|
Name |
Accession |
Description |
Interval |
E-value |
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
6-307 |
7.87e-156 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 437.63 E-value: 7.87e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 6 FDIAIIGAGPAGMTAAVYASRANLKTVMIERGIPGGQMANTEEVENFPGF-EMITGPDLSTKMFEHAKKFGAVYQYGDIK 84
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATTKEIENYPGFpEGISGPELAERLREQAERFGAEILLEEVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 85 SVEDKGEYKVINFGN-KELTAKAVIIATGAEYKKIGVPGEQELGGRGVSYCAVCDGAFFKNKRLFVIGGGDSAVEEGTFL 163
Cdd:COG0492 81 SVDKDDGPFRVTTDDgTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 164 TKFADKVTIVHRRDELRAQRILQDRAFKNDKIDFIWSHTLKSInEKDGKVGSVTLTSTKDGSEETHEADGVFIYIGMKPL 243
Cdd:COG0492 161 TKFASKVTLIHRRDELRASKILVERLRANPKIEVLWNTEVTEI-EGDGRVEGVTLKNVKTGEEKELEVDGVFVAIGLKPN 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 584796428 244 TAPFKDLGI-TNDVGYIVTKDDMTTSVPGIFAAGDVRDKGLRQIVTATGDGSIAAQSAAEYIEHL 307
Cdd:COG0492 240 TELLKGLGLeLDEDGYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAARYLEPL 304
|
|
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
7-304 |
5.70e-155 |
|
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: 435.13 E-value: 5.70e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 7 DIAIIGAGPAGMTAAVYASRANLKTVMIERGIPGGQMANTEEVENFPGF-EMITGPDLSTKMFEHAKKFGAVYQYGDIKS 85
Cdd:TIGR01292 1 DVIIIGAGPAGLTAAIYAARANLKPLLIEGMEPGGQLTTTTEVENYPGFpEGISGPELMEKMKEQAVKFGAEIIYEEVIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 86 VEDKGEYKVINFGNK-ELTAKAVIIATGAEYKKIGVPGEQELGGRGVSYCAVCDGAFFKNKRLFVIGGGDSAVEEGTFLT 164
Cdd:TIGR01292 81 VDKSDRPFKVYTGDGkEYTAKAVIIATGASARKLGIPGEDEFWGRGVSYCATCDGPFFKNKEVAVVGGGDSAIEEALYLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 165 KFADKVTIVHRRDELRAQRILQDRAFKNDKIDFIWSHTLKSINEkDGKVGSVTLTSTKDGSEETHEADGVFIYIGMKPLT 244
Cdd:TIGR01292 161 RIAKKVTLVHRRDKFRAEKILLDRLKKNPKIEFLWNSTVEEIVG-DNKVEGVKIKNTVTGEEEELEVDGVFIAIGHEPNT 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 245 APFKDLGITNDVGYIVTKDDMTTSVPGIFAAGDVRDKGLRQIVTATGDGSIAAQSAAEYI 304
Cdd:TIGR01292 240 ELLKGLLELDENGYIVTDEGMRTSVPGVFAAGDVRDKGYRQAVTAAGDGCIAALSAERYL 299
|
|
| AhpF_homolog |
TIGR03143 |
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase ... |
1-311 |
6.22e-91 |
|
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: 280.90 E-value: 6.22e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 1 MTEIdFDIAIIGAGPAGMTAAVYASRANLKTVMIERGIPGGQMANTEEVENFPGFEMITGPDLSTKMFEHAKKFGAVYQY 80
Cdd:TIGR03143 1 MEEI-YDLIIIGGGPAGLSAGIYAGRAKLDTLIIEKDDFGGQITITSEVVNYPGILNTTGPELMQEMRQQAQDFGVKFLQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 81 GDIKSVEDKGEYKVINFGNKELTAKAVIIATGAEYKKIGVPGEQELGGRGVSYCAVCDGAFFKNKRLFVIGGGDSAVEEG 160
Cdd:TIGR03143 80 AEVLDVDFDGDIKTIKTARGDYKTLAVLIATGASPRKLGFPGEEEFTGRGVAYCATCDGEFFTGMDVFVIGGGFAAAEEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 161 TFLTKFADKVTIVHRRDELRAQRILQDRAFKNDKIDFIWSHTLKSINeKDGKVGSVTLTSTKDGSEETHEAD------GV 234
Cdd:TIGR03143 160 VFLTRYASKVTVIVREPDFTCAKLIAEKVKNHPKIEVKFNTELKEAT-GDDGLRYAKFVNNVTGEITEYKAPkdagtfGV 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 584796428 235 FIYIGMKPLTAPFKDLGITNDVGYIVTKDDMTTSVPGIFAAGDVRDKGLRQIVTATGDGSIAAQSAAEYIEHLNDQA 311
Cdd:TIGR03143 239 FVFVGYAPSSELFKGVVELDKRGYIPTNEDMETNVPGVYAAGDLRPKELRQVVTAVADGAIAATSAERYVKELKEKL 315
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
6-304 |
3.02e-75 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 239.29 E-value: 3.02e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 6 FDIAIIGAGPAGMTAAVYASRANLKTVMI-ERGipGGQMANTEEVENFPGFEMITGPDLSTKMFEHAKkfgavyQYG-DI 83
Cdd:PRK15317 212 YDVLVVGGGPAGAAAAIYAARKGIRTGIVaERF--GGQVLDTMGIENFISVPETEGPKLAAALEEHVK------EYDvDI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 84 ------KSVEDKGEYKVINFGNKE-LTAKAVIIATGAEYKKIGVPGEQELGGRGVSYCAVCDGAFFKNKRLFVIGGGDSA 156
Cdd:PRK15317 284 mnlqraSKLEPAAGLIEVELANGAvLKAKTVILATGARWRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSG 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 157 VEEGTFLTKFADKVTIVHRRDELRAQRILQDRAFKNDKIDFIWSHTLKSINEKDGKVGSVTLTSTKDGSEETHEADGVFI 236
Cdd:PRK15317 364 VEAAIDLAGIVKHVTVLEFAPELKADQVLQDKLRSLPNVTIITNAQTTEVTGDGDKVTGLTYKDRTTGEEHHLELEGVFV 443
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 584796428 237 YIGMKPLTAPFKDLGITNDVGYIVTKDDMTTSVPGIFAAGDVRDKGLRQIVTATGDGSIAAQSAAEYI 304
Cdd:PRK15317 444 QIGLVPNTEWLKGTVELNRRGEIIVDARGATSVPGVFAAGDCTTVPYKQIIIAMGEGAKAALSAFDYL 511
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
10-310 |
1.09e-65 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 209.15 E-value: 1.09e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 10 IIGAGPAGMTAAVYASRANLKTVMIERGIPGGQMANTEEVENFPGFEM-ITGPDLSTKMFEHAKKFGAVYQYGDIKSVED 88
Cdd:PRK10262 11 ILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNdLTGPLLMERMHEHATKFETEIIFDHINKVDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 89 KGEYKVINFGNKELTAKAVIIATGAEYKKIGVPGEQELGGRGVSYCAVCDGAFFKNKRLFVIGGGDSAVEEGTFLTKFAD 168
Cdd:PRK10262 91 QNRPFRLTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIAS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 169 KVTIVHRRDELRAQRILQDRAFKNDKIDFIWSHTLKSINEKDGKVGSVTLTSTKDGSE----ETHEADGVFIYIGMKPLT 244
Cdd:PRK10262 171 EVHLIHRRDGFRAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNsdniESLDVAGLFVAIGHSPNT 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 584796428 245 APFK-DLGITNdvGYIVTKDDM-----TTSVPGIFAAGDVRDKGLRQIVTATGDGSIAAQSAAEYIEHLNDQ 310
Cdd:PRK10262 251 AIFEgQLELEN--GYIKVQSGIhgnatQTSIPGVFAAGDVMDHIYRQAITSAGTGCMAALDAERYLDGLADA 320
|
|
| Pyr_redox_2 |
pfam07992 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
6-293 |
6.95e-61 |
|
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: 196.00 E-value: 6.95e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 6 FDIAIIGAGPAGMTAAVYASRANLKTVMIERG--IPGGQMANTEEVENFPGFEMI--TGPDLSTKMFEHAKKFGAVYQYG 81
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEgtCPYGGCVLSKALLGAAEAPEIasLWADLYKRKEEVVKKLNNGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 82 DIKSVE--DKGEYKVINFGNK-----ELTAKAVIIATGAEYKKIGVPGEQELGGRGVSYCAVCDGAFFKN--KRLFVIGG 152
Cdd:pfam07992 81 LGTEVVsiDPGAKKVVLEELVdgdgeTITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLlpKRVVVVGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 153 GDSAVEEGTFLTKFADKVTIVHRRDEL------RAQRILQDRaFKNDKIDFIWSHTLKSINEKDGKVgsvtLTSTKDGSE 226
Cdd:pfam07992 161 GYIGVELAAALAKLGKEVTLIEALDRLlrafdeEISAALEKA-LEKNGVEVRLGTSVKEIIGDGDGV----EVILKDGTE 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 584796428 227 EthEADGVFIYIGMKPLTAPFKDLGI-TNDVGYIVTKDDMTTSVPGIFAAGDVRDKGLRQIVTATGDG 293
Cdd:pfam07992 236 I--DADLVVVAIGRRPNTELLEAAGLeLDERGGIVVDEYLRTSVPGIYAAGDCRVGGPELAQNAVAQG 301
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
4-278 |
1.23e-36 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 136.46 E-value: 1.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 4 IDFDIAIIGAGPAGMTAAVYASRANLKTVMIERGIPGGQMANT---------------EEVENFPGFE-MITGPDLSTK- 66
Cdd:PRK06292 2 EKYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGTCLNVgcipskaliaaaeafHEAKHAEEFGiHADGPKIDFKk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 67 MFEHAKKFgavyQYGDIKSVED-----------KGEYKV-----INFGNKELTAKAVIIATGAeyKKIGVPG-EQELGGR 129
Cdd:PRK06292 82 VMARVRRE----RDRFVGGVVEglekkpkidkiKGTARFvdpntVEVNGERIEAKNIVIATGS--RVPPIPGvWLILGDR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 130 GVSYcavcDGAFFKN---KRLFVIGGGDSAVEEGTFLTKFADKVTIVHRRDEL----------RAQRILQDRafkndkID 196
Cdd:PRK06292 156 LLTS----DDAFELDklpKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRIlpledpevskQAQKILSKE------FK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 197 FIWSHTLKSINEKDGKVGSVTltsTKDGSEETHEADGVFIYIGMKPLTAP--FKDLGI-TNDVGYIVTKDDMTTSVPGIF 273
Cdd:PRK06292 226 IKLGAKVTSVEKSGDEKVEEL---EKGGKTETIEADYVLVATGRRPNTDGlgLENTGIeLDERGRPVVDEHTQTSVPGIY 302
|
....*
gi 584796428 274 AAGDV 278
Cdd:PRK06292 303 AAGDV 307
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
3-281 |
2.88e-34 |
|
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: 129.82 E-value: 2.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 3 EIDFDIAIIGAGPAGMTAAVYASRANLKTVMIERGIPGGQMANT---------------EEVENFPGF------EMITGP 61
Cdd:COG1249 1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGTCLNVgcipskallhaaevaHEARHAAEFgisagaPSVDWA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 62 DLSTKMFEHAKKFGAVYQYG----DIKSVED----KGEYKVINFGNKELTAKAVIIATGAEYKKIGVPGEQElgGRGVSY 133
Cdd:COG1249 81 ALMARKDKVVDRLRGGVEELlkknGVDVIRGrarfVDPHTVEVTGGETLTADHIVIATGSRPRVPPIPGLDE--VRVLTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 134 cavcDGAFFKN---KRLFVIGGGDSAVEEGTFLTKFADKVTIVHRRDEL------RAQRILQdRAFKNDKIDFIWSHTLK 204
Cdd:COG1249 159 ----DEALELEelpKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLlpgedpEISEALE-KALEKEGIDILTGAKVT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 205 SInEKDGkvGSVTLTSTKDGSEETHEADGVFIYIGMKPLTApfkDLGI------TNDVGYIVTKDDMTTSVPGIFAAGDV 278
Cdd:COG1249 234 SV-EKTG--DGVTVTLEDGGGEEAVEADKVLVATGRRPNTD---GLGLeaagveLDERGGIKVDEYLRTSVPGIYAIGDV 307
|
...
