRAN--GINIMTNENPAKVT----------LNADGSKHVtfesgktLDVDVVMMAIGRVPRT 290
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 242124088 481 ELAE--KLGCELRPDGFIKVDPTQRTSVERVYAAGDVTGGV 519
Cdd:TIGR01423 291 QTLQldKVGVELTKKGAIQVDEFSRTNVPNIYAIGDVTDRV 331
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
387-515 |
2.70e-13 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 71.91 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 387 VIVGGGNTALTDALHLKHLGIETTIVHRGDKFRAEkvlQDSVNREGINIIWNSQV-----TEIIGEDQVESARIVNKDGT 461
Cdd:PRK07846 170 VIVGGGFIAAEFAHVFSALGVRVTVVNRSGRLLRH---LDDDISERFTELASKRWdvrlgRNVVGVSQDGSGVTLRLDDG 246
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 242124088 462 ETIlDTDVVFVAIGHTANTEL--AEKLGCELRPDGFIKVDPTQRTSVERVYAAGDV 515
Cdd:PRK07846 247 STV-EADVLLVATGRVPNGDLldAAAAGVDVDEDGRVVVDEYQRTSAEGVFALGDV 301
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
385-458 |
3.06e-13 |
|
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: 64.92 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 385 KAVIVGGGNTALTDALHLKHLGIETTIVHRGDKFR------AEKVLQDSVNREGINIIWNSQVTEIIGEDQVESARIVNK 458
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLpgfdpeIAKILQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLTDG 80
|
|
| TRX_GRX_like |
cd02973 |
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins ... |
142-206 |
4.06e-13 |
|
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins that show similarity to both TRX and GRX, including the C-terminal TRX-fold subdomain of Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO). All members contain a redox-active CXXC motif and may function as PDOs. The archaeal proteins Mj0307 and Mt807 show structures more similar to GRX, but activities more similar to TRX. Some members of the family are similar to PfPDO in that they contain a second CXXC motif located in a second TRX-fold subdomain at the N-terminus; the superimposable N- and C-terminal TRX subdomains form a compact structure. PfPDO is postulated to be the archaeal counterpart of bacterial DsbA and eukaryotic protein disulfide isomerase (PDI). The C-terminal CXXC motif of PfPDO is required for its oxidase, reductase and isomerase activities. Also included in the family is the C-terminal TRX-fold subdomain of the N-terminal domain (NTD) of bacterial AhpF, which has a similar fold as PfPDO with two TRX-fold subdomains but without the second CXXC motif.
Pssm-ID: 239271 [Multi-domain] Cd Length: 67 Bit Score: 64.13 E-value: 4.06e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242124088 142 VKIFASPTCPYCPGQAINAFKAAVArPDKISAWNISTLDNENMAHEYKVGSVPHTDINDTVTFTG 206
Cdd:cd02973 3 IEVFVSPTCPYCPDAVQAANRIAAL-NPNISAEMIDAAEFPDLADEYGVMSVPAIVINGKVEFVG 66
|
|
| PfPDO_like_N |
cd02975 |
Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO)-like family, N-terminal TRX-fold ... |
12-119 |
1.52e-12 |
|
Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO)-like family, N-terminal TRX-fold subdomain; composed of proteins with similarity to PfPDO, a redox active thermostable protein believed to be the archaeal counterpart of bacterial DsbA and eukaryotic protein disulfide isomerase (PDI), which are both involved in oxidative protein folding. PfPDO contains two redox active CXXC motifs in two contiguous TRX-fold subdomains. The active site in the N-terminal TRX-fold subdomain is required for isomerase but not for reductase activity of PfPDO. The exclusive presence of PfPDO-like proteins in extremophiles may suggest that they have a special role in adaptation to extreme conditions.
Pssm-ID: 239273 [Multi-domain] Cd Length: 113 Bit Score: 64.33 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 12 NFIPEESREYL-EKLFAEFKRTVTIEVYTAEgEHREYNDFTLNICRAFNVISDKIELREY--AVDSEMGKNRNIIATPTV 88
Cdd:cd02975 1 GLLSDEDRKALkEEFFKEMKNPVDLVVFSSK-EGCQYCEVTKQLLEELSELSDKLKLEIYdfDEDKEKAEKYGVERVPTT 79
|
90 100 110
....*....|....*....|....*....|....
