|
Name |
Accession |
Description |
Interval |
E-value |
| TRX_reduct |
TIGR01292 |
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ... |
7-304 |
2.72e-156 |
|
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: 438.60 E-value: 2.72e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 7 DVAIIGAGPAGMTAAVYASRANLSTVMIERGMPGGQMANTEEVENFPGF-EMITGPDLSTKMFEHAKKFGAEYQYGDIKS 85
Cdd:TIGR01292 1 DVIIIGAGPAGLTAAIYAARANLKPLLIEGMEPGGQLTTTTEVENYPGFpEGISGPELMEKMKEQAVKFGAEIIYEEVIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 86 IEDKGDYKEINLGNK-EITARAVIISTGAEYKKIGVPGEQELGGRGVSYCAVCDGAFFKNKNLFVIGGGDSAVEEGAFLT 164
Cdd:TIGR01292 81 VDKSDRPFKVYTGDGkEYTAKAVIIATGASARKLGIPGEDEFWGRGVSYCATCDGPFFKNKEVAVVGGGDSAIEEALYLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 165 KFADKVTIVHRRDELRAQKILQDRAFKNDKIDFIWSHTLKSINEkDGKVGSVTLVSTKDASEQTLDADGVFIYIGMKPLT 244
Cdd:TIGR01292 161 RIAKKVTLVHRRDKFRAEKILLDRLKKNPKIEFLWNSTVEEIVG-DNKVEGVKIKNTVTGEEEELEVDGVFIAIGHEPNT 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 245 APFVNLGITNDMGYIVTEDNMSTKVPGIFAAGDVRDKGLRQIVTATGDGSIAAQSAIDYI 304
Cdd:TIGR01292 240 ELLKGLLELDENGYIVTDEGMRTSVPGVFAAGDVRDKGYRQAVTAAGDGCIAALSAERYL 299
|
|
| TrxB |
COG0492 |
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones]; |
6-308 |
3.82e-156 |
|
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440258 [Multi-domain] Cd Length: 305 Bit Score: 438.40 E-value: 3.82e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 6 YDVAIIGAGPAGMTAAVYASRANLSTVMIERGMPGGQMANTEEVENFPGF-EMITGPDLSTKMFEHAKKFGAEYQYGDIK 84
Cdd:COG0492 1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPGGQLATTKEIENYPGFpEGISGPELAERLREQAERFGAEILLEEVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 85 SIEDKGDYKEINLGN-KEITARAVIISTGAEYKKIGVPGEQELGGRGVSYCAVCDGAFFKNKNLFVIGGGDSAVEEGAFL 163
Cdd:COG0492 81 SVDKDDGPFRVTTDDgTEYEAKAVIIATGAGPRKLGLPGEEEFEGRGVSYCATCDGFFFRGKDVVVVGGGDSALEEALYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 164 TKFADKVTIVHRRDELRAQKILQDRAFKNDKIDFIWSHTLKSInEKDGKVGSVTLVSTKDASEQTLDADGVFIYIGMKPL 243
Cdd:COG0492 161 TKFASKVTLIHRRDELRASKILVERLRANPKIEVLWNTEVTEI-EGDGRVEGVTLKNVKTGEEKELEVDGVFVAIGLKPN 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515497732 244 TAPFVNLGI-TNDMGYIVTEDNMSTKVPGIFAAGDVRDKGLRQIVTATGDGSIAAQSAIDYIEELK 308
Cdd:COG0492 240 TELLKGLGLeLDEDGYIVVDEDMETSVPGVFAAGDVRDYKYRQAATAAGEGAIAALSAARYLEPLK 305
|
|
| AhpF_homolog |
TIGR03143 |
putative alkyl hydroperoxide reductase F subunit; This family of thioredoxin reductase ... |
1-310 |
9.35e-92 |
|
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: 283.21 E-value: 9.35e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 1 MTEInYDVAIIGAGPAGMTAAVYASRANLSTVMIERGMPGGQMANTEEVENFPGFEMITGPDLSTKMFEHAKKFGAEYQY 80
Cdd:TIGR03143 1 MEEI-YDLIIIGGGPAGLSAGIYAGRAKLDTLIIEKDDFGGQITITSEVVNYPGILNTTGPELMQEMRQQAQDFGVKFLQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 81 GDIKSIEDKGDYKEINLGNKEITARAVIISTGAEYKKIGVPGEQELGGRGVSYCAVCDGAFFKNKNLFVIGGGDSAVEEG 160
Cdd:TIGR03143 80 AEVLDVDFDGDIKTIKTARGDYKTLAVLIATGASPRKLGFPGEEEFTGRGVAYCATCDGEFFTGMDVFVIGGGFAAAEEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 161 AFLTKFADKVTIVHRRDELRAQKILQDRAFKNDKIDFIWSHTLKSINeKDGKVGSVTLVSTKDASEQTLDAD------GV 234
Cdd:TIGR03143 160 VFLTRYASKVTVIVREPDFTCAKLIAEKVKNHPKIEVKFNTELKEAT-GDDGLRYAKFVNNVTGEITEYKAPkdagtfGV 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515497732 235 FIYIGMKPLTAPFVNLGITNDMGYIVTEDNMSTKVPGIFAAGDVRDKGLRQIVTATGDGSIAAQSAIDYIEELKDK 310
Cdd:TIGR03143 239 FVFVGYAPSSELFKGVVELDKRGYIPTNEDMETNVPGVYAAGDLRPKELRQVVTAVADGAIAATSAERYVKELKEK 314
|
|
| PRK15317 |
PRK15317 |
alkyl hydroperoxide reductase subunit F; Provisional |
6-304 |
1.22e-75 |
|
alkyl hydroperoxide reductase subunit F; Provisional
Pssm-ID: 237942 [Multi-domain] Cd Length: 517 Bit Score: 240.45 E-value: 1.22e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 6 YDVAIIGAGPAGMTAAVYASRANLSTVMI-ERGmpGGQMANTEEVENFPGFEMITGPDLSTKMFEHAKkfgaeyQYG-DI 83
Cdd:PRK15317 212 YDVLVVGGGPAGAAAAIYAARKGIRTGIVaERF--GGQVLDTMGIENFISVPETEGPKLAAALEEHVK------EYDvDI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 84 ------KSIEDKGDYKEINLGNKE-ITARAVIISTGAEYKKIGVPGEQELGGRGVSYCAVCDGAFFKNKNLFVIGGGDSA 156
Cdd:PRK15317 284 mnlqraSKLEPAAGLIEVELANGAvLKAKTVILATGARWRNMNVPGEDEYRNKGVAYCPHCDGPLFKGKRVAVIGGGNSG 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 157 VEEGAFLTKFADKVTIVHRRDELRAQKILQDRAFKNDKIDFIWSHTLKSINEKDGKVGSVTLVSTKDASEQTLDADGVFI 236
Cdd:PRK15317 364 VEAAIDLAGIVKHVTVLEFAPELKADQVLQDKLRSLPNVTIITNAQTTEVTGDGDKVTGLTYKDRTTGEEHHLELEGVFV 443
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515497732 237 YIGMKPLTAPFVNLGITNDMGYIVTEDNMSTKVPGIFAAGDVRDKGLRQIVTATGDGSIAAQSAIDYI 304
Cdd:PRK15317 444 QIGLVPNTEWLKGTVELNRRGEIIVDARGATSVPGVFAAGDCTTVPYKQIIIAMGEGAKAALSAFDYL 511
|
|
| PRK10262 |
PRK10262 |
thioredoxin reductase; Provisional |
10-310 |
1.52e-65 |
|
thioredoxin reductase; Provisional
Pssm-ID: 182343 [Multi-domain] Cd Length: 321 Bit Score: 208.76 E-value: 1.52e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 10 IIGAGPAGMTAAVYASRANLSTVMIERGMPGGQMANTEEVENFPGFEM-ITGPDLSTKMFEHAKKFGAEYQYGDIKSIED 88
Cdd:PRK10262 11 ILGSGPAGYTAAVYAARANLQPVLITGMEKGGQLTTTTEVENWPGDPNdLTGPLLMERMHEHATKFETEIIFDHINKVDL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 89 KGDYKEINLGNKEITARAVIISTGAEYKKIGVPGEQELGGRGVSYCAVCDGAFFKNKNLFVIGGGDSAVEEGAFLTKFAD 168
Cdd:PRK10262 91 QNRPFRLTGDSGEYTCDALIIATGASARYLGLPSEEAFKGRGVSACATCDGFFYRNQKVAVIGGGNTAVEEALYLSNIAS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 169 KVTIVHRRDELRAQKILQDRAFKNDKIDFIWSHTLKSINEKDGKVGSVTLVSTKDASE----QTLDADGVFIYIGMKPLT 244
Cdd:PRK10262 171 EVHLIHRRDGFRAEKILIKRLMDKVENGNIILHTNRTLEEVTGDQMGVTGVRLRDTQNsdniESLDVAGLFVAIGHSPNT 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515497732 245 APFV-NLGITNdmGYIVTEDNM-----STKVPGIFAAGDVRDKGLRQIVTATGDGSIAAQSAIDYIEELKDK 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 |
8.90e-60 |
|
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: 193.30 E-value: 8.90e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 6 YDVAIIGAGPAGMTAAVYASRANLSTVMIERG--MPGGQMANTEEVENFPGFEMI--TGPDLSTKMFEHAKKFGAEYQYG 81
Cdd:pfam07992 1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEgtCPYGGCVLSKALLGAAEAPEIasLWADLYKRKEEVVKKLNNGIEVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 82 D----IKSIEDKGDYKEINL---GNKEITARAVIISTGAEYKKIGVPGEQELGGRGVSYCAVCDGAFFKN--KNLFVIGG 152
Cdd:pfam07992 81 LgtevVSIDPGAKKVVLEELvdgDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLlpKRVVVVGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 153 GDSAVEEGAFLTKFADKVTIVHRRDEL------RAQKILQDRaFKNDKIDFIWSHTLKSINEKDGKVgsvtlvSTKDASE 226
Cdd:pfam07992 161 GYIGVELAAALAKLGKEVTLIEALDRLlrafdeEISAALEKA-LEKNGVEVRLGTSVKEIIGDGDGV------EVILKDG 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515497732 227 QTLDADGVFIYIGMKPLTAPFVNLGI-TNDMGYIVTEDNMSTKVPGIFAAGDVRDKGLRQIVTATGDG 293
Cdd:pfam07992 234 TEIDADLVVVAIGRRPNTELLEAAGLeLDERGGIVVDEYLRTSVPGIYAAGDCRVGGPELAQNAVAQG 301
|
|
| PRK06292 |
PRK06292 |
dihydrolipoamide dehydrogenase; Validated |
4-278 |
2.18e-34 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235774 [Multi-domain] Cd Length: 460 Bit Score: 130.30 E-value: 2.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 4 INYDVAIIGAGPAGMTAAVYASRANLSTVMIERGMPGGQMANT---------------EEVENFPGFE-MITGPDLSTK- 66
Cdd:PRK06292 2 EKYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLGGTCLNVgcipskaliaaaeafHEAKHAEEFGiHADGPKIDFKk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 67 MFEHAKKFgaeyQYGDIKSIED-----------KG-----DYKEINLGNKEITARAVIISTGAeyKKIGVPG-EQELGGR 129
Cdd:PRK06292 82 VMARVRRE----RDRFVGGVVEglekkpkidkiKGtarfvDPNTVEVNGERIEAKNIVIATGS--RVPPIPGvWLILGDR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 130 GVSYcavcDGAFFKN---KNLFVIGGGDSAVEEGAFLTKFADKVTIVHRRDEL----------RAQKILQDRafkndkID 196
Cdd:PRK06292 156 LLTS----DDAFELDklpKSLAVIGGGVIGLELGQALSRLGVKVTVFERGDRIlpledpevskQAQKILSKE------FK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 197 FIWSHTLKSInEKDGKVGSVtlVSTKDASEQTLDADGVFIYIGMKPLTAP--FVNLGI-TNDMGYIVTEDNMSTKVPGIF 273
Cdd:PRK06292 226 IKLGAKVTSV-EKSGDEKVE--ELEKGGKTETIEADYVLVATGRRPNTDGlgLENTGIeLDERGRPVVDEHTQTSVPGIY 302
|
....*
gi 515497732 274 AAGDV 278
Cdd:PRK06292 303 AAGDV 307
|
|
| Lpd |
COG1249 |
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ... |
3-281 |
4.98e-32 |
|
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: 123.66 E-value: 4.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 3 EINYDVAIIGAGPAGMTAAVYASRANLSTVMIERGMPGGQMANT---------------EEVENFPGFEMITGP---DLS 64
Cdd:COG1249 1 MKDYDLVVIGAGPGGYVAAIRAAQLGLKVALVEKGRLGGTCLNVgcipskallhaaevaHEARHAAEFGISAGApsvDWA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 65 tKMFEHAKKF------GAEYQYGD--IKSIEDKG---DYKEINL-GNKEITARAVIISTGAEYKKIGVPGEQElgGRGVS 132
Cdd:COG1249 81 -ALMARKDKVvdrlrgGVEELLKKngVDVIRGRArfvDPHTVEVtGGETLTADHIVIATGSRPRVPPIPGLDE--VRVLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 133 YcavcDGAFFKN---KNLFVIGGGDSAVEEGAFLTKFADKVTIVHRRDEL------RAQKILQdRAFKNDKIDFIWSHTL 203
Cdd:COG1249 158 S----DEALELEelpKSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDRLlpgedpEISEALE-KALEKEGIDILTGAKV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 204 KSInEKDGkvGSVTLVSTKDASEQTLDADGVFIYIGMKPLTApfvNLGI------TNDMGYIVTEDNMSTKVPGIFAAGD 277
Cdd:COG1249 233 TSV-EKTG--DGVTVTLEDGGGEEAVEADKVLVATGRRPNTD---GLGLeaagveLDERGGIKVDEYLRTSVPGIYAIGD 306
|
....
