|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02918 |
PLN02918 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase |
1-546 |
0e+00 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase
Pssm-ID: 215496 [Multi-domain] Cd Length: 544 Bit Score: 1065.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 1 MILIRRTRAMTCFLTQLLPLSLANRLHNTCTISKSSRDLHNYLAGNAlGYTCPIPRPAFCSSSSQVHSFSCKSSSGVTRD 80
Cdd:PLN02918 1 NIKSTATMTFTFLLQSLLPLPISPPPPHSSSLSSSPSPTQRFLTPSQ-GSRLPPRRRALCTKSQDPRWRRAMASLAVIPN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 81 MQQSIQTPesISYLTQHDAAEIDEILMGPLGFSVDQLMELAGLSVATSIAEVYKPSEFNRVLAICGPGNNGGDGLVAAHH 160
Cdd:PLN02918 80 MQDSGSPP--LSYLTQREAAEIDETLMGPLGFSVDQLMELAGLSVAASIAEVYKPGEYSRVLAICGPGNNGGDGLVAARH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 161 LYHFGYKPFVCYPKRTSKSLYNGLVTQLESLSVPFLAVEDLPSDLSKDFDILLDAMFGFSFHGAPRPPFDDLIHKMVHLN 240
Cdd:PLN02918 158 LHHFGYKPFVCYPKRTAKPLYTGLVTQLESLSVPFVSVEDLPADLSKDFDIIVDAMFGFSFHGAPRPPFDDLIRRLVSLQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 241 KCNQT-RKSVIVSVDIPSGWHVEEGDVDGEGMKPDMLVSLTAPKLCARKFSGPHHFLGGRFVPPSIVEKYKLHLPPYPGT 319
Cdd:PLN02918 238 NYEQTlKHPVIVSVDIPSGWHVEEGDHEGGGIKPDMLVSLTAPKLCAKKFRGPHHFLGGRFVPPSIVEKYKLHLPPYPGT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 320 SMCVRIGKPPQIDISALRENYISPEFLEEQVEANPVDQFKKWFDDAVAAGLKEPNAMALSTVGKDGKPSSRMVLLKGVDK 399
Cdd:PLN02918 318 SMCVRIGKPPSVDISALRENYISPELLEEQVETDPTDQFRKWFDEAVAAGLREPNAMALSTANKDGKPSSRMVLLKGVDK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 400 DGFVWYTNYESQKGRELFENPRAALLFYWDGLNRQVRVEGSVQKVSDGESREYFSSRPRGSQIGAIVSKQSSVVPGRHVL 479
Cdd:PLN02918 398 NGFVWYTNYESQKGSDLSENPSAALLFYWEELNRQVRVEGSVQKVPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVL 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1000977988 480 HQQYKELEEKFSNISLIPKPKHWGGYRLEPERFEFWQGQQSRLHDRLQYVPEEINGKQVWKIVRLAP 546
Cdd:PLN02918 478 YQEYKELEKKYSDGSVIPKPKNWGGYRLKPNLFEFWQGQQSRLHDRLQYSLQEVNGKPVWKIHRLAP 544
|
|
| PdxH |
COG0259 |
Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine ... |
332-546 |
2.90e-120 |
|
Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine/pyridoxamine 5'-phosphate oxidase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 440029 Cd Length: 212 Bit Score: 352.96 E-value: 2.90e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 332 DISALRENYISPEFLEEQVEANPVDQFKKWFDDAVAAGLKEPNAMALSTVGKDGKPSSRMVLLKGVDKDGFVWYTNYESQ 411
Cdd:COG0259 3 DLADLRREYTKGGLDESDLPADPLALFARWLEEAEAAGVPEPNAMTLATVDADGRPSARTVLLKGVDERGFVFYTNYESR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 412 KGRELFENPRAALLFYWDGLNRQVRVEGSVQKVSDGESREYFSSRPRGSQIGAIVSKQSSVVPGRHVLHQQYKELEEKFS 491
Cdd:COG0259 83 KGRELAANPRAALTFFWPELERQVRIEGRVEKVSAAESDAYFASRPRGSQLGAWASPQSQPIASREELEARFAELEARFA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1000977988 492 NISlIPKPKHWGGYRLEPERFEFWQGQQSRLHDRLQYVPEEingkQVWKIVRLAP 546
Cdd:COG0259 163 GGD-VPRPPHWGGYRVVPDRIEFWQGRPSRLHDRLRYTRED----GGWTIERLAP 212
|
|
| pdxH |
TIGR00558 |
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is ... |