gi 242124088 89 LISPDE---YDIRFLGAPAGEEGRALVEALNLAS 119
Cdd:cd02975 80 IFLQDGgkdGGIRYYGLPAGYEFASLIEDIVRVS 113
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
227-516 |
1.41e-11 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 66.76 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 227 VEEQRAAKAETTEDTVYEDVDLAIIGGGPAGMSAGIYAKRSGLSCIILE----------KQGVGGQVAL---TPK----- 288
Cdd:PLN02507 7 IDGEVAKVNADEANATHYDFDLFVIGAGSGGVRAARFSANFGAKVGICElpfhpissesIGGVGGTCVIrgcVPKkilvy 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 289 -------VENYPGFT-NIQG---FELVEILGSHARE-------YTDIQQFAEVKDVKYGPRI------EITT---DEKNY 341
Cdd:PLN02507 87 gatfggeFEDAKNYGwEINEkvdFNWKKLLQKKTDEilrlngiYKRLLANAGVKLYEGEGKIvgpnevEVTQldgTKLRY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 342 RAKGVLLATGVNVRMLGVPGEDkfyghgvsYCATCD-----GNFYKggKAVIVGGGNTALTDALHLKHLGIETTIVHR-- 414
Cdd:PLN02507 167 TAKHILIATGSRAQRPNIPGKE--------LAITSDealslEELPK--RAVVLGGGYIAVEFASIWRGMGATVDLFFRke 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 415 ------GDKFRAekVLQDSVNREGINIIWNSQVTEIigeDQVESARIVNKDGTETILdTDVVFVAIGHTANTELA--EKL 486
Cdd:PLN02507 237 lplrgfDDEMRA--VVARNLEGRGINLHPRTNLTQL---TKTEGGIKVITDHGEEFV-ADVVLFATGRAPNTKRLnlEAV 310
|
330 340 350
....*....|....*....|....*....|
gi 242124088 487 GCELRPDGFIKVDPTQRTSVERVYAAGDVT 516
Cdd:PLN02507 311 GVELDKAGAVKVDEYSRTNIPSIWAIGDVT 340
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
245-519 |
1.85e-10 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 63.30 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 245 DVDLAIIGGGPAGMSAGIYAKRSGLSCIILE---------KQGVGG---QVALTP-KVENYPGF--------TNIQGFE- 302
Cdd:PTZ00052 5 MYDLVVIGGGSGGMAAAKEAAAHGKKVALFDyvkpstqgtKWGLGGtcvNVGCVPkKLMHYAANigsifhhdSQMYGWKt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 303 --------LVEILGSHAR---------------EYtdIQQFAEVKD---VKYGPrieiTTDEKNYRAKGVLLATGVNVRM 356
Cdd:PTZ00052 85 sssfnwgkLVTTVQNHIRslnfsyrtglrsskvEY--INGLAKLKDehtVSYGD----NSQEETITAKYILIATGGRPSI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 357 L-GVPGedkfyghGVSYCATCDGNFYKG---GKAVIVGGGNTALTDALHLKHLGIETT-----IVHRG-DKFRAEKVL-- 424
Cdd:PTZ00052 159 PeDVPG-------AKEYSITSDDIFSLSkdpGKTLIVGASYIGLETAGFLNELGFDVTvavrsIPLRGfDRQCSEKVVey 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 425 ---QDSVNREGINIIWNSQVTEIIgedqvesaRIVNKDGTETILDTdvVFVAIGHTANTEL--AEKLGCELRPDGfIKVD 499
Cdd:PTZ00052 232 mkeQGTLFLEGVVPINIEKMDDKI--------KVLFSDGTTELFDT--VLYATGRKPDIKGlnLNAIGVHVNKSN-KIIA 300
|
330 340
....*....|....*....|
gi 242124088 500 PTQRTSVERVYAAGDVTGGV 519
Cdd:PTZ00052 301 PNDCTNIPNIFAVGDVVEGR 320
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
385-515 |
3.66e-10 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 62.11 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 385 KAVIVGGGNTALTDALHLKHLGIETTIVHRGDKFRA------EKVLQDSVNREGINIIWNSQVTEIIGEDqvesarIVNK 458
Cdd:PRK13512 150 KALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKlmdadmNQPILDELDKREIPYRLNEEIDAINGNE------VTFK 223
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 242124088 459 DG-TEtilDTDVVFVAIGHTANTELAEKLGCELRPDGFIKVDPTQRTSVERVYAAGDV 515
Cdd:PRK13512 224 SGkVE---HYDMIIEGVGTHPNSKFIESSNIKLDDKGFIPVNDKFETNVPNIYAIGDI 278
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
388-518 |
3.92e-10 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 62.07 E-value: 3.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 388 IVGGGNTALTDALHLKHLGIETTIVHRGDKF--RAEKVL----QDSVNREGINIIWNSQVTEIIGEDqvESARIVNKDGT 461
