|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
1-519 |
0e+00 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 1049.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 1 MLDANLKAQLKSYLERVTRPIEIVASLDDGAKSQEMLALLNDVISVSKDVTLNDSGTDARTPSFSLSSPGHDISLRFAGI 80
Cdd:PRK15317 1 MLDANLKTQLKQYLELLERPIELVASLDDSEKSAELKELLEEIASLSDKITVEEDSLDVRKPSFSITRPGEDTGVRFAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 81 PMGHEFTSLVLALLQVGGYPPKVSAETIEQVRALEGEFHFETYFSQSCQNCPDVVQALNLMAVLNPGIKHVAIDGALFQD 160
Cdd:PRK15317 81 PMGHEFTSLVLALLQVGGHPPKLDQEVIEQIKALDGDFHFETYVSLSCHNCPDVVQALNLMAVLNPNITHTMIDGALFQD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 161 EVTDRKIMSVPSIYLNGELFGQGRMGLEEILAKIDTGAGARQAEKLNAKQAFDVLVVGGGPAGSAAAVYAARKGIRTGVA 240
Cdd:PRK15317 161 EVEARNIMAVPTVFLNGEEFGQGRMTLEEILAKLDTGAAARAAEELNAKDPYDVLVVGGGPAGAAAAIYAARKGIRTGIV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 241 AERFGGQVLDTMAIENFISVQHTEGPKLAVALEEHVKQYEVDIMNLQRADKLIPGAagELHEVKFASGASLKAKTLILAT 320
Cdd:PRK15317 241 AERFGGQVLDTMGIENFISVPETEGPKLAAALEEHVKEYDVDIMNLQRASKLEPAA--GLIEVELANGAVLKAKTVILAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 321 GARWREMNVPGEQQYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVSHVTLLEFDVQLRADAVLQRKLHS 400
Cdd:PRK15317 319 GARWRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVKHVTVLEFAPELKADQVLQDKLRS 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 401 LPNVTVITSAQTTEVMGDEQKVNGLRYKNRTTGEEITVPLEGIFVQIGLLPNSEWLKGAIELSPRGEIVVDSRGETSVPG 480
Cdd:PRK15317 399 LPNVTIITNAQTTEVTGDGDKVTGLTYKDRTTGEEHHLELEGVFVQIGLVPNTEWLKGTVELNRRGEIIVDARGATSVPG 478
|
490 500 510
....*....|....*....|....*....|....*....
gi 2205733253 481 IFAAGDVTVAPYKQIIIALGEGAKASLSAFDHLIRTSAP 519
Cdd:PRK15317 479 VFAAGDCTTVPYKQIIIAMGEGAKAALSAFDYLIRNSAA 517
|
|
| AhpF |
TIGR03140 |
alkyl hydroperoxide reductase subunit F; This enzyme is the partner of the peroxiredoxin ... |
1-515 |
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: 804.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 1 MLDANLKAQLKSYLERVTRPIEIVASLDDGAKSQEMLALLNDVISVSKDVTLN-DSGTDARTPSFSLSSPGHDISLRFAG 79
Cdd:TIGR03140 1 MLDQSLLAQLKSYLASLENPVTLVLSAGSHEKSKELLELLDEIASLSDKISLTqNTADTLRKPSFTILRDGADTGIRFAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 80 IPMGHEFTSLVLALLQVGGYPPKVSAETIEQVRALEGEFHFETYFSQSCQNCPDVVQALNLMAVLNPGIKHVAIDGALFQ 159
Cdd:TIGR03140 81 IPGGHEFTSLVLAILQVGGHGPKLDEGIIDRIRRLNGPLHFETYVSLTCQNCPDVVQALNQMALLNPNISHTMIDGALFQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 160 DEVTDRKIMSVPSIYLNGELFGQGRMGLEEILAKIDTGAGARQAEKLNAKQAFDVLVVGGGPAGSAAAVYAARKGIRTGV 239
Cdd:TIGR03140 161 DEVEALGIQGVPAVFLNGEEFHNGRMDLAELLEKLEETAGVEAASALEQLDPYDVLVVGGGPAGAAAAIYAARKGLRTAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 240 AAERFGGQVLDTMAIENFISVQHTEGPKLAVALEEHVKQYEVDIMNLQRADKLIpgAAGELHEVKFASGASLKAKTLILA 319
Cdd:TIGR03140 241 VAERIGGQVKDTVGIENLISVPYTTGSQLAANLEEHIKQYPIDLMENQRAKKIE--TEDGLIVVTLESGEVLKAKSVIVA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 320 TGARWREMNVPGEQQYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVSHVTLLEFDVQLRADAVLQRKLH 399
Cdd:TIGR03140 319 TGARWRKLGVPGEKEYIGKGVAYCPHCDGPFFKGKDVAVIGGGNSGIEAAIDLAGIVRHVTVLEFADELKADKVLQDKLK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 400 SLPNVTVITSAQTTEVMGDEQKVNGLRYKNRTTGEEITVPLEGIFVQIGLLPNSEWLKGAIELSPRGEIVVDSRGETSVP 479
Cdd:TIGR03140 399 SLPNVDILTSAQTTEIVGDGDKVTGIRYQDRNSGEEKQLDLDGVFVQIGLVPNTEWLKDAVELNRRGEIVIDERGRTSVP 478
|
490 500 510
....*....|....*....|....*....|....*.
gi 2205733253 480 GIFAAGDVTVAPYKQIIIALGEGAKASLSAFDHLIR 515
Cdd:TIGR03140 479 GIFAAGDVTTVPYKQIIIAMGEGAKAALSAFDYLIR 514
|
|
| AhpF |
COG3634 |
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms]; |
1-196 |
4.32e-110 |
|
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];
Pssm-ID: 442851 [Multi-domain] Cd Length: 200 Bit Score: 325.55 E-value: 4.32e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 1 MLDANLKAQLKSYLERVTRPIEIVASLDDGAKSQEMLALLNDVISVSKDVTLN--DSGTDARTPSFSLSSPGHDISLRFA 78
Cdd:COG3634 3 MLDDELKAQLKEYLEKLKNPVELVLFLDDCEKSEELRELLEEIASLSDKISLEvyDKDDVERAPSFAILRDGEDTGIRFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 79 GIPMGHEFTSLVLALLQVGGYPPKVSAETIEQVRALEGEFHFETYFSQSCQNCPDVVQALNLMAVLNPGIKHVAIDGALF 158
Cdd:COG3634 83 GIPSGHEFTSLVLALLQVSGHPPKLSEETIEQIKALDGPVHFEVFVSLSCPNCPDVVQALNLMAVLNPNITHEMIDGAEF 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 2205733253 159 QDEVTDRKIMSVPSIYLNGELFGQGRMGLEEILAKIDT 196
Cdd:COG3634 163 PDEAEKYGVMSVPTVVLNGEVFFVGRMPEEEILEKLDT 200
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
232-513 |
2.15e-92 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 283.93 E-value: 2.15e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 232 RKGIRTGV-AAERFGGQVLDTMAIENFISV-QHTEGPKLAVALEEHVKQYEVDIMnLQRADKLIPgaAGELHEVKFASGA 309
Cdd:COG0492 21 RAGLKTLViEGGEPGGQLATTKEIENYPGFpEGISGPELAERLREQAERFGAEIL-LEEVTSVDK--DDGPFRVTTDDGT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 310 SLKAKTLILATGARWREMNVPGEQQYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVSHVTLLEFDVQLR 389
Cdd:COG0492 98 EYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYLTKFASKVTLIHRRDELR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 390 ADAVLQRKLHSLPNVTVITSAQTTEVMGDEqKVNGLRYKNRTTGEEITVPLEGIFVQIGLLPNSEWLKGA-IELSPRGEI 468
Cdd:COG0492 178 ASKILVERLRANPKIEVLWNTEVTEIEGDG-RVEGVTLKNVKTGEEKELEVDGVFVAIGLKPNTELLKGLgLELDEDGYI 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2205733253 469 VVDSRGETSVPGIFAAGDVTVAPYKQIIIALGEGAKASLSAFDHL 513
Cdd:COG0492 257 VVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAARYL 301
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
244-513 |
2.95e-76 |
|
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: 242.15 E-value: 2.95e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 244 FGGQVLDTMAIENFISVQHT-EGPKLAVALEEHVKQYEVDIM--NLQRADKlipgaAGELHEVKFASGASLKAKTLILAT 320
Cdd:TIGR01292 33 PGGQLTTTTEVENYPGFPEGiSGPELMEKMKEQAVKFGAEIIyeEVIKVDK-----SDRPFKVYTGDGKEYTAKAVIIAT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 321 GARWREMNVPGEQQYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVSHVTLLEFDVQLRADAVLQRKLHS 400
Cdd:TIGR01292 108 GASARKLGIPGEDEFWGRGVSYCATCDGPFFKNKEVAVVGGGDSAIEEALYLTRIAKKVTLVHRRDKFRAEKILLDRLKK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 401 LPNVTVITSAQTTEVMGDEqKVNGLRYKNRTTGEEITVPLEGIFVQIGLLPNSEWLKGAIELSPRGEIVVDSRGETSVPG 480
Cdd:TIGR01292 188 NPKIEFLWNSTVEEIVGDN-KVEGVKIKNTVTGEEEELEVDGVFIAIGHEPNTELLKGLLELDENGYIVTDEGMRTSVPG 266
|
250 260 270
....*....|....*....|....*....|...
