|
Name |
Accession |
Description |
Interval |
E-value |
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
119-432 |
3.11e-45 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 159.90 E-value: 3.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 119 EILVIGGGPAGLEASLWAAKAGADVILLDQnPKLGGQLV--KQTHKFFGSAkenAGTRGVTIAKKLIEEVvATSNITVYS 196
Cdd:COG0492 2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEG-GEPGGQLAttKEIENYPGFP---EGISGPELAERLREQA-ERFGAEILL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 197 GfTAFGW-FQGSVCAADQDHAVLFHPRKVIVATGAAEKMLMFKNNDMP---GVFGAGAAQTLMnvygiKPGNKVLMVGAG 272
Cdd:COG0492 77 E-EVTSVdKDDGPFRVTTDDGTEYEAKAVIIATGAGPRKLGLPGEEEFegrGVSYCATCDGFF-----FRGKDVVVVGGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 273 NVGLIVSYQLMQAGIEVvgviegaprvggYLVH------ASKI------ARNGVRIMTRHTVLEAVGTDHVEAAIIAEVD 340
Cdd:COG0492 151 DSALEEALYLTKFASKV------------TLIHrrdelrASKIlverlrANPKIEVLWNTEVTEIEGDGRVEGVTLKNVK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 341 ekwqpiPGTEQRVECDTICLSAGLKPSTELLEQAKLDLAYTGELggwvaKRNWAMRTSNPDIFAAGDASG--IEEASTAM 418
Cdd:COG0492 219 ------TGEEKELEVDGVFVAIGLKPNTELLKGLGLELDEDGYI-----VVDEDMETSVPGVFAAGDVRDykYRQAATAA 287
|
330
....*....|....
gi 2015191093 419 MEGKIAGLQAAYDL 432
Cdd:COG0492 288 GEGAIAALSAARYL 301
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
120-421 |
1.26e-32 |
|
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: 125.89 E-value: 1.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 120 ILVIGGGPAGLEASLWAAKAGADVILLDQNP-KLGGQLVKqtHKFFGSAKENAGTRGVTIA-KKLIEEVVA--TSNITVY 195
Cdd:pfam07992 3 VVVIGGGPAGLAAALTLAQLGGKVTLIEDEGtCPYGGCVL--SKALLGAAEAPEIASLWADlYKRKEEVVKklNNGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 196 SGFTAFGWFQGS--VCAADQDHAVLFHP--RKVIVATGAAEKMLmfknnDMPGV--FGAGAAQTLMNVYGIKPG---NKV 266
Cdd:pfam07992 81 LGTEVVSIDPGAkkVVLEELVDGDGETItyDRLVIATGARPRLP-----PIPGVelNVGFLVRTLDSAEALRLKllpKRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 267 LMVGAGNVGLIVSYQLMQAGIEVVgVIEGAPRVGGYLVH-ASKIA-----RNGVRIMTRHTVLEAVGTDHVEAAIIaevd 340
Cdd:pfam07992 156 VVVGGGYIGVELAAALAKLGKEVT-LIEALDRLLRAFDEeISAALekaleKNGVEVRLGTSVKEIIGDGDGVEVIL---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 341 ekwqpipGTEQRVECDTICLSAGLKPSTELLEQAKLDLaytGELGGWVAKRNwaMRTSNPDIFAAGDA--SGIEEASTAM 418
Cdd:pfam07992 231 -------KDGTEIDADLVVVAIGRRPNTELLEAAGLEL---DERGGIVVDEY--LRTSVPGIYAAGDCrvGGPELAQNAV 298
|
...
gi 2015191093 419 MEG 421
Cdd:pfam07992 299 AQG 301
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
223-429 |
9.22e-29 |
|
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: 115.68 E-value: 9.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 223 KVIVATGAAEKMLMFKNNDMPGVFGAGA---AQTLMNVYGIKPGNKVLMVGAGNVGLIVSYQLMQAGIEVVgVIEGAPRV 299
Cdd:COG0446 81 KLVLATGARPRPPPIPGLDLPGVFTLRTlddADALREALKEFKGKRAVVIGGGPIGLELAEALRKRGLKVT-LVERAPRL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 300 GGYL-------VHAsKIARNGVRIMTRHTVLEAVGTDHVEAAIiaevdekwqpipGTEQRVECDTICLSAGLKPSTELLE 372
Cdd:COG0446 160 LGVLdpemaalLEE-ELREHGVELRLGETVVAIDGDDKVAVTL------------TDGEEIPADLVVVAPGVRPNTELAK 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2015191093 373 QAKLDLaytGELGGWVAKRNwaMRTSNPDIFAAGDASG-----------IEEASTAMMEGKIAGLQAA 429
Cdd:COG0446 227 DAGLAL---GERGWIKVDET--LQTSDPDVYAAGDCAEvphpvtgktvyIPLASAANKQGRVAAENIL 289
|
|
| Fer2_4 |
pfam13510 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
17-99 |
1.32e-27 |
|
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which a beta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated. This cluster appears within sarcosine oxidase proteins.
Pssm-ID: 433268 [Multi-domain] Cd Length: 82 Bit Score: 105.31 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 17 GNPVHVTYDGRQITAYPQETVAMALYASGVKqYSTSSRFYRPRGMFCAIGKCSSCMMRVDGIPNTRTCVLQVRDGMEVET 96
Cdd:pfam13510 1 SRPVTFTFDGRPVTAPEGDTIAAALLANGVR-VPRSCKYGRPRGIFCAMGECRNCLVEVDGVPNVRACTTPVREGMVVRT 79
|
...
gi 2015191093 97 QHG 99
Cdd:pfam13510 80 QNG 82
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
223-407 |
3.05e-22 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 98.29 E-value: 3.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 223 KVIVATGAAEKMLMFKNNDMPGVFGAGaaqTLMNVYGI----KPGNKVLMVGAGNVGLIVSYQLMQAGIEVVgVIEGAPR 298
Cdd:COG1251 101 KLVLATGSRPRVPPIPGADLPGVFTLR---TLDDADALraalAPGKRVVVIGGGLIGLEAAAALRKRGLEVT-VVERAPR 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 299 V--------GGYLVHAsKIARNGVRIMTRHTVLEAVGTDHVEAAIIAEvdekwqpipGTEqrVECDTICLSAGLKPSTEL 370
Cdd:COG1251 177 LlprqldeeAGALLQR-LLEALGVEVRLGTGVTEIEGDDRVTGVRLAD---------GEE--LPADLVVVAIGVRPNTEL 244
|
170 180 190
....*....|....*....|....*....|....*..
