|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
1-516 |
0e+00 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 965.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 1 MLDTNLKQQLNGYLQYIVNPIEISVSGNDSDKSAELLALASEIAEMSPKISLT-DGTNARKPSMSIAPQGQAPRVHFAGI 79
Cdd:PRK15317 1 MLDANLKTQLKQYLELLERPIELVASLDDSEKSAELKELLEEIASLSDKITVEeDSLDVRKPSFSITRPGEDTGVRFAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 80 PMGHEFTSLVLALLQSGGHPSKADPAVLEQVKNLKGEFHFETYISLSCHNCPDVVQALNLMSTLNPGITHTMIDGALFQD 159
Cdd:PRK15317 81 PMGHEFTSLVLALLQVGGHPPKLDQEVIEQIKALDGDFHFETYVSLSCHNCPDVVQALNLMAVLNPNITHTMIDGALFQD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 160 EVNERQIMAVPNVYLNGQPFSQGRISLEEIVAKLDTGAAERKAQELSEKAPYDMLVVGGGPAGAAAAIYAARKGIRTAIV 239
Cdd:PRK15317 161 EVEARNIMAVPTVFLNGEEFGQGRMTLEEILAKLDTGAAARAAEELNAKDPYDVLVVGGGPAGAAAAIYAARKGIRTGIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 240 AERFGGQVMDTVGIENFISVPYTEGPKLAASLEQHVKQYGVEVITEQRAAAISK-DGYVNVDLASGATLKSRAVILATGA 318
Cdd:PRK15317 241 AERFGGQVLDTMGIENFISVPETEGPKLAAALEEHVKEYDVDIMNLQRASKLEPaAGLIEVELANGAVLKAKTVILATGA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 319 RWRDLNVPGELEYRTKGVAYCPHCDGPFFKGKRVAVIGGGNSGIEAAIDLAGIVEHVTVVEFADTLRADDVLQKKARSMG 398
Cdd:PRK15317 321 RWRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVKHVTVLEFAPELKADQVLQDKLRSLP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 399 NIDIIMSARTTEVIGDGSKVVGMDYEDRTTGEIKHLAVAGIFVQIGLVPNTEFLKGSeVALTRFGEIEIDTKGATSLPGV 478
Cdd:PRK15317 401 NVTIITNAQTTEVTGDGDKVTGLTYKDRTTGEEHHLELEGVFVQIGLVPNTEWLKGT-VELNRRGEIIVDARGATSVPGV 479
|
490 500 510
....*....|....*....|....*....|....*...
gi 919384098 479 YAAGDATTVPFKQIIISMGAGATAALGAFDYLIRNPAP 516
Cdd:PRK15317 480 FAAGDCTTVPYKQIIIAMGEGAKAALSAFDYLIRNSAA 517
|
|
| AhpF |
TIGR03140 |
alkyl hydroperoxide reductase subunit F; This enzyme is the partner of the peroxiredoxin ... |
1-513 |
0e+00 |
|
alkyl hydroperoxide reductase subunit F; This enzyme is the partner of the peroxiredoxin (alkyl hydroperoxide reductase) AhpC which contains the peroxide-reactive cysteine. AhpF contains the reductant (NAD(P)H) binding domain (pfam00070) and presumably acts to resolve the disulfide which forms after oxidation of the active site cysteine in AphC. This proteins contains two paired conserved cysteine motifs, CxxCP and CxHCDGP. [Cellular processes, Detoxification, Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 274444 [Multi-domain] Cd Length: 515 Bit Score: 779.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 1 MLDTNLKQQLNGYLQYIVNPIEISVSGNDSDKSAELLALASEIAEMSPKISLT--DGTNARKPSMSIAPQGQAPRVHFAG 78
Cdd:TIGR03140 1 MLDQSLLAQLKSYLASLENPVTLVLSAGSHEKSKELLELLDEIASLSDKISLTqnTADTLRKPSFTILRDGADTGIRFAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 79 IPMGHEFTSLVLALLQSGGHPSKADPAVLEQVKNLKGEFHFETYISLSCHNCPDVVQALNLMSTLNPGITHTMIDGALFQ 158
Cdd:TIGR03140 81 IPGGHEFTSLVLAILQVGGHGPKLDEGIIDRIRRLNGPLHFETYVSLTCQNCPDVVQALNQMALLNPNISHTMIDGALFQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 159 DEVNERQIMAVPNVYLNGQPFSQGRISLEEIVAKLDTGAAERKAQELSEKAPYDMLVVGGGPAGAAAAIYAARKGIRTAI 238
Cdd:TIGR03140 161 DEVEALGIQGVPAVFLNGEEFHNGRMDLAELLEKLEETAGVEAASALEQLDPYDVLVVGGGPAGAAAAIYAARKGLRTAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 239 VAERFGGQVMDTVGIENFISVPYTEGPKLAASLEQHVKQYGVEVITEQRAAAISK-DGYVNVDLASGATLKSRAVILATG 317
Cdd:TIGR03140 241 VAERIGGQVKDTVGIENLISVPYTTGSQLAANLEEHIKQYPIDLMENQRAKKIETeDGLIVVTLESGEVLKAKSVIVATG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 318 ARWRDLNVPGELEYRTKGVAYCPHCDGPFFKGKRVAVIGGGNSGIEAAIDLAGIVEHVTVVEFADTLRADDVLQKKARSM 397
Cdd:TIGR03140 321 ARWRKLGVPGEKEYIGKGVAYCPHCDGPFFKGKDVAVIGGGNSGIEAAIDLAGIVRHVTVLEFADELKADKVLQDKLKSL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 398 GNIDIIMSARTTEVIGDGSKVVGMDYEDRTTGEIKHLAVAGIFVQIGLVPNTEFLKGSeVALTRFGEIEIDTKGATSLPG 477
Cdd:TIGR03140 401 PNVDILTSAQTTEIVGDGDKVTGIRYQDRNSGEEKQLDLDGVFVQIGLVPNTEWLKDA-VELNRRGEIVIDERGRTSVPG 479
|
490 500 510
....*....|....*....|....*....|....*.
gi 919384098 478 VYAAGDATTVPFKQIIISMGAGATAALGAFDYLIRN 513
Cdd:TIGR03140 480 IFAAGDVTTVPYKQIIIAMGEGAKAALSAFDYLIRQ 515
|
|
| AhpF |
COG3634 |
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms]; |
1-195 |
1.21e-106 |
|
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];
Pssm-ID: 442851 [Multi-domain] Cd Length: 200 Bit Score: 316.69 E-value: 1.21e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 1 MLDTNLKQQLNGYLQYIVNPIEISVSGNDSDKSAELLALASEIAEMSPKISLT---DGTNARKPSMSIAPQGQAPRVHFA 77
Cdd:COG3634 3 MLDDELKAQLKEYLEKLKNPVELVLFLDDCEKSEELRELLEEIASLSDKISLEvydKDDVERAPSFAILRDGEDTGIRFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 78 GIPMGHEFTSLVLALLQSGGHPSKADPAVLEQVKNLKGEFHFETYISLSCHNCPDVVQALNLMSTLNPGITHTMIDGALF 157
Cdd:COG3634 83 GIPSGHEFTSLVLALLQVSGHPPKLSEETIEQIKALDGPVHFEVFVSLSCPNCPDVVQALNLMAVLNPNITHEMIDGAEF 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 919384098 158 QDEVNERQIMAVPNVYLNGQPFSQGRISLEEIVAKLDT 195
Cdd:COG3634 163 PDEAEKYGVMSVPTVVLNGEVFFVGRMPEEEILEKLDT 200
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
231-496 |
3.33e-85 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 265.83 E-value: 3.33e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 231 RKGIRTAIV-AERFGGQVMDTVGIENFISVPY-TEGPKLAASLEQHVKQYGVEVITEqRAAAISKDG-YVNVDLASGATL 307
Cdd:COG0492 21 RAGLKTLVIeGGEPGGQLATTKEIENYPGFPEgISGPELAERLREQAERFGAEILLE-EVTSVDKDDgPFRVTTDDGTEY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 308 KSRAVILATGARWRDLNVPGELEYRTKGVAYCPHCDGPFFKGKRVAVIGGGNSGIEAAIDLAGIVEHVTVVEFADTLRAD 387
Cdd:COG0492 100 EAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYLTKFASKVTLIHRRDELRAS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 388 DVLQKKARSMGNIDIIMSARTTEVIGDGsKVVGMDYEDRTTGEIKHLAVAGIFVQIGLVPNTEFLKGSEVALTRFGEIEI 467
Cdd:COG0492 180 KILVERLRANPKIEVLWNTEVTEIEGDG-RVEGVTLKNVKTGEEKELEVDGVFVAIGLKPNTELLKGLGLELDEDGYIVV 258
|
250 260
....*....|....*....|....*....
