|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05434 |
PRK05434 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
4-512 |
0e+00 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235463 Cd Length: 507 Bit Score: 983.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 4 SKKPMVLVILDGYGYREEQQDNAIFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDLTR 83
Cdd:PRK05434 3 MKKPVVLIILDGWGYREETEGNAIALAKTPNLDRLWANYPHTLLSASGLAVGLPDGQMGNSEVGHLNIGAGRIVYQDLTR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 84 LDVEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRSAE 163
Cdd:PRK05434 83 INKAIEDGSFFENPALLDAIDKAKKNGGALHLMGLLSDGGVHSHIDHLFALLELAKEEGVKKVYVHAFLDGRDTPPKSAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 164 SSLKKFEEKFAALGKGRVASIIGRYYAMDRDNRWDRVEKAYDLLTLAQGEFQADTAVAGLQAAYARDENDEFVKATVIra 243
Cdd:PRK05434 163 GYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVLGEGPFTAESAVEALEASYARGETDEFVKPTVI-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 244 EGQPDAAMEDGDALIFMNFRADRAREITRAFVNADFDGFARkKVVNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWMAK 323
Cdd:PRK05434 241 GGEPVAGIEDGDAVIFFNFRADRARQITRAFTDPDFDGFDR-VPKLLNFVTMTQYDADLKVPVAFPPESLKNTLGEVLAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 324 NDKTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKSGKYDTIICNYPNGD 403
Cdd:PRK05434 320 AGLTQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIILNFANPD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 404 MVGHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDPATGQAHTAHTNLPVPLIYVGDKNVKAvEG 483
Cdd:PRK05434 400 MVGHTGNLEAAVKAVEAVDECLGRVVDAVLKVGGTLLITADHGNAEQMIDPETGQPHTAHTTNPVPFILVGGKALRL-EG 478
|
490 500
....*....|....*....|....*....
gi 485719030 484 GKLSDIAPTMLSLMGMEIPQEMTGKPLFI 512
Cdd:PRK05434 479 GKLADIAPTILDLLGLEQPAEMTGKSLIE 507
|
|
| GpmI |
COG0696 |
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ... |
4-512 |
0e+00 |
|
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: 972.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 4 SKKPMVLVILDGYGYREEQQDNAIFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDLTR 83
Cdd:COG0696 1 RKKPVVLIILDGWGIREETEGNAIALANTPNLDRLWATYPHTLLRASGEAVGLPDGQMGNSEVGHLNIGAGRVVYQDLTR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 84 LDVEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRSAE 163
Cdd:COG0696 81 INKAIEDGSFFENPVLLDAIDKAKENGGALHLMGLLSDGGVHSHIDHLKALLELAKEEGVKKVYVHAFLDGRDTPPKSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 164 SSLKKFEEKFAALGKGRVASIIGRYYAMDRDNRWDRVEKAYDLLTLAQGEfQADTAVAGLQAAYARDENDEFVKATVIRA 243
Cdd:COG0696 161 GYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVNGEGE-TAASAVEAIEASYARGETDEFVKPTVIVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 244 EGQPDAAMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKV-VNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWMA 322
Cdd:COG0696 240 YGKPVATIEDGDAVIFFNFRADRARQLTRAFTDPDFDGFDRGKRpKLLYFVTMTEYDETFDVPVAFPPENLKNTLGEVLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 323 KNDKTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKSGKYDTIICNYPNG 402
Cdd:COG0696 320 KAGLKQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIVLNFANP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 403 DMVGHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDPATGQAHTAHTNLPVPLIYVG-DKNVKAV 481
Cdd:COG0696 400 DMVGHTGVLEAAIKAVEAVDECLGRVVDAVLAAGGTLLITADHGNAEQMIDPDTGGPHTAHTTNPVPFILVGgDKGVKLR 479
|
490 500 510
....*....|....*....|....*....|.
