|
Name |
Accession |
Description |
Interval |
E-value |
| deoB |
TIGR01696 |
phosphopentomutase; This protein is involved in the purine and pyrimidine salvage pathway. It ... |
7-386 |
0e+00 |
|
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: 733.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 7 RVHLIVMDSVGIGEAPDAADFKDEGSHTLRHTLEGFD-QTLPNLEKLGLGNIDKLPVVNAVEQPEAYYTKLSEASVGKDT 85
Cdd:TIGR01696 1 RVFLIVMDSVGIGEAPDAADFGDEGAHTLGHIAEACAkLNLPNLTKLGLGKIHEPAGVDGNEEPIAYYAKAHEASSGKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 86 MTGHWEIMGLNIMQPFKVYPNGFPEELIQQIEEMTGRKVVANKPASGTQIIDEWGEHQMKTGDLIVYTSADPVLQIAAHE 165
Cdd:TIGR01696 81 MTGHWEIMGLPILFPFKVFPNGFPQELLQKLEERAGRKYLGNKPASGTVILDELGEEHMKTGKLIVYTSADSVLQIAAHE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 166 DIIPLEELYDICEKVRELTKDPKYLIGRIIARPYVGEPGNFTRTSNRHDYALKPFGKTVLDHLKDGGYDVIAIGKINDIY 245
Cdd:TIGR01696 161 ETFPLEELYEICEIARELTTDPKYNIGRIIARPFVGEPGNFQRTGNRHDYALKPFAPTVLQKLKDEGHDVISIGKIADIY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 246 DGEGVTEAVRTKSNMDGMDQLMKIVKKDFTGISFLNLVDFDALYGHRRDKPGYAQAIKDFDDRLPELFSNLKEDDLVIIT 325
Cdd:TIGR01696 241 DGEGITKKVRTTSNMDGMDATIKEMKEDFTGISFTNLVDFDALWGHRRDVAGYAAALELFDRRLPELFSLLREDDLLIIT 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613365656 326 ADHGNDPTAPGTDHTREYIPVIMYSPKFKGGHALESDTTFSSIGATIADNFNVTLPEFGKS 386
Cdd:TIGR01696 321 ADHGNDPTWTGTDHTREYIPVLVYSPKVKPGHSLGHRETFADIGATIADNFGTSDPEYGKS 381
|
|
| PRK05362 |
PRK05362 |
phosphopentomutase; Provisional |
5-392 |
0e+00 |
|
phosphopentomutase; Provisional
Pssm-ID: 235430 Cd Length: 394 Bit Score: 725.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 5 FNRVHLIVMDSVGIGEAPDAADFKDEGSHTLRHTLEGF--DQTLPNLEKLGLGNIDK---LPVVNAVEQPEAYYTKLSEA 79
Cdd:PRK05362 1 MKRVFLIVLDSVGIGAAPDAAKFGDEGADTLGHIAEARkgGLKLPNLAKLGLGNIATgtpIAGVPANAEPIGYYGKAQEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 80 SVGKDTMTGHWEIMGLNIMQPFKVYPNGFPEELIQQIEEMTGR-KVVANKPASGTQIIDEWGEHQMKTGDLIVYTSADPV 158
Cdd:PRK05362 81 SSGKDTPTGHWEIMGVPVLFPFGYFPNGFPQELIDEIEERAGRpGILGNKHASGTEIIDELGEEHMKTGKPIVYTSADSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 159 LQIAAHEDIIPLEELYDICEKVRELTKDPKYLIGRIIARPYVGEPGNFTRTSNRHDYALKPFGKTVLDHLKDGGYDVIAI 238
Cdd:PRK05362 161 FQIAAHEEVFGLEELYRICEIAREILLDRPYNVGRVIARPFVGEPGNFTRTGNRHDYALKPPAPTVLDKLKEAGGEVIAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 239 GKINDIYDGEGVTEAVRTKSNMDGMDQLMKIVK-KDFTGISFLNLVDFDALYGHRRDKPGYAQAIKDFDDRLPELFSNLK 317
Cdd:PRK05362 241 GKIADIFAGQGITEKVKTKSNMDGMDATIEEMKeAGDNGLVFTNLVDFDSLYGHRRDVAGYAAALEEFDARLPELLAALK 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613365656 318 EDDLVIITADHGNDPTAPGTDHTREYIPVIMYSPKFKGGhALESDTTFSSIGATIADNFNVTLPEFGKSYLKELK 392
Cdd:PRK05362 321 EDDLLIITADHGNDPTWPGTDHTREYVPLLVYGPKFKGG-SLGHRETFADIGATIADNFGVEPMEYGKSFLDELK 394
|
|
