|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05362 |
PRK05362 |
phosphopentomutase; Provisional |
3-396 |
0e+00 |
|
phosphopentomutase; Provisional
Pssm-ID: 235430 Cd Length: 394 Bit Score: 684.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 3 FKRVFTVVLDSAGIGEASDAANFNDVGADTLGHIGAFYGEQFKLPNLQKLGLGNIRASDPIKGVPAAQPALGYFGKMQET 82
Cdd:PRK05362 1 MKRVFLIVLDSVGIGAAPDAAKFGDEGADTLGHIAEARKGGLKLPNLAKLGLGNIATGTPIAGVPANAEPIGYYGKAQEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 83 SVGKDSMDGHWEMMGLPVKEPLGFFPNGFPNELIQKLAAFSGRSVIV-NRPYSGTDVIRDYGEEQLATGALIVYTSGDSV 161
Cdd:PRK05362 81 SSGKDTPTGHWEIMGVPVLFPFGYFPNGFPQELIDEIEERAGRPGILgNKHASGTEIIDELGEEHMKTGKPIVYTSADSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 162 LQIAANEAVITLEELYRICEYARQITIEKPYRIGRVIARPFKGqDKDHFERTSDRHDYTLEPTGTTDMDRLKAAGLDVLA 241
Cdd:PRK05362 161 FQIAAHEEVFGLEELYRICEIAREILLDRPYNVGRVIARPFVG-EPGNFTRTGNRHDYALKPPAPTVLDKLKEAGGEVIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 242 VGKINDIFSGKGITSGVHTESNHDGMVQTIKNAQT-DFTGFSFTNLVDFDAMYGHRRNPEGYGAALMAFDQQLGELLAVL 320
Cdd:PRK05362 240 VGKIADIFAGQGITEKVKTKSNMDGMDATIEEMKEaGDNGLVFTNLVDFDSLYGHRRDVAGYAAALEEFDARLPELLAAL 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510997130 321 KPDDLLLITADHGNDPGFRGTDHTREYVPLLAYSSRLAGnQSLGVRSTFADLGATILENFDCPAGEVGTSFLTQLK 396
Cdd:PRK05362 320 KEDDLLIITADHGNDPTWPGTDHTREYVPLLVYGPKFKG-GSLGHRETFADIGATIADNFGVEPMEYGKSFLDELK 394
|
|
| DeoB |
COG1015 |
Phosphopentomutase [Carbohydrate transport and metabolism]; |
3-392 |
0e+00 |
|
Phosphopentomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440639 Cd Length: 385 Bit Score: 681.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 3 FKRVFTVVLDSAGIGEASDAANFNDVGADTLGHIGAFYGEqFKLPNLQKLGLGNIrasDPIKGVPAAQPALGYFGKMQET 82
Cdd:COG1015 1 MKRAILIVLDSVGIGEAPDAAKFGDEGANTLGHIAEAVGG-LNLPNLARLGLGNI---APLAGLPPVEEPLGAYGKMAEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 83 SVGKDSMDGHWEMMGLPVKEPLGFFPNGFPNELIQKLAAFSGRSVIVNRPYSGTDVIRDYGEEQLATGALIVYTSGDSVL 162
Cdd:COG1015 77 SAGKDTTTGHWEIAGLPVEFPFPTFPDGFPEELIDEFEERTGRGVLGNKPASGTEIIEELGEEHMRTGKPIVYTSADSVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 163 QIAANEAVITLEELYRICEYARQITiEKPYRIGRVIARPFKGqDKDHFERTSDRHDYTLEPTGTTDMDRLKAAGLDVLAV 242
Cdd:COG1015 157 QIAAHEEVFPLEELYRLCEIARELL-DGEYAVGRVIARPFVG-EPGNFVRTANRHDYALKPPGPTLLDRLKEAGGDVIAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 243 GKINDIFSGKGITSGVHTESNHDGMVQTIKNAQTDFTGFSFTNLVDFDAMYGHRRNPEGYGAALMAFDQQLGELLAVLKP 322
Cdd:COG1015 235 GKISDIFAGRGITESVKTKGNADGMDKTLEAMDEAFGGLIFTNLVDFDSLYGHRRDVAGYAKALEEFDARLPELLAALRP 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 323 DDLLLITADHGNDPGFRGTDHTREYVPLLAYSSRLAGNQSLGVRSTFADLGATILENFDCPAGEVGTSFL 392
Cdd:COG1015 315 DDLLIITADHGNDPTWPGTDHTREYVPLLVYGPGLKPGGNLGTRETFADIGATIADHFGVPPPGHGTSFL 384
|
|
| PPM |
cd16009 |
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ... |
4-391 |
0e+00 |
|
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase superfamily members that interconvert alpha-D-ribose 5-phosphate (ribose 5-phosphate) and alpha-D-ribose 1-phosphate (ribose 1-phosphate). This reaction bridges glucose metabolism and RNA biosynthesis. PPM is a Mn(2+)-dependent enzyme and protein phosphorylation activates the enzyme.