gi 515497732 278 VRDK 281
Cdd:COG1249 307 VTGG 310
|
|
| GltD |
COG0493 |
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ... |
8-302 |
1.74e-26 |
|
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: 107.91 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 8 VAIIGAGPAGMTAAVYASRANLSTVMIERG-MPGGQMAN------------TEEVENF--PGFEMITGpdlstkmfehaK 72
Cdd:COG0493 124 VAVVGSGPAGLAAAYQLARAGHEVTVFEALdKPGGLLRYgipefrlpkdvlDREIELIeaLGVEFRTN-----------V 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 73 KFGaeyqyGDIkSIED-KGDYKeinlgnkeitarAVIISTGAE-YKKIGVPGEqELGG--------RGVSYCAVCDGAFF 142
Cdd:COG0493 193 EVG-----KDI-TLDElLEEFD------------AVFLATGAGkPRDLGIPGE-DLKGvhsamdflTAVNLGEAPDTILA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 143 KNKNLFVIGGGD-------SAVEEGAfltkfaDKVTIVHRRD--ELRAQKILQDRAfKNDKIDFIWSHTLKSIN-EKDGK 212
Cdd:COG0493 254 VGKRVVVIGGGNtamdcarTALRLGA------ESVTIVYRRTreEMPASKEEVEEA-LEEGVEFLFLVAPVEIIgDENGR 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 213 VGSVTLVSTK----DA-----------SEQTLDADGVFIYIGMKPLTAPFVN-LGI-TNDMGYIVT-EDNMSTKVPGIFA 274
Cdd:COG0493 327 VTGLECVRMElgepDEsgrrrpvpiegSEFTLPADLVILAIGQTPDPSGLEEeLGLeLDKRGTIVVdEETYQTSLPGVFA 406
|
330 340
....*....|....*....|....*...
gi 515497732 275 AGDVRdKGLRQIVTATGDGSIAAQsAID 302
Cdd:COG0493 407 GGDAV-RGPSLVVWAIAEGRKAAR-AID 432
|
|
| PRK11749 |
PRK11749 |
dihydropyrimidine dehydrogenase subunit A; Provisional |
8-310 |
3.86e-24 |
|
dihydropyrimidine dehydrogenase subunit A; Provisional
Pssm-ID: 236967 [Multi-domain] Cd Length: 457 Bit Score: 101.79 E-value: 3.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 8 VAIIGAGPAGMTAAVYASRANLS-TVMIERGMPGGQManteeVENFPGFEMitgP-DLSTKMFEHAKKFGAEYQY----G 81
Cdd:PRK11749 143 VAVIGAGPAGLTAAHRLARKGYDvTIFEARDKAGGLL-----RYGIPEFRL---PkDIVDREVERLLKLGVEIRTntevG 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 82 DIKSIED-KGDYKeinlgnkeitarAVIISTGA-EYKKIGVPGEqELGG--RGVSYC-----AVCDGAFFKNKNLFVIGG 152
Cdd:PRK11749 215 RDITLDElRAGYD------------AVFIGTGAgLPRFLGIPGE-NLGGvySAVDFLtrvnqAVADYDLPVGKRVVVIGG 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 153 GD-------SAVEEGAfltkfaDKVTIVHRRD--ELRAQKILQDRAfKNDKIDFIWSHTLKSINEKDGKVGSVTLVSTK- 222
Cdd:PRK11749 282 GNtamdaarTAKRLGA------ESVTIVYRRGreEMPASEEEVEHA-KEEGVEFEWLAAPVEILGDEGRVTGVEFVRMEl 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 223 ---DAS----------EQTLDADGVFIYIGMKPLTAPFVN---LGITNDMGYIVTEDNMSTKVPGIFAAGDVRdKGLRQI 286
Cdd:PRK11749 355 gepDASgrrrvpiegsEFTLPADLVIKAIGQTPNPLILSTtpgLELNRWGTIIADDETGRTSLPGVFAGGDIV-TGAATV 433
|
330 340
....*....|....*....|....*
gi 515497732 287 VTATGDGSIAAQsAID-YIEELKDK 310
Cdd:PRK11749 434 VWAVGDGKDAAE-AIHeYLEGAASA 457
|
|
| PRK06416 |
PRK06416 |
dihydrolipoamide dehydrogenase; Reviewed |
2-304 |
2.07e-23 |
|
dihydrolipoamide dehydrogenase; Reviewed
Pssm-ID: 235798 [Multi-domain] Cd Length: 462 Bit Score: 99.45 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 2 TEINYDVAIIGAGPAGMTAAVYASRANLSTVMIERGMPGGQMANT---------------EEVENFPGFEMITGP---DL 63
Cdd:PRK06416 1 FAFEYDVIVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLGGTCLNRgcipskallhaaeraDEARHSEDFGIKAENvgiDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 64 sTKMFEHA---------------KKFGAEYQYGDIKsIEDKGdykEIN----LGNKEITARAVIISTGAeyKKIGVPGeQ 124
Cdd:PRK06416 81 -KKVQEWKngvvnrltggvegllKKNKVDIIRGEAK-LVDPN---TVRvmteDGEQTYTAKNIILATGS--RPRELPG-I 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 125 ELGGRGVSYCavcDGAF---FKNKNLFVIGGGDSAVEEGAFLTKFADKVTIVHRRDELRA------QKILQdRAFKNDKI 195
Cdd:PRK06416 153 EIDGRVIWTS---DEALnldEVPKSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPgedkeiSKLAE-RALKKRGI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 196 DFIWSHTLKSINEKDGKVgSVTLVstKDASEQTLDADGVFIYIGMKPLTAP--FVNLGITNDMGYIVTEDNMSTKVPGIF 273
Cdd:PRK06416 229 KIKTGAKAKKVEQTDDGV-TVTLE--DGGKEETLEADYVLVAVGRRPNTENlgLEELGVKTDRGFIEVDEQLRTNVPNIY 305
|
330 340 350
....*....|....*....|....*....|....*..
gi 515497732 274 AAGDVRDkGLRQIVTATGDGSIAAQ------SAIDYI 304
Cdd:PRK06416 306 AIGDIVG-GPMLAHKASAEGIIAAEaiagnpHPIDYR 341
|
|
| lipoamide_DH |
TIGR01350 |
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ... |
5-281 |
3.50e-23 |
|
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: 98.87 E-value: 3.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 5 NYDVAIIGAGPAGMTAAVYASRANLSTVMIERGMPGGQ------------MANTEEVENFP-----GFEmITGPDLS-TK 66
Cdd:TIGR01350 1 AYDVIVIGGGPGGYVAAIRAAQLGLKVALVEKEYLGGTclnvgciptkalLHSAEVYDEIKhakdlGIE-VENVSVDwEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 67 MFEHA---------------KKFGAEyQYGDIKSIEDKGDYkEINLGNKE--ITARAVIISTGAEYKKIgvPGEQELGGR 129
Cdd:TIGR01350 80 MQKRKnkvvkklvggvsgllKKNKVT-VIKGEAKFLDPGTV-SVTGENGEetLEAKNIIIATGSRPRSL--PGPFDFDGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 130 GV--SycavcDGAFF---KNKNLFVIGGGDSAVEEGAFLTKFADKVTIVHRRDELRAQ------KILQdRAFKNDKIDFI 198
Cdd:TIGR01350 156 VVitS-----TGALNleeVPESLVIIGGGVIGIEFASIFASLGSKVTVIEMLDRILPGedaevsKVLQ-KALKKKGVKIL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 199 WSHTLKSINEKDGKVgsvtLVSTKDASEQTLDADGVFIYIGMKPLTAPFV--NLGI-TNDMGYIVTEDNMSTKVPGIFAA 275
Cdd:TIGR01350 230 TNTKVTAVEKNDDQV----TYENKGGETETLTGEKVLVAVGRKPNTEGLGleKLGVeLDERGRIVVDEYMRTNVPGIYAI 305
|
....*.
gi 515497732 276 GDVRDK 281
Cdd:TIGR01350 306 GDVIGG 311
|
|
| PRK12770 |
PRK12770 |
putative glutamate synthase subunit beta; Provisional |
8-306 |
1.99e-20 |
|
putative glutamate synthase subunit beta; Provisional
Pssm-ID: 237197 [Multi-domain] Cd Length: 352 Bit Score: 90.05 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 8 VAIIGAGPAGMTAAVY-ASRANLSTVMIERGMPGGQMAnteevenF--PGFEM-ITGPDLSTKMFEHAkkfGAEYQ---- 79
Cdd:PRK12770 21 VAIIGAGPAGLAAAGYlACLGYEVHVYDKLPEPGGLML-------FgiPEFRIpIERVREGVKELEEA---GVVFHtrtk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 80 -YGDIKSIEDKGD--YKEInLGNKEITAR--AVIISTGA-EYKKIGVPGEqELGG-----------RGVSYC-----AVC 137
Cdd:PRK12770 91 vCCGEPLHEEEGDefVERI-VSLEELVKKydAVLIATGTwKSRKLGIPGE-DLPGvysaleylfriRAAKLGylpweKVP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 138 DgafFKNKNLFVIGGGDSAVE--EGAFLTKfADKVTIVHRR--DELRAQK----ILQDRAfkndkIDFIWSHTLKSINEk 209
Cdd:PRK12770 169 P---VEGKKVVVVGAGLTAVDaaLEAVLLG-AEKVYLAYRRtiNEAPAGKyeieRLIARG-----VEFLELVTPVRIIG- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 210 DGKVGSVTLVSTK---------------DASEQTLDADGVFIYIGMKPlTAPFVN--LGI-TNDMGYIVTEDNMSTKVPG 271
Cdd:PRK12770 239 EGRVEGVELAKMRlgepdesgrprpvpiPGSEFVLEADTVVFAIGEIP-TPPFAKecLGIeLNRKGEIVVDEKHMTSREG 317
|
330 340 350
....*....|....*....|....*....|....*
gi 515497732 272 IFAAGDVRdKGLRQIVTATGDGSIAAQSAIDYIEE 306
Cdd:PRK12770 318 VFAAGDVV-TGPSKIGKAIKSGLRAAQSIHEWLDL 351
|
|
| gltD |
PRK12810 |
glutamate synthase subunit beta; Reviewed |
8-305 |
7.31e-18 |
|
glutamate synthase subunit beta; Reviewed
Pssm-ID: 237213 [Multi-domain] Cd Length: 471 Bit Score: 83.67 E-value: 7.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 8 VAIIGAGPAGMTAAVYASRANLSTVMIER-GMPGGQManteeveNF--PGFEMitGPDLSTKMFEHAKKFGAEYQYGdik 84
Cdd:PRK12810 146 VAVVGSGPAGLAAADQLARAGHKVTVFERaDRIGGLL-------RYgiPDFKL--EKEVIDRRIELMEAEGIEFRTN--- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 85 siedkgdykeINLGnKEITAR-------AVIISTGAE-YKKIGVPGEqELGGrgVsYCAV-------------CDGAFF- 142
Cdd:PRK12810 214 ----------VEVG-KDITAEellaeydAVFLGTGAYkPRDLGIPGR-DLDG--V-HFAMdfliqntrrvlgdETEPFIs 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 143 -KNKNLFVIGGGD-------SAVEEGAfltkfadkvTIVHRRD------ELRAQKILQDRAFKNDKID--------FIWS 200
Cdd:PRK12810 279 aKGKHVVVIGGGDtgmdcvgTAIRQGA---------KSVTQRDimpmppSRRNKNNPWPYWPMKLEVSnaheegveREFN 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 201 HTLKSINEKDGKVGSVTLVSTKDA---------SEQTLDADGVFIYIGMKPLTAPFVN-LGI-TNDMGYIVTED-NMSTK 268
Cdd:PRK12810 350 VQTKEFEGENGKVTGVKVVRTELGegdfepvegSEFVLPADLVLLAMGFTGPEAGLLAqFGVeLDERGRVAAPDnAYQTS 429
|
330 340 350
....*....|....*....|....*....|....*..