gi 2205733253 481 IFAAGDVTVAPYKQIIIALGEGAKASLSAFDHL 513
Cdd:TIGR01292 267 VFAAGDVRDKGYRQAVTAAGDGCIAALSAERYL 299
|
|
| AhpF_NTD_C |
cd03026 |
TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) ... |
105-193 |
8.58e-51 |
|
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: 8.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 105 AETIEQVRALEGEFHFETYFSQSCQNCPDVVQALNLMAVLNPGIKHVAIDGALFQDEVTDRKIMSVPSIYLNGELFGQGR 184
Cdd:cd03026 1 EDLLEQIRRLNGPINFETYVSLSCHNCPDVVQALNLMAVLNPNIEHEMIDGALFQDEVEERGIMSVPAIFLNGELFGFGR 80
|
....*....
gi 2205733253 185 MGLEEILAK 193
Cdd:cd03026 81 MTLEEILAK 89
|
|
| AhpF_homolog |
TIGR03143 |
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase ... |
242-509 |
1.55e-44 |
|
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: 164.95 E-value: 1.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 242 ERFGGQVLDTMAIENFISVQHTEGPKLAVALEEHVKQYEVDIMNlqrADKLIPGAAGELHEVKFASGaSLKAKTLILATG 321
Cdd:TIGR03143 36 DDFGGQITITSEVVNYPGILNTTGPELMQEMRQQAQDFGVKFLQ---AEVLDVDFDGDIKTIKTARG-DYKTLAVLIATG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 322 ARWREMNVPGEQQYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVSHVTLLEFDVQLRADAVLQRKLHSL 401
Cdd:TIGR03143 112 ASPRKLGFPGEEEFTGRGVAYCATCDGEFFTGMDVFVIGGGFAAAEEAVFLTRYASKVTVIVREPDFTCAKLIAEKVKNH 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 402 PNVTVITSAQTTEVMGDEqKVNGLRYKNRTTGEEIT--VPLE----GIFVQIGLLPNSEWLKGAIELSPRGEIVVDSRGE 475
Cdd:TIGR03143 192 PKIEVKFNTELKEATGDD-GLRYAKFVNNVTGEITEykAPKDagtfGVFVFVGYAPSSELFKGVVELDKRGYIPTNEDME 270
|
250 260 270
....*....|....*....|....*....|....
gi 2205733253 476 TSVPGIFAAGDVTVAPYKQIIIALGEGAKASLSA 509
Cdd:TIGR03143 271 TNVPGVYAAGDLRPKELRQVVTAVADGAIAATSA 304
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
238-502 |
1.62e-44 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 159.02 E-value: 1.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 238 GVAAERFGGQVLDTMAIENFISVQHT--EGPKLAVALEEHVKQYEVDIMNLQR--ADKLIPGAAG-ELHEVKFASGASLK 312
Cdd:pfam07992 30 EDEGTCPYGGCVLSKALLGAAEAPEIasLWADLYKRKEEVVKKLNNGIEVLLGteVVSIDPGAKKvVLEELVDGDGETIT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 313 AKTLILATGARWREMNVPGEQQYRNKGVAYCPHCDGPLFK--GKRVAVIGGGNSGVEAAIDLAGIVSHVTLLE------- 383
Cdd:pfam07992 110 YDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKllPKRVVVVGGGYIGVELAAALAKLGKEVTLIEaldrllr 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 384 -FDVQLRAdavLQRKLHSLPNVTVITSAQTTEVMGDEQKVNglryknRTTGEEITVPLEGIFVQIGLLPNSEWLKGA-IE 461
Cdd:pfam07992 190 aFDEEISA---ALEKALEKNGVEVRLGTSVKEIIGDGDGVE------VILKDGTEIDADLVVVAIGRRPNTELLEAAgLE 260
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2205733253 462 LSPRGEIVVDSRGETSVPGIFAAGDVTVAPYKQIIIALGEG 502
Cdd:pfam07992 261 LDERGGIVVDEYLRTSVPGIYAAGDCRVGGPELAQNAVAQG 301
|
|
| AhpF_NTD_N |
cd02974 |
Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) family, N-terminal ... |
1-94 |
9.36e-43 |
|
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: 147.34 E-value: 9.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 1 MLDANLKAQLKSYLERVTRPIEIVASLDDGAKSQEMLALLNDVISVSKDVTLNDSGTDARTPSFSLSSPGHDISLRFAGI 80
Cdd:cd02974 1 MLDANLKQQLKAYLERLENPVELVASLDDSEKSAELLELLEEIASLSDKITLEEDNDDERKPSFSINRPGEDTGIRFAGI 80
|
90
....*....|....