gi 919384098 468 DTKGATSLPGVYAAGDATTVPFKQIIISM 496
Cdd:COG0492 259 DEDMETSVPGVFAAGDVRDYKYRQAATAA 287
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
231-495 |
7.19e-70 |
|
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: 225.97 E-value: 7.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 231 RKGIRTAIVaERF--GGQVMDTVGIENFISVP-YTEGPKLAASLEQHVKQYGVEVITEQRAAAISKDGYVNVDLASGATL 307
Cdd:TIGR01292 20 RANLKPLLI-EGMepGGQLTTTTEVENYPGFPeGISGPELMEKMKEQAVKFGAEIIYEEVIKVDKSDRPFKVYTGDGKEY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 308 KSRAVILATGARWRDLNVPGELEYRTKGVAYCPHCDGPFFKGKRVAVIGGGNSGIEAAIDLAGIVEHVTVVEFADTLRAD 387
Cdd:TIGR01292 99 TAKAVIIATGASARKLGIPGEDEFWGRGVSYCATCDGPFFKNKEVAVVGGGDSAIEEALYLTRIAKKVTLVHRRDKFRAE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 388 DVLQKKARSMGNIDIIMSARTTEVIGDgSKVVGMDYEDRTTGEIKHLAVAGIFVQIGLVPNTEFLKGsEVALTRFGEIEI 467
Cdd:TIGR01292 179 KILLDRLKKNPKIEFLWNSTVEEIVGD-NKVEGVKIKNTVTGEEEELEVDGVFIAIGHEPNTELLKG-LLELDENGYIVT 256
|
250 260
....*....|....*....|....*...
gi 919384098 468 DTKGATSLPGVYAAGDATTVPFKQIIIS 495
Cdd:TIGR01292 257 DEGMRTSVPGVFAAGDVRDKGYRQAVTA 284
|
|
| AhpF_NTD_C |
cd03026 |
TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) ... |
105-192 |
1.19e-50 |
|
TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) subfamily, C-terminal TRX-fold subdomain; AhpF is a homodimeric flavoenzyme which catalyzes the NADH-dependent reduction of the peroxiredoxin AhpC, which then reduces hydrogen peroxide and organic hydroperoxides. AhpF contains an NTD containing two contiguous TRX-fold subdomains similar to Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO). It also contains a catalytic core similar to TRX reductase containing FAD and NADH binding domains with an active site disulfide. The proposed mechanism of action of AhpF is similar to a TRX/TRX reductase system. The flow of reducing equivalents goes from NADH -> catalytic core of AhpF -> NTD of AhpF -> AhpC -> peroxide substrates. The catalytic CXXC motif of the NTD of AhpF is contained in its C-terminal TRX subdomain.
Pssm-ID: 239324 [Multi-domain] Cd Length: 89 Bit Score: 168.24 E-value: 1.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 105 AVLEQVKNLKGEFHFETYISLSCHNCPDVVQALNLMSTLNPGITHTMIDGALFQDEVNERQIMAVPNVYLNGQPFSQGRI 184
Cdd:cd03026 2 DLLEQIRRLNGPINFETYVSLSCHNCPDVVQALNLMAVLNPNIEHEMIDGALFQDEVEERGIMSVPAIFLNGELFGFGRM 81
|
....*...
gi 919384098 185 SLEEIVAK 192
Cdd:cd03026 82 TLEEILAK 89
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
231-483 |
2.31e-43 |
|
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: 155.94 E-value: 2.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 231 RKGIRTAIVAER---FGGQVMDTVGIENFISVPYT--EGPKLAASLEQHVKQYGVEVITEQRAAAISKD---GYV---NV 299
Cdd:pfam07992 21 QLGGKVTLIEDEgtcPYGGCVLSKALLGAAEAPEIasLWADLYKRKEEVVKKLNNGIEVLLGTEVVSIDpgaKKVvleEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 300 DLASGATLKSRAVILATGARWRDLNVPGELEYRTKGVAYCPHCDGPFFK--GKRVAVIGGGNSGIEAAIDLAGIVEHVTV 377
Cdd:pfam07992 101 VDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKllPKRVVVVGGGYIGVELAAALAKLGKEVTL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 378 VEFADTL------RADDVLQKKARSMGnIDIIMSARTTEVIGDGSKVvgmdyeDRTTGEIKHLAVAGIFVQIGLVPNTEF 451
Cdd:pfam07992 181 IEALDRLlrafdeEISAALEKALEKNG-VEVRLGTSVKEIIGDGDGV------EVILKDGTEIDADLVVVAIGRRPNTEL 253
|
250 260 270
....*....|....*....|....*....|..
gi 919384098 452 LKGSEVALTRFGEIEIDTKGATSLPGVYAAGD 483
Cdd:pfam07992 254 LEAAGLELDERGGIVVDEYLRTSVPGIYAAGD 285
|
|
| AhpF_NTD_N |
cd02974 |
Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) family, N-terminal ... |
1-93 |
8.99e-40 |
|
Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) family, N-terminal TRX-fold subdomain; AhpF is a homodimeric flavoenzyme which catalyzes the NADH-dependent reduction of the peroxiredoxin AhpC, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. AhpF contains an NTD forming two contiguous TRX-fold subdomain similar to Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO). It also contains a catalytic core similar to TRX reductase containing FAD and NADH binding domains with an active site disulfide. The proposed mechanism of action of AhpF is similar to a TRX/TRX reductase system. The flow of reducing equivalents goes from NADH -> catalytic core of AhpF -> NTD of AhpF -> AhpC -> peroxide substrates. The N-terminal TRX-fold subdomain of AhpF NTD is redox inactive, but is proposed to contain an important residue that aids in the catalytic function of the redox-active CXXC motif contained in the C-terminal TRX-fold subdomain.
Pssm-ID: 239272 [Multi-domain] Cd Length: 94 Bit Score: 139.25 E-value: 8.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 1 MLDTNLKQQLNGYLQYIVNPIEISVSGNDSDKSAELLALASEIAEMSPKISL-TDGTNARKPSMSIAPQGQAPRVHFAGI 79
Cdd:cd02974 1 MLDANLKQQLKAYLERLENPVELVASLDDSEKSAELLELLEEIASLSDKITLeEDNDDERKPSFSINRPGEDTGIRFAGI 80
|
90
....*....|....