gi 515497732 269 VPGIFAAGDVRdKGLRQIVTATGDGSIAAQSAIDYIE 305
Cdd:PRK12810 430 NPKVFAAGDMR-RGQSLVVWAIAEGRQAARAIDAYLM 465
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
94-278 |
4.02e-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: 80.24 E-value: 4.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 94 EINLGNKEITAR--------AVIISTGAEYKKIGVPGeqeLGGRGVSYCAVCDGAF--------FKNKNLFVIGGG---- 153
Cdd:COG0446 61 AIDPEAKTVTLRdgetlsydKLVLATGARPRPPPIPG---LDLPGVFTLRTLDDADalrealkeFKGKRAVVIGGGpigl 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 154 ---DSAVEEGAfltkfadKVTIVHRRDEL----------RAQKILQDRafkndKIDFIWSHTLKSInEKDGKVGsVTLvs 220
Cdd:COG0446 138 elaEALRKRGL-------KVTLVERAPRLlgvldpemaaLLEEELREH-----GVELRLGETVVAI-DGDDKVA-VTL-- 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 515497732 221 tkdASEQTLDADGVFIYIGMKPLTAPFVNLGI-TNDMGYIVTEDNMSTKVPGIFAAGDV 278
Cdd:COG0446 202 ---TDGEEIPADLVVVAPGVRPNTELAKDAGLaLGERGWIKVDETLQTSDPDVYAAGDC 257
|
|
| PRK06370 |
PRK06370 |
FAD-containing oxidoreductase; |
6-302 |
9.41e-17 |
|
FAD-containing oxidoreductase;
Pssm-ID: 235787 [Multi-domain] Cd Length: 463 Bit Score: 80.25 E-value: 9.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 6 YDVAIIGAGPAGMTAAVYASRANLSTVMIERGMPGGQMANT------------------EEVENFpGFEmITGP---DLS 64
Cdd:PRK06370 6 YDAIVIGAGQAGPPLAARAAGLGMKVALIERGLLGGTCVNTgcvptktliasaraahlaRRAAEY-GVS-VGGPvsvDFK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 65 TKMfEHAKKFGAEYQYGDIKSIEDK------------GDYKEINLGNKEITARAVIISTGAEYKKIGVPGEQELGgrgvs 132
Cdd:PRK06370 84 AVM-ARKRRIRARSRHGSEQWLRGLegvdvfrgharfESPNTVRVGGETLRAKRIFINTGARAAIPPIPGLDEVG----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 133 ycavcdgaFFKNKNLF----------VIGGGDSAVEEGAFLTKFADKVTIVHR------RDELRAQKILQDrAFKNDKID 196
Cdd:PRK06370 158 --------YLTNETIFsldelpehlvIIGGGYIGLEFAQMFRRFGSEVTVIERgprllpREDEDVAAAVRE-ILEREGID 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 197 FIWSHTLKSInEKDGKVGSVTLvsTKDASEQTLDADGVFIYIGMKPLTAPFvNL---GITND-MGYIVTEDNMSTKVPGI 272
Cdd:PRK06370 229 VRLNAECIRV-ERDGDGIAVGL--DCNGGAPEITGSHILVAVGRVPNTDDL-GLeaaGVETDaRGYIKVDDQLRTTNPGI 304
|
330 340 350
....*....|....*....|....*....|
gi 515497732 273 FAAGDVRDKGlRQIVTATGDGSIAAQSAID 302
Cdd:PRK06370 305 YAAGDCNGRG-AFTHTAYNDARIVAANLLD 333
|
|
| Pyr_redox_3 |
pfam13738 |
Pyridine nucleotide-disulphide oxidoreductase; |
15-276 |
2.90e-15 |
|
Pyridine nucleotide-disulphide oxidoreductase;
Pssm-ID: 404603 [Multi-domain] Cd Length: 296 Bit Score: 74.57 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 15 PAGMTAAVYASRANLSTVMI-ERGMPG---------GQMANTEEVENfpGFEMI--------TGPDLSTKMfEHAKkfGA 76
Cdd:pfam13738 1 PAGIGCAIALKKAGLEDYLIlEKGNIGnsfyrypthMTFFSPSFTSN--GFGIPdlnaispgTSPAFTFNR-EHPS--GN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 77 EY-QY---------------GDIKSIEDKGDYKEINLGNKEITARAVIISTGaEYKKIGVPGEQELGgrgVSYCAVCDGA 140
Cdd:pfam13738 76 EYaEYlrrvadhfelpinlfEEVTSVKKEDDGFVVTTSKGTYQARYVIIATG-EFDFPNKLGVPELP---KHYSYVKDFH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 141 FFKNKNLFVIGGGDSAVEEGAFLTKFADKVTIVHRRDELRAQK----------ILQ--DRAFKNDKIDFIWSHTLKSINE 208
Cdd:pfam13738 152 PYAGQKVVVIGGYNSAVDAALELVRKGARVTVLYRGSEWEDRDsdpsyslspdTLNrlEELVKNGKIKAHFNAEVKEITE 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 209 KDGKVgsvtLVSTKDASEQTLDADGVFIyIGMKPLTAPFVNLGI-TNDMGYIV-TEDNMSTKVPGIFAAG 276
Cdd:pfam13738 232 VDVSY----KVHTEDGRKVTSNDDPILA-TGYHPDLSFLKKGLFeLDEDGRPVlTEETESTNVPGLFLAG 296
|
|
| PRK12771 |
PRK12771 |
putative glutamate synthase (NADPH) small subunit; Provisional |
8-302 |
1.75e-14 |
|
putative glutamate synthase (NADPH) small subunit; Provisional
Pssm-ID: 237198 [Multi-domain] Cd Length: 564 Bit Score: 73.76 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 8 VAIIGAGPAGMTAAVYASRANLSTVMIERG-MPGGQManteeveNF--PGFEmitgpdLSTKMFEHakkfgaeyqygDIK 84
Cdd:PRK12771 140 VAVIGGGPAGLSAAYHLRRMGHAVTIFEAGpKLGGMM-------RYgiPAYR------LPREVLDA-----------EIQ 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 85 SIEDKGdyKEINLGNK---EITAR-------AVIISTGAEY-KKIGVPGEQelGGRGVSycAVcdgAFFKN--------- 144
Cdd:PRK12771 196 RILDLG--VEVRLGVRvgeDITLEqlegefdAVFVAIGAQLgKRLPIPGED--AAGVLD--AV---DFLRAvgegeppfl 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 145 -KNLFVIGGGD-------SAVEEGAfltkfaDKVTIVHRR--DELRAQKILQDRAFkNDKIDFIWSHTLKSINEKDGKVG 214
Cdd:PRK12771 267 gKRVVVIGGGNtamdaarTARRLGA------EEVTIVYRRtrEDMPAHDEEIEEAL-REGVEINWLRTPVEIEGDENGAT 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 215 SVTLV-------------STKDASEQTLDADGVFIYIGMKPLTAPFVNL-GITNDMGYIVTEDN-MSTKVPGIFAAGDVR 279
Cdd:PRK12771 340 GLRVItvekmeldedgrpSPVTGEEETLEADLVVLAIGQDIDSAGLESVpGVEVGRGVVQVDPNfMMTGRPGVFAGGDMV 419
|
330 340
....*....|....*....|...
gi 515497732 280 dKGLRQIVTATGDGSIAAQSaID 302
Cdd:PRK12771 420 -PGPRTVTTAIGHGKKAARN-ID 440
|
|
| PRK06116 |
PRK06116 |
glutathione reductase; Validated |
91-281 |
2.31e-14 |
|
glutathione reductase; Validated
Pssm-ID: 235701 [Multi-domain] Cd Length: 450 Bit Score: 73.27 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 91 DYKEINLGNKEITARAVIISTGAEYKKIGVPGEQelggrgvsYCAVCDGAFFKN---KNLFVIGGGDSAVEEGAFLTKFA 167
Cdd:PRK06116 119 DAHTVEVNGERYTADHILIATGGRPSIPDIPGAE--------YGITSDGFFALEelpKRVAVVGAGYIAVEFAGVLNGLG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 168 DKVTIVHRRDE-LRA-----QKILQDrAFKNDKIDFIWSHTLKSInEKDGKvGSVTLvSTKDAseQTLDADGVFIYIGMK 241
Cdd:PRK06116 191 SETHLFVRGDApLRGfdpdiRETLVE-EMEKKGIRLHTNAVPKAV-EKNAD-GSLTL-TLEDG--ETLTVDCLIWAIGRE 264
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 515497732 242 PLTApfvNLGI------TNDMGYIVTEDNMSTKVPGIFAAGDVRDK 281
Cdd:PRK06116 265 PNTD---GLGLenagvkLNEKGYIIVDEYQNTNVPGIYAVGDVTGR 307
|
|
| PRK06327 |
PRK06327 |
dihydrolipoamide dehydrogenase; Validated |
5-278 |
2.41e-14 |
|
dihydrolipoamide dehydrogenase; Validated
Pssm-ID: 235779 [Multi-domain] Cd Length: 475 Bit Score: 73.04 E-value: 2.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 5 NYDVAIIGAGPAGMTAAVYASRANLSTVMIE-------RGMPGGQ------------MANTEEVEN----FPGFEmITGP 61
Cdd:PRK06327 4 QFDVVVIGAGPGGYVAAIRAAQLGLKVACIEawknpkgKPALGGTclnvgcipskalLASSEEFENaghhFADHG-IHVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 62 DLST---KMFEH----AKKF--GAEYQ---------YGDIKSIEDKGDYKEINL---GNKEITARAVIISTGAEYKKI-G 119
Cdd:PRK06327 83 GVKIdvaKMIARkdkvVKKMtgGIEGLfkknkitvlKGRGSFVGKTDAGYEIKVtgeDETVITAKHVIIATGSEPRHLpG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 120 VPGEQELggrgvsycaVCD--GAF-FKN--KNLFVIGGGDSAVEEGAFLTKFADKVTIVHRRDELRA---QKILQD--RA 189
Cdd:PRK06327 163 VPFDNKI---------ILDntGALnFTEvpKKLAVIGAGVIGLELGSVWRRLGAEVTILEALPAFLAaadEQVAKEaaKA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 190 FKNDKIDFiwsHTLKSINE-KDGKVGSVTLVSTKDASEQTLDADGVFIYIGMKPLTApfvNLG------ITNDMGYIVTE 262
Cdd:PRK06327 234 FTKQGLDI---HLGVKIGEiKTGGKGVSVAYTDADGEAQTLEVDKLIVSIGRVPNTD---GLGleavglKLDERGFIPVD 307
|
330
....*....|....*.