353-546 |
1.39e-116 |
|
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is designed to find only true pyridoxamine-phosphate oxidase and to ignore the related protein PhzG involved in phenazine biosynthesis. This protein from E. coli was characterized as a homodimer with two FMN per dimer. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
Pssm-ID: 273138 Cd Length: 190 Bit Score: 342.56 E-value: 1.39e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 353 NPVDQFKKWFDDAVAAGLKEPNAMALSTVGKDGKPSSRMVLLKGVDKDGFVWYTNYESQKGRELFENPRAALLFYWDGLN 432
Cdd:TIGR00558 1 DPIEQFERWFEEAIEAELPEPNAMTLATVDADGRPSARIVLLKGFDERGFVFYTNYESRKGQELAANPKAALLFPWHSLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 433 RQVRVEGSVQKVSDGESREYFSSRPRGSQIGAIVSKQSSVVPGRHVLHQQYKELEEKFSNiSLIPKPKHWGGYRLEPERF 512
Cdd:TIGR00558 81 RQVRIEGRVEKVSREESDAYFASRPRGSQIGAWASQQSRPIASREELEARFAELKARFPD-GEVPRPEFWGGYRVVPDEI 159
|
170 180 190
....*....|....*....|....*....|....
gi 1000977988 513 EFWQGQQSRLHDRLQYVPEeinGKQVWKIVRLAP 546
Cdd:TIGR00558 160 EFWQGRPSRLHDRFRYRRD---GDGSWRIERLAP 190
|
|
| phena_PhzG |
NF038138 |
phenazine biosynthesis FMN-dependent oxidase PhzG; |
343-546 |
9.82e-54 |
|
phenazine biosynthesis FMN-dependent oxidase PhzG;
Pssm-ID: 468380 Cd Length: 205 Bit Score: 180.64 E-value: 9.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 343 PEFLEEqvEANPVDQFKKWFDDAVAAGLKEPNAMALSTVGKDGKPSSRMVLLKGVDKDGFVWYTNYESQKGRELFENPRA 422
Cdd:NF038138 11 PEFDAP--PAEPLGLLRRWLEAAVALGVREPRALALATADADGRPSTRIVVVKEVSDRGLVFTTHAGSRKGRELAANPWA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 423 ALLFYWDGLNRQVRVEGSVQKVSDGESREYFSSRPRGSQIGAIVSKQSSVVPGRHVLHQQYKELEEkfsNISLIPKPKHW 502
Cdd:NF038138 89 SGVLYWRETSQQISLSGPVERLPDAESDALWAARPVATHAMTAASRQSEPLDDEAALRAEARELAE---AGGPLPRPARF 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1000977988 503 GGYRLEPERFEFWQGQQSRLHDRLQYvpeEINGKQvWKIVRLAP 546
Cdd:NF038138 166 VGYRLVPEEVEFWAAGPDRLHRRLRY---DRDGDG-WTHVRLQP 205
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
114-285 |
1.08e-40 |
|
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a set of catalytic residues and structural features that are different from the conventional dehydrogenases. YjeF-N domain is fused to Ribokinases in bacteria (YjeF), where they may be phosphatases, and to divergent Sm and the FDF domain in eukaryotes (Dcp3p and FLJ21128), where they may be involved in decapping and catalyze hydrolytic RNA-processing reactions.
Pssm-ID: 427546 [Multi-domain] Cd Length: 168 Bit Score: 144.68 E-value: 1.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 114 VDQLMELAGLSVATSIAEVYKPSEfNRVLAICGPGNNGGDGLVAAHHLYHFGYK--PFVCYPKRTSKSLYNGLVTQLESL 191
Cdd:pfam03853 1 SAVLMENAGRAAARVLKALLSPAG-PKVLILCGPGNNGGDGLAAARHLANRGAKvtVLLLGPEEKLSEDARRQLDLFKKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 192 SVPFLA---VEDLPSDLSkDFDILLDAMFGFSFHGAPRPPFDDLIhkmvhlNKCNQTRKsVIVSVDIPSGWHVEEGDVDG 268
Cdd:pfam03853 80 GGKIVTdnpDEDLEKLLS-PVDLIIDALLGTGLSGPLRGEYAALI------EWINQSGA-PVLAVDIPSGLDADTGAVLG 151
|
170
....*....|....*..