Pssm-ID: 293733 Cd Length: 382 Bit Score: 631.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 4 KRVFTVVLDSAGIGEASDAANFNDVGADTLGHIGAFYGEqFKLPNLQKLGLGNIrasDPIKGVPAAQPALGYFGKMQETS 83
Cdd:cd16009 1 KRVILIVLDSFGIGAMPDAAKFGDEGANTLGHIAEAVPG-LNLPNLEKLGLGNI---VGIEGGPPKENPIAAYGKMREAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 84 VGKDSMDGHWEMMGLPVKEPLGFFPNGFPNELIQKLAAFSGRSVIVNRPYSGTDVIRDYGEEQLATGALIVYTSGDSVLQ 163
Cdd:cd16009 77 AGKDTTTGHWEIMGLKPKKPFPTFPNGFPKELIDEFEKATGRKGLGNKPASGTEIIKELGEEHLKTGAPIVYTSADSVFQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 164 IAANEAVITLEELYRICEYARQITiEKPYRIGRVIARPFKGQDKDHFERTSDRHDYTLEPTGTTDMDRLKAAGLDVLAVG 243
Cdd:cd16009 157 IAAHEEVIPLEELYRICEIAREIL-DGEYKVGRVIARPFVGETGVYFKRTSNRHDYALVPPGKTVLDILKEAGIPVIGIG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 244 KINDIFSGKGITSGVHTESNHDGMVQTIKNAQTDFTGFSFTNLVDFDAMYGHRRNPEGYGAALMAFDQQLGELLAVLKPD 323
Cdd:cd16009 236 KIADIFAGRGITESIHTKSNADGMEKTLEALKEDFNGLIFTNLVDFDMLYGHRRDPEGYAEALEEFDRRLPELLAKLKED 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510997130 324 DLLLITADHGNDPGFRGTDHTREYVPLLAYSSRLAGNQsLGVRSTFADLGATILENFDCPAGEVGTSF 391
Cdd:cd16009 316 DLLIITADHGNDPTIGGTDHTREYVPLLVYGKGLKGVN-LGTRETFADIGATIADNFGVEPPENGTSF 382
|
|
| deoB |
TIGR01696 |
phosphopentomutase; This protein is involved in the purine and pyrimidine salvage pathway. It ... |
5-390 |
1.61e-176 |
|
phosphopentomutase; This protein is involved in the purine and pyrimidine salvage pathway. It catalyzes the conversion of D-ribose 1-phosphate to D-ribose 5-phosphate and the conversion of 2-deoxy-D-ribose 1-phosphate to 2-deoxy-D-ribose 5-phosphate. The seed members of this protein are characterized deoB proteins from E.Coli(SP:P07651) and Bacillus (SP:P46353). This model matches pfam01676 for Metalloenzyme superfamily. [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 162494 Cd Length: 381 Bit Score: 496.72 E-value: 1.61e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 5 RVFTVVLDSAGIGEASDAANFNDVGADTLGHIGAFYGEQfKLPNLQKLGLGNIrasDPIKGVPAAQPALGYFGKMQETSV 84
Cdd:TIGR01696 1 RVFLIVMDSVGIGEAPDAADFGDEGAHTLGHIAEACAKL-NLPNLTKLGLGKI---HEPAGVDGNEEPIAYYAKAHEASS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 85 GKDSMDGHWEMMGLPVKEPLGFFPNGFPNELIQKLAAFSGRSVIVNRPYSGTDVIRDYGEEQLATGALIVYTSGDSVLQI 164
Cdd:TIGR01696 77 GKDTMTGHWEIMGLPILFPFKVFPNGFPQELLQKLEERAGRKYLGNKPASGTVILDELGEEHMKTGKLIVYTSADSVLQI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 165 AANEAVITLEELYRICEYARQITIEKPYRIGRVIARPFKGqDKDHFERTSDRHDYTLEPTGTTDMDRLKAAGLDVLAVGK 244
Cdd:TIGR01696 157 AAHEETFPLEELYEICEIARELTTDPKYNIGRIIARPFVG-EPGNFQRTGNRHDYALKPFAPTVLQKLKDEGHDVISIGK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 245 INDIFSGKGITSGVHTESNHDGMVQTIKNAQTDFTGFSFTNLVDFDAMYGHRRNPEGYGAALMAFDQQLGELLAVLKPDD 324
Cdd:TIGR01696 236 IADIYDGEGITKKVRTTSNMDGMDATIKEMKEDFTGISFTNLVDFDALWGHRRDVAGYAAALELFDRRLPELFSLLREDD 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510997130 325 LLLITADHGNDPGFRGTDHTREYVPLLAYSSRLAGNQSLGVRSTFADLGATILENFDCPAGEVGTS 390
Cdd:TIGR01696 316 LLIITADHGNDPTWTGTDHTREYIPVLVYSPKVKPGHSLGHRETFADIGATIADNFGTSDPEYGKS 381
|
|
| Metalloenzyme |
pfam01676 |
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ... |
4-380 |
1.30e-59 |
|
Metalloenzyme superfamily; This family includes phosphopentomutase and 2,3-bisphosphoglycerate-independent phosphoglycerate mutase. This family is also related to pfam00245. The alignment contains the most conserved residues that are probably involved in metal binding and catalysis.