gi 2205733253 81 PMGHEFTSLVLALL 94
Cdd:cd02974 81 PMGHEFTSLVLALL 94
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
245-513 |
1.90e-36 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 137.50 E-value: 1.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 245 GGQVLDTMAIENFI-SVQHTEGPKLAVALEEHVKQYEVDIM-------NLQRADKLIPGAAGELhevkfasgaslKAKTL 316
Cdd:PRK10262 41 GGQLTTTTEVENWPgDPNDLTGPLLMERMHEHATKFETEIIfdhinkvDLQNRPFRLTGDSGEY-----------TCDAL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 317 ILATGARWREMNVPGEQQYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVSHVTLLEFDVQLRADAVLQR 396
Cdd:PRK10262 110 IIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIASEVHLIHRRDGFRAEKILIK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 397 KLH---SLPNVTVITSAQTTEVMGDEQKVNGLRYKNRTTGEEI-TVPLEGIFVQIGLLPNSEWLKGAIELSpRGEIVVDS 472
Cdd:PRK10262 190 RLMdkvENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNSDNIeSLDVAGLFVAIGHSPNTAIFEGQLELE-NGYIKVQS 268
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2205733253 473 -----RGETSVPGIFAAGDVTVAPYKQIIIALGEGAKASLSAFDHL 513
Cdd:PRK10262 269 gihgnATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYL 314
|
|
| TRX_GRX_like |
cd02973 |
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins ... |
118-184 |
6.74e-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: 6.74e-30
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2205733253 118 FHFETYFSQSCQNCPDVVQALNLMAVLNPGIKHVAIDGALFQDEVTDRKIMSVPSIYLNGELFGQGR 184
Cdd:cd02973 1 VNIEVFVSPTCPYCPDAVQAANRIAALNPNISAEMIDAAEFPDLADEYGVMSVPAIVINGKVEFVGR 67
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
257-503 |
4.65e-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: 108.36 E-value: 4.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 257 FISVQHTEGPKLAVALEEHVKQYEVDIMNLQRADKLIPGAagelHEVKFASGASLKAKTLILATGARWREMNVPGEQQ-- 334
Cdd:COG0446 27 YVGGGIKDPEDLLVRTPESFERKGIDVRTGTEVTAIDPEA----KTVTLRDGETLSYDKLVLATGARPRPPPIPGLDLpg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 335 -YRNKGVAYCPHCDGPL--FKGKRVAVIGGGNSGVEAAIDL--AGIvsHVTLLEfdvqlRADAVLQR----------KLH 399
Cdd:COG0446 103 vFTLRTLDDADALREALkeFKGKRAVVIGGGPIGLELAEALrkRGL--KVTLVE-----RAPRLLGVldpemaalleEEL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 400 SLPNVTVITSAQTTEVMGDEQKVNGLryknrTTGEEITVPLegIFVQIGLLPNSEWLKGA-IELSPRGEIVVDSRGETSV 478
Cdd:COG0446 176 REHGVELRLGETVVAIDGDDKVAVTL-----TDGEEIPADL--VVVAPGVRPNTELAKDAgLALGERGWIKVDETLQTSD 248
|
250 260
....*....|....*....|....*....
gi 2205733253 479 PGIFAAGDVTVAPY----KQIIIALGEGA 503
Cdd:COG0446 249 PDVYAAGDCAEVPHpvtgKTVYIPLASAA 277
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
301-488 |
1.15e-24 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 105.99 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 301 HEVKFASGASLKAKTLILATGARWREMNVPGEQQ-----YRNKG-----VAYCPhcdgplfKGKRVAVIGGGNSGVEAAI 370
Cdd:COG1251 87 RTVTLADGETLPYDKLVLATGSRPRVPPIPGADLpgvftLRTLDdadalRAALA-------PGKRVVVIGGGLIGLEAAA 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 371 DLAGIVSHVTLLEF-----DVQLRADA--VLQRKLHSLpNVTVITSAQTTEVMGDEqKVNGLRYKNrttGEEITVPLegI 443
Cdd:COG1251 160 ALRKRGLEVTVVERaprllPRQLDEEAgaLLQRLLEAL-GVEVRLGTGVTEIEGDD-RVTGVRLAD---GEELPADL--V 232
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2205733253 444 FVQIGLLPNSEWLKGA-IELSpRGeIVVDSRGETSVPGIFAAGDVT 488
Cdd:COG1251 233 VVAIGVRPNTELARAAgLAVD-RG-IVVDDYLRTSDPDIYAAGDCA 276
|
|
| GlrX_arch |
TIGR02187 |
Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal ... |
7-177 |
1.11e-20 |
|
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: 90.58 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 7 KAQLK-SYLERVTRPIEIVASLDDGAKS----QEMLALLNDVISVSKDVTL------NDSGTDA-------RTPSFSLSS 68
Cdd:TIGR02187 6 REILKeLFLKELKNPVEIVVFTDNDKEGcqycKETEQLLEELSEVSPKLKLeiydfdTPEDKEEaekygveRVPTTIILE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 69 PGHDISLRFAGIPMGHEFTSLVLALLQVGGYPPKVSAETIEQVRALEGEFHFETYFSQSCQNCPDVVQALNLMAVLNPGI 148
Cdd:TIGR02187 86 EGKDGGIRYTGIPAGYEFAALIEDIVRVSQGEPGLSEKTVELLQSLDEPVRIEVFVTPTCPYCPYAVLMAHKFALANDKI 165
|
170 180
....*....|....*....|....*....
gi 2205733253 149 KHVAIDGALFQDEVTDRKIMSVPSIYLNG 177
Cdd:TIGR02187 166 LGEMIEANENPDLAEKYGVMSVPKIVINK 194
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
317-505 |
6.35e-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: 92.12 E-value: 6.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 317 ILATGA-RWREMNVPGEQ------------QYrNKGVAYcphcDGPLFKGKRVAVIGGGNSgveaAIDLAGI-----VSH 378
Cdd:COG0493 211 FLATGAgKPRDLGIPGEDlkgvhsamdfltAV-NLGEAP----DTILAVGKRVVVIGGGNT----AMDCARTalrlgAES 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 379 VTLLEFDVQLRADAVLQRKLHSL-PNVTVITSAQTTEVMGDEQ-KVNGLRYKN---------------RTTGEEITVPLE 441
Cdd:COG0493 282 VTIVYRRTREEMPASKEEVEEALeEGVEFLFLVAPVEIIGDENgRVTGLECVRmelgepdesgrrrpvPIEGSEFTLPAD 361
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2205733253 442 GIFVQIGLLPNSEWLKGA--IELSPRGEIVVDSR-GETSVPGIFAAGDVTVAPyKQIIIALGEGAKA 505
Cdd:COG0493 362 LVILAIGQTPDPSGLEEElgLELDKRGTIVVDEEtYQTSLPGVFAGGDAVRGP-SLVVWAIAEGRKA 427
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
301-488 |
7.83e-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: 7.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 301 HEVKFASGASLKAKTLILATGARWREMNVPGEqqyrnkgvaycphcDGPLFKG-----------KRVAVIGGGNSGVEAA 369
Cdd:COG1249 119 HTVEVTGGETLTADHIVIATGSRPRVPPIPGL--------------DEVRVLTsdealeleelpKSLVVIGGGYIGLEFA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 370 IDLAGIVSHVTLLEFDVQL--RAD----AVLQRKLHSLpNVTVITSAQTTEVMGDEQKVNgLRYKNRTTGEEITVplEGI 443
Cdd:COG1249 185 QIFARLGSEVTLVERGDRLlpGEDpeisEALEKALEKE-GIDILTGAKVTSVEKTGDGVT-VTLEDGGGEEAVEA--DKV 260
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2205733253 444 FVQIGLLPNSEWL---KGAIELSPRGEIVVDSRGETSVPGIFAAGDVT 488
Cdd:COG1249 261 LVATGRRPNTDGLgleAAGVELDERGGIKVDEYLRTSVPGIYAIGDVT 308
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
318-505 |
5.80e-18 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 86.39 E-value: 5.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 318 LATGA-RWREMNVPGEQqyrNKGVAYC---------PHCDGPLFKGKRVAVIGGGNSgveaAIDLAGI-----VSHVTLL 382
Cdd:PRK11749 231 IGTGAgLPRFLGIPGEN---LGGVYSAvdfltrvnqAVADYDLPVGKRVVVIGGGNT----AMDAARTakrlgAESVTIV 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 383 -----------EFDVQL-RADAVlqrklhslpnvTVITSAQTTEVMGDEQKVNGLRY--------------KNRTTGEEI 436
Cdd:PRK11749 304 yrrgreempasEEEVEHaKEEGV-----------EFEWLAAPVEILGDEGRVTGVEFvrmelgepdasgrrRVPIEGSEF 372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2205733253 437 TVPLEGIFVQIGLLPNSEWLKGA--IELSPRGEIVVDSR-GETSVPGIFAAGDVtVAPYKQIIIALGEGAKA 505
Cdd:PRK11749 373 TLPADLVIKAIGQTPNPLILSTTpgLELNRWGTIIADDEtGRTSLPGVFAGGDI-VTGAATVVWAVGDGKDA 443
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
242-485 |
9.04e-17 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 80.73 E-value: 9.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 242 ERFGgqVLDTMAIEN------FISVQHTEGPKLAVALEEHVKQYEVDIMNLQRADKLIPgaAGELHEVKfASGASLKAKT 315
Cdd:pfam13738 47 NGFG--IPDLNAISPgtspafTFNREHPSGNEYAEYLRRVADHFELPINLFEEVTSVKK--EDDGFVVT-TSKGTYQARY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 316 LILATGarwrEMNVPgeqqYRNKGVAYCPHC----DGPLFKGKRVAVIGGGNSGVEAAIDLAGIVSHVTLL--------- 382
Cdd:pfam13738 122 VIIATG----EFDFP----NKLGVPELPKHYsyvkDFHPYAGQKVVVIGGYNSAVDAALELVRKGARVTVLyrgsewedr 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 383 --EFDVQLRADaVLQRkLHSLPN---VTVITSAQTTEVmgdeqKVNGLRYKNRTT-GEEITVPLEGIFVqIGLLPNSEWL 456
Cdd:pfam13738 194 dsDPSYSLSPD-TLNR-LEELVKngkIKAHFNAEVKEI-----TEVDVSYKVHTEdGRKVTSNDDPILA-TGYHPDLSFL 265
|
250 260 270
....*....|....*....|....*....|.