Cdd:PRK07251 162 IIGGGNIGLEFAGLYNKLGSKVTVLDAASTIlpREEPSVaalaKQYMEEDGITFLLNAHTTEVKNDG--DQVLVVTEDET 239
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 242124088 462 ETIldtDVVFVAIGHTANTE-LA-EKLGCELRPDGFIKVDPTQRTSVERVYAAGDVTGG 518
Cdd:PRK07251 240 YRF---DALLYATGRKPNTEpLGlENTDIELTERGAIKVDDYCQTSVPGVFAVGDVNGG 295
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
245-517 |
2.39e-09 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 59.78 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 245 DVDLAIIGGGPAGMSAGIYAKRSGLSCIILEK-QGVGG--------------QVALtpKVENY---PGFTNIQGFELVEI 306
Cdd:PRK05249 5 DYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERyRNVGGgcthtgtipskalrEAVL--RLIGFnqnPLYSSYRVKLRITF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 307 --LGSHAREYTDIQ------QFA--EVkDVKYGP-------RIEITTDE---KNYRAKGVLLATGVN-VRMLGVPgedkF 365
Cdd:PRK05249 83 adLLARADHVINKQvevrrgQYErnRV-DLIQGRarfvdphTVEVECPDgevETLTADKIVIATGSRpYRPPDVD----F 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 366 YGHGVsycatCDGN-----FYKGGKAVIVGGGNTALTDALHLKHLGIETTIVHRGDKF----RAEKV--LQDSVNREGIN 434
Cdd:PRK05249 158 DHPRI-----YDSDsilslDHLPRSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLlsflDDEISdaLSYHLRDSGVT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 435 IIWNSQVTEIIGEDqvesarivnkDGTETILD------TDVVFVAIGHTANTElaeKLGCE---LRPD--GFIKVDPTQR 503
Cdd:PRK05249 233 IRHNEEVEKVEGGD----------DGVIVHLKsgkkikADCLLYANGRTGNTD---GLNLEnagLEADsrGQLKVNENYQ 299
|
330
....*....|....
gi 242124088 504 TSVERVYAAGDVTG 517
Cdd:PRK05249 300 TAVPHIYAVGDVIG 313
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
386-516 |
2.61e-09 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 59.78 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 386 AVIvGGGNTALTDALHLKHLGIETTIVHRGDKFRAE-----KVLQDSVNREGINIIWNSQVTEiigedqvesariVNKDG 460
Cdd:PRK13748 274 AVI-GSSVVALELAQAFARLGSKVTILARSTLFFREdpaigEAVTAAFRAEGIEVLEHTQASQ------------VAHVD 340
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 242124088 461 TETILDT-------DVVFVAIGHTANT-ELA-EKLGCELRPDGFIKVDPTQRTSVERVYAAGDVT 516
Cdd:PRK13748 341 GEFVLTTghgelraDKLLVATGRAPNTrSLAlDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCT 405
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
382-514 |
1.53e-08 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 57.44 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 382 KGGKAVIVGGGNTALTDALHLKHLGIETTIVHRGDKFRAEKV-------LQDSVNREGINIIWNSQVTEIIGEDQVESAR 454
Cdd:PRK14989 144 RSKRGAVVGGGLLGLEAAGALKNLGVETHVIEFAPMLMAEQLdqmggeqLRRKIESMGVRVHTSKNTLEIVQEGVEARKT 223
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 455 IVNKDGTEtiLDTDVVFVAIGHTANTELAEKLGCELRPDGFIKVDPTQRTSVERVYAAGD 514
Cdd:PRK14989 224 MRFADGSE--LEVDFIVFSTGIRPQDKLATQCGLAVAPRGGIVINDSCQTSDPDIYAIGE 281
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
382-518 |
1.67e-08 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 57.53 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 382 KGGKAVIVGGGNTALTDALHLKHLGIETTIVHRGDK----FRAEKvLQDSVnREGINIIWNSQVTEIIGEDQV------- 450
Cdd:PRK12779 446 KGKEVFVIGGGNTAMDAARTAKRLGGNVTIVYRRTKsempARVEE-LHHAL-EEGINLAVLRAPREFIGDDHThfvthal 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 451 ----------ESARIVNKDGTETI-LDTDVVFVAIGHTANTELAE-KLGCELRPDGFIKVDP-TQRTSVERVYAAGDVTG 517
Cdd:PRK12779 524 ldvnelgepdKSGRRSPKPTGEIErVPVDLVIMALGNTANPIMKDaEPGLKTNKWGTIEVEKgSQRTSIKGVYSGGDAAR 603
|
.