Pssm-ID: 396305 Cd Length: 410 Bit Score: 198.78 E-value: 1.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 4 KRVFTVVLDSAGIGEAsdaanfNDVGADTLGHIGafygeqfKLPNLQKLglgnirasdpIKGVPAA-QPALG-YFGKMQE 81
Cdd:pfam01676 1 KKVVLIVLDGWGDRPA------EDLNAKTPLHIA-------KTPNMDKL----------AKEYPEQlIGASGlAVGLPEG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 82 TSVGKDSmdGHWEMMGLPVKEPLGFFPNGFPNELIQKLAAFSGRSVIVNRPYSGTDVIRDYGEEQLATGALIVYTSGDSV 161
Cdd:pfam01676 58 QMGGSDV--GHLEIGGGRIVYQYLGRGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHSHIEHLLALIAL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 162 LQIAANEAVITLEEL------YRICEYARQITIEKPYRIGRVIARPFkGQDKDHFERTSDRHDYTLEPTGTTDMDRLKAA 235
Cdd:pfam01676 136 AKEAGAIKVHLLGDGddrpvgYILDGDAVITINFRFDRRRARILRLF-LLDPDFFDRDRVRHDALHVPTKTLYELKLPSA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 236 GLDVLAVGKINDIF------------------------------------------SGKGITSGVHTESNHDGMVQTIKN 273
Cdd:pfam01676 215 GAFVPEEGKNTDGEvleghglkqlriaetekyahvtffwgggreppfpgeerylipSPKVATYDLQPEMSAMEITDKLLE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 274 AQTDFTGFSFTNLVDFDaMYGHRRNPEGYGAALMAFDQQLGELLAVLKPDD-LLLITADHGNDPGFRGTDHTREYVPLLA 352
Cdd:pfam01676 295 ALKEKYDFVFVNFANTD-MVGHTGDVEGKVKAIEAVDERLGELLDALEEDDgLLIITADHGNPEEMKDTDHTREPVPILI 373
|
410 420 430
....*....|....*....|....*....|...
gi 510997130 353 YSSRLAGNQSLGV-----RSTFADLGATILENF 380
Cdd:pfam01676 374 YGKGVRPDQVLFGekfreRGGLADIAATILMLL 406
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05362 |
PRK05362 |
phosphopentomutase; Provisional |
3-396 |
0e+00 |
|
phosphopentomutase; Provisional
Pssm-ID: 235430 Cd Length: 394 Bit Score: 684.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 3 FKRVFTVVLDSAGIGEASDAANFNDVGADTLGHIGAFYGEQFKLPNLQKLGLGNIRASDPIKGVPAAQPALGYFGKMQET 82
Cdd:PRK05362 1 MKRVFLIVLDSVGIGAAPDAAKFGDEGADTLGHIAEARKGGLKLPNLAKLGLGNIATGTPIAGVPANAEPIGYYGKAQEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 83 SVGKDSMDGHWEMMGLPVKEPLGFFPNGFPNELIQKLAAFSGRSVIV-NRPYSGTDVIRDYGEEQLATGALIVYTSGDSV 161
Cdd:PRK05362 81 SSGKDTPTGHWEIMGVPVLFPFGYFPNGFPQELIDEIEERAGRPGILgNKHASGTEIIDELGEEHMKTGKPIVYTSADSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 162 LQIAANEAVITLEELYRICEYARQITIEKPYRIGRVIARPFKGqDKDHFERTSDRHDYTLEPTGTTDMDRLKAAGLDVLA 241
Cdd:PRK05362 161 FQIAAHEEVFGLEELYRICEIAREILLDRPYNVGRVIARPFVG-EPGNFTRTGNRHDYALKPPAPTVLDKLKEAGGEVIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 242 VGKINDIFSGKGITSGVHTESNHDGMVQTIKNAQT-DFTGFSFTNLVDFDAMYGHRRNPEGYGAALMAFDQQLGELLAVL 320
Cdd:PRK05362 240 VGKIADIFAGQGITEKVKTKSNMDGMDATIEEMKEaGDNGLVFTNLVDFDSLYGHRRDVAGYAAALEEFDARLPELLAAL 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510997130 321 KPDDLLLITADHGNDPGFRGTDHTREYVPLLAYSSRLAGnQSLGVRSTFADLGATILENFDCPAGEVGTSFLTQLK 396
Cdd:PRK05362 320 KEDDLLIITADHGNDPTWPGTDHTREYVPLLVYGPKFKG-GSLGHRETFADIGATIADNFGVEPMEYGKSFLDELK 394
|
|
| DeoB |
COG1015 |
Phosphopentomutase [Carbohydrate transport and metabolism]; |
3-392 |
0e+00 |
|
Phosphopentomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440639 Cd Length: 385 Bit Score: 681.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 3 FKRVFTVVLDSAGIGEASDAANFNDVGADTLGHIGAFYGEqFKLPNLQKLGLGNIrasDPIKGVPAAQPALGYFGKMQET 82