gi 919384098 80 PMGHEFTSLVLALL 93
Cdd:cd02974 81 PMGHEFTSLVLALL 94
|
|
| AhpF_homolog |
TIGR03143 |
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase ... |
211-493 |
2.64e-37 |
|
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: 144.92 E-value: 2.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 211 YDMLVVGGGPAGAAAAIYAARKGIRTAIV-AERFGGQVMDTVGIENFISVPYTEGPKLAASLEQHVKQYGVEVITEQrAA 289
Cdd:TIGR03143 5 YDLIIIGGGPAGLSAGIYAGRAKLDTLIIeKDDFGGQITITSEVVNYPGILNTTGPELMQEMRQQAQDFGVKFLQAE-VL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 290 AISKDGYVNVDLASGATLKSRAVILATGARWRDLNVPGELEYRTKGVAYCPHCDGPFFKGKRVAVIGGGNSGIEAAIDLA 369
Cdd:TIGR03143 84 DVDFDGDIKTIKTARGDYKTLAVLIATGASPRKLGFPGEEEFTGRGVAYCATCDGEFFTGMDVFVIGGGFAAAEEAVFLT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 370 GIVEHVTVVEFADTLRADDVLQKKARSMGNIDIIMSARTTEVIGDGsKVVGMDYEDRTTGEI------KHLAVAGIFVQI 443
Cdd:TIGR03143 164 RYASKVTVIVREPDFTCAKLIAEKVKNHPKIEVKFNTELKEATGDD-GLRYAKFVNNVTGEIteykapKDAGTFGVFVFV 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 919384098 444 GLVPNTEFLKGsEVALTRFGEIEIDTKGATSLPGVYAAGDATTVPFKQII 493
Cdd:TIGR03143 243 GYAPSSELFKG-VVELDKRGYIPTNEDMETNVPGVYAAGDLRPKELRQVV 291
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
244-495 |
3.80e-32 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 125.94 E-value: 3.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 244 GGQVMDTVGIENFISVPYT-EGPKLAASLEQHVKQYGVEVITEQRAAAISKDGYVNVDLASGAtLKSRAVILATGARWRD 322
Cdd:PRK10262 41 GGQLTTTTEVENWPGDPNDlTGPLLMERMHEHATKFETEIIFDHINKVDLQNRPFRLTGDSGE-YTCDALIIATGASARY 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 323 LNVPGELEYRTKGVAYCPHCDGPFFKGKRVAVIGGGNSGIEAAIDLAGIVEHVTVVEFADTLRADDVLQKKAR---SMGN 399
Cdd:PRK10262 120 LGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDGFRAEKILIKRLMdkvENGN 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 400 IDIIMSARTTEVIGDGSKVVGMDYED-RTTGEIKHLAVAGIFVQIGLVPNTEFLKGSEVALTRFGEIEIDTKG---ATSL 475
Cdd:PRK10262 200 IILHTNRTLEEVTGDQMGVTGVRLRDtQNSDNIESLDVAGLFVAIGHSPNTAIFEGQLELENGYIKVQSGIHGnatQTSI 279
|
250 260
....*....|....*....|
gi 919384098 476 PGVYAAGDATTVPFKQIIIS 495
Cdd:PRK10262 280 PGVFAAGDVMDHIYRQAITS 299
|
|
| AhpF_homolog |
TIGR03143 |
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase ... |
1-190 |
3.28e-31 |
|
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: 127.20 E-value: 3.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 1 MLDTNLKQQLNGYLQYIVNPIEISVSGNDSD-KSAELLALASEIAEMSPKI---SLTDGTNA---------RKPSMSI-A 66
Cdd:TIGR03143 348 LLDDSLRQQLVGIFGRLENPVTLLLFLDGSNeKSAELQSFLGEFASLSEKLnseAVNRGEEPesetlpkitKLPTVALlD 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 67 PQGQAPRVHFAGIPMGHEFTSLVLALLQSGGHPSKADPAVLEQVKNLKGEFHFETYISLSCHNCPDVVQALNLMSTLNPG 146
Cdd:TIGR03143 428 DDGNYTGLKFHGVPSGHELNSFILALYNAAGPGQPLGEELLEKIKKITKPVNIKIGVSLSCTLCPDVVLAAQRIASLNPN 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 919384098 147 ITHTMIDGALFQDEVNERQIMAVPNVYLNGQPFSQGRISLEEIV 190
Cdd:TIGR03143 508 VEAEMIDVSHFPDLKDEYGIMSVPAIVVDDQQVYFGKKTIEEML 551
|
|
| TRX_GRX_like |
cd02973 |
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins ... |
117-183 |
5.98e-30 |
|
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: 111.51 E-value: 5.98e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 919384098 117 FHFETYISLSCHNCPDVVQALNLMSTLNPGITHTMIDGALFQDEVNERQIMAVPNVYLNGQPFSQGR 183
Cdd:cd02973 1 VNIEVFVSPTCPYCPDAVQAANRIAALNPNISAEMIDAAEFPDLADEYGVMSVPAIVINGKVEFVGR 67
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
272-488 |
1.15e-27 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 114.85 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 272 EQHVKQYGVEVITEQRAAAISKDGYVnVDLASGATLKSRAVILATGARWRDLNVPG-ELE----YRTKG-----VAYCPh 341
Cdd:COG1251 63 ADFYEENGIDLRLGTRVTAIDRAART-VTLADGETLPYDKLVLATGSRPRVPPIPGaDLPgvftLRTLDdadalRAALA- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 342 cdgpffKGKRVAVIGGGNSGIEAAIDLAGIVEHVTVVEFADTL-------RADDVLQKKARSMGnIDIIMSARTTEVIGD 414
Cdd:COG1251 141 ------PGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLlprqldeEAGALLQRLLEALG-VEVRLGTGVTEIEGD 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 919384098 415 GsKVVGMDYEDRTTgeikhLAVAGIFVQIGLVPNTEFLKGSEVALTRfGeIEIDTKGATSLPGVYAAGDATTVP 488
Cdd:COG1251 214 D-RVTGVRLADGEE-----LPADLVVVAIGVRPNTELARAAGLAVDR-G-IVVDDYLRTSDPDIYAAGDCAEHP 279
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
266-489 |
1.20e-26 |
|
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: 110.29 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 266 KLAASLEQHVKQYGVEVITEQRAAAISKDGYVnVDLASGATLKSRAVILATGARWRDLNVPGeleYRTKGVAYCPHCDG- 344
Cdd:COG0446 37 DLLVRTPESFERKGIDVRTGTEVTAIDPEAKT-VTLRDGETLSYDKLVLATGARPRPPPIPG---LDLPGVFTLRTLDDa 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 345 -------PFFKGKRVAVIGGGNSGIEAAIDL--AGIveHVTVVEFADTL--RAD----DVLQKKARSMGnIDIIMSARTT 409
Cdd:COG0446 113 dalrealKEFKGKRAVVIGGGPIGLELAEALrkRGL--KVTLVERAPRLlgVLDpemaALLEEELREHG-VELRLGETVV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 410 EVIGDGSKVVgmdyedRTT--GEIK--HLAVAgifvqIGLVPNTEFLKGSEVALTRFGEIEIDTKGATSLPGVYAAGDAT 485
Cdd:COG0446 190 AIDGDDKVAV------TLTdgEEIPadLVVVA-----PGVRPNTELAKDAGLALGERGWIKVDETLQTSDPDVYAAGDCA 258
|
....
gi 919384098 486 TVPF 489
Cdd:COG0446 259 EVPH 262
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
273-486 |
1.22e-20 |
|
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: 94.43 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 273 QHVKQYGVEVITEQRaaaiskdgyVNVDLaSGATLKSR--AVILATGA-RWRDLNVPGE--------LEY---RTKGVAY 338
Cdd:COG0493 179 ELIEALGVEFRTNVE---------VGKDI-TLDELLEEfdAVFLATGAgKPRDLGIPGEdlkgvhsaMDFltaVNLGEAP 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 339 cphcDGPFFKGKRVAVIGGGNSgieaAIDLAGI-----VEHVTVVEF--ADTLRADDVLQKKARSMGnIDIIMSARTTEV 411
Cdd:COG0493 249 ----DTILAVGKRVVVIGGGNT----AMDCARTalrlgAESVTIVYRrtREEMPASKEEVEEALEEG-VEFLFLVAPVEI 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 412 IGD-GSKVVGMDYED---------------RTTGEIKHLAVAGIFVQIGLVPNTEFLKGS-EVALTRFGEIEIDTK-GAT 473
Cdd:COG0493 320 IGDeNGRVTGLECVRmelgepdesgrrrpvPIEGSEFTLPADLVILAIGQTPDPSGLEEElGLELDKRGTIVVDEEtYQT 399
|
250
....*....|...