gi 242124088 518 G 518
Cdd:PRK12779 604 G 604
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
233-517 |
2.22e-08 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 56.79 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 233 AKAETTEDTVYEDVDLA----IIGGGPAGMSAGIYAKRSGLSCIILEKQGV-GGQVALTPKVenYPGFTNIQgfELVEIL 307
Cdd:COG1148 124 AKAKLLEPLEPIKVPVNkralVIGGGIAGMTAALELAEQGYEVYLVEKEPElGGRAAQLHKT--FPGLDCPQ--CILEPL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 308 GSHAREYTDIQQF--AEVKDVK-YGPRIEIT-----TDEKNYRAKGVLLATGVNvrmLGVPGEDKFYGHGVS-------- 371
Cdd:COG1148 200 IAEVEANPNITVYtgAEVEEVSgYVGNFTVTikkgpREEIEIEVGAIVLATGFK---PYDPTKLGEYGYGKYpnvitnle 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 372 ---------YCATCDGnfyKGGKAVI----VG-----GGN---------TALTDALHLKHL--GIETTIVHR-------G 415
Cdd:COG1148 277 lerllaagkILRPSDG---KEPKSVAfiqcVGsrdeeNGLpycsrvccmYALKQALYLKEKnpDADVYIFYRdirtygkY 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 416 DKFRAEkvlqdsVNREGINIIwNSQVTEIIgEDQVESARIVNKD---GTETILDTDVVFVAIG---HTANTELAEKLGCE 489
Cdd:COG1148 354 EEFYRR------AREDGVRFI-RGRVAEIE-EDEGGKLVVTVEDtllGEPVEIEADLVVLATGmvpSEDNEELAKLLKLP 425
|
330 340 350
....*....|....*....|....*....|...
gi 242124088 490 LRPDGFI-----KVDPTQrTSVERVYAAGDVTG 517
Cdd:COG1148 426 LDQDGFFleahpKLRPVE-TATDGIFLAGAAHG 457
|
|
| redox_disulf_1 |
TIGR00411 |
small redox-active disulfide protein 1; This protein is homologous to a family of proteins ... |
142-211 |
2.52e-08 |
|
small redox-active disulfide protein 1; This protein is homologous to a family of proteins that includes thioredoxins, glutaredoxins, protein-disulfide isomerases, and others, some of which have several such domains. The sequence of this protein at the redox-active disufide site, CPYC, matches glutaredoxins rather than thioredoxins, although its overall sequence seems closer to thioredoxins. It is suggested to be a ribonucleotide-reducing system component distinct from thioredoxin or glutaredoxin. [Unknown function, General]
Pssm-ID: 129505 [Multi-domain] Cd Length: 82 Bit Score: 51.42 E-value: 2.52e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 142 VKIFASPTCPYCPGQAINAFKAAVARPDKISAWNISTLDNENMAHEYKVGSVPHTDINDTVTFTGLEPEE 211
Cdd:TIGR00411 3 IELFTSPTCPYCPAAKRVVEEVAKEMGDAVEVEYINVMENPQKAMEYGIMAVPAIVINGDVEFIGAPTKE 72
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
231-516 |
1.91e-07 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 53.73 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 231 RAAKAETTEDTVYEDVDLAIIGGGPAGMSAGIYAKRSGLSCIILE----------KQGVGGQVAL---TPK-----VENY 292
Cdd:PLN02546 65 RAAAPNGAESERHYDFDLFTIGAGSGGVRASRFASNFGASAAVCElpfatissdtLGGVGGTCVLrgcVPKkllvyASKY 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 293 PG-FTNIQGF---------------------ELVEILGShareYTDIQQFAEVKDVKYGPRI----EITTDEKNYRAKGV 346
Cdd:PLN02546 145 SHeFEESRGFgwkyetepkhdwntlianknaELQRLTGI----YKNILKNAGVTLIEGRGKIvdphTVDVDGKLYTARNI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 347 LLATGVNVRMLGVPGEDkfygHGVSYCATCDGNfYKGGKAVIVGGGNTALTDALHLKHLGIETTIVhrgdkFRAEKVLQD 426
Cdd:PLN02546 221 LIAVGGRPFIPDIPGIE----HAIDSDAALDLP-SKPEKIAIVGGGYIALEFAGIFNGLKSDVHVF-----IRQKKVLRG 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 427 svnreginiiWNSQVTEIIGE-----------DQVESARIVNKDGT-------ETILDTDVVFVAIGHTANTE-LA-EKL 486
Cdd:PLN02546 291 ----------FDEEVRDFVAEqmslrgiefhtEESPQAIIKSADGSlslktnkGTVEGFSHVMFATGRKPNTKnLGlEEV 360
|
330 340 350
....*....|....*....|....*....|
gi 242124088 487 GCELRPDGFIKVDPTQRTSVERVYAAGDVT 516
Cdd:PLN02546 361 GVKMDKNGAIEVDEYSRTSVPSIWAVGDVT 390
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
384-520 |
3.18e-06 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 49.63 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 384 GKAVIVGGGNTALTDALHLKHLGIETTIVHRGDKF--RAEKVLQDSVNR----EGINIIWNSQVTEII---GEDQVESAr 454
Cdd:PRK08010 159 GHLGILGGGYIGVEFASMFANFGSKVTILEAASLFlpREDRDIADNIATilrdQGVDIILNAHVERIShheNQVQVHSE- 237
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 242124088 455 ivnkdgtETILDTDVVFVAIGH---TANTELaEKLGCELRPDGFIKVDPTQRTSVERVYAAGDVTGGVR 520
Cdd:PRK08010 238 -------HAQLAVDALLIASGRqpaTASLHP-ENAGIAVNERGAIVVDKYLHTTADNIWAMGDVTGGLQ 298
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
247-284 |
3.85e-06 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 49.21 E-value: 3.85e-06
10 20 30
....*....|....*....|....*....|....*....
