|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
3-509 |
0e+00 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 1003.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 3 LDAEIMQQLEQYLTLLENDIVIKVNAGNDKVSVDMVRLIDEIAKLTPKIHVEKAELD-RTPSFSVNRPNEDTGIVFAGIP 81
Cdd:PRK15317 2 LDANLKTQLKQYLELLERPIELVASLDDSEKSAELKELLEEIASLSDKITVEEDSLDvRKPSFSITRPGEDTGVRFAGIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 82 LGHEFNSLVLALLQVGGRAPKVDEALINQIKGIKGEYHFETYVSLSCHNCPDVVQALNIMSVLNPNITHTMIDGAVFREE 161
Cdd:PRK15317 82 MGHEFTSLVLALLQVGGHPPKLDQEVIEQIKALDGDFHFETYVSLSCHNCPDVVQALNLMAVLNPNITHTMIDGALFQDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 162 VESKGIMAVPTIYLNGNFFESGRLTLEEILAKLGQ---ATESPSINEKEPFDVLVIGGGPAGVSSAIYAARKGLRTGIIA 238
Cdd:PRK15317 162 VEARNIMAVPTVFLNGEEFGQGRMTLEEILAKLDTgaaARAAEELNAKDPYDVLVVGGGPAGAAAAIYAARKGIRTGIVA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 239 ERFGGQILDTLGIENFISVPYTEGPKLAENFKEHVKRYDIDVMERQRAKSIRRN-ELLEVELEKGAVVKSKTVIIATGAR 317
Cdd:PRK15317 242 ERFGGQVLDTMGIENFISVPETEGPKLAAALEEHVKEYDVDIMNLQRASKLEPAaGLIEVELANGAVLKAKTVILATGAR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 318 WRNVNVPGEKEFKNKGVAYCPHCDGPLFAGKDVAVIGGGNSGIEAAIDLAGIVRHVTVLEFLPQLKADKVLQERLYRLPN 397
Cdd:PRK15317 322 WRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSGVEAAIDLAGIVKHVTVLEFAPELKADQVLQDKLRSLPN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 398 VTVLTNVQTKEFTG-KEKLDGITYIERDTNQEKHIEVQGVFVQIGLVPNTEWLEGTIERNAMGEIIVNEKNETSMPGVFA 476
Cdd:PRK15317 402 VTIITNAQTTEVTGdGDKVTGLTYKDRTTGEEHHLELEGVFVQIGLVPNTEWLKGTVELNRRGEIIVDARGATSVPGVFA 481
|
490 500 510
....*....|....*....|....*....|...
gi 316941602 477 AGDCTNSPYKQIVIAMGSGATAALSAFDYLIRN 509
Cdd:PRK15317 482 AGDCTTVPYKQIIIAMGEGAKAALSAFDYLIRN 514
|
|
| AhpF |
TIGR03140 |
alkyl hydroperoxide reductase subunit F; This enzyme is the partner of the peroxiredoxin ... |
3-509 |
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: 828.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 3 LDAEIMQQLEQYLTLLENDIVIKVNAGNDKVSVDMVRLIDEIAKLTPKIHVEKAELD--RTPSFSVNRPNEDTGIVFAGI 80
Cdd:TIGR03140 2 LDQSLLAQLKSYLASLENPVTLVLSAGSHEKSKELLELLDEIASLSDKISLTQNTADtlRKPSFTILRDGADTGIRFAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 81 PLGHEFNSLVLALLQVGGRAPKVDEALINQIKGIKGEYHFETYVSLSCHNCPDVVQALNIMSVLNPNITHTMIDGAVFRE 160
Cdd:TIGR03140 82 PGGHEFTSLVLAILQVGGHGPKLDEGIIDRIRRLNGPLHFETYVSLTCQNCPDVVQALNQMALLNPNISHTMIDGALFQD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 161 EVESKGIMAVPTIYLNGNFFESGRLTLEEILAKL--GQATESPS-INEKEPFDVLVIGGGPAGVSSAIYAARKGLRTGII 237
Cdd:TIGR03140 162 EVEALGIQGVPAVFLNGEEFHNGRMDLAELLEKLeeTAGVEAASaLEQLDPYDVLVVGGGPAGAAAAIYAARKGLRTAMV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 238 AERFGGQILDTLGIENFISVPYTEGPKLAENFKEHVKRYDIDVMERQRAKSI-RRNELLEVELEKGAVVKSKTVIIATGA 316
Cdd:TIGR03140 242 AERIGGQVKDTVGIENLISVPYTTGSQLAANLEEHIKQYPIDLMENQRAKKIeTEDGLIVVTLESGEVLKAKSVIVATGA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 317 RWRNVNVPGEKEFKNKGVAYCPHCDGPLFAGKDVAVIGGGNSGIEAAIDLAGIVRHVTVLEFLPQLKADKVLQERLYRLP 396
Cdd:TIGR03140 322 RWRKLGVPGEKEYIGKGVAYCPHCDGPFFKGKDVAVIGGGNSGIEAAIDLAGIVRHVTVLEFADELKADKVLQDKLKSLP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 397 NVTVLTNVQTKEFTGK-EKLDGITYIERDTNQEKHIEVQGVFVQIGLVPNTEWLEGTIERNAMGEIIVNEKNETSMPGVF 475
Cdd:TIGR03140 402 NVDILTSAQTTEIVGDgDKVTGIRYQDRNSGEEKQLDLDGVFVQIGLVPNTEWLKDAVELNRRGEIVIDERGRTSVPGIF 481
|
490 500 510
....*....|....*....|....*....|....
gi 316941602 476 AAGDCTNSPYKQIVIAMGSGATAALSAFDYLIRN 509
Cdd:TIGR03140 482 AAGDVTTVPYKQIIIAMGEGAKAALSAFDYLIRQ 515
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
209-506 |
6.86e-115 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 341.33 E-value: 6.86e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 209 FDVLVIGGGPAGVSSAIYAARKGLRTGII-AERFGGQILDTLGIENFISVPY-TEGPKLAENFKEHVKRYDIDVMErQRA 286
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIeGGEPGGQLATTKEIENYPGFPEgISGPELAERLREQAERFGAEILL-EEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 287 KSIRR-NELLEVELEKGAVVKSKTVIIATGARWRNVNVPGEKEFKNKGVAYCPHCDGPLFAGKDVAVIGGGNSGIEAAID 365
Cdd:COG0492 80 TSVDKdDGPFRVTTDDGTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 366 LAGIVRHVTVLEFLPQLKADKVLQERLYRLPNVTVLTNVQTKEFTGKEKLDGITYIERDTNQEKHIEVQGVFVQIGLVPN 445
Cdd:COG0492 160 LTKFASKVTLIHRRDELRASKILVERLRANPKIEVLWNTEVTEIEGDGRVEGVTLKNVKTGEEKELEVDGVFVAIGLKPN 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 316941602 446 TEWLEGT-IERNAMGEIIVNEKNETSMPGVFAAGDCTNSPYKQIVIAMGSGATAALSAFDYL 506
Cdd:COG0492 240 TELLKGLgLELDEDGYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAARYL 301
|
|
| AhpF |
COG3634 |
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms]; |
1-194 |
3.67e-103 |
|
Alkyl hydroperoxide reductase subunit AhpF [Defense mechanisms];
Pssm-ID: 442851 [Multi-domain] Cd Length: 200 Bit Score: 307.44 E-value: 3.67e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 1 MFLDAEIMQQLEQYLTLLENDIVIKVNAGNDKVSVDMVRLIDEIAKLTPKIHVE---KAELDRTPSFSVNRPNEDTGIVF 77
Cdd:COG3634 2 AMLDDELKAQLKEYLEKLKNPVELVLFLDDCEKSEELRELLEEIASLSDKISLEvydKDDVERAPSFAILRDGEDTGIRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 78 AGIPLGHEFNSLVLALLQVGGRAPKVDEALINQIKGIKGEYHFETYVSLSCHNCPDVVQALNIMSVLNPNITHTMIDGAV 157
Cdd:COG3634 82 AGIPSGHEFTSLVLALLQVSGHPPKLSEETIEQIKALDGPVHFEVFVSLSCPNCPDVVQALNLMAVLNPNITHEMIDGAE 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 316941602 158 FREEVESKGIMAVPTIYLNGNFFESGRLTLEEILAKL 194
Cdd:COG3634 162 FPDEAEKYGVMSVPTVVLNGEVFFVGRMPEEEILEKL 198
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
210-506 |
4.20e-97 |
|
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: 295.69 E-value: 4.20e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 210 DVLVIGGGPAGVSSAIYAARKGLRTGIIaERF--GGQILDTLGIENFISVP-YTEGPKLAENFKEHVKRYDIDVMERQRA 286
Cdd:TIGR01292 1 DVIIIGAGPAGLTAAIYAARANLKPLLI-EGMepGGQLTTTTEVENYPGFPeGISGPELMEKMKEQAVKFGAEIIYEEVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 287 KSIRRNELLEVELEKGAVVKSKTVIIATGARWRNVNVPGEKEFKNKGVAYCPHCDGPLFAGKDVAVIGGGNSGIEAAIDL 366
Cdd:TIGR01292 80 KVDKSDRPFKVYTGDGKEYTAKAVIIATGASARKLGIPGEDEFWGRGVSYCATCDGPFFKNKEVAVVGGGDSAIEEALYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 367 AGIVRHVTVLEFLPQLKADKVLQERLYRLPNVTVLTNVQTKEFTGKEKLDGITYIERDTNQEKHIEVQGVFVQIGLVPNT 446
Cdd:TIGR01292 160 TRIAKKVTLVHRRDKFRAEKILLDRLKKNPKIEFLWNSTVEEIVGDNKVEGVKIKNTVTGEEEELEVDGVFIAIGHEPNT 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 447 EWLEGTIERNAMGEIIVNEKNETSMPGVFAAGDCTNSPYKQIVIAMGSGATAALSAFDYL 506
Cdd:TIGR01292 240 ELLKGLLELDENGYIVTDEGMRTSVPGVFAAGDVRDKGYRQAVTAAGDGCIAALSAERYL 299
|
|
| AhpF_homolog |
TIGR03143 |
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase ... |
206-506 |
4.85e-57 |
|
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase homologs is found adjacent to alkylhydroperoxide reductase C subunit predominantly in cases where there is only one C subunit in the genome and that genome is lacking the F subunit partner (also a thioredcxin reductase homolog) that is usually found (TIGR03140).
Pssm-ID: 132187 [Multi-domain] Cd Length: 555 Bit Score: 198.85 E-value: 4.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 206 KEPFDVLVIGGGPAGVSSAIYAARKGLRTGII-AERFGGQILDTLGIENFISVPYTEGPKL-------AENFK-EHVKRY 276
Cdd:TIGR03143 2 EEIYDLIIIGGGPAGLSAGIYAGRAKLDTLIIeKDDFGGQITITSEVVNYPGILNTTGPELmqemrqqAQDFGvKFLQAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 277 DIDVMERQRAKSIRRNEllevelekgAVVKSKTVIIATGARWRNVNVPGEKEFKNKGVAYCPHCDGPLFAGKDVAVIGGG 356
Cdd:TIGR03143 82 VLDVDFDGDIKTIKTAR---------GDYKTLAVLIATGASPRKLGFPGEEEFTGRGVAYCATCDGEFFTGMDVFVIGGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 357 NSGIEAAIDLAGIVRHVTVLEFLPQLKADKVLQERLYRLPNVTVLTNVQTKEFTGKEKLDGITYIERDTNQEKHIEVQ-- 434
Cdd:TIGR03143 153 FAAAEEAVFLTRYASKVTVIVREPDFTCAKLIAEKVKNHPKIEVKFNTELKEATGDDGLRYAKFVNNVTGEITEYKAPkd 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 316941602 435 ----GVFVQIGLVPNTEWLEGTIERNAMGEIIVNEKNETSMPGVFAAGDCTNSPYKQIVIAMGSGATAALSAFDYL 506
Cdd:TIGR03143 233 agtfGVFVFVGYAPSSELFKGVVELDKRGYIPTNEDMETNVPGVYAAGDLRPKELRQVVTAVADGAIAATSAERYV 308
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
209-495 |
3.69e-56 |
|
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.