gi 919384098 474 SLPGVYAAGDATT 486
Cdd:COG0493 400 SLPGVFAGGDAVR 412
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
266-485 |
8.51e-20 |
|
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: 92.07 E-value: 8.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 266 KLAASLEQHVKQYGVEVITEQraAAISKDGYVNVDlaSGATLKSRAVILATGARWRDLNVPGELEYR---TKGV---AYC 339
Cdd:COG1249 92 RLRGGVEELLKKNGVDVIRGR--ARFVDPHTVEVT--GGETLTADHIVIATGSRPRVPPIPGLDEVRvltSDEAlelEEL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 340 PhcdgpffkgKRVAVIGGGNSGIEaaidLAGI-----VEhVTVVEFADTL--RAD----DVLQKKARSMGnIDIIMSART 408
Cdd:COG1249 168 P---------KSLVVIGGGYIGLE----FAQIfarlgSE-VTLVERGDRLlpGEDpeisEALEKALEKEG-IDILTGAKV 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 409 TEVIGDGSKVVgMDYEDRttGEIKHLAVAGIFVQIGLVPNTEFLkGSE---VALTRFGEIEIDTKGATSLPGVYAAGDAT 485
Cdd:COG1249 233 TSVEKTGDGVT-VTLEDG--GGEEAVEADKVLVATGRRPNTDGL-GLEaagVELDERGGIKVDEYLRTSVPGIYAIGDVT 308
|
|
| GlrX_arch |
TIGR02187 |
Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal ... |
13-178 |
6.39e-19 |
|
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: 85.57 E-value: 6.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 13 YLQYIVNPIEISVSgNDSDKSA-----ELLALASEIAEMSPKISLT----DGTNARK----------PSMSIAPQGQAPR 73
Cdd:TIGR02187 13 FLKELKNPVEIVVF-TDNDKEGcqyckETEQLLEELSEVSPKLKLEiydfDTPEDKEeaekygvervPTTIILEEGKDGG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 74 VHFAGIPMGHEFTSLVLALLQSGGHPSKADPAVLEQVKNLKGEFHFETYISLSCHNCPDVVQALNLMSTLNPGITHTMID 153
Cdd:TIGR02187 92 IRYTGIPAGYEFAALIEDIVRVSQGEPGLSEKTVELLQSLDEPVRIEVFVTPTCPYCPYAVLMAHKFALANDKILGEMIE 171
|
170 180
....*....|....*....|....*
gi 919384098 154 GALFQDEVNERQIMAVPNVYLNGQP 178
Cdd:TIGR02187 172 ANENPDLAEKYGVMSVPKIVINKGV 196
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
265-486 |
5.53e-18 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 86.39 E-value: 5.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 265 PK-LAASLEQHVKQYGVEVITEQraaAISKDgyvnvdlASGATLKSR--AVILATGA-RWRDLNVPGE--------LEY- 331
Cdd:PRK11749 189 PKdIVDREVERLLKLGVEIRTNT---EVGRD-------ITLDELRAGydAVFIGTGAgLPRFLGIPGEnlggvysaVDFl 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 332 -RTKGVAYcphcDGPFFKGKRVAVIGGGNSgieaAIDLAGI-----VEHVTVV---EFADtLRADDVLQKKARSMGnIDI 402
Cdd:PRK11749 259 tRVNQAVA----DYDLPVGKRVVVIGGGNT----AMDAARTakrlgAESVTIVyrrGREE-MPASEEEVEHAKEEG-VEF 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 403 IMSARTTEVIGDGSKVVGMDYEdRT---------------TGEIKHLAVAGIFVQIGLVPNTEFLKGS-EVALTRFGEIE 466
Cdd:PRK11749 329 EWLAAPVEILGDEGRVTGVEFV-RMelgepdasgrrrvpiEGSEFTLPADLVIKAIGQTPNPLILSTTpGLELNRWGTII 407
|
250 260
....*....|....*....|.
gi 919384098 467 IDTK-GATSLPGVYAAGDATT 486
Cdd:PRK11749 408 ADDEtGRTSLPGVFAGGDIVT 428
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
266-485 |
1.95e-17 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 84.81 E-value: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 266 KLAASLEQHVKQYGVEVIteQRAAAISKDGYVNVDLASGA-TLKSRAVILATGARWRDLnvPGeLEYRTKGVAYCPHCDG 344
Cdd:PRK06416 93 RLTGGVEGLLKKNKVDII--RGEAKLVDPNTVRVMTEDGEqTYTAKNIILATGSRPREL--PG-IEIDGRVIWTSDEALN 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 345 PFFKGKRVAVIGGGNSGIEAAIDLAGIVEHVTVVEFADTLRA--D----DVLQKKARSMGnIDIIMSARTTEVIgDGSKV 418
Cdd:PRK06416 168 LDEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPgeDkeisKLAERALKKRG-IKIKTGAKAKKVE-QTDDG 245
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 419 VGMDYEDrtTGEIKHLAVAGIFVQIGLVPNTEFLkGSE---VALTRfGEIEIDTKGATSLPGVYAAGDAT 485
Cdd:PRK06416 246 VTVTLED--GGKEETLEADYVLVAVGRRPNTENL-GLEelgVKTDR-GFIEVDEQLRTNVPNIYAIGDIV 311
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
308-490 |
9.35e-14 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 72.71 E-value: 9.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 308 KSRAVILATGA-RWRDLNVPGE--------LEY--RTKGV--AYCPHCDGPFFKGKRVAVIGGGNSGIEAAID--LAGiV 372
Cdd:PRK12770 118 KYDAVLIATGTwKSRKLGIPGEdlpgvysaLEYlfRIRAAklGYLPWEKVPPVEGKKVVVVGAGLTAVDAALEavLLG-A 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 373 EHVTVVeFADTLR---ADDVLQKKARSMGnIDIIMSARTTEVIGDGS---------KVVGMDYEDR-----TTGEIKHLA 435
Cdd:PRK12770 197 EKVYLA-YRRTINeapAGKYEIERLIARG-VEFLELVTPVRIIGEGRvegvelakmRLGEPDESGRprpvpIPGSEFVLE 274
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 919384098 436 VAGIFVQIGLVPNTEFLKGS-EVALTRFGEIEIDTKGATSLPGVYAAGDATTVPFK 490
Cdd:PRK12770 275 ADTVVFAIGEIPTPPFAKEClGIELNRKGEIVVDEKHMTSREGVFAAGDVVTGPSK 330
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
294-488 |
1.23e-13 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 72.90 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 294 DGYVNVDlasGATLKSRAVILATGARwrDLNVPGELE------YRTKGVAYCPHCdgPffkgKRVAVIGGGNSGIEAAID 367
Cdd:PRK06292 119 PNTVEVN---GERIEAKNIVIATGSR--VPPIPGVWLilgdrlLTSDDAFELDKL--P----KSLAVIGGGVIGLELGQA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 368 LAGIVEHVTVVEFADTL--RADDVLQKKARSM--GNIDIIMSARTTEVIGDGSKVVGmdyEDRTTGEIKHLAVAGIFVQI 443
Cdd:PRK06292 188 LSRLGVKVTVFERGDRIlpLEDPEVSKQAQKIlsKEFKIKLGAKVTSVEKSGDEKVE---ELEKGGKTETIEADYVLVAT 264
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 919384098 444 GLVPNTEFLKGSE--VALTRFGEIEIDTKGATSLPGVYAAGDATTVP 488
Cdd:PRK06292 265 GRRPNTDGLGLENtgIELDERGRPVVDEHTQTSVPGIYAAGDVNGKP 311
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
307-485 |
2.13e-13 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 72.09 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 307 LKSRAVILATGARWRDLNVPGELE----YRTKGVAYCPHcdgpffKGKRVAVIGGGNSGIEAAIDLAGIVEHVTVVEFAD 382
Cdd:PRK07251 117 LTAETIVINTGAVSNVLPIPGLADskhvYDSTGIQSLET------LPERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAAS 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 383 TL--RADDVLQKKAR----SMGnIDIIMSARTTEVIGDGSKVVgmdyedrTTGEIKHLAVAGIFVQIGLVPNTE--FLKG 454
Cdd:PRK07251 191 TIlpREEPSVAALAKqymeEDG-ITFLLNAHTTEVKNDGDQVL-------VVTEDETYRFDALLYATGRKPNTEplGLEN 262
|
170 180 190
....*....|....*....|....*....|.