gi 242124088 247 DLAIIGGGPAGMSAGIYAKRSGLSCIILEK-QGVGGQVA 284
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKgQPFGGATA 39
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
244-281 |
4.45e-06 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 49.06 E-value: 4.45e-06
10 20 30
....*....|....*....|....*....|....*...
gi 242124088 244 EDVDLAIIGGGPAGMSAGIYAKRSGLSCIILEKQGVGG 281
Cdd:COG1053 2 HEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRG 39
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
249-351 |
1.07e-05 |
|
flavoprotein, HI0933 family; The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 272992 [Multi-domain] Cd Length: 400 Bit Score: 47.98 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 249 AIIGGGPAGMSAGIYAKRSGLSCIILEK-QGVGGQVALTPK--------------VENYPG-----------FTNIQGFE 302
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLEKnKKIGKKLLISGGgrcnltnscptpefVAYYPRngkflrsalsrFSNKDLID 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 242124088 303 LVEILG------SHAREYT------DIQQF---------------AEVKDVKYGP-RIEITTDEKNYRAKGVLLATG 351
Cdd:TIGR00275 81 FFESLGlelkveEDGRVFPcsdsaaDVLDAllnelkelgveiltnSKVKSIEKEDgGFGVETSGGEYEADKVIIATG 157
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
382-515 |
2.45e-05 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 46.84 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 382 KGGKAVIVGGGNTALTDALHLKHLGIETTIVHRGDKFR---AEKVLQDSV-NR---EGINIIWNSQVTEIIGEDQVEsar 454
Cdd:PRK09754 143 PERSVVIVGAGTIGLELAASATQRRCKVTVIELAATVMgrnAPPPVQRYLlQRhqqAGVRILLNNAIEHVVDGEKVE--- 219
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 242124088 455 iVNKDGTETILdTDVVFVAIGHTANTELAEKLGceLRPDGFIKVDPTQRTSVERVYAAGDV 515
Cdd:PRK09754 220 -LTLQSGETLQ-ADVVIYGIGISANDQLAREAN--LDTANGIVIDEACRTCDPAIFAGGDV 276
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
244-286 |
3.21e-05 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 46.67 E-value: 3.21e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 242124088 244 EDVDLAIIGGGPAGMSAGIYAKRSGLSCIILEKQG-VGGQVALT 286
Cdd:PRK12844 5 ETYDVVVVGSGGGGMCAALAAADSGLEPLIVEKQDkVGGSTAMS 48
|
|
| PRK06481 |
PRK06481 |
flavocytochrome c; |
232-493 |
3.63e-05 |
|
flavocytochrome c;
Pssm-ID: 180584 [Multi-domain] Cd Length: 506 Bit Score: 46.37 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 232 AAKAETTEDTVYEDVDLAIIGGGPAGMSAGIYAKRSGLSCIILEKQGVGGqvaltpkvenypgftniqGFELVEILGSHA 311
Cdd:PRK06481 48 SKTSYTDPSELKDKYDIVIVGAGGAGMSAAIEAKDAGMNPVILEKMPVAG------------------GNTMKASSGMNA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 312 REyTDIQQFAEVKDvkygprieitTDEKNYRA--KGvllATGVNvrmlgvpgeDK-----FYGHGVSYCATCDGNFYKGG 384
Cdd:PRK06481 110 SE-TKFQKAQGIAD----------SNDKFYEEtlKG---GGGTN---------DKallryFVDNSASAIDWLDSMGIKLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 385 KAVIVGGGNTALTdalHLKHLG--IETTIVhrgdkfraeKVLQDSVNREGINIIWNSQVTEIIGED-QVESARI-VNKDG 460
Cdd:PRK06481 167 NLTITGGMSEKRT---HRPHDGsaVGGYLV---------DGLLKNVQERKIPLFVNADVTKITEKDgKVTGVKVkINGKE 234
|
250 260 270
....*....|....*....|....*....|...
gi 242124088 461 TETILDTDVVFVAIGHTANTELAEKlgceLRPD 493
Cdd:PRK06481 235 TKTISSKAVVVTTGGFGANKDMIAK----YRPD 263
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
247-282 |
3.64e-05 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 46.45 E-value: 3.64e-05
10 20 30
....*....|....*....|....*....|....*..