gi 2015191093 371 LEQAKLDLAytgelGGWVAkrNWAMRTSNPDIFAAGD 407
Cdd:COG1251 245 ARAAGLAVD-----RGIVV--DDYLRTSDPDIYAAGD 274
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
120-424 |
3.78e-16 |
|
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: 80.18 E-value: 3.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 120 ILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGGQLVkqthkfFGsakenagtrgvtIAK-KLIEEVVAT-------SN 191
Cdd:COG0493 124 VAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGGLLR------YG------------IPEfRLPKDVLDReielieaLG 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 192 ITVYSGFTAfgwfqGSVCAADQ-----DHavlfhprkVIVATGA-AEKMLMFKNNDMPGVFGA-----GAAQTLMNVYGI 260
Cdd:COG0493 186 VEFRTNVEV-----GKDITLDElleefDA--------VFLATGAgKPRDLGIPGEDLKGVHSAmdfltAVNLGEAPDTIL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 261 KPGNKVLMVGAGNVGLIVSYQLMQAGIEVVGVIEGAPR--VGGYL--VHASKiaRNGVRIMTRHTVLEAVGTD--HVEAA 334
Cdd:COG0493 253 AVGKRVVVIGGGNTAMDCARTALRLGAESVTIVYRRTReeMPASKeeVEEAL--EEGVEFLFLVAPVEIIGDEngRVTGL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 335 IIAEV-----DE----KWQPIPGTEQRVECDTICLSAGLKPSTELLEQAkLDLAYTGelGGWVAKRNWAMRTSNPDIFAA 405
Cdd:COG0493 331 ECVRMelgepDEsgrrRPVPIEGSEFTLPADLVILAIGQTPDPSGLEEE-LGLELDK--RGTIVVDEETYQTSLPGVFAG 407
|
330 340
....*....|....*....|...
gi 2015191093 406 GDA-SGieeAST---AMMEGKIA 424
Cdd:COG0493 408 GDAvRG---PSLvvwAIAEGRKA 427
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
120-429 |
1.04e-14 |
|
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: 75.89 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 120 ILVIGGGPAGLEASLWAAKAGADVILLDQnPKLGG-----------------QLVKQTHKF--FGSakeNAGTRGVTIAK 180
Cdd:COG1249 6 LVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLGGtclnvgcipskallhaaEVAHEARHAaeFGI---SAGAPSVDWAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 181 -------------KLIEEVVATSNITVYSGFtafGWFQGsvcaadqDHAV------LFHPRKVIVATGAAEKMLmfknnD 241
Cdd:COG1249 82 lmarkdkvvdrlrGGVEELLKKNGVDVIRGR---ARFVD-------PHTVevtggeTLTADHIVIATGSRPRVP-----P 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 242 MPGVFGAGA-----AQTLMNVygikPGnKVLMVGAGNVGLIVSYQLMQAGIEVVgVIEGAPR--------VGGYLVHASK 308
Cdd:COG1249 147 IPGLDEVRVltsdeALELEEL----PK-SLVVIGGGYIGLEFAQIFARLGSEVT-LVERGDRllpgedpeISEALEKALE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 309 iaRNGVRIMTRHTVLEAVGTDHvEAAIIAEVDekwqpipGTEQRVECDTICLSAGLKPSTELLEQAKLDLAYTGelGGWV 388
Cdd:COG1249 221 --KEGIDILTGAKVTSVEKTGD-GVTVTLEDG-------GGEEAVEADKVLVATGRRPNTDGLGLEAAGVELDE--RGGI 288
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2015191093 389 aKRNWAMRTSNPDIFAAGDASGIEE-ASTAMMEGKIAGLQAA 429
Cdd:COG1249 289 -KVDEYLRTSVPGIYAIGDVTGGPQlAHVASAEGRVAAENIL 329
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
120-432 |
7.95e-14 |
|
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: 71.89 E-value: 7.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 120 ILVIGGGPAGLEASLWAAKAGADVILLDqNPKLGGQLVKQT--------------HKFFGSAKENAGTRGVTIAKKLIEE 185
Cdd:TIGR01292 2 VIIIGAGPAGLTAAIYAARANLKPLLIE-GMEPGGQLTTTTevenypgfpegisgPELMEKMKEQAVKFGAEIIYEEVIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 186 V-VATSNITVYSG----FTAfgwfqgsvcaadqdhavlfhpRKVIVATGAAEKMLMFKNNDMpgVFGAGAAQTLMNVYGI 260
Cdd:TIGR01292 81 VdKSDRPFKVYTGdgkeYTA---------------------KAVIIATGASARKLGIPGEDE--FWGRGVSYCATCDGPF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 261 KPGNKVLMVGAGNVGLIVSYQLMQAGIEVvgviegaprvggYLVH------ASKI------ARNGVRIMTRHTVLEAVGT 328
Cdd:TIGR01292 138 FKNKEVAVVGGGDSAIEEALYLTRIAKKV------------TLVHrrdkfrAEKIlldrlkKNPKIEFLWNSTVEEIVGD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 329 DHVEAAIIAEVDEkwqpipGTEQRVECDTICLSAGLKPSTELLE-QAKLDlaytgELGGWVAKRNwaMRTSNPDIFAAGD 407
Cdd:TIGR01292 206 NKVEGVKIKNTVT------GEEEELEVDGVFIAIGHEPNTELLKgLLELD-----ENGYIVTDEG--MRTSVPGVFAAGD 272
|
330 340
....*....|....*....|....*..
gi 2015191093 408 --ASGIEEASTAMMEGKIAGLQAAYDL 432
Cdd:TIGR01292 273 vrDKGYRQAVTAAGDGCIAALSAERYL 299
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
223-407 |
4.34e-13 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 71.78 E-value: 4.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 223 KVIVATGAAEKMLMFKNNDMPGVFGAGA---AQTLMNvyGIKPGNKVLMVGAGNVGLIVSYQLMQAGIEVvGVIEGAPRV 299
Cdd:TIGR02374 99 KLILATGSYPFILPIPGADKKGVYVFRTiedLDAIMA--MAQRFKKAAVIGGGLLGLEAAVGLQNLGMDV-SVIHHAPGL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 300 --------GGYLVhASKIARNGVRIMTRHTVLEAVGTDHVEAAIIAEvdekwqpipGTEqrVECDTICLSAGLKPSTELL 371
Cdd:TIGR02374 176 makqldqtAGRLL-QRELEQKGLTFLLEKDTVEIVGATKADRIRFKD---------GSS--LEADLIVMAAGIRPNDELA 243
|
170 180 190
....*....|....*....|....*....|....*.
gi 2015191093 372 EQAKLDLAytgelGGWVAkrNWAMRTSNPDIFAAGD 407
Cdd:TIGR02374 244 VSAGIKVN-----RGIIV--NDSMQTSDPDIYAVGE 272
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
117-232 |
1.60e-12 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 69.50 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 117 NAEILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGGQlVKQTHKFFGSAKENAgtrgvTIAKKLIEEVVATSNITVY- 195
Cdd:COG1148 140 NKRALVIGGGIAGMTAALELAEQGYEVYLVEKEPELGGR-AAQLHKTFPGLDCPQ-----CILEPLIAEVEANPNITVYt 213
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2015191093 196 -------SGFTafGWFQGSVCAADQDHAVLFHpRKVIVATGAAE 232
Cdd:COG1148 214 gaeveevSGYV--GNFTVTIKKGPREEIEIEV-GAIVLATGFKP 254
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
113-424 |
5.08e-11 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 65.15 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 113 VKEKNA-EILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGGQLVKQTHKFFGSAK------ENAGTRGVTIAKklieE 185
Cdd:PRK12778 426 VAEKNGkKVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGGVLKYGIPEFRLPKKivdveiENLKKLGVKFET----D 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 186 VVATSNITVysgftafgwfqgsvcaaDQDHAVLFhpRKVIVATGAAEKMLM-FKNNDMPGVFGAGAAQT---LMNVYG-- 259
Cdd:PRK12778 502 VIVGKTITI-----------------EELEEEGF--KGIFIASGAGLPNFMnIPGENSNGVMSSNEYLTrvnLMDAASpd 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 260 ----IKPGNKVLMVGAGNVGLIVSYQLMQAGIEVVGVI-----EGAPRVGGYLVHASKiarNGVRIMTRHTVLEAVGTDH 330
Cdd:PRK12778 563 sdtpIKFGKKVAVVGGGNTAMDSARTAKRLGAERVTIVyrrseEEMPARLEEVKHAKE---EGIEFLTLHNPIEYLADEK 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 331 --VEAAI-----IAEVDEKWQ----PIPGTEQRVECDTICLSAGLKPStELLEQAKLDLaytgELGGW---VAKRNwaMR 396
Cdd:PRK12778 640 gwVKQVVlqkmeLGEPDASGRrrpvAIPGSTFTVDVDLVIVSVGVSPN-PLVPSSIPGL----ELNRKgtiVVDEE--MQ 712
|
330 340
....*....|....*....|....*....