gi 1000977988 269 EGMKPDMLVSLTAPKLC 285
Cdd:pfam03853 152 TAVRADHTVTFGAPKPG 168
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02918 |
PLN02918 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase |
1-546 |
0e+00 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase
Pssm-ID: 215496 [Multi-domain] Cd Length: 544 Bit Score: 1065.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 1 MILIRRTRAMTCFLTQLLPLSLANRLHNTCTISKSSRDLHNYLAGNAlGYTCPIPRPAFCSSSSQVHSFSCKSSSGVTRD 80
Cdd:PLN02918 1 NIKSTATMTFTFLLQSLLPLPISPPPPHSSSLSSSPSPTQRFLTPSQ-GSRLPPRRRALCTKSQDPRWRRAMASLAVIPN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 81 MQQSIQTPesISYLTQHDAAEIDEILMGPLGFSVDQLMELAGLSVATSIAEVYKPSEFNRVLAICGPGNNGGDGLVAAHH 160
Cdd:PLN02918 80 MQDSGSPP--LSYLTQREAAEIDETLMGPLGFSVDQLMELAGLSVAASIAEVYKPGEYSRVLAICGPGNNGGDGLVAARH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 161 LYHFGYKPFVCYPKRTSKSLYNGLVTQLESLSVPFLAVEDLPSDLSKDFDILLDAMFGFSFHGAPRPPFDDLIHKMVHLN 240
Cdd:PLN02918 158 LHHFGYKPFVCYPKRTAKPLYTGLVTQLESLSVPFVSVEDLPADLSKDFDIIVDAMFGFSFHGAPRPPFDDLIRRLVSLQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 241 KCNQT-RKSVIVSVDIPSGWHVEEGDVDGEGMKPDMLVSLTAPKLCARKFSGPHHFLGGRFVPPSIVEKYKLHLPPYPGT 319
Cdd:PLN02918 238 NYEQTlKHPVIVSVDIPSGWHVEEGDHEGGGIKPDMLVSLTAPKLCAKKFRGPHHFLGGRFVPPSIVEKYKLHLPPYPGT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 320 SMCVRIGKPPQIDISALRENYISPEFLEEQVEANPVDQFKKWFDDAVAAGLKEPNAMALSTVGKDGKPSSRMVLLKGVDK 399
Cdd:PLN02918 318 SMCVRIGKPPSVDISALRENYISPELLEEQVETDPTDQFRKWFDEAVAAGLREPNAMALSTANKDGKPSSRMVLLKGVDK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 400 DGFVWYTNYESQKGRELFENPRAALLFYWDGLNRQVRVEGSVQKVSDGESREYFSSRPRGSQIGAIVSKQSSVVPGRHVL 479
Cdd:PLN02918 398 NGFVWYTNYESQKGSDLSENPSAALLFYWEELNRQVRVEGSVQKVPESESENYFHSRPRGSQIGAIVSKQSSVVPGRHVL 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1000977988 480 HQQYKELEEKFSNISLIPKPKHWGGYRLEPERFEFWQGQQSRLHDRLQYVPEEINGKQVWKIVRLAP 546
Cdd:PLN02918 478 YQEYKELEKKYSDGSVIPKPKNWGGYRLKPNLFEFWQGQQSRLHDRLQYSLQEVNGKPVWKIHRLAP 544
|
|
| PLN03049 |
PLN03049 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
83-546 |
0e+00 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215550 [Multi-domain] Cd Length: 462 Bit Score: 900.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 83 QSIQTPESISYLTQHDAAEIDEILMGPLGFSVDQLMELAGLSVATSIAEVYKPSEFNRVLAICGPGNNGGDGLVAAHHLY 162
Cdd:PLN03049 4 QHLHNPDSISYLSQREAIAIDEHLMGPLGFSVDQLMELAGLSVASAIAEVYSPSEYRRVLALCGPGNNGGDGLVAARHLH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 163 HFGYKPFVCYPKRTSKSLYNGLVTQLESLSVPFLAVEDLPSDLSKDFDILLDAMFGFSFHGAPRPPFDDLIHKMVHLNKc 242
Cdd:PLN03049 84 HFGYKPSICYPKRTDKPLYNGLVTQLESLSVPFLSVEDLPSDLSSQFDIVVDAMFGFSFHGAPRPPFDDLIQKLVRAAG- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 243 nqtrKSVIVSVDIPSGWHVEEGDVDGEGMKPDMLVSLTAPKLCARKFSGPHHFLGGRFVPPSIVEKYKLHLPPYPGTSMC 322