Pssm-ID: 400379 [Multi-domain] Cd Length: 301 Bit Score: 189.45 E-value: 3.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 209 FDVLVIGGGPAGVSSAIYAARKGLRTGIIAER---FGGQILDTLGIENFISVPYT--EGPKLAENFKEHVKRY--DIDVM 281
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEgtcPYGGCVLSKALLGAAEAPEIasLWADLYKRKEEVVKKLnnGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 282 ERQRAKSIRRNE----LLEVELEKGAVVKSKTVIIATGARWRNVNVPGEKEFKNKGVAYCPHCDGPLFA--GKDVAVIGG 355
Cdd:pfam07992 81 LGTEVVSIDPGAkkvvLEELVDGDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKllPKRVVVVGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 356 GNSGIEAAIDLAGIVRHVTVLEFLPQL------KADKVLQERLYRLpNVTVLTNVQTKEFTGKEklDGITYIerdTNQEK 429
Cdd:pfam07992 161 GYIGVELAAALAKLGKEVTLIEALDRLlrafdeEISAALEKALEKN-GVEVRLGTSVKEIIGDG--DGVEVI---LKDGT 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 316941602 430 HIEVQGVFVQIGLVPNTEWLEGT-IERNAMGEIIVNEKNETSMPGVFAAGDCTNSPYKQIVIAMGSG 495
Cdd:pfam07992 235 EIDADLVVVAIGRRPNTELLEAAgLELDERGGIVVDEYLRTSVPGIYAAGDCRVGGPELAQNAVAQG 301
|
|
| AhpF_NTD_C |
cd03026 |
TRX-GRX-like family, Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) ... |
105-193 |
1.45e-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: 170.17 E-value: 1.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 105 EALINQIKGIKGEYHFETYVSLSCHNCPDVVQALNIMSVLNPNITHTMIDGAVFREEVESKGIMAVPTIYLNGNFFESGR 184
Cdd:cd03026 1 EDLLEQIRRLNGPINFETYVSLSCHNCPDVVQALNLMAVLNPNIEHEMIDGALFQDEVEERGIMSVPAIFLNGELFGFGR 80
|
....*....
gi 316941602 185 LTLEEILAK 193
Cdd:cd03026 81 MTLEEILAK 89
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
211-506 |
5.11e-45 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 160.61 E-value: 5.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 211 VLVIGGGPAGVSSAIYAARKGLRTGII-AERFGGQILDTLGIENFISVPYT-EGPKLAENFKEHVKRYDIDVMERQRAKS 288
Cdd:PRK10262 9 LLILGSGPAGYTAAVYAARANLQPVLItGMEKGGQLTTTTEVENWPGDPNDlTGPLLMERMHEHATKFETEIIFDHINKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 289 IRRNELLEVELEKGAVVkSKTVIIATGARWRNVNVPGEKEFKNKGVAYCPHCDGPLFAGKDVAVIGGGNSGIEAAIDLAG 368
Cdd:PRK10262 89 DLQNRPFRLTGDSGEYT-CDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 369 IVRHVTVLEFLPQLKADKVLQERLY---RLPNVTVLTNVQTKEFTGKEKldGITYIE-RDTNQEKHIE---VQGVFVQIG 441
Cdd:PRK10262 168 IASEVHLIHRRDGFRAEKILIKRLMdkvENGNIILHTNRTLEEVTGDQM--GVTGVRlRDTQNSDNIEsldVAGLFVAIG 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 316941602 442 LVPNTEWLEGTIE-RNAMGEI---IVNEKNETSMPGVFAAGDCTNSPYKQIVIAMGSGATAALSAFDYL 506
Cdd:PRK10262 246 HSPNTAIFEGQLElENGYIKVqsgIHGNATQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYL 314
|
|
| AhpF_NTD_N |
cd02974 |
Alkyl hydroperoxide reductase F subunit (AhpF) N-terminal domain (NTD) family, N-terminal ... |
2-94 |
4.28e-42 |
|
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: 145.03 E-value: 4.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 2 FLDAEIMQQLEQYLTLLENDIVIKVNAGNDKVSVDMVRLIDEIAKLTPKIHVEKAELD-RTPSFSVNRPNEDTGIVFAGI 80
Cdd:cd02974 1 MLDANLKQQLKAYLERLENPVELVASLDDSEKSAELLELLEEIASLSDKITLEEDNDDeRKPSFSINRPGEDTGIRFAGI 80
|
90
....*....|....
gi 316941602 81 PLGHEFNSLVLALL 94
Cdd:cd02974 81 PMGHEFTSLVLALL 94
|
|
| AhpF_homolog |
TIGR03143 |
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase ... |
2-195 |
2.21e-35 |
|
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: 139.14 E-value: 2.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 2 FLDAEIMQQLEQYLTLLENDIVIKVNA-GNDKVSVDMVRLIDEIAKLTPKIHVE------------KAELDRTPSFSVNR 68
Cdd:TIGR03143 348 LLDDSLRQQLVGIFGRLENPVTLLLFLdGSNEKSAELQSFLGEFASLSEKLNSEavnrgeepesetLPKITKLPTVALLD 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 69 PNED-TGIVFAGIPLGHEFNSLVLALLQVGGRAPKVDEALINQIKGIKGEYHFETYVSLSCHNCPDVVQALNIMSVLNPN 147
Cdd:TIGR03143 428 DDGNyTGLKFHGVPSGHELNSFILALYNAAGPGQPLGEELLEKIKKITKPVNIKIGVSLSCTLCPDVVLAAQRIASLNPN 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 316941602 148 ITHTMIDGAVFREEVESKGIMAVPTIYLNGNFFESGRLTLEEILAKLG 195
Cdd:TIGR03143 508 VEAEMIDVSHFPDLKDEYGIMSVPAIVVDDQQVYFGKKTIEEMLELIG 555
|
|
| TRX_GRX_like |
cd02973 |
Thioredoxin (TRX)-Glutaredoxin (GRX)-like family; composed of archaeal and bacterial proteins ... |
118-184 |
1.40e-31 |
|
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: 116.13 E-value: 1.40e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 316941602 118 YHFETYVSLSCHNCPDVVQALNIMSVLNPNITHTMIDGAVFREEVESKGIMAVPTIYLNGNFFESGR 184
Cdd:cd02973 1 VNIEVFVSPTCPYCPDAVQAANRIAALNPNISAEMIDAAEFPDLADEYGVMSVPAIVINGKVEFVGR 67
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
211-501 |
4.66e-31 |
|
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: 124.86 E-value: 4.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 211 VLVIGGGPAGVSSAIYAARKGLRTGII--AERFGGqiLDTLGIENFisvpytegpKLAenfKEHVKRyDIDVMERqraks 288
Cdd:COG0493 124 VAVVGSGPAGLAAAYQLARAGHEVTVFeaLDKPGG--LLRYGIPEF---------RLP---KDVLDR-EIELIEA----- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 289 irrnelLEVELEKGAVV-KSKT----------VIIATGA-RWRNVNVPGEK--------EF---KNKGVAYcphcDGPLF 345
Cdd:COG0493 184 ------LGVEFRTNVEVgKDITldelleefdaVFLATGAgKPRDLGIPGEDlkgvhsamDFltaVNLGEAP----DTILA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 346 AGKDVAVIGGGNSGIEAAidlagivrhVTVLeflpQLKADKVLQerLYRLP-----------------NVTVLTNVQTKE 408
Cdd:COG0493 254 VGKRVVVIGGGNTAMDCA---------RTAL----RLGAESVTI--VYRRTreempaskeeveealeeGVEFLFLVAPVE 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 409 FTGKE--KLDGITYI---------------ERDTNQEKHIEVQGVFVQIGLVPNTEWLEGT--IERNAMGEIIVNEKN-E 468
Cdd:COG0493 319 IIGDEngRVTGLECVrmelgepdesgrrrpVPIEGSEFTLPADLVILAIGQTPDPSGLEEElgLELDKRGTIVVDEETyQ 398
|
330 340 350
....*....|....*....|....*....|...
gi 316941602 469 TSMPGVFAAGDCTNSPyKQIVIAMGSGATAALS 501
Cdd:COG0493 399 TSLPGVFAGGDAVRGP-SLVVWAIAEGRKAARA 430
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
209-484 |
4.78e-29 |
|
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation
Pssm-ID: 440861 [Multi-domain] Cd Length: 456 Bit Score: 119.42 E-value: 4.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 209 FDVLVIGGGPAGVSSAIYAARKGLRTGII-AERFGG-----------------------QILDTLGIEnfISVPYTEGPK 264
Cdd:COG1249 4 YDLVVIGAGPGGYVAAIRAAQLGLKVALVeKGRLGGtclnvgcipskallhaaevaheaRHAAEFGIS--AGAPSVDWAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 265 -----------LAENFKEHVKRYDIDVMeRQRAKSIRRNElleVELEKGAVVKSKTVIIATGARWRNVNVPGEkefknkg 333
Cdd:COG1249 82 lmarkdkvvdrLRGGVEELLKKNGVDVI-RGRARFVDPHT---VEVTGGETLTADHIVIATGSRPRVPPIPGL------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 334 vaycphcDGPLF-----------AGKDVAVIGGGNSGIEaaidLAGIVR----HVTVLEFLPQL--KAD----KVLQERL 392
Cdd:COG1249 151 -------DEVRVltsdealeleeLPKSLVVIGGGYIGLE----FAQIFArlgsEVTLVERGDRLlpGEDpeisEALEKAL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 393 YRLpNVTVLTNVQTKEFTGKEklDGITYIERDTNQEKHIEVQGVFVQIGLVPNTEW--LEGT-IERNAMGEIIVNEKNET 469
Cdd:COG1249 220 EKE-GIDILTGAKVTSVEKTG--DGVTVTLEDGGGEEAVEADKVLVATGRRPNTDGlgLEAAgVELDERGGIKVDEYLRT 296
|
330
....*....|....*
gi 316941602 470 SMPGVFAAGDCTNSP 484
Cdd:COG1249 297 SVPGIYAIGDVTGGP 311
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
271-496 |
2.21e-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: 109.13 E-value: 2.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 271 EHVKRYDIDVMERQRAKSIRRNELlEVELEKGAVVKSKTVIIATGARWRNVNVPGEKE---FKNKGVAYCPHCDGPL--F 345
Cdd:COG0446 44 ESFERKGIDVRTGTEVTAIDPEAK-TVTLRDGETLSYDKLVLATGARPRPPPIPGLDLpgvFTLRTLDDADALREALkeF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 346 AGKDVAVIGGGNSGIEAAIDLAGIVRHVTVLEFLPQL--KADK----VLQERLYRLpNVTVLTNVQTKEFTGKEKLdGIT 419
Cdd:COG0446 123 KGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLlgVLDPemaaLLEEELREH-GVELRLGETVVAIDGDDKV-AVT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 420 YIERDTnqekhIEVQGVFVQIGLVPNTEWLEGT-IERNAMGEIIVNEKNETSMPGVFAAGDCTNSPY----KQIVIAMGS 494
Cdd:COG0446 201 LTDGEE-----IPADLVVVAPGVRPNTELAKDAgLALGERGWIKVDETLQTSDPDVYAAGDCAEVPHpvtgKTVYIPLAS 275
|
..