gi 485719030 482 EGGKLSDIAPTMLSLMGMEIPQEMTGKPLFI 512
Cdd:COG0696 480 EDGRLADIAPTILELMGLPQPAEMTGKSLIE 510
|
|
| iPGM |
cd16010 |
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
6-510 |
0e+00 |
|
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: 900.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 6 KPMVLVILDGYGYREEQQDNAIFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDLTRLD 85
Cdd:cd16010 1 KPVVLIILDGWGIRPEDEGNAIALAKTPNLDRLWATYPHTLLKASGEAVGLPDGQMGNSEVGHLNIGAGRIVYQDLTRIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 86 VEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRSAESS 165
Cdd:cd16010 81 KAIEDGSFFKNEALLKAIEHAKKNNSTLHLMGLLSDGGVHSHIDHLFALLELAKKEGVKKVYVHAFTDGRDTPPKSALKY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 166 LKKFEEKFAALGKGRVASIIGRYYAMDRDNRWDRVEKAYDLLTLAQGEfQADTAVAGLQAAYARDENDEFVKATVIRAEG 245
Cdd:cd16010 161 LKELEEKLKELGVGKIASVSGRYYAMDRDKRWDRTEKAYDALVLGEGE-KAESAEEAIEASYAKGITDEFIPPTVIGDEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 246 QPdaaMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKVVNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWMAKND 325
Cdd:cd16010 240 GT---IKDGDAVIFFNFRADRARQITRAFTDPDFDGFDRKKPKNLYFVTMTEYDKDLPVPVAFPPPKIKNTLGEVLSKAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 326 KTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKSGKYDTIICNYPNGDMV 405
Cdd:cd16010 317 LKQLRIAETEKYAHVTYFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLIEAIKSGKYDFIVVNFANPDMV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 406 GHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDPATGQAHTAHTNLPVPLIYVG-DKNVKAVEGG 484
Cdd:cd16010 397 GHTGNLEAAVKAVEAVDECLGRIVEAVLENGGTLLITADHGNAEEMIDPETGGPHTAHTTNPVPFIIVDpGLKRKLLKDG 476
|
490 500
....*....|....*....|....*.
gi 485719030 485 KLSDIAPTMLSLMGMEIPQEMTGKPL 510
Cdd:cd16010 477 GLADVAPTILDLLGIEKPKEMTGKSL 502
|
|
| pgm_bpd_ind |
TIGR01307 |
phosphoglycerate mutase (2,3-diphosphoglycerate-independent); This protein is about double in ... |
6-511 |
0e+00 |
|
phosphoglycerate mutase (2,3-diphosphoglycerate-independent); This protein is about double in length of, and devoid of homology to the form of phosphoglycerate mutase that uses 2,3-bisphosphoglycerate as a cofactor. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 130374 [Multi-domain] Cd Length: 501 Bit Score: 881.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 6 KPMVLVILDGYGYREEQQDNAIFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDLTRLD 85
Cdd:TIGR01307 1 KKVVLVILDGWGYRNDDDGNAIFAAKTPTMDELIAAYPYSLLDASGLDVGLPDGQMGNSEVGHLNIGAGRVVYQDLVRIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 86 VEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRSAESS 165
Cdd:TIGR01307 81 QAIKDGEFFANPALLGAIDRAKDNNGKLHLMGLVSDGGVHSHIDHLIALIELAAERGIEKVVLHAFTDGRDTAPKSAESY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 166 LKKFEEKFAALGKGRVASIIGRYYAMDRDNRWDRVEKAYDLLTLAQGeFQADTAVAGLQAAYARDENDEFVKATVIRAEG 245
Cdd:TIGR01307 161 LEQLQAFLKEIGNGRIATISGRYYAMDRDQRWDRVEIAYKAITGGDG-FEFSDPVAYIQDAYARDITDEFIKPTIIGNGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 246 qpdaAMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKVVNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWMAKND 325
Cdd:TIGR01307 240 ----ALKDGDAVIFFNFRADRAREITRALVNSDFDGFPREKNPKLDFVTMTQYDGTFPSPVAFPPQSLTNTLGEVLAKHD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 326 KTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKSGKYDTIICNYPNGDMV 405
Cdd:TIGR01307 316 LTQLRIAETEKYAHVTFFFNGGVEVPFAGETRTLIPSPKVATYDLQPEMSAKAVTDAVLEAIAQGKFDLIVVNFANPDMV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 406 GHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDPAtGQAHTAHTNLPVPLIYVGDKNVKAV-EGG 484
Cdd:TIGR01307 396 GHTGNFEAAIKAVEALDVCLGRIVEACKKVGGTLFLTADHGNAEEMIDEN-GNPHTAHTTNPVPFVCVGAKNVKLIrEGG 474
|
490 500
....*....|....*....|....*..