gi 2015191093 397 TSNPDIFAAGDA-SGIEEASTAMMEGKIA 424
Cdd:PRK12778 713 SSIPGIYAGGDIvRGGATVILAMGDGKRA 741
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
110-424 |
7.72e-10 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 60.80 E-value: 7.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 110 MKGVKEKNAEILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGGQLVKQTHKFfGSAKENAGTRGVTIAKKL---IE-E 185
Cdd:PRK12831 133 SETEEKKGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGGVLVYGIPEF-RLPKETVVKKEIENIKKLgvkIEtN 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 186 VVATSNITVYSGFTAFGWfqgsvcaadqdhavlfhpRKVIVATGAAEKMLM-FKNNDMPGVFGAGAAQT---LMNVYG-- 259
Cdd:PRK12831 212 VVVGKTVTIDELLEEEGF------------------DAVFIGSGAGLPKFMgIPGENLNGVFSANEFLTrvnLMKAYKpe 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 260 ----IKPGNKVLMVGAGNVGLIVSYQLMQAGIEVV-----GVIEGAPRVGGylVHASKiaRNGVRIMTRHTVLEAVGTDH 330
Cdd:PRK12831 274 ydtpIKVGKKVAVVGGGNVAMDAARTALRLGAEVHivyrrSEEELPARVEE--VHHAK--EEGVIFDLLTNPVEILGDEN 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 331 --VEAA--IIAEVDE-------KWQPIPGTEQRVECDTICLSAGLKPSTELLEQAK-LDLAYTGELggwVAKRNWAMrTS 398
Cdd:PRK12831 350 gwVKGMkcIKMELGEpdasgrrRPVEIEGSEFVLEVDTVIMSLGTSPNPLISSTTKgLKINKRGCI---VADEETGL-TS 425
|
330 340
....*....|....*....|....*....
gi 2015191093 399 NPDIFAAGDAsgIEEAST---AMMEGKIA 424
Cdd:PRK12831 426 KEGVFAGGDA--VTGAATvilAMGAGKKA 452
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
120-439 |
5.49e-09 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 58.27 E-value: 5.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 120 ILVIGGGPAGLEASLWAAKAGADVILLDQNPkLGG-----------QLVKQTHKFfgSAKENAGTRGVTIAKKLI----- 183
Cdd:PRK06292 6 VIVIGAGPAGYVAARRAAKLGKKVALIEKGP-LGGtclnvgcipskALIAAAEAF--HEAKHAEEFGIHADGPKIdfkkv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 184 ----------------EEVVATSNITVYSGFtafGWF--QGSVCAADQdhavLFHPRKVIVATGAAEKMLmfknndmPGV 245
Cdd:PRK06292 83 marvrrerdrfvggvvEGLEKKPKIDKIKGT---ARFvdPNTVEVNGE----RIEAKNIVIATGSRVPPI-------PGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 246 FGAGAAQTLMNVYGIKPGN---KVLMVGAGNVGLivsyQLMQA----GIEVVgVIEGAPRVGGYLVH-----ASKIARNG 313
Cdd:PRK06292 149 WLILGDRLLTSDDAFELDKlpkSLAVIGGGVIGL----ELGQAlsrlGVKVT-VFERGDRILPLEDPevskqAQKILSKE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 314 VRIMTRHTVlEAVGTDHVEAAIIAEVDekwqpipGTEQRVECDTICLSAGLKPSTELLEQAKLDLAYTGElgGWVaKRNW 393
Cdd:PRK06292 224 FKIKLGAKV-TSVEKSGDEKVEELEKG-------GKTETIEADYVLVATGRRPNTDGLGLENTGIELDER--GRP-VVDE 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2015191093 394 AMRTSNPDIFAAGDASGIEE-ASTAMMEGKIAGLQAA-YDLGHMDVPV 439
Cdd:PRK06292 293 HTQTSVPGIYAAGDVNGKPPlLHEAADEGRIAAENAAgDVAGGVRYHP 340
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
223-411 |
9.21e-09 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 57.36 E-value: 9.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 223 KVIVATGAAEKMLMFKNNDMPGVFG------AGAAQTLMNVYGIKpgnKVLMVGAGNVGLIVSYQLMQAGIEVVgVIEGA 296
Cdd:PRK09564 106 KLMIATGARPIIPPIKNINLENVYTlksmedGLALKELLKDEEIK---NIVIIGAGFIGLEAVEAAKHLGKNVR-IIQLE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 297 PRVGGYL-------VHASKIARNGVRIMTRHTVLEAVGTDHVEAAIIaevdekwqpipgTEQRVECDTICLSAGLKPSTE 369
Cdd:PRK09564 182 DRILPDSfdkeitdVMEEELRENGVELHLNEFVKSLIGEDKVEGVVT------------DKGEYEADVVIVATGVKPNTE 249
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2015191093 370 LLEQAKLDLAYTGELggwvaKRNWAMRTSNPDIFAAGDASGI 411
Cdd:PRK09564 250 FLEDTGLKTLKNGAI-----IVDEYGETSIENIYAAGDCATI 286
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
101-424 |
2.17e-08 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 56.34 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 101 GKFPDVQAAMKGVKeknaeILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGGQLVkqthkfFGSA-----KEnagtrg 175
Cdd:PRK11749 129 GWVLFKRAPKTGKK-----VAVIGAGPAGLTAAHRLARKGYDVTIFEARDKAGGLLR------YGIPefrlpKD------ 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 176 vtIAKKLIEEVVAtSNITVYSGfTAFGwfqGSVCAAD--QDH-AVLfhprkviVATGAAE-KMLMFKNNDMPGVFGAG-- 249
Cdd:PRK11749 192 --IVDREVERLLK-LGVEIRTN-TEVG---RDITLDElrAGYdAVF-------IGTGAGLpRFLGIPGENLGGVYSAVdf 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 250 -AAQTLMNV-YGIKPGNKVLMVGAGNVGlivsyqlMQAGieVVGVIEGAPRVggYLVH--------ASK----IAR-NGV 314
Cdd:PRK11749 258 lTRVNQAVAdYDLPVGKRVVVIGGGNTA-------MDAA--RTAKRLGAESV--TIVYrrgreempASEeeveHAKeEGV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 315 RIMTRHTVLEAVGTDHVEAAIIAEVDE---------KWQPIPGTEQRVECDTICLSAGLKPSTELLEQAKlDLAYTGElG 385
Cdd:PRK11749 327 EFEWLAAPVEILGDEGRVTGVEFVRMElgepdasgrRRVPIEGSEFTLPADLVIKAIGQTPNPLILSTTP-GLELNRW-G 404
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2015191093 386 GWVAKRNwAMRTSNPDIFAAGDAsgIEEAST---AMMEGKIA 424
Cdd:PRK11749 405 TIIADDE-TGRTSLPGVFAGGDI--VTGAATvvwAVGDGKDA 443
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
121-153 |
3.59e-08 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 55.44 E-value: 3.59e-08
10 20 30
....*....|....*....|....*....|...