gi 316941602 495 GA 496
Cdd:COG0446 276 AA 277
|
|
| GlrX_arch |
TIGR02187 |
Glutaredoxin-like domain protein; This family of archaeal proteins contains a C-terminal ... |
4-178 |
1.18e-24 |
|
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: 101.75 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 4 DAEIMQQLEQYLTLLENDIVIKVNAGNDKVSV----DMVRLIDEIAKLTPKIH--------------VEKAELDRTPSFS 65
Cdd:TIGR02187 3 EEDREILKELFLKELKNPVEIVVFTDNDKEGCqyckETEQLLEELSEVSPKLKleiydfdtpedkeeAEKYGVERVPTTI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 66 VNRPNEDTGIVFAGIPLGHEFNSLVLALLQVGGRAPKVDEALINQIKGIKGEYHFETYVSLSCHNCPDVVQALNIMSVLN 145
Cdd:TIGR02187 83 ILEEGKDGGIRYTGIPAGYEFAALIEDIVRVSQGEPGLSEKTVELLQSLDEPVRIEVFVTPTCPYCPYAVLMAHKFALAN 162
|
170 180 190
....*....|....*....|....*....|...
gi 316941602 146 PNITHTMIDGAVFREEVESKGIMAVPTIYLNGN 178
Cdd:TIGR02187 163 DKILGEMIEANENPDLAEKYGVMSVPKIVINKG 195
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
210-481 |
2.45e-24 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 104.84 E-value: 2.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 210 DVLVIGGGPAGVSsaiyAARKglrtgIIAERFGGQILdTLGIENFisVPYtEGPKLAENFKEHV-------------KRY 276
Cdd:COG1251 3 RIVIIGAGMAGVR----AAEE-----LRKLDPDGEIT-VIGAEPH--PPY-NRPPLSKVLAGETdeedlllrpadfyEEN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 277 DIDVMERQRAKSIRRNELlEVELEKGAVVKSKTVIIATGARWRNVNVPG-EKEfknkGV-------------AYCPhcdg 342
Cdd:COG1251 70 GIDLRLGTRVTAIDRAAR-TVTLADGETLPYDKLVLATGSRPRVPPIPGaDLP----GVftlrtlddadalrAALA---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 343 plfAGKDVAVIGGGNSGIEAAIDLAGIVRHVTVLEFLPQL-------KADKVLQERLYRLpNVTVLTNVQTKEFTGKEKL 415
Cdd:COG1251 141 ---PGKRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRLlprqldeEAGALLQRLLEAL-GVEVRLGTGVTEIEGDDRV 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 316941602 416 DGITyierdTNQEKHIEVQGVFVQIGLVPNTEWLEGT---IERnamGeIIVNEKNETSMPGVFAAGDCT 481
Cdd:COG1251 217 TGVR-----LADGEELPADLVVVAIGVRPNTELARAAglaVDR---G-IVVDDYLRTSDPDIYAAGDCA 276
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
209-506 |
2.41e-22 |
|
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.
Pssm-ID: 273568 [Multi-domain] Cd Length: 460 Bit Score: 99.64 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 209 FDVLVIGGGPAGVSSAIYAARKGLRTGII-AERFGGQIL-----------------------DTLGIEnfisvpyTEGPK 264
Cdd:TIGR01350 2 YDVIVIGGGPGGYVAAIRAAQLGLKVALVeKEYLGGTCLnvgciptkallhsaevydeikhaKDLGIE-------VENVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 265 LaeNFKEHVKR------------------YDIDVMErQRAKSIRRNElLEVELEKGA-VVKSKTVIIATGARWRnvNVPG 325
Cdd:TIGR01350 75 V--DWEKMQKRknkvvkklvggvsgllkkNKVTVIK-GEAKFLDPGT-VSVTGENGEeTLEAKNIIIATGSRPR--SLPG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 326 EKEFKNKGVaycpHCDGPLFAGKDV----AVIGGGNSGIEAAIDLAGIVRHVTVLEF----LPQLKAD--KVLQERLYRL 395
Cdd:TIGR01350 149 PFDFDGKVV----ITSTGALNLEEVpeslVIIGGGVIGIEFASIFASLGSKVTVIEMldriLPGEDAEvsKVLQKALKKK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 396 pNVTVLTNVQTKEFTGKEklDGITYIERDTNQEKhIEVQGVFVQIGLVPNTEW--LEGT-IERNAMGEIIVNEKNETSMP 472
Cdd:TIGR01350 225 -GVKILTNTKVTAVEKND--DQVTYENKGGETET-LTGEKVLVAVGRKPNTEGlgLEKLgVELDERGRIVVDEYMRTNVP 300
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 316941602 473 GVFAAGDCTNSP------YKQIVIAMGSGATAALSAFDYL 506
Cdd:TIGR01350 301 GIYAIGDVIGGPmlahvaSHEGIVAAENIAGKEPAHIDYD 340
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
211-506 |
3.61e-21 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 96.02 E-value: 3.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 211 VLVIGGGPAGVSSAIYAARKGLRTGII--AERFGGqiLDTLGIENFisvpytegpKLAenfKEHVKRYdIDVMERqraks 288
Cdd:PRK11749 143 VAVIGAGPAGLTAAHRLARKGYDVTIFeaRDKAGG--LLRYGIPEF---------RLP---KDIVDRE-VERLLK----- 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 289 irrnelLEVELEKGAVV-KSKT----------VIIATGA-RWRNVNVPGEkEFKN--KGVAYCP-----HCDGPLFAGKD 349
Cdd:PRK11749 203 ------LGVEIRTNTEVgRDITldelragydaVFIGTGAgLPRFLGIPGE-NLGGvySAVDFLTrvnqaVADYDLPVGKR 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 350 VAVIGGGNSGIEAAidlagivrhVTVLeflpQLKADKVLQerLYR-----LP------------NVTVLTNVQTKEFTGK 412
Cdd:PRK11749 276 VVVIGGGNTAMDAA---------RTAK----RLGAESVTI--VYRrgreeMPaseeevehakeeGVEFEWLAAPVEILGD 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 413 EK-LDGITYI-----ERD---------TNQEKHIEVQGVFVQIGLVPNTEWLEGT--IERNAMGEIIVNEKN-ETSMPGV 474
Cdd:PRK11749 341 EGrVTGVEFVrmelgEPDasgrrrvpiEGSEFTLPADLVIKAIGQTPNPLILSTTpgLELNRWGTIIADDETgRTSLPGV 420
|
330 340 350
....*....|....*....|....*....|..
gi 316941602 475 FAAGDCTNsPYKQIVIAMGSGATAALSAFDYL 506
Cdd:PRK11749 421 FAGGDIVT-GAATVVWAVGDGKDAAEAIHEYL 451
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
209-484 |
3.75e-21 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 96.01 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 209 FDVLVIGGGPAGVSSAIYAARKGLRTGII-AERFGGQILdtlgienfisvpyTEG--P-KL----AENFKE--------- 271
Cdd:PRK06292 4 YDVIVIGAGPAGYVAARRAAKLGKKVALIeKGPLGGTCL-------------NVGciPsKAliaaAEAFHEakhaeefgi 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 272 HVKRYDID---VMERQR------AKSIRRNEL-------------------LEVeleKGAVVKSKTVIIATGARWRnvNV 323
Cdd:PRK06292 71 HADGPKIDfkkVMARVRrerdrfVGGVVEGLEkkpkidkikgtarfvdpntVEV---NGERIEAKNIVIATGSRVP--PI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 324 PGEKEFKNKGV---------AYCPhcdgplfagKDVAVIGGGNSGIEAAIDLAGIVRHVTVLEFLPQL----------KA 384
Cdd:PRK06292 146 PGVWLILGDRLltsddafelDKLP---------KSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRIlpledpevskQA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 385 DKVLQERLYrlpnvtVLTNVQTKEFTgKEKLDGITYIERDTNQEKhIEVQGVFVQIGLVPNTEWL---EGTIERNAMGEI 461
Cdd:PRK06292 217 QKILSKEFK------IKLGAKVTSVE-KSGDEKVEELEKGGKTET-IEADYVLVATGRRPNTDGLgleNTGIELDERGRP 288
|
330 340
....*....|....*....|...
gi 316941602 462 IVNEKNETSMPGVFAAGDCTNSP 484
Cdd:PRK06292 289 VVDEHTQTSVPGIYAAGDVNGKP 311
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
207-376 |
1.51e-20 |
|
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: 93.77 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 207 EPFDVLVIGGGPAGVSSAIYAARKGLRTGII--AERFGGQILD------TLGIENFIS----VPYTE-------GPKLAE 267
Cdd:COG2072 5 EHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLekADDVGGTWRDnrypglRLDTPSHLYslpfFPNWSddpdfptGDEILA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 268 NFKEHVKRYDI--DVMERQRAKSIRRNE---LLEVELEKGAVVKSKTVIIATGARWR-NV-NVPGEKEFKnkGVAYcpHC 340
Cdd:COG2072 85 YLEAYADKFGLrrPIRFGTEVTSARWDEadgRWTVTTDDGETLTARFVVVATGPLSRpKIpDIPGLEDFA--GEQL--HS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 316941602 341 ---DGPL-FAGKDVAVIGGGNSGIEAAIDLAGIVRHVTVL 376
Cdd:COG2072 161 adwRNPVdLAGKRVLVVGTGASAVQIAPELARVAAHVTVF 200
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
218-478 |
6.54e-20 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 89.98 E-value: 6.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 218 PAGVSSAIYAARKGLRTGIIAER--------------------FGGQILDTLGIeNFIS----------VPYTEGPKLAE 267
Cdd:pfam13738 1 PAGIGCAIALKKAGLEDYLILEKgnignsfyrypthmtffspsFTSNGFGIPDL-NAISpgtspaftfnREHPSGNEYAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 268 NFKEHVKRYDIDVMERQRAKSI-RRNELLEVELEKGaVVKSKTVIIATGaRWRNVNVPGekeFKNKGV--AYCPHCDgpL 344
Cdd:pfam13738 80 YLRRVADHFELPINLFEEVTSVkKEDDGFVVTTSKG-TYQARYVIIATG-EFDFPNKLG---VPELPKhySYVKDFH--P 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 345 FAGKDVAVIGGGNSGIEAAIDLAGIVRHVTVL---EFLPQLKADKVL------QERLYRLPN---VTVLTNVQTKEFTGK 412
Cdd:pfam13738 153 YAGQKVVVIGGYNSAVDAALELVRKGARVTVLyrgSEWEDRDSDPSYslspdtLNRLEELVKngkIKAHFNAEVKEITEV 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 316941602 413 EKldgiTYIERDTNQEKHIEVQGVFVQIGLVPNTEWLE-GTIERNAMGEIIVNEK-NETSMPGVFAAG 478
Cdd:pfam13738 233 DV----SYKVHTEDGRKVTSNDDPILATGYHPDLSFLKkGLFELDEDGRPVLTEEtESTNVPGLFLAG 296
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
209-484 |
3.19e-19 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 90.37 E-value: 3.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 209 FDVLVIGGGPAGVSSAIYAARKGLRTGIIAERFGGQILDTLG-----------------IENFisvpytegPKLAENFKE 271
Cdd:PRK06327 5 FDVVVIGAGPGGYVAAIRAAQLGLKVACIEAWKNPKGKPALGgtclnvgcipskallasSEEF--------ENAGHHFAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 272 H---VKRYDIDV---MERQ-------------------------RAKSIRRNEL---LEVELEKGAVVKSKTVIIATGAR 317
Cdd:PRK06327 77 HgihVDGVKIDVakmIARKdkvvkkmtggieglfkknkitvlkgRGSFVGKTDAgyeIKVTGEDETVITAKHVIIATGSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 318 WRNVnvPGEKeFKNKGVaycpHC-DGPLFAG---KDVAVIGGGNSGIEaaidLAGIVR----HVTVLEFLPQL------- 382
Cdd:PRK06327 157 PRHL--PGVP-FDNKII----LDnTGALNFTevpKKLAVIGAGVIGLE----LGSVWRrlgaEVTILEALPAFlaaadeq 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 383 ---KADKVLQERlyrlpNVTVLTNVQTKEFTGKEKLDGITYIERDTNqEKHIEVQGVFVQIGLVPNTEWL--EGT-IERN 456
Cdd:PRK06327 226 vakEAAKAFTKQ-----GLDIHLGVKIGEIKTGGKGVSVAYTDADGE-AQTLEVDKLIVSIGRVPNTDGLglEAVgLKLD 299
|
330 340
....*....|....*....|....*...