gi 515497732 263 DNMSTKVPGIFAAGDV 278
Cdd:PRK06327 308 DHCRTNVPNVYAIGDV 323
|
|
| Pyr_redox |
pfam00070 |
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ... |
146-217 |
7.34e-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: 65.69 E-value: 7.34e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515497732 146 NLFVIGGGDSAVEEGAFLTKFADKVTIVHRRDELR------AQKILQDRAFKNdKIDFIWSHTLKSINEKDGKVGSVT 217
Cdd:pfam00070 1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLLpgfdpeIAKILQEKLEKN-GIEFLLNTTVEAIEGNGDGVVVVL 77
|
|
| PRK12778 |
PRK12778 |
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ... |
8-306 |
1.42e-13 |
|
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;
Pssm-ID: 237200 [Multi-domain] Cd Length: 752 Bit Score: 71.31 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 8 VAIIGAGPAGMTAAV-YASRANLSTVMIERGMPGGQManteeVENFPGFEM---ITGPDLstkmfEHAKKFGAEYQY--- 80
Cdd:PRK12778 434 VAVIGSGPAGLSFAGdLAKRGYDVTVFEALHEIGGVL-----KYGIPEFRLpkkIVDVEI-----ENLKKLGVKFETdvi 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 81 -GDIKSIEDKgdykeinlgnKEITARAVIISTGAEYKK-IGVPGEQELGGRGVS-----------YCAVCDGAFFKNKNL 147
Cdd:PRK12778 504 vGKTITIEEL----------EEEGFKGIFIASGAGLPNfMNIPGENSNGVMSSNeyltrvnlmdaASPDSDTPIKFGKKV 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 148 FVIGGGDSAVEEGAFLTKF-ADKVTIVHRR--DELRAQKILQDRAfKNDKIDFIWSHT-LKSINEKDGKVGSVTLVSTK- 222
Cdd:PRK12778 574 AVVGGGNTAMDSARTAKRLgAERVTIVYRRseEEMPARLEEVKHA-KEEGIEFLTLHNpIEYLADEKGWVKQVVLQKMEl 652
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 223 ---DAS-----------EQTLDADGVFIYIGMKP---LTAPFVNLGItNDMGYIVTEDNMSTKVPGIFAAGDVRdKGLRQ 285
Cdd:PRK12778 653 gepDASgrrrpvaipgsTFTVDVDLVIVSVGVSPnplVPSSIPGLEL-NRKGTIVVDEEMQSSIPGIYAGGDIV-RGGAT 730
|
330 340
....*....|....*....|.
gi 515497732 286 IVTATGDGSIAAQSAIDYIEE 306
Cdd:PRK12778 731 VILAMGDGKRAAAAIDEYLSS 751
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
8-277 |
5.17e-13 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 69.37 E-value: 5.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 8 VAIIGAGPAGMTAAVY-ASRANLSTVMIERGMPGGQMAnteevENFPGF---EMITGPDLstkmfEHAKKFGAEYQYGDI 83
Cdd:PRK12814 196 VAIIGAGPAGLTAAYYlLRKGHDVTIFDANEQAGGMMR-----YGIPRFrlpESVIDADI-----APLRAMGAEFRFNTV 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 84 KSiedkgdyKEINLGNKEITARAVIISTGAEY-KKIGVPGEQELG-GRGVSYCA-VCDG-AFFKNKNLFVIGGGDSAVEe 159
Cdd:PRK12814 266 FG-------RDITLEELQKEFDAVLLAVGAQKaSKMGIPGEELPGvISGIDFLRnVALGtALHPGKKVVVIGGGNTAID- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 160 gAFLTKF---ADKVTIVHRR--DELRAQKILQDRAFKNDKIDFIWSHTLkSINEKDGKVgSVTLVSTK----DAS----- 225
Cdd:PRK12814 338 -AARTALrlgAESVTILYRRtrEEMPANRAEIEEALAEGVSLRELAAPV-SIERSEGGL-ELTAIKMQqgepDESgrrrp 414
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 226 ------EQTLDADGVFIYIGMK--PLTAPFVNLGITNDMGYIVTEDNMSTKVPGIFAAGD 277
Cdd:PRK12814 415 vpvegsEFTLQADTVISAIGQQvdPPIAEAAGIGTSRNGTVKVDPETLQTSVAGVFAGGD 474
|
|
| PRK07251 |
PRK07251 |
FAD-containing oxidoreductase; |
5-278 |
3.11e-12 |
|
FAD-containing oxidoreductase;
Pssm-ID: 180907 [Multi-domain] Cd Length: 438 Bit Score: 66.70 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 5 NYDVAIIGAGPAGMTAAVYASRANLSTVMIERG--MPGGQMANteeVENFPGFEMITGPD------------------LS 64
Cdd:PRK07251 3 TYDLIVIGFGKAGKTLAAKLASAGKKVALVEESkaMYGGTCIN---IGCIPTKTLLVAAEknlsfeqvmatkntvtsrLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 65 TKMFEHAKKFGAEYQYGDIKSIEDKgdYKEINLGN--KEITARAVIISTGAEYKKIGVPGEQELGGrgvsycaVCDGAFF 142
Cdd:PRK07251 80 GKNYAMLAGSGVDLYDAEAHFVSNK--VIEVQAGDekIELTAETIVINTGAVSNVLPIPGLADSKH-------VYDSTGI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 143 KN-----KNLFVIGGGDSAVEEGAFLTKFADKVTIVHRRDEL--RAQKILQDRA---FKNDKIDFIWSHTLKSINEKDGK 212
Cdd:PRK07251 151 QSletlpERLGIIGGGNIGLEFAGLYNKLGSKVTVLDAASTIlpREEPSVAALAkqyMEEDGITFLLNAHTTEVKNDGDQ 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515497732 213 VgsvtLVSTKDaseQTLDADGVFIYIGMKPLTAPfvnLGITN------DMGYIVTEDNMSTKVPGIFAAGDV 278
Cdd:PRK07251 231 V----LVVTED---ETYRFDALLYATGRKPNTEP---LGLENtdieltERGAIKVDDYCQTSVPGVFAVGDV 292
|
|
| PRK12831 |
PRK12831 |
putative oxidoreductase; Provisional |
8-305 |
3.17e-11 |
|
putative oxidoreductase; Provisional
Pssm-ID: 183780 [Multi-domain] Cd Length: 464 Bit Score: 63.50 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 8 VAIIGAGPAGMTAAVY-ASRANLSTVMIERGMPGGQManteeVENFPGFEMitgP--DLSTKMFEHAKKFGAEYQYGDIK 84
Cdd:PRK12831 143 VAVIGSGPAGLTCAGDlAKMGYDVTIFEALHEPGGVL-----VYGIPEFRL---PkeTVVKKEIENIKKLGVKIETNVVV 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 85 SiedkgdyKEINLGN--KEITARAVIISTGAEYKKI-GVPGEQELG-----------GRGVSYCAVCDGAFFKNKNLFVI 150
Cdd:PRK12831 215 G-------KTVTIDEllEEEGFDAVFIGSGAGLPKFmGIPGENLNGvfsanefltrvNLMKAYKPEYDTPIKVGKKVAVV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 151 GGGDSAVEEGAFLTKFADKVTIVHRR--DELRAQKILQDRAfKNDKIDFIW-SHTLKSINEKDGKVGSVTLVSTK----D 223
Cdd:PRK12831 288 GGGNVAMDAARTALRLGAEVHIVYRRseEELPARVEEVHHA-KEEGVIFDLlTNPVEILGDENGWVKGMKCIKMElgepD 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 224 AS-----------EQTLDADGVFIYIGMKP---LTAPFVNLGItNDMGYIVT-EDNMSTKVPGIFAAGD-VRdkGLRQIV 287
Cdd:PRK12831 367 ASgrrrpveiegsEFVLEVDTVIMSLGTSPnplISSTTKGLKI-NKRGCIVAdEETGLTSKEGVFAGGDaVT--GAATVI 443
|
330
....*....|....*...
gi 515497732 288 TATGDGSIAAQSAIDYIE 305
Cdd:PRK12831 444 LAMGAGKKAAKAIDEYLS 461
|
|
| NirB |
COG1251 |
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion]; |
7-278 |
6.84e-11 |
|
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
Pssm-ID: 440863 [Multi-domain] Cd Length: 402 Bit Score: 62.47 E-value: 6.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 7 DVAIIGAGPAGMTAA---------------------VYaSRANLSTVMiergmpGGQMAnteevenfpgFEMITGPDLst 65
Cdd:COG1251 3 RIVIIGAGMAGVRAAeelrkldpdgeitvigaephpPY-NRPPLSKVL------AGETD----------EEDLLLRPA-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 66 kmfEHAKKFGAEYQYGD-IKSIEDKGdyKEINLGN-KEITARAVIISTGAEYKKIGVPGeQELGG----RGVSYCAVCDG 139
Cdd:COG1251 64 ---DFYEENGIDLRLGTrVTAIDRAA--RTVTLADgETLPYDKLVLATGSRPRVPPIPG-ADLPGvftlRTLDDADALRA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 140 AFFKNKNLFVIGGG-------DSAVEEGAfltkfadKVTIVHRRDEL-------RAQKILQdRAFKNDKIDFIWSHTLKS 205
Cdd:COG1251 138 ALAPGKRVVVIGGGligleaaAALRKRGL-------EVTVVERAPRLlprqldeEAGALLQ-RLLEALGVEVRLGTGVTE 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515497732 206 InEKDGKVGSVTLvstkdASEQTLDADGVFIYIGMKPLTAPFVNLGITNDMGyIVTEDNMSTKVPGIFAAGDV 278
Cdd:COG1251 210 I-EGDDRVTGVRL-----ADGEELPADLVVVAIGVRPNTELARAAGLAVDRG-IVVDDYLRTSDPDIYAAGDC 275
|
|
| PRK08010 |
PRK08010 |
pyridine nucleotide-disulfide oxidoreductase; Provisional |
6-278 |
2.64e-10 |
|
pyridine nucleotide-disulfide oxidoreductase; Provisional
Pssm-ID: 181196 [Multi-domain] Cd Length: 441 Bit Score: 60.80 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 6 YDVAIIGAGPAGMTAAVYASRANLSTVMIER--GMPGGQMAN---------TEEVENFPGFEMITGPDLSTKMFEHAKKF 74
Cdd:PRK08010 4 YQAVIIGFGKAGKTLAVTLAKAGWRVALIEQsnAMYGGTCINigciptktlVHDAQQHTDFVRAIQRKNEVVNFLRNKNF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 75 GAEYQYGDIKSIEDKGDYKEINL-------GNKEITARAVIISTGAEYKKIGVPGEQELGGrgvsycaVCDGAFFKN--- 144
Cdd:PRK08010 84 HNLADMPNIDVIDGQAEFINNHSlrvhrpeGNLEIHGEKIFINTGAQTVVPPIPGITTTPG-------VYDSTGLLNlke 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 145 --KNLFVIGGGDSAVEEGAFLTKFADKVTIVH-------RRDELRAQKILqdRAFKNDKIDFIWSHTLKSINEKDGKVGs 215
Cdd:PRK08010 157 lpGHLGILGGGYIGVEFASMFANFGSKVTILEaaslflpREDRDIADNIA--TILRDQGVDIILNAHVERISHHENQVQ- 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515497732 216 vtlVSTKDASeqtLDADGVFIYIGMKPLTAPF--VNLGI-TNDMGYIVTEDNMSTKVPGIFAAGDV 278
Cdd:PRK08010 234 ---VHSEHAQ---LAVDALLIASGRQPATASLhpENAGIaVNERGAIVVDKYLHTTADNIWAMGDV 293
|
|
| TGR |
TIGR01438 |
thioredoxin and glutathione reductase selenoprotein; This homodimeric, FAD-containing member ... |
5-298 |
1.38e-09 |
|
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: 58.71 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 5 NYDVAIIGAGPAGMTAAVYASRANLSTVMIERGMP---------GGQMANteeVENFPGFEMITGPDLStKMFEHAKKFG 75
Cdd:TIGR01438 2 DYDLIVIGGGSGGLAAAKEAAAYGAKVMLLDFVTPtplgtrwgiGGTCVN---VGCIPKKLMHQAALLG-QALKDSRNYG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 76 --------------AEYQYGDIKSI---------EDKGDYKE--------------INLGNKEI-TARAVIISTGAEYKK 117
Cdd:TIGR01438 78 wkveetvkhdwkrlVEAVQNHIGSLnwgyrvalrEKKVKYENayaefvdkhrikatNKKGKEKIySAERFLIATGERPRY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 118 IGVPGEQElggrgvsYCAVCDGAF----FKNKNLfVIGGGDSAVEEGAFLTKFADKVTIVHRRDELRAQkilqDRAFKND 193
Cdd:TIGR01438 158 PGIPGAKE-------LCITSDDLFslpyCPGKTL-VVGASYVALECAGFLAGIGLDVTVMVRSILLRGF----DQDCANK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 194 KIDFIWSHTLKSIN----EKDGKVGSVTLVSTKDASEQTLDA-DGVFIYIGMKPLTAPF----VNLGITNDMGYIVTEDN 264
Cdd:TIGR01438 226 VGEHMEEHGVKFKRqfvpIKVEQIEAKVLVEFTDSTNGIEEEyDTVLLAIGRDACTRKLnlenVGVKINKKTGKIPADEE 305
|
330 340 350
....*....|....*....|....*....|....