gi 2015191093 121 LVIGGGPAGLEASLWAAKAGADVILLDQNPKLG 153
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEKNPKVG 33
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
331-408 |
4.91e-08 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 55.17 E-value: 4.91e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2015191093 331 VEAAIIAEVDEKWQPIPGTEQRVECDTICLSAGLKPSTE-LLEQAKLDLAYTGElggwVAKRNWAMRTSNPDIFAAGDA 408
Cdd:PRK12810 365 VKVVRTELGEGDFEPVEGSEFVLPADLVLLAMGFTGPEAgLLAQFGVELDERGR----VAAPDNAYQTSNPKVFAAGDM 439
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
120-443 |
6.06e-08 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 55.12 E-value: 6.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 120 ILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGGQLVKQTHKFFGSAkenagtrgvTIAKKLIEEVVATSNITVYSgfT 199
Cdd:PRK12814 196 VAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRYGIPRFRLPE---------SVIDADIAPLRAMGAEFRFN--T 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 200 AFGWfQGSVCAADQDHAVLFhprkviVATGAAEKMLM-FKNNDMPGV-----FGAGAAQTLMnvygIKPGNKVLMVGAGN 273
Cdd:PRK12814 265 VFGR-DITLEELQKEFDAVL------LAVGAQKASKMgIPGEELPGVisgidFLRNVALGTA----LHPGKKVVVIGGGN 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 274 VGLIVSYQLMQAGIEVVGVI-----EGAPrvggylVHASKIAR---NGVRI--MTRHTVLEAVGTDHVEAAII---AEVD 340
Cdd:PRK12814 334 TAIDAARTALRLGAESVTILyrrtrEEMP------ANRAEIEEalaEGVSLreLAAPVSIERSEGGLELTAIKmqqGEPD 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 341 E----KWQPIPGTEQRVECDTICLSAGLKPSTELLEQAKLDLAYTGElggwVAKRNWAMRTSNPDIFAAGD-ASGIEEAS 415
Cdd:PRK12814 408 EsgrrRPVPVEGSEFTLQADTVISAIGQQVDPPIAEAAGIGTSRNGT----VKVDPETLQTSVAGVFAGGDcVTGADIAI 483
|
330 340
....*....|....*....|....*...
gi 2015191093 416 TAMMEGKIAGLqaAYDLGHMDVPVEEQK 443
Cdd:PRK12814 484 NAVEQGKRAAH--AIDLFLNGKPVTAPV 509
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
120-424 |
6.75e-08 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 54.88 E-value: 6.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 120 ILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGGQLVkqthkfFG---------------SAKENAGTR---GVTIAKK 181
Cdd:PRK12771 140 VAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMR------YGipayrlprevldaeiQRILDLGVEvrlGVRVGED 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 182 LIEEVVAtsnitvySGFTAfgwfqgsvcaadqdhavlfhprkVIVATGA-AEKMLMFKNNDMPGVFGAGAAQTLMNVyGI 260
Cdd:PRK12771 214 ITLEQLE-------GEFDA-----------------------VFVAIGAqLGKRLPIPGEDAAGVLDAVDFLRAVGE-GE 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 261 KP--GNKVLMVGAGNVGLIVSYQLMQAGIEVVGVIEGAPRVgGYLVHASKIA---RNGVRIMTRHTVLEAVGTDHVEAA- 334
Cdd:PRK12771 263 PPflGKRVVVIGGGNTAMDAARTARRLGAEEVTIVYRRTRE-DMPAHDEEIEealREGVEINWLRTPVEIEGDENGATGl 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 335 -----IIAEVDEK-W-QPIPGTEQRVECDTICLSAGLKPSTELLEQAkldlayTGEL--GGWV-AKRNWAMrTSNPDIFA 404
Cdd:PRK12771 342 rvitvEKMELDEDgRpSPVTGEEETLEADLVVLAIGQDIDSAGLESV------PGVEvgRGVVqVDPNFMM-TGRPGVFA 414
|
330 340
....*....|....*....|.
gi 2015191093 405 AGDA-SGIEEASTAMMEGKIA 424
Cdd:PRK12771 415 GGDMvPGPRTVTTAIGHGKKA 435
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
120-157 |
2.25e-07 |
|
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases and related proteins.
Pssm-ID: 432816 [Multi-domain] Cd Length: 420 Bit Score: 53.00 E-value: 2.25e-07
10 20 30
....*....|....*....|....*....|....*...
gi 2015191093 120 ILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGGQLV 157
Cdd:pfam12831 2 VVVVGGGPAGVAAAIAAARAGAKVLLVERRGFLGGMLT 39
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
121-153 |
2.37e-07 |
|
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: 52.60 E-value: 2.37e-07
10 20 30
....*....|....*....|....*....|...
gi 2015191093 121 LVIGGGPAGLEASLWAAKAGADVILLDQNPKLG 153
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLEKNKKIG 33
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
120-153 |
2.61e-07 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 52.58 E-value: 2.61e-07
10 20 30
....*....|....*....|....*....|....
gi 2015191093 120 ILVIGGGPAGLEASLWAAKAGADVILLDQNPKLG 153
Cdd:pfam03486 3 VIVIGGGAAGLMAAISAAKRGRRVLLIEKGKKLG 36
|
|
| PRK09754 |
PRK09754 |
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional |
219-407 |
2.82e-07 |
|
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
Pssm-ID: 170080 [Multi-domain] Cd Length: 396 Bit Score: 52.62 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 219 FHPRKVIVATGAAEKMLMFKNNDMPGVFG---AGAAQTLMNVygIKPGNKVLMVGAGNVGLIVSYQLMQAGIEVVgVIEG 295
Cdd:PRK09754 99 WHWDQLFIATGAAARPLPLLDALGERCFTlrhAGDAARLREV--LQPERSVVIVGAGTIGLELAASATQRRCKVT-VIEL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 296 APRVGG---------YLVHASKIArnGVRIMTRHTVLEAVGTDHVEAAIiaevdekwqpipGTEQRVECDTICLSAGLKP 366
Cdd:PRK09754 176 AATVMGrnapppvqrYLLQRHQQA--GVRILLNNAIEHVVDGEKVELTL------------QSGETLQADVVIYGIGISA 241
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2015191093 367 STELLEQAKLDLAytgelGGWVAKRnwAMRTSNPDIFAAGD 407
Cdd:PRK09754 242 NDQLAREANLDTA-----NGIVIDE--ACRTCDPAIFAGGD 275
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
120-163 |
3.74e-07 |
|
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: 52.14 E-value: 3.74e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2015191093 120 ILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGGQLvkQTHKF 163
Cdd:COG1232 4 VAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGGLI--RTVEV 45
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
120-424 |
4.39e-07 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 51.91 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 120 ILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGGQLVkqthkfFGSAKENAGTRGVTIAKKLIEE--VVATSNITVYsg 197
Cdd:PRK12770 21 VAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGGLML------FGIPEFRIPIERVREGVKELEEagVVFHTRTKVC-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 198 ftafgwfqgsvCAADQDH--AVLFHPRK------------VIVATGAAE-KMLMFKNNDMPGVFGAgaAQTL----MNVY 258
Cdd:PRK12770 93 -----------CGEPLHEeeGDEFVERIvsleelvkkydaVLIATGTWKsRKLGIPGEDLPGVYSA--LEYLfrirAAKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 259 GIKP--------GNKVLMVGAGNVGLIVSYQLMQAGIEVVGV-----IEGAPrVGGYLVhaSKIARNGVRIMTRHTVLEA 325
Cdd:PRK12770 160 GYLPwekvppveGKKVVVVGAGLTAVDAALEAVLLGAEKVYLayrrtINEAP-AGKYEI--ERLIARGVEFLELVTPVRI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 326 VGTDHVEAAIIA-----EVDEKWQ----PIPGTEQRVECDTICLSAGLKPsTELLEQAKLDLAYT--GELggwvaKRNWA 394
Cdd:PRK12770 237 IGEGRVEGVELAkmrlgEPDESGRprpvPIPGSEFVLEADTVVFAIGEIP-TPPFAKECLGIELNrkGEI-----VVDEK 310
|
330 340 350
....*....|....*....|....*....|.