| DeoB |
COG1015 |
Phosphopentomutase [Carbohydrate transport and metabolism]; |
5-389 |
0e+00 |
|
Phosphopentomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440639 Cd Length: 385 Bit Score: 724.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 5 FNRVHLIVMDSVGIGEAPDAADFKDEGSHTLRHTLE---GFDqtLPNLEKLGLGNIDKLPVVNAVEQPEAYYTKLSEASV 81
Cdd:COG1015 1 MKRAILIVLDSVGIGEAPDAAKFGDEGANTLGHIAEavgGLN--LPNLARLGLGNIAPLAGLPPVEEPLGAYGKMAEVSA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 82 GKDTMTGHWEIMGLNIMQPFKVYPNGFPEELIQQIEEMTGRKVVANKPASGTQIIDEWGEHQMKTGDLIVYTSADPVLQI 161
Cdd:COG1015 79 GKDTTTGHWEIAGLPVEFPFPTFPDGFPEELIDEFEERTGRGVLGNKPASGTEIIEELGEEHMRTGKPIVYTSADSVFQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 162 AAHEDIIPLEELYDICEKVRELTKDPkYLIGRIIARPYVGEPGNFTRTSNRHDYALKPFGKTVLDHLKDGGYDVIAIGKI 241
Cdd:COG1015 159 AAHEEVFPLEELYRLCEIARELLDGE-YAVGRVIARPFVGEPGNFVRTANRHDYALKPPGPTLLDRLKEAGGDVIAVGKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 242 NDIYDGEGVTEAVRTKSNMDGMDQLMKIVKKDFTGISFLNLVDFDALYGHRRDKPGYAQAIKDFDDRLPELFSNLKEDDL 321
Cdd:COG1015 238 SDIFAGRGITESVKTKGNADGMDKTLEAMDEAFGGLIFTNLVDFDSLYGHRRDVAGYAKALEEFDARLPELLAALRPDDL 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613365656 322 VIITADHGNDPTAPGTDHTREYIPVIMYSPKFKGGHALESDTTFSSIGATIADNFNVTLPEFGKSYLK 389
Cdd:COG1015 318 LIITADHGNDPTWPGTDHTREYVPLLVYGPGLKPGGNLGTRETFADIGATIADHFGVPPPGHGTSFLS 385
|
|
| PPM |
cd16009 |
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ... |
6-386 |
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: 647.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 6 NRVHLIVMDSVGIGEAPDAADFKDEGSHTLRHTLEGFDQ-TLPNLEKLGLGNIDKLPVVNAVEQPEAYYTKLSEASVGKD 84
Cdd:cd16009 1 KRVILIVLDSFGIGAMPDAAKFGDEGANTLGHIAEAVPGlNLPNLEKLGLGNIVGIEGGPPKENPIAAYGKMREASAGKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 85 TMTGHWEIMGLNIMQPFKVYPNGFPEELIQQIEEMTGRKVVANKPASGTQIIDEWGEHQMKTGDLIVYTSADPVLQIAAH 164
Cdd:cd16009 81 TTTGHWEIMGLKPKKPFPTFPNGFPKELIDEFEKATGRKGLGNKPASGTEIIKELGEEHLKTGAPIVYTSADSVFQIAAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 165 EDIIPLEELYDICEKVRELTkDPKYLIGRIIARPYVGEPG-NFTRTSNRHDYALKPFGKTVLDHLKDGGYDVIAIGKIND 243
Cdd:cd16009 161 EEVIPLEELYRICEIAREIL-DGEYKVGRVIARPFVGETGvYFKRTSNRHDYALVPPGKTVLDILKEAGIPVIGIGKIAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 244 IYDGEGVTEAVRTKSNMDGMDQLMKIVKKDFTGISFLNLVDFDALYGHRRDKPGYAQAIKDFDDRLPELFSNLKEDDLVI 323
Cdd:cd16009 240 IFAGRGITESIHTKSNADGMEKTLEALKEDFNGLIFTNLVDFDMLYGHRRDPEGYAEALEEFDRRLPELLAKLKEDDLLI 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613365656 324 ITADHGNDPTAPGTDHTREYIPVIMYSPKFKGGhALESDTTFSSIGATIADNFNVTLPEFGKS 386
Cdd:cd16009 320 ITADHGNDPTIGGTDHTREYVPLLVYGKGLKGV-NLGTRETFADIGATIADNFGVEPPENGTS 381
|
|
| Metalloenzyme |
pfam01676 |
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ... |
7-378 |