Cdd:PLN03049 163 ----PPPIVSVDIPSGWHVEEGDVNGEGLKPDMLVSLTAPKLCAKMFKGPHHFLGGRFVPPAIVEKFKLHLPPYPGTSMC 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 323 VRIGKPPQIDISALRENYISPEFLEEQVEANPVDQFKKWFDDAVAAGLKEPNAMALSTVGKDGKPSSRMVLLKGVDKDGF 402
Cdd:PLN03049 239 VRIGKTPSVDIAALRENYVGPELLEEQVNADPIDQFKEWFDDAVAAGLREPNAMTLATAGEDGRPSARIVLLKGVDKRGF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 403 VWYTNYESQKGRELFENPRAALLFYWDGLNRQVRVEGSVQKVSDGESREYFSSRPRGSQIGAIVSKQSSVVPGRHVLHQQ 482
Cdd:PLN03049 319 VWYTNYDSRKAHELSANPKASLVFYWDGLHRQVRVEGSVEKVSEEESDQYFHSRPRGSQIGALVSKQSTVIPGRHILDQS 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1000977988 483 YKELEEKFSNISLIPKPKHWGGYRLEPERFEFWQGQQSRLHDRLQYVPEEINGKQVWKIVRLAP 546
Cdd:PLN03049 399 YKELEAKYADSSAIPKPKHWGGYRLKPELIEFWQGRESRLHDRLQYTREEINGKSVWKIDRLAP 462
|
|
| PdxH |
COG0259 |
Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine ... |
332-546 |
2.90e-120 |
|
Pyridoxine/pyridoxamine 5'-phosphate oxidase [Coenzyme transport and metabolism]; Pyridoxine/pyridoxamine 5'-phosphate oxidase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 440029 Cd Length: 212 Bit Score: 352.96 E-value: 2.90e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 332 DISALRENYISPEFLEEQVEANPVDQFKKWFDDAVAAGLKEPNAMALSTVGKDGKPSSRMVLLKGVDKDGFVWYTNYESQ 411
Cdd:COG0259 3 DLADLRREYTKGGLDESDLPADPLALFARWLEEAEAAGVPEPNAMTLATVDADGRPSARTVLLKGVDERGFVFYTNYESR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 412 KGRELFENPRAALLFYWDGLNRQVRVEGSVQKVSDGESREYFSSRPRGSQIGAIVSKQSSVVPGRHVLHQQYKELEEKFS 491
Cdd:COG0259 83 KGRELAANPRAALTFFWPELERQVRIEGRVEKVSAAESDAYFASRPRGSQLGAWASPQSQPIASREELEARFAELEARFA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1000977988 492 NISlIPKPKHWGGYRLEPERFEFWQGQQSRLHDRLQYVPEEingkQVWKIVRLAP 546
Cdd:COG0259 163 GGD-VPRPPHWGGYRVVPDRIEFWQGRPSRLHDRLRYTRED----GGWTIERLAP 212
|
|
| pdxH |
TIGR00558 |
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is ... |
353-546 |
1.39e-116 |
|
pyridoxamine-phosphate oxidase; This model is similar to Pyridox_oxidase from Pfam but is designed to find only true pyridoxamine-phosphate oxidase and to ignore the related protein PhzG involved in phenazine biosynthesis. This protein from E. coli was characterized as a homodimer with two FMN per dimer. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
Pssm-ID: 273138 Cd Length: 190 Bit Score: 342.56 E-value: 1.39e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 353 NPVDQFKKWFDDAVAAGLKEPNAMALSTVGKDGKPSSRMVLLKGVDKDGFVWYTNYESQKGRELFENPRAALLFYWDGLN 432
Cdd:TIGR00558 1 DPIEQFERWFEEAIEAELPEPNAMTLATVDADGRPSARIVLLKGFDERGFVFYTNYESRKGQELAANPKAALLFPWHSLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 433 RQVRVEGSVQKVSDGESREYFSSRPRGSQIGAIVSKQSSVVPGRHVLHQQYKELEEKFSNiSLIPKPKHWGGYRLEPERF 512
Cdd:TIGR00558 81 RQVRIEGRVEKVSREESDAYFASRPRGSQIGAWASQQSRPIASREELEARFAELKARFPD-GEVPRPEFWGGYRVVPDEI 159
|
170 180 190
....*....|....*....|....*....|....