gi 316941602 457 AMGEIIVNEKNETSMPGVFAAGDCTNSP 484
Cdd:PRK06327 300 ERGFIPVDDHCRTNVPNVYAIGDVVRGP 327
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
207-479 |
1.91e-17 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 84.81 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 207 EPFDVLVIGGGPAGVSSAIYAARKGLRTGII-AERFGG-----------------------QILDTLGIEN-FISV---- 257
Cdd:PRK06416 3 FEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVeKEKLGGtclnrgcipskallhaaeradeaRHSEDFGIKAeNVGIdfkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 258 --PYTEG--PKLAENFKEHVKRYDIDVMeRQRAKSIRRNELlEVELEKGA-VVKSKTVIIATGARWRNVnvPGeKEFKNK 332
Cdd:PRK06416 83 vqEWKNGvvNRLTGGVEGLLKKNKVDII-RGEAKLVDPNTV-RVMTEDGEqTYTAKNIILATGSRPREL--PG-IEIDGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 333 GVAYCPHCDGPLFAGKDVAVIGGGNSGIEaaidLAGIVR----HVTVLEFLPQLKA--DK---VLQERLYRLPNVTVLTN 403
Cdd:PRK06416 158 VIWTSDEALNLDEVPKSLVVIGGGYIGVE----FASAYAslgaEVTIVEALPRILPgeDKeisKLAERALKKRGIKIKTG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 404 VQTKEFTGKEklDGITYIERDTNQEKHIEVQGVFVQIGLVPNTE--WLEGT---IERnamGEIIVNEKNETSMPGVFAAG 478
Cdd:PRK06416 234 AKAKKVEQTD--DGVTVTLEDGGKEETLEADYVLVAVGRRPNTEnlGLEELgvkTDR---GFIEVDEQLRTNVPNIYAIG 308
|
.
gi 316941602 479 D 479
Cdd:PRK06416 309 D 309
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
211-480 |
8.40e-17 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 82.90 E-value: 8.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 211 VLVIGGGPAGVSSAIYAARKGLRTGII--AERFGGqiLDTLGIENFisvpytegpKLAenfKEHVKRyDIDVME----RQ 284
Cdd:PRK12810 146 VAVVGSGPAGLAAADQLARAGHKVTVFerADRIGG--LLRYGIPDF---------KLE---KEVIDR-RIELMEaegiEF 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 285 RA-----KSIRRNELLEvelEKGAVVksktviIATGA-RWRNVNVPGEK--------EF---KNKGVAYCPHCDGPLFAG 347
Cdd:PRK12810 211 RTnvevgKDITAEELLA---EYDAVF------LGTGAyKPRDLGIPGRDldgvhfamDFliqNTRRVLGDETEPFISAKG 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 348 KDVAVIGGGNSGIEAaidLAGIVRH----VTVLEFLPQL--KADKVLQERLYRLPN---------VTVLTNVQTKEFTGK 412
Cdd:PRK12810 282 KHVVVIGGGDTGMDC---VGTAIRQgaksVTQRDIMPMPpsRRNKNNPWPYWPMKLevsnaheegVEREFNVQTKEFEGE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 413 E-KLDGITYIERD---------TNQEKHIEVQGVFVQIGLV-PNTEWL-EGTIERNAMGEIIVNEKN-ETSMPGVFAAGD 479
Cdd:PRK12810 359 NgKVTGVKVVRTElgegdfepvEGSEFVLPADLVLLAMGFTgPEAGLLaQFGVELDERGRVAAPDNAyQTSNPKVFAAGD 438
|
.
gi 316941602 480 C 480
Cdd:PRK12810 439 M 439
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
207-491 |
1.22e-16 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 82.17 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 207 EPFDVLVIGGGPAGVSSAIYAARKGLRTGIIaER--FGGQILdtlgieNFISVPytegPKL-------------AENFKE 271
Cdd:PRK06370 4 QRYDAIVIGAGQAGPPLAARAAGLGMKVALI-ERglLGGTCV------NTGCVP----TKTliasaraahlarrAAEYGV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 272 HV-KRYDID---VMERQRAKSIRRNELLEVELEK----------------------GAVVKSKTVIIATGARWRNVNVPG 325
Cdd:PRK06370 73 SVgGPVSVDfkaVMARKRRIRARSRHGSEQWLRGlegvdvfrgharfespntvrvgGETLRAKRIFINTGARAAIPPIPG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 326 EKE---FKNKGV---AYCPhcdgplfagKDVAVIGGGNSGIEAAIDLAGIVRHVTVLEFLPQL------KADKVLQERLY 393
Cdd:PRK06370 153 LDEvgyLTNETIfslDELP---------EHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPRLlpredeDVAAAVREILE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 394 RLpNVTVLTNVQTKEFTGKEklDGITYIERDTNQEKHIEVQGVFVQIGLVPNTEWL---EGTIERNAMGEIIVNEKNETS 470
Cdd:PRK06370 224 RE-GIDVRLNAECIRVERDG--DGIAVGLDCNGGAPEITGSHILVAVGRVPNTDDLgleAAGVETDARGYIKVDDQLRTT 300
|
330 340 350
....*....|....*....|....*....|
gi 316941602 471 MPGVFAAGDCtNSPYK---------QIVIA 491
Cdd:PRK06370 301 NPGIYAAGDC-NGRGAfthtayndaRIVAA 329
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
205-506 |
9.84e-16 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 78.49 E-value: 9.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 205 EKEPFDVLVIGGGPAGVSSAIYAARKGLRTGI---IAERfGGQILdtLGIENFiSVPytegpklAENFKEHVKRydidvM 281
Cdd:PRK12770 15 PPTGKKVAIIGAGPAGLAAAGYLACLGYEVHVydkLPEP-GGLML--FGIPEF-RIP-------IERVREGVKE-----L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 282 ERQ------RAKSIRRNELLE----------VELEKgAVVKSKTVIIATGA-RWRNVNVPGEK------------EFKNK 332
Cdd:PRK12770 79 EEAgvvfhtRTKVCCGEPLHEeegdefveriVSLEE-LVKKYDAVLIATGTwKSRKLGIPGEDlpgvysaleylfRIRAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 333 GVAYCPHCDGPLFAGKDVAVIGGGNSGIEAAID--LAGiVRHVTVL--EFLPQLKADKVLQERLYRLpNVTVLTNVQTKE 408
Cdd:PRK12770 158 KLGYLPWEKVPPVEGKKVVVVGAGLTAVDAALEavLLG-AEKVYLAyrRTINEAPAGKYEIERLIAR-GVEFLELVTPVR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 409 FTGKEKLDGITYI---------------ERDTNQEKHIEVQGVFVQIGLVP----NTEWLegTIERNAMGEIIVNEKNET 469
Cdd:PRK12770 236 IIGEGRVEGVELAkmrlgepdesgrprpVPIPGSEFVLEADTVVFAIGEIPtppfAKECL--GIELNRKGEIVVDEKHMT 313
|
330 340 350
....*....|....*....|....*....|....*..
gi 316941602 470 SMPGVFAAGDCTNSPYKqIVIAMGSGATAALSAFDYL 506
Cdd:PRK12770 314 SREGVFAAGDVVTGPSK-IGKAIKSGLRAAQSIHEWL 349
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
211-506 |
2.73e-15 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 78.14 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 211 VLVIGGGPAGVSSAIYAARKGLRTGII-AERFGGQILdTLGIENFiSVPytegpklaenfKEHVKRYDIDVMERQRAKsI 289
Cdd:PRK12831 143 VAVIGSGPAGLTCAGDLAKMGYDVTIFeALHEPGGVL-VYGIPEF-RLP-----------KETVVKKEIENIKKLGVK-I 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 290 RRN----------ELLEVElekgavvKSKTVIIATGARW-RNVNVPGE--------KEF---KNKGVAYCPHCDGPLFAG 347
Cdd:PRK12831 209 ETNvvvgktvtidELLEEE-------GFDAVFIGSGAGLpKFMGIPGEnlngvfsaNEFltrVNLMKAYKPEYDTPIKVG 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 348 KDVAVIGGGNSGIEAAidlagivRhvTVLeflpQLKADKVLqerLYR-----LP------------NVTVLTNVQTKEFT 410
Cdd:PRK12831 282 KKVAVVGGGNVAMDAA-------R--TAL----RLGAEVHI---VYRrseeeLParveevhhakeeGVIFDLLTNPVEIL 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 411 GKEK--LDGITYI-----ERD----------TNQEKHIEVQGVFVQIGLVPNTEWLEGT--IERNAMGEIIVNEKN-ETS 470
Cdd:PRK12831 346 GDENgwVKGMKCIkmelgEPDasgrrrpveiEGSEFVLEVDTVIMSLGTSPNPLISSTTkgLKINKRGCIVADEETgLTS 425
|
330 340 350
....*....|....*....|....*....|....*.