gi 584796428 279 RDK 281
Cdd:COG1249 308 TGG 310
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
8-303 |
2.89e-28 |
|
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis
Pssm-ID: 440259 [Multi-domain] Cd Length: 434 Bit Score: 112.92 E-value: 2.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 8 IAIIGAGPAGMTAAVYASRANLKTVMIER----------GIPGGQMANT---EEVENF--PGFEMITGpdlstkmfehaK 72
Cdd:COG0493 124 VAVVGSGPAGLAAAYQLARAGHEVTVFEAldkpggllryGIPEFRLPKDvldREIELIeaLGVEFRTN-----------V 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 73 KFGavyqyGDIkSVED-KGEYKvinfgnkeltakAVIIATGAE-YKKIGVPGEqELGG--------RGVSYCAVCDGAFF 142
Cdd:COG0493 193 EVG-----KDI-TLDElLEEFD------------AVFLATGAGkPRDLGIPGE-DLKGvhsamdflTAVNLGEAPDTILA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 143 KNKRLFVIGGGD-------SAVEEGtfltkfADKVTIVHRRD--ELRAQRILQDRAfKNDKIDFIWSHTLKSIN-EKDGK 212
Cdd:COG0493 254 VGKRVVVIGGGNtamdcarTALRLG------AESVTIVYRRTreEMPASKEEVEEA-LEEGVEFLFLVAPVEIIgDENGR 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 213 VGSVTLTSTK---------------DGSEETHEADGVFIYIGMKP-LTAPFKDLGI-TNDVGYIVT-KDDMTTSVPGIFA 274
Cdd:COG0493 327 VTGLECVRMElgepdesgrrrpvpiEGSEFTLPADLVILAIGQTPdPSGLEEELGLeLDKRGTIVVdEETYQTSLPGVFA 406
|
330 340
....*....|....*....|....*....
gi 584796428 275 AGDVRdKGLRQIVTATGDGSIAAQSAAEY 303
Cdd:COG0493 407 GGDAV-RGPSLVVWAIAEGRKAARAIDRY 434
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
2-278 |
2.05e-26 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 107.92 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 2 TEIDFDIAIIGAGPAGMTAAVYASRANLKTVMIERGIPGGQMANT---------------EEVENFPGFEMITGP---DL 63
Cdd:PRK06416 1 FAFEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGTCLNRgcipskallhaaeraDEARHSEDFGIKAENvgiDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 64 sTKMFEHA---------------KKFGAVYQYGDIKsVEDKGEYKVIN-FGNKELTAKAVIIATGAeyKKIGVPGeQELG 127
Cdd:PRK06416 81 -KKVQEWKngvvnrltggvegllKKNKVDIIRGEAK-LVDPNTVRVMTeDGEQTYTAKNIILATGS--RPRELPG-IEID 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 128 GRGVSYCavcDGAF---FKNKRLFVIGGGDSAVEEGTFLTKFADKVTIVHRRDELRA------QRILQdRAFKNDKIDFI 198
Cdd:PRK06416 156 GRVIWTS---DEALnldEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPgedkeiSKLAE-RALKKRGIKIK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 199 WSHTLKSINEKDGkvgSVTLTSTKDGSEETHEADGVFIYIGMKPLTAP--FKDLGITNDVGYIVTKDDMTTSVPGIFAAG 276
Cdd:PRK06416 232 TGAKAKKVEQTDD---GVTVTLEDGGKEETLEADYVLVAVGRRPNTENlgLEELGVKTDRGFIEVDEQLRTNVPNIYAIG 308
|
..
gi 584796428 277 DV 278
Cdd:PRK06416 309 DI 310
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
8-305 |
2.07e-25 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 105.26 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 8 IAIIGAGPAGMTAAVYASRANLKTVMIER----------GIPGgqmanteevenfpgFEMitgP-DLSTKMFEHAKKFGA 76
Cdd:PRK11749 143 VAVIGAGPAGLTAAHRLARKGYDVTIFEArdkaggllryGIPE--------------FRL---PkDIVDREVERLLKLGV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 77 VYQY----GDIKSVED-KGEYKvinfgnkeltakAVIIATGA-EYKKIGVPGEqELGG--RGVSYC-----AVCDGAFFK 143
Cdd:PRK11749 206 EIRTntevGRDITLDElRAGYD------------AVFIGTGAgLPRFLGIPGE-NLGGvySAVDFLtrvnqAVADYDLPV 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 144 NKRLFVIGGGDSAVE-EGTFLTKFADKVTIVHRRD--ELRAQRILQDRAfKNDKIDFIWSHTLKSINEKDGKVGSVTLTS 220
Cdd:PRK11749 273 GKRVVVIGGGNTAMDaARTAKRLGAESVTIVYRRGreEMPASEEEVEHA-KEEGVEFEWLAAPVEILGDEGRVTGVEFVR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 221 TK--------------DGSEETHEADGVFIYIGMKP---LTAPFKDLGITNDVGYIVTKDDMTTSVPGIFAAGDVRdKGL 283
Cdd:PRK11749 352 MElgepdasgrrrvpiEGSEFTLPADLVIKAIGQTPnplILSTTPGLELNRWGTIIADDETGRTSLPGVFAGGDIV-TGA 430
|
330 340
....*....|....*....|..
gi 584796428 284 RQIVTATGDGSIAAQSAAEYIE 305
Cdd:PRK11749 431 ATVVWAVGDGKDAAEAIHEYLE 452
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
6-301 |
2.87e-25 |
|
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: 105.03 E-value: 2.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 6 FDIAIIGAGPAGMTAAVYASRANLKTVMIERGIPGGQ------------MANTEEVENFP-----GFEmITGPDLS-TKM 67
Cdd:TIGR01350 2 YDVIVIGGGPGGYVAAIRAAQLGLKVALVEKEYLGGTclnvgciptkalLHSAEVYDEIKhakdlGIE-VENVSVDwEKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 68 FEHAKKF--------------GAVYQYGDIKSVEDKGEYKVINFGNKE-LTAKAVIIATGAEYKKIgvPGEQELGGRGV- 131
Cdd:TIGR01350 81 QKRKNKVvkklvggvsgllkkNKVTVIKGEAKFLDPGTVSVTGENGEEtLEAKNIIIATGSRPRSL--PGPFDFDGKVVi 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 132 -SycavcDGAFF---KNKRLFVIGGGDSAVEEGTFLTKFADKVTIVHRRDELRAQ------RILQdRAFKNDKIDFIWSH 201
Cdd:TIGR01350 159 tS-----TGALNleeVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGedaevsKVLQ-KALKKKGVKILTNT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 202 TLKSINEKDGKVgsvtLTSTKDGSEETHEADGVFIYIGMKPLT--APFKDLGI-TNDVGYIVTKDDMTTSVPGIFAAGDV 278
Cdd:TIGR01350 233 KVTAVEKNDDQV----TYENKGGETETLTGEKVLVAVGRKPNTegLGLEKLGVeLDERGRIVVDEYMRTNVPGIYAIGDV 308
|
330 340
....*....|....*....|...
gi 584796428 279 RDKGLRQIVtATGDGSIAAQSAA 301
Cdd:TIGR01350 309 IGGPMLAHV-ASHEGIVAAENIA 330
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
8-305 |
3.17e-23 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 97.75 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 8 IAIIGAGPAGMTAAVY-ASRANLKTVMIERGIPGGQMAnteevenF--PGFEM-ITGPDLSTKMFEHAkkfGAVYQ---- 79
Cdd:PRK12770 21 VAIIGAGPAGLAAAGYlACLGYEVHVYDKLPEPGGLML-------FgiPEFRIpIERVREGVKELEEA---GVVFHtrtk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 80 -YGDIKSVEDKGEYKVINF-GNKELTAK--AVIIATGA-EYKKIGVPGEqELGG-----------RGVSYCAVCDGAFF- 142
Cdd:PRK12770 91 vCCGEPLHEEEGDEFVERIvSLEELVKKydAVLIATGTwKSRKLGIPGE-DLPGvysaleylfriRAAKLGYLPWEKVPp 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 143 -KNKRLFVIGGGDSAV---EEGTFLTkfADKVTIVHRR--DELRAQR----ILQDRAfkndkIDFIWSHTLKSINEkDGK 212
Cdd:PRK12770 170 vEGKKVVVVGAGLTAVdaaLEAVLLG--AEKVYLAYRRtiNEAPAGKyeieRLIARG-----VEFLELVTPVRIIG-EGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 213 VGSVTLTSTK---------------DGSEETHEADGVFIYIGMKPlTAPFK--DLGI-TNDVGYIVTKDDMTTSVPGIFA 274
Cdd:PRK12770 242 VEGVELAKMRlgepdesgrprpvpiPGSEFVLEADTVVFAIGEIP-TPPFAkeCLGIeLNRKGEIVVDEKHMTSREGVFA 320
|
330 340 350
....*....|....*....|....*....|.