gi 1000977988 513 EFWQGQQSRLHDRLQYVPEeinGKQVWKIVRLAP 546
Cdd:TIGR00558 160 EFWQGRPSRLHDRFRYRRD---GDGSWRIERLAP 190
|
|
| PLN03050 |
PLN03050 |
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional |
89-325 |
9.89e-115 |
|
pyridoxine (pyridoxamine) 5'-phosphate oxidase; Provisional
Pssm-ID: 215551 [Multi-domain] Cd Length: 246 Bit Score: 339.93 E-value: 9.89e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 89 ESISYLTQHDAAEIDEILMGPLGFSVDQLMELAGLSVATSIAEVYK-------PSEFNRVLAICGPGNNGGDGLVAAHHL 161
Cdd:PLN03050 4 IQTGYLNAQDAAALDEELMSTPGFSLEQLMELAGLSVAEAVYEVADgekasnpPGRHPRVLLVCGPGNNGGDGLVAARHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 162 YHFGYKPFVCYPKRTSKSLYNGLVTQLESLSVPFLAV----EDLPSDLSKDFDILLDAMFGFSFHGAPRPPFDDLIHKMV 237
Cdd:PLN03050 84 AHFGYEVTVCYPKQSSKPHYENLVTQCEDLGIPFVQAiggtNDSSKPLETTYDVIVDAIFGFSFHGAPRAPFDTLLAQMV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 238 HLnkcnQTRKSVIVSVDIPSGWHVEEGDVDGEGMKPDMLVSLTAPKLCARKFSGpHHFLGGRFVPPSIVEKYKLHLPPYP 317
Cdd:PLN03050 164 QQ----QKSPPPIVSVDVPSGWDVDEGDVSGTGMRPDVLVSLTAPKLSAKKFEG-RHFVGGRFLPPAIAEKYGLQKPPYP 238
|
....*...
gi 1000977988 318 GTSMCVRI 325
Cdd:PLN03050 239 GVSQVMEV 246
|
|
| PRK05679 |
PRK05679 |
pyridoxal 5'-phosphate synthase; |
347-546 |
8.33e-108 |
|
pyridoxal 5'-phosphate synthase;
Pssm-ID: 235555 Cd Length: 195 Bit Score: 320.24 E-value: 8.33e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 347 EEQVEANPVDQFKKWFDDAVAAGLKEPNAMALSTVGKDGKPSSRMVLLKGVDKDGFVWYTNYESQKGRELFENPRAALLF 426
Cdd:PRK05679 1 RADLPAEPLALFERWLAEAVKAELNDPNAMTLATVDEDGRPSQRIVLLKGFDERGFVFYTNYESRKGRQLAANPKAALLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 427 YWDGLNRQVRVEGSVQKVSDGESREYFSSRPRGSQIGAIVSKQSSVVPGRHVLHQQYKELEEKFSnISLIPKPKHWGGYR 506
Cdd:PRK05679 81 PWKSLERQVRVEGRVEKVSAEESDAYFASRPRGSQIGAWASKQSRPISSRAALEAKFAEVKAKFA-QGEVPRPPHWGGYR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1000977988 507 LEPERFEFWQGQQSRLHDRLQYVPEEingkQVWKIVRLAP 546
Cdd:PRK05679 160 VVPESIEFWQGRPSRLHDRILYRRDD----GGWKIERLAP 195
|
|
| phena_PhzG |
NF038138 |
phenazine biosynthesis FMN-dependent oxidase PhzG; |
343-546 |
9.82e-54 |
|
phenazine biosynthesis FMN-dependent oxidase PhzG;
Pssm-ID: 468380 Cd Length: 205 Bit Score: 180.64 E-value: 9.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 343 PEFLEEqvEANPVDQFKKWFDDAVAAGLKEPNAMALSTVGKDGKPSSRMVLLKGVDKDGFVWYTNYESQKGRELFENPRA 422
Cdd:NF038138 11 PEFDAP--PAEPLGLLRRWLEAAVALGVREPRALALATADADGRPSTRIVVVKEVSDRGLVFTTHAGSRKGRELAANPWA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 423 ALLFYWDGLNRQVRVEGSVQKVSDGESREYFSSRPRGSQIGAIVSKQSSVVPGRHVLHQQYKELEEkfsNISLIPKPKHW 502
Cdd:NF038138 89 SGVLYWRETSQQISLSGPVERLPDAESDALWAARPVATHAMTAASRQSEPLDDEAALRAEARELAE---AGGPLPRPARF 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1000977988 503 GGYRLEPERFEFWQGQQSRLHDRLQYvpeEINGKQvWKIVRLAP 546