gi 242124088 247 DLAIIGGGPAGMSAGIYAKRSGLSCIILEKQG-VGGQ 282
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVERRGfLGGM 37
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
244-281 |
4.26e-05 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 46.05 E-value: 4.26e-05
10 20 30
....*....|....*....|....*....|....*...
gi 242124088 244 EDVDLAIIGGGPAGMSAGIYAKRSGLSCIILEKQGVGG 281
Cdd:COG0665 1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGS 38
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
388-514 |
4.39e-05 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 46.06 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 388 IVGGG--NTALtdALHLKHLGIETTIVHRGDKFRAEKV-------LQDSVNREGINIIWNSQVTEIigeDQVESARIVNK 458
Cdd:PRK04965 146 VVGGGliGTEL--AMDLCRAGKAVTLVDNAASLLASLMppevssrLQHRLTEMGVHLLLKSQLQGL---EKTDSGIRATL 220
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 242124088 459 DGTETIlDTDVVFVAIGHTANTELAEKLGCELRpDGfIKVDPTQRTSVERVYAAGD 514
Cdd:PRK04965 221 DSGRSI-EVDAVIAAAGLRPNTALARRAGLAVN-RG-IVVDSYLQTSAPDIYALGD 273
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
250-284 |
5.97e-05 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 40.98 E-value: 5.97e-05
10 20 30
....*....|....*....|....*....|....*.
gi 242124088 250 IIGGGPAGMSAGIYAKRSGLSCIILEKQ-GVGGQVA 284
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRdRLGGNAY 36
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
244-277 |
8.35e-05 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 44.93 E-value: 8.35e-05
10 20 30
....*....|....*....|....*....|....
gi 242124088 244 EDVDLAIIGGGPAGMSAGIYAKRSGLSCIILEKQ 277
Cdd:COG0654 2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERA 35
|
|
| GlpB |
COG3075 |
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]; |
247-285 |
8.54e-05 |
|
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 442309 Cd Length: 415 Bit Score: 45.17 E-value: 8.54e-05
10 20 30
....*....|....*....|....*....|....*....
gi 242124088 247 DLAIIGGGPAGMSAGIYAKRSGLSCIILEKqgvgGQVAL 285
Cdd:COG3075 4 DVVVIGGGLAGLTAAIRAAEAGLRVAIVSA----GQSAL 38
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
248-523 |
1.06e-04 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 45.32 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 248 LAIIGGGPAGMSAGIYAKRSGLSCIILEKQGVGGQVAltpkveNYpgftNIQGFELV-EILGSHAREYTDIQ-QFAEVKD 325
Cdd:PRK12775 433 VAICGSGPAGLAAAADLVKYGVDVTVYEALHVVGGVL------QY----GIPSFRLPrDIIDREVQRLVDIGvKIETNKV 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 326 VKYGPRIEITTDEKNYRAkgVLLATGVNV-RMLGVPGEDKfyghGVSYCAT---CDGNFYKG------------GKAVIV 389
Cdd:PRK12775 503 IGKTFTVPQLMNDKGFDA--VFLGVGAGApTFLGIPGEFA----GQVYSANeflTRVNLMGGdkfpfldtpislGKSVVV 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 390 -GGGNTALtDALHL-KHLGIETT-IVHRGDKFRAEKVLQD--SVNREGINIIWNSQVTEI-----------------IGE 447
Cdd:PRK12775 577 iGAGNTAM-DCLRVaKRLGAPTVrCVYRRSEAEAPARIEEirHAKEEGIDFFFLHSPVEIyvdaegsvrgmkveemeLGE 655
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 448 DQVESARIVNKDGTETILDTDVVFVAIGHTANTELAEKL-GCELRPDGFI-----KVDPTQRTSVERVYAAGD-VTGGVR 520
Cdd:PRK12775 656 PDEKGRRKPMPTGEFKDLECDTVIYALGTKANPIITQSTpGLALNKWGNIaaddgKLESTQSTNLPGVFAGGDiVTGGAT 735
|
...
gi 242124088 521 QII 523
Cdd:PRK12775 736 VIL 738
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
249-276 |
1.10e-04 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 44.66 E-value: 1.10e-04
10 20
....*....|....*....|....*...
gi 242124088 249 AIIGGGPAGMSAGIYAKRSGLSCIILEK 276
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEK 28
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
247-281 |
1.50e-04 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 44.46 E-value: 1.50e-04
10 20 30
....*....|....*....|....*....|....*.