gi 2205733253 457 KGA-IELSPRGEIVVDSRG-ETSVPGIFAAG 485
Cdd:pfam13738 266 KKGlFELDEDGRPVLTEETeSTNVPGLFLAG 296
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
316-506 |
9.88e-17 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 81.57 E-value: 9.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 316 LILATGA-RWREMNVPGEQQyrnKGV---------------AYCPHCDGPLFKGKRVAVIGGGNSGVEAAID--LAGiVS 377
Cdd:PRK12770 122 VLIATGTwKSRKLGIPGEDL---PGVysaleylfriraaklGYLPWEKVPPVEGKKVVVVGAGLTAVDAALEavLLG-AE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 378 HVTLL-------------EFDvQLRADAVLQRKLhSLP-------NVTVITSAQTTEVMGDEqkvNGLRYKNRTTGEEIT 437
Cdd:PRK12770 198 KVYLAyrrtineapagkyEIE-RLIARGVEFLEL-VTPvriigegRVEGVELAKMRLGEPDE---SGRPRPVPIPGSEFV 272
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2205733253 438 VPLEGIFVQIGLLPNSEWLKGA--IELSPRGEIVVDSRGETSVPGIFAAGDVTVAPYKqIIIALGEGAKAS 506
Cdd:PRK12770 273 LEADTVVFAIGEIPTPPFAKEClgIELNRKGEIVVDEKHMTSREGVFAAGDVVTGPSK-IGKAIKSGLRAA 342
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
325-505 |
1.53e-15 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 78.91 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 325 REMNVPGEQQYR-----------NKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVSHVTLL----EFDVQLR 389
Cdd:PRK12831 242 KFMGIPGENLNGvfsanefltrvNLMKAYKPEYDTPIKVGKKVAVVGGGNVAMDAARTALRLGAEVHIVyrrsEEELPAR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 390 ADAVLQRKLHSlpnVTVITSAQTTEVMGDEQ-KVNGLRY------------KNR---TTGEEITVPLEGIFVQIGLLPN- 452
Cdd:PRK12831 322 VEEVHHAKEEG---VIFDLLTNPVEILGDENgWVKGMKCikmelgepdasgRRRpveIEGSEFVLEVDTVIMSLGTSPNp 398
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2205733253 453 --SEWLKGaIELSPRGEIVVDSR-GETSVPGIFAAGD-VTVApyKQIIIALGEGAKA 505
Cdd:PRK12831 399 liSSTTKG-LKINKRGCIVADEEtGLTSKEGVFAGGDaVTGA--ATVILAMGAGKKA 452
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
311-488 |
2.14e-14 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 75.21 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 311 LKAKTLILATGARWRemNVPGEQQ------YRNKGVAYCPHCdgPlfkgKRVAVIGGGNSGVEAAIDLAGIVSHVTLLEF 384
Cdd:PRK06292 129 IEAKNIVIATGSRVP--PIPGVWLilgdrlLTSDDAFELDKL--P----KSLAVIGGGVIGLELGQALSRLGVKVTVFER 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 385 ----------DVQLRADAVLQRKLHslpnvtVITSAQTTEVmgdEQKVNGLRYKNRTTGEEITVPLEGIFVQIGLLPNSE 454
Cdd:PRK06292 201 gdrilpledpEVSKQAQKILSKEFK------IKLGAKVTSV---EKSGDEKVEELEKGGKTETIEADYVLVATGRRPNTD 271
|
170 180 190
....*....|....*....|....*....|....*..
gi 2205733253 455 WL---KGAIELSPRGEIVVDSRGETSVPGIFAAGDVT 488
Cdd:PRK06292 272 GLgleNTGIELDERGRPVVDEHTQTSVPGIYAAGDVN 308
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
276-491 |
3.02e-14 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 74.79 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 276 VKQYEVDIMNLQR---ADKLIPGAAGELHEvkfasgaSLKAKTLILATGARWREMNVPG----EQQYRNKGVAYCPHcdg 348
Cdd:PRK07251 86 LAGSGVDLYDAEAhfvSNKVIEVQAGDEKI-------ELTAETIVINTGAVSNVLPIPGladsKHVYDSTGIQSLET--- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 349 plfKGKRVAVIGGGNSGVEAAIDLAGIVSHVTLLEfdvqlRADAVLQRKLHSLPN----------VTVITSAQTTEVMGD 418
Cdd:PRK07251 156 ---LPERLGIIGGGNIGLEFAGLYNKLGSKVTVLD-----AASTILPREEPSVAAlakqymeedgITFLLNAHTTEVKND 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2205733253 419 EQKVnglryknRTTGEEITVPLEGIFVQIGLLPNSEWL---KGAIELSPRGEIVVDSRGETSVPGIFAAGDVTVAP 491
Cdd:PRK07251 228 GDQV-------LVVTEDETYRFDALLYATGRKPNTEPLgleNTDIELTERGAIKVDDYCQTSVPGVFAVGDVNGGP 296
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
307-487 |
4.76e-13 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 71.00 E-value: 4.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 307 SGASLKAKTLILATGARWREMNVPGEQQ---YRNKGV---AYCPhcdgplfkgKRVAVIGGGNSGVEAAIDLAGIVSHVT 380
Cdd:PRK06370 128 GGETLRAKRIFINTGARAAIPPIPGLDEvgyLTNETIfslDELP---------EHLVIIGGGYIGLEFAQMFRRFGSEVT 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 381 LLEFDVQL--RAD----AVLQRKLHSLpNVTVITSAQTTEVmgdEQKVNGLRYKNRTTGEEITVPLEGIFVQIGLLPNSE 454
Cdd:PRK06370 199 VIERGPRLlpREDedvaAAVREILERE-GIDVRLNAECIRV---ERDGDGIAVGLDCNGGAPEITGSHILVAVGRVPNTD 274
|
170 180 190
....*....|....*....|....*....|....*.