Cdd:COG1015 1 MKRAILIVLDSVGIGEAPDAAKFGDEGANTLGHIAEAVGG-LNLPNLARLGLGNI---APLAGLPPVEEPLGAYGKMAEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 83 SVGKDSMDGHWEMMGLPVKEPLGFFPNGFPNELIQKLAAFSGRSVIVNRPYSGTDVIRDYGEEQLATGALIVYTSGDSVL 162
Cdd:COG1015 77 SAGKDTTTGHWEIAGLPVEFPFPTFPDGFPEELIDEFEERTGRGVLGNKPASGTEIIEELGEEHMRTGKPIVYTSADSVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 163 QIAANEAVITLEELYRICEYARQITiEKPYRIGRVIARPFKGqDKDHFERTSDRHDYTLEPTGTTDMDRLKAAGLDVLAV 242
Cdd:COG1015 157 QIAAHEEVFPLEELYRLCEIARELL-DGEYAVGRVIARPFVG-EPGNFVRTANRHDYALKPPGPTLLDRLKEAGGDVIAV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 243 GKINDIFSGKGITSGVHTESNHDGMVQTIKNAQTDFTGFSFTNLVDFDAMYGHRRNPEGYGAALMAFDQQLGELLAVLKP 322
Cdd:COG1015 235 GKISDIFAGRGITESVKTKGNADGMDKTLEAMDEAFGGLIFTNLVDFDSLYGHRRDVAGYAKALEEFDARLPELLAALRP 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 323 DDLLLITADHGNDPGFRGTDHTREYVPLLAYSSRLAGNQSLGVRSTFADLGATILENFDCPAGEVGTSFL 392
Cdd:COG1015 315 DDLLIITADHGNDPTWPGTDHTREYVPLLVYGPGLKPGGNLGTRETFADIGATIADHFGVPPPGHGTSFL 384
|
|
| PPM |
cd16009 |
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ... |
4-391 |
0e+00 |
|
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase superfamily members that interconvert alpha-D-ribose 5-phosphate (ribose 5-phosphate) and alpha-D-ribose 1-phosphate (ribose 1-phosphate). This reaction bridges glucose metabolism and RNA biosynthesis. PPM is a Mn(2+)-dependent enzyme and protein phosphorylation activates the enzyme.
Pssm-ID: 293733 Cd Length: 382 Bit Score: 631.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 4 KRVFTVVLDSAGIGEASDAANFNDVGADTLGHIGAFYGEqFKLPNLQKLGLGNIrasDPIKGVPAAQPALGYFGKMQETS 83
Cdd:cd16009 1 KRVILIVLDSFGIGAMPDAAKFGDEGANTLGHIAEAVPG-LNLPNLEKLGLGNI---VGIEGGPPKENPIAAYGKMREAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 84 VGKDSMDGHWEMMGLPVKEPLGFFPNGFPNELIQKLAAFSGRSVIVNRPYSGTDVIRDYGEEQLATGALIVYTSGDSVLQ 163
Cdd:cd16009 77 AGKDTTTGHWEIMGLKPKKPFPTFPNGFPKELIDEFEKATGRKGLGNKPASGTEIIKELGEEHLKTGAPIVYTSADSVFQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 164 IAANEAVITLEELYRICEYARQITiEKPYRIGRVIARPFKGQDKDHFERTSDRHDYTLEPTGTTDMDRLKAAGLDVLAVG 243
Cdd:cd16009 157 IAAHEEVIPLEELYRICEIAREIL-DGEYKVGRVIARPFVGETGVYFKRTSNRHDYALVPPGKTVLDILKEAGIPVIGIG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 244 KINDIFSGKGITSGVHTESNHDGMVQTIKNAQTDFTGFSFTNLVDFDAMYGHRRNPEGYGAALMAFDQQLGELLAVLKPD 323
Cdd:cd16009 236 KIADIFAGRGITESIHTKSNADGMEKTLEALKEDFNGLIFTNLVDFDMLYGHRRDPEGYAEALEEFDRRLPELLAKLKED 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510997130 324 DLLLITADHGNDPGFRGTDHTREYVPLLAYSSRLAGNQsLGVRSTFADLGATILENFDCPAGEVGTSF 391
Cdd:cd16009 316 DLLIITADHGNDPTIGGTDHTREYVPLLVYGKGLKGVN-LGTRETFADIGATIADNFGVEPPENGTSF 382
|
|
| deoB |
TIGR01696 |
phosphopentomutase; This protein is involved in the purine and pyrimidine salvage pathway. It ... |
5-390 |
1.61e-176 |
|
phosphopentomutase; This protein is involved in the purine and pyrimidine salvage pathway. It catalyzes the conversion of D-ribose 1-phosphate to D-ribose 5-phosphate and the conversion of 2-deoxy-D-ribose 1-phosphate to 2-deoxy-D-ribose 5-phosphate. The seed members of this protein are characterized deoB proteins from E.Coli(SP:P07651) and Bacillus (SP:P46353). This model matches pfam01676 for Metalloenzyme superfamily. [Purines, pyrimidines, nucleosides, and nucleotides, Other]