Cdd:NF038138 166 VGYRLVPEEVEFWAAGPDRLHRRLRY---DRDGDG-WTHVRLQP 205
|
|
| yjeF_nterm |
TIGR00197 |
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology ... |
98-303 |
1.65e-42 |
|
yjeF N-terminal region; The protein region corresponding to this model shows no clear homology to any protein of known function. This model is built on yeast protein YNL200C and the N-terminal regions of E. coli yjeF and its orthologs in various species. The C-terminal region of yjeF and its orthologs shows similarity to hydroxyethylthiazole kinase (thiM) and other enzymes involved in thiamine biosynthesis. Yeast YKL151C and B. subtilis yxkO match the yjeF C-terminal domain but lack this region. [Unknown function, General]
Pssm-ID: 272956 [Multi-domain] Cd Length: 205 Bit Score: 151.02 E-value: 1.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 98 DAAEIDEILMGPLGFSVDQLMELAGLSVATSIAEVYKPSEfnRVLAICGPGNNGGDGLVAAHHLYhfGYKPFVCYPKRTS 177
Cdd:TIGR00197 7 KDMAIDKENAEYLGLTLDLLMENAGKAVAQAVLQAYPLAG--HVIIFCGPGNNGGDGFVVARHLK--GFGVEVFLLKKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 178 K-SLYNGLVTQLESLSVPFLAVEDLPSDLSKDFDILLDAMFGFSFHGAPRPPFDDLIHkmvHLNKcnqtRKSVIVSVDIP 256
Cdd:TIGR00197 83 RiECTEQAEVNLKALKVGGISIDEGNLVKPEDCDVIIDAILGTGFKGKLREPFKTIVE---SINE----LPAPIVSVDIP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1000977988 257 SGWHVEEGDVDGEGMKPDMLVSLTAPKLC---ARKFSGPHHFLGGRFVPP 303
Cdd:TIGR00197 156 SGLDVDTGAIEGPAVNADLTITFHAIKPCllsDRADVTGELKVGGIGIPP 205
|
|
| YjeF_N |
pfam03853 |
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a ... |
114-285 |
1.08e-40 |
|
YjeF-related protein N-terminus; YjeF-N domain is a novel version of the Rossmann fold with a set of catalytic residues and structural features that are different from the conventional dehydrogenases. YjeF-N domain is fused to Ribokinases in bacteria (YjeF), where they may be phosphatases, and to divergent Sm and the FDF domain in eukaryotes (Dcp3p and FLJ21128), where they may be involved in decapping and catalyze hydrolytic RNA-processing reactions.
Pssm-ID: 427546 [Multi-domain] Cd Length: 168 Bit Score: 144.68 E-value: 1.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 114 VDQLMELAGLSVATSIAEVYKPSEfNRVLAICGPGNNGGDGLVAAHHLYHFGYK--PFVCYPKRTSKSLYNGLVTQLESL 191
Cdd:pfam03853 1 SAVLMENAGRAAARVLKALLSPAG-PKVLILCGPGNNGGDGLAAARHLANRGAKvtVLLLGPEEKLSEDARRQLDLFKKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 192 SVPFLA---VEDLPSDLSkDFDILLDAMFGFSFHGAPRPPFDDLIhkmvhlNKCNQTRKsVIVSVDIPSGWHVEEGDVDG 268
Cdd:pfam03853 80 GGKIVTdnpDEDLEKLLS-PVDLIIDALLGTGLSGPLRGEYAALI------EWINQSGA-PVLAVDIPSGLDADTGAVLG 151
|
170
....*....|....*..