gi 584796428 275 AGDVRdKGLRQIVTATGDGSIAAQSAAEYIE 305
Cdd:PRK12770 321 AGDVV-TGPSKIGKAIKSGLRAAQSIHEWLD 350
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
8-305 |
9.52e-19 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 85.99 E-value: 9.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 8 IAIIGAGPAGMTAAVYASRANLKTVMIER----------GIPG------------GQManTEEvenfpGFEMITGPDLSt 65
Cdd:PRK12810 146 VAVVGSGPAGLAAADQLARAGHKVTVFERadriggllryGIPDfklekevidrriELM--EAE-----GIEFRTNVEVG- 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 66 kmfehakkfgavyqyGDIKSVEDKGEYKvinfgnkeltakAVIIATGAE-YKKIGVPGEqELGGrgVsYCAV-------- 136
Cdd:PRK12810 218 ---------------KDITAEELLAEYD------------AVFLGTGAYkPRDLGIPGR-DLDG--V-HFAMdfliqntr 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 137 -----CDGAFF--KNKRLFVIGGGDSAVE-EGTFLTKFADKVTivhRRD------ELRAQRILQDRAFKNDKID------ 196
Cdd:PRK12810 267 rvlgdETEPFIsaKGKHVVVIGGGDTGMDcVGTAIRQGAKSVT---QRDimpmppSRRNKNNPWPYWPMKLEVSnaheeg 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 197 --FIWSHTLKSINEKDGKVGSVTLTSTK---------DGSEETHEADGVFIYIGMKPLTAP-FKDLGI-TNDVGYIVTKD 263
Cdd:PRK12810 344 veREFNVQTKEFEGENGKVTGVKVVRTElgegdfepvEGSEFVLPADLVLLAMGFTGPEAGlLAQFGVeLDERGRVAAPD 423
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 584796428 264 -DMTTSVPGIFAAGDVRdKGLRQIVTATGDGSIAAQSAAEYIE 305
Cdd:PRK12810 424 nAYQTSNPKVFAAGDMR-RGQSLVVWAIAEGRQAARAIDAYLM 465
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
5-278 |
1.08e-17 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 83.05 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 5 DFDIAIIGAGPAGMTAAVYASRANLKTVMIE-------RGIPGGQ------------MANTEEVEN----FPGFEmITGP 61
Cdd:PRK06327 4 QFDVVVIGAGPGGYVAAIRAAQLGLKVACIEawknpkgKPALGGTclnvgcipskalLASSEEFENaghhFADHG-IHVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 62 DLST---KMFehAKKFGAVYQYGD--------------------IKSVEDKGEYKVINFGNKELTAKAVIIATGAEYKKI 118
Cdd:PRK06327 83 GVKIdvaKMI--ARKDKVVKKMTGgieglfkknkitvlkgrgsfVGKTDAGYEIKVTGEDETVITAKHVIIATGSEPRHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 119 -GVPGEQELggrgvsycaVCD--GAF-FKN--KRLFVIGGGDSAVEEGTFLTKFADKVTIVHRRDELRA---QRILQD-- 187
Cdd:PRK06327 161 pGVPFDNKI---------ILDntGALnFTEvpKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAaadEQVAKEaa 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 188 RAFKNDKIDFiwsHTLKSINE-KDGKVGsVTLTST-KDGSEETHEADGVFIYIGMKPLTapfKDLG------ITNDVGYI 259
Cdd:PRK06327 232 KAFTKQGLDI---HLGVKIGEiKTGGKG-VSVAYTdADGEAQTLEVDKLIVSIGRVPNT---DGLGleavglKLDERGFI 304
|
330
....*....|....*....
gi 584796428 260 VTKDDMTTSVPGIFAAGDV 278
Cdd:PRK06327 305 PVDDHCRTNVPNVYAIGDV 323
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
95-278 |
1.92e-17 |
|
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: 81.01 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 95 INFGNKELTAK--------AVIIATGAEYKKIGVPGeqeLGGRGVSYCAVCDGAF--------FKNKRLFVIGGG----- 153
Cdd:COG0446 62 IDPEAKTVTLRdgetlsydKLVLATGARPRPPPIPG---LDLPGVFTLRTLDDADalrealkeFKGKRAVVIGGGpigle 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 154 --DSAVEEGTfltkfadKVTIVHRRDEL----------RAQRILQDRafkndKIDFIWSHTLKSInEKDGKVGsVTLTSt 221
Cdd:COG0446 139 laEALRKRGL-------KVTLVERAPRLlgvldpemaaLLEEELREH-----GVELRLGETVVAI-DGDDKVA-VTLTD- 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 584796428 222 kdgsEETHEADGVFIYIGMKPLTAPFKDLGI-TNDVGYIVTKDDMTTSVPGIFAAGDV 278
Cdd:COG0446 204 ----GEEIPADLVVVAPGVRPNTELAKDAGLaLGERGWIKVDETLQTSDPDVYAAGDC 257
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
6-278 |
4.97e-17 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 81.02 E-value: 4.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 6 FDIAIIGAGPAGMTAAVYASRANLKTVMIERGIPGGQMANTEEVenfPGFEMITgpdlSTKMFEHAKK------------ 73
Cdd:PRK06370 6 YDAIVIGAGQAGPPLAARAAGLGMKVALIERGLLGGTCVNTGCV---PTKTLIA----SARAAHLARRaaeygvsvggpv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 74 ---FGAVYQYGDIKSVEDKGEY----------------------KVINFGNKELTAKAVIIATGAEYKKIGVPGEQELGg 128
Cdd:PRK06370 79 svdFKAVMARKRRIRARSRHGSeqwlrglegvdvfrgharfespNTVRVGGETLRAKRIFINTGARAAIPPIPGLDEVG- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 129 rgvsycavcdgaFFKN----------KRLFVIGGGDSAVEEGTFLTKFADKVTIVHR------RDELRAQRILQDrAFKN 192
Cdd:PRK06370 158 ------------YLTNetifsldelpEHLVIIGGGYIGLEFAQMFRRFGSEVTVIERgprllpREDEDVAAAVRE-ILER 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 193 DKIDFIWSHTLKSInEKDGkvGSVTLTSTKDGSEETHEADGVFIYIGMKPLTapfKDLGI------TNDVGYIVTKDDMT 266
Cdd:PRK06370 225 EGIDVRLNAECIRV-ERDG--DGIAVGLDCNGGAPEITGSHILVAVGRVPNT---DDLGLeaagveTDARGYIKVDDQLR 298
|
330
....*....|..
gi 584796428 267 TSVPGIFAAGDV 278
Cdd:PRK06370 299 TTNPGIYAAGDC 310
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
98-281 |
5.57e-17 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 80.97 E-value: 5.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 98 GNKELTAKAVIIATGAEYKKIGVPGEQelggrgvsYCAVCDGAFFKN---KRLFVIGGGDSAVEEGTFLTKFADKVTIVH 174
Cdd:PRK06116 126 NGERYTADHILIATGGRPSIPDIPGAE--------YGITSDGFFALEelpKRVAVVGAGYIAVEFAGVLNGLGSETHLFV 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 175 RRDE-LRA-----QRILQDrAFKNDKIDFIWSHTLKSInEKDGKvGSVTLTsTKDGseETHEADGVFIYIGMKPLTapfK 248
Cdd:PRK06116 198 RGDApLRGfdpdiRETLVE-EMEKKGIRLHTNAVPKAV-EKNAD-GSLTLT-LEDG--ETLTVDCLIWAIGREPNT---D 268
|
170 180 190
....*....|....*....|....*....|....*....
gi 584796428 249 DLGI------TNDVGYIVTKDDMTTSVPGIFAAGDVRDK 281
Cdd:PRK06116 269 GLGLenagvkLNEKGYIIVDEYQNTNVPGIYAVGDVTGR 307
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
15-276 |
2.43e-16 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 77.65 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 15 PAGMTAAVYASRANLKTVMI-ERGIPG---------GQMANTEEVENfpGFEMI--------TGPDLSTKMfEHAKKFGA 76
Cdd:pfam13738 1 PAGIGCAIALKKAGLEDYLIlEKGNIGnsfyrypthMTFFSPSFTSN--GFGIPdlnaispgTSPAFTFNR-EHPSGNEY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 77 VYQYG--------------DIKSVE-DKGEYKVINfgNKE-LTAKAVIIATGaEYKKIGVPGEQELGgrgVSYCAVCDGA 140
Cdd:pfam13738 78 AEYLRrvadhfelpinlfeEVTSVKkEDDGFVVTT--SKGtYQARYVIIATG-EFDFPNKLGVPELP---KHYSYVKDFH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 141 FFKNKRLFVIGGGDSAVEEGTFLTKFADKVTIVHRRDELRA--------------QRIlqDRAFKNDKIDFIWSHTLKSI 206
Cdd:pfam13738 152 PYAGQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDrdsdpsyslspdtlNRL--EELVKNGKIKAHFNAEVKEI 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 584796428 207 NEKDGKVgsvtLTSTKDGseETHEADGVFIY-IGMKPLTAPFKDLGI-TNDVGYIV-TKDDMTTSVPGIFAAG 276
Cdd:pfam13738 230 TEVDVSY----KVHTEDG--RKVTSNDDPILaTGYHPDLSFLKKGLFeLDEDGRPVlTEETESTNVPGLFLAG 296
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
8-304 |
5.25e-16 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 78.63 E-value: 5.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 8 IAIIGAGPAGMTAAVYASRANLKTVMIER----------GIPGGQMANT---EEVENFpgfemitgpdlstkmfehaKKF 74
Cdd:PRK12778 434 VAVIGSGPAGLSFAGDLAKRGYDVTVFEAlheiggvlkyGIPEFRLPKKivdVEIENL-------------------KKL 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 75 GAVYQY----GDIKSVEDKGEYKVinfgnkeltaKAVIIATGAEYKK-IGVPGEQELGGRGVS-----------YCAVCD 138
Cdd:PRK12778 495 GVKFETdvivGKTITIEELEEEGF----------KGIFIASGAGLPNfMNIPGENSNGVMSSNeyltrvnlmdaASPDSD 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 139 GAFFKNKRLFVIGGGDSAVEEG-TFLTKFADKVTIVHRR--DELRAqRILQDRAFKNDKIDFIWSHT-LKSINEKDGKVG 214
Cdd:PRK12778 565 TPIKFGKKVAVVGGGNTAMDSArTAKRLGAERVTIVYRRseEEMPA-RLEEVKHAKEEGIEFLTLHNpIEYLADEKGWVK 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 215 SVTLTSTK---------------DGSEETHEADGVFIYIGMKP---LTAPFKDLGItNDVGYIVTKDDMTTSVPGIFAAG 276
Cdd:PRK12778 644 QVVLQKMElgepdasgrrrpvaiPGSTFTVDVDLVIVSVGVSPnplVPSSIPGLEL-NRKGTIVVDEEMQSSIPGIYAGG 722
|
330 340
....*....|....*....|....*...
gi 584796428 277 DVRdKGLRQIVTATGDGSIAAQSAAEYI 304
Cdd:PRK12778 723 DIV-RGGATVILAMGDGKRAAAAIDEYL 749
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
8-303 |
2.34e-15 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 76.45 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 8 IAIIGAGPAGMTAAVYASRANLKTVMIERG-IPGGQManteeveNF--PGFEM-----------ITGPDLSTKMfEHakK 73
Cdd:PRK12771 140 VAVIGGGPAGLSAAYHLRRMGHAVTIFEAGpKLGGMM-------RYgiPAYRLprevldaeiqrILDLGVEVRL-GV--R 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 74 FGavyqyGDIKSVEDKGEYKvinfgnkeltakAVIIATGAEY-KKIGVPGEQelGGRGVSycAVcdgAFFKN-------- 144
Cdd:PRK12771 210 VG-----EDITLEQLEGEFD------------AVFVAIGAQLgKRLPIPGED--AAGVLD--AV---DFLRAvgegeppf 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 145 --KRLFVIGGGD-------SAVEEGtfltkfADKVTIVHRR--DELRAQRILQDRAFkNDKIDFIWSHTLKSINEKDGKV 213
Cdd:PRK12771 266 lgKRVVVIGGGNtamdaarTARRLG------AEEVTIVYRRtrEDMPAHDEEIEEAL-REGVEINWLRTPVEIEGDENGA 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 214 GSVTLT-------------STKDGSEETHEADGVFIYIGMKPLTAPFKDL-GITNDVGYIVT-KDDMTTSVPGIFAAGDV 278
Cdd:PRK12771 339 TGLRVItvekmeldedgrpSPVTGEEETLEADLVVLAIGQDIDSAGLESVpGVEVGRGVVQVdPNFMMTGRPGVFAGGDM 418
|
330 340
....*....|....*....|....*
gi 584796428 279 RdKGLRQIVTATGDGSIAAQSAAEY 303
Cdd:PRK12771 419 V-PGPRTVTTAIGHGKKAARNIDAF 442
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
101-311 |
1.55e-14 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 73.25 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 101 ELTAKAVIIATGAEYKKIGVPGeQELGG----RGVSYCAVCDGAFFKNKRLFVIGGG-------DSAVEEGTfltkfadK 169
Cdd:COG1251 96 TLPYDKLVLATGSRPRVPPIPG-ADLPGvftlRTLDDADALRAALAPGKRVVVIGGGligleaaAALRKRGL-------E 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 170 VTIVHRRDEL-------RAQRILQdRAFKNDKIDFIWSHTLKSInEKDGKVGSVTLtstKDGseETHEADGVFIYIGMKP 242
Cdd:COG1251 168 VTVVERAPRLlprqldeEAGALLQ-RLLEALGVEVRLGTGVTEI-EGDDRVTGVRL---ADG--EELPADLVVVAIGVRP 240
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 584796428 243 LTAPFKDLGITNDVGyIVTKDDMTTSVPGIFAAGDVrdkglrqivtATGDGSIAAQSAAEYIEHLNDQA 311
Cdd:COG1251 241 NTELARAAGLAVDRG-IVVDDYLRTSDPDIYAAGDC----------AEHPGPVYGRRVLELVAPAYEQA 298
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
146-221 |
3.15e-14 |
|
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: 66.84 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 146 RLFVIGGGDSAVEEGTFLTKFADKVTIVHRRDELR------AQRILQDRAFKNdKIDFIWSHTLKSInEKDGKVGSVTLT 219
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLpgfdpeIAKILQEKLEKN-GIEFLLNTTVEAI-EGNGDGVVVVLT 78
|
..