Pssm-ID: 162494 Cd Length: 381 Bit Score: 496.72 E-value: 1.61e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 5 RVFTVVLDSAGIGEASDAANFNDVGADTLGHIGAFYGEQfKLPNLQKLGLGNIrasDPIKGVPAAQPALGYFGKMQETSV 84
Cdd:TIGR01696 1 RVFLIVMDSVGIGEAPDAADFGDEGAHTLGHIAEACAKL-NLPNLTKLGLGKI---HEPAGVDGNEEPIAYYAKAHEASS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 85 GKDSMDGHWEMMGLPVKEPLGFFPNGFPNELIQKLAAFSGRSVIVNRPYSGTDVIRDYGEEQLATGALIVYTSGDSVLQI 164
Cdd:TIGR01696 77 GKDTMTGHWEIMGLPILFPFKVFPNGFPQELLQKLEERAGRKYLGNKPASGTVILDELGEEHMKTGKLIVYTSADSVLQI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 165 AANEAVITLEELYRICEYARQITIEKPYRIGRVIARPFKGqDKDHFERTSDRHDYTLEPTGTTDMDRLKAAGLDVLAVGK 244
Cdd:TIGR01696 157 AAHEETFPLEELYEICEIARELTTDPKYNIGRIIARPFVG-EPGNFQRTGNRHDYALKPFAPTVLQKLKDEGHDVISIGK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 245 INDIFSGKGITSGVHTESNHDGMVQTIKNAQTDFTGFSFTNLVDFDAMYGHRRNPEGYGAALMAFDQQLGELLAVLKPDD 324
Cdd:TIGR01696 236 IADIYDGEGITKKVRTTSNMDGMDATIKEMKEDFTGISFTNLVDFDALWGHRRDVAGYAAALELFDRRLPELFSLLREDD 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510997130 325 LLLITADHGNDPGFRGTDHTREYVPLLAYSSRLAGNQSLGVRSTFADLGATILENFDCPAGEVGTS 390
Cdd:TIGR01696 316 LLIITADHGNDPTWTGTDHTREYIPVLVYSPKVKPGHSLGHRETFADIGATIADNFGTSDPEYGKS 381
|
|
| Metalloenzyme |
pfam01676 |
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ... |
4-380 |
1.30e-59 |
|
Metalloenzyme superfamily; This family includes phosphopentomutase and 2,3-bisphosphoglycerate-independent phosphoglycerate mutase. This family is also related to pfam00245. The alignment contains the most conserved residues that are probably involved in metal binding and catalysis.
Pssm-ID: 396305 Cd Length: 410 Bit Score: 198.78 E-value: 1.30e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 4 KRVFTVVLDSAGIGEAsdaanfNDVGADTLGHIGafygeqfKLPNLQKLglgnirasdpIKGVPAA-QPALG-YFGKMQE 81
Cdd:pfam01676 1 KKVVLIVLDGWGDRPA------EDLNAKTPLHIA-------KTPNMDKL----------AKEYPEQlIGASGlAVGLPEG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 82 TSVGKDSmdGHWEMMGLPVKEPLGFFPNGFPNELIQKLAAFSGRSVIVNRPYSGTDVIRDYGEEQLATGALIVYTSGDSV 161
Cdd:pfam01676 58 QMGGSDV--GHLEIGGGRIVYQYLGRGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHSHIEHLLALIAL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 162 LQIAANEAVITLEEL------YRICEYARQITIEKPYRIGRVIARPFkGQDKDHFERTSDRHDYTLEPTGTTDMDRLKAA 235
Cdd:pfam01676 136 AKEAGAIKVHLLGDGddrpvgYILDGDAVITINFRFDRRRARILRLF-LLDPDFFDRDRVRHDALHVPTKTLYELKLPSA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 236 GLDVLAVGKINDIF------------------------------------------SGKGITSGVHTESNHDGMVQTIKN 273
Cdd:pfam01676 215 GAFVPEEGKNTDGEvleghglkqlriaetekyahvtffwgggreppfpgeerylipSPKVATYDLQPEMSAMEITDKLLE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 274 AQTDFTGFSFTNLVDFDaMYGHRRNPEGYGAALMAFDQQLGELLAVLKPDD-LLLITADHGNDPGFRGTDHTREYVPLLA 352
Cdd:pfam01676 295 ALKEKYDFVFVNFANTD-MVGHTGDVEGKVKAIEAVDERLGELLDALEEDDgLLIITADHGNPEEMKDTDHTREPVPILI 373
|
410 420 430
....*....|....*....|....*....|...