gi 1000977988 269 EGMKPDMLVSLTAPKLC 285
Cdd:pfam03853 152 TAVRADHTVTFGAPKPG 168
|
|
| Nnr1 |
COG0062 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and ... |
94-291 |
2.63e-39 |
|
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate epimerase domain [Nucleotide transport and metabolism];
Pssm-ID: 439832 [Multi-domain] Cd Length: 499 Bit Score: 150.02 E-value: 2.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 94 LTQHDAAEIDEILMGPLGFSVDQLMELAGLSVATSIAEVYkPSEFNRVLAICGPGNNGGDGLVAAHHLYHFGYKPFVCYP 173
Cdd:COG0062 4 LTAAQMRALDRAAIEALGIPGLVLMERAGRAVARAIRRRF-PSAARRVLVLCGPGNNGGDGLVAARLLAEAGYNVTVFLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 174 KRTSK----SLYNglVTQLESLSVPFLAVEDLPSDLSkDFDILLDAMFGFSFHGAPRPPFDDLIHKMvhlnkcNQTRKSV 249
Cdd:COG0062 83 GDPEKlsgdAAAN--LERLKAAGIPILELDDELPELA-EADLIVDALFGTGLSRPLRGPYAELIEAI------NASGAPV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1000977988 250 iVSVDIPSGWHVEEGDVDGEGMKPDMLVSLTAPKLC-----ARKFSG 291
Cdd:COG0062 154 -LAVDIPSGLDADTGEVLGAAVRADLTVTFGAPKPGlllgpGRDYCG 199
|
|
| Putative_PNPOx |
pfam01243 |
Pyridoxamine 5'-phosphate oxidase; Family of domains with putative PNPOx function. Family ... |
362-448 |
9.08e-31 |
|
Pyridoxamine 5'-phosphate oxidase; Family of domains with putative PNPOx function. Family members were predicted to encode pyridoxamine 5'-phosphate oxidase, based on sequence similarity. However, there is no experimental data to validate the predicted activity and purified proteins, such as Swiss:Q06199 and its paralogs, do not possess this activity, nor do they bind to flavin mononucleotide (FMN). To date, the only time functional oxidase activity has been experimentally demonstrated is when the sequences contain both pfam01243 and pfam10590. Moreover, some of the family members that contain both domains have been shown to be involved in phenazine biosynthesis. While some molecular function has been experimentally validated for the proteins containing both domains, the role performed by each domain on its own is unknown.
Pssm-ID: 426149 [Multi-domain] Cd Length: 88 Bit Score: 114.65 E-value: 9.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 362 FDDAVAAGLKEPNAMALSTVGKDGKPSSRMVLLK-GVDKDGFVWYTNYESQKGRELFENPRAALLFYWDGLNRQVRVEGS 440
Cdd:pfam01243 1 LTEEIREFLAEPNAVVLATVDKDGRPNVRPVGLKyGFDTVGILFATNTDSRKARNLEENPRVALLFGDPELRRGVRIEGT 80
|
....*...
gi 1000977988 441 VQKVSDGE 448
Cdd:pfam01243 81 AEIVTDGE 88
|
|
| PNP_phzG_C |
pfam10590 |
Pyridoxine 5'-phosphate oxidase C-terminal dimerization region; This domain represents one of ... |
502-546 |
1.59e-20 |
|
Pyridoxine 5'-phosphate oxidase C-terminal dimerization region; This domain represents one of the two dimerization regions of the protein, located at the edge of the dimer interface, at the C-terminus, being the last three beta strands, S6, S7, and S8 along with the last three residues to the end. In Swiss:P21159, S6 runs from residues 178-192, S7 from 200-206 and S8 from 211-215. the extended loop, of residues 167-177 may well be involved in the pocket formed between the two dimers that positions the FMN molecule.To date, the only time functional oxidase or phenazine biosynthesis activities have been experimentally demonstrated is when the sequences contain both pfam01243 and pfam10590. It is unknown the role performed by each domain in bringing about molecular functions of either oxidase or phenazine activity.