gi 242124088 247 DLAIIGGGPAGMSAGIYAKRSGLSCIILEKQG-VGG 281
Cdd:COG1233 5 DVVVIGAGIGGLAAAALLARAGYRVTVLEKNDtPGG 40
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
244-284 |
1.78e-04 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 44.26 E-value: 1.78e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 242124088 244 EDVDLAIIGGGPAGMSAGIYAKRSGLSCIILEKQG-VGGQVA 284
Cdd:PRK07843 6 QEYDVVVVGSGAAGMVAALTAAHRGLSTVVVEKAPhYGGSTA 47
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
246-296 |
1.95e-04 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 44.05 E-value: 1.95e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 242124088 246 VDLAIIGGGPAGMSAGIYAKRSGLSCIILEKQG-VGGQVAltpkVENYPGFT 296
Cdd:COG1232 2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDrVGGLIR----TVEVDGFR 49
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
245-285 |
2.02e-04 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 44.07 E-value: 2.02e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 242124088 245 DVDLAIIGGGPAGMSAGIYAKRSGLSCIILEKqgvgGQVAL 285
Cdd:PRK05329 2 KFDVLVIGGGLAGLTAALAAAEAGKRVALVAK----GQGAL 38
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
247-351 |
2.19e-04 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 43.72 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 247 DLAIIGGGPAGMSAGIYAKRSGLSCIILEK-QGVGGQVALTPK---------------VENYPG-----------FTNIQ 299
Cdd:pfam03486 2 DVIVIGGGAAGLMAAISAAKRGRRVLLIEKgKKLGRKILISGGgrcnvtnlseepdnfLSRYPGnpkflksalsrFTPWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 300 GFELVEILG------SHAREYTD-------------------IQQF--AEVKDVKY--GPRIEITTDEKNYRAKGVLLAT 350
Cdd:pfam03486 82 FIAFFESLGvplkeeDHGRLFPDsdkasdivdallnelkelgVKIRlrTRVLSVEKddDGRFRVKTGGEELEADSLVLAT 161
|
.
gi 242124088 351 G 351
Cdd:pfam03486 162 G 162
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
246-294 |
2.60e-04 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 43.91 E-value: 2.60e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 242124088 246 VDLAIIGGGPAGMSAGIYAKRSGLSCIILEKQGV-GGQVALTPKVENYPG 294
Cdd:PRK12842 10 CDVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVfGGTTAFSGGVLWIPG 59
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
247-292 |
3.94e-04 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 42.69 E-value: 3.94e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 242124088 247 DLAIIGGGPAGMSAGIYAKRSGLSCIILEKQGVGGQV----ALTPKVENY 292
Cdd:TIGR02032 2 DVVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPRYKpcggALSPRALEE 51
|
|
| COG2509 |
COG2509 |
FAD-dependent dehydrogenase [General function prediction only]; |
214-276 |
5.36e-04 |
|
FAD-dependent dehydrogenase [General function prediction only];
Pssm-ID: 441999 [Multi-domain] Cd Length: 466 Bit Score: 42.79 E-value: 5.36e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 242124088 214 MLQLLFLKPLEEvvEEQRAAKAETTEDTVYEDVDLAIIGGGPAGMSAGIYAKRSGLSCIILEK 276
Cdd:COG2509 1 MIRTNLKLPLDD--EEALKAAIAKKLGIPSLKYDVVIVGAGPAGLFAALELAEAGLKPLVLER 61
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
248-523 |
6.76e-04 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 42.32 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 248 LAIIGGGPAGMSAGIYAKRSGLSCIILEKQ-GVGGQVALtpkvenypgftNIQGFELVEILGSHAREY-----TDIQQFA 321
Cdd:PRK12809 313 VAVIGAGPAGLGCADILARAGVQVDVFDRHpEIGGMLTF-----------GIPPFKLDKTVLSQRREIftamgIDFHLNC 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 322 EV-KDVKYGPRIEittdekNYRAkgVLLATGVNVRM-LGVPGEDK---------FYGH-----GVSYCATCDGNFYKGGK 385
Cdd:PRK12809 382 EIgRDITFSDLTS------EYDA--VFIGVGTYGMMrADLPHEDApgviqalpfLTAHtrqlmGLPESEEYPLTDVEGKR 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 386 AVIVGGGNTALtDALH--LKHLGIETTIVHRGDKFRAEKVLQDSVN--REGINIIWNSQVTEII---------------- 445
Cdd:PRK12809 454 VVVLGGGDTTM-DCLRtsIRLNAASVTCAYRRDEVSMPGSRKEVVNarEEGVEFQFNVQPQYIAcdedgrltavglirta 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 446 ----GEDQVESARIVNkdGTETILDTDVVFVAIGHTAN-TELAEKLGCELRPDGFIKVD-----PTQrTSVERVYAAGDV 515
Cdd:PRK12809 533 mgepGPDGRRRPRPVA--GSEFELPADVLIMAFGFQAHaMPWLQGSGIKLDKWGLIQTGdvgylPTQ-THLKKVFAGGDA 609
|
....*...