gi 2205733253 455 WL---KGAIELSPRGEIVVDSRGETSVPGIFAAGDV 487
Cdd:PRK06370 275 DLgleAAGVETDARGYIKVDDQLRTTNPGIYAAGDC 310
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
302-491 |
4.84e-13 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 70.95 E-value: 4.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 302 EVKFASGA-SLKAKTLILATGARWREMnvPGeQQYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVSHVT 380
Cdd:PRK06416 123 RVMTEDGEqTYTAKNIILATGSRPREL--PG-IEIDGRVIWTSDEALNLDEVPKSLVVIGGGYIGVEFASAYASLGAEVT 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 381 LLE--------FDVQLraDAVLQRKLHSlPNVTVITSAQTTEVmgdEQKVNGLRYKNRTTGEEITVPLEGIFVQIGLLPN 452
Cdd:PRK06416 200 IVEalprilpgEDKEI--SKLAERALKK-RGIKIKTGAKAKKV---EQTDDGVTVTLEDGGKEETLEADYVLVAVGRRPN 273
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2205733253 453 SEWL---KGAIELSpRGEIVVDSRGETSVPGIFAAGDVTVAP 491
Cdd:PRK06416 274 TENLgleELGVKTD-RGFIEVDEQLRTNVPNIYAIGDIVGGP 314
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
314-513 |
1.46e-12 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 70.16 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 314 KTLILATGARW-REMNVPGEQ--------QY---RNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVSHVTL 381
Cdd:PRK12778 519 KGIFIASGAGLpNFMNIPGENsngvmssnEYltrVNLMDAASPDSDTPIKFGKKVAVVGGGNTAMDSARTAKRLGAERVT 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 382 LefdVQLRADAVLQRKLHSLPN-----VTVITSAQTTEVMGDE---------QKV-------NGLRYKNRTTGEEITVPL 440
Cdd:PRK12778 599 I---VYRRSEEEMPARLEEVKHakeegIEFLTLHNPIEYLADEkgwvkqvvlQKMelgepdaSGRRRPVAIPGSTFTVDV 675
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2205733253 441 EGIFVQIGLLPN---SEWLKGaIELSPRGEIVVDSRGETSVPGIFAAGDVtVAPYKQIIIALGEGAKASLSAFDHL 513
Cdd:PRK12778 676 DLVIVSVGVSPNplvPSSIPG-LELNRKGTIVVDEEMQSSIPGIYAGGDI-VRGGATVILAMGDGKRAAAAIDEYL 749
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
306-494 |
4.70e-11 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 65.62 E-value: 4.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 306 ASGASLKAKTLILATGARWREMNVPGEQQYRNKGVAYCPHCDGPLF---KGKRVAVIGGGNSGVEAAIDLA--GIVSHVT 380
Cdd:TIGR02374 90 DAGRTLSYDKLILATGSYPFILPIPGADKKGVYVFRTIEDLDAIMAmaqRFKKAAVIGGGLLGLEAAVGLQnlGMDVSVI 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 381 -----LLEFDVQLRADAVLQRKLHSLpNVTVITSAQTTEVMGDEqKVNGLRYKNrttGEEITVPLegIFVQIGLLPNSEw 455
Cdd:TIGR02374 170 hhapgLMAKQLDQTAGRLLQRELEQK-GLTFLLEKDTVEIVGAT-KADRIRFKD---GSSLEADL--IVMAAGIRPNDE- 241
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2205733253 456 LKGAIELSPRGEIVVDSRGETSVPGIFAAGDVT---------VAP-YKQ 494
Cdd:TIGR02374 242 LAVSAGIKVNRGIIVNDSMQTSDPDIYAVGECAehngrvyglVAPlYEQ 290
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
313-488 |
1.18e-10 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 63.64 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 313 AKTLILATGARWREMNVPGEQqyrnkgvaYCPHCDG-------PlfkgKRVAVIGGGNSGVEaaidLAGIV----SHVTL 381
Cdd:PRK06116 132 ADHILIATGGRPSIPDIPGAE--------YGITSDGffaleelP----KRVAVVGAGYIAVE----FAGVLnglgSETHL 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 382 LefdvqLRADAVLQRKLHSL----------PNVTVITSAQTTEVMGDEQKVNGLRYKNrttGEEITVplEGIFVQIGLLP 451
Cdd:PRK06116 196 F-----VRGDAPLRGFDPDIretlveemekKGIRLHTNAVPKAVEKNADGSLTLTLED---GETLTV--DCLIWAIGREP 265
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2205733253 452 NSEWL---KGAIELSPRGEIVVDSRGETSVPGIFAAGDVT 488
Cdd:PRK06116 266 NTDGLgleNAGVKLNEKGYIIVDEYQNTNVPGIYAVGDVT 305
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
354-503 |
1.35e-10 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 63.52 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 354 KRVAVIGGGNSGVEAAIDLAGIVSHVTLLEfdvqlRADAVLQRKLHS-----------LPNVTVITSAQTTEVMGdEQKV 422
Cdd:PRK09564 150 KNIVIIGAGFIGLEAVEAAKHLGKNVRIIQ-----LEDRILPDSFDKeitdvmeeelrENGVELHLNEFVKSLIG-EDKV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 423 NGLRYKNRTTGEEITVplegifVQIGLLPNSEWLKGA-IELSPRGEIVVDSRGETSVPGIFAAGDVTV----APYKQIII 497
Cdd:PRK09564 224 EGVVTDKGEYEADVVI------VATGVKPNTEFLEDTgLKTLKNGAIIVDEYGETSIENIYAAGDCATiyniVSNKNVYV 297
|
....*.
gi 2205733253 498 ALGEGA 503
Cdd:PRK09564 298 PLATTA 303
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
316-497 |
1.32e-09 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 59.93 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 316 LILATGARWREMNVPGE---------QQYRNkgvaycphCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVSHVTLLEFDV 386
Cdd:PRK04965 103 LVLATGASAFVPPIPGRelmltlnsqQEYRA--------AETQLRDAQRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAA 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 387 QLRA----DAVLQRKLHSLPNVTViTSAQTTEVMGDEQKVNGLRYKnRTTGEEITVplEGIFVQIGLLPNSEWLKGAIEL 462
Cdd:PRK04965 175 SLLAslmpPEVSSRLQHRLTEMGV-HLLLKSQLQGLEKTDSGIRAT-LDSGRSIEV--DAVIAAAGLRPNTALARRAGLA 250
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2205733253 463 SPRGeIVVDSRGETSVPGIFAAGDVT-----VAPYKQIII 497
Cdd:PRK04965 251 VNRG-IVVDSYLQTSAPDIYALGDCAeingqVLPFLQPIQ 289
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
302-382 |
1.47e-09 |
|
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: 59.88 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 302 EVKFASGASLKAKTLILATGArWREMNVP---------GEQ----QYRNkgvaycphcdgPL-FKGKRVAVIGGGNSGVE 367
Cdd:COG2072 118 TVTTDDGETLTARFVVVATGP-LSRPKIPdipgledfaGEQlhsaDWRN-----------PVdLAGKRVLVVGTGASAVQ 185
|
90
....*....|....*
gi 2205733253 368 AAIDLAGIVSHVTLL 382
Cdd:COG2072 186 IAPELARVAAHVTVF 200
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
347-505 |
1.74e-09 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 60.27 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 347 DGPLFKGKRVAVIGGGNSGVEAA-------IDLAGIVSHVTL-----LEFDVQlraDAVLQrklhslpNVTVITSAQTTE 414
Cdd:PRK12771 261 GEPPFLGKRVVVIGGGNTAMDAArtarrlgAEEVTIVYRRTRedmpaHDEEIE---EALRE-------GVEINWLRTPVE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 415 VMGDEQKVNGLRY----------KNR---TTGEEITVPLEGIFVQIGLLPNSEWLKGAIEL-SPRGEIVVDSRGE-TSVP 479
Cdd:PRK12771 331 IEGDENGATGLRVitvekmeldeDGRpspVTGEEETLEADLVVLAIGQDIDSAGLESVPGVeVGRGVVQVDPNFMmTGRP 410
|
170 180
....*....|....*....|....*.