Pssm-ID: 463161 Cd Length: 42 Bit Score: 84.48 E-value: 1.59e-20
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1000977988 502 WGGYRLEPERFEFWQGQQSRLHDRLQYVPEEINGkqvWKIVRLAP 546
Cdd:pfam10590 1 WGGYRLVPEEIEFWQGRPSRLHDRIRYTREGDGG---WTIERLAP 42
|
|
| PRK10565 |
PRK10565 |
putative carbohydrate kinase; Provisional |
80-295 |
4.68e-10 |
|
putative carbohydrate kinase; Provisional
Pssm-ID: 182554 [Multi-domain] Cd Length: 508 Bit Score: 62.00 E-value: 4.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 80 DMQQSIQTPESISYLTQHDAAEideilmgpLGFSVDQLMELAGLSvATSIAEVYKPSEfNRVLAICGPGNNGGDGLVAAH 159
Cdd:PRK10565 12 SIPHSVWPADDIRRGEREAADA--------LGLTLYELMLRAGEA-AFQVARSAYPDA-RHWLVLCGHGNNGGDGYVVAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 160 hlyhfgykpfvcypkrtskslynglVTQLESLSVPFLAVED---LPSD---------------------LSKDFDILLDA 215
Cdd:PRK10565 82 -------------------------LAQAAGIDVTLLAQESdkpLPEEaalareawlnaggeihaadivWPESVDLIVDA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 216 MFGFSFHGAPRPPFDDLIHKmvhlnkCNQTRKSViVSVDIPSGWHVEEGDVDGEGMKPDMLVSLTA--PKLC---ARKFS 290
Cdd:PRK10565 137 LLGTGLRQAPREPYAALIDQ------ANAHPAPV-VALDIPSGLLAETGATPGAVINADHTVTFIAlkPGLLtgkARDVV 209
|
....*
gi 1000977988 291 GPHHF 295
Cdd:PRK10565 210 GQLHF 214
|
|
| YzzA |
COG3871 |
General stress protein 26 (function unknown) [Function unknown]; |
364-451 |
5.47e-09 |
|
General stress protein 26 (function unknown) [Function unknown];
Pssm-ID: 443080 [Multi-domain] Cd Length: 132 Bit Score: 54.55 E-value: 5.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 364 DAVAAGLKEPNAMALSTVGKDGKPSSRMVLLKGVDKDGFVW-YTNYESQKGRELFENPRAALLFYWDGLNRQVRVEGSVQ 442
Cdd:COG3871 9 EKLWELLEDIRTAMLATVDADGRPHSRPMWFQVDVDDGTLWfFTSRDSAKVRNIRRDPRVSLSFADPGDDRYVSVEGTAE 88
|
....*....
gi 1000977988 443 KVSDGESRE 451
Cdd:COG3871 89 IVDDRAKID 97
|
|
| Rv1155_F420 |
TIGR03618 |
PPOX class probable F420-dependent enzyme; A Genome Properties metabolic reconstruction for ... |
370-479 |
8.78e-04 |
|
PPOX class probable F420-dependent enzyme; A Genome Properties metabolic reconstruction for F420 biosynthesis shows that slightly over 10 percent of all prokaryotes with fully sequenced genomes, including about two thirds of the Actinomyces, make F420. The Partial Phylogenetic Profiling algorithm identifies this members of this protein family as high-scoring proteins to the F420 biosynthesis profile. A member of this family, Rv1155, was crytallized after expression in Escherichia coli, which does not synthesize F420; the crystal structure shown to resemble FMN-binding proteins, but with a recognizable empty cleft corresponding to, yet differing profounding from, the FMN site of pyridoxine 5'-phosphate oxidase. We propose that this protein family consists of F420-binding enzymes. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 274679 [Multi-domain] Cd Length: 126 Bit Score: 39.59 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000977988 370 LKEPNAMALSTVGKDGKPSSRMVLLkGVDKDGFVWYTNYESQKGRELFENPRAALLFYW-DGLNRQVRVEGSVQKVSDGE 448
Cdd:TIGR03618 5 LSERRLAVLATIRPDGRPQLSPVWF-ALDGDELVFSTTAGRAKARNLRRDPRVSLSVLDpDGPYRYVEIEGTAEVSPDPD 83
|
90 100 110
....*....|....*....|....*....|....*
gi 1000977988 449 SREYF----SSRPRGSQiGAIVSKQSSVVPGRHVL 479
Cdd:TIGR03618 84 AVRDLvdrlAERYRGAA-GEDEYRRPMVDPRRVVV 117
|
|
| |