gi 584796428 220 ST 221
Cdd:pfam00070 79 DG 80
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
8-277 |
1.48e-13 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 70.91 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 8 IAIIGAGPAGMTAAVYASRANLK-TVMIERGIPGGQMAnteevENFPGF---EMITGPDLstkmfEHAKKFGAVYQYG-- 81
Cdd:PRK12814 196 VAIIGAGPAGLTAAYYLLRKGHDvTIFDANEQAGGMMR-----YGIPRFrlpESVIDADI-----APLRAMGAEFRFNtv 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 82 ---DIKSVEDKGEYKvinfgnkeltakAVIIATGAEY-KKIGVPGEQELG-GRGVSYCA-VCDG-AFFKNKRLFVIGGGD 154
Cdd:PRK12814 266 fgrDITLEELQKEFD------------AVLLAVGAQKaSKMGIPGEELPGvISGIDFLRnVALGtALHPGKKVVVIGGGN 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 155 SAVEEG-TFLTKFADKVTIVHRR--DELRAQRILQDRAFKNDKIDFIWSHTLkSINEKDgkvGSVTLTSTK--------- 222
Cdd:PRK12814 334 TAIDAArTALRLGAESVTILYRRtrEEMPANRAEIEEALAEGVSLRELAAPV-SIERSE---GGLELTAIKmqqgepdes 409
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 584796428 223 --------DGSEETHEADGVFIYIGMK--PLTAPFKDLGITNDVGYIVTKDDMTTSVPGIFAAGD 277
Cdd:PRK12814 410 grrrpvpvEGSEFTLQADTVISAIGQQvdPPIAEAAGIGTSRNGTVKVDPETLQTSVAGVFAGGD 474
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
8-305 |
6.87e-13 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 68.51 E-value: 6.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 8 IAIIGAGPAGMTAAVYASRANLKTVMIER-GIPGGQManteeVENFPGFEMitgP--DLSTKMFEHAKKFGavyqygdIK 84
Cdd:PRK12831 143 VAVIGSGPAGLTCAGDLAKMGYDVTIFEAlHEPGGVL-----VYGIPEFRL---PkeTVVKKEIENIKKLG-------VK 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 85 SVEDKGEYKVINFGN--KELTAKAVIIATGAEYKKI-GVPGEQELG-----------GRGVSYCAVCDGAFFKNKRLFVI 150
Cdd:PRK12831 208 IETNVVVGKTVTIDEllEEEGFDAVFIGSGAGLPKFmGIPGENLNGvfsanefltrvNLMKAYKPEYDTPIKVGKKVAVV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 151 GGGDSAVEEGTFLTKFADKVTIVHRR--DELRAqRILQDRAFKNDKIDFIW-SHTLKSINEKDGKVGSVTLTSTK----- 222
Cdd:PRK12831 288 GGGNVAMDAARTALRLGAEVHIVYRRseEELPA-RVEEVHHAKEEGVIFDLlTNPVEILGDENGWVKGMKCIKMElgepd 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 223 ----------DGSEETHEADGVFIYIGMKP---LTAPFKDLGItNDVGYIVTKDDM-TTSVPGIFAAGD-VRdkGLRQIV 287
Cdd:PRK12831 367 asgrrrpveiEGSEFVLEVDTVIMSLGTSPnplISSTTKGLKI-NKRGCIVADEETgLTSKEGVFAGGDaVT--GAATVI 443
|
330
....*....|....*...
gi 584796428 288 TATGDGSIAAQSAAEYIE 305
Cdd:PRK12831 444 LAMGAGKKAAKAIDEYLS 461
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
6-278 |
1.48e-11 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 64.77 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 6 FDIAIIGAGPAGMTAAVYASRANLKTVMIERG--IPGGQMANteeVENFPGFEMITGPDlSTKMFEHA------------ 71
Cdd:PRK07251 4 YDLIVIGFGKAGKTLAAKLASAGKKVALVEESkaMYGGTCIN---IGCIPTKTLLVAAE-KNLSFEQVmatkntvtsrlr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 72 -KKFGAVYQYGdIKSVEDKGEY---KVINF----GNKELTAKAVIIATGAEYKKIGVPGEQELGGrgvsycaVCDGAFFK 143
Cdd:PRK07251 80 gKNYAMLAGSG-VDLYDAEAHFvsnKVIEVqagdEKIELTAETIVINTGAVSNVLPIPGLADSKH-------VYDSTGIQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 144 N-----KRLFVIGGGDSAVEEGTFLTKFADKVTIVHRRDEL--RAQRILQDRA---FKNDKIDFIWSHTLKSINEKDGKV 213
Cdd:PRK07251 152 SletlpERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTIlpREEPSVAALAkqyMEEDGITFLLNAHTTEVKNDGDQV 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 584796428 214 gsvtLTSTKDgseETHEADGVFIYIGMKPLTAPfkdLGITN------DVGYIVTKDDMTTSVPGIFAAGDV 278
Cdd:PRK07251 232 ----LVVTED---ETYRFDALLYATGRKPNTEP---LGLENtdieltERGAIKVDDYCQTSVPGVFAVGDV 292
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
5-298 |
1.74e-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: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 5 DFDIAIIGAGPAGMTAAVYASRANLKTVMIERGIP---------GGQMANteeVENFPGfEMITGPDLSTKMFEHAKKFG 75
Cdd:TIGR01438 2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPtplgtrwgiGGTCVN---VGCIPK-KLMHQAALLGQALKDSRNYG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 76 avYQYGD---------IKSVEDK-----------------------GEYK---VINFGNKE-----LTAKAVIIATGAEY 115
Cdd:TIGR01438 78 --WKVEEtvkhdwkrlVEAVQNHigslnwgyrvalrekkvkyenayAEFVdkhRIKATNKKgkekiYSAERFLIATGERP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 116 KKIGVPGEQElggrgvsYCAVCDGAFFKNK---RLFVIGGGDSAVEEGTFLTKFADKVTIVHRRDELRAqrilQDRAFKN 192
Cdd:TIGR01438 156 RYPGIPGAKE-------LCITSDDLFSLPYcpgKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRG----FDQDCAN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 193 DKIDFIWSHTLKSIN----EKDGKVGS---VTLTSTKDGSEEthEADGVFIYIGMKPLTapfKDLGITN-------DVGY 258
Cdd:TIGR01438 225 KVGEHMEEHGVKFKRqfvpIKVEQIEAkvlVEFTDSTNGIEE--EYDTVLLAIGRDACT---RKLNLENvgvkinkKTGK 299
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 584796428 259 IVTKDDMTTSVPGIFAAGDVRDKGLRQIVTATGDGSIAAQ 298
Cdd:TIGR01438 300 IPADEEEQTNVPYIYAVGDILEDKPELTPVAIQAGRLLAQ 339
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
1-278 |
1.30e-10 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 61.71 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 1 MTEIDFDIAIIGAGPAGMTAAVYASRANLKTVMIERG-IPGGQMANT---------EEVENFPGF------------EMI 58
Cdd:PRK05249 1 MHMYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYrNVGGGCTHTgtipskalrEAVLRLIGFnqnplyssyrvkLRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 59 TGPDLS----------TKMFEHAKKFGAVYQYGDIKSVEDKGEYKVI--NFGNKELTAKAVIIATGAE-YKKIGVPgeqe 125
Cdd:PRK05249 81 TFADLLaradhvinkqVEVRRGQYERNRVDLIQGRARFVDPHTVEVEcpDGEVETLTADKIVIATGSRpYRPPDVD---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 126 lggrgvsycavcdgafFKNKRLF----------------VIGGGDSAVEEGTFLTKFADKVTIVHRRDELRA---QRILQ 186
Cdd:PRK05249 157 ----------------FDHPRIYdsdsilsldhlprsliIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSfldDEISD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 187 D--RAFKNDKIDFIWSHTLKSINEKDGKVgsvtLTSTKDGSeeTHEADGVFIYIGMKPLTapfKDLGI------TNDVGY 258
Cdd:PRK05249 221 AlsYHLRDSGVTIRHNEEVEKVEGGDDGV----IVHLKSGK--KIKADCLLYANGRTGNT---DGLNLenagleADSRGQ 291
|
330 340
....*....|....*....|
gi 584796428 259 IVTKDDMTTSVPGIFAAGDV 278
Cdd:PRK05249 292 LKVNENYQTAVPHIYAVGDV 311
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
10-278 |
1.46e-10 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 61.57 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 10 IIGAGPAGMTAAVYASRANLKTVMIER--GIPGGQMAN---------TEEVENFPGFEMITGPDLSTKMFEHAKKFGAVY 78
Cdd:PRK08010 8 IIGFGKAGKTLAVTLAKAGWRVALIEQsnAMYGGTCINigciptktlVHDAQQHTDFVRAIQRKNEVVNFLRNKNFHNLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 79 QYGDIKSVEDKGEYkvINF---------GNKELTAKAVIIATGAEYKKIGVPGEQELGGrgvsycaVCDGAFFKN----- 144
Cdd:PRK08010 88 DMPNIDVIDGQAEF--INNhslrvhrpeGNLEIHGEKIFINTGAQTVVPPIPGITTTPG-------VYDSTGLLNlkelp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 145 KRLFVIGGGDSAVEEGTFLTKFADKVTIVH-------RRDELRAQ---RILQDRAfkndkIDFIWSHTLKSINEKDGKVG 214
Cdd:PRK08010 159 GHLGILGGGYIGVEFASMFANFGSKVTILEaaslflpREDRDIADniaTILRDQG-----VDIILNAHVERISHHENQVQ 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 584796428 215 SVTltstkdgSEETHEADGVFIYIGMKPLTAPF--KDLGI-TNDVGYIVTKDDMTTSVPGIFAAGDV 278
Cdd:PRK08010 234 VHS-------EHAQLAVDALLIASGRQPATASLhpENAGIaVNERGAIVVDKYLHTTADNIWAMGDV 293
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
8-298 |
7.19e-10 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 59.65 E-value: 7.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 8 IAIIGAGPAGMTAAVYASRANLKTVMIERGIPGGQMANTeeveNFPGFEMITG-----PDLSTKM---FEHAKKFGAVYQ 79
Cdd:PRK12809 313 VAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTF----GIPPFKLDKTvlsqrREIFTAMgidFHLNCEIGRDIT 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 80 YGDIKSVEDK-----GEYKVINFGNKELTAKAVIIA----TGAEYKKIGVPGEQELGGRGVsycavcdgaffKNKRLFVI 150
Cdd:PRK12809 389 FSDLTSEYDAvfigvGTYGMMRADLPHEDAPGVIQAlpflTAHTRQLMGLPESEEYPLTDV-----------EGKRVVVL 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 151 GGGDSAVE-EGTFLTKFADKVTIVHRRDELRA----QRILQDRafkNDKIDFIWSHTLKSI-NEKDGKVGSVTLTSTK-- 222
Cdd:PRK12809 458 GGGDTTMDcLRTSIRLNAASVTCAYRRDEVSMpgsrKEVVNAR---EEGVEFQFNVQPQYIaCDEDGRLTAVGLIRTAmg 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 223 -------------DGSEETHEADGVFIYIGMKPLTAPF-KDLGI---------TNDVGYIVTKddmtTSVPGIFAAGDVR 279
Cdd:PRK12809 535 epgpdgrrrprpvAGSEFELPADVLIMAFGFQAHAMPWlQGSGIkldkwgliqTGDVGYLPTQ----THLKKVFAGGDAV 610
|
330
....*....|....*....