1.96e-61 |
|
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: 203.40 E-value: 1.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 7 RVHLIVMDSVGIGEApdaadfKDEGSHTLRHTLEgfdqtLPNLEKLgLGNIDKLPVVNAVEqpeaYYTKLSEASVGKDTm 86
Cdd:pfam01676 2 KVVLIVLDGWGDRPA------EDLNAKTPLHIAK-----TPNMDKL-AKEYPEQLIGASGL----AVGLPEGQMGGSDV- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 87 tGHWEIMGLNIMQPFKVYPNGFPEELIQQIEEMTGRKVVANKPASGTQIIDEWGEHQMKTGDLIVYTSADPVLQIAAHED 166
Cdd:pfam01676 65 -GHLEIGGGRIVYQYLGRGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHSHIEHLLALIALAKEAGAIK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 167 IIPLEELYD------ICEKVRELTKDPKYLIGRIIARPYVGEPGNFTRTSNRHDYALKPFGKTVLDHLKDGGYDVIAIGK 240
Cdd:pfam01676 144 VHLLGDGDDrpvgyiLDGDAVITINFRFDRRRARILRLFLLDPDFFDRDRVRHDALHVPTKTLYELKLPSAGAFVPEEGK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 241 INDIYDGEGVT-------EAVR------------------------------------TKSNMDGMDQLMKIVKKDFTgI 277
Cdd:pfam01676 224 NTDGEVLEGHGlkqlriaETEKyahvtffwgggreppfpgeerylipspkvatydlqpEMSAMEITDKLLEALKEKYD-F 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 278 SFLNLVDFDALyGHRRDKPGYAQAIKDFDDRLPELFSNLKEDD-LVIITADHGNDPTAPGTDHTREYIPVIMYSPKFKGG 356
Cdd:pfam01676 303 VFVNFANTDMV-GHTGDVEGKVKAIEAVDERLGELLDALEEDDgLLIITADHGNPEEMKDTDHTREPVPILIYGKGVRPD 381
|
410 420
....*....|....*....|....*..
gi 613365656 357 HALE-----SDTTFSSIGATIADNFNV 378
Cdd:pfam01676 382 QVLFgekfrERGGLADIAATILMLLGL 408
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| deoB |
TIGR01696 |
phosphopentomutase; This protein is involved in the purine and pyrimidine salvage pathway. It ... |
7-386 |
0e+00 |
|
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: 733.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 7 RVHLIVMDSVGIGEAPDAADFKDEGSHTLRHTLEGFD-QTLPNLEKLGLGNIDKLPVVNAVEQPEAYYTKLSEASVGKDT 85
Cdd:TIGR01696 1 RVFLIVMDSVGIGEAPDAADFGDEGAHTLGHIAEACAkLNLPNLTKLGLGKIHEPAGVDGNEEPIAYYAKAHEASSGKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 86 MTGHWEIMGLNIMQPFKVYPNGFPEELIQQIEEMTGRKVVANKPASGTQIIDEWGEHQMKTGDLIVYTSADPVLQIAAHE 165
Cdd:TIGR01696 81 MTGHWEIMGLPILFPFKVFPNGFPQELLQKLEERAGRKYLGNKPASGTVILDELGEEHMKTGKLIVYTSADSVLQIAAHE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 166 DIIPLEELYDICEKVRELTKDPKYLIGRIIARPYVGEPGNFTRTSNRHDYALKPFGKTVLDHLKDGGYDVIAIGKINDIY 245
Cdd:TIGR01696 161 ETFPLEELYEICEIARELTTDPKYNIGRIIARPFVGEPGNFQRTGNRHDYALKPFAPTVLQKLKDEGHDVISIGKIADIY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 246 DGEGVTEAVRTKSNMDGMDQLMKIVKKDFTGISFLNLVDFDALYGHRRDKPGYAQAIKDFDDRLPELFSNLKEDDLVIIT 325
Cdd:TIGR01696 241 DGEGITKKVRTTSNMDGMDATIKEMKEDFTGISFTNLVDFDALWGHRRDVAGYAAALELFDRRLPELFSLLREDDLLIIT 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 613365656 326 ADHGNDPTAPGTDHTREYIPVIMYSPKFKGGHALESDTTFSSIGATIADNFNVTLPEFGKS 386