gi 510997130 353 YSSRLAGNQSLGV-----RSTFADLGATILENF 380
Cdd:pfam01676 374 YGKGVRPDQVLFGekfreRGGLADIAATILMLL 406
|
|
| PRK12383 |
PRK12383 |
putative mutase; Provisional |
4-396 |
3.10e-51 |
|
putative mutase; Provisional
Pssm-ID: 237085 Cd Length: 406 Bit Score: 176.70 E-value: 3.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 4 KRVFTVVLDSAGIGEASDAANF--NDVGADTLGHIGAFYGeQFKLPNLQKLGLGNIRASDPIKGVPAAQPALGYFGKMQE 81
Cdd:PRK12383 2 ARFVVLVIDSFGVGAMKDVTLVrpQDAGANTCGHILSQLP-HLQLPTLEKLGLINALGYAPGDMQPSPSATWGVAELQHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 82 tsvGKDSMDGHWEMMG----LPVKEPLGFFPNGFPNELIQklAAFSgrsviVNRPYSGTDVIrdygeeqLATGALIVyts 157
Cdd:PRK12383 81 ---GADTFMGHQEIMGtrplPPLRMPFSDVIDRVEQALES--AGYQ-----VERRGDGLQFL-------LVNQAVAI--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 158 GDS-------VLQIAANEAVITLEELYRICEYARQITiekpyRIGRVIArpFKGQD------KDHFERTSD--------- 215
Cdd:PRK12383 141 GDNleadlgqVYNVTANLSVISFDDALKIGRIVREQV-----QVGRVIV--FGGLLtdsqriLDAAESKEGrfiginapk 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 216 ----------RH-DYTLEPTgTTDMDRLKAAGLDVLAVGKINDIFS---GKGITSGVHTESNHDGMVQTIKNAQTdftGF 281
Cdd:PRK12383 214 sgvydngyqvVHlGYGVDPK-VQVPQKLYEAGVPVVLVGKVADIVNnpyGVSWQNLVDTQRVMDITLDEFNTHPT---AF 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 282 SFTNLVDFDAMyGHRRNPEGYGAALMAFDQQLGELLAVLKPDDLLLITADHGNDPGFRGTDHTREYVPLLAYSSRLaGNQ 361
Cdd:PRK12383 290 ICTNIQETDLA-GHAEDVARYAERLEVVDRNLARLLEAMTPDDCLVVMADHGNDPTIGHSHHTREVVPLLVYQKGL-QAT 367
|
410 420 430
....*....|....*....|....*....|....*
gi 510997130 362 SLGVRSTFADLGATILENFDCPAGEVGTSFLTQLK 396
Cdd:PRK12383 368 QLGVRTTLSDVGATVCEFFGAPPPQNGRSFLSSLR 402
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
216-380 |
8.86e-14 |
|
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.
Pssm-ID: 293732 [Multi-domain] Cd Length: 237 Bit Score: 70.14 E-value: 8.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 216 RHDYTLEPTGTTDMDRLKAAGLDVLAVGkindifsgkgitsgvhtesnhdgMVQTIKNAQTDFTGFSFTNLVDFD-AMYG 294
Cdd:cd00016 80 SRAAGKDEDGPTIPELLKQAGYRTGVIG-----------------------LLKAIDETSKEKPFVLFLHFDGPDgPGHA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 295 HRRNPEGYGAALMAFDQQLGELLAVLKP-----DDLLLITADHGNDPGFRG----------TDHTREYVPLLAYSSRLAG 359
Cdd:cd00016 137 YGPNTPEYYDAVEEIDERIGKVLDALKKagdadDTVIIVTADHGGIDKGHGgdpkadgkadKSHTGMRVPFIAYGPGVKK 216
|
170 180
....*....|....*....|.
gi 510997130 360 NQSLGVRSTFADLGATILENF 380
Cdd:cd00016 217 GGVKHELISQYDIAPTLADLL 237
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
221-392 |
2.15e-08 |
|
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293767 [Multi-domain] Cd Length: 271 Bit Score: 54.86 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 221 LEPTGTTDMDRLKAAGLDVLAVGKINDIFSGKGITSGVHTESNHDGMVQTIKNAQTDFTGFSFTNLVDF-DAMYGHRR-- 297
Cdd:cd16148 72 LEPDDPTLAEILRKAGYYTAAVSSNPHLFGGPGFDRGFDTFEDFRGQEGDPGEEGDERAERVTDRALEWlDRNADDDPff 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 298 ---------NPEGYGAALMAFDQQLGELLAVLKP----DD-LLLITADHG---NDPGFRGTDHTREY-----VPLLAYSS 355
Cdd:cd16148 152 lflhyfdphEPYLYDAEVRYVDEQIGRLLDKLKElgllEDtLVIVTSDHGeefGEHGLYWGHGSNLYdeqlhVPLIIRWP 231
|
170 180 190
....*....|....*....|....*....|....*....
gi 510997130 356 RLAGNQSLGVRSTFADLGATILENF--DCPAGEVGTSFL 392
Cdd:cd16148 232 GKEPGKRVDALVSHIDIAPTLLDLLgvEPPDYSDGRSLL 270
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
194-333 |
1.97e-07 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 52.44 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 194 IGRVIARPFKGQDKDHFERTSDRHDYTLEPTGTTDMDRLKAAGLDVLAV------------GKINDIFSGKGITSGVHTE 261
Cdd:COG1524 87 VGNGWYDPELGRVVNSLSWVEDGFGSNSLLPVPTIFERARAAGLTTAAVfwpsfegsglidAARPYPYDGRKPLLGNPAA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 262 SNH--DGMVQTIKNAQTDFTgfsFTNLVDFDAMyGHRRNPEG--YGAALMAFDQQLGELLAVLKPDD-----LLLITADH 332
Cdd:COG1524 167 DRWiaAAALELLREGRPDLL---LVYLPDLDYA-GHRYGPDSpeYRAALREVDAALGRLLDALKARGlyegtLVIVTADH 242
|
.