gi 584796428 280 dKGLRQIVTATGDGSIAAQ 298
Cdd:PRK12809 611 -HGADLVVTAMAAGRQAAR 628
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
4-304 |
1.19e-09 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 59.18 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 4 IDFD-----IAIIGAGPAGMTAAVYASRANLKTVMIER----------GIPGGQMAnteevENFPGFEMITGPDLSTKmF 68
Cdd:PRK12775 424 PRFSkklgkVAICGSGPAGLAAAADLVKYGVDVTVYEAlhvvggvlqyGIPSFRLP-----RDIIDREVQRLVDIGVK-I 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 69 EHAKKFGAVYQYGDIksVEDKGeykvinfgnkeltAKAVIIATGAEYKK-IGVPGE---------------QELGGRGVS 132
Cdd:PRK12775 498 ETNKVIGKTFTVPQL--MNDKG-------------FDAVFLGVGAGAPTfLGIPGEfagqvysanefltrvNLMGGDKFP 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 133 YCavcDGAFFKNKRLFVIGGGDSAVEEGTFLTKF-ADKVTIVHRRDELRA-QRILQDRAFKNDKIDFIWSHT-LKSINEK 209
Cdd:PRK12775 563 FL---DTPISLGKSVVVIGAGNTAMDCLRVAKRLgAPTVRCVYRRSEAEApARIEEIRHAKEEGIDFFFLHSpVEIYVDA 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 210 DGKVGSVTLTSTKDGSEETH--------------EADGVFIYIGMKP---LTAPFKDLGItNDVGYIVTKDDM-----TT 267
Cdd:PRK12775 640 EGSVRGMKVEEMELGEPDEKgrrkpmptgefkdlECDTVIYALGTKAnpiITQSTPGLAL-NKWGNIAADDGKlestqST 718
|
330 340 350
....*....|....*....|....*....|....*..
gi 584796428 268 SVPGIFAAGDVRDKGlRQIVTATGDGSIAAQSAAEYI 304
Cdd:PRK12775 719 NLPGVFAGGDIVTGG-ATVILAMGAGRRAARSIATYL 754
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
6-189 |
1.29e-09 |
|
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: 58.10 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 6 FDIAIIGAGPAGMTAAVYASRANLKTVMIERG-------------------------------------IPGGQMANTEE 48
Cdd:TIGR02032 1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKKsfprykpcggalspraleeldlpgelivnlvrgarffSPNGDSVEIPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 49 vENFPGFeMITGPDLSTKMFEHAKKFGAVYQYGD-IKSVE--DKGEYKVINFGNKELTAKAVIIATGAEY---KKIGVPG 122
Cdd:TIGR02032 81 -ETELAY-VIDRDAFDEQLAERAQEAGAELRLGTrVLDVEihDDRVVVIVRGSEGTVTAKIVIGADGSRSivaKKLGLKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 123 EQ-ELGGRGVSYCAV----CDGAF---FKNKRL------FVIGGGDSAVEEGTFLTKFADKVTIVHRRDELRAQRILQDR 188
Cdd:TIGR02032 159 EPrEYGVAARAEVEMpdeeVDEDFvevYIDRGIvpggygWVFPKGDGTANVGVGSRSAEEGEDPKKYLKDFLARRPELKD 238
|
.
gi 584796428 189 A 189
Cdd:TIGR02032 239 A 239
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
3-305 |
2.07e-09 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 58.33 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 3 EIDFDIAIIGAGPAGMTAAVYASRANLKTVMIER-GIPGGQMANTEEVenFPGFEmiTGPDLSTKMFEHAKKFGA--VYQ 79
Cdd:COG1148 138 PVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKePELGGRAAQLHKT--FPGLD--CPQCILEPLIAEVEANPNitVYT 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 80 YGDIKSVE-DKGEYKVI----NFGNKELTAKAVIIATGA-EYK----------------------------KIGVPGEQE 125
Cdd:COG1148 214 GAEVEEVSgYVGNFTVTikkgPREEIEIEVGAIVLATGFkPYDptklgeygygkypnvitnlelerllaagKILRPSDGK 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 126 L----------GGR----GVSYC-AVCDGAFFKNKRLfvigggdsaveegtFLTKFAD-KVTIVHRrdELRAQRILQD-- 187
Cdd:COG1148 294 EpksvafiqcvGSRdeenGLPYCsRVCCMYALKQALY--------------LKEKNPDaDVYIFYR--DIRTYGKYEEfy 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 188 RAFKNDKIDFIWShTLKSINEKDGKVGSVTLTSTKDGSEETHEADGVFIYIGMKPLTAP---FKDLGI-TNDVGYIVTKD 263
Cdd:COG1148 358 RRAREDGVRFIRG-RVAEIEEDEGGKLVVTVEDTLLGEPVEIEADLVVLATGMVPSEDNeelAKLLKLpLDQDGFFLEAH 436
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 584796428 264 D----MTTSVPGIFAAGDVRdkGLRQIVTATGDGSIAAQSAAEYIE 305
Cdd:COG1148 437 PklrpVETATDGIFLAGAAH--GPKDIPESIAQATAAAARAIQLLS 480
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
8-297 |
2.83e-09 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 57.85 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 8 IAIIGAGPAGMTAAVYASRANLKTVMIERGIPGGQMANTEEVenfPGFEMI--------------------TGPDLS-TK 66
Cdd:PRK13748 101 VAVIGSGGAAMAAALKAVEQGARVTLIERGTIGGTCVNVGCV---PSKIMIraahiahlrrespfdggiaaTVPTIDrSR 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 67 MFE----------HAKKFGAVYQYGDIKSVEDKGEYK--------VINFGNKELTAKAVIIATGAEYKKIGVPGEQElgg 128
Cdd:PRK13748 178 LLAqqqarvdelrHAKYEGILDGNPAITVLHGEARFKddqtlivrLNDGGERVVAFDRCLIATGASPAVPPIPGLKE--- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 129 rgVSYCAVCDGAFFKN--KRLFVIGGGDSAVEEGTFLTKFADKVTIVHR-----RDELRAQRILQDrAFKNDKIDfIWSH 201
Cdd:PRK13748 255 --TPYWTSTEALVSDTipERLAVIGSSVVALELAQAFARLGSKVTILARstlffREDPAIGEAVTA-AFRAEGIE-VLEH 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 202 TLKSINEKDGkvGSVTLTsTKDGseeTHEADGVFIYIGMKPLTAPF--KDLGIT-NDVGYIVTKDDMTTSVPGIFAAGDV 278
Cdd:PRK13748 331 TQASQVAHVD--GEFVLT-TGHG---ELRADKLLVATGRAPNTRSLalDAAGVTvNAQGAIVIDQGMRTSVPHIYAAGDC 404
|
330 340
....*....|....*....|
gi 584796428 279 RDKglRQIV-TATGDGSIAA 297
Cdd:PRK13748 405 TDQ--PQFVyVAAAAGTRAA 422
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
8-304 |
4.51e-09 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 57.45 E-value: 4.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 8 IAIIGAGPAGMTAAVYASRANLKTVMIER----------GIPGGQ-----MANTEEVENFPG--FEMIT--GPD--LSTK 66
Cdd:PRK12769 330 VAIIGAGPAGLACADVLARNGVAVTVYDRhpeigglltfGIPAFKldkslLARRREIFSAMGieFELNCevGKDisLESL 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 67 MFEHAKKFGAVYQYGDIKS---VED-KGEYKVINFgnkeltakavIIATGAEykkigVPGEQELGGRgvSYCAVCDgaff 142
Cdd:PRK12769 410 LEDYDAVFVGVGTYRSMKAglpNEDaPGVYDALPF----------LIANTKQ-----VMGLEELPEE--PFINTAG---- 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 143 knKRLFVIGGGDSAVE-EGTFLTKFADKVTIVHRRDElrAQRILQDRAFKNDK---IDFIWS-HTLKSINEKDGKVGSVT 217
Cdd:PRK12769 469 --LNVVVLGGGDTAMDcVRTALRHGASNVTCAYRRDE--ANMPGSKKEVKNAReegANFEFNvQPVALELNEQGHVCGIR 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 218 LTSTK---------------DGSEETHEADGVFIYIGMKPLTAPF-KDLGI-TNDVGYIVTKDD----MTTSVPGIFAAG 276
Cdd:PRK12769 545 FLRTRlgepdaqgrrrpvpiPGSEFVMPADAVIMAFGFNPHGMPWlESHGVtVDKWGRIIADVEsqyrYQTSNPKIFAGG 624
|
330 340
....*....|....*....|....*....
gi 584796428 277 D-VRDKGLrqIVTATGDGSIAAQSAAEYI 304
Cdd:PRK12769 625 DaVRGADL--VVTAMAEGRHAAQGIIDWL 651
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
2-281 |
2.93e-08 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 54.82 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 2 TEIDFDIAIIGAGPAGMTAAVYASRANLKTVMIE--------------------RG-IP----------GGQMantEEVE 50
Cdd:PLN02507 22 THYDFDLFVIGAGSGGVRAARFSANFGAKVGICElpfhpissesiggvggtcviRGcVPkkilvygatfGGEF---EDAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 51 NFpGFEMITGPDLSTKMFEHAK-----KFGAVYQ----------YGDIKSVEDKGEYKVINFGNKEL--TAKAVIIATGA 113
Cdd:PLN02507 99 NY-GWEINEKVDFNWKKLLQKKtdeilRLNGIYKrllanagvklYEGEGKIVGPNEVEVTQLDGTKLryTAKHILIATGS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 114 EYKKIGVPGeQELGgrgvsycAVCDGAFFKN---KRLFVIGGGDSAVEEGTFLTKFADKVTIVHRR--------DELRAq 182
Cdd:PLN02507 178 RAQRPNIPG-KELA-------ITSDEALSLEelpKRAVVLGGGYIAVEFASIWRGMGATVDLFFRKelplrgfdDEMRA- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 183 riLQDRAFKNDKIDFIWSHTLKSINEKDGKVGSVTltstkDGSEEtHEADGVFIYIGMKPLTA--PFKDLGITND-VGYI 259
Cdd:PLN02507 249 --VVARNLEGRGINLHPRTNLTQLTKTEGGIKVIT-----DHGEE-FVADVVLFATGRAPNTKrlNLEAVGVELDkAGAV 320
|
330 340
....*....|....*....|..