Cdd:TIGR01696 321 ADHGNDPTWTGTDHTREYIPVLVYSPKVKPGHSLGHRETFADIGATIADNFGTSDPEYGKS 381
|
|
| PRK05362 |
PRK05362 |
phosphopentomutase; Provisional |
5-392 |
0e+00 |
|
phosphopentomutase; Provisional
Pssm-ID: 235430 Cd Length: 394 Bit Score: 725.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 5 FNRVHLIVMDSVGIGEAPDAADFKDEGSHTLRHTLEGF--DQTLPNLEKLGLGNIDK---LPVVNAVEQPEAYYTKLSEA 79
Cdd:PRK05362 1 MKRVFLIVLDSVGIGAAPDAAKFGDEGADTLGHIAEARkgGLKLPNLAKLGLGNIATgtpIAGVPANAEPIGYYGKAQEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 80 SVGKDTMTGHWEIMGLNIMQPFKVYPNGFPEELIQQIEEMTGR-KVVANKPASGTQIIDEWGEHQMKTGDLIVYTSADPV 158
Cdd:PRK05362 81 SSGKDTPTGHWEIMGVPVLFPFGYFPNGFPQELIDEIEERAGRpGILGNKHASGTEIIDELGEEHMKTGKPIVYTSADSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 159 LQIAAHEDIIPLEELYDICEKVRELTKDPKYLIGRIIARPYVGEPGNFTRTSNRHDYALKPFGKTVLDHLKDGGYDVIAI 238
Cdd:PRK05362 161 FQIAAHEEVFGLEELYRICEIAREILLDRPYNVGRVIARPFVGEPGNFTRTGNRHDYALKPPAPTVLDKLKEAGGEVIAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 239 GKINDIYDGEGVTEAVRTKSNMDGMDQLMKIVK-KDFTGISFLNLVDFDALYGHRRDKPGYAQAIKDFDDRLPELFSNLK 317
Cdd:PRK05362 241 GKIADIFAGQGITEKVKTKSNMDGMDATIEEMKeAGDNGLVFTNLVDFDSLYGHRRDVAGYAAALEEFDARLPELLAALK 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 613365656 318 EDDLVIITADHGNDPTAPGTDHTREYIPVIMYSPKFKGGhALESDTTFSSIGATIADNFNVTLPEFGKSYLKELK 392
Cdd:PRK05362 321 EDDLLIITADHGNDPTWPGTDHTREYVPLLVYGPKFKGG-SLGHRETFADIGATIADNFGVEPMEYGKSFLDELK 394
|
|
| DeoB |
COG1015 |
Phosphopentomutase [Carbohydrate transport and metabolism]; |
5-389 |
0e+00 |
|
Phosphopentomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440639 Cd Length: 385 Bit Score: 724.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 5 FNRVHLIVMDSVGIGEAPDAADFKDEGSHTLRHTLE---GFDqtLPNLEKLGLGNIDKLPVVNAVEQPEAYYTKLSEASV 81
Cdd:COG1015 1 MKRAILIVLDSVGIGEAPDAAKFGDEGANTLGHIAEavgGLN--LPNLARLGLGNIAPLAGLPPVEEPLGAYGKMAEVSA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 82 GKDTMTGHWEIMGLNIMQPFKVYPNGFPEELIQQIEEMTGRKVVANKPASGTQIIDEWGEHQMKTGDLIVYTSADPVLQI 161
Cdd:COG1015 79 GKDTTTGHWEIAGLPVEFPFPTFPDGFPEELIDEFEERTGRGVLGNKPASGTEIIEELGEEHMRTGKPIVYTSADSVFQI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 162 AAHEDIIPLEELYDICEKVRELTKDPkYLIGRIIARPYVGEPGNFTRTSNRHDYALKPFGKTVLDHLKDGGYDVIAIGKI 241
Cdd:COG1015 159 AAHEEVFPLEELYRLCEIARELLDGE-YAVGRVIARPFVGEPGNFVRTANRHDYALKPPGPTLLDRLKEAGGDVIAVGKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 242 NDIYDGEGVTEAVRTKSNMDGMDQLMKIVKKDFTGISFLNLVDFDALYGHRRDKPGYAQAIKDFDDRLPELFSNLKEDDL 321
Cdd:COG1015 238 SDIFAGRGITESVKTKGNADGMDKTLEAMDEAFGGLIFTNLVDFDSLYGHRRDVAGYAKALEEFDARLPELLAALRPDDL 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 613365656 322 VIITADHGNDPTAPGTDHTREYIPVIMYSPKFKGGHALESDTTFSSIGATIADNFNVTLPEFGKSYLK 389
Cdd:COG1015 318 LIITADHGNDPTWPGTDHTREYVPLLVYGPGLKPGGNLGTRETFADIGATIADHFGVPPPGHGTSFLS 385