gi 2015191093 395 MRTSNPDIFAAGDA-SGIEEASTAMMEGKIA 424
Cdd:PRK12770 311 HMTSREGVFAAGDVvTGPSKIGKAIKSGLRA 341
|
|
| PTZ00306 |
PTZ00306 |
NADH-dependent fumarate reductase; Provisional |
118-160 |
1.15e-06 |
|
NADH-dependent fumarate reductase; Provisional
Pssm-ID: 140327 [Multi-domain] Cd Length: 1167 Bit Score: 51.32 E-value: 1.15e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2015191093 118 AEILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGGQLVKQT 160
Cdd:PTZ00306 410 ARVIVVGGGLAGCSAAIEAASCGAQVILLEKEAKLGGNSAKAT 452
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
120-154 |
3.66e-06 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 49.08 E-value: 3.66e-06
10 20 30
....*....|....*....|....*....|....*
gi 2015191093 120 ILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGG 154
Cdd:COG1233 6 VVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
|
|
| COG3573 |
COG3573 |
Predicted oxidoreductase [General function prediction only]; |
114-155 |
4.12e-06 |
|
Predicted oxidoreductase [General function prediction only];
Pssm-ID: 442794 [Multi-domain] Cd Length: 551 Bit Score: 49.02 E-value: 4.12e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2015191093 114 KEKNAEILVIGGGPAGLEASLWAAKAGADVILLDQNP--KLGGQ 155
Cdd:COG3573 2 AAMDADVIVVGAGLAGLVAAAELADAGRRVLLLDQEPeaNLGGQ 45
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
116-436 |
6.72e-06 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 48.38 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 116 KNAEILVIGGGPAGLEASLWAAKAGADVILLD--QNPKLGGQL--------------VKQTHKFFGSAKENAGTRGV--- 176
Cdd:PRK06327 3 KQFDVVVIGAGPGGYVAAIRAAQLGLKVACIEawKNPKGKPALggtclnvgcipskaLLASSEEFENAGHHFADHGIhvd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 177 --------------TIAKKL---IEEVVATSNITVYSGFTAF------GWfqgSVCAADQDHAVLfHPRKVIVATGAAEK 233
Cdd:PRK06327 83 gvkidvakmiarkdKVVKKMtggIEGLFKKNKITVLKGRGSFvgktdaGY---EIKVTGEDETVI-TAKHVIIATGSEPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 234 MLmfknndmPGV-FGAgaAQTLMNVYGIKPG---NKVLMVGAGNVGLIVSYQLMQAGIEVVgVIEGAPRVGGylVHASKI 309
Cdd:PRK06327 159 HL-------PGVpFDN--KIILDNTGALNFTevpKKLAVIGAGVIGLELGSVWRRLGAEVT-ILEALPAFLA--AADEQV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 310 A--------RNGVRIMTRHTVLE-AVGTDHVEaaiIAEVDEKwqpipGTEQRVECDTICLSAGLKPSTE--LLEQAKLDL 378
Cdd:PRK06327 227 AkeaakaftKQGLDIHLGVKIGEiKTGGKGVS---VAYTDAD-----GEAQTLEVDKLIVSIGRVPNTDglGLEAVGLKL 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2015191093 379 AYTGelggwVAKRNWAMRTSNPDIFAAGD-ASGIEEASTAMMEGKIAGLQAAYDLGHMD 436
Cdd:PRK06327 299 DERG-----FIPVDDHCRTNVPNVYAIGDvVRGPMLAHKAEEEGVAVAERIAGQKGHID 352
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
120-157 |
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: 46.13 E-value: 2.88e-05
10 20 30
....*....|....*....|....*....|....*...
gi 2015191093 120 ILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGGQLV 157
Cdd:pfam00890 2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGGATA 39
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
265-412 |
3.44e-05 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 46.06 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 265 KVLMVGAGNVGLIVSYQLMQAGIEVVgVIEGA---------PRVGGYLVHAskIARNGVRIMTRHTVleaVGTDHVEAAI 335
Cdd:PRK04965 143 RVLVVGGGLIGTELAMDLCRAGKAVT-LVDNAasllaslmpPEVSSRLQHR--LTEMGVHLLLKSQL---QGLEKTDSGI 216
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2015191093 336 IAEVDEkwqpipgtEQRVECDTICLSAGLKPSTELLEQAKLDLaytgELGGWVakrNWAMRTSNPDIFAAGDASGIE 412
Cdd:PRK04965 217 RATLDS--------GRSIEVDAVIAAAGLRPNTALARRAGLAV----NRGIVV---DSYLQTSAPDIYALGDCAEIN 278
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
120-154 |
5.92e-05 |
|
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: 45.23 E-value: 5.92e-05
10 20 30
....*....|....*....|....*....|....*
gi 2015191093 120 ILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGG 154
Cdd:COG3349 6 VVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
|
|
| PRK06134 |
PRK06134 |
putative FAD-binding dehydrogenase; Reviewed |
108-154 |
6.18e-05 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 180419 [Multi-domain] Cd Length: 581 Bit Score: 45.48 E-value: 6.18e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2015191093 108 AAMKGVKEKNAEILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGG 154
Cdd:PRK06134 3 SAAAYPPDLECDVLVIGSGAAGLSAAVTAAWHGLKVIVVEKDPVFGG 49
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
122-410 |
6.38e-05 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 45.19 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 122 VIGGGPAGLEASLWAAKAGADVILLDQNPkLGGQLVKqthkfFG---------SAKE-----NAGTRGVTIA-------- 179
Cdd:PRK06370 10 VIGAGQAGPPLAARAAGLGMKVALIERGL-LGGTCVN-----TGcvptktliaSARAahlarRAAEYGVSVGgpvsvdfk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 180 --KKLIEEVVATS------------NITVYSG---FTAfgwfQGSVCAADQdhavLFHPRKVIVATGAAEKMLmfknnDM 242
Cdd:PRK06370 84 avMARKRRIRARSrhgseqwlrgleGVDVFRGharFES----PNTVRVGGE----TLRAKRIFINTGARAAIP-----PI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 243 PGVFGAGA--AQTLMNVYGIKPgnKVLMVGAGNVGLivsyQLMQA----GIEVVgVIEGAPRVggyLVH----ASKI--- 309
Cdd:PRK06370 151 PGLDEVGYltNETIFSLDELPE--HLVIIGGGYIGL----EFAQMfrrfGSEVT-VIERGPRL---LPRededVAAAvre 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 310 --ARNGVRIMTRHTVLEAVGTDHveaAIIAEVDekwqpIPGTEQRVECDTICLSAGLKPSTEL--LEQAKLDlayTGELG 385
Cdd:PRK06370 221 ilEREGIDVRLNAECIRVERDGD---GIAVGLD-----CNGGAPEITGSHILVAVGRVPNTDDlgLEAAGVE---TDARG 289
|
330 340
....*....|....*....|....*
gi 2015191093 386 GwvAKRNWAMRTSNPDIFAAGDASG 410
Cdd:PRK06370 290 Y--IKVDDQLRTTNPGIYAAGDCNG 312
|
|
| PRK12834 |
PRK12834 |
putative FAD-binding dehydrogenase; Reviewed |
117-155 |
7.47e-05 |
|
putative FAD-binding dehydrogenase; Reviewed
Pssm-ID: 183782 [Multi-domain] Cd Length: 549 Bit Score: 45.27 E-value: 7.47e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2015191093 117 NAEILVIGGGPAGLEASLWAAKAGADVILLDQNPK--LGGQ 155
Cdd:PRK12834 4 DADVIVVGAGLAGLVAAAELADAGKRVLLLDQENEanLGGQ 44
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
120-157 |
8.00e-05 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 44.85 E-value: 8.00e-05
10 20 30
....*....|....*....|....*....|....*...