gi 485719030 485 KLSDIAPTMLSLMGMEIPQEMTGKPLF 511
Cdd:TIGR01307 475 VLADIAPTILDLMGLEQPAEMTGKSLL 501
|
|
| Metalloenzyme |
pfam01676 |
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ... |
6-501 |
4.63e-151 |
|
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: 437.99 E-value: 4.63e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 6 KPMVLVILDGYGYREEQQDNA---IFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDLT 82
Cdd:pfam01676 1 KKVVLIVLDGWGDRPAEDLNAktpLHIAKTPNMDKLAKEYPEQLIGASGLAVGLPEGQMGGSDVGHLEIGGGRIVYQYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 83 RLDVEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPrsa 162
Cdd:pfam01676 81 RGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHSHIEHLLALIALAKEAGAIKVHLLGDGDDRPVGY--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 163 esslkkfeekfaalgkgrvasiigryyamdrdnrwdrvekaydlltlaqgefqadtavaglqaayardendefvkatvir 242
Cdd:pfam01676 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 243 aegqpdAAMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKVVNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWMA 322
Cdd:pfam01676 158 ------ILDGDAVITINFRFDRRRARILRLFLLDPDFFDRDRVRHDALHVPTKTLYELKLPSAGAFVPEEGKNTDGEVLE 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 323 KNDKTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKsGKYDTIICNYPNG 402
Cdd:pfam01676 232 GHGLKQLRIAETEKYAHVTFFWGGGREPPFPGEERYLIPSPKVATYDLQPEMSAMEITDKLLEALK-EKYDFVFVNFANT 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 403 DMVGHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDpatgqahTAHTNLPVPLIYVGDK------ 476
Cdd:pfam01676 311 DMVGHTGDVEGKVKAIEAVDERLGELLDALEEDDGLLIITADHGNPEEMKD-------TDHTREPVPILIYGKGvrpdqv 383
|
490 500
....*....|....*....|....*..
gi 485719030 477 --NVKAVEGGKLSDIAPTMLSLMGMEI 501
Cdd:pfam01676 384 lfGEKFRERGGLADIAATILMLLGLKK 410
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05434 |
PRK05434 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
4-512 |
0e+00 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235463 Cd Length: 507 Bit Score: 983.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 4 SKKPMVLVILDGYGYREEQQDNAIFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDLTR 83
Cdd:PRK05434 3 MKKPVVLIILDGWGYREETEGNAIALAKTPNLDRLWANYPHTLLSASGLAVGLPDGQMGNSEVGHLNIGAGRIVYQDLTR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 84 LDVEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRSAE 163
Cdd:PRK05434 83 INKAIEDGSFFENPALLDAIDKAKKNGGALHLMGLLSDGGVHSHIDHLFALLELAKEEGVKKVYVHAFLDGRDTPPKSAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 164 SSLKKFEEKFAALGKGRVASIIGRYYAMDRDNRWDRVEKAYDLLTLAQGEFQADTAVAGLQAAYARDENDEFVKATVIra 243
Cdd:PRK05434 163 GYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVLGEGPFTAESAVEALEASYARGETDEFVKPTVI-- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 244 EGQPDAAMEDGDALIFMNFRADRAREITRAFVNADFDGFARkKVVNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWMAK 323
Cdd:PRK05434 241 GGEPVAGIEDGDAVIFFNFRADRARQITRAFTDPDFDGFDR-VPKLLNFVTMTQYDADLKVPVAFPPESLKNTLGEVLAK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 324 NDKTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKSGKYDTIICNYPNGD 403
Cdd:PRK05434 320 AGLTQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIILNFANPD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 404 MVGHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDPATGQAHTAHTNLPVPLIYVGDKNVKAvEG 483
Cdd:PRK05434 400 MVGHTGNLEAAVKAVEAVDECLGRVVDAVLKVGGTLLITADHGNAEQMIDPETGQPHTAHTTNPVPFILVGGKALRL-EG 478
|
490 500
....*....|....*....|....*....