|
|
| PPM |
cd16009 |
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ... |
6-386 |
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: 647.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 6 NRVHLIVMDSVGIGEAPDAADFKDEGSHTLRHTLEGFDQ-TLPNLEKLGLGNIDKLPVVNAVEQPEAYYTKLSEASVGKD 84
Cdd:cd16009 1 KRVILIVLDSFGIGAMPDAAKFGDEGANTLGHIAEAVPGlNLPNLEKLGLGNIVGIEGGPPKENPIAAYGKMREASAGKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 85 TMTGHWEIMGLNIMQPFKVYPNGFPEELIQQIEEMTGRKVVANKPASGTQIIDEWGEHQMKTGDLIVYTSADPVLQIAAH 164
Cdd:cd16009 81 TTTGHWEIMGLKPKKPFPTFPNGFPKELIDEFEKATGRKGLGNKPASGTEIIKELGEEHLKTGAPIVYTSADSVFQIAAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 165 EDIIPLEELYDICEKVRELTkDPKYLIGRIIARPYVGEPG-NFTRTSNRHDYALKPFGKTVLDHLKDGGYDVIAIGKIND 243
Cdd:cd16009 161 EEVIPLEELYRICEIAREIL-DGEYKVGRVIARPFVGETGvYFKRTSNRHDYALVPPGKTVLDILKEAGIPVIGIGKIAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 244 IYDGEGVTEAVRTKSNMDGMDQLMKIVKKDFTGISFLNLVDFDALYGHRRDKPGYAQAIKDFDDRLPELFSNLKEDDLVI 323
Cdd:cd16009 240 IFAGRGITESIHTKSNADGMEKTLEALKEDFNGLIFTNLVDFDMLYGHRRDPEGYAEALEEFDRRLPELLAKLKEDDLLI 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613365656 324 ITADHGNDPTAPGTDHTREYIPVIMYSPKFKGGhALESDTTFSSIGATIADNFNVTLPEFGKS 386
Cdd:cd16009 320 ITADHGNDPTIGGTDHTREYVPLLVYGKGLKGV-NLGTRETFADIGATIADNFGVEPPENGTS 381
|
|
| Metalloenzyme |
pfam01676 |
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ... |
7-378 |
1.96e-61 |
|
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: 203.40 E-value: 1.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 7 RVHLIVMDSVGIGEApdaadfKDEGSHTLRHTLEgfdqtLPNLEKLgLGNIDKLPVVNAVEqpeaYYTKLSEASVGKDTm 86
Cdd:pfam01676 2 KVVLIVLDGWGDRPA------EDLNAKTPLHIAK-----TPNMDKL-AKEYPEQLIGASGL----AVGLPEGQMGGSDV- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 87 tGHWEIMGLNIMQPFKVYPNGFPEELIQQIEEMTGRKVVANKPASGTQIIDEWGEHQMKTGDLIVYTSADPVLQIAAHED 166
Cdd:pfam01676 65 -GHLEIGGGRIVYQYLGRGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHSHIEHLLALIALAKEAGAIK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 167 IIPLEELYD------ICEKVRELTKDPKYLIGRIIARPYVGEPGNFTRTSNRHDYALKPFGKTVLDHLKDGGYDVIAIGK 240
Cdd:pfam01676 144 VHLLGDGDDrpvgyiLDGDAVITINFRFDRRRARILRLFLLDPDFFDRDRVRHDALHVPTKTLYELKLPSAGAFVPEEGK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 241 INDIYDGEGVT-------EAVR------------------------------------TKSNMDGMDQLMKIVKKDFTgI 277
Cdd:pfam01676 224 NTDGEVLEGHGlkqlriaETEKyahvtffwgggreppfpgeerylipspkvatydlqpEMSAMEITDKLLEALKEKYD-F 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 278 SFLNLVDFDALyGHRRDKPGYAQAIKDFDDRLPELFSNLKEDD-LVIITADHGNDPTAPGTDHTREYIPVIMYSPKFKGG 356
Cdd:pfam01676 303 VFVNFANTDMV-GHTGDVEGKVKAIEAVDERLGELLDALEEDDgLLIITADHGNPEEMKDTDHTREPVPILIYGKGVRPD 381
|
410 420
....*....|....*....|....*..