gi 316941602 471 MPGVFAAGDCTNSPyKQIVIAMGSGATAALSAFDYL 506
Cdd:PRK12831 426 KEGVFAGGDAVTGA-ATVILAMGAGKKAAKAIDEYL 460
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
211-480 |
4.93e-15 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 77.00 E-value: 4.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 211 VLVIGGGPAGVSSAIYAAR--KGL------RTGIIAerFGgqildTLGIENFISVPYTEGPKLAENFKEHVKRYDIDVME 282
Cdd:PRK09564 3 IIIIGGTAAGMSAAAKAKRlnKELeitvyeKTDIVS--FG-----ACGLPYFVGGFFDDPNTMIARTPEEFIKSGIDVKT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 283 RQRAKSI-RRNELLEVE-LEKGAVVKSK--TVIIATGARwrnVNVPGEKEFKNKGVAYCPHCDGPLF--------AGKDV 350
Cdd:PRK09564 76 EHEVVKVdAKNKTITVKnLKTGSIFNDTydKLMIATGAR---PIIPPIKNINLENVYTLKSMEDGLAlkellkdeEIKNI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 351 AVIGGGNSGIEAAIDLAGIVRHVTVLEF----LPQlKADK----VLQERLyRLPNVTVLTNVQTKEFTGKEKLDGITyie 422
Cdd:PRK09564 153 VIIGAGFIGLEAVEAAKHLGKNVRIIQLedriLPD-SFDKeitdVMEEEL-RENGVELHLNEFVKSLIGEDKVEGVV--- 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 316941602 423 rdTNQEKhIEVQGVFVQIGLVPNTEWLEGT-IERNAMGEIIVNEKNETSMPGVFAAGDC 480
Cdd:PRK09564 228 --TDKGE-YEADVVIVATGVKPNTEFLEDTgLKTLKNGAIIVDEYGETSIENIYAAGDC 283
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
201-506 |
1.29e-13 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 73.62 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 201 PSINEKEPFDVLVIGGGPAGVSSAIYAARKG---------------LRTGIIAERFGGQILDtLGIENFIsvpytegpKL 265
Cdd:PRK12778 424 PEVAEKNGKKVAVIGSGPAGLSFAGDLAKRGydvtvfealheiggvLKYGIPEFRLPKKIVD-VEIENLK--------KL 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 266 AENFKEHV---KRYDIDVMERQRAKSIrrnellevelekgavvksktvIIATGARWRN-VNVPGE--------KEF---K 330
Cdd:PRK12778 495 GVKFETDVivgKTITIEELEEEGFKGI---------------------FIASGAGLPNfMNIPGEnsngvmssNEYltrV 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 331 NKGVAYCPHCDGPLFAGKDVAVIGGGNSGIEAA-------IDLAGIVRHVTVLEFLPQLKADKVLQERlyrlpNVTVLTN 403
Cdd:PRK12778 554 NLMDAASPDSDTPIKFGKKVAVVGGGNTAMDSArtakrlgAERVTIVYRRSEEEMPARLEEVKHAKEE-----GIEFLTL 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 404 VQTKEFTGKEK-------LDGITYIERD----------TNQEKHIEVQGVFVQIGLVPNTEWLEGT--IERNAMGEIIVN 464
Cdd:PRK12778 629 HNPIEYLADEKgwvkqvvLQKMELGEPDasgrrrpvaiPGSTFTVDVDLVIVSVGVSPNPLVPSSIpgLELNRKGTIVVD 708
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 316941602 465 EKNETSMPGVFAAGDCTNSPyKQIVIAMGSGATAALSAFDYL 506
Cdd:PRK12778 709 EEMQSSIPGIYAGGDIVRGG-ATVILAMGDGKRAAAAIDEYL 749
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
209-482 |
1.71e-13 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 72.50 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 209 FDVLVIGGGPAGVSSAIYAARKGLRTGII-AERFGGQILdtlgieNFISVP---YTEGPKLAENFKEHVKRYDIDVMERQ 284
Cdd:PRK06116 5 YDLIVIGGGSGGIASANRAAMYGAKVALIeAKRLGGTCV------NVGCVPkklMWYGAQIAEAFHDYAPGYGFDVTENK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 285 ---------RAKSIRR-----NELLE---VELEKG--AVVKSKTV------------IIATGARWRNVNVPGEKefknkg 333
Cdd:PRK06116 79 fdwaklianRDAYIDRlhgsyRNGLEnngVDLIEGfaRFVDAHTVevngerytadhiLIATGGRPSIPDIPGAE------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 334 vaYCPHCDGpLFA----GKDVAVIGGGNSGIEaaidLAGI-----------VRHVTVL-EFLPQLKadKVLQERLYRlPN 397
Cdd:PRK06116 153 --YGITSDG-FFAleelPKRVAVVGAGYIAVE----FAGVlnglgsethlfVRGDAPLrGFDPDIR--ETLVEEMEK-KG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 398 VTVLTNVQTKEFtgkEKL-DGITYIERDTNQEkhIEVQGVFVQIGLVPNTEW--LEGT-IERNAMGEIIVNEKNETSMPG 473
Cdd:PRK06116 223 IRLHTNAVPKAV---EKNaDGSLTLTLEDGET--LTVDCLIWAIGREPNTDGlgLENAgVKLNEKGYIIVDEYQNTNVPG 297
|
....*....
gi 316941602 474 VFAAGDCTN 482
Cdd:PRK06116 298 IYAVGDVTG 306
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
211-506 |
1.64e-11 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 66.44 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 211 VLVIGGGPAGVSSAIYAARKG---------------LRTGIIAERFGGQILDT-------LGIEnfisvpytegpklaen 268
Cdd:PRK12771 140 VAVIGGGPAGLSAAYHLRRMGhavtifeagpklggmMRYGIPAYRLPREVLDAeiqrildLGVE---------------- 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 269 fkehvKRYDIDVMErqraksirrnELLEVELEKG--AvvksktVIIATGA-RWRNVNVPGEK--------EF-KNKGVay 336
Cdd:PRK12771 204 -----VRLGVRVGE----------DITLEQLEGEfdA------VFVAIGAqLGKRLPIPGEDaagvldavDFlRAVGE-- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 337 cphcDGPLFAGKDVAVIGGGNSGIEAA-------IDLAGIVRHVTVlEFLPQLK--ADKVLQErlyrlpNVTVLTNVQTK 407
Cdd:PRK12771 261 ----GEPPFLGKRVVVIGGGNTAMDAArtarrlgAEEVTIVYRRTR-EDMPAHDeeIEEALRE------GVEINWLRTPV 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 408 EFTGKE---------KLDGITYIERDTNQ-----EKHIEVQGVFVQIGLVPNTEWLEG-TIERNAMGEIIVNEKNE-TSM 471
Cdd:PRK12771 330 EIEGDEngatglrviTVEKMELDEDGRPSpvtgeEETLEADLVVLAIGQDIDSAGLESvPGVEVGRGVVQVDPNFMmTGR 409
|
330 340 350
....*....|....*....|....*....|....*
gi 316941602 472 PGVFAAGDCTNSPyKQIVIAMGSGATAALSAFDYL 506
Cdd:PRK12771 410 PGVFAGGDMVPGP-RTVTTAIGHGKKAARNIDAFL 443
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
209-504 |
6.21e-11 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 64.41 E-value: 6.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 209 FDVLVIGGGPAGVSSAIYAARKGLRTGII--AERFGGQILDT------------LGIENFISVPYTEGPKLAENF----- 269
Cdd:PRK05249 6 YDLVVIGSGPAGEGAAMQAAKLGKRVAVIerYRNVGGGCTHTgtipskalreavLRLIGFNQNPLYSSYRVKLRItfadl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 270 ---KEHVKRYDIDVMERQ-----------RAKSIRRNElLEVELEKGAV--VKSKTVIIATGARWRNvnvPGEKEFKNKG 333
Cdd:PRK05249 86 larADHVINKQVEVRRGQyernrvdliqgRARFVDPHT-VEVECPDGEVetLTADKIVIATGSRPYR---PPDVDFDHPR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 334 V---------AYCPhcdgplfagKDVAVIGGGNSGIEAAIDLAGIVRHVTV-------LEFLpqlkaDKVLQERL-YRLP 396
Cdd:PRK05249 162 IydsdsilslDHLP---------RSLIIYGAGVIGCEYASIFAALGVKVTLintrdrlLSFL-----DDEISDALsYHLR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 397 N--VTVLTNvqtKEFTGKEKLDGITYIERDTnqEKHIEVQGVFVQIGLVPNTEWLE----GtIERNAMGEIIVNEKNETS 470
Cdd:PRK05249 228 DsgVTIRHN---EEVEKVEGGDDGVIVHLKS--GKKIKADCLLYANGRTGNTDGLNlenaG-LEADSRGQLKVNENYQTA 301
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 316941602 471 MPGVFAAGDctnspykqiVI--------AMGSGATAALSAFD 504
Cdd:PRK05249 302 VPHIYAVGD---------VIgfpslasaSMDQGRIAAQHAVG 334
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
209-479 |
6.57e-11 |
|
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member of the pyridine nucleotide disulfide oxidoreductase family contains a C-terminal motif Cys-SeCys-Gly, where SeCys is selenocysteine encoded by TGA (in some sequence reports interpreted as a stop codon). In some members of this subfamily, Cys-SeCys-Gly is replaced by Cys-Cys-Gly. The reach of the selenium atom at the C-term arm of the protein is proposed to allow broad substrate specificity.
Pssm-ID: 273624 [Multi-domain] Cd Length: 484 Bit Score: 64.49 E-value: 6.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 209 FDVLVIGGGPAGVSSAIYAARKGLRTGII--------AERFG----------------------GQIL---DTLGIeNFI 255
Cdd:TIGR01438 3 YDLIVIGGGSGGLAAAKEAAAYGAKVMLLdfvtptplGTRWGiggtcvnvgcipkklmhqaallGQALkdsRNYGW-KVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 256 SVPYTEGPKLAENFKEHVKRYDIDVMERQRAKSIR-RNELLEV----------ELEKGAVVKSKTVIIATGARWRNVNVP 324
Cdd:TIGR01438 82 ETVKHDWKRLVEAVQNHIGSLNWGYRVALREKKVKyENAYAEFvdkhrikatnKKGKEKIYSAERFLIATGERPRYPGIP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 325 GEKEFKNKG-----VAYCPhcdgplfaGKDVaVIGGGNSGIEAAIDLAGIVRHVTV------LEFLPQLKADKV---LQE 390
Cdd:TIGR01438 162 GAKELCITSddlfsLPYCP--------GKTL-VVGASYVALECAGFLAGIGLDVTVmvrsilLRGFDQDCANKVgehMEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 391 RLYRLPNVTV---LTNVQTK---EFTGKEKLDGITYierDTnqekhievqgVFVQIGLVPNTEWLE------GTIERNam 458
Cdd:TIGR01438 233 HGVKFKRQFVpikVEQIEAKvlvEFTDSTNGIEEEY---DT----------VLLAIGRDACTRKLNlenvgvKINKKT-- 297
|
330 340
....*....|....*....|.