gi 2205733253 480 GIFAAGDVTVAPyKQIIIALGEGAKA 505
Cdd:PRK12771 411 GVFAGGDMVPGP-RTVTTAIGHGKKA 435
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
302-510 |
1.87e-09 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 59.83 E-value: 1.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 302 EVKFASGASLK--AKTLILATGARWREMNVPGEQQYRNKGVAYCPHcDGPlfkgKRVAVIGGGNSGVEAAIDLAGIVSHV 379
Cdd:PLN02507 155 EVTQLDGTKLRytAKHILIATGSRAQRPNIPGKELAITSDEALSLE-ELP----KRAVVLGGGYIAVEFASIWRGMGATV 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 380 TLL--------EFDVQLRadAVLQR-------KLHSLPNVTVIT-SAQTTEVMGDEqkvnglryknrttGEEITVplEGI 443
Cdd:PLN02507 230 DLFfrkelplrGFDDEMR--AVVARnlegrgiNLHPRTNLTQLTkTEGGIKVITDH-------------GEEFVA--DVV 292
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2205733253 444 FVQIGLLPNSEWLK---GAIELSPRGEIVVDSRGETSVPGIFAAGDVT----VAPykqiiIALGEGAKASLSAF 510
Cdd:PLN02507 293 LFATGRAPNTKRLNleaVGVELDKAGAVKVDEYSRTNIPSIWAIGDVTnrinLTP-----VALMEGTCFAKTVF 361
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
311-503 |
3.38e-09 |
|
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.
Pssm-ID: 200098 [Multi-domain] Cd Length: 486 Bit Score: 59.22 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 311 LKAKTLILATGArWREM-NVPGEQQYRNKGVAYcpHCDGPlfkGKRVAVIGGGNSGVEAA------------IDLAgIVS 377
Cdd:TIGR01423 150 LQAEHILLATGS-WPQMlGIPGIEHCISSNEAF--YLDEP---PRRVLTVGGGFISVEFAgifnaykprggkVTLC-YRN 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 378 HVTLLEFDVQLRADAVLQRKLHSlpnVTVITSAQTTEVmgdEQKVNGLRYKNRTTGEEITVPLegIFVQIGLLPNSEWL- 456
Cdd:TIGR01423 223 NMILRGFDSTLRKELTKQLRANG---INIMTNENPAKV---TLNADGSKHVTFESGKTLDVDV--VMMAIGRVPRTQTLq 294
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2205733253 457 --KGAIELSPRGEIVVDSRGETSVPGIFAAGDVT----VAPykqiiIALGEGA 503
Cdd:TIGR01423 295 ldKVGVELTKKGAIQVDEFSRTNVPNIYAIGDVTdrvmLTP-----VAINEGA 342
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
260-489 |
3.67e-09 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 58.78 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 260 VQHTEGPKlAVALEEHVKQYEVDIMNLQRADKLIPGAagelHEVKFASGASLKAKTLILATGARWRE---MNVPGEQQYR 336
Cdd:PRK09754 53 LEDSPQLQ-QVLPANWWQENNVHLHSGVTIKTLGRDT----RELVLTNGESWHWDQLFIATGAAARPlplLDALGERCFT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 337 NKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVSHVTLLEF--DVQLR-ADAVLQRKL---HSLPNVTVITSA 410
Cdd:PRK09754 128 LRHAGDAARLREVLQPERSVVIVGAGTIGLELAASATQRRCKVTVIELaaTVMGRnAPPPVQRYLlqrHQQAGVRILLNN 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2205733253 411 QTTEVMGDEQKVNGLryknrTTGEeiTVPLEGIFVQIGLLPNSEWLKGAiELSPRGEIVVDSRGETSVPGIFAAGDVTV 489
Cdd:PRK09754 208 AIEHVVDGEKVELTL-----QSGE--TLQADVVIYGIGISANDQLAREA-NLDTANGIVIDEACRTCDPAIFAGGDVAI 278
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
317-486 |
7.96e-09 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 57.87 E-value: 7.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 317 ILATGA-RWREMNVPGE--------------QQYRNKGVAYCPHCDgplFKGKRVAVIGGGNSGVEAAidlagivshVTl 381
Cdd:PRK12810 233 FLGTGAyKPRDLGIPGRdldgvhfamdfliqNTRRVLGDETEPFIS---AKGKHVVVIGGGDTGMDCV---------GT- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 382 lefdvQLR--ADAVLQRKLHSLP-------------------------NVTVITSAQTTEVMGDEQKVNGLR-------Y 427
Cdd:PRK12810 300 -----AIRqgAKSVTQRDIMPMPpsrrnknnpwpywpmklevsnaheeGVEREFNVQTKEFEGENGKVTGVKvvrtelgE 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2205733253 428 KNRT--TGEEITVPLEGIFVQIGLLPNSE-WLK-GAIELSPRGEIVVDSRG-ETSVPGIFAAGD 486
Cdd:PRK12810 375 GDFEpvEGSEFVLPADLVLLAMGFTGPEAgLLAqFGVELDERGRVAAPDNAyQTSNPKVFAAGD 438
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
355-422 |
1.37e-08 |
|
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: 51.82 E-value: 1.37e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2205733253 355 RVAVIGGGNSGVEAAIDLAGIVSHVTLLEFDVQLR------ADAVLQRKLHSLpNVTVITSAQTTEVMGDEQKV 422
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLpgfdpeIAKILQEKLEKN-GIEFLLNTTVEAIEGNGDGV 73
|
|
| Thioredoxin_3 |
pfam13192 |
Thioredoxin domain; |
124-194 |
2.90e-08 |
|
Thioredoxin domain;
Pssm-ID: 433026 [Multi-domain] Cd Length: 71 Bit Score: 50.68 E-value: 2.90e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2205733253 124 FSQSCQNCPDVVQALNlMAVLNPGIKHVAIDGALFQdEVTDRKIMSVPSIYLNGELFGQGRMGLEEILAKI 194
Cdd:pfam13192 1 LGPGCPKCPQLEKAVK-EAAAELGIDAEVEKVTDFP-EIAKYGVMSTPALVINGKVVSSGKVPSEEEIRKL 69
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
302-491 |
3.24e-08 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 56.09 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 302 EVKFASGASLKAKTLILATGARWREM-NVPgeqqYRNKGVaycpHC-DGPL-FKG--KRVAVIGGGNSGVEAAIDLAGIV 376
Cdd:PRK06327 135 KVTGEDETVITAKHVIIATGSEPRHLpGVP----FDNKII----LDnTGALnFTEvpKKLAVIGAGVIGLELGSVWRRLG 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 377 SHVTLLEF--------DVQLRADAVLQRKLHSLpnvTVITSAQTTEVmgdEQKVNGLRYK-NRTTGEEITVPLEGIFVQI 447
Cdd:PRK06327 207 AEVTILEAlpaflaaaDEQVAKEAAKAFTKQGL---DIHLGVKIGEI---KTGGKGVSVAyTDADGEAQTLEVDKLIVSI 280
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2205733253 448 GLLPNSEWL---KGAIELSPRGEIVVDSRGETSVPGIFAAGDVTVAP 491
Cdd:PRK06327 281 GRVPNTDGLgleAVGLKLDERGFIPVDDHCRTNVPNVYAIGDVVRGP 327
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
352-514 |