gi 613365656 357 HALE-----SDTTFSSIGATIADNFNV 378
Cdd:pfam01676 382 QVLFgekfrERGGLADIAATILMLLGL 408
|
|
| PRK12383 |
PRK12383 |
putative mutase; Provisional |
7-392 |
5.87e-55 |
|
putative mutase; Provisional
Pssm-ID: 237085 Cd Length: 406 Bit Score: 186.33 E-value: 5.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 7 RVHLIVMDSVGIGEAPDAADFK--DEGSHTLRHTLEGFDQ-TLPNLEKLGLGNIDKLPVVNAVEQPEAYYTKLSEASVGK 83
Cdd:PRK12383 3 RFVVLVIDSFGVGAMKDVTLVRpqDAGANTCGHILSQLPHlQLPTLEKLGLINALGYAPGDMQPSPSATWGVAELQHEGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 84 DTMTGHWEIMGLN----IMQPFKVYPNGFPEELIQQieemtGRKVvaNKPASGTQIIdeWGEHQMKTGDLIvytSADP-- 157
Cdd:PRK12383 83 DTFMGHQEIMGTRplppLRMPFSDVIDRVEQALESA-----GYQV--ERRGDGLQFL--LVNQAVAIGDNL---EADLgq 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 158 VLQIAAHEDIIPLEELYDICEKVRELTKDPKYL--------IGRIIARPYVGEPG----NFTRT-SNRHDYALKPFGKTV 224
Cdd:PRK12383 151 VYNVTANLSVISFDDALKIGRIVREQVQVGRVIvfgglltdSQRILDAAESKEGRfigiNAPKSgVYDNGYQVVHLGYGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 225 lDH-------LKDGGYDVIAIGKINDI--------YDGEGVTEAVrtksnmdgMDQLMKIVKKDFTGISFLNLVDFDaLY 289
Cdd:PRK12383 231 -DPkvqvpqkLYEAGVPVVLVGKVADIvnnpygvsWQNLVDTQRV--------MDITLDEFNTHPTAFICTNIQETD-LA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 290 GHRRDKPGYAQAIKDFDDRLPELFSNLKEDDLVIITADHGNDPTAPGTDHTREYIPVIMYSPKFKGGHaLESDTTFSSIG 369
Cdd:PRK12383 301 GHAEDVARYAERLEVVDRNLARLLEAMTPDDCLVVMADHGNDPTIGHSHHTREVVPLLVYQKGLQATQ-LGVRTTLSDVG 379
|
410 420
....*....|....*....|...
gi 613365656 370 ATIADNFNVTLPEFGKSYLKELK 392
Cdd:PRK12383 380 ATVCEFFGAPPPQNGRSFLSSLR 402
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
200-376 |
6.48e-20 |
|
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: 87.86 E-value: 6.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 200 VGEPGNFTRTSNRHDYALKPFGKTVLDHLKDGGYDVIAIGkindiydgegvteavrtksnmdgMDQLMKIVKKDFTGISF 279
Cdd:cd00016 68 YTGNGSADPELPSRAAGKDEDGPTIPELLKQAGYRTGVIG-----------------------LLKAIDETSKEKPFVLF 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 280 LNLVDFD-ALYGHRRDKPGYAQAIKDFDDRLPELFSNLK-----EDDLVIITADHGNDP----------TAPGTDHTREY 343
Cdd:cd00016 125 LHFDGPDgPGHAYGPNTPEYYDAVEEIDERIGKVLDALKkagdaDDTVIIVTADHGGIDkghggdpkadGKADKSHTGMR 204
|
170 180 190
....*....|....*....|....*....|...