gi 510997130 333 G 333
Cdd:COG1524 243 G 243
|
|
| iPGM_like |
cd16011 |
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate ... |
233-356 |
2.16e-06 |
|
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate independent phosphoglycerate mutase (iPGM) and bacterial phosphopentomutases; The proteins in this subfamily of alkaline phosphatase are not characterized. Their sequences show similarity to 2 3 bisphosphoglycerate independent phosphoglycerate mutase (iPGM) which catalyzes the interconversion of 3-phosphoglycerate to 2-phosphoglycerate, and to bacterial phosphopentomutases (PPMs) which interconvert alpha-D-ribose 5-phosphate (ribose 5-phosphate) and alpha-D-ribose 1-phosphate (ribose 1-phosphate).
Pssm-ID: 293735 Cd Length: 368 Bit Score: 49.39 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 233 KAAGLDVLAVGkindifsgkGITSGVHTesNHDGMVQTIKNAqtdftgfsftnLVDFDAMY---------GHRRNPEGYG 303
Cdd:cd16011 223 RLAGMDVIEVP---------GATGYLDT--DYEGKAEAALEA-----------LKDYDFVFvhvkapdeaGHDGDPEAKV 280
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 304 AALMAFDQQLGELL--AVLKPDDLLLITADHgndpgfrGT-----DHTREYVPLLAYSSR 356
Cdd:cd16011 281 KAIERIDKAIVGPLleLLDGEDFVIVVTPDH-------STpcslkTHSGDPVPFLIYGPG 333
|
|
| ApgM |
COG3635 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type [Carbohydrate ... |
233-360 |
4.11e-06 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type [Carbohydrate transport and metabolism]; 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 442852 Cd Length: 398 Bit Score: 48.60 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 233 KAAGLDVLAVgkindifsgKGITSGVHTesNHDGMVQTIKNAqtdftgfsftnLVDFDAMY---------GHRRNPEGYG 303
Cdd:COG3635 254 KLAGMDVIDV---------PGATGYLDT--NYAGKAEAALEA-----------LKDYDFVYvhveapdeaGHDGDLEEKV 311
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510997130 304 AALMAFDQQ-LGELLAVLKPDD--LLLITADHgndPGF-RGTDHTREYVPLLAYSSRLAGN 360
Cdd:COG3635 312 KAIERIDRRvVGPLLEGLEKFEdyRILVTPDH---PTPiSLRTHSGDPVPFLIYGPGVRPD 369
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
296-396 |
1.31e-05 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 46.80 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 296 RRNPEGYGAALMAFDQQLGELLAVLK----PDD-LLLITADHG---NDPGFRGTDHT------ReyVPLLAY-SSRLAGN 360
Cdd:COG3119 196 RRARAAYAAMIEEVDDQVGRLLDALEelglADNtIVVFTSDNGpslGEHGLRGGKGTlyeggiR--VPLIVRwPGKIKAG 273
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 510997130 361 QslgVRSTFA---DLGATILE--NFDCPAGEVGTSFLTQLK 396
Cdd:COG3119 274 S---VSDALVsliDLLPTLLDlaGVPIPEDLDGRSLLPLLT 311
|
|
| iPGM |
cd16010 |
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
305-390 |
2.26e-05 |
|
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- independent phosphoglycerate mutase (iPGM) catalyzes the interconversion of 3-phosphoglycerate (3PGA) and 2-phosphoglycerate (2PGA). They are the predominant PGM in plants and some other bacteria, including endospore forming Gram-positive bacteria and their close relatives. The two steps catalysis is a phosphatase reaction removing the phosphate from 2- or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The iPGM exists as a dimer, each monomer binding 2 magnesium atoms, which are essential for enzymatic activity.
Pssm-ID: 293734 Cd Length: 503 Bit Score: 46.25 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 305 ALMAFDQQLGELL-AVLKPDDLLLITADHGN-----DP--GFRGTDHTREYVPLLAYSSRLagNQSLGVRSTFADLGATI 376
Cdd:cd16010 408 AVEAVDECLGRIVeAVLENGGTLLITADHGNaeemiDPetGGPHTAHTTNPVPFIIVDPGL--KRKLLKDGGLADVAPTI 485
|
90
....*....|....*.
gi 510997130 377 LE--NFDCPAGEVGTS 390
Cdd:cd16010 486 LDllGIEKPKEMTGKS 501
|
|
| PRK05434 |
PRK05434 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
292-378 |
4.40e-05 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235463 Cd Length: 507 Bit Score: 45.48 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 292 MYGHRRNPEgygAALMA---FDQQLGELL-AVLKPDDLLLITADHGN-----DPGFRG--TDHTREYVPLLayssrLAGN 360
Cdd:PRK05434 400 MVGHTGNLE---AAVKAveaVDECLGRVVdAVLKVGGTLLITADHGNaeqmiDPETGQphTAHTTNPVPFI-----LVGG 471
|
90
....*....|....*....