gi 485719030 484 GKLSDIAPTMLSLMGMEIPQEMTGKPLFI 512
Cdd:PRK05434 479 GKLADIAPTILDLLGLEQPAEMTGKSLIE 507
|
|
| GpmI |
COG0696 |
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ... |
4-512 |
0e+00 |
|
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: 972.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 4 SKKPMVLVILDGYGYREEQQDNAIFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDLTR 83
Cdd:COG0696 1 RKKPVVLIILDGWGIREETEGNAIALANTPNLDRLWATYPHTLLRASGEAVGLPDGQMGNSEVGHLNIGAGRVVYQDLTR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 84 LDVEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRSAE 163
Cdd:COG0696 81 INKAIEDGSFFENPVLLDAIDKAKENGGALHLMGLLSDGGVHSHIDHLKALLELAKEEGVKKVYVHAFLDGRDTPPKSAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 164 SSLKKFEEKFAALGKGRVASIIGRYYAMDRDNRWDRVEKAYDLLTLAQGEfQADTAVAGLQAAYARDENDEFVKATVIRA 243
Cdd:COG0696 161 GYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVNGEGE-TAASAVEAIEASYARGETDEFVKPTVIVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 244 EGQPDAAMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKV-VNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWMA 322
Cdd:COG0696 240 YGKPVATIEDGDAVIFFNFRADRARQLTRAFTDPDFDGFDRGKRpKLLYFVTMTEYDETFDVPVAFPPENLKNTLGEVLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 323 KNDKTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKSGKYDTIICNYPNG 402
Cdd:COG0696 320 KAGLKQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIVLNFANP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 403 DMVGHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDPATGQAHTAHTNLPVPLIYVG-DKNVKAV 481
Cdd:COG0696 400 DMVGHTGVLEAAIKAVEAVDECLGRVVDAVLAAGGTLLITADHGNAEQMIDPDTGGPHTAHTTNPVPFILVGgDKGVKLR 479
|
490 500 510
....*....|....*....|....*....|.
gi 485719030 482 EGGKLSDIAPTMLSLMGMEIPQEMTGKPLFI 512
Cdd:COG0696 480 EDGRLADIAPTILELMGLPQPAEMTGKSLIE 510
|
|
| iPGM |
cd16010 |
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
6-510 |
0e+00 |
|
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: 900.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 6 KPMVLVILDGYGYREEQQDNAIFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDLTRLD 85
Cdd:cd16010 1 KPVVLIILDGWGIRPEDEGNAIALAKTPNLDRLWATYPHTLLKASGEAVGLPDGQMGNSEVGHLNIGAGRIVYQDLTRIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 86 VEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRSAESS 165
Cdd:cd16010 81 KAIEDGSFFKNEALLKAIEHAKKNNSTLHLMGLLSDGGVHSHIDHLFALLELAKKEGVKKVYVHAFTDGRDTPPKSALKY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 166 LKKFEEKFAALGKGRVASIIGRYYAMDRDNRWDRVEKAYDLLTLAQGEfQADTAVAGLQAAYARDENDEFVKATVIRAEG 245
Cdd:cd16010 161 LKELEEKLKELGVGKIASVSGRYYAMDRDKRWDRTEKAYDALVLGEGE-KAESAEEAIEASYAKGITDEFIPPTVIGDEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 246 QPdaaMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKVVNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWMAKND 325
Cdd:cd16010 240 GT---IKDGDAVIFFNFRADRARQITRAFTDPDFDGFDRKKPKNLYFVTMTEYDKDLPVPVAFPPPKIKNTLGEVLSKAG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 326 KTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKSGKYDTIICNYPNGDMV 405
Cdd:cd16010 317 LKQLRIAETEKYAHVTYFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLIEAIKSGKYDFIVVNFANPDMV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 406 GHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDPATGQAHTAHTNLPVPLIYVG-DKNVKAVEGG 484
Cdd:cd16010 397 GHTGNLEAAVKAVEAVDECLGRIVEAVLENGGTLLITADHGNAEEMIDPETGGPHTAHTTNPVPFIIVDpGLKRKLLKDG 476
|
490 500
....*....|....*....|....*.