3.35e-08 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 56.28 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 352 KGKRVAVIGGGNSGVEAAIDLA--GIVSHVtlLEFDVQLRADAV-------LQRKLHSLpNVTVITSAQTTE-VMGDEQK 421
Cdd:PRK14989 144 RSKRGAVVGGGLLGLEAAGALKnlGVETHV--IEFAPMLMAEQLdqmggeqLRRKIESM-GVRVHTSKNTLEiVQEGVEA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 422 VNGLRYKNRTTGE-EITVPLEGIFVQIGLLPNSEwlkgaIELSPRGEIVVDSRGETSVPGIFAAGDvtVAPYKQIIIAL- 499
Cdd:PRK14989 221 RKTMRFADGSELEvDFIVFSTGIRPQDKLATQCG-----LAVAPRGGIVINDSCQTSDPDIYAIGE--CASWNNRVFGLv 293
|
170
....*....|....*
gi 2205733253 500 GEGAKASLSAFDHLI 514
Cdd:PRK14989 294 APGYKMAQVAVDHLL 308
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
301-493 |
5.75e-08 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 54.96 E-value: 5.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 301 HEVKFASGASLKAKTLILATGARWREMNVPGEQqyrnkGVAYcpHCDGPLFK----GKRVAVIGGGNSGVEAAIDLAGIV 376
Cdd:PRK07846 117 KTLRTGDGEEITADQVVIAAGSRPVIPPVIADS-----GVRY--HTSDTIMRlpelPESLVIVGGGFIAAEFAHVFSALG 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 377 SHVTLLE-FDVQLRA--DAVLQRklhslpnVTVITSAQ-----TTEVMGDEQKVNGLRYknrTTGEEITVPLEGIFVQIG 448
Cdd:PRK07846 190 VRVTVVNrSGRLLRHldDDISER-------FTELASKRwdvrlGRNVVGVSQDGSGVTL---RLDDGSTVEADVLLVATG 259
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2205733253 449 LLPNSEWL---KGAIELSPRGEIVVDSRGETSVPGIFAAGDVTvAPYK 493
Cdd:PRK07846 260 RVPNGDLLdaaAAGVDVDEDGRVVVDEYQRTSAEGVFALGDVS-SPYQ 306
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
354-506 |
7.03e-08 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 55.16 E-value: 7.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 354 KRVAVIGGGNsgveAAIDLAGIVSHVTLLEF---DVQLRAdavLQRKLHSLP------------NVTVITSAQTTEVMGD 418
Cdd:PRK13984 419 RSLVVIGGGN----VAMDIARSMARLQKMEYgevNVKVTS---LERTFEEMPadmeeieegleeGVVIYPGWGPMEVVIE 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 419 EQKVNGLRYKNRTT--------------GEEITVPLEGIFVQIGLLPNSEWL----KGAIELSpRGEIVVDSRGETSVPG 480
Cdd:PRK13984 492 NDKVKGVKFKKCVEvfdeegrfnpkfdeSDQIIVEADMVVEAIGQAPDYSYLpeelKSKLEFV-RGRILTNEYGQTSIPW 570
|
170 180
....*....|....*....|....*.
gi 2205733253 481 IFAAGDVTVAPykQIIIALGEGAKAS 506
Cdd:PRK13984 571 LFAGGDIVHGP--DIIHGVADGYWAA 594
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
308-499 |
9.92e-08 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 54.62 E-value: 9.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 308 GASLKAKTLILATGARWREMNVpgeqqyrnKGVAYCPHCDG--PLFKGKRVAVIGGGNSGVEaaidLAGIVS-------- 377
Cdd:PTZ00058 198 GQVIEGKNILIAVGNKPIFPDV--------KGKEFTISSDDffKIKEAKRIGIAGSGYIAVE----LINVVNrlgaesyi 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 378 ----HVTLLEFDVQLRADAVLQRKLHslpNVTVITSAQTTEVMGDEQKvnGLRYKNRTTGEEITvpLEGIFVQIGLLPNS 453
Cdd:PTZ00058 266 fargNRLLRKFDETIINELENDMKKN---NINIITHANVEEIEKVKEK--NLTIYLSDGRKYEH--FDYVIYCVGRSPNT 338
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2205733253 454 EWL--KGAIELSPRGEIVVDSRGETSVPGIFAAGDVTVAPYKQIIIAL 499
Cdd:PTZ00058 339 EDLnlKALNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKKNQEIEDL 386
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
354-491 |
4.04e-07 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 52.46 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 354 KRVAVIGGGNSGVEAAIDLAGIVSHVTLLEFDVQL-RADAVLQRKlhslpnVTVITSAQTTEVMGDEQkVNGLRYKNR-- 430
Cdd:PRK13748 271 ERLAVIGSSVVALELAQAFARLGSKVTILARSTLFfREDPAIGEA------VTAAFRAEGIEVLEHTQ-ASQVAHVDGef 343
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2205733253 431 --TTGEEiTVPLEGIFVQIGLLPNSEWL---KGAIELSPRGEIVVDSRGETSVPGIFAAGDVTVAP 491
Cdd:PRK13748 344 vlTTGHG-ELRADKLLVATGRAPNTRSLaldAAGVTVNAQGAIVIDQGMRTSVPHIYAAGDCTDQP 408
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
268-487 |
1.62e-06 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 50.13 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 268 LAVALEEHVKQYEVDIMnLQRADKLIPGAagelHEVKFASGASLKAKTLILATGARWREMNVPGEQQYrnkGVAYCPHCD 347
Cdd:COG1252 58 IAIPLRELLRRAGVRFI-QGEVTGIDPEA----RTVTLADGRTLSYDYLVIATGSVTNFFGIPGLAEH---ALPLKTLED 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 348 GPLF--------------KGKRVAVIGGGNSGVEaaidLAGIVSH-----------------VTLLE--------FDVQL 388
Cdd:COG1252 130 ALALrerllaaferaerrRLLTIVVVGGGPTGVE----LAGELAEllrkllrypgidpdkvrITLVEagprilpgLGEKL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 389 RADAvlQRKLHSLpNVTVITSAQTTEVMGDeqkvnGLRYKNrttGEEI-------TVPLEGifvqigllpnSEWLKGA-I 460
Cdd:COG1252 206 SEAA--EKELEKR-GVEVHTGTRVTEVDAD-----GVTLED---GEEIpadtviwAAGVKA----------PPLLADLgL 264
|
250 260
....*....|....*....|....*...
gi 2205733253 461 ELSPRGEIVVDSRGET-SVPGIFAAGDV 487
Cdd:COG1252 265 PTDRRGRVLVDPTLQVpGHPNVFAIGDC 292
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
352-509 |
1.72e-06 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 50.55 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 352 KGKRVAVIGGGNSGVEAAIDLAGIVSHVTLLefdvqlradavlqrklHSLPNVTVITSAQTTEVMGDEQKVNGLRYK--- 428
Cdd:PRK13512 147 QVDKALVVGAGYISLEVLENLYERGLHPTLI----------------HRSDKINKLMDADMNQPILDELDKREIPYRlne 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 429 --NRTTGEEITVP------LEGIFVQIGLLPNSEWLKGA-IELSPRGEIVVDSRGETSVPGIFAAGDVTVAPYK------ 493
Cdd:PRK13512 211 eiDAINGNEVTFKsgkvehYDMIIEGVGTHPNSKFIESSnIKLDDKGFIPVNDKFETNVPNIYAIGDIITSHYRhvdlpa 290
|
170
....*....|....*.