gi 2015191093 120 ILVIGGGPAGLEASLWAAKAGADVILLDQNpKLGGQLV 157
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIERD-GLGGAAV 40
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
119-154 |
1.70e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 44.11 E-value: 1.70e-04
10 20 30
....*....|....*....|....*....|....*.
gi 2015191093 119 EILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGG 154
Cdd:PRK07208 6 SVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGG 41
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
345-433 |
2.69e-04 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 43.58 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 345 PIPGTEQRVECDTICLSAGLKP-STELLEQAKLDLAYTGELGGWVAKRnWAMRTSNPDIFAAGDA-SGIEEASTAMMEGK 422
Cdd:PRK12769 563 PIPGSEFVMPADAVIMAFGFNPhGMPWLESHGVTVDKWGRIIADVESQ-YRYQTSNPKIFAGGDAvRGADLVVTAMAEGR 641
|
90
....*....|.
gi 2015191093 423 IAGLQAAYDLG 433
Cdd:PRK12769 642 HAAQGIIDWLG 652
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
120-154 |
2.69e-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: 43.28 E-value: 2.69e-04
10 20 30
....*....|....*....|....*....|....*
gi 2015191093 120 ILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGG 154
Cdd:COG1053 6 VVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRGG 40
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
116-150 |
2.91e-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: 2.91e-04
10 20 30
....*....|....*....|....*....|....*
gi 2015191093 116 KNAEILVIGGGPAGLEASLWAAKAGADVILLDQNP 150
Cdd:COG0654 2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAP 36
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
266-301 |
3.59e-04 |
|
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: 42.93 E-value: 3.59e-04
10 20 30
....*....|....*....|....*....|....*.
gi 2015191093 266 VLMVGAGNVGLIVSYQLMQAGIEVVgVIEGAPRVGG 301
Cdd:COG2072 9 VVVIGAGQAGLAAAYHLRRAGIDFV-VLEKADDVGG 43
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
120-154 |
3.89e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 42.57 E-value: 3.89e-04
10 20 30
....*....|....*....|....*....|....*
gi 2015191093 120 ILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGG 154
Cdd:PRK07233 2 IAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGG 36
|
|
| Kch |
COG1226 |
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism]; |
260-337 |
6.69e-04 |
|
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];
Pssm-ID: 440839 [Multi-domain] Cd Length: 279 Bit Score: 41.64 E-value: 6.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 260 IKPGNKVLMVGAGNVGLIVSYQLMQAGIEVVgVIEGAPRvggylvHASKIARNGVRIM----TRHTVLEAVGTDHVEAAI 335
Cdd:COG1226 121 IDLEGHVIIAGFGRVGQIVARLLRAEGIPFV-VIDLDPE------RVEELRRFGIKVYygdaTRPDVLEAAGIERARALV 193
|
..
gi 2015191093 336 IA 337
Cdd:COG1226 194 VA 195
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
113-147 |
7.00e-04 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 41.81 E-value: 7.00e-04
10 20 30
....*....|....*....|....*....|....*
gi 2015191093 113 VKEKNAEILVIGGGPAGLEASLWAAKAGADVILLD 147
Cdd:PRK07494 3 MEKEHTDIAVIGGGPAGLAAAIALARAGASVALVA 37
|
|
| PRK13800 |
PRK13800 |
fumarate reductase/succinate dehydrogenase flavoprotein subunit; |
102-148 |
7.06e-04 |
|
fumarate reductase/succinate dehydrogenase flavoprotein subunit;
Pssm-ID: 237512 [Multi-domain] Cd Length: 897 Bit Score: 42.14 E-value: 7.06e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2015191093 102 KFPDVQAAMkgvkEKNAEILVIGGGPAGLEASLWAAKAGADVILLDQ 148
Cdd:PRK13800 2 QIPALTDAL----RLDCDVLVIGGGTAGTMAALTAAEHGANVLLLEK 44
|
|
| PRK12842 |
PRK12842 |
putative succinate dehydrogenase; Reviewed |
119-154 |
8.08e-04 |
|
putative succinate dehydrogenase; Reviewed
Pssm-ID: 237224 [Multi-domain] Cd Length: 574 Bit Score: 41.99 E-value: 8.08e-04
10 20 30
....*....|....*....|....*....|....*.
gi 2015191093 119 EILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGG 154
Cdd:PRK12842 11 DVLVIGSGAGGLSAAITARKLGLDVVVLEKEPVFGG 46
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
120-154 |
8.81e-04 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 41.68 E-value: 8.81e-04
10 20 30
....*....|....*....|....*....|....*
gi 2015191093 120 ILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGG 154
Cdd:PRK05249 8 LVVIGSGPAGEGAAMQAAKLGKRVAVIERYRNVGG 42
|
|
| PLN02328 |
PLN02328 |
lysine-specific histone demethylase 1 homolog |
259-317 |
8.90e-04 |
|
lysine-specific histone demethylase 1 homolog
Pssm-ID: 215187 [Multi-domain] Cd Length: 808 Bit Score: 41.90 E-value: 8.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2015191093 259 GIKPGNkVLMVGAGNVGLIVSYQLMQAGIEVVgVIEGAPRVGGYlVHASKIARNGVRIM 317
Cdd:PLN02328 235 GVEPAN-VVVVGAGLAGLVAARQLLSMGFKVV-VLEGRARPGGR-VKTMKMKGDGVVAA 290
|
|
| PanE |
COG1893 |
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ... |
265-316 |
1.00e-03 |
|
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 441497 [Multi-domain] Cd Length: 305 Bit Score: 41.00 E-value: 1.00e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2015191093 265 KVLMVGAGNVGLIVSYQLMQAGIEVVGVIEGAprvggylvHASKIARNGVRI 316
Cdd:COG1893 2 KIAILGAGAIGGLLGARLARAGHDVTLVARGA--------HAEALRENGLRL 45
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
122-155 |
1.07e-03 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 37.51 E-value: 1.07e-03
10 20 30
....*....|....*....|....*....|....