gi 485719030 485 KLSDIAPTMLSLMGMEIPQEMTGKPL 510
Cdd:cd16010 477 GLADVAPTILDLLGIEKPKEMTGKSL 502
|
|
| pgm_bpd_ind |
TIGR01307 |
phosphoglycerate mutase (2,3-diphosphoglycerate-independent); This protein is about double in ... |
6-511 |
0e+00 |
|
phosphoglycerate mutase (2,3-diphosphoglycerate-independent); This protein is about double in length of, and devoid of homology to the form of phosphoglycerate mutase that uses 2,3-bisphosphoglycerate as a cofactor. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 130374 [Multi-domain] Cd Length: 501 Bit Score: 881.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 6 KPMVLVILDGYGYREEQQDNAIFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDLTRLD 85
Cdd:TIGR01307 1 KKVVLVILDGWGYRNDDDGNAIFAAKTPTMDELIAAYPYSLLDASGLDVGLPDGQMGNSEVGHLNIGAGRVVYQDLVRIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 86 VEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRSAESS 165
Cdd:TIGR01307 81 QAIKDGEFFANPALLGAIDRAKDNNGKLHLMGLVSDGGVHSHIDHLIALIELAAERGIEKVVLHAFTDGRDTAPKSAESY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 166 LKKFEEKFAALGKGRVASIIGRYYAMDRDNRWDRVEKAYDLLTLAQGeFQADTAVAGLQAAYARDENDEFVKATVIRAEG 245
Cdd:TIGR01307 161 LEQLQAFLKEIGNGRIATISGRYYAMDRDQRWDRVEIAYKAITGGDG-FEFSDPVAYIQDAYARDITDEFIKPTIIGNGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 246 qpdaAMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKVVNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWMAKND 325
Cdd:TIGR01307 240 ----ALKDGDAVIFFNFRADRAREITRALVNSDFDGFPREKNPKLDFVTMTQYDGTFPSPVAFPPQSLTNTLGEVLAKHD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 326 KTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKSGKYDTIICNYPNGDMV 405
Cdd:TIGR01307 316 LTQLRIAETEKYAHVTFFFNGGVEVPFAGETRTLIPSPKVATYDLQPEMSAKAVTDAVLEAIAQGKFDLIVVNFANPDMV 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 406 GHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDPAtGQAHTAHTNLPVPLIYVGDKNVKAV-EGG 484
Cdd:TIGR01307 396 GHTGNFEAAIKAVEALDVCLGRIVEACKKVGGTLFLTADHGNAEEMIDEN-GNPHTAHTTNPVPFVCVGAKNVKLIrEGG 474
|
490 500
....*....|....*....|....*..
gi 485719030 485 KLSDIAPTMLSLMGMEIPQEMTGKPLF 511
Cdd:TIGR01307 475 VLADIAPTILDLMGLEQPAEMTGKSLL 501
|
|
| Metalloenzyme |
pfam01676 |
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ... |
6-501 |
4.63e-151 |
|
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: 437.99 E-value: 4.63e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 6 KPMVLVILDGYGYREEQQDNA---IFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDLT 82
Cdd:pfam01676 1 KKVVLIVLDGWGDRPAEDLNAktpLHIAKTPNMDKLAKEYPEQLIGASGLAVGLPEGQMGGSDVGHLEIGGGRIVYQYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 83 RLDVEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPrsa 162
Cdd:pfam01676 81 RGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHSHIEHLLALIALAKEAGAIKVHLLGDGDDRPVGY--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 163 esslkkfeekfaalgkgrvasiigryyamdrdnrwdrvekaydlltlaqgefqadtavaglqaayardendefvkatvir 242
Cdd:pfam01676 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 243 aegqpdAAMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKVVNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWMA 322
Cdd:pfam01676 158 ------ILDGDAVITINFRFDRRRARILRLFLLDPDFFDRDRVRHDALHVPTKTLYELKLPSAGAFVPEEGKNTDGEVLE 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 323 KNDKTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKsGKYDTIICNYPNG 402
Cdd:pfam01676 232 GHGLKQLRIAETEKYAHVTFFWGGGREPPFPGEERYLIPSPKVATYDLQPEMSAMEITDKLLEALK-EKYDFVFVNFANT 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 403 DMVGHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDpatgqahTAHTNLPVPLIYVGDK------ 476
Cdd:pfam01676 311 DMVGHTGDVEGKVKAIEAVDERLGELLDALEEDDGLLIITADHGNPEEMKD-------TDHTREPVPILIYGKGvrpdqv 383
|
490 500
....*....|....*....|....*..