gi 919384098 455 SEVALTRFGEIEIDTKGATSLPGVYAAGDAT 485
Cdd:PRK07251 263 TDIELTERGAIKVDDYCQTSVPGVFAVGDVN 293
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
350-487 |
4.37e-13 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 71.22 E-value: 4.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 350 KRVAVIGGGNSGIEAAIDLAGIVEHVTVVEFADTLRAD-------DVLQKKARSMGnIDIIMSARTTEVIGDGsKVVGMd 422
Cdd:PRK09564 150 KNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLEDRILPDsfdkeitDVMEEELRENG-VELHLNEFVKSLIGED-KVEGV- 226
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919384098 423 yedRTT-GEIKHLAVagiFVQIGLVPNTEFLKGSEVALTRFGEIEIDTKGATSLPGVYAAGDATTV 487
Cdd:PRK09564 227 ---VTDkGEYEADVV---IVATGVKPNTEFLEDTGLKTLKNGAIIVDEYGETSIENIYAAGDCATI 286
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
351-419 |
4.45e-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: 64.53 E-value: 4.45e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 919384098 351 RVAVIGGGNSGIEAAIDLAGIVEHVTVVEFADTLR------ADDVLQKKARSMGnIDIIMSARTTEVIGDGSKVV 419
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLpgfdpeIAKILQEKLEKNG-IEFLLNTTVEAIEGNGDGVV 74
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
271-378 |
2.72e-12 |
|
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: 68.74 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 271 LEQHVkQYGVEViteQRAAAISKDGYVNVDLASGATLKSRAVILATGArWRDLNVP---GELEYrtKGVAYcpHC---DG 344
Cdd:COG2072 95 LRRPI-RFGTEV---TSARWDEADGRWTVTTDDGETLTARFVVVATGP-LSRPKIPdipGLEDF--AGEQL--HSadwRN 165
|
90 100 110
....*....|....*....|....*....|....*
gi 919384098 345 PF-FKGKRVAVIGGGNSGIEAAIDLAGIVEHVTVV 378
Cdd:COG2072 166 PVdLAGKRVLVVGTGASAVQIAPELARVAAHVTVF 200
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
256-482 |
4.91e-12 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 66.86 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 256 FISVPYTEGPKLAASLEQHVKQYGVEVITEQRAAAISK--DGYVnVDlASGATLKSRAVILATGaRWRDLNVPGELEYRt 333
Cdd:pfam13738 66 TFNREHPSGNEYAEYLRRVADHFELPINLFEEVTSVKKedDGFV-VT-TSKGTYQARYVIIATG-EFDFPNKLGVPELP- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 334 KGVAYCPHCDgPFFkGKRVAVIGGGNSGIEAAIDLAGIVEHVTVV---EFADTLRAD-------DVLQ--KKARSMGNID 401
Cdd:pfam13738 142 KHYSYVKDFH-PYA-GQKVVVIGGYNSAVDAALELVRKGARVTVLyrgSEWEDRDSDpsyslspDTLNrlEELVKNGKIK 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 402 IIMSARTTEVIGDGSKVVgMDYEDRTTGEIKHLAVAGifvqIGLVPNTEFLKGSEVALTRFGEIEIDTKG-ATSLPGVYA 480
Cdd:pfam13738 220 AHFNAEVKEITEVDVSYK-VHTEDGRKVTSNDDPILA----TGYHPDLSFLKKGLFELDEDGRPVLTEETeSTNVPGLFL 294
|
..
gi 919384098 481 AG 482
Cdd:pfam13738 295 AG 296
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
294-485 |
1.43e-10 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 63.41 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 294 DGY-VNVDLASGATLKSRAVILATGARWRDL-NVP----------GELEYRTkgvayCPhcdgpffkgKRVAVIGGGNSG 361
Cdd:PRK06327 130 AGYeIKVTGEDETVITAKHVIIATGSEPRHLpGVPfdnkiildntGALNFTE-----VP---------KKLAVIGAGVIG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 362 IEAAIDLAGIVEHVTVVEFADTL--RADDVLQK---KARSMGNIDIIMSARTTEvIGDGSKVVGMDYEDRTtGEIKHLAV 436
Cdd:PRK06327 196 LELGSVWRRLGAEVTILEALPAFlaAADEQVAKeaaKAFTKQGLDIHLGVKIGE-IKTGGKGVSVAYTDAD-GEAQTLEV 273
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 919384098 437 AGIFVQIGLVPNTEFLkGSE---VALTRFGEIEIDTKGATSLPGVYAAGDAT 485
Cdd:PRK06327 274 DKLIVSIGRVPNTDGL-GLEavgLKLDERGFIPVDDHCRTNVPNVYAIGDVV 324
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
310-486 |
1.47e-10 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 63.50 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 310 RAVILATGARW-RDLNVPGEL--------EYRTK---GVAYCPHCDGPFFKGKRVAVIGGGNSGIEAAIDLAGIVEHVTV 377
Cdd:PRK12831 230 DAVFIGSGAGLpKFMGIPGENlngvfsanEFLTRvnlMKAYKPEYDTPIKVGKKVAVVGGGNVAMDAARTALRLGAEVHI 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 378 V----EFADTLRADDVlqKKARSMGnidIIMSART--TEVIGD------GSKVVGMDYEDR----------TTGEIKHLA 435
Cdd:PRK12831 310 VyrrsEEELPARVEEV--HHAKEEG---VIFDLLTnpVEILGDengwvkGMKCIKMELGEPdasgrrrpveIEGSEFVLE 384
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 919384098 436 VAGIFVQIGLVPN---TEFLKGSEValTRFGEIEID-TKGATSLPGVYAAGDATT 486
Cdd:PRK12831 385 VDTVIMSLGTSPNpliSSTTKGLKI--NKRGCIVADeETGLTSKEGVFAGGDAVT 437
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
234-483 |
1.94e-10 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 63.60 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 234 IRTAIVAERFGGQVMDTVGIENFISVPYTEGPKLA------ASLEQH--------VKQ-----YGVEVITEQRAAAISKD 294
Cdd:PRK14989 9 IGNGMVGHRFIEDLLDKADAANFDITVFCEEPRIAydrvhlSSYFSHhtaeelslVREgfyekHGIKVLVGERAITINRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 295 GYVnVDLASGATLKSRAVILATGAR-W---------RDLNVpgeleYRT----KGVAYCPHcdgpffKGKRVAVIGGGNS 360
Cdd:PRK14989 89 EKV-IHSSAGRTVFYDKLIMATGSYpWippikgsetQDCFV-----YRTiedlNAIEACAR------RSKRGAVVGGGLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 361 GIEAAIDLA--GIVEHvtVVEFADTLRAD-------DVLQKKARSMGnIDIIMSARTTEVIGDGSKVVG-MDYEDRTTge 430
Cdd:PRK14989 157 GLEAAGALKnlGVETH--VIEFAPMLMAEqldqmggEQLRRKIESMG-VRVHTSKNTLEIVQEGVEARKtMRFADGSE-- 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 919384098 431 ikhLAVAGIFVQIGLVPNTEFLKGSEVALTRFGEIEIDTKGATSLPGVYAAGD 483
Cdd:PRK14989 232 ---LEVDFIVFSTGIRPQDKLATQCGLAVAPRGGIVINDSCQTSDPDIYAIGE 281
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
297-484 |
1.62e-09 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 60.18 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 297 VNVDLaSGATLKSR--AVILATGA-RWRDLNVPGE--------LEY---RTKGVAycPHCDGPFF--KGKRVAVIGGGNS 360
Cdd:PRK12810 216 VGKDI-TAEELLAEydAVFLGTGAyKPRDLGIPGRdldgvhfaMDFliqNTRRVL--GDETEPFIsaKGKHVVVIGGGDT 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 361 GIEA---AIDL-AgivEHVTVVEFAD---TLRADDVL---------QKKARSMGnIDIIMSARTTEVIGDGSKVVGMDYE 424
Cdd:PRK12810 293 GMDCvgtAIRQgA---KSVTQRDIMPmppSRRNKNNPwpywpmkleVSNAHEEG-VEREFNVQTKEFEGENGKVTGVKVV 368
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919384098 425 DRTTGEIKHLAVAG---------IFVQIGLV-PNTEFLKGSEVALTRFGEIEIDTKG-ATSLPGVYAAGDA 484
Cdd:PRK12810 369 RTELGEGDFEPVEGsefvlpadlVLLAMGFTgPEAGLLAQFGVELDERGRVAAPDNAyQTSNPKVFAAGDM 439
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
210-483 |
5.13e-09 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 58.29 E-value: 5.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 210 PYDMLVVGGGPAGAAAAIYAARKGIRTAIVaER--FGGqvmDTVgieNFISVPytegPKL------AASLEQHVKQYGVE 281
Cdd:PRK06370 5 RYDAIVIGAGQAGPPLAARAAGLGMKVALI-ERglLGG---TCV---NTGCVP----TKTliasarAAHLARRAAEYGVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 282 VITE---------QRAAAISKD----------GYVNVDL--------------ASGATLKSRAVILATGARWRDLNVPG- 327
Cdd:PRK06370 74 VGGPvsvdfkavmARKRRIRARsrhgseqwlrGLEGVDVfrgharfespntvrVGGETLRAKRIFINTGARAAIPPIPGl 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 328 -ELEYRTK----GVAYCPhcdgpffkgKRVAVIGGGNSGIEAAIDLAGIVEHVTVVEFADTL--RAD----DVLQKKARS 396
Cdd:PRK06370 154 dEVGYLTNetifSLDELP---------EHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLlpREDedvaAAVREILER 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 397 MGnIDIIMSARTTEVIGDGS-KVVGMDyedrTTGEIKHLAVAGIFVQIGLVPNTEFLkGSE---VALTRFGEIEIDTKGA 472
Cdd:PRK06370 225 EG-IDVRLNAECIRVERDGDgIAVGLD----CNGGAPEITGSHILVAVGRVPNTDDL-GLEaagVETDARGYIKVDDQLR 298
|
330
....*....|.