gi 242124088 516 TGGVRQII 523
Cdd:PRK12809 610 VHGADLVV 617
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
245-278 |
7.06e-04 |
|
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
Pssm-ID: 396193 [Multi-domain] Cd Length: 348 Bit Score: 41.93 E-value: 7.06e-04
10 20 30
....*....|....*....|....*....|....
gi 242124088 245 DVDLAIIGGGPAGMSAGIYAKRSGLSCIILEKQG 278
Cdd:pfam01494 1 ETDVLIVGGGPAGLMLALLLARAGVRVVLVERHA 34
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
247-282 |
1.09e-03 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 41.23 E-value: 1.09e-03
10 20 30
....*....|....*....|....*....|....*.
gi 242124088 247 DLAIIGGGPAGMSAGIYAKRSGLSCIILEKQGVGGQ 282
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGS 36
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
247-286 |
1.32e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 41.65 E-value: 1.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 242124088 247 DLAIIGGGPAGMSAGIYAKRSGLSCIILEK-QGVGGQVALT 286
Cdd:PRK12843 18 DVIVIGAGAAGMSAALFAAIAGLKVLLVERtEYVGGTTATS 58
|
|
| PRK06185 |
PRK06185 |
FAD-dependent oxidoreductase; |
244-278 |
1.92e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 235729 [Multi-domain] Cd Length: 407 Bit Score: 40.61 E-value: 1.92e-03
10 20 30
....*....|....*....|....*....|....*
gi 242124088 244 EDVDLAIIGGGPAGMSAGIYAKRSGLSCIILEKQG 278
Cdd:PRK06185 5 ETTDCCIVGGGPAGMMLGLLLARAGVDVTVLEKHA 39
|
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
238-286 |
2.59e-03 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 40.56 E-value: 2.59e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 242124088 238 TEDTVYEDVDLAIIGGGPAGMSAGIYAKRSGLSCIILEKQGV-GGQVALT 286
Cdd:PRK12835 4 DEQNFDREVDVLVVGSGGGGMTAALTAAARGLDTLVVEKSAHfGGSTALS 53
|
|
| PLN02976 |
PLN02976 |
amine oxidase |
192-283 |
2.62e-03 |
|
amine oxidase
Pssm-ID: 215527 [Multi-domain] Cd Length: 1713 Bit Score: 41.01 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 242124088 192 SVPHTDINDTVTFTGLEPEEKFMLQllflkpleeVVEEQRAAKAETTEDTVYEDVD---LAIIGGGPAGMSAGIYAKRSG 268
Cdd:PLN02976 646 SPSSSVLDSPETLSVIKPELRNELQ---------SVQSNSCIEMGGNHCVLCDSVDrkkIIVVGAGPAGLTAARHLQRQG 716
|
90
....*....|....*.
gi 242124088 269 LSCIILE-KQGVGGQV 283
Cdd:PLN02976 717 FSVTVLEaRSRIGGRV 732
|
|
| PRK08274 |
PRK08274 |
FAD-dependent tricarballylate dehydrogenase TcuA; |
245-276 |
2.79e-03 |
|
FAD-dependent tricarballylate dehydrogenase TcuA;
Pssm-ID: 236214 [Multi-domain] Cd Length: 466 Bit Score: 40.24 E-value: 2.79e-03
10 20 30
....*....|....*....|....*....|..
gi 242124088 245 DVDLAIIGGGPAGMSAGIYAKRSGLSCIILEK 276
Cdd:PRK08274 4 MVDVLVIGGGNAALCAALAAREAGASVLLLEA 35
|
|
| glycerol3P_GlpB |
TIGR03378 |
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ... |
247-285 |
3.82e-03 |
|
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are the B subunit, product of the glpB gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase. [Energy metabolism, Anaerobic]
Pssm-ID: 213807 Cd Length: 419 Bit Score: 40.00 E-value: 3.82e-03
10 20 30
....*....|....*....|....*....|....*....
gi 242124088 247 DLAIIGGGPAGMSAGIYAKRSGLSCIILEKqgvgGQVAL 285
Cdd:TIGR03378 2 DVIIIGGGLAGLSCALRLAEAGKKCAIIAA----GQSAL 36
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
244-281 |
7.06e-03 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 39.13 E-value: 7.06e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 242124088 244 EDVDLAIIGGGPAGMSAGiYA-KRSGLSCIILEKQG-VGG 281
Cdd:COG1231 6 RGKDVVIVGAGLAGLAAA-RElRKAGLDVTVLEARDrVGG 44
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
246-277 |
8.15e-03 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 38.77 E-value: 8.15e-03
10 20 30
....*....|....*....|....*....|..
gi 242124088 246 VDLAIIGGGPAGMSAGIYAKRSGLSCIILEKQ 277
Cdd:PRK09126 4 SDIVVVGAGPAGLSFARSLAGSGLKVTLIERQ 35
|
|
| |