gi 2205733253 494 QIIIALGEGAKASLSA 509
Cdd:PRK13512 291 SVPLAWGAHRAASIVA 306
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
311-487 |
3.85e-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: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 311 LKAKTLILATGARWREMNVPGEQQYRNKG-----VAYCPhcdgplfkGKRVaVIGGGNSGVEAAIDLAGIVSHVTLLEFD 385
Cdd:TIGR01438 142 YSAERFLIATGERPRYPGIPGAKELCITSddlfsLPYCP--------GKTL-VVGASYVALECAGFLAGIGLDVTVMVRS 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 386 VQLRA---DAVLQRKLH-SLPNVTVITS--AQTTEVMGDEQKVNGLRYKNRTTGEEITVPLegifvQIGLLPNSEWL--- 456
Cdd:TIGR01438 213 ILLRGfdqDCANKVGEHmEEHGVKFKRQfvPIKVEQIEAKVLVEFTDSTNGIEEEYDTVLL-----AIGRDACTRKLnle 287
|
170 180 190
....*....|....*....|....*....|..
gi 2205733253 457 KGAIELSPR-GEIVVDSRGETSVPGIFAAGDV 487
Cdd:TIGR01438 288 NVGVKINKKtGKIPADEEEQTNVPYIYAVGDI 319
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
304-488 |
2.15e-05 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 47.52 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 304 KFASGASLKAK---TLILATGARW-REMNVPGEQ-----------QYRNKGVAYCPHCDGPL--FKGKRVAVIGGGNSGV 366
Cdd:PRK12779 381 KTATLEDLKAAgfwKIFVGTGAGLpTFMNVPGEHllgvmsaneflTRVNLMRGLDDDYETPLpeVKGKEVFVIGGGNTAM 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 367 EAAIDLAGIVSHVTLLEFDVQLRADAVLQRKLHSLP---NVTVITSAqtTEVMGDEQK---------VNGL-------RY 427
Cdd:PRK12779 461 DAARTAKRLGGNVTIVYRRTKSEMPARVEELHHALEegiNLAVLRAP--REFIGDDHThfvthalldVNELgepdksgRR 538
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2205733253 428 KNRTTGEEITVPLEGIFVQIGLLPNSeWLKGA---IELSPRGEIVV--DSRgETSVPGIFAAGDVT 488
Cdd:PRK12779 539 SPKPTGEIERVPVDLVIMALGNTANP-IMKDAepgLKTNKWGTIEVekGSQ-RTSIKGVYSGGDAA 602
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
447-488 |
2.44e-05 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 46.78 E-value: 2.44e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2205733253 447 IGLLPNSEWL---KGAIELSPRGEIVVDSRGETSVPGIFAAGDVT 488
Cdd:PRK07845 270 VGSVPNTAGLgleEAGVELTPSGHITVDRVSRTSVPGIYAAGDCT 314
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
308-510 |
2.70e-05 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 46.79 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 308 GASLKAKTLILATGARWREMNVPGEQQYRNKGVAYcphcDGPlFKGKRVAVIGGGNSGVEAAIDLAGIVSHV-------- 379
Cdd:PLN02546 212 GKLYTARNILIAVGGRPFIPDIPGIEHAIDSDAAL----DLP-SKPEKIAIVGGGYIALEFAGIFNGLKSDVhvfirqkk 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 380 TLLEFDVQLRaDAVLQRKlhSLPNVTVITSAQTTEVMGDEQKVNGLRyknrtTGEEITVPLEGIFVQIGLLPNSEWL--- 456
Cdd:PLN02546 287 VLRGFDEEVR-DFVAEQM--SLRGIEFHTEESPQAIIKSADGSLSLK-----TNKGTVEGFSHVMFATGRKPNTKNLgle 358
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2205733253 457 KGAIELSPRGEIVVDSRGETSVPGIFAAGDVT----VAPykqiiIALGEGAKASLSAF 510
Cdd:PLN02546 359 EVGVKMDKNGAIEVDEYSRTSVPSIWAVGDVTdrinLTP-----VALMEGGALAKTLF 411
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
274-487 |
3.10e-05 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 46.30 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 274 EHVKQYEVDIM--NLQRAD-KLIPGAAGEL--H--EVKFASGAS--LKAKTLILATGARwremnvPgeqqYRNKGVAycp 344
Cdd:PRK05249 90 DHVINKQVEVRrgQYERNRvDLIQGRARFVdpHtvEVECPDGEVetLTADKIVIATGSR------P----YRPPDVD--- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 345 hcdgplFKGKRV----------------AVIGGGNSGVEAAIDLAGIVSHVTL-------LEF-DVQLrADAvLQRKLHS 400
Cdd:PRK05249 157 ------FDHPRIydsdsilsldhlprslIIYGAGVIGCEYASIFAALGVKVTLintrdrlLSFlDDEI-SDA-LSYHLRD 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 401 LpNVTVITSAQTTEVMGDEQKV-----NGLRYK-------NRTTGEEITVPLEgifvQIGLLPNSewlkgaielspRGEI 468
Cdd:PRK05249 229 S-GVTIRHNEEVEKVEGGDDGVivhlkSGKKIKadcllyaNGRTGNTDGLNLE----NAGLEADS-----------RGQL 292
|
250
....*....|....*....
gi 2205733253 469 VVDSRGETSVPGIFAAGDV 487
Cdd:PRK05249 293 KVNENYQTAVPHIYAVGDV 311
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
354-417 |
2.11e-04 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 44.08 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 354 KRVAVIGGGNSGVEAAIDLA--GIvsHVTLLE---------------FDVQLRADAVLQRKLHSL---PNVTVITSAQTT 413
Cdd:COG1148 141 KRALVIGGGIAGMTAALELAeqGY--EVYLVEkepelggraaqlhktFPGLDCPQCILEPLIAEVeanPNITVYTGAEVE 218
|
....
gi 2205733253 414 EVMG 417
Cdd:COG1148 219 EVSG 222
|
|
| PRK08275 |
PRK08275 |
putative oxidoreductase; Provisional |
470-520 |
3.37e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 181346 [Multi-domain] Cd Length: 554 Bit Score: 43.12 E-value: 3.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2205733253 470 VDSRGETSVPGIFAAGDVTVAPYKQIIIALGEGAKASLSAFDHLIRTSAPA 520
Cdd:PRK08275 361 VNEKAETTVPGLYAAGDMASVPHNYMLGAFTYGWFAGENAAEYVAGRDLPE 411
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
355-488 |
4.30e-04 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 42.69 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 355 RVAVIGGGNSGVEAAIDLAGIVSHVTLLEfdvqlRADAVLQRKLHSLP-NVTVITSAQTTEVM--GDEQKVNGLRYKNRT 431
Cdd:PRK08010 160 HLGILGGGYIGVEFASMFANFGSKVTILE-----AASLFLPREDRDIAdNIATILRDQGVDIIlnAHVERISHHENQVQV 234
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 432 TGEEITVPLEGIFVQIGLLPNSEWLK---GAIELSPRGEIVVDSRGETSVPGIFAAGDVT 488
Cdd:PRK08010 235 HSEHAQLAVDALLIASGRQPATASLHpenAGIAVNERGAIVVDKYLHTTADNIWAMGDVT 294
|
|
| PfPDO_like_N |
cd02975 |
Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO)-like family, N-terminal TRX-fold ... |
19-97 |
5.52e-04 |
|
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: 39.68 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205733253 19 RPIEIV--ASLDDGAKSQEMLALLNDVISVSKDVTLN----DSGTDA-------RTPSFSLS-SPGHDISLRFAGIPMGH 84
Cdd:cd02975 21 NPVDLVvfSSKEGCQYCEVTKQLLEELSELSDKLKLEiydfDEDKEKaekygveRVPTTIFLqDGGKDGGIRYYGLPAGY 100
|
90
....*....|...
gi 2205733253 85 EFTSLVLALLQVG 97
Cdd:cd02975 101 EFASLIEDIVRVS 113
|
|
| |