gi 510997130 361 QSLGVRS-TFADLGATILE 378
Cdd:PRK05434 472 KALRLEGgKLADIAPTILD 490
|
|
| ALP |
cd16012 |
Alkaline Phosphatase; Alkaline phosphatases are non-specific membrane-bound ... |
294-361 |
1.05e-04 |
|
Alkaline Phosphatase; Alkaline phosphatases are non-specific membrane-bound phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Mammalian alkaline phosphatase is divided into four isozymes depending upon the site of tissue expression. They are Intestinal ALP, Placental ALP, Germ cell ALP and tissue nonspecific alkaline phosphatase or liver/bone/kidney (L/B/K) ALP.
Pssm-ID: 293736 Cd Length: 283 Bit Score: 43.57 E-value: 1.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510997130 294 GHRRNPEGYGAALMAFDQQLGELLA-VLKPDD-LLLITADHGndpgfrgTDHTREYVPLLAY---SSRLAGNQ 361
Cdd:cd16012 204 GHANDAARAIEETLAFDKAVKVALDfAKKDGDtLVIVTADHE-------TGHTGEDVPVFAYgpgAELFGGVY 269
|
|
| MrcA |
COG5009 |
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis]; |
120-170 |
2.00e-04 |
|
Membrane carboxypeptidase/penicillin-binding protein [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 444033 [Multi-domain] Cd Length: 785 Bit Score: 43.61 E-value: 2.00e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 510997130 120 AAFSGRSVIVNRPYSgTDVIR-----DYGEEQLATGALIVYTSGDSVLQIAANEAV 170
Cdd:COG5009 250 ARYHGASAEVDAPYF-AEMVRrelveRYGEDALYTGGLKVYTTLDPRLQEAAEKAL 304
|
|
| GpmI |
COG0696 |
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ... |
304-378 |
2.39e-04 |
|
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and metabolism]; Phosphoglycerate mutase (BPG-independent), AlkP superfamily is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440460 Cd Length: 511 Bit Score: 43.12 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 304 AALMAFDQQLGELL-AVLKPDDLLLITADHGN-----DPGFRG--TDHTREYVPLLAYSSRLAGNQSLGVRstFADLGAT 375
Cdd:COG0696 413 KAVEAVDECLGRVVdAVLAAGGTLLITADHGNaeqmiDPDTGGphTAHTTNPVPFILVGGDKGVKLREDGR--LADIAPT 490
|
...
gi 510997130 376 ILE 378
Cdd:COG0696 491 ILE 493
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
212-378 |
4.98e-04 |
|
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
Pssm-ID: 293746 [Multi-domain] Cd Length: 236 Bit Score: 41.27 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 212 RTSDRHDYTLEPTGTTDMDRLKAAGLDVLAVGKindifsgkgitsgvhtesNHDGMVQTIKNAQTD--FtgfsFTNlVDF 289
Cdd:cd16022 68 RGNVGNGGGLPPDEPTLAELLKEAGYRTALIGK------------------WHDEAIDFIERRDKDkpF----FLY-VSF 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 290 DAMygHrrNPEGYGAALMAFDQQLGELLAVLKPDDLL-----LITADHG---NDPGFRGTdHTREY-----VPLLA-YSS 355
Cdd:cd16022 125 NAP--H--PPFAYYAMVSAIDDQIGRILDALEELGLLdntliVFTSDHGdmlGDHGLRGK-KGSLYeggirVPFIVrWPG 199
|
170 180
....*....|....*....|...
gi 510997130 356 RLAGNQSLGVRSTFADLGATILE 378
Cdd:cd16022 200 KIPAGQVSDALVSLLDLLPTLLD 222
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
310-384 |
9.00e-03 |
|
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase/phosphodiesterase hydrolyses phosphonate monoesters or phosphate diesters using a posttranslationally formed formylglycine as the catalytic nucleophile. PMH is the member of the alkaline phosphatase superfamily. The structure of PMH is more homologous to arylsulfatase than alkaline phosphatase. Sulfatases also use formylglycine as catalytic nucleophile.
Pssm-ID: 293752 [Multi-domain] Cd Length: 449 Bit Score: 38.01 E-value: 9.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510997130 310 DQQLGELLAVLKP----DDLLLI-TADHGN---DPGFRGTDHTRE---YVPLLAYS-SRLAGNQSLGVRSTFA---DLGA 374
Cdd:cd16028 248 DDHLGRLFDYLKEtgqwDDTLIVfTSDHGEqlgDHWLWGKDGFFDqayRVPLIVRDpRREADATRGQVVDAFTesvDVMP 327
|
90
....*....|
gi 510997130 375 TILENFDCPA 384
Cdd:cd16028 328 TILDWLGGEI 337
|
|
| |