gi 613365656 344 IPVIMYSPKFKGGHALESDTTFSSIGATIADNF 376
Cdd:cd00016 205 VPFIAYGPGVKKGGVKHELISQYDIAPTLADLL 237
|
|
| iPGM_like |
cd16011 |
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate ... |
290-351 |
9.76e-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: 47.08 E-value: 9.76e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613365656 290 GHRRDKPGYAQAIKDFDDRLPELFSNL--KEDDLVIITADHgndPT--APGTdHTREYIPVIMYSP 351
Cdd:cd16011 271 GHDGDPEAKVKAIERIDKAIVGPLLELldGEDFVIVVTPDH---STpcSLKT-HSGDPVPFLIYGP 332
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
221-338 |
1.78e-05 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 46.28 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 221 GKTVLDHLKDGGYDVIAI------------GKINDIYDGEGVTEAVRtKSNMDGMDQLMKIVKKDFTGISFLNLVDFDAl 288
Cdd:COG1524 118 VPTIFERARAAGLTTAAVfwpsfegsglidAARPYPYDGRKPLLGNP-AADRWIAAAALELLREGRPDLLLVYLPDLDY- 195
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 613365656 289 YGHRR--DKPGYAQAIKDFDDRLPELFSNLK-----EDDLVIITADHGNDPTAPGTD 338
Cdd:COG1524 196 AGHRYgpDSPEYRAALREVDAALGRLLDALKarglyEGTLVIVTADHGMVDVPPDID 252
|
|
| ApgM |
COG3635 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type [Carbohydrate ... |
290-351 |
2.21e-05 |
|
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: 46.29 E-value: 2.21e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613365656 290 GHRRDKPGYAQAIKDFDDR-LPELFSNLK--EDDLVIITADHgndPTA-PGTDHTREYIPVIMYSP 351
Cdd:COG3635 302 GHDGDLEEKVKAIERIDRRvVGPLLEGLEkfEDYRILVTPDH---PTPiSLRTHSGDPVPFLIYGP 364
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
298-389 |
3.80e-05 |
|
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: 44.85 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 298 YAQAIKDFDDRLPELFSNLKE----DD-LVIITADHG---NDPTAPGTDHTREY-----IPVIMYSPKFKGGHALESDTT 364
Cdd:cd16148 165 YDAEVRYVDEQIGRLLDKLKElgllEDtLVIVTSDHGeefGEHGLYWGHGSNLYdeqlhVPLIIRWPGKEPGKRVDALVS 244
|
90 100
....*....|....*....|....*..
gi 613365656 365 FSSIGATIADNFNVTLPEF--GKSYLK 389
Cdd:cd16148 245 HIDIAPTLLDLLGVEPPDYsdGRSLLP 271
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
298-390 |
5.41e-05 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 45.03 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 298 YAQAIKDFDDRLPELFSNLKEDD-----LVIITADHGndPTAPGTDHTREY-----IPVIMYSPKFKGGHalESDTTFSS 367
Cdd:COG1368 419 YLNAVRYADQALGEFIEKLKKSGwydntIFVIYGDHG--PRSPGKTDYENPleryrVPLLIYSPGLKKPK--VIDTVGSQ 494
|
90 100
....*....|....*....|....*...
gi 613365656 368 --IGATIADNFNVTLPE---FGKSYLKE 390
Cdd:COG1368 495 idIAPTLLDLLGIDYPSyyaFGRDLLSP 522
|
|
| Enpp |
cd16018 |
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ... |
273-361 |
7.82e-05 |
|
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide pyrophosphatases/phosphodiesterases (ENPPs) hydrolyze 5'-phosphodiester bonds in nucleotides and their derivatives, resulting in the release of 5'-nucleotide monophosphates. ENPPs have multiple physiological roles, including nucleotide recycling, modulation of purinergic receptor signaling, regulation of extracellular pyrophosphate levels, stimulation of cell motility, and possible roles in regulation of insulin receptor (IR) signaling and activity of ecto-kinases. The eukaryotic ENPP family contains at least five members that have different tissue distribution and physiological roles.