gi 515497732 265 MSTKVPGIFAAGDVRDKGLRQIVTATGDGSIAAQ 298
Cdd:TIGR01438 306 EQTNVPYIYAVGDILEDKPELTPVAIQAGRLLAQ 339
|
|
| GG-red-SF |
TIGR02032 |
geranylgeranyl reductase family; This model represents a subfamily which includes ... |
6-187 |
2.28e-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: 57.33 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 6 YDVAIIGAGPAGMTAAVYASRANLSTVMIERG-------------------------------------MPGGQMANTEE 48
Cdd:TIGR02032 1 YDVVVVGAGPAGASAAYRLADKGLRVLLLEKKsfprykpcggalspraleeldlpgelivnlvrgarffSPNGDSVEIPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 49 vENFPGFeMITGPDLSTKMFEHAKKFGAEYQYGD-IKSIEDKGDYKEINL--GNKEITARAVIISTGAEY---KKIGVPG 122
Cdd:TIGR02032 81 -ETELAY-VIDRDAFDEQLAERAQEAGAELRLGTrVLDVEIHDDRVVVIVrgSEGTVTAKIVIGADGSRSivaKKLGLKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 123 EQ-ELGGRGVSYCAV----CDGAF---FKNKNL------FVIGGGDSAVEEGAFLTKFADKVTIVHRRDE-LRAQKILQD 187
Cdd:TIGR02032 159 EPrEYGVAARAEVEMpdeeVDEDFvevYIDRGIvpggygWVFPKGDGTANVGVGSRSAEEGEDPKKYLKDfLARRPELKD 238
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
8-306 |
6.27e-09 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 56.96 E-value: 6.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 8 VAIIGAGPAGMTAAVYASRANLSTVMIERGMPGGQMANTeeveNFPGFEMITG-----PDLSTKM---FEHAKKFGAEYQ 79
Cdd:PRK12809 313 VAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTF----GIPPFKLDKTvlsqrREIFTAMgidFHLNCEIGRDIT 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 80 YGDIKSIEDK-----GDYKEINLGNKEITARAVIIS----TGAEYKKIGVPGEQELGGRGVsycavcdgaffKNKNLFVI 150
Cdd:PRK12809 389 FSDLTSEYDAvfigvGTYGMMRADLPHEDAPGVIQAlpflTAHTRQLMGLPESEEYPLTDV-----------EGKRVVVL 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 151 GGGDSAVE-EGAFLTKFADKVTIVHRRDELRA----QKILQDRafkNDKIDFIWSHTLKSI-NEKDGKVGSVTLVSTK-- 222
Cdd:PRK12809 458 GGGDTTMDcLRTSIRLNAASVTCAYRRDEVSMpgsrKEVVNAR---EEGVEFQFNVQPQYIaCDEDGRLTAVGLIRTAmg 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 223 -------------DASEQTLDADGVFIYIGMKPLTAPFVN-LGI---------TNDMGYIVTEdnmsTKVPGIFAAGDVR 279
Cdd:PRK12809 535 epgpdgrrrprpvAGSEFELPADVLIMAFGFQAHAMPWLQgSGIkldkwgliqTGDVGYLPTQ----THLKKVFAGGDAV 610
|
330 340
....*....|....*....|....*..
gi 515497732 280 dKGLRQIVTATGDGSIAAQSAIDYIEE 306
Cdd:PRK12809 611 -HGADLVVTAMAAGRQAARDMLTLFDT 636
|
|
| Ndh |
COG1252 |
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion]; |
7-278 |
1.09e-08 |
|
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
Pssm-ID: 440864 [Multi-domain] Cd Length: 386 Bit Score: 55.91 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 7 DVAIIGAGPAGMTAAVYASR---ANLSTVMIER-----------GMPGGQMaNTEEVEnfpgfemitgPDLStkmfEHAK 72
Cdd:COG1252 3 RIVIVGGGFAGLEAARRLRKklgGDAEVTLIDPnpyhlfqpllpEVAAGTL-SPDDIA----------IPLR----ELLR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 73 KFGAEYQYGDIKSIEDKGdyKEINLGN-KEITARAVIISTGAEYKKIGVPGEQElggRGVSYCAVCDGAFFKNK------ 145
Cdd:COG1252 68 RAGVRFIQGEVTGIDPEA--RTVTLADgRTLSYDYLVIATGSVTNFFGIPGLAE---HALPLKTLEDALALRERllaafe 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 146 --------NLFVIGGGDSAVEeGAF--------LTKFAD------KVTIVHRRDEL----------RAQKILQDRafknd 193
Cdd:COG1252 143 raerrrllTIVVVGGGPTGVE-LAGelaellrkLLRYPGidpdkvRITLVEAGPRIlpglgeklseAAEKELEKR----- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 194 KIDFIWSHTLKSINEkdgkvGSVTLvstkdASEQTLDADGVFIYIGMKPltAPFV-NLGI-TNDMGYIVTEDNM-STKVP 270
Cdd:COG1252 217 GVEVHTGTRVTEVDA-----DGVTL-----EDGEEIPADTVIWAAGVKA--PPLLaDLGLpTDRRGRVLVDPTLqVPGHP 284
|
....*...
gi 515497732 271 GIFAAGDV 278
Cdd:COG1252 285 NVFAIGDC 292
|
|
| PRK05249 |
PRK05249 |
Si-specific NAD(P)(+) transhydrogenase; |
1-278 |
1.11e-08 |
|
Si-specific NAD(P)(+) transhydrogenase;
Pssm-ID: 235373 [Multi-domain] Cd Length: 461 Bit Score: 55.93 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 1 MTEINYDVAIIGAGPAGMTAAVYASRANLSTVMIERG-MPGGQMANT---------EEVENFPGF------------EMI 58
Cdd:PRK05249 1 MHMYDYDLVVIGSGPAGEGAAMQAAKLGKRVAVIERYrNVGGGCTHTgtipskalrEAVLRLIGFnqnplyssyrvkLRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 59 TGPDLS----------TKMFEHAkkfgaeYQYGDIKSIEDKG---DYKEINL----GNKE-ITARAVIISTGAE-YKKIG 119
Cdd:PRK05249 81 TFADLLaradhvinkqVEVRRGQ------YERNRVDLIQGRArfvDPHTVEVecpdGEVEtLTADKIVIATGSRpYRPPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 120 VPgeqelggrgvsycavcdgafFKNKNLF----------------VIGGGDSAVEEGAFLTKFADKVTIVHRRDELRA-- 181
Cdd:PRK05249 155 VD--------------------FDHPRIYdsdsilsldhlprsliIYGAGVIGCEYASIFAALGVKVTLINTRDRLLSfl 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 182 -QKILQD--RAFKNDKIDFIWSHTLKSINEKDGKVgSVTLvstkdASEQTLDADGVFIYIGMKPLTApfvNLGI------ 252
Cdd:PRK05249 215 dDEISDAlsYHLRDSGVTIRHNEEVEKVEGGDDGV-IVHL-----KSGKKIKADCLLYANGRTGNTD---GLNLenagle 285
|
330 340
....*....|....*....|....*.
gi 515497732 253 TNDMGYIVTEDNMSTKVPGIFAAGDV 278
Cdd:PRK05249 286 ADSRGQLKVNENYQTAVPHIYAVGDV 311
|
|
| COG1233 |
COG1233 |
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ... |
5-61 |
1.53e-08 |
|
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440846 [Multi-domain] Cd Length: 491 Bit Score: 55.63 E-value: 1.53e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 515497732 5 NYDVAIIGAGPAGMTAAVYASRANLSTVMIER-GMPGGqMANTEEvenFPGFEMITGP 61
Cdd:COG1233 3 MYDVVVIGAGIGGLAAAALLARAGYRVTVLEKnDTPGG-RARTFE---RPGFRFDVGP 56
|
|
| TIGR00275 |
TIGR00275 |
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ... |
9-127 |
1.59e-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: 55.29 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 9 AIIGAGPAGMTAAVYASRANLSTVMIERG--------MPGGQMAN-------TEEVENFPG------------------- 54
Cdd:TIGR00275 1 IIIGGGAAGLMAAITAARAGLSVLLLEKNkkigkkllISGGGRCNltnscptPEFVAYYPRngkflrsalsrfsnkdlid 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 55 -FEMItGPDLST----KMF--------------EHAKKFGAEYQYG-DIKSIEDKGDYKEINLGNKEITARAVIISTG-A 113
Cdd:TIGR00275 81 fFESL-GLELKVeedgRVFpcsdsaadvldallNELKELGVEILTNsKVKSIEKEDGGFGVETSGGEYEADKVIIATGgL 159
|
170
....*....|....*....
gi 515497732 114 EYKKIGVPGE-----QELG 127
Cdd:TIGR00275 160 SYPQLGSTGDgyeiaESLG 178
|
|
| PRK12775 |
PRK12775 |
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ... |
8-304 |
3.37e-08 |
|
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional
Pssm-ID: 183738 [Multi-domain] Cd Length: 1006 Bit Score: 54.95 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 8 VAIIGAGPAGMTAAVYASRANLSTVMIER----------GMPGGQMAnteevENFPGFEMITGPDLSTKmFEHAKKFGAE 77
Cdd:PRK12775 433 VAICGSGPAGLAAAADLVKYGVDVTVYEAlhvvggvlqyGIPSFRLP-----RDIIDREVQRLVDIGVK-IETNKVIGKT 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 78 YQYGDIksIEDKGdykeinlgnkeitARAVIISTGAEYKK-IGVPGE---------------QELGGRGVSYCavcDGAF 141
Cdd:PRK12775 507 FTVPQL--MNDKG-------------FDAVFLGVGAGAPTfLGIPGEfagqvysanefltrvNLMGGDKFPFL---DTPI 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 142 FKNKNLFVIGGGDSAVEEGAFLTKF-ADKVTIVHRRDELRA-QKILQDRAFKNDKIDFIWSHT-LKSINEKDGKVGSVTL 218
Cdd:PRK12775 569 SLGKSVVVIGAGNTAMDCLRVAKRLgAPTVRCVYRRSEAEApARIEEIRHAKEEGIDFFFLHSpVEIYVDAEGSVRGMKV 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 219 --VSTKDASEQ------------TLDADGVFIYIGMKP---LTAPFVNLGItNDMGYIVTEDNM-----STKVPGIFAAG 276
Cdd:PRK12775 649 eeMELGEPDEKgrrkpmptgefkDLECDTVIYALGTKAnpiITQSTPGLAL-NKWGNIAADDGKlestqSTNLPGVFAGG 727
|
330 340
....*....|....*....|....*...
gi 515497732 277 DVRDKGlRQIVTATGDGSIAAQSAIDYI 304
Cdd:PRK12775 728 DIVTGG-ATVILAMGAGRRAARSIATYL 754
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
145-304 |
3.87e-08 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 54.37 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 145 KNLFVIGGGDSAVE-EGAFLTKFADKVTIVHRRDElrAQKILQDRAFKNDK---IDFIWS-HTLKSINEKDGKVGSVTLV 219
Cdd:PRK12769 469 LNVVVLGGGDTAMDcVRTALRHGASNVTCAYRRDE--ANMPGSKKEVKNAReegANFEFNvQPVALELNEQGHVCGIRFL 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 220 STK----DA-----------SEQTLDADGVFIYIGMKPLTAPFV-NLGI-TNDMGYIVTEDN----MSTKVPGIFAAGD- 277
Cdd:PRK12769 547 RTRlgepDAqgrrrpvpipgSEFVMPADAVIMAFGFNPHGMPWLeSHGVtVDKWGRIIADVEsqyrYQTSNPKIFAGGDa 626
|
170 180
....*....|....*....|....*..