gi 919384098 473 TSLPGVYAAGD 483
Cdd:PRK06370 299 TTNPGIYAAGD 309
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
277-483 |
1.11e-08 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 57.92 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 277 QYGVEVITEQRAAAISKDGYVnVDLASGATLKSRAVILATGARWRDLNVPGE-----LEYRTkgVAYCPHCDGPFFKGKR 351
Cdd:TIGR02374 66 KHGITLYTGETVIQIDTDQKQ-VITDAGRTLSYDKLILATGSYPFILPIPGAdkkgvYVFRT--IEDLDAIMAMAQRFKK 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 352 VAVIGGGNSGIEAAIDLAGIVEHVTVVEFADTLRADDV-------LQKKARSMGnIDIIMSARTTEVIGDGsKVVGMDYE 424
Cdd:TIGR02374 143 AAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAKQLdqtagrlLQRELEQKG-LTFLLEKDTVEIVGAT-KADRIRFK 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 919384098 425 DRTTgeikhLAVAGIFVQIGLVPNTEFlkGSEVALTRFGEIEIDTKGATSLPGVYAAGD 483
Cdd:TIGR02374 221 DGSS-----LEADLIVMAAGIRPNDEL--AVSAGIKVNRGIIVNDSMQTSDPDIYAVGE 272
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
279-487 |
1.43e-08 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 57.18 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 279 GVEVITEQRAAAISKDG--YVNVDLASGA--TLKSRAVILATGARWRDLnvPGeleyrtkgvaycPHCDG---------- 344
Cdd:PRK07845 106 GVRVIAGRGRLIDPGLGphRVKVTTADGGeeTLDADVVLIATGASPRIL--PT------------AEPDGeriltwrqly 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 345 -----PffkgKRVAVIGGGNSGIEAAIDLAGIVEHVTVV---------EFADtlrADDVLQKKARSMGnIDIIMSAR--T 408
Cdd:PRK07845 172 dldelP----EHLIVVGSGVTGAEFASAYTELGVKVTLVssrdrvlpgEDAD---AAEVLEEVFARRG-MTVLKRSRaeS 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 409 TEVIGDGSKVVgmdYEDRTTGEIKHLAVAgifvqIGLVPNTEFLkGSE---VALTRFGEIEIDTKGATSLPGVYAAGDAT 485
Cdd:PRK07845 244 VERTGDGVVVT---LTDGRTVEGSHALMA-----VGSVPNTAGL-GLEeagVELTPSGHITVDRVSRTSVPGIYAAGDCT 314
|
..
gi 919384098 486 TV 487
Cdd:PRK07845 315 GV 316
|
|
| Thioredoxin_3 |
pfam13192 |
Thioredoxin domain; |
123-193 |
3.38e-08 |
|
Thioredoxin domain;
Pssm-ID: 433026 [Multi-domain] Cd Length: 71 Bit Score: 50.29 E-value: 3.38e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919384098 123 ISLSCHNCPDVVQALNLMSTlNPGITHTMIDGALFQdEVNERQIMAVPNVYLNGQPFSQGRISLEEIVAKL 193
Cdd:pfam13192 1 LGPGCPKCPQLEKAVKEAAA-ELGIDAEVEKVTDFP-EIAKYGVMSTPALVINGKVVSSGKVPSEEEIRKL 69
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
267-488 |
6.21e-08 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 54.75 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 267 LAASLEQHVKQYGVEVITEqRAAAISKDGYVnVDLASGATLKSRAVILATGARWRDLNVPGELEYrtkgvayCPHCDGP- 345
Cdd:COG1252 58 IAIPLRELLRRAGVRFIQG-EVTGIDPEART-VTLADGRTLSYDYLVIATGSVTNFFGIPGLAEH-------ALPLKTLe 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 346 -----------FF------KGKRVAVIGGGNSGIEaaidLAGIVEH-----------------VTVVEFADTL------R 385
Cdd:COG1252 129 dalalrerllaAFeraerrRLLTIVVVGGGPTGVE----LAGELAEllrkllrypgidpdkvrITLVEAGPRIlpglgeK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 386 ADDVLQKKARSMGnIDIIMSARTTEVigDGSKVVgmdYEDRTTGEIKHLAVAGifvqiGLVPNtEFLKGSEVALTRFGEI 465
Cdd:COG1252 205 LSEAAEKELEKRG-VEVHTGTRVTEV--DADGVT---LEDGEEIPADTVIWAA-----GVKAP-PLLADLGLPTDRRGRV 272
|
250 260
....*....|....*....|....
gi 919384098 466 EID-TKGATSLPGVYAAGDATTVP 488
Cdd:COG1252 273 LVDpTLQVPGHPNVFAIGDCAAVP 296
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
313-483 |
2.06e-07 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 53.00 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 313 ILATGARWRDLNVPG-EL--------EYRTkgvaycphCDGPFFKGKRVAVIGGGNSGIEAAIDLAGIVEHVTVVEFADT 383
Cdd:PRK04965 104 VLATGASAFVPPIPGrELmltlnsqqEYRA--------AETQLRDAQRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAAS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 384 LRA----DDV---LQKKARSMGnIDIIMSAR--TTEVIGDGSKVvgmdyedrTTGEIKHLAVAGIFVQIGLVPNTEFLKG 454
Cdd:PRK04965 176 LLAslmpPEVssrLQHRLTEMG-VHLLLKSQlqGLEKTDSGIRA--------TLDSGRSIEVDAVIAAAGLRPNTALARR 246
|
170 180
....*....|....*....|....*....
gi 919384098 455 SEVALTRfGeIEIDTKGATSLPGVYAAGD 483
Cdd:PRK04965 247 AGLAVNR-G-IVVDSYLQTSAPDIYALGD 273
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
311-486 |
4.74e-07 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 52.44 E-value: 4.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 311 AVILATGARW-RDLNVPGE--------LEYRTKG---VAYCPHCDGPFFKGKRVAVIGGGNSGIEA---AIDLAGivEHV 375
Cdd:PRK12778 520 GIFIASGAGLpNFMNIPGEnsngvmssNEYLTRVnlmDAASPDSDTPIKFGKKVAVVGGGNTAMDSartAKRLGA--ERV 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 376 TVV----EFADTLRADDVlqKKARSMGnIDIIMSARTTEVIGD------GSKVVGMDY-EDRTTGEIKHLAVAG------ 438
Cdd:PRK12778 598 TIVyrrsEEEMPARLEEV--KHAKEEG-IEFLTLHNPIEYLADekgwvkQVVLQKMELgEPDASGRRRPVAIPGstftvd 674
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 919384098 439 ---IFVQIGLVPN---TEFLKGSEvaLTRFGEIEIDTKGATSLPGVYAAGDATT 486
Cdd:PRK12778 675 vdlVIVSVGVSPNplvPSSIPGLE--LNRKGTIVVDEEMQSSIPGIYAGGDIVR 726
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
300-490 |
1.44e-06 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 50.72 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 300 DLASGATLKSRAVILATGARWRDLNVPGE--LEYRTKG----VAYCPhcdgpffkgKRVAVIGGGNSGIEAAIDLAGIVE 373
Cdd:PRK07846 120 RTGDGEEITADQVVIAAGSRPVIPPVIADsgVRYHTSDtimrLPELP---------ESLVIVGGGFIAAEFAHVFSALGV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 374 HVTVVEFADT-LRA--DDVLQKKARSMGN-IDIIMSARTTEVIGDGSKV-VGMDYEDRTTGEIkhlavagIFVQIGLVPN 448
Cdd:PRK07846 191 RVTVVNRSGRlLRHldDDISERFTELASKrWDVRLGRNVVGVSQDGSGVtLRLDDGSTVEADV-------LLVATGRVPN 263
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 919384098 449 TEFLKGSE--VALTRFGEIEIDTKGATSLPGVYAAGDATTvPFK 490
Cdd:PRK07846 264 GDLLDAAAagVDVDEDGRVVVDEYQRTSAEGVFALGDVSS-PYQ 306
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
306-485 |
2.67e-06 |
|
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: 49.97 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 306 TLKSRAVILATGARWRDLNVPGeleyrtkgVAYCPHCDGPFF---KGKRVAVIGGGNSGIEaaidLAGIVE-------HV 375
Cdd:TIGR01423 149 RLQAEHILLATGSWPQMLGIPG--------IEHCISSNEAFYldePPRRVLTVGGGFISVE----FAGIFNaykprggKV 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 376 TVVE--------FADTLRADdvLQKKARSMGnIDIIMSARTTEVI--GDGSKVVGMDyedrtTGeiKHLAVAGIFVQIGL 445
Cdd:TIGR01423 217 TLCYrnnmilrgFDSTLRKE--LTKQLRANG-INIMTNENPAKVTlnADGSKHVTFE-----SG--KTLDVDVVMMAIGR 286
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 919384098 446 VPNTEFLK--GSEVALTRFGEIEIDTKGATSLPGVYAAGDAT 485
Cdd:TIGR01423 287 VPRTQTLQldKVGVELTKKGAIQVDEFSRTNVPNIYAIGDVT 328
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
348-492 |
3.79e-06 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 49.40 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 348 KGKRVAVIGGGNSGIEAAIDLAGIVEHVTVVEfadtlraddvlqkkaRSmGNIDIIMSARTTEVIGDGSKVVGMDYE--- 424
Cdd:PRK13512 147 QVDKALVVGAGYISLEVLENLYERGLHPTLIH---------------RS-DKINKLMDADMNQPILDELDKREIPYRlne 210
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 919384098 425 --DRTTGEIKHLAVAG------IFVQIGLVPNTEFLKGSEVALTRFGEIEIDTKGATSLPGVYAAGDATTVPFKQI 492
Cdd:PRK13512 211 eiDAINGNEVTFKSGKvehydmIIEGVGTHPNSKFIESSNIKLDDKGFIPVNDKFETNVPNIYAIGDIITSHYRHV 286
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
306-483 |
4.14e-06 |
|
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.