gi 584796428 260 VTKDDMTTSVPGIFAAGDVRDK 281
Cdd:PLN02507 321 KVDEYSRTNIPSIWAIGDVTNR 342
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
3-277 |
3.07e-08 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 54.62 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 3 EIDFDIAIIGAGPAGMTAAVYASRANLKTVMIERGIPGGQMANT---------------EEVEN-----FPGFEMITGPD 62
Cdd:PTZ00058 46 RMVYDLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGTCVNVgcvpkkimfnaasihDILENsrhygFDTQFSFNLPL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 63 LSTKMFEHAKKFGAVYQY----GDIKSVEDKGE---------YKVINFGN-----------------------KELTAKA 106
Cdd:PTZ00058 126 LVERRDKYIRRLNDIYRQnlkkDNVEYFEGKGSllsenqvliKKVSQVDGeadesdddevtivsagvsqlddgQVIEGKN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 107 VIIATGaeykkiGVPGEQELggRGVSYCAVCDGaFFK---NKRLFVIGGGDSAVEEGTFLTKFADKVTIVHRR------- 176
Cdd:PTZ00058 206 ILIAVG------NKPIFPDV--KGKEFTISSDD-FFKikeAKRIGIAGSGYIAVELINVVNRLGAESYIFARGnrllrkf 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 177 DELRAQRILQDraFKNDKIDFIWSHTLKSInEKDGKVGSVTLTStkDGSEETHeADGVFIYIGMKPLTAPF--KDLGITN 254
Cdd:PTZ00058 277 DETIINELEND--MKKNNINIITHANVEEI-EKVKEKNLTIYLS--DGRKYEH-FDYVIYCVGRSPNTEDLnlKALNIKT 350
|
330 340
....*....|....*....|...
gi 584796428 255 DVGYIVTKDDMTTSVPGIFAAGD 277
Cdd:PTZ00058 351 PKGYIKVDDNQRTSVKHIYAVGD 373
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
5-61 |
4.24e-08 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 54.09 E-value: 4.24e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 584796428 5 DFDIAIIGAGPAGMTAAVYASRANLKTVMIER-GIPGGqMANTEEvenFPGFEMITGP 61
Cdd:COG1233 3 MYDVVVIGAGIGGLAAAALLARAGYRVTVLEKnDTPGG-RARTFE---RPGFRFDVGP 56
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
7-278 |
5.75e-08 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 53.60 E-value: 5.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 7 DIAIIGAGPAGMTAAVYASR---ANLKTVMIER-----------GIPGGQMaNTEEVEnfpgfemitgPDLStkmfEHAK 72
Cdd:COG1252 3 RIVIVGGGFAGLEAARRLRKklgGDAEVTLIDPnpyhlfqpllpEVAAGTL-SPDDIA----------IPLR----ELLR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 73 KFGAVYQYGDIKSvedkgeykvINFGNKELTAK--------AVIIATGAEYKKIGVPGEQElggRGVSYCAVCDGAFFKN 144
Cdd:COG1252 68 RAGVRFIQGEVTG---------IDPEARTVTLAdgrtlsydYLVIATGSVTNFFGIPGLAE---HALPLKTLEDALALRE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 145 K--------------RLFVIGGGDSAVEegtFLTKFAD----------------KVTIVHRRDEL----------RAQRI 184
Cdd:COG1252 136 RllaaferaerrrllTIVVVGGGPTGVE---LAGELAEllrkllrypgidpdkvRITLVEAGPRIlpglgeklseAAEKE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 185 LQDRafkndKIDFIWSHTLKSINEkdgkvGSVTLtstKDGseETHEADGVFIYIGMKPlTAPFKDLGI-TNDVGYIVTKD 263
Cdd:COG1252 213 LEKR-----GVEVHTGTRVTEVDA-----DGVTL---EDG--EEIPADTVIWAAGVKA-PPLLADLGLpTDRRGRVLVDP 276
|
330
....*....|....*.
gi 584796428 264 DM-TTSVPGIFAAGDV 278
Cdd:COG1252 277 TLqVPGHPNVFAIGDC 292
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
9-127 |
9.90e-08 |
|
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: 52.98 E-value: 9.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 9 AIIGAGPAGMTAAVYASRANLKTVMIERG--------IPGGQMAN-------TEEVENFPG------------------- 54
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLEKNkkigkkllISGGGRCNltnscptPEFVAYYPRngkflrsalsrfsnkdlid 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 55 -FEMItGPDLST----KMF--------------EHAKKFGAVYQYG-DIKSVEDKGEYKVINFGNKELTAKAVIIATG-A 113
Cdd:TIGR00275 81 fFESL-GLELKVeedgRVFpcsdsaadvldallNELKELGVEILTNsKVKSIEKEDGGFGVETSGGEYEADKVIIATGgL 159
|
170
....*....|....*....
gi 584796428 114 EYKKIGVPGE-----QELG 127
Cdd:TIGR00275 160 SYPQLGSTGDgyeiaESLG 178
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
7-43 |
2.66e-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: 51.46 E-value: 2.66e-07
10 20 30
....*....|....*....|....*....|....*...
gi 584796428 7 DIAIIGAGPAGMTAAVYASRANLKTVMIE-RGIPGGQM 43
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVErRGFLGGML 38
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
1-176 |
3.49e-07 |
|
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: 51.02 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 1 MTEIDFDIAIIGAGPAGMTAAVYASRANLKTVMIERG------------------IPGGQMAnteevenFPGFEMITG-P 61
Cdd:COG2072 2 AATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKAddvggtwrdnrypglrldTPSHLYS-------LPFFPNWSDdP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 62 DLSTK-----MFEH-AKKFGAV--YQYG-DIKSV---EDKGEYKVINFGNKELTAKAVIIATGAEYKKI--GVPGEQELG 127
Cdd:COG2072 75 DFPTGdeilaYLEAyADKFGLRrpIRFGtEVTSArwdEADGRWTVTTDDGETLTARFVVVATGPLSRPKipDIPGLEDFA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 584796428 128 GRGVSYCAVCDGAFFKNKRLFVIGGGDSAVEEGTFLTKFADKVTIVHRR 176
Cdd:COG2072 155 GEQLHSADWRNPVDLAGKRVLVVGTGASAVQIAPELARVAAHVTVFQRT 203
|
|
| PRK12779 |
PRK12779 |
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ... |
8-298 |
9.44e-07 |
|
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional
Pssm-ID: 183740 [Multi-domain] Cd Length: 944 Bit Score: 50.22 E-value: 9.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 8 IAIIGAGPAGM-TAAVYASRANLKTV---------MIERGIPGGQMANteevenfpgfEMITgpDLSTKMFEHAKKFGAV 77
Cdd:PRK12779 309 IAVVGSGPSGLiNAYLLAVEGFPVTVfeafhdlggVLRYGIPEFRLPN----------QLID--DVVEKIKLLGGRFVKN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 78 YQYGDIKSVEDkgeYKVINFGNkeltakaVIIATGAEYKK-IGVPGEQELGGRG-------VSYCAVCDGAF------FK 143
Cdd:PRK12779 377 FVVGKTATLED---LKAAGFWK-------IFVGTGAGLPTfMNVPGEHLLGVMSanefltrVNLMRGLDDDYetplpeVK 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 144 NKRLFVIGGGDSAVEEGTFLTKFADKVTIVHRR--DELRAQ-----RILQD----------RAFKNDKIDFIWSHTLKSI 206
Cdd:PRK12779 447 GKEVFVIGGGNTAMDAARTAKRLGGNVTIVYRRtkSEMPARveelhHALEEginlavlrapREFIGDDHTHFVTHALLDV 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 207 NEKDGKVGSVTLTSTKDGSEETHEADGVFIYIG------MKPLTAPFKdlgiTNDVGYI-VTKDDMTTSVPGIFAAGDVR 279
Cdd:PRK12779 527 NELGEPDKSGRRSPKPTGEIERVPVDLVIMALGntanpiMKDAEPGLK----TNKWGTIeVEKGSQRTSIKGVYSGGDAA 602
|
330
....*....|....*....
gi 584796428 280 DKGLRQIvTATGDGSIAAQ 298
Cdd:PRK12779 603 RGGSTAI-RAAGDGQAAAK 620
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
8-277 |
2.73e-06 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 48.50 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 8 IAIIGAGPAGMTAAVYASRAN--LKTVMIER---------GIP---GGQMANTEevenfpgfEMItgpdlsTKMFEHAKK 73
Cdd:PRK09564 3 IIIIGGTAAGMSAAAKAKRLNkeLEITVYEKtdivsfgacGLPyfvGGFFDDPN--------TMI------ARTPEEFIK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 74 FGAvyqygdikSVEDKGEYKVINFGNKELTAK-------------AVIIATGAeyKKIgVPGEQELGGRGVSYC-AVCDG 139
Cdd:PRK09564 69 SGI--------DVKTEHEVVKVDAKNKTITVKnlktgsifndtydKLMIATGA--RPI-IPPIKNINLENVYTLkSMEDG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 140 AFFK-------NKRLFVIGGGDSAVEEGTFLTKFADKVTIVHrrdelRAQRILQDrAFKNDKIDFIWS---------HTL 203
Cdd:PRK09564 138 LALKellkdeeIKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQ-----LEDRILPD-SFDKEITDVMEEelrengvelHLN 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 584796428 204 KSINEKDGKvGSVTLTSTKDGseeTHEADGVFIYIGMKPLTAPFKDLGI-TNDVGYIVTKDDMTTSVPGIFAAGD 277
Cdd:PRK09564 212 EFVKSLIGE-DKVEGVVTDKG---EYEADVVIVATGVKPNTEFLEDTGLkTLKNGAIIVDEYGETSIENIYAAGD 282
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
7-62 |
4.00e-06 |
|
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: 47.90 E-value: 4.00e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 584796428 7 DIAIIGAGPAGMTAAVYASRANLKTVMIERGI-PGGQMAnTEEVENFPgFEmiTGPD 62
Cdd:COG1232 3 RVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDrVGGLIR-TVEVDGFR-ID--RGPH 55
|
|
| COG2509 |
COG2509 |
FAD-dependent dehydrogenase [General function prediction only]; |
5-37 |
4.43e-06 |
|
FAD-dependent dehydrogenase [General function prediction only];
Pssm-ID: 441999 [Multi-domain] Cd Length: 466 Bit Score: 47.80 E-value: 4.43e-06
10 20 30
....*....|....*....|....*....|...
gi 584796428 5 DFDIAIIGAGPAGMTAAVYASRANLKTVMIERG 37
Cdd:COG2509 30 KYDVVIVGAGPAGLFAALELAEAGLKPLVLERG 62
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
3-41 |
7.16e-06 |
|
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 440673 [Multi-domain] Cd Length: 443 Bit Score: 47.14 E-value: 7.16e-06
10 20 30
....*....|....*....|....*....|....*....
gi 584796428 3 EIDFDIAIIGAGPAGMTAAVYASRANLKTVMIERGIPGG 41
Cdd:COG1053 1 DHEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRG 39
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
6-37 |
8.04e-06 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 46.81 E-value: 8.04e-06
10 20 30
....*....|....*....|....*....|..
gi 584796428 6 FDIAIIGAGPAGMTAAVYASRANLKTVMIERG 37
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKG 32
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
145-277 |
9.39e-06 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 46.83 E-value: 9.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 145 KRLFVIGGGDSAVEEGTFLTKFADKVTIVHRRDEL-----------RAQRILQDRAfkndkIDFIWSHTLKSINEKDGKV 213
Cdd:PRK04965 142 QRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASLlaslmppevssRLQHRLTEMG-----VHLLLKSQLQGLEKTDSGI 216
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 584796428 214 gSVTLTStkdgsEETHEADGVFIYIGMKPLTAPFKDLGITNDVGyIVTKDDMTTSVPGIFAAGD 277
Cdd:PRK04965 217 -RATLDS-----GRSIEVDAVIAAAGLRPNTALARRAGLAVNRG-IVVDSYLQTSAPDIYALGD 273
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
6-281 |
9.56e-06 |
|
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.