gi 515497732 278 VRDKGLrqIVTATGDGSIAAQSAIDYI 304
Cdd:PRK12769 627 VRGADL--VVTAMAEGRHAAQGIIDWL 651
|
|
| PRK13748 |
PRK13748 |
putative mercuric reductase; Provisional |
8-297 |
4.06e-08 |
|
putative mercuric reductase; Provisional
Pssm-ID: 184298 [Multi-domain] Cd Length: 561 Bit Score: 54.39 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 8 VAIIGAGPAGMTAAVYASRANLSTVMIERGMPGGQMANTEEVenfPGFEMI--------------------TGPDLS-TK 66
Cdd:PRK13748 101 VAVIGSGGAAMAAALKAVEQGARVTLIERGTIGGTCVNVGCV---PSKIMIraahiahlrrespfdggiaaTVPTIDrSR 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 67 MFE----------HAKKFGAEYQYGDIKSIEDKGDYKEINL--------GNKEITARAVIISTGAEYKKIGVPGEQElgg 128
Cdd:PRK13748 178 LLAqqqarvdelrHAKYEGILDGNPAITVLHGEARFKDDQTlivrlndgGERVVAFDRCLIATGASPAVPPIPGLKE--- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 129 rgVSYCAVCDGAFFKN--KNLFVIGGGDSAVEEGAFLTKFADKVTIVHRR------DELRAQKILQdrAFKNDKIDfIWS 200
Cdd:PRK13748 255 --TPYWTSTEALVSDTipERLAVIGSSVVALELAQAFARLGSKVTILARStlffreDPAIGEAVTA--AFRAEGIE-VLE 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 201 HTLKS-INEKDGKvgsvtLVSTKDASEqtLDADGVFIYIGMKPLTAPfVNL---GIT-NDMGYIVTEDNMSTKVPGIFAA 275
Cdd:PRK13748 330 HTQASqVAHVDGE-----FVLTTGHGE--LRADKLLVATGRAPNTRS-LALdaaGVTvNAQGAIVIDQGMRTSVPHIYAA 401
|
330 340
....*....|....*....|...
gi 515497732 276 GDVRDKglRQIV-TATGDGSIAA 297
Cdd:PRK13748 402 GDCTDQ--PQFVyVAAAAGTRAA 422
|
|
| PTZ00058 |
PTZ00058 |
glutathione reductase; Provisional |
3-277 |
7.27e-08 |
|
glutathione reductase; Provisional
Pssm-ID: 185420 [Multi-domain] Cd Length: 561 Bit Score: 53.47 E-value: 7.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 3 EINYDVAIIGAGPAGMTAAVYASRANLSTVMIERGMPGGQMAN----------------------------TEEVENFPG 54
Cdd:PTZ00058 46 RMVYDLIVIGGGSGGMAAARRAARNKAKVALVEKDYLGGTCVNvgcvpkkimfnaasihdilensrhygfdTQFSFNLPL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 55 F-----EMITG---------PDLSTKMFEHAKKFGAEYQYGDIKSIEDKGDYKEINlgNKEITARAVIISTGAEYKK--- 117
Cdd:PTZ00058 126 LverrdKYIRRlndiyrqnlKKDNVEYFEGKGSLLSENQVLIKKVSQVDGEADESD--DDEVTIVSAGVSQLDDGQVieg 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 118 ----IGVPGEQELGG-RGVSYCAVCDGaFFK---NKNLFVIGGGDSAVEEGAFLTKFADKVTIVHRR-------DELRAQ 182
Cdd:PTZ00058 204 knilIAVGNKPIFPDvKGKEFTISSDD-FFKikeAKRIGIAGSGYIAVELINVVNRLGAESYIFARGnrllrkfDETIIN 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 183 KILQDraFKNDKIDFIWSHTLKSInEKDGKVGSVTLVSTKDASEQtldADGVFIYIGMKPLTAPfVNLGITNDM---GYI 259
Cdd:PTZ00058 283 ELEND--MKKNNINIITHANVEEI-EKVKEKNLTIYLSDGRKYEH---FDYVIYCVGRSPNTED-LNLKALNIKtpkGYI 355
|
330
....*....|....*...
gi 515497732 260 VTEDNMSTKVPGIFAAGD 277
Cdd:PTZ00058 356 KVDDNQRTSVKHIYAVGD 373
|
|
| FAD_oxidored |
pfam12831 |
FAD dependent oxidoreductase; This family of proteins contains FAD dependent oxidoreductases ... |
7-43 |
8.18e-08 |
|
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: 8.18e-08
10 20 30
....*....|....*....|....*....|....*...
gi 515497732 7 DVAIIGAGPAGMTAAVYASRANLSTVMIE-RGMPGGQM 43
Cdd:pfam12831 1 DVVVVGGGPAGVAAAIAAARAGAKVLLVErRGFLGGML 38
|
|
| trypano_reduc |
TIGR01423 |
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ... |
6-281 |
1.12e-06 |
|
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.
Pssm-ID: 200098 [Multi-domain] Cd Length: 486 Bit Score: 49.97 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 6 YDVAIIGAGPAGM-----TAAVYASRANLSTVMIERGMP-----GGQMANteeVENFPGFEMITGPDLSTKMFEHAKkFG 75
Cdd:TIGR01423 4 FDLVVIGAGSGGLeagwnAATLYKKRVAVVDVQTHHGPPfyaalGGTCVN---VGCVPKKLMVTGAQYMDTLRESAG-FG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 76 AEYQYGDIK--------------------------------------SIEDKG-----DYKEINLGNKE-ITARAVIIST 111
Cdd:TIGR01423 80 WEFDRSSVKanwkaliaaknkavldinksyegmfadtegltfflgwgALEDKNvvlvrESADPKSAVKErLQAEHILLAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 112 GAEYKKIGVPGeqelggrgVSYCAVCDGAFFKN---KNLFVIGGGDSAVEEGAFLTKF---ADKVTIVHRRD-------- 177
Cdd:TIGR01423 160 GSWPQMLGIPG--------IEHCISSNEAFYLDeppRRVLTVGGGFISVEFAGIFNAYkprGGKVTLCYRNNmilrgfds 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 178 ELRAQKILQDRAfknDKIDFIWSHTLKSINEKDGKVGSVTLVSTKdaseqTLDADGVFIYIGMKPLTAPFV--NLGIT-N 254
Cdd:TIGR01423 232 TLRKELTKQLRA---NGINIMTNENPAKVTLNADGSKHVTFESGK-----TLDVDVVMMAIGRVPRTQTLQldKVGVElT 303
|
330 340
....*....|....*....|....*..
gi 515497732 255 DMGYIVTEDNMSTKVPGIFAAGDVRDK 281
Cdd:TIGR01423 304 KKGAIQVDEFSRTNVPNIYAIGDVTDR 330
|
|
| COG2509 |
COG2509 |
FAD-dependent dehydrogenase [General function prediction only]; |
5-37 |
1.55e-06 |
|
FAD-dependent dehydrogenase [General function prediction only];
Pssm-ID: 441999 [Multi-domain] Cd Length: 466 Bit Score: 49.34 E-value: 1.55e-06
10 20 30
....*....|....*....|....*....|...
gi 515497732 5 NYDVAIIGAGPAGMTAAVYASRANLSTVMIERG 37
Cdd:COG2509 30 KYDVVIVGAGPAGLFAALELAEAGLKPLVLERG 62
|
|
| HemY |
COG1232 |
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ... |
6-62 |
1.68e-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: 49.06 E-value: 1.68e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 515497732 6 YDVAIIGAGPAGMTAAVYASRANLSTVMIERG-MPGGQMAnTEEVENFPgFEmiTGPD 62
Cdd:COG1232 2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASdRVGGLIR-TVEVDGFR-ID--RGPH 55
|
|
| PRK07843 |
PRK07843 |
3-oxosteroid 1-dehydrogenase; |
1-36 |
1.70e-06 |
|
3-oxosteroid 1-dehydrogenase;
Pssm-ID: 236111 [Multi-domain] Cd Length: 557 Bit Score: 49.26 E-value: 1.70e-06
10 20 30
....*....|....*....|....*....|....*.
gi 515497732 1 MTEINYDVAIIGAGPAGMTAAVYASRANLSTVMIER 36
Cdd:PRK07843 3 MTVQEYDVVVVGSGAAGMVAALTAAHRGLSTVVVEK 38
|
|
| SdhA |
COG1053 |
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ... |
3-41 |
1.74e-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: 49.06 E-value: 1.74e-06
10 20 30
....*....|....*....|....*....|....*....
gi 515497732 3 EINYDVAIIGAGPAGMTAAVYASRANLSTVMIERGMPGG 41
Cdd:COG1053 1 DHEYDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRG 39
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
3-114 |
1.90e-06 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 49.09 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 3 EINYDVAIIGAGPAGMTAAVYASRANLSTVMIER-GMPGGQMANTEEVenFPGFEmiTGPDLSTKMFEHAKKF------- 74
Cdd:COG1148 138 PVNKRALVIGGGIAGMTAALELAEQGYEVYLVEKePELGGRAAQLHKT--FPGLD--CPQCILEPLIAEVEANpnitvyt 213
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 515497732 75 GAEyqygdIKSIE-DKGDYK-EINLGNK---EITARAVIISTGAE 114
Cdd:COG1148 214 GAE-----VEEVSgYVGNFTvTIKKGPReeiEIEVGAIVLATGFK 253
|
|
| DadA |
COG0665 |
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism]; |
4-41 |
2.01e-06 |
|
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
Pssm-ID: 440429 [Multi-domain] Cd Length: 364 Bit Score: 48.75 E-value: 2.01e-06
10 20 30
....*....|....*....|....*....|....*...
gi 515497732 4 INYDVAIIGAGPAGMTAAVYASRANLSTVMIERGMPGG 41
Cdd:COG0665 1 ATADVVVIGGGIAGLSTAYHLARRGLDVTVLERGRPGS 38
|
|
| CzcO |
COG2072 |
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ... |
6-176 |
3.34e-06 |
|
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: 48.32 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 6 YDVAIIGAGPAGMTAAVYASRANLSTVMIERG-MPGG--------------QMANTEevenFPGFEMITG-PDLSTK--- 66
Cdd:COG2072 7 VDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKAdDVGGtwrdnrypglrldtPSHLYS----LPFFPNWSDdPDFPTGdei 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 67 --MFEH-AKKFGAE--YQYG-DIKSI---EDKGDYkEINLGN-KEITARAVIISTGAEYKKI--GVPGEQELGGRGVSYC 134
Cdd:COG2072 83 laYLEAyADKFGLRrpIRFGtEVTSArwdEADGRW-TVTTDDgETLTARFVVVATGPLSRPKipDIPGLEDFAGEQLHSA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 515497732 135 AVCDGAFFKNKNLFVIGGGDSAVEEGAFLTKFADKVTIVHRR 176
Cdd:COG2072 162 DWRNPVDLAGKRVLVVGTGASAVQIAPELARVAAHVTVFQRT 203
|
|
| UbiH |
COG0654 |
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ... |
5-36 |
3.81e-06 |
|
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: 47.63 E-value: 3.81e-06
10 20 30
....*....|....*....|....*....|..
gi 515497732 5 NYDVAIIGAGPAGMTAAVYASRANLSTVMIER 36
Cdd:COG0654 3 RTDVLIVGGGPAGLALALALARAGIRVTVVER 34
|
|
| HI0933_like |
pfam03486 |
HI0933-like protein; |
6-37 |
3.98e-06 |
|
HI0933-like protein;
Pssm-ID: 427330 [Multi-domain] Cd Length: 406 Bit Score: 47.96 E-value: 3.98e-06
10 20 30
....*....|....*....|....*....|..
gi 515497732 6 YDVAIIGAGPAGMTAAVYASRANLSTVMIERG 37
Cdd:pfam03486 1 FDVIVIGGGAAGLMAAISAAKRGRRVLLIEKG 32
|
|
| PRK05329 |
PRK05329 |
glycerol-3-phosphate dehydrogenase subunit GlpB; |
4-38 |
6.61e-06 |
|
glycerol-3-phosphate dehydrogenase subunit GlpB;
Pssm-ID: 235412 Cd Length: 422 Bit Score: 47.15 E-value: 6.61e-06
10 20 30
....*....|....*....|....*....|....*
gi 515497732 4 INYDVAIIGAGPAGMTAAVYASRANLSTVMIERGM 38
Cdd:PRK05329 1 MKFDVLVIGGGLAGLTAALAAAEAGKRVALVAKGQ 35
|
|
| GlpB |
COG3075 |
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism]; |
4-38 |
1.39e-05 |
|
Anaerobic glycerol-3-phosphate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 442309 Cd Length: 415 Bit Score: 46.33 E-value: 1.39e-05
10 20 30
....*....|....*....|....*....|....*
gi 515497732 4 INYDVAIIGAGPAGMTAAVYASRANLSTVMIERGM 38
Cdd:COG3075 1 MKFDVVVIGGGLAGLTAAIRAAEAGLRVAIVSAGQ 35
|
|
| FAD_binding_2 |
pfam00890 |
FAD binding domain; This family includes members that bind FAD. This family includes the ... |
7-37 |
2.53e-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: 45.36 E-value: 2.53e-05
10 20 30
....*....|....*....|....*....|.