Pssm-ID: 273624 [Multi-domain] Cd Length: 484 Bit Score: 49.47 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 306 TLKSRAVILATGARWRDLNVPGELEYRTKG-----VAYCPhcdgpffkGKRVaVIGGGNSGIEAAIDLAGIVEHVTVVEF 380
Cdd:TIGR01438 141 IYSAERFLIATGERPRYPGIPGAKELCITSddlfsLPYCP--------GKTL-VVGASYVALECAGFLAGIGLDVTVMVR 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 381 ADTLRADDvlQKKARSMGN---------IDIIMSARTTEvIGDGSKVVGMDYEDRTTGEIKHLAVAgifvqIGLVPNTEF 451
Cdd:TIGR01438 212 SILLRGFD--QDCANKVGEhmeehgvkfKRQFVPIKVEQ-IEAKVLVEFTDSTNGIEEEYDTVLLA-----IGRDACTRK 283
|
170 180 190
....*....|....*....|....*....|....*
gi 919384098 452 LKGSEVALT---RFGEIEIDTKGATSLPGVYAAGD 483
Cdd:TIGR01438 284 LNLENVGVKinkKTGKIPADEEEQTNVPYIYAVGD 318
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
313-485 |
7.79e-06 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 48.23 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 313 IL-ATGARWRDLNVPGeleyrtkgVAYCPHCDGPFF---KGKRVAVIGGGNSGIEaaidLAGI-----VEHVTVV----- 378
Cdd:PRK06116 135 ILiATGGRPSIPDIPG--------AEYGITSDGFFAleeLPKRVAVVGAGYIAVE----FAGVlnglgSETHLFVrgdap 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 379 ------EFADTLRadDVLQKKarsmgNIDIIMSARTTEVI--GDGSKVVGMDyedrtTGEIkhLAVAGIFVQIGLVPNTE 450
Cdd:PRK06116 203 lrgfdpDIRETLV--EEMEKK-----GIRLHTNAVPKAVEknADGSLTLTLE-----DGET--LTVDCLIWAIGREPNTD 268
|
170 180 190
....*....|....*....|....*....|....*...
gi 919384098 451 FLkGSE---VALTRFGEIEIDTKGATSLPGVYAAGDAT 485
Cdd:PRK06116 269 GL-GLEnagVKLNEKGYIIVDEYQNTNVPGIYAVGDVT 305
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
297-485 |
1.13e-05 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 47.89 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 297 VNVDLASGATLKSRA--VILATGARWRDLNVPGELEYRTKGVAYCPHcDGPffkgKRVAVIGGGNSGIEAAIDLAGIVEH 374
Cdd:PLN02507 154 VEVTQLDGTKLRYTAkhILIATGSRAQRPNIPGKELAITSDEALSLE-ELP----KRAVVLGGGYIAVEFASIWRGMGAT 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 375 VTVV--------EFADTLRAddVLqkkARSMGNIDIIMSARTT----EVIGDGSKVVGMDYEDrttgeikHLAVAGIFVq 442
Cdd:PLN02507 229 VDLFfrkelplrGFDDEMRA--VV---ARNLEGRGINLHPRTNltqlTKTEGGIKVITDHGEE-------FVADVVLFA- 295
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 919384098 443 IGLVPNTEFLKGSEVA--LTRFGEIEIDTKGATSLPGVYAAGDAT 485
Cdd:PLN02507 296 TGRAPNTKRLNLEAVGveLDKAGAVKVDEYSRTNIPSIWAIGDVT 340
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
264-319 |
2.34e-05 |
|
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: 46.34 E-value: 2.34e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 919384098 264 GPKLAASLEQHVKQYGVEVITEQRAAAISKDGYVNVDLASGATLKSRAVILATGAR 319
Cdd:COG0446 164 DPEMAALLEEELREHGVELRLGETVVAIDGDDKVAVTLTDGEEIPADLVVVAPGVR 219
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
299-483 |
4.66e-05 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 45.69 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 299 VDLASGATLKSRAVILATGARWRD---LNVPGELEYRTKGVAYCPHCDGPFFKGKRVAVIGGGNSGIEAAIDLAGIVEHV 375
Cdd:PRK09754 91 LVLTNGESWHWDQLFIATGAAARPlplLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAASATQRRCKV 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 376 TVVEFADTLRA-------DDVLQKKARSMGnIDIIMSARTTEVIgDGSKVV-GMDYEDRTTGEIkhlavagIFVQIGLVP 447
Cdd:PRK09754 171 TVIELAATVMGrnapppvQRYLLQRHQQAG-VRILLNNAIEHVV-DGEKVElTLQSGETLQADV-------VIYGIGISA 241
|
170 180 190
....*....|....*....|....*....|....*.
gi 919384098 448 NTEFlkGSEVALTRFGEIEIDTKGATSLPGVYAAGD 483
Cdd:PRK09754 242 NDQL--AREANLDTANGIVIDEACRTCDPAIFAGGD 275
|
|
| PfPDO_like_N |
cd02975 |
Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO)-like family, N-terminal TRX-fold ... |
14-89 |
5.97e-05 |
|
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: 42.38 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 14 LQYIVNPIEISV-SGNDSDKSAE-LLALASEIAEMSPKISL------TDGTNARK------PSMSIAP-QGQAPRVHFAG 78
Cdd:cd02975 16 FKEMKNPVDLVVfSSKEGCQYCEvTKQLLEELSELSDKLKLeiydfdEDKEKAEKygvervPTTIFLQdGGKDGGIRYYG 95
|
90
....*....|.
gi 919384098 79 IPMGHEFTSLV 89
Cdd:cd02975 96 LPAGYEFASLI 106
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
311-486 |
6.18e-05 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 46.09 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 311 AVILATGARWRD-LNVPGEL--------EYRTK----GVAYCPHCDGPFFKGKRVAVIGGGNSGIEaAIDLAGIVEHVTV 377
Cdd:PRK12775 520 AVFLGVGAGAPTfLGIPGEFagqvysanEFLTRvnlmGGDKFPFLDTPISLGKSVVVIGAGNTAMD-CLRVAKRLGAPTV 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 378 ------VEFADTLRADDVlqKKARSMGnIDIIMSARTTEVIGDGSKVV-GMDYEDR--------------TTGEIKHLAV 436
Cdd:PRK12775 599 rcvyrrSEAEAPARIEEI--RHAKEEG-IDFFFLHSPVEIYVDAEGSVrGMKVEEMelgepdekgrrkpmPTGEFKDLEC 675
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 919384098 437 AGIFVQIGLVPNTEFLKGSE-VALTRFGEI-----EIDTKGATSLPGVYAAGDATT 486
Cdd:PRK12775 676 DTVIYALGTKANPIITQSTPgLALNKWGNIaaddgKLESTQSTNLPGVFAGGDIVT 731
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
265-319 |
2.12e-04 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 43.42 E-value: 2.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 919384098 265 PKLAASLEQHVKQYGVEVITEQRAAAISKD-GYVNVDLASGATLKSRAVILATGAR 319
Cdd:COG0644 86 ARFDRWLAEQAEEAGAEVRTGTRVTDVLRDdGRVVVRTGDGEEIRADYVVDADGAR 141
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
350-436 |
2.39e-04 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 43.70 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 350 KRVAVIGGGNSGIEAAIDLA--GIveHVTVVEFADTL------------RADDV------LQKKARSMGNIDIIMSARTT 409
Cdd:COG1148 141 KRALVIGGGIAGMTAALELAeqGY--EVYLVEKEPELggraaqlhktfpGLDCPqcilepLIAEVEANPNITVYTGAEVE 218
|
90 100
....*....|....*....|....*...