gi 485719030 477 --NVKAVEGGKLSDIAPTMLSLMGMEI 501
Cdd:pfam01676 384 lfGEKFRERGGLADIAATILMLLGLKK 410
|
|
| PLN02538 |
PLN02538 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase |
5-505 |
1.74e-128 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
Pssm-ID: 215295 Cd Length: 558 Bit Score: 385.57 E-value: 1.74e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 5 KKPMVLVILDGYGYREEQQDNAIFSAKTPVMDALWANRPHT--LIDASGLEVGLP-DRQMGNSEVGHVNLGAGRIVYQDL 81
Cdd:PLN02538 20 GKPLLLIVLDGWGENAPDEFNAIHVAPTPTMDSLKAGAPERwrLVKAHGTAVGLPsDDDMGNSEVGHNALGAGRIFAQGA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 82 TRLDVEIKDRAFFANPVLTGAvdKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRS 161
Cdd:PLN02538 100 KLVDLALASGKIFEGEGFKYI--KEAFATGTLHLIGLLSDGGVHSRLDQLQLLLKGAAERGAKRIRVHVLTDGRDVPDGS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 162 AESSLKKFEEKFAAL-GKG---RVASIIGRYY-AMDR-DNRWDRVEKAYD--LLTLAQGEFQ-ADTAVAGLQAAyARDEN 232
Cdd:PLN02538 178 SVGFVETLEKDLAELrEKGcdaRIASGGGRMYvTMDRyENDWNVVKRGWDahVLGEAPHKFKsALEAVKKLREE-PPPAN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 233 DEFVKATVI-RAEGQPDAAMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKVVNVDFVMLTEYAADIKTAVAY--P 309
Cdd:PLN02538 257 DQYLPPFVIvDEDGKPVGPIEDGDAVVTFNFRADRMVMIAKALEYEDFDKFDRVRVPKIRYAGMLQYDGELKLPSHYlvS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 310 PASLVNTFGEWMAKNDKTQLRISETEKYAHVTFFFNGGVEESF--KGEDRILINSPKVATYDLQPEMSSAELTEKLVAAI 387
Cdd:PLN02538 337 PPLIERTSGEYLVANGVRTFACSETVKFGHVTFFWNGNRSGYFneKLEEYVEIPSDNGIPFNVQPKMKALEIAEKARDAL 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 388 KSGKYDTIICNYPNGDMVGHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQM--RD----PATG---- 457
Cdd:PLN02538 417 LSGKFDQVRVNLANGDMVGHTGDLEATIVACEAVDAAVKEILDAVEQVGGIYLVTADHGNAEDMvkRDksgkPLLDkdgn 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 485719030 458 -QAHTAHTNLPVPLIYVG---DKNVK---AVEGGKLSDIAPTMLSLMGMEIPQEM 505
Cdd:PLN02538 497 pQILTSHTLAPVPVAIGGpglPPGVRfrdDLPTAGLANVAATVMNLHGFEAPADY 551
|
|
| iPGM_N |
pfam06415 |
BPG-independent PGAM N-terminus (iPGM_N); This family represents the N-terminal region of the ... |
85-300 |
3.64e-128 |
|
BPG-independent PGAM N-terminus (iPGM_N); This family represents the N-terminal region of the 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (or phosphoglyceromutase or BPG-independent PGAM) protein (EC:5.4.2.1). The family is found in conjunction with pfam01676 (located in the C-terminal region of the protein).