Pssm-ID: 200098 [Multi-domain] Cd Length: 486 Bit Score: 46.89 E-value: 9.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 6 FDIAIIGAGPAGM-----TAAVYASRANLKTVMIERGIP-----GGQMANteeVENFPGFEMITGPDLSTKMFEHAKkFG 75
Cdd:TIGR01423 4 FDLVVIGAGSGGLeagwnAATLYKKRVAVVDVQTHHGPPfyaalGGTCVN---VGCVPKKLMVTGAQYMDTLRESAG-FG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 76 AVYQYGDIK-------------------SVED-----KGEYKVINFGNKE--------------------LTAKAVIIAT 111
Cdd:TIGR01423 80 WEFDRSSVKanwkaliaaknkavldinkSYEGmfadtEGLTFFLGWGALEdknvvlvresadpksavkerLQAEHILLAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 112 GAEYKKIGVPGeqelggrgVSYCAVCDGAFFKN---KRLFVIGGGDSAVEEGTFLTKF---ADKVTIVHRRD-------- 177
Cdd:TIGR01423 160 GSWPQMLGIPG--------IEHCISSNEAFYLDeppRRVLTVGGGFISVEFAGIFNAYkprGGKVTLCYRNNmilrgfds 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 178 ELRAQRILQDRAfknDKIDFIwshtlksINEKDGKVgsvtlTSTKDGSE-------ETHEADGVFIYIGMKPLTAPFK-- 248
Cdd:TIGR01423 232 TLRKELTKQLRA---NGINIM-------TNENPAKV-----TLNADGSKhvtfesgKTLDVDVVMMAIGRVPRTQTLQld 296
|
330 340 350
....*....|....*....|....*....|....
gi 584796428 249 DLGIT-NDVGYIVTKDDMTTSVPGIFAAGDVRDK 281
Cdd:TIGR01423 297 KVGVElTKKGAIQVDEFSRTNVPNIYAIGDVTDR 330
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
5-36 |
1.02e-05 |
|
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis
Pssm-ID: 440419 [Multi-domain] Cd Length: 326 Bit Score: 46.47 E-value: 1.02e-05
10 20 30
....*....|....*....|....*....|..
gi 584796428 5 DFDIAIIGAGPAGMTAAVYASRANLKTVMIER 36
Cdd:COG0654 3 RTDVLIVGGGPAGLALALALARAGIRVTVVER 34
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
10-53 |
1.20e-05 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 42.52 E-value: 1.20e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 584796428 10 IIGAGPAGMTAAVYASRANLKTVMIERG-IPGGQMAnTEEVENFP 53
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRdRLGGNAY-SYRVPGYV 44
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
4-41 |
2.18e-05 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 45.67 E-value: 2.18e-05
10 20 30
....*....|....*....|....*....|....*...
gi 584796428 4 IDFDIAIIGAGPAGMTAAVYASRANLKTVMIERGIPGG 41
Cdd:COG0665 1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGS 38
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
4-37 |
2.28e-05 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 45.61 E-value: 2.28e-05
10 20 30
....*....|....*....|....*....|....
gi 584796428 4 IDFDIAIIGAGPAGMTAAVYASRANLKTVMIERG 37
Cdd:PRK05329 1 MKFDVLVIGGGLAGLTAALAAAEAGKRVALVAKG 34
|
|
| GlpB |
COG3075 |
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]; |
4-37 |
3.48e-05 |
|
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 442309 Cd Length: 415 Bit Score: 45.17 E-value: 3.48e-05
10 20 30
....*....|....*....|....*....|....
gi 584796428 4 IDFDIAIIGAGPAGMTAAVYASRANLKTVMIERG 37
Cdd:COG3075 1 MKFDVVVIGGGLAGLTAAIRAAEAGLRVAIVSAG 34
|
|
| Thi4 |
pfam01946 |
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme. |
7-43 |
3.65e-05 |
|
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
Pssm-ID: 460393 Cd Length: 232 Bit Score: 44.39 E-value: 3.65e-05
10 20 30
....*....|....*....|....*....|....*....
gi 584796428 7 DIAIIGAGPAGMTAAVY-ASRANLKTVMIERGI-PGGQM 43
Cdd:pfam01946 19 DVVIVGAGSSGLTAAYYlAKNRGLKVAIIERSVsPGGGA 57
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
7-37 |
5.52e-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: 44.20 E-value: 5.52e-05
10 20 30
....*....|....*....|....*....|.
gi 584796428 7 DIAIIGAGPAGMTAAVYASRANLKTVMIERG 37
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKG 31
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
6-36 |
7.32e-05 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 44.34 E-value: 7.32e-05
10 20 30
....*....|....*....|....*....|.
gi 584796428 6 FDIAIIGAGPAGMTAAVYASRANLKTVMIER 36
Cdd:PRK12843 17 FDVIVIGAGAAGMSAALFAAIAGLKVLLVER 47
|
|
| PLN02546 |
PLN02546 |
glutathione reductase |
3-281 |
8.72e-05 |
|
glutathione reductase
Pssm-ID: 215301 [Multi-domain] Cd Length: 558 Bit Score: 44.10 E-value: 8.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 3 EIDFDIAIIGAGPAGMTAAVYASRANLKTVMIErgIPGGQMAnTEEVENFPGFEMITG--PD----LSTKM---FEHAKK 73
Cdd:PLN02546 77 HYDFDLFTIGAGSGGVRASRFASNFGASAAVCE--LPFATIS-SDTLGGVGGTCVLRGcvPKkllvYASKYsheFEESRG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 74 FGAVYQ------------------------YGDI------KSVEDKGEY---KVINFGNKELTAKAVIIATGAEYKKIGV 120
Cdd:PLN02546 154 FGWKYEtepkhdwntlianknaelqrltgiYKNIlknagvTLIEGRGKIvdpHTVDVDGKLYTARNILIAVGGRPFIPDI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 121 PGEQelggrgvsYCAVCDGAF---FKNKRLFVIGGGDSAVEegtFLTKFADKVTIVHRRdeLRAQRILqdRAFKNDKIDF 197
Cdd:PLN02546 234 PGIE--------HAIDSDAALdlpSKPEKIAIVGGGYIALE---FAGIFNGLKSDVHVF--IRQKKVL--RGFDEEVRDF 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 198 IWSH-TLKSInEKDGKVGSVTLTSTKDGS------EETHEA-DGVFIYIGMKPLTapfKDLGI------TNDVGYIVTKD 263
Cdd:PLN02546 299 VAEQmSLRGI-EFHTEESPQAIIKSADGSlslktnKGTVEGfSHVMFATGRKPNT---KNLGLeevgvkMDKNGAIEVDE 374
|
330
....*....|....*...
gi 584796428 264 DMTTSVPGIFAAGDVRDK 281
Cdd:PLN02546 375 YSRTSVPSIWAVGDVTDR 392
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
1-39 |
9.55e-05 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 43.74 E-value: 9.55e-05
10 20 30
....*....|....*....|....*....|....*....
gi 584796428 1 MTEIDFDIAIIGAGPAGMTAAVYASRANLKTVMIERGIP 39
Cdd:PRK07494 3 MEKEHTDIAVIGGGPAGLAAAIALARAGASVALVAPEPP 41
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
9-37 |
1.02e-04 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 43.50 E-value: 1.02e-04
10 20
....*....|....*....|....*....
gi 584796428 9 AIIGAGPAGMTAAVYASRANLKTVMIERG 37
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEKN 29
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
8-112 |
1.18e-04 |
|
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: 43.26 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 8 IAIIGAGPAGMTAAVYASRANLKTVMIERGipggqmanteevenfPGFEMITGPDLSTKMFEHAKKFGAVYQYGD-IKSV 86
Cdd:COG0446 127 AVVIGGGPIGLELAEALRKRGLKVTLVERA---------------PRLLGVLDPEMAALLEEELREHGVELRLGEtVVAI 191
|
90 100
....*....|....*....|....*.
gi 584796428 87 EDKGEYKVINFGNKELTAKAVIIATG 112
Cdd:COG0446 192 DGDDKVAVTLTDGEEIPADLVVVAPG 217
|
|
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
3-36 |
1.21e-04 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 43.36 E-value: 1.21e-04
10 20 30
....*....|....*....|....*....|....
gi 584796428 3 EIDFDIAIIGAGPAGMTAAVYASRANLKTVMIER 36
Cdd:PRK06183 8 AHDTDVVIVGAGPVGLTLANLLGQYGVRVLVLER 41
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
6-44 |
1.35e-04 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 42.94 E-value: 1.35e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 584796428 6 FDIAIIGAGPAGMTAAVYASRANLKTVMIE--RGiPGGQMA 44
Cdd:COG3380 4 PDIAIIGAGIAGLAAARALQDAGHEVTVFEksRG-VGGRMA 43
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
7-42 |
1.36e-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: 43.16 E-value: 1.36e-04
10 20 30
....*....|....*....|....*....|....*.
gi 584796428 7 DIAIIGAGPAGMTAAVYASRANLKTVMIERGIPGGQ 42
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGS 36
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
1-36 |
1.40e-04 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 43.10 E-value: 1.40e-04
10 20 30
....*....|....*....|....*....|....*.