Pssm-ID: 293742 [Multi-domain] Cd Length: 267 Bit Score: 44.11 E-value: 7.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 273 DFTGISFlnlVDFDAlYGHR--RDKPGYAQAIKDFDDRLPELFSNLKEDDL-----VIITADHGNDPTA-PGTD-HTREY 343
Cdd:cd16018 158 DLILLYF---EEPDS-AGHKygPDSPEVNEALKRVDRRLGYLIEALKERGLlddtnIIVVSDHGMTDVGtHGYDnELPDM 233
|
90
....*....|....*....
gi 613365656 344 IPVIMYS-PKFKGGHALES 361
Cdd:cd16018 234 RAIFIARgPAFKKGKKLGP 252
|
|
| PRK04024 |
PRK04024 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
243-351 |
1.54e-04 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235203 Cd Length: 412 Bit Score: 43.36 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 243 DIYDGEGVTEAVRTksnmdgmdQLMKIVKK--------DFTgisFLNLVDFDAlYGHRRDKPGYAQAIKDFDDRLPELFS 314
Cdd:PRK04024 265 DVITVEGATGGKDT--------NYMAKAKAavellkeyDFV---LLNIKGTDE-AGHDGDFEGKVEVIEKIDKMLGYILD 332
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 613365656 315 NLKEDDLVI-ITADHgndpTAPGT--DHTREYIPVIMYSP 351
Cdd:PRK04024 333 NLDLDEVYIaVTGDH----STPVEvkDHSGDPVPILIYGP 368
|
|
| ALP |
cd16012 |
Alkaline Phosphatase; Alkaline phosphatases are non-specific membrane-bound ... |
290-357 |
3.18e-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: 42.03 E-value: 3.18e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 613365656 290 GHRRDKPGYAQAIKDFDDRLPELFSNLKEDD--LVIITADHgndptapGTDHTREYIPVIMYSP---KFKGGH 357
Cdd:cd16012 204 GHANDAARAIEETLAFDKAVKVALDFAKKDGdtLVIVTADH-------ETGHTGEDVPVFAYGPgaeLFGGVY 269
|
|
| LTA_synthase |
cd16015 |
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ... |
298-374 |
7.02e-04 |
|
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.
Pssm-ID: 293739 [Multi-domain] Cd Length: 283 Bit Score: 41.13 E-value: 7.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 298 YAQAIKDFDDRLPELFSNLKEDD-----LVIITADHG-----NDPTAPGTDHTREYIPVIMYSPKFKGGhaLESDTTFSS 367
Cdd:cd16015 194 YLNAIHYTDKALGEFIEKLKKSGlyentIIVIYGDHLpslgsDYDETDEDPLDLYRTPLLIYSPGLKKP--KKIDRVGSQ 271
|
....*....
gi 613365656 368 --IGATIAD 374
Cdd:cd16015 272 idIAPTLLD 280
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
292-392 |
5.50e-03 |
|
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) belongs to the sulfatase family and catalyses the cleavage of N-linked sulfate groups from the GAGs heparin sulfate and heparin. The active site is characterized by the amino-acid sequence motif C(X)PSR that is highly conserved among most sulfatases. The cysteine residue is post-translationally converted to a formylglycine (FGly) residue, which is crucial for the catalytic process. Loss of function of SGSH results a disease called mucopolysaccharidosis type IIIA (Sanfilippo A syndrome), a fatal childhood-onset neurodegenerative disease with mild facial, visceral and skeletal abnormalities.
Pssm-ID: 293751 [Multi-domain] Cd Length: 373 Bit Score: 38.64 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613365656 292 RRDKPGYAQAIKDFDDRLPELFSNLKEDDL-----VIITADHGND-PTAPGT--DH-TReyIPVIMYSP-KFKGGHALES 361
Cdd:cd16027 185 REDLADYYDEIERLDQQVGEILDELEEDGLldntiVIFTSDHGMPfPRAKGTlyDSgLR--VPLIVRWPgKIKPGSVSDA 262
|
90 100 110
....*....|....*....|....*....|...
gi 613365656 362 DTTFSSIGATIADNFNVTLPEF--GKSYLKELK 392
Cdd:cd16027 263 LVSFIDLAPTLLDLAGIEPPEYlqGRSFLPLLK 295
|
|
| GpmI |
COG0696 |
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ... |
322-372 |
8.87e-03 |
|
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: 38.11 E-value: 8.87e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 613365656 322 VIITADHGN-----DPTA--PGTDHTREYIPVIMYSPkfKGGHALESDTTFSSIGATI 372
Cdd:COG0696 436 LLITADHGNaeqmiDPDTggPHTAHTTNPVPFILVGG--DKGVKLREDGRLADIAPTI 491
|
|
| |