gi 2015191093 122 VIGGGPAGLEASLWAAKAGADVILLDQNPKLGGQ 155
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGN 34
|
|
| PRK08274 |
PRK08274 |
FAD-dependent tricarballylate dehydrogenase TcuA; |
119-151 |
1.17e-03 |
|
FAD-dependent tricarballylate dehydrogenase TcuA;
Pssm-ID: 236214 [Multi-domain] Cd Length: 466 Bit Score: 41.40 E-value: 1.17e-03
10 20 30
....*....|....*....|....*....|...
gi 2015191093 119 EILVIGGGPAGLEASLWAAKAGADVILLDQNPK 151
Cdd:PRK08274 6 DVLVIGGGNAALCAALAAREAGASVLLLEAAPR 38
|
|
| Ala_dh_like |
cd01620 |
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ... |
89-194 |
1.19e-03 |
|
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such as the hexameric L-alanine dehydrogenase of Phormidium lapideum, contain 2 Rossmann fold-like domains linked by an alpha helical region. Related proteins include Saccharopine Dehydrogenase (SDH), bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme, N(5)-(carboxyethyl)ornithine synthase, and Rubrum transdehydrogenase. Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyrucate to L-alanine via reductive amination. Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matirx side. DI contains 2 domains with Rossmann folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with one dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than classical Rossmann domains.
Pssm-ID: 240621 [Multi-domain] Cd Length: 317 Bit Score: 40.85 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 89 RDGMEVETQHGDGKFPDVQAAMKGVKEknAEILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGGQLvkqthkffgsaK 168
Cdd:cd01620 136 YAGVQLGAYELARIQGGRMGGAGGVPP--AKVLIIGAGVVGLGAAKIAKKLGANVLVYDIKEEKLKGV-----------E 202
|
90 100
....*....|....*....|....*.
gi 2015191093 169 ENAGTRGVTIAKKLIEEVVATSNITV 194
Cdd:cd01620 203 TLGGSRLRYSQKEELEKELKQTDILI 228
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
118-150 |
1.35e-03 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 40.66 E-value: 1.35e-03
10 20 30
....*....|....*....|....*....|...
gi 2015191093 118 AEILVIGGGPAGLEASLWAAKAGADVILLDQNP 150
Cdd:COG0665 3 ADVVVIGGGIAGLSTAYHLARRGLDVTVLERGR 35
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
265-301 |
1.37e-03 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 41.06 E-value: 1.37e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2015191093 265 KVLMVGAGNVGLIVSYQLMQAGIEVVgVIEGAPRVGG 301
Cdd:COG1231 9 DVVIVGAGLAGLAAARELRKAGLDVT-VLEARDRVGG 44
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
292-425 |
1.45e-03 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 40.89 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 292 VIEGAPRVGGYL-VHASKIARN-----GVRIMTRHTVlEAVGTDHVEAAiiaevdekwqpipgTEQRVECDTICLSAGLK 365
Cdd:COG1252 190 LVEAGPRILPGLgEKLSEAAEKelekrGVEVHTGTRV-TEVDADGVTLE--------------DGEEIPADTVIWAAGVK 254
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 366 PSTELleqAKLDLAyTGELGGWVAKRNwaMRT-SNPDIFAAGDASGIEE---------ASTAMMEGKIAG 425
Cdd:COG1252 255 APPLL---ADLGLP-TDRRGRVLVDPT--LQVpGHPNVFAIGDCAAVPDpdgkpvpktAQAAVQQAKVLA 318
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
265-301 |
1.57e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 40.64 E-value: 1.57e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2015191093 265 KVLMVGAGNVGLIVSYQLMQAGIEVVgVIEGAPRVGG 301
Cdd:PRK07233 1 KIAIVGGGIAGLAAAYRLAKRGHEVT-VFEADDQLGG 36
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
116-410 |
1.61e-03 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 40.89 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 116 KNAEILVIGGGPAG--LEASLwaAKAGADVILLDQNPKL-GGQLVK----QTHKFFGSAKENAGTRGVTIAKKLI----- 183
Cdd:PRK07251 2 LTYDLIVIGFGKAGktLAAKL--ASAGKKVALVEESKAMyGGTCINigciPTKTLLVAAEKNLSFEQVMATKNTVtsrlr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 184 ---EEVVATSNITVYSGFTAFGWFQGSVCAADQDHAVLfHPRKVIVATGAAEKMLMFKN-NDMPGVFGAGAAQTLMNvyg 259
Cdd:PRK07251 80 gknYAMLAGSGVDLYDAEAHFVSNKVIEVQAGDEKIEL-TAETIVINTGAVSNVLPIPGlADSKHVYDSTGIQSLET--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 260 iKPgNKVLMVGAGNVGLIVSYQLMQAGIEVVgVIEGAPRV-GGYLVHASKIARNgvrimtrhtVLEAVGTDHVEAAIIAE 338
Cdd:PRK07251 156 -LP-ERLGIIGGGNIGLEFAGLYNKLGSKVT-VLDAASTIlPREEPSVAALAKQ---------YMEEDGITFLLNAHTTE 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2015191093 339 V-DEKWQPIPGTE-QRVECDTICLSAGLKPSTELLEQAKLDLAYTgELGGwvAKRNWAMRTSNPDIFAAGDASG 410
Cdd:PRK07251 224 VkNDGDQVLVVTEdETYRFDALLYATGRKPNTEPLGLENTDIELT-ERGA--IKVDDYCQTSVPGVFAVGDVNG 294
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
265-303 |
1.68e-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: 40.59 E-value: 1.68e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2015191093 265 KVLMVGAGNVGLIVSYQLMQAGIEVVgVIEGAPRVGGYL 303
Cdd:COG1232 3 RVAVIGGGIAGLTAAYRLAKAGHEVT-VLEASDRVGGLI 40
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
101-192 |
1.68e-03 |
|
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.
Pssm-ID: 214966 [Multi-domain] Cd Length: 149 Bit Score: 39.03 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 101 GKFPDVQAAMKGVKekNAEILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGGQLvkqthkffgsaKENAGTRGVTIAK 180
Cdd:smart01002 6 GGFGMLLTGAGGVP--PAKVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPARLRQL-----------ESLLGARFTTLYS 72
|
90
....*....|....
gi 2015191093 181 --KLIEEVVATSNI 192
Cdd:smart01002 73 qaELLEEAVKEADL 86
|
|
| carotene-cycl |
TIGR01790 |
lycopene cyclase family protein; This family includes lycopene beta and epsilion cyclases ... |
119-166 |
1.83e-03 |
|
lycopene cyclase family protein; This family includes lycopene beta and epsilion cyclases (which form beta and delta carotene, respectively) from bacteria and plants as well as the plant capsanthin/capsorubin and neoxanthin cyclases which appear to have evolved from the plant lycopene cyclases. The plant lycopene epsilon cyclases also transform neurosporene to alpha zeacarotene.