gi 584796428 1 MTEIDFDIAIIGAGPAGMTAAVYASRANLKTVMIER 36
Cdd:PRK07843 3 MTVQEYDVVVVGSGAAGMVAALTAAHRGLSTVVVEK 38
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
5-280 |
2.53e-04 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 42.50 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 5 DFDIAIIGAGPAGMTAAVYASRANLKTVMIERGIP---------GGQMANT----EEVENFPG-----FEMITGP----- 61
Cdd:PTZ00052 5 MYDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPstqgtkwglGGTCVNVgcvpKKLMHYAAnigsiFHHDSQMygwkt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 62 -------DLSTKMFEHAKKFGAVYQYG----------DIKSVEDKGEYKVINFGNKEL-TAKAVIIATGAE-YKKIGVPG 122
Cdd:PTZ00052 85 sssfnwgKLVTTVQNHIRSLNFSYRTGlrsskveyinGLAKLKDEHTVSYGDNSQEETiTAKYILIATGGRpSIPEDVPG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 123 EQElggrgvsYCAVCDGAFFKNK---RLFVIGGGDSAVEEGTFLTKFADKVTIVHRRDELRAqrilqdrafkndkIDFIW 199
Cdd:PTZ00052 165 AKE-------YSITSDDIFSLSKdpgKTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRG-------------FDRQC 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 200 SHTLKSINEKDG---KVGSVTLTSTK----------DGSEEthEADGVFIYIGMKPLTAPFK--DLGI-TNDVGYIVTKD 263
Cdd:PTZ00052 225 SEKVVEYMKEQGtlfLEGVVPINIEKmddkikvlfsDGTTE--LFDTVLYATGRKPDIKGLNlnAIGVhVNKSNKIIAPN 302
|
330
....*....|....*..
gi 584796428 264 DmTTSVPGIFAAGDVRD 280
Cdd:PTZ00052 303 D-CTNIPNIFAVGDVVE 318
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
145-278 |
2.89e-04 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 42.08 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 145 KRLFVIGGGDSAVEEGTFLTKFADKVTIVHRRDELRA-------QRILQDraFKNDKIDFIWSHTLKSINEKdgkvgSVT 217
Cdd:PRK13512 149 DKALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKlmdadmnQPILDE--LDKREIPYRLNEEIDAINGN-----EVT 221
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 584796428 218 LTSTKdgseeTHEADGVFIYIGMKPLTAPFKDLGIT-NDVGYIVTKDDMTTSVPGIFAAGDV 278
Cdd:PRK13512 222 FKSGK-----VEHYDMIIEGVGTHPNSKFIESSNIKlDDKGFIPVNDKFETNVPNIYAIGDI 278
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
6-36 |
3.72e-04 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 41.85 E-value: 3.72e-04
10 20 30
....*....|....*....|....*....|.
gi 584796428 6 FDIAIIGAGPAGMTAAVYASRANLKTVMIER 36
Cdd:PRK09126 4 SDIVVVGAGPAGLSFARSLAGSGLKVTLIER 34
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
13-113 |
4.66e-04 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 41.11 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 13 AGPAGMTAAVYASRANLKTVMIERG------IPGG-----------QMANTEEVEN--------FPGFEMITGP------ 61
Cdd:COG0644 1 AGPAGSAAARRLARAGLSVLLLEKGsfpgdkICGGgllpraleelePLGLDEPLERpvrgarfySPGGKSVELPpgrggg 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 62 ------DLSTKMFEHAKKFGAVYQYG-DIKSVE-DKGEYKVINFGNKELTAKAVIIATGA 113
Cdd:COG0644 81 yvvdraRFDRWLAEQAEEAGAEVRTGtRVTDVLrDDGRVVVRTGDGEEIRADYVVDADGA 140
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
101-278 |
4.80e-04 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 41.48 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 101 ELTAKAVIIATGAEYKKIGVPGEQELGgrgvsycavcdgaFFKN----------KRLFVIGGGDSAVEEGTFLTKFADKV 170
Cdd:PRK07846 126 EITADQVVIAAGSRPVIPPVIADSGVR-------------YHTSdtimrlpelpESLVIVGGGFIAAEFAHVFSALGVRV 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 171 TIVHRRDE-LRAQRILQDRAFKN---DKIDFIWSHTLKSINEKDgkvGSVTLTsTKDGSeeTHEADGVFIYIGMKP---- 242
Cdd:PRK07846 193 TVVNRSGRlLRHLDDDISERFTElasKRWDVRLGRNVVGVSQDG---SGVTLR-LDDGS--TVEADVLLVATGRVPngdl 266
|
170 180 190
....*....|....*....|....*....|....*.
gi 584796428 243 LTAPFKDLGITNDvGYIVTKDDMTTSVPGIFAAGDV 278
Cdd:PRK07846 267 LDAAAAGVDVDED-GRVVVDEYQRTSAEGVFALGDV 301
|
|
| glycerol3P_GlpB |
TIGR03378 |
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ... |
6-37 |
4.81e-04 |
|
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: 41.54 E-value: 4.81e-04
10 20 30
....*....|....*....|....*....|..
gi 584796428 6 FDIAIIGAGPAGMTAAVYASRANLKTVMIERG 37
Cdd:TIGR03378 1 FDVIIIGGGLAGLSCALRLAEAGKKCAIIAAG 32
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
5-36 |
9.67e-04 |
|
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
Pssm-ID: 396193 [Multi-domain] Cd Length: 348 Bit Score: 40.39 E-value: 9.67e-04
10 20 30
....*....|....*....|....*....|..
gi 584796428 5 DFDIAIIGAGPAGMTAAVYASRANLKTVMIER 36
Cdd:pfam01494 1 ETDVLIVGGGPAGLMLALLLARAGVRVVLVER 32
|
|
| PRK07233 |
PRK07233 |
hypothetical protein; Provisional |
8-53 |
1.14e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235977 [Multi-domain] Cd Length: 434 Bit Score: 40.26 E-value: 1.14e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 584796428 8 IAIIGAGPAGMTAAVYASRANLKTVMIER-GIPGGqMANTEEVENFP 53
Cdd:PRK07233 2 IAIVGGGIAGLAAAYRLAKRGHEVTVFEAdDQLGG-LAASFEFGGLP 47
|
|
| PRK07845 |
PRK07845 |
flavoprotein disulfide reductase; Reviewed |
8-278 |
1.45e-03 |
|
flavoprotein disulfide reductase; Reviewed
Pssm-ID: 236112 [Multi-domain] Cd Length: 466 Bit Score: 39.84 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 8 IAIIGAGPAGMTAAVYASRANLKTVMIERGIPGGQMANTEEVenfPGFEMITGPDLSTKmFEHAKKFG------------ 75
Cdd:PRK07845 4 IVIIGGGPGGYEAALVAAQLGADVTVIERDGLGGAAVLTDCV---PSKTLIATAEVRTE-LRRAAELGirfiddgearvd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 76 -----------AVYQYGDIKS---------VEDKGEYKVINFGN------------KELTAKAVIIATGAEykkigvPge 123
Cdd:PRK07845 80 lpavnarvkalAAAQSADIRArleregvrvIAGRGRLIDPGLGPhrvkvttadggeETLDADVVLIATGAS------P-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 124 QELGGrgvsycAVCDGAFFKNKR-----------LFVIGGGDSAVEEGTFLTKFADKVTIVHRRDEL------RAQRILQ 186
Cdd:PRK07845 152 RILPT------AEPDGERILTWRqlydldelpehLIVVGSGVTGAEFASAYTELGVKVTLVSSRDRVlpgedaDAAEVLE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584796428 187 D-------RAFKNDKIDfiwshtlKSINEKDGKVgsVTLTstkDGS--EETHeadgVFIYIGMKPLTApfkDLGI----- 252
Cdd:PRK07845 226 EvfarrgmTVLKRSRAE-------SVERTGDGVV--VTLT---DGRtvEGSH----ALMAVGSVPNTA---GLGLeeagv 286
|
330 340
....*....|....*....|....*..
gi 584796428 253 -TNDVGYIVTKDDMTTSVPGIFAAGDV 278
Cdd:PRK07845 287 eLTPSGHITVDRVSRTSVPGIYAAGDC 313
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
7-41 |
1.80e-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: 39.84 E-value: 1.80e-03
10 20 30
....*....|....*....|....*....|....*.
gi 584796428 7 DIAIIGAGPAGMTAAVYASRANLKTVMIE-RGIPGG 41
Cdd:COG3349 5 RVVVVGGGLAGLAAAVELAEAGFRVTLLEaRPRLGG 40
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
7-36 |
2.53e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 39.10 E-value: 2.53e-03
10 20 30
....*....|....*....|....*....|
gi 584796428 7 DIAIIGAGPAGMTAAVYASRANLKTVMIER 36
Cdd:PRK07208 6 SVVIIGAGPAGLTAAYELLKRGYPVTVLEA 35
|
|
| PRK08275 |
PRK08275 |
putative oxidoreductase; Provisional |
267-305 |
2.71e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 181346 [Multi-domain] Cd Length: 554 Bit Score: 39.27 E-value: 2.71e-03
10 20 30
....*....|....*....|....*....|....*....
gi 584796428 267 TSVPGIFAAGDVRDKGLRQIVTATGDGSIAAQSAAEYIE 305
Cdd:PRK08275 367 TTVPGLYAAGDMASVPHNYMLGAFTYGWFAGENAAEYVA 405
|
|
| PRK10015 |
PRK10015 |
oxidoreductase; Provisional |
1-41 |
3.87e-03 |
|
oxidoreductase; Provisional
Pssm-ID: 182194 [Multi-domain] Cd Length: 429 Bit Score: 38.80 E-value: 3.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 584796428 1 MTEIDFDIAIIGAGPAGMTAAVYASRANLKTVMIERGIPGG 41
Cdd:PRK10015 1 MSDDKFDAIVVGAGVAGSVAALVMARAGLDVLVIERGDSAG 41
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
7-41 |
5.22e-03 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 38.36 E-value: 5.22e-03
10 20 30
....*....|....*....|....*....|....*.
gi 584796428 7 DIAIIGAGPAGMTAAVYASRANLKTVMIE-RGIPGG 41
Cdd:COG1231 9 DVVIVGAGLAGLAAARELRKAGLDVTVLEaRDRVGG 44
|
|
| PRK06185 |
PRK06185 |
FAD-dependent oxidoreductase; |
1-36 |
5.22e-03 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 235729 [Multi-domain] Cd Length: 407 Bit Score: 38.30 E-value: 5.22e-03
10 20 30
....*....|....*....|....*....|....*.
gi 584796428 1 MTEIDFDIAIIGAGPAGMTAAVYASRANLKTVMIER 36
Cdd:PRK06185 2 AEVETTDCCIVGGGPAGMMLGLLLARAGVDVTVLEK 37
|
|
| solA |
PRK11259 |
N-methyl-L-tryptophan oxidase; |
6-43 |
5.39e-03 |
|
N-methyl-L-tryptophan oxidase;
Pssm-ID: 236887 [Multi-domain] Cd Length: 376 Bit Score: 38.28 E-value: 5.39e-03
10 20 30
....*....|....*....|....*....|....*...
gi 584796428 6 FDIAIIGAGPAGMTAAVYASRANLKTVMIERGIPGGQM 43
Cdd:PRK11259 4 YDVIVIGLGSMGSAAGYYLARRGLRVLGLDRFMPPHQQ 41
|
|
| PRK09231 |
PRK09231 |
fumarate reductase flavoprotein subunit; Validated |
4-39 |
7.61e-03 |
|
fumarate reductase flavoprotein subunit; Validated
Pssm-ID: 236421 [Multi-domain] Cd Length: 582 Bit Score: 37.69 E-value: 7.61e-03
10 20 30
....*....|....*....|....*....|....*...
gi 584796428 4 IDFDIAIIGAGPAGMTAAVYASRAN--LKTVMIERGIP 39
Cdd:PRK09231 3 FQADLAIIGAGGAGLRAAIAAAEANpnLKIALISKVYP 40
|
|
| |