gi 316941602 459 GEIIVNEKNETSMPGVFAAGD 479
Cdd:TIGR01438 298 GKIPADEEEQTNVPYIYAVGD 318
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
196-500 |
1.32e-10 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 63.63 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 196 QATESPSINEKEPFDVLVIGGGPAGVSSAIYAARKGLRTGIIaER--FGG----------QIL---------------DT 248
Cdd:PRK13748 86 LGGADKHSGNERPLHVAVIGSGGAAMAAALKAVEQGARVTLI-ERgtIGGtcvnvgcvpsKIMiraahiahlrrespfDG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 249 lGIENfiSVPYTEGPKLAENFKEHVK-----RYDiDVMERQRAKSIRRNEL-------LEVELEKGA--VVKSKTVIIAT 314
Cdd:PRK13748 165 -GIAA--TVPTIDRSRLLAQQQARVDelrhaKYE-GILDGNPAITVLHGEArfkddqtLIVRLNDGGerVVAFDRCLIAT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 315 GARWRNVNVPGEKEfknkgVAYCPHCDGpLFAG---KDVAVIGGGNSGIEAAIDLAGIVRHVTVLE----FLpqlKADKV 387
Cdd:PRK13748 241 GASPAVPPIPGLKE-----TPYWTSTEA-LVSDtipERLAVIGSSVVALELAQAFARLGSKVTILArstlFF---REDPA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 388 LQERL---YRLPNVTVLTNVQTKEftgkekldgITYIER----DTNqekHIEVQG--VFVQIGLVPNTEWLE---GTIER 455
Cdd:PRK13748 312 IGEAVtaaFRAEGIEVLEHTQASQ---------VAHVDGefvlTTG---HGELRAdkLLVATGRAPNTRSLAldaAGVTV 379
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 316941602 456 NAMGEIIVNEKNETSMPGVFAAGDCTNSPykQIV-IAMGSGATAAL 500
Cdd:PRK13748 380 NAQGAIVIDQGMRTSVPHIYAAGDCTDQP--QFVyVAAAAGTRAAI 423
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
207-484 |
8.42e-10 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 60.92 E-value: 8.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 207 EPFDVLVIGGGPAGVSSAIYAARKGLRTGIIAER---FGGQILdtlgieNFISVPYTEGPKLAEN---FKEHVKRYDIdV 280
Cdd:PRK07251 2 LTYDLIVIGFGKAGKTLAAKLASAGKKVALVEESkamYGGTCI------NIGCIPTKTLLVAAEKnlsFEQVMATKNT-V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 281 MERQRAK-----------------SIRRNELLEVEL-EKGAVVKSKTVIIATGARWRNVNVPGEKEFKN----KGVAYCP 338
Cdd:PRK07251 75 TSRLRGKnyamlagsgvdlydaeaHFVSNKVIEVQAgDEKIELTAETIVINTGAVSNVLPIPGLADSKHvydsTGIQSLE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 339 HCDgplfagKDVAVIGGGNSGIEAAIDLAGIVRHVTVLE----FLPQLK------ADKVLQERlyrlpNVTVLTNVQTKE 408
Cdd:PRK07251 155 TLP------ERLGIIGGGNIGLEFAGLYNKLGSKVTVLDaastILPREEpsvaalAKQYMEED-----GITFLLNAHTTE 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 316941602 409 FTGKEKLDGITyierdTNQEKHIeVQGVFVQIGLVPNTE--WLEGT-IERNAMGEIIVNEKNETSMPGVFAAGDCTNSP 484
Cdd:PRK07251 224 VKNDGDQVLVV-----TEDETYR-FDALLYATGRKPNTEplGLENTdIELTERGAIKVDDYCQTSVPGVFAVGDVNGGP 296
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
196-487 |
2.94e-09 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 59.24 E-value: 2.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 196 QATESPSINEKEP---FDVLVIGGGPAGVSSAIYAARKGLRTGIIAERFGG---------------------QILDTLGI 251
Cdd:PTZ00058 33 EASSAPTHLKKKPrmvYDLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGgtcvnvgcvpkkimfnaasihDILENSRH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 252 ENFISVPYTEGPKLAEN-----------FKEHVKRYDIDVMeRQRAKSIRRNELL------------------------- 295
Cdd:PTZ00058 113 YGFDTQFSFNLPLLVERrdkyirrlndiYRQNLKKDNVEYF-EGKGSLLSENQVLikkvsqvdgeadesdddevtivsag 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 296 EVELEKGAVVKSKTVIIATGarwrnvnvpGEKEFKN-KGVAYCPHCDG--PLFAGKDVAVIGGGnsgiEAAIDLAGIVR- 371
Cdd:PTZ00058 192 VSQLDDGQVIEGKNILIAVG---------NKPIFPDvKGKEFTISSDDffKIKEAKRIGIAGSG----YIAVELINVVNr 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 372 -----HVTVLEFLPQLKADKVLQERL---YRLPNVTVLTNVQTKEFTgKEKLDGITYIERDTNQEKHIEVqgVFVQIGLV 443
Cdd:PTZ00058 259 lgaesYIFARGNRLLRKFDETIINELendMKKNNINIITHANVEEIE-KVKEKNLTIYLSDGRKYEHFDY--VIYCVGRS 335
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 316941602 444 PNTEWL--EGTIERNAMGEIIVNEKNETSMPGVFAAGDCTNSPYKQ 487
Cdd:PTZ00058 336 PNTEDLnlKALNIKTPKGYIKVDDNQRTSVKHIYAVGDCCMVKKNQ 381
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
348-480 |
4.06e-09 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 59.07 E-value: 4.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 348 KDVAVIGGGNSGIEAAIDLAGIVRHVTVLEFLPQLKADKV-------LQERLYRLpNVTVLTNVQTKEFTGKEKLDGITY 420
Cdd:TIGR02374 141 KKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAKQLdqtagrlLQRELEQK-GLTFLLEKDTVEIVGATKADRIRF 219
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 316941602 421 IERDTnqekhIEVQGVFVQIGLVPNTEW-LEGTIERNamGEIIVNEKNETSMPGVFAAGDC 480
Cdd:TIGR02374 220 KDGSS-----LEADLIVMAAGIRPNDELaVSAGIKVN--RGIIVNDSMQTSDPDIYAVGEC 273
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
350-414 |
1.91e-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: 51.44 E-value: 1.91e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 316941602 350 VAVIGGGNSGIEAAIDLAGIVRHVTVLEFLPQLK------ADKVLQERLYRLpNVTVLTNVQTKEFTGKEK 414
Cdd:pfam00070 2 VVVVGGGYIGLELAGALARLGSKVTVVERRDRLLpgfdpeIAKILQEKLEKN-GIEFLLNTTVEAIEGNGD 71
|
|
| GlpB |
COG3075 |
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]; |
209-272 |
4.81e-08 |
|
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 442309 Cd Length: 415 Bit Score: 55.19 E-value: 4.81e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 316941602 209 FDVLVIGGGPAGVSSAIYAARKGLRTGIIAE-----RFGGQILDTLG---IENFISVPYTEGPKLAENFKEH 272
Cdd:COG3075 3 FDVVVIGGGLAGLTAAIRAAEAGLRVAIVSAgqsalHFSSGSLDLLGylpDGEPVADPFDALADLPEQAPEH 74
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
340-480 |
5.95e-08 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 54.92 E-value: 5.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 340 CDGPLFAGKDVAVIGGGNSGIEAAIDLAGIVRHVTVLE----FLPQLKADKV---LQERLYRLpNVTVLTN--VQTKEFT 410
Cdd:PRK04965 134 AETQLRDAQRVLVVGGGLIGTELAMDLCRAGKAVTLVDnaasLLASLMPPEVssrLQHRLTEM-GVHLLLKsqLQGLEKT 212
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 316941602 411 GkeklDGItyieRDT-NQEKHIEVQGVFVQIGLVPNTEWLEG---TIERNamgeIIVNEKNETSMPGVFAAGDC 480
Cdd:PRK04965 213 D----SGI----RATlDSGRSIEVDAVIAAAGLRPNTALARRaglAVNRG----IVVDSYLQTSAPDIYALGDC 274
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
210-480 |
8.29e-08 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 54.37 E-value: 8.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 210 DVLVIGGGPAGVSsAIYAARKGLRTGI----IAER----FGG---QIL-DTLGIENfISVPYtegpklaenfKEHVKRYD 277
Cdd:COG1252 3 RIVIVGGGFAGLE-AARRLRKKLGGDAevtlIDPNpyhlFQPllpEVAaGTLSPDD-IAIPL----------RELLRRAG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 278 IDVMeRQRAKSIRRNELlEVELEKGAVVKSKTVIIATGARWRNVNVPGEKEfknkgvaYCPHCDGP------------LF 345
Cdd:COG1252 71 VRFI-QGEVTGIDPEAR-TVTLADGRTLSYDYLVIATGSVTNFFGIPGLAE-------HALPLKTLedalalrerllaAF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 346 ------AGKDVAVIGGGNSGIEAAIDLAGIVRH-------------VTVLE----FLPQL------KADKVLQERlyrlp 396
Cdd:COG1252 142 eraerrRLLTIVVVGGGPTGVELAGELAELLRKllrypgidpdkvrITLVEagprILPGLgeklseAAEKELEKR----- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 397 NVTVLTNVQTKEFTGkeklDGITyierdTNQEKHIEVQGVFVQIGLVPNtEWLEGT-IERNAMGEIIVNEKNET-SMPGV 474
Cdd:COG1252 217 GVEVHTGTRVTEVDA----DGVT-----LEDGEEIPADTVIWAAGVKAP-PLLADLgLPTDRRGRVLVDPTLQVpGHPNV 286
|
....*.
gi 316941602 475 FAAGDC 480
Cdd:COG1252 287 FAIGDC 292
|
|
| PfPDO_like_N |
cd02975 |
Pyrococcus furiosus protein disulfide oxidoreductase (PfPDO)-like family, N-terminal TRX-fold ... |
4-97 |
8.79e-08 |
|
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: 50.47 E-value: 8.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 4 DAEIMQQLEQYLTLLENDIVIKVNAGND--KVSVDMVRLIDEIAKLTPKIH------------VEKAELDRTPSFSVNR- 68
Cdd:cd02975 5 DEDRKALKEEFFKEMKNPVDLVVFSSKEgcQYCEVTKQLLEELSELSDKLKleiydfdedkekAEKYGVERVPTTIFLQd 84
|
90 100
....*....|....*....|....*....
gi 316941602 69 PNEDTGIVFAGIPLGHEFNSLVLALLQVG 97
Cdd:cd02975 85 GGKDGGIRYYGLPAGYEFASLIEDIVRVS 113
|
|
| Thioredoxin_3 |
pfam13192 |
Thioredoxin domain; |
124-194 |
1.56e-07 |
|
Thioredoxin domain;
Pssm-ID: 433026 [Multi-domain] Cd Length: 71 Bit Score: 48.36 E-value: 1.56e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 316941602 124 VSLSCHNCPDVVQALNiMSVLNPNITHTMIDGAVFrEEVESKGIMAVPTIYLNGNFFESGRLTLEEILAKL 194
Cdd:pfam13192 1 LGPGCPKCPQLEKAVK-EAAAELGIDAEVEKVTDF-PEIAKYGVMSTPALVINGKVVSSGKVPSEEEIRKL 69
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
203-317 |
3.53e-07 |
|
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: 52.12 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 203 INEKEPFDVLVIGGGPAGVSSAIYAARKGLRTGIIaERfGGQILDTLGienfisvpytegPKLAENFKEHVKRYDIDVME 282
Cdd:COG0446 119 LKEFKGKRAVVIGGGPIGLELAEALRKRGLKVTLV-ER-APRLLGVLD------------PEMAALLEEELREHGVELRL 184
|
90 100 110
....*....|....*....|....*....|....*
gi 316941602 283 RQRAKSIRRNELLEVELEKGAVVKSKTVIIATGAR 317
Cdd:COG0446 185 GETVVAIDGDDKVAVTLTDGEEIPADLVVVAPGVR 219
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
210-244 |
1.06e-06 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 51.07 E-value: 1.06e-06
10 20 30
....*....|....*....|....*....|....*...
gi 316941602 210 DVLVIGGGPAGVSSAIYAARKGLRTgIIAERF---GGQ 244
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKV-LLVERRgflGGM 37
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
209-482 |
1.07e-06 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 50.97 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 209 FDVLVIGGGPAGVSSAIYAARKGLRTGII--------------------------------AERFGGQILDT--LGIENF 254
Cdd:PLN02507 26 FDLFVIGAGSGGVRAARFSANFGAKVGICelpfhpissesiggvggtcvirgcvpkkilvyGATFGGEFEDAknYGWEIN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 255 ISVPYtEGPKLAENFKEHVKRYD-----------IDVMErQRAKSIRRNELlEVELEKGAVVK--SKTVIIATGARWRNV 321
Cdd:PLN02507 106 EKVDF-NWKKLLQKKTDEILRLNgiykrllanagVKLYE-GEGKIVGPNEV-EVTQLDGTKLRytAKHILIATGSRAQRP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 322 NVPGeKEFKNKGVAYCPHCDGPlfagKDVAVIGGGNSGIEAAIDLAGIVRHVTVL--EFLPQLKADKVLQERLYR-LPNV 398
Cdd:PLN02507 183 NIPG-KELAITSDEALSLEELP----KRAVVLGGGYIAVEFASIWRGMGATVDLFfrKELPLRGFDDEMRAVVARnLEGR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 399 TVLTNVQTKeFTGKEKLDGITYIERDTNQEkhIEVQGVFVQIGLVPNTEWL---EGTIERNAMGEIIVNEKNETSMPGVF 475
Cdd:PLN02507 258 GINLHPRTN-LTQLTKTEGGIKVITDHGEE--FVADVVLFATGRAPNTKRLnleAVGVELDKAGAVKVDEYSRTNIPSIW 334
|
....*..