gi 515497732 7 DVAIIGAGPAGMTAAVYASRANLSTVMIERG 37
Cdd:pfam00890 1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKG 31
|
|
| solA |
PRK11259 |
N-methyl-L-tryptophan oxidase; |
6-43 |
3.43e-05 |
|
N-methyl-L-tryptophan oxidase;
Pssm-ID: 236887 [Multi-domain] Cd Length: 376 Bit Score: 44.83 E-value: 3.43e-05
10 20 30
....*....|....*....|....*....|....*...
gi 515497732 6 YDVAIIGAGPAGMTAAVYASRANLSTVMIERGMPGGQM 43
Cdd:PRK11259 4 YDVIVIGLGSMGSAAGYYLARRGLRVLGLDRFMPPHQQ 41
|
|
| NAD_binding_8 |
pfam13450 |
NAD(P)-binding Rossmann-like domain; |
10-53 |
4.13e-05 |
|
NAD(P)-binding Rossmann-like domain;
Pssm-ID: 433218 [Multi-domain] Cd Length: 67 Bit Score: 40.98 E-value: 4.13e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 515497732 10 IIGAGPAGMTAAVYASRANLSTVMIERG-MPGGQMAnTEEVENFP 53
Cdd:pfam13450 1 IVGAGLAGLVAAALLAKRGFRVLVLEKRdRLGGNAY-SYRVPGYV 44
|
|
| DAO |
pfam01266 |
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ... |
7-42 |
4.45e-05 |
|
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: 44.70 E-value: 4.45e-05
10 20 30
....*....|....*....|....*....|....*.
gi 515497732 7 DVAIIGAGPAGMTAAVYASRANLSTVMIERGMPGGQ 42
Cdd:pfam01266 1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGS 36
|
|
| FAD_binding_3 |
pfam01494 |
FAD binding domain; This domain is involved in FAD binding in a number of enzymes. |
6-36 |
5.75e-05 |
|
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: 44.24 E-value: 5.75e-05
10 20 30
....*....|....*....|....*....|.
gi 515497732 6 YDVAIIGAGPAGMTAAVYASRANLSTVMIER 36
Cdd:pfam01494 2 TDVLIVGGGPAGLMLALLLARAGVRVVLVER 32
|
|
| mhpA |
PRK06183 |
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase; |
3-36 |
6.77e-05 |
|
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
Pssm-ID: 235727 [Multi-domain] Cd Length: 500 Bit Score: 44.13 E-value: 6.77e-05
10 20 30
....*....|....*....|....*....|....
gi 515497732 3 EINYDVAIIGAGPAGMTAAVYASRANLSTVMIER 36
Cdd:PRK06183 8 AHDTDVVIVGAGPVGLTLANLLGQYGVRVLVLER 41
|
|
| PRK12843 |
PRK12843 |
FAD-dependent oxidoreductase; |
6-36 |
7.23e-05 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 237225 [Multi-domain] Cd Length: 578 Bit Score: 44.34 E-value: 7.23e-05
10 20 30
....*....|....*....|....*....|.
gi 515497732 6 YDVAIIGAGPAGMTAAVYASRANLSTVMIER 36
Cdd:PRK12843 17 FDVIVIGAGAAGMSAALFAAIAGLKVLLVER 47
|
|
| PRK07494 |
PRK07494 |
UbiH/UbiF family hydroxylase; |
1-39 |
8.61e-05 |
|
UbiH/UbiF family hydroxylase;
Pssm-ID: 181001 [Multi-domain] Cd Length: 388 Bit Score: 43.74 E-value: 8.61e-05
10 20 30
....*....|....*....|....*....|....*....
gi 515497732 1 MTEINYDVAIIGAGPAGMTAAVYASRANLSTVMIERGMP 39
Cdd:PRK07494 3 MEKEHTDIAVIGGGPAGLAAAIALARAGASVALVAPEPP 41
|
|
| YhiN |
COG2081 |
Predicted flavoprotein YhiN [General function prediction only]; |
9-119 |
9.23e-05 |
|
Predicted flavoprotein YhiN [General function prediction only];
Pssm-ID: 441684 [Multi-domain] Cd Length: 402 Bit Score: 43.50 E-value: 9.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 9 AIIGAGPAGMTAAVYASRANLSTVMIERgMP----------GGQM--ANTEEVENF-------PGF-------------- 55
Cdd:COG2081 1 IVIGAGAAGLMAAITAAERGARVLLLEK-NPkvgrkilisgGGRCnfTNSEPLPEFlnyyggnPHFlksalsrftpedli 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 56 EMITGPDLSTK-------------------MFEH-AKKFGAEYQYG-DIKSIEDKGDYKEINLGN-KEITARAVIISTG- 112
Cdd:COG2081 80 AFFEGLGIETKeessgrvfpdsskasdilrALLAeLREAGVEIRLRtRVTGIEKEDGGFGVETPDgETVRADAVVLATGg 159
|
....*..
gi 515497732 113 AEYKKIG 119
Cdd:COG2081 160 LSYPKLG 166
|
|
| YobN |
COG1231 |
Monoamine oxidase [Amino acid transport and metabolism]; |
6-41 |
1.82e-04 |
|
Monoamine oxidase [Amino acid transport and metabolism];
Pssm-ID: 440844 [Multi-domain] Cd Length: 440 Bit Score: 42.99 E-value: 1.82e-04
10 20 30
....*....|....*....|....*....|....*..
gi 515497732 6 YDVAIIGAGPAGMTAAVYASRANLSTVMIE-RGMPGG 41
Cdd:COG1231 8 KDVVIVGAGLAGLAAARELRKAGLDVTVLEaRDRVGG 44
|
|
| Thi4 |
pfam01946 |
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme. |
7-43 |
2.02e-04 |
|
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
Pssm-ID: 460393 Cd Length: 232 Bit Score: 42.07 E-value: 2.02e-04
10 20 30
....*....|....*....|....*....|....*....
gi 515497732 7 DVAIIGAGPAGMTAAVY-ASRANLSTVMIERGM-PGGQM 43
Cdd:pfam01946 19 DVVIVGAGSSGLTAAYYlAKNRGLKVAIIERSVsPGGGA 57
|
|
| COG3380 |
COG3380 |
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only]; |
7-44 |
2.05e-04 |
|
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
Pssm-ID: 442607 [Multi-domain] Cd Length: 331 Bit Score: 42.56 E-value: 2.05e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 515497732 7 DVAIIGAGPAGMTAAVYASRANLSTVMIE--RGmPGGQMA 44
Cdd:COG3380 5 DIAIIGAGIAGLAAARALQDAGHEVTVFEksRG-VGGRMA 43
|
|
| FixC |
COG0644 |
Dehydrogenase (flavoprotein) [Energy production and conversion]; |
13-113 |
2.15e-04 |
|
Dehydrogenase (flavoprotein) [Energy production and conversion];
Pssm-ID: 440409 [Multi-domain] Cd Length: 281 Bit Score: 42.26 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 13 AGPAGMTAAVYASRANLSTVMIERG-------MPGGQMANT-EEVENFP------------GFEMITG------------ 60
Cdd:COG0644 1 AGPAGSAAARRLARAGLSVLLLEKGsfpgdkiCGGGLLPRAlEELEPLGldeplerpvrgaRFYSPGGksvelppgrggg 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 61 -----PDLSTKMFEHAKKFGAEYQYG-DIKSIEDKGDYKEINLGN-KEITARAVIISTGA 113
Cdd:COG0644 81 yvvdrARFDRWLAEQAEEAGAEVRTGtRVTDVLRDDGRVVVRTGDgEEIRADYVVDADGA 140
|
|
| PRK07846 |
PRK07846 |
mycothione reductase; Reviewed |
6-278 |
3.21e-04 |
|
mycothione reductase; Reviewed
Pssm-ID: 181142 [Multi-domain] Cd Length: 451 Bit Score: 42.25 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 6 YDVAIIGAGPAGMtaaVYASR-ANLSTVMIERGMPGGQMANteeVENFPgfemitgpdlsTKMF----------EHAKKF 74
Cdd:PRK07846 2 YDLIIIGTGSGNS---ILDERfADKRIAIVEKGTFGGTCLN---VGCIP-----------TKMFvyaadvartiREAARL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 75 G--AEYQYGDIKSIEDK--------------------------------GDYKEINLGN-KEITARAVIISTGAEYKKIG 119
Cdd:PRK07846 65 GvdAELDGVRWPDIVSRvfgridpiaaggeeyrgrdtpnidvyrgharfIGPKTLRTGDgEEITADQVVIAAGSRPVIPP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 120 VPGEQELGgrgvsycavcdgaFFKN----------KNLFVIGGGDSAVEEGAFLTKFADKVTIVHRRDE-LRAQKILQDR 188
Cdd:PRK07846 145 VIADSGVR-------------YHTSdtimrlpelpESLVIVGGGFIAAEFAHVFSALGVRVTVVNRSGRlLRHLDDDISE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 189 AFKN---DKIDFIWSHTLKSINEKDGKVgSVTLvstkdASEQTLDADGVFIYIGMKP----LTAPFVNLGITNDmGYIVT 261
Cdd:PRK07846 212 RFTElasKRWDVRLGRNVVGVSQDGSGV-TLRL-----DDGSTVEADVLLVATGRVPngdlLDAAAAGVDVDED-GRVVV 284
|
330
....*....|....*..
gi 515497732 262 EDNMSTKVPGIFAAGDV 278
Cdd:PRK07846 285 DEYQRTSAEGVFALGDV 301
|
|
| PRK09126 |
PRK09126 |
FAD-dependent hydroxylase; |
5-36 |
5.98e-04 |
|
FAD-dependent hydroxylase;
Pssm-ID: 236385 [Multi-domain] Cd Length: 392 Bit Score: 41.08 E-value: 5.98e-04
10 20 30
....*....|....*....|....*....|..
gi 515497732 5 NYDVAIIGAGPAGMTAAVYASRANLSTVMIER 36
Cdd:PRK09126 3 HSDIVVVGAGPAGLSFARSLAGSGLKVTLIER 34
|
|
| PRK04965 |
PRK04965 |
NADH:flavorubredoxin reductase NorW; |
145-277 |
6.01e-04 |
|
NADH:flavorubredoxin reductase NorW;
Pssm-ID: 179902 [Multi-domain] Cd Length: 377 Bit Score: 41.06 E-value: 6.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 145 KNLFVIGGGDSAVEEGAFLTKFADKVTIVHRRDEL-----------RAQKILQDRAfkndkIDFIWSHTLKSINEKDGKV 213
Cdd:PRK04965 142 QRVLVVGGGLIGTELAMDLCRAGKAVTLVDNAASLlaslmppevssRLQHRLTEMG-----VHLLLKSQLQGLEKTDSGI 216
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515497732 214 gSVTLvstkdASEQTLDADGVFIYIGMKPLTAPFVNLGITNDMGyIVTEDNMSTKVPGIFAAGD 277
Cdd:PRK04965 217 -RATL-----DSGRSIEVDAVIAAAGLRPNTALARRAGLAVNRG-IVVDSYLQTSAPDIYALGD 273
|
|
| PRK06481 |
PRK06481 |
flavocytochrome c; |
6-39 |
6.71e-04 |
|
flavocytochrome c;
Pssm-ID: 180584 [Multi-domain] Cd Length: 506 Bit Score: 40.97 E-value: 6.71e-04
10 20 30
....*....|....*....|....*....|....