gi 919384098 410 EVIGD-GSKVVGMDYEDRTTGEIKHLAV 436
Cdd:COG1148 219 EVSGYvGNFTVTIKKGPREEIEIEVGAI 246
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
264-319 |
3.27e-04 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 43.20 E-value: 3.27e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 919384098 264 GPKLAASLEQHVKQYGVEVITEQRAAAISKDGyvnVDLASGATLKSRAVILATGAR 319
Cdd:COG1252 202 GEKLSEAAEKELEKRGVEVHTGTRVTEVDADG---VTLEDGEEIPADTVIWAAGVK 254
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
275-485 |
3.33e-04 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 43.33 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 275 VKQYGVEVItEQRAAAISKDGyVNVDlasGATLKSRAVILATGARWRDLNVPGeLEYRTKGVAycpHCDGPFfKGKRVAV 354
Cdd:PLN02546 188 LKNAGVTLI-EGRGKIVDPHT-VDVD---GKLYTARNILIAVGGRPFIPDIPG-IEHAIDSDA---ALDLPS-KPEKIAI 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 355 IGGGNSGIEAAIDLAGIVEHVTV-VEFADTLRA--DDVLQKKARSMGNIDI-IMSARTTEVI---GDGSkvVGMDYEDRT 427
Cdd:PLN02546 258 VGGGYIALEFAGIFNGLKSDVHVfIRQKKVLRGfdEEVRDFVAEQMSLRGIeFHTEESPQAIiksADGS--LSLKTNKGT 335
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 919384098 428 TGEIKHLAVAgifvqIGLVPNTEFLkGSE---VALTRFGEIEIDTKGATSLPGVYAAGDAT 485
Cdd:PLN02546 336 VEGFSHVMFA-----TGRKPNTKNL-GLEevgVKMDKNGAIEVDEYSRTSVPSIWAVGDVT 390
|
|
| YdhS |
COG4529 |
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only]; |
267-369 |
9.22e-04 |
|
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
Pssm-ID: 443597 [Multi-domain] Cd Length: 466 Bit Score: 41.86 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 267 LAASLEQHVKQYGVEVITeQRAAAISKD--GYVnVDLASGATLKSRAVILATGARWRDLnvPGELEYRTKGV---AYCPH 341
Cdd:COG4529 109 LAEALARAPAGVRLRHIR-AEVVDLERDdgGYR-VTLADGETLRADAVVLATGHPPPAP--PPGLAAGSPRYiadPWPPG 184
|
90 100
....*....|....*....|....*...
gi 919384098 342 CDGPFFKGKRVAVIGGGNSGIEAAIDLA 369
Cdd:COG4529 185 ALARIPPDARVLIIGTGLTAIDVVLSLA 212
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
234-319 |
1.17e-03 |
|
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: 41.08 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 234 IRTAIVAERFGGQVMDTV-----GIENFISVPYTEgpkLAASLEQHVKQYGVEVITEQRAAAISKDG-YVNVDLASGATL 307
Cdd:COG0654 71 IRGIRVRDGSDGRVLARFdaaetGLPAGLVVPRAD---LERALLEAARALGVELRFGTEVTGLEQDAdGVTVTLADGRTL 147
|
90
....*....|..
gi 919384098 308 KSRAVILATGAR 319
Cdd:COG0654 148 RADLVVGADGAR 159
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
350-488 |
1.18e-03 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 41.68 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 350 KRVAVIGGGNSGIEAAIDLAGIVEHVTVVEFADTLRADDVLQKKA-----RSMGnIDIIMSARTTEVIGDGSKVVgmdye 424
Cdd:PRK13748 271 ERLAVIGSSVVALELAQAFARLGSKVTILARSTLFFREDPAIGEAvtaafRAEG-IEVLEHTQASQVAHVDGEFV----- 344
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 919384098 425 dRTT--GEIKhlaVAGIFVQIGLVPNTEFL--KGSEVALTRFGEIEIDTKGATSLPGVYAAGDATTVP 488
Cdd:PRK13748 345 -LTTghGELR---ADKLLVATGRAPNTRSLalDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQP 408
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
334-493 |
1.41e-03 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 41.14 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 334 KGVAYCPHCDGpFFK---GKRVAVIGGGnsgiEAAIDLAGIV-----EHVTVVEFADTLRA--DDVLQKKARSM--GNID 401
Cdd:PTZ00058 220 KGKEFTISSDD-FFKikeAKRIGIAGSG----YIAVELINVVnrlgaESYIFARGNRLLRKfdETIINELENDMkkNNIN 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 402 IIMSARTTEVIGDGSKVVGMDYEDRTtgeiKHLAVAGIFVQIGLVPNTEFLKGSEVA-LTRFGEIEIDTKGATSLPGVYA 480
Cdd:PTZ00058 295 IITHANVEEIEKVKEKNLTIYLSDGR----KYEHFDYVIYCVGRSPNTEDLNLKALNiKTPKGYIKVDDNQRTSVKHIYA 370
|
170
....*....|...
gi 919384098 481 AGDATTVPFKQII 493
Cdd:PTZ00058 371 VGDCCMVKKNQEI 383
|
|
| Lys_Orn_oxgnase |
pfam13434 |
L-lysine 6-monooxygenase/L-ornithine 5-monooxygenase; This is a family of Rossmann fold ... |
268-377 |
1.70e-03 |
|
L-lysine 6-monooxygenase/L-ornithine 5-monooxygenase; This is a family of Rossmann fold oxidoreductases that catalyze NADPH-dependent hydroxylation and are involved in siderophore biosynthesis. This family includes L-ornithine 5-monooxygenase, which catalyzes the hydroxylation of L-ornithine at the N5 position, and L-lysine 6-monooxygenase, which catalyzes the hydroxylation of lysine at the N6 position (EC:1.14.13.59).
Pssm-ID: 433204 [Multi-domain] Cd Length: 338 Bit Score: 40.65 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 268 AASLEQHVkQYGVEVITEQRAAAISKDGY-VNVDLASGA--TLKSRAVILATGarwrdlnvpgeleyrtkGVAYCPHC-- 342
Cdd:pfam13434 105 ASHLPNRL-RFGQEVESVEPDAERGEPLLrVRVRDADGEetTFLARNLVLGTG-----------------GEPYIPECar 166
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 919384098 343 -DGPFF-------------KGKRVAVIGGGNSGIEAAIDLAGIVEHVTV 377
Cdd:pfam13434 167 gGERVFhsseyleridrlaAKKRIAVVGSGQSAAEIFRDLLRRGPAYEL 215
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
311-488 |
1.74e-03 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 41.01 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 311 AVILATGA-RWRDLNVPGEleyRTKGV--------AYcpHCDGPFFKGKRVAVIGGGNSGIEAA-------IDLAGIVEH 374
Cdd:PRK12771 225 AVFVAIGAqLGKRLPIPGE---DAAGVldavdflrAV--GEGEPPFLGKRVVVIGGGNTAMDAArtarrlgAEEVTIVYR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 919384098 375 VTVVE-FADTLRADDVLQKkarsmgNIDIIMSARTTEVIGDGSKVVG----------MDYEDR---TTGEIKHLAVAGIF 440
Cdd:PRK12771 300 RTREDmPAHDEEIEEALRE------GVEINWLRTPVEIEGDENGATGlrvitvekmeLDEDGRpspVTGEEETLEADLVV 373
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 919384098 441 VQIGLVPNTEFLKGSEVALTRFGEIEID-TKGATSLPGVYAAGDATTVP 488
Cdd:PRK12771 374 LAIGQDIDSAGLESVPGVEVGRGVVQVDpNFMMTGRPGVFAGGDMVPGP 422
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
348-379 |
9.72e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 38.46 E-value: 9.72e-03
10 20 30
....*....|....*....|....*....|..
gi 919384098 348 KGKRVAVIGGGNSGIEAAIDLAGIVEHVTVVE 379
Cdd:PRK12831 139 KGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFE 170
|
|
| |