gi 316941602 476 AAGDCTN 482
Cdd:PLN02507 335 AIGDVTN 341
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
209-272 |
1.12e-06 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 51.00 E-value: 1.12e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 316941602 209 FDVLVIGGGPAGVSSAIYAARKGLRTGIIAE-----RFGGQILDTLGI---ENFISVPYTEGPKLAENFKEH 272
Cdd:PRK05329 3 FDVLVIGGGLAGLTAALAAAEAGKRVALVAKgqgalHFSSGSIDLLGYlpdGQPVSDPFEALAALAEQAPEH 74
|
|
| GIDA |
pfam01134 |
Glucose inhibited division protein A; |
210-329 |
1.23e-06 |
|
Glucose inhibited division protein A;
Pssm-ID: 250388 [Multi-domain] Cd Length: 391 Bit Score: 50.63 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 210 DVLVIGGGPAGVSSAIYAARKGLRTGIIAERFG----------------GQI---LDTLG---------------IENFI 255
Cdd:pfam01134 1 DVIVIGGGHAGCEAALAAARMGAKVLLITHNTDtiaelscnpsiggiakGHLvreIDALGglmgkaadktgiqfrMLNTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 256 SVPYTEGPKLA---ENFKEHVKRY-----DIDVMErQRAKSI--RRNELLEVELEKGAVVKSKTVIIATGARWRNVNVPG 325
Cdd:pfam01134 81 KGPAVRALRAQvdrDLYSKEMTETlenhpNLTLIQ-GEVTDLipENGKVKGVVTEDGEEYKAKAVVLATGTFLNGKIHIG 159
|
....
gi 316941602 326 EKEF 329
Cdd:pfam01134 160 LKCY 163
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
209-332 |
1.28e-06 |
|
geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]
Pssm-ID: 273936 [Multi-domain] Cd Length: 295 Bit Score: 50.01 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 209 FDVLVIGGGPAGVSSAIYAARKGLRTGII-AERFGGQILDTLGIENFISVPYTEGPKLAENFKEHVKRY-------DIDV 280
Cdd:TIGR02032 1 YDVVVVGAGPAGASAAYRLADKGLRVLLLeKKSFPRYKPCGGALSPRALEELDLPGELIVNLVRGARFFspngdsvEIPI 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 281 mERQRAKSIRRNE----LLEVELEKGAVV----KSKTVIIATGARWRNVNvPGEKEFKNK 332
Cdd:TIGR02032 81 -ETELAYVIDRDAfdeqLAERAQEAGAELrlgtRVLDVEIHDDRVVVIVR-GSEGTVTAK 138
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
209-481 |
8.39e-06 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 48.09 E-value: 8.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 209 FDVLVIGGGPAGVSSAIYAARKGLRTGII---AERFGGQILDTLGI-----------ENFISVPYTEGPKLA-----ENF 269
Cdd:PRK08010 4 YQAVIIGFGKAGKTLAVTLAKAGWRVALIeqsNAMYGGTCINIGCIptktlvhdaqqHTDFVRAIQRKNEVVnflrnKNF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 270 KEHVKRYDIDVMErQRAKSIRRNELLEVELEKGAVVKSKTVIIATGARWRNVNVPGEKE----FKNKGVAYCPHCDGPLf 345
Cdd:PRK08010 84 HNLADMPNIDVID-GQAEFINNHSLRVHRPEGNLEIHGEKIFINTGAQTVVPPIPGITTtpgvYDSTGLLNLKELPGHL- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 346 agkdvAVIGGGNSGIEAAIDLAGIVRHVTVLE----FLPQLKAD------KVLQERlyrlpNVTVLTNVQTKEFTGKEkl 415
Cdd:PRK08010 162 -----GILGGGYIGVEFASMFANFGSKVTILEaaslFLPREDRDiadniaTILRDQ-----GVDIILNAHVERISHHE-- 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 316941602 416 dgiTYIERDTNQEKHIeVQGVFVQIGLVPNTEWLE---GTIERNAMGEIIVNEKNETSMPGVFAAGDCT 481
Cdd:PRK08010 230 ---NQVQVHSEHAQLA-VDALLIASGRQPATASLHpenAGIAVNERGAIVVDKYLHTTADNIWAMGDVT 294
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
210-245 |
2.88e-05 |
|
FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.
Pssm-ID: 395718 [Multi-domain] Cd Length: 398 Bit Score: 46.51 E-value: 2.88e-05
10 20 30
....*....|....*....|....*....|....*...
gi 316941602 210 DVLVIGGGPAGVSSAIYAARKGLRTGII--AERFGGQI 245
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVekGQPFGGAT 38
|
|
| PLN02464 |
PLN02464 |
glycerol-3-phosphate dehydrogenase |
207-240 |
5.01e-05 |
|
glycerol-3-phosphate dehydrogenase
Pssm-ID: 215257 [Multi-domain] Cd Length: 627 Bit Score: 45.93 E-value: 5.01e-05
10 20 30
....*....|....*....|....*....|....
gi 316941602 207 EPFDVLVIGGGPAGVSSAIYAARKGLRTGIIaER 240
Cdd:PLN02464 70 EPLDVLVVGGGATGAGVALDAATRGLRVGLV-ER 102
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
209-243 |
5.28e-05 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 45.61 E-value: 5.28e-05
10 20 30
....*....|....*....|....*....|....*..
gi 316941602 209 FDVLVIGGGPAGVSSAIYAARKGLRTGII--AERFGG 243
Cdd:COG1233 4 YDVVVIGAGIGGLAAAALLARAGYRVTVLekNDTPGG 40
|
|
| glycerol3P_GlpB |
TIGR03378 |
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ... |
209-238 |
5.90e-05 |
|
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are the B subunit, product of the glpB gene, of a three-subunit, membrane-anchored, FAD-dependent anaerobic glycerol-3-phosphate dehydrogenase. [Energy metabolism, Anaerobic]
Pssm-ID: 213807 Cd Length: 419 Bit Score: 45.39 E-value: 5.90e-05
10 20 30
....*....|....*....|....*....|
gi 316941602 209 FDVLVIGGGPAGVSSAIYAARKGLRTGIIA 238
Cdd:TIGR03378 1 FDVIIIGGGLAGLSCALRLAEAGKKCAIIA 30
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
440-488 |
6.07e-05 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 45.54 E-value: 6.07e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 316941602 440 IGLVPNTEWLEGT-IERNAMGEIIVNEKNETSMPGVFAAGDCTNSPYKQI 488
Cdd:PRK13512 237 VGTHPNSKFIESSnIKLDDKGFIPVNDKFETNVPNIYAIGDIITSHYRHV 286
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
197-498 |
6.45e-05 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 45.64 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 197 ATESPSINEKE-PFDVLVIGGGPAGVSSAIYAARKGLRTGIIAERFGGQILDTLGIENFISV-----P---YTEGPKLAE 267
Cdd:PLN02546 67 AAPNGAESERHyDFDLFTIGAGSGGVRASRFASNFGASAAVCELPFATISSDTLGGVGGTCVlrgcvPkklLVYASKYSH 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 268 NFKEHVK---RYDIDV------------MERQRAKSIRRNELLEVELE----KGAVVKSKTV------------IIATGA 316
Cdd:PLN02546 147 EFEESRGfgwKYETEPkhdwntlianknAELQRLTGIYKNILKNAGVTliegRGKIVDPHTVdvdgklytarniLIAVGG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 317 RWRNVNVPGEKEFKNKGVAYcphcDGPLFAGKdVAVIGGGNSGIEAAIDLAGIVRHVTVleFLPQLKADKVLQERLYRLp 396
Cdd:PLN02546 227 RPFIPDIPGIEHAIDSDAAL----DLPSKPEK-IAIVGGGYIALEFAGIFNGLKSDVHV--FIRQKKVLRGFDEEVRDF- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 397 nVTVLTNVQTKEFTGKEKLDGIT-----YIERDTNQEKHIEVQGVFVQIGLVPNTEWL---EGTIERNAMGEIIVNEKNE 468
Cdd:PLN02546 299 -VAEQMSLRGIEFHTEESPQAIIksadgSLSLKTNKGTVEGFSHVMFATGRKPNTKNLgleEVGVKMDKNGAIEVDEYSR 377
|
330 340 350
....*....|....*....|....*....|
gi 316941602 469 TSMPGVFAAGDCTNSPYKQIVIAMGSGATA 498
Cdd:PLN02546 378 TSVPSIWAVGDVTDRINLTPVALMEGGALA 407
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
202-238 |
7.94e-05 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 44.89 E-value: 7.94e-05
10 20 30
....*....|....*....|....*....|....*..
gi 316941602 202 SINEKEPFDVLVIGGGPAGVSSAIYAARKGLRTGIIA 238
Cdd:PRK07494 1 SLMEKEHTDIAVIGGGPAGLAAAIALARAGASVALVA 37
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
209-329 |
8.29e-05 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 44.88 E-value: 8.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 209 FDVLVIGGGPAGVSSAIYAARKGLRTGII--AERFGGQILDT-----------LGIENFISvPYTEGPKL---------A 266
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIekGKKLGRKILISgggrcnvtnlsEEPDNFLS-RYPGNPKFlksalsrftP 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 316941602 267 ENFKEHVKRYDIDVMER---------QRAKSIRRneLLEVELEKGAVVksktviIATGARWRNVNVPGEKEF 329
Cdd:pfam03486 80 WDFIAFFESLGVPLKEEdhgrlfpdsDKASDIVD--ALLNELKELGVK------IRLRTRVLSVEKDDDGRF 143
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
188-317 |
1.24e-04 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 44.35 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 188 EEILAKLGQAtespsiNEKEPFDVLVIGGGPAGV--SSAIYAARKGLRT--GIIAERF-------GGQILDTLgienfis 256
Cdd:COG1252 135 ERLLAAFERA------ERRRLLTIVVVGGGPTGVelAGELAELLRKLLRypGIDPDKVritlveaGPRILPGL------- 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 316941602 257 vpyteGPKLAENFKEHVKRYDIDVMERQRAKSIRRNellEVELEKGAVVKSKTVIIATGAR 317
Cdd:COG1252 202 -----GEKLSEAAEKELEKRGVEVHTGTRVTEVDAD---GVTLEDGEEIPADTVIWAAGVK 254
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
199-506 |
1.28e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 44.76 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 199 ESPSINEKepfdVLVIGGGPAGVSSAIYAARKGLRTGIIAE--RFGGQIldTLGIENFiSVPYTEGPKlaenfkehvkry 276
Cdd:PRK13984 278 EPEKKNKK----VAIVGSGPAGLSAAYFLATMGYEVTVYESlsKPGGVM--RYGIPSY-RLPDEALDK------------ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 277 DIDVMERQRAK-----SIRRNELLEvELEKgavvKSKTVIIATG-ARWRNVNVPGE------------KEFKNKGVAYCP 338
Cdd:PRK13984 339 DIAFIEALGVKihlntRVGKDIPLE-ELRE----KHDAVFLSTGfTLGRSTRIPGTdhpdviqalpllREIRDYLRGEGP 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 339 HCDGPlfagKDVAVIGGGNSGIEAAIDLA-------GIVR-HVTVLEF-LPQLKAD-----KVLQERLYRLPN---VTVL 401
Cdd:PRK13984 414 KPKIP----RSLVVIGGGNVAMDIARSMArlqkmeyGEVNvKVTSLERtFEEMPADmeeieEGLEEGVVIYPGwgpMEVV 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 402 TN------VQTKEFTGKEKLDGITYIERDTNQEKHIEVQGVFVQIGLVPNTEWLEGTIERN---AMGEIIVNEKNETSMP 472
Cdd:PRK13984 490 IEndkvkgVKFKKCVEVFDEEGRFNPKFDESDQIIVEADMVVEAIGQAPDYSYLPEELKSKlefVRGRILTNEYGQTSIP 569
|
330 340 350
....*....|....*....|....*....|....