gi 515497732 6 YDVAIIGAGPAGMTAAVYASRANLSTVMIERgMP 39
Cdd:PRK06481 62 YDIVIVGAGGAGMSAAIEAKDAGMNPVILEK-MP 94
|
|
| PLN02507 |
PLN02507 |
glutathione reductase |
100-281 |
6.95e-04 |
|
glutathione reductase
Pssm-ID: 215281 [Multi-domain] Cd Length: 499 Bit Score: 40.95 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 100 KEITARAVIISTGAEYKKIGVPGeQELGgrgvsycAVCDGAFFKN---KNLFVIGGGDSAVEEGAFLTKFADKVTIVHRR 176
Cdd:PLN02507 164 LRYTAKHILIATGSRAQRPNIPG-KELA-------ITSDEALSLEelpKRAVVLGGGYIAVEFASIWRGMGATVDLFFRK 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 177 --------DELRAqkiLQDRAFKNDKIDFIWSHTLKSINEKDGKVGSVTlvstkDASEQtLDADGVFIYIGMKPLTAPfV 248
Cdd:PLN02507 236 elplrgfdDEMRA---VVARNLEGRGINLHPRTNLTQLTKTEGGIKVIT-----DHGEE-FVADVVLFATGRAPNTKR-L 305
|
170 180 190
....*....|....*....|....*....|....*..
gi 515497732 249 NL---GITND-MGYIVTEDNMSTKVPGIFAAGDVRDK 281
Cdd:PLN02507 306 NLeavGVELDkAGAVKVDEYSRTNIPSIWAIGDVTNR 342
|
|
| COG3349 |
COG3349 |
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ... |
7-41 |
8.66e-04 |
|
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];
Pssm-ID: 442577 [Multi-domain] Cd Length: 445 Bit Score: 40.61 E-value: 8.66e-04
10 20 30
....*....|....*....|....*....|....*.
gi 515497732 7 DVAIIGAGPAGMTAAVYASRANLSTVMIE-RGMPGG 41
Cdd:COG3349 5 RVVVVGGGLAGLAAAVELAEAGFRVTLLEaRPRLGG 40
|
|
| PRK06185 |
PRK06185 |
FAD-dependent oxidoreductase; |
1-36 |
9.37e-04 |
|
FAD-dependent oxidoreductase;
Pssm-ID: 235729 [Multi-domain] Cd Length: 407 Bit Score: 40.61 E-value: 9.37e-04
10 20 30
....*....|....*....|....*....|....*.
gi 515497732 1 MTEINYDVAIIGAGPAGMTAAVYASRANLSTVMIER 36
Cdd:PRK06185 2 AEVETTDCCIVGGGPAGMMLGLLLARAGVDVTVLEK 37
|
|
| PRK12844 |
PRK12844 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
6-44 |
1.03e-03 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 183787 [Multi-domain] Cd Length: 557 Bit Score: 40.51 E-value: 1.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 515497732 6 YDVAIIGAGPAGMTAAVYASRANLSTVMIER-GMPGGQMA 44
Cdd:PRK12844 7 YDVVVVGSGGGGMCAALAAADSGLEPLIVEKqDKVGGSTA 46
|
|
| PRK10015 |
PRK10015 |
oxidoreductase; Provisional |
1-55 |
1.40e-03 |
|
oxidoreductase; Provisional
Pssm-ID: 182194 [Multi-domain] Cd Length: 429 Bit Score: 39.96 E-value: 1.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515497732 1 MTEINYDVAIIGAGPAGMTAAVYASRANLSTVMIERG-------MPGGQMANTEEVENFPGF 55
Cdd:PRK10015 1 MSDDKFDAIVVGAGVAGSVAALVMARAGLDVLVIERGdsagcknMTGGRLYAHTLEAIIPGF 62
|
|
| FadH2 |
COG0446 |
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ... |
8-112 |
1.79e-03 |
|
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: 39.41 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 8 VAIIGAGPAGMTAAVYASRANLSTVMIERGmpggqmanteevenfPGFEMITGPDLSTKMFEHAKKFGAEYQYGD-IKSI 86
Cdd:COG0446 127 AVVIGGGPIGLELAEALRKRGLKVTLVERA---------------PRLLGVLDPEMAALLEEELREHGVELRLGEtVVAI 191
|
90 100
....*....|....*....|....*.
gi 515497732 87 EDKGDYKEINLGNKEITARAVIISTG 112
Cdd:COG0446 192 DGDDKVAVTLTDGEEIPADLVVVAPG 217
|
|
| PRK08294 |
PRK08294 |
phenol 2-monooxygenase; Provisional |
7-36 |
2.10e-03 |
|
phenol 2-monooxygenase; Provisional
Pssm-ID: 236223 [Multi-domain] Cd Length: 634 Bit Score: 39.58 E-value: 2.10e-03
10 20 30
....*....|....*....|....*....|.
gi 515497732 7 DVAIIGAGPAGMTAAVYASR-ANLSTVMIER 36
Cdd:PRK08294 34 DVLIVGCGPAGLTLAAQLSAfPDITTRIVER 64
|
|
| PRK07208 |
PRK07208 |
hypothetical protein; Provisional |
7-36 |
2.11e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 235967 [Multi-domain] Cd Length: 479 Bit Score: 39.49 E-value: 2.11e-03
10 20 30
....*....|....*....|....*....|
gi 515497732 7 DVAIIGAGPAGMTAAVYASRANLSTVMIER 36
Cdd:PRK07208 6 SVVIIGAGPAGLTAAYELLKRGYPVTVLEA 35
|
|
| glycerol3P_GlpB |
TIGR03378 |
glycerol-3-phosphate dehydrogenase, anaerobic, B subunit; Members of this protein family are ... |
6-37 |
2.92e-03 |
|
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: 38.85 E-value: 2.92e-03
10 20 30
....*....|....*....|....*....|..
gi 515497732 6 YDVAIIGAGPAGMTAAVYASRANLSTVMIERG 37
Cdd:TIGR03378 1 FDVIIIGGGLAGLSCALRLAEAGKKCAIIAAG 32
|
|
| sdhA |
PRK07803 |
succinate dehydrogenase flavoprotein subunit; Reviewed |
1-51 |
2.95e-03 |
|
succinate dehydrogenase flavoprotein subunit; Reviewed
Pssm-ID: 236101 [Multi-domain] Cd Length: 626 Bit Score: 39.25 E-value: 2.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515497732 1 MTEI---NYDVAIIGAGPAGMTAAVYASRANLS-------------TVMIERGMpGGQMANTEEVEN 51
Cdd:PRK07803 1 MTEVerhSYDVVVIGAGGAGLRAAIEARERGLRvavvckslfgkahTVMAEGGC-AAAMGNVNPKDN 66
|
|
| PRK09564 |
PRK09564 |
coenzyme A disulfide reductase; Reviewed |
143-277 |
2.97e-03 |
|
coenzyme A disulfide reductase; Reviewed
Pssm-ID: 181958 [Multi-domain] Cd Length: 444 Bit Score: 38.87 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 143 KNKNLFVIGGGDSAVEEGAFLTKFADKVTIVHrrdelRAQKILQDrAFKNDKIDFIWS---------HTLKSINEKDGKv 213
Cdd:PRK09564 148 EIKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQ-----LEDRILPD-SFDKEITDVMEEelrengvelHLNEFVKSLIGE- 220
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515497732 214 GSVTLVSTkdaSEQTLDADGVFIYIGMKPLTAPFVNLGI-TNDMGYIVTEDNMSTKVPGIFAAGD 277
Cdd:PRK09564 221 DKVEGVVT---DKGEYEADVVIVATGVKPNTEFLEDTGLkTLKNGAIIVDEYGETSIENIYAAGD 282
|
|
| PTZ00052 |
PTZ00052 |
thioredoxin reductase; Provisional |
6-280 |
3.97e-03 |
|
thioredoxin reductase; Provisional
Pssm-ID: 185416 [Multi-domain] Cd Length: 499 Bit Score: 38.65 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 6 YDVAIIGAGPAGMTAAVYASRANLSTVMIERGMP---------GGQMANT----EEVENFPG-----FEMITGP------ 61
Cdd:PTZ00052 6 YDLVVIGGGSGGMAAAKEAAAHGKKVALFDYVKPstqgtkwglGGTCVNVgcvpKKLMHYAAnigsiFHHDSQMygwkts 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 62 ------DLSTKMFEHAKKFGAEYQYG----------DIKSIEDKGDYKEINLGNKE-ITARAVIISTGAE-YKKIGVPGE 123
Cdd:PTZ00052 86 ssfnwgKLVTTVQNHIRSLNFSYRTGlrsskveyinGLAKLKDEHTVSYGDNSQEEtITAKYILIATGGRpSIPEDVPGA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 124 QElggrgvsYCAVCDGAFFKNKN---LFVIGGGDSAVEEGAFLTKFADKVTIVHRRDELR------AQKILQdrAFKNDK 194
Cdd:PTZ00052 166 KE-------YSITSDDIFSLSKDpgkTLIVGASYIGLETAGFLNELGFDVTVAVRSIPLRgfdrqcSEKVVE--YMKEQG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 195 IDFIWSHTLKSINEKDGKVgsvtLVSTKDASEQTLDAdgVFIYIGMKP----LTAPFVNLGITNDMGYIVTEDnmSTKVP 270
Cdd:PTZ00052 237 TLFLEGVVPINIEKMDDKI----KVLFSDGTTELFDT--VLYATGRKPdikgLNLNAIGVHVNKSNKIIAPND--CTNIP 308
|
330
....*....|
gi 515497732 271 GIFAAGDVRD 280
Cdd:PTZ00052 309 NIFAVGDVVE 318
|
|
| PLN02463 |
PLN02463 |
lycopene beta cyclase |
6-35 |
4.61e-03 |
|
lycopene beta cyclase
Pssm-ID: 178082 [Multi-domain] Cd Length: 447 Bit Score: 38.54 E-value: 4.61e-03
10 20 30
....*....|....*....|....*....|
gi 515497732 6 YDVAIIGAGPAGMTAAVYASRANLSTVMIE 35
Cdd:PLN02463 29 VDLVVVGGGPAGLAVAQQVSEAGLSVCCID 58
|
|
| PRK13512 |
PRK13512 |
coenzyme A disulfide reductase; Provisional |
145-278 |
6.10e-03 |
|
coenzyme A disulfide reductase; Provisional
Pssm-ID: 184103 [Multi-domain] Cd Length: 438 Bit Score: 38.23 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515497732 145 KNLFVIGGGDSAVEEGAFLTKFADKVTIVHRRDELRA-------QKILQDraFKNDKIDFIWSHTLKSINEKdgkvgSVT 217
Cdd:PRK13512 149 DKALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKlmdadmnQPILDE--LDKREIPYRLNEEIDAINGN-----EVT 221
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515497732 218 LVSTKdaseqTLDADGVFIYIGMKPLTAPFVNLGIT-NDMGYIVTEDNMSTKVPGIFAAGDV 278
Cdd:PRK13512 222 FKSGK-----VEHYDMIIEGVGTHPNSKFIESSNIKlDDKGFIPVNDKFETNVPNIYAIGDI 278
|
|
| PRK09231 |
PRK09231 |
fumarate reductase flavoprotein subunit; Validated |
4-28 |
8.19e-03 |
|
fumarate reductase flavoprotein subunit; Validated
Pssm-ID: 236421 [Multi-domain] Cd Length: 582 Bit Score: 37.69 E-value: 8.19e-03
|
| PRK12835 |
PRK12835 |
3-ketosteroid-delta-1-dehydrogenase; Reviewed |
6-37 |
8.22e-03 |
|
3-ketosteroid-delta-1-dehydrogenase; Reviewed
Pssm-ID: 237221 [Multi-domain] Cd Length: 584 Bit Score: 37.86 E-value: 8.22e-03
10 20 30
....*....|....*....|....*....|..
gi 515497732 6 YDVAIIGAGPAGMTAAVYASRANLSTVMIERG 37
Cdd:PRK12835 12 VDVLVVGSGGGGMTAALTAAARGLDTLVVEKS 43
|
|
| PRK08275 |
PRK08275 |
putative oxidoreductase; Provisional |
263-307 |
9.32e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 181346 [Multi-domain] Cd Length: 554 Bit Score: 37.72 E-value: 9.32e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 515497732 263 DNMSTKVPGIFAAGDVRDKGLRQIVTATGDGSIAAQSAIDYIEEL 307
Cdd:PRK08275 363 EKAETTVPGLYAAGDMASVPHNYMLGAFTYGWFAGENAAEYVAGR 407
|
|
| |