Pssm-ID: 130850 [Multi-domain] Cd Length: 388 Bit Score: 40.49 E-value: 1.83e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2015191093 119 EILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGGQlvkQTHKFFGS 166
Cdd:TIGR01790 1 DLAVIGGGPAGLAIALELARPGLRVQLIEPHPPIPGN---HTYGVWDD 45
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
265-338 |
2.53e-03 |
|
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: 36.80 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 265 KVLMVGAGNVGLIVSYQLMQAGIEVVgVIEGAPRVGGYLVH------ASKIARNGVRIMTRHTVLEAVGTDHVEAAIIAE 338
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVT-VVERRDRLLPGFDPeiakilQEKLEKNGIEFLLNTTVEAIEGNGDGVVVVLTD 79
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
286-424 |
2.61e-03 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 40.13 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 286 GIEVVgVIEGAPR-VGGYLVHASKIARN-----GVRIMTRHTVLEAV-GTDHVEAAIiaEVDEKwqpipgtEQRVECDTi 358
Cdd:PRK06416 195 GAEVT-IVEALPRiLPGEDKEISKLAERalkkrGIKIKTGAKAKKVEqTDDGVTVTL--EDGGK-------EETLEADY- 263
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 359 CLSA-GLKPSTEL--LEQAKLDLAytgelGGWVaKRNWAMRTSNPDIFAAGD-ASGIEEASTAMMEGKIA 424
Cdd:PRK06416 264 VLVAvGRRPNTENlgLEELGVKTD-----RGFI-EVDEQLRTNVPNIYAIGDiVGGPMLAHKASAEGIIA 327
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
118-148 |
3.51e-03 |
|
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
Pssm-ID: 396193 [Multi-domain] Cd Length: 348 Bit Score: 39.62 E-value: 3.51e-03
10 20 30
....*....|....*....|....*....|.
gi 2015191093 118 AEILVIGGGPAGLEASLWAAKAGADVILLDQ 148
Cdd:pfam01494 2 TDVLIVGGGPAGLMLALLLARAGVRVVLVER 32
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
101-156 |
4.11e-03 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 39.62 E-value: 4.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2015191093 101 GKFPDVQAamkgVKEKNAEILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGGQL 156
Cdd:PRK12809 298 GWRPDVSK----VVPRSEKVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGML 349
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
120-148 |
4.27e-03 |
|
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: 39.22 E-value: 4.27e-03
10 20
....*....|....*....|....*....
gi 2015191093 120 ILVIGGGPAGLEASLWAAKAGADVILLDQ 148
Cdd:TIGR02032 3 VVVVGAGPAGASAAYRLADKGLRVLLLEK 31
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
119-154 |
4.50e-03 |
|
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.
Pssm-ID: 426168 [Multi-domain] Cd Length: 339 Bit Score: 39.30 E-value: 4.50e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2015191093 119 EILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGG 154
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGS 36
|
|
| TrkA |
COG0569 |
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
264-337 |
4.62e-03 |
|
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 38.89 E-value: 4.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2015191093 264 NKVLMVGAGNVGLIVSYQLMQAGIEVVgVIEGAPRVggylvhASKIARNGVRIM----TRHTVLEAVGTDHVEAAIIA 337
Cdd:COG0569 96 MHVIIIGAGRVGRSLARELEEEGHDVV-VIDKDPER------VERLAEEDVLVIvgdaTDEEVLEEAGIEDADAVIAA 166
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
306-409 |
5.16e-03 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 39.36 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2015191093 306 ASKIARNG--VRIMTRHTVL--------EAVGT----------DHVEAAIIAEVDEKWqpIPGTEQ-RVECDTICLSAGL 364
Cdd:PRK13748 286 AQAFARLGskVTILARSTLFfredpaigEAVTAafraegievlEHTQASQVAHVDGEF--VLTTGHgELRADKLLVATGR 363
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2015191093 365 KPSTelleqAKLDLAYTG----ELGGWVAKRnwAMRTSNPDIFAAGDAS 409
Cdd:PRK13748 364 APNT-----RSLALDAAGvtvnAQGAIVIDQ--GMRTSVPHIYAAGDCT 405
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
119-154 |
6.35e-03 |
|
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: 38.69 E-value: 6.35e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2015191093 119 EILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGG 154
Cdd:COG2072 8 DVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGG 43
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
119-154 |
6.49e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 38.95 E-value: 6.49e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2015191093 119 EILVIGGGPAGLEASLWAAKAGADVILLDQNPKLGG 154
Cdd:PRK12843 18 DVIVIGAGAAGMSAALFAAIAGLKVLLVERTEYVGG 53
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
265-316 |
6.71e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 38.72 E-value: 6.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2015191093 265 KVLMVGAGNVGLIVSYQLMQAGIEVVgVIEGAPRVGGylvhaskIAR----NGVRI 316
Cdd:PRK07208 6 SVVIIGAGPAGLTAAYELLKRGYPVT-VLEADPVVGG-------ISRtvtyKGNRF 53
|
|
| AlaDh_PNT_C |
pfam01262 |
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ... |
101-150 |
7.55e-03 |
|
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.
Pssm-ID: 426165 [Multi-domain] Cd Length: 213 Bit Score: 37.86 E-value: 7.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2015191093 101 GKFPDVQAAmkgvkeknaEILVIGGGPAGLEASLWAAKAGADVILLDQNP 150
Cdd:pfam01262 21 GGVPGVAPA---------KVLVIGGGVAGLNAAATAKGLGAIVTILDVRP 61
|
|
| PRK06522 |
PRK06522 |
2-dehydropantoate 2-reductase; Reviewed |
265-340 |
8.03e-03 |
|
2-dehydropantoate 2-reductase; Reviewed
Pssm-ID: 235821 [Multi-domain] Cd Length: 304 Bit Score: 38.29 E-value: 8.03e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2015191093 265 KVLMVGAGNVGLIVSYQLMQAGIEVVGVIegapRVGGylvHASKIARNGVRIMTRHTVLEAVGTDhvEAAIIAEVD 340
Cdd:PRK06522 2 KIAILGAGAIGGLFGAALAQAGHDVTLVA----RRGA---HLDALNENGLRLEDGEITVPVLAAD--DPAELGPQD 68
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
265-326 |
8.93e-03 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 38.00 E-value: 8.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2015191093 265 KVLMVGAGNVGLIVSYQLMQAGIEVVgVIEGAPRVGGYLVhASKIARNGVRIMTRHTVLEAV 326
Cdd:COG0654 5 DVLIVGGGPAGLALALALARAGIRVT-VVERAPPPRPDGR-GIALSPRSLELLRRLGLWDRL 64
|
|
| PRK11883 |
PRK11883 |
protoporphyrinogen oxidase; Reviewed |
120-165 |
9.79e-03 |
|
protoporphyrinogen oxidase; Reviewed
Pssm-ID: 237009 [Multi-domain] Cd Length: 451 Bit Score: 38.29 E-value: 9.79e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2015191093 120 ILVIGGGPAGLEASLWAAKAG--ADVILLDQNPKLGGQLvkQTHKFFG 165
Cdd:PRK11883 3 VAIIGGGITGLSAAYRLHKKGpdADITLLEASDRLGGKI--QTVRKDG 48
|
|
| |