gi 316941602 473 GVFAAGDCTNSPykQIVIAMGSGATAALSAFDYL 506
Cdd:PRK13984 570 WLFAGGDIVHGP--DIIHGVADGYWAAEGIDMYL 601
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
348-411 |
1.69e-04 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 44.08 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 348 KDVAVIGGGNSGIEAAIDLAGIVRHVTVLEFLPQL-----KADKVLQ-------------ERLYRLPNVTVLTNVQTKEF 409
Cdd:COG1148 141 KRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELggraaQLHKTFPgldcpqcilepliAEVEANPNITVYTGAEVEEV 220
|
..
gi 316941602 410 TG 411
Cdd:COG1148 221 SG 222
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
209-243 |
1.86e-04 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 44.05 E-value: 1.86e-04
10 20 30
....*....|....*....|....*....|....*..
gi 316941602 209 FDVLVIGGGPAGVSSAIYAARKGLRTGII--AERFGG 243
Cdd:COG1053 4 YDVVVVGSGGAGLRAALEAAEAGLKVLVLekVPPRGG 40
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
432-481 |
2.01e-04 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 43.70 E-value: 2.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 316941602 432 EVQG--VFVQIGLVPNTEWL---EGTIERNAMGEIIVNEKNETSMPGVFAAGDCT 481
Cdd:PRK07845 260 TVEGshALMAVGSVPNTAGLgleEAGVELTPSGHITVDRVSRTSVPGIYAAGDCT 314
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
205-243 |
2.26e-04 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 43.87 E-value: 2.26e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 316941602 205 EKEPFDVLVIGGGPAGVSSAIYAARKGLRTGII--AERFGG 243
Cdd:PRK07843 4 TVQEYDVVVVGSGAAGMVAALTAAHRGLSTVVVekAPHYGG 44
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
207-252 |
2.53e-04 |
|
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: 43.00 E-value: 2.53e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 207 EPFDVLVIGGGPAGVSSAIYAARKGLRTGII----AERFGG----------QILDTLGIE 252
Cdd:COG0654 2 MRTDVLIVGGGPAGLALALALARAGIRVTVVerapPPRPDGrgialsprslELLRRLGLW 61
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
199-243 |
3.03e-04 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 43.57 E-value: 3.03e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 316941602 199 ESPSINEKEPFDVLVIGGGPAGVSSAIYAARKGLRTGII--AERFGG 243
Cdd:PRK12843 7 ELSPERWDAEFDVIVIGAGAAGMSAALFAAIAGLKVLLVerTEYVGG 53
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
210-285 |
3.79e-04 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 42.77 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 210 DVLVIGGGPAGVSSAIYAARKGLRTGIIAE----------RFGGQI---LDTLGIENFISVpYTEGPKLaenFKEHVKRY 276
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERgddpgsgasgRNAGLIhpgLRYLEPSELARL-ALEALDL---WEELEEEL 76
|
....*....
gi 316941602 277 DIDVMERQR 285
Cdd:pfam01266 77 GIDCGFRRC 85
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
210-233 |
4.94e-04 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 42.20 E-value: 4.94e-04
10 20
....*....|....*....|....
gi 316941602 210 DVLVIGGGPAGVSSAIYAARKGLR 233
Cdd:COG0665 4 DVVVIGGGIAGLSTAYHLARRGLD 27
|
|
| PRK07121 |
PRK07121 |
FAD-binding protein; |
210-243 |
5.27e-04 |
|
FAD-binding protein;
Pssm-ID: 180854 [Multi-domain] Cd Length: 492 Bit Score: 42.57 E-value: 5.27e-04
10 20 30
....*....|....*....|....*....|....
gi 316941602 210 DVLVIGGGPAGVSSAIYAARKGLRTgIIAERFGG 243
Cdd:PRK07121 22 DVVVVGFGAAGACAAIEAAAAGARV-LVLERAAG 54
|
|
| sdhA |
PRK07803 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
205-237 |
5.60e-04 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 236101 [Multi-domain] Cd Length: 626 Bit Score: 42.72 E-value: 5.60e-04
10 20 30
....*....|....*....|....*....|...
gi 316941602 205 EKEPFDVLVIGGGPAGVSSAIYAARKGLRTGII 237
Cdd:PRK07803 5 ERHSYDVVVIGAGGAGLRAAIEARERGLRVAVV 37
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
210-243 |
9.27e-04 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 42.01 E-value: 9.27e-04
10 20 30
....*....|....*....|....*....|....*..
gi 316941602 210 DVLVIGGGPAGVSSAIYAARKGLRTgIIAE---RFGG 243
Cdd:PRK06134 14 DVLVIGSGAAGLSAAVTAAWHGLKV-IVVEkdpVFGG 49
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
310-499 |
1.01e-03 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 41.74 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 310 VIIATGARW-RNVNVPGE--------KEF---KNKGVAYCPHCDGPL--FAGKDVAVIGGGNSGIEAAIDLAGIVRHVTV 375
Cdd:PRK12779 396 IFVGTGAGLpTFMNVPGEhllgvmsaNEFltrVNLMRGLDDDYETPLpeVKGKEVFVIGGGNTAMDAARTAKRLGGNVTI 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 376 LEFLPQLKADKVLQERLYRLPNVTVLTNVQT-KEFTGKEK--------LDGITYIERD---------TNQEKHIEVQGVF 437
Cdd:PRK12779 476 VYRRTKSEMPARVEELHHALEEGINLAVLRApREFIGDDHthfvthalLDVNELGEPDksgrrspkpTGEIERVPVDLVI 555
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 316941602 438 VQIGLVPN--TEWLEGTIERNAMGEIIVNE-KNETSMPGVFAAGDCTNSPYKQIViAMGSGATAA 499
Cdd:PRK12779 556 MALGNTANpiMKDAEPGLKTNKWGTIEVEKgSQRTSIKGVYSGGDAARGGSTAIR-AAGDGQAAA 619
|
|
| PRK08275 |
PRK08275 |
putative oxidoreductase; Provisional |
463-506 |
1.28e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 181346 [Multi-domain] Cd Length: 554 Bit Score: 41.19 E-value: 1.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 316941602 463 VNEKNETSMPGVFAAGDCTNSPYKQIVIAMGSGATAALSAFDYL 506
Cdd:PRK08275 361 VNEKAETTVPGLYAAGDMASVPHNYMLGAFTYGWFAGENAAEYV 404
|
|
| COG3573 |
COG3573 |
Predicted oxidoreductase [General function prediction only]; |
210-244 |
2.38e-03 |
|
Predicted oxidoreductase [General function prediction only];
Pssm-ID: 442794 [Multi-domain] Cd Length: 551 Bit Score: 40.55 E-value: 2.38e-03
10 20 30
....*....|....*....|....*....|....*....
gi 316941602 210 DVLVIGGGPAGVSSAIYAARKGLRTGII----AERFGGQ 244
Cdd:COG3573 7 DVIVVGAGLAGLVAAAELADAGRRVLLLdqepEANLGGQ 45
|
|
| MnmG |
COG0445 |
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ... |
209-250 |
2.46e-03 |
|
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440214 [Multi-domain] Cd Length: 626 Bit Score: 40.37 E-value: 2.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 316941602 209 FDVLVIGGGPAGVSSAIYAARKGLRTGIIAERfggqiLDTLG 250
Cdd:COG0445 7 YDVIVVGGGHAGCEAALAAARMGAKTLLLTHN-----LDTIG 43
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
346-382 |
2.56e-03 |
|
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];
Pssm-ID: 442577 [Multi-domain] Cd Length: 445 Bit Score: 40.22 E-value: 2.56e-03
10 20 30
....*....|....*....|....*....|....*..
gi 316941602 346 AGKDVAVIGGGNSGIEAAIDLAGIVRHVTVLEFLPQL 382
Cdd:COG3349 2 MPPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRL 38
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
212-315 |
4.17e-03 |
|
flavoprotein, HI0933 family; The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 272992 [Multi-domain] Cd Length: 400 Bit Score: 39.50 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 212 LVIGGGPAGVSSAIYAARKGLRTGII--AERFGGQIL------------------------------------DTLGIEN 253
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLekNKKIGKKLLisgggrcnltnscptpefvayyprngkflrsalsrfSNKDLID 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 316941602 254 F---ISVPYTEGPK------------LAENFKEHVKRYDIDVMERQRAKSIRRNEL-LEVELEKGaVVKSKTVIIATG 315
Cdd:TIGR00275 81 FfesLGLELKVEEDgrvfpcsdsaadVLDALLNELKELGVEILTNSKVKSIEKEDGgFGVETSGG-EYEADKVIIATG 157
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
210-243 |
4.31e-03 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 39.68 E-value: 4.31e-03
10 20 30
....*....|....*....|....*....|....*..
gi 316941602 210 DVLVIGGGPAGVSSAIYAARKGLRTgIIAER---FGG 243
Cdd:PRK12842 11 DVLVIGSGAGGLSAAITARKLGLDV-VVLEKepvFGG 46
|
|
| PRK08626 |
PRK08626 |
fumarate reductase flavoprotein subunit; Provisional |
210-234 |
5.76e-03 |
|
fumarate reductase flavoprotein subunit; Provisional
Pssm-ID: 181507 [Multi-domain] Cd Length: 657 Bit Score: 39.19 E-value: 5.76e-03
10 20
....*....|....*....|....*
gi 316941602 210 DVLVIGGGPAGVSSAIYAARKGLRT 234
Cdd:PRK08626 7 DALVIGAGLAGLRVAIAAAQRGLDT 31
|
|
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
207-240 |
6.69e-03 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 39.12 E-value: 6.69e-03
10 20 30
....*....|....*....|....*....|....
gi 316941602 207 EPFDVLVIGGGPAGVSSAIYAARKGLRTgIIAER 240
Cdd:PRK06183 9 HDTDVVIVGAGPVGLTLANLLGQYGVRV-LVLER 41
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
209-249 |
7.93e-03 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 38.77 E-value: 7.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 316941602 209 FDVLVIGGGPAGVSSAIYAARKGLRTGIIaERfggQILDTL 249
Cdd:PRK09126 4 SDIVVVGAGPAGLSFARSLAGSGLKVTLI-ER---QPLAAL 40
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
210-245 |
9.56e-03 |
|
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis
Pssm-ID: 440845 [Multi-domain] Cd Length: 443 Bit Score: 38.27 E-value: 9.56e-03
10 20 30
....*....|....*....|....*....|....*...
gi 316941602 210 DVLVIGGGPAGVSSAIYAARKGLRTGII--AERFGGQI 245
Cdd:COG1232 3 RVAVIGGGIAGLTAAYRLAKAGHEVTVLeaSDRVGGLI 40
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
203-315 |
9.65e-03 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 37.97 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316941602 203 INEKEPF---DVLVIGGGPAGVSSAIYAARKGLRTGIIAERFGgqiLDTLGIENFISV-PYTEgpklaENFKEHVKRYDI 278
Cdd:pfam13738 147 VKDFHPYagqKVVVIGGYNSAVDAALELVRKGARVTVLYRGSE---WEDRDSDPSYSLsPDTL-----NRLEELVKNGKI 218
|
90 100 110
....*....|....*....|....*....|....*....
gi 316941602 279 DVMERQRAKSIRRNEL-LEVELEKGAVVKSKT-VIIATG 315
Cdd:pfam13738 219 KAHFNAEVKEITEVDVsYKVHTEDGRKVTSNDdPILATG 257
|
|
| |