Pssm-ID: 461901 Cd Length: 217 Bit Score: 372.12 E-value: 3.64e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 85 DVEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRSAES 164
Cdd:pfam06415 2 NKAIEDGSFFENPALLKAIENAKANGGALHLMGLLSDGGVHSHIDHLFALLELAKEEGVKKVYVHAFLDGRDTPPKSALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 165 SLKKFEEKFAALGKGRVASIIGRYYAMDRDNRWDRVEKAYDLLTLAQGEFqADTAVAGLQAAYARDENDEFVKATVIRAE 244
Cdd:pfam06415 82 YLEQLEAKLAELGVGKIATVSGRYYAMDRDKRWDRVEKAYDALVLGEGES-AADAVEAIEASYARGETDEFVKPTVIVDD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 485719030 245 GQPDAAMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKVV-NVDFVMLTEYAA 300
Cdd:pfam06415 161 GKPVGTIKDGDSVIFFNFRPDRAREITRAFTDPDFDGFERRKRPkDLHFVTMTQYDA 217
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
390-497 |
7.52e-08 |
|
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: 53.19 E-value: 7.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 390 GKYDTIICNYPNGDMVGHT--GVMEAAVKAVEALDHCVEEVAKAVESVG----GQLLITADHGNAEQ---MRDPATGQAH 460
Cdd:cd00016 118 EKPFVLFLHFDGPDGPGHAygPNTPEYYDAVEEIDERIGKVLDALKKAGdaddTVIIVTADHGGIDKghgGDPKADGKAD 197
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 485719030 461 TAHTNLPVPLIYVGD---KNVKAVEGGKLSDIAPTMLSLM 497
Cdd:cd00016 198 KSHTGMRVPFIAYGPgvkKGGVKHELISQYDIAPTLADLL 237
|
|
| PRK12383 |
PRK12383 |
putative mutase; Provisional |
371-503 |
5.29e-07 |
|
putative mutase; Provisional
Pssm-ID: 237085 Cd Length: 406 Bit Score: 51.89 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 371 QPEMSSAELTEKLVAAIKSGKYDTIICNYPNGDMVGHTGVMEAAVKAVEALDHCVEEVAKAVESvGGQLLITADHGNaeq 450
Cdd:PRK12383 266 QNLVDTQRVMDITLDEFNTHPTAFICTNIQETDLAGHAEDVARYAERLEVVDRNLARLLEAMTP-DDCLVVMADHGN--- 341
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 485719030 451 mrDPATGqaHTAHTNLPVPLIYVGdKNVKAVEGGK---LSDIAPTMLSLMGMEIPQ 503
Cdd:PRK12383 342 --DPTIG--HSHHTREVVPLLVYQ-KGLQATQLGVrttLSDVGATVCEFFGAPPPQ 392
|
|
| PPM |
cd16009 |
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ... |
439-506 |
1.83e-06 |
|
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: 50.14 E-value: 1.83e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 485719030 439 LLITADHGNaeqmrDPATGqaHTAHTNLPVPLIYVGdKNVKAVEGGK---LSDIAPTMLSLMGMEIPQEMT 506
Cdd:cd16009 318 LIITADHGN-----DPTIG--GTDHTREYVPLLVYG-KGLKGVNLGTretFADIGATIADNFGVEPPENGT 380
|
|
| sulfatase_like |
cd16037 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
418-511 |
1.60e-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: 293760 [Multi-domain] Cd Length: 321 Bit Score: 46.77 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 418 VEALDHCVEEVAKAVESVG----GQLLITADHGnaEQMRDPATGQAHT-----AHtnlpVPLIYVGDKnvkaVEGGK--- 485
Cdd:cd16037 168 VEFLDENIGRVLDALEELGlldnTLIIYTSDHG--DMLGERGLWGKSTmyeesVR----VPMIISGPG----IPAGKrvk 237
|
90 100 110
....*....|....*....|....*....|
gi 485719030 486 ----LSDIAPTMLSLMGMEIPQEMTGKPLF 511
Cdd:cd16037 238 tpvsLVDLAPTILEAAGAPPPPDLDGRSLL 267
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
375-446 |
3.58e-05 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 45.89 E-value: 3.58e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 485719030 375 SSAELTEKLVAAIKSGKYDTIICNYPNGDMVGH-TGVM-EAAVKAVEALDHCVEEVAKAVESVGG----QLLITADHG 446
Cdd:COG1524 166 ADRWIAAAALELLREGRPDLLLVYLPDLDYAGHrYGPDsPEYRAALREVDAALGRLLDALKARGLyegtLVIVTADHG 243
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
421-511 |
1.13e-04 |
|
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: 44.08 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 421 LDHCVEEVAKAVESVGgqLL------ITADHGnaEQM--RDPATGQAHTAH-TNLPVPL-IYVGDKNVKAVEGGKLS--D 488
Cdd:cd16148 172 VDEQIGRLLDKLKELG--LLedtlviVTSDHG--EEFgeHGLYWGHGSNLYdEQLHVPLiIRWPGKEPGKRVDALVShiD 247
|
90 100
....*....|....*....|...
gi 485719030 489 IAPTMLSLMGMEIPQEMTGKPLF 511
Cdd:cd16148 248 IAPTLLDLLGVEPPDYSDGRSLL 270
|
|
| SGSH |
cd16027 |
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ... |
417-511 |
1.44e-04 |
|
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: 44.04 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 417 AVEALDHCVEEVAKAVESVGgqLL------ITADHGNAeQMR------DPATGqahtahtnlpVPLIYVGDKNVKAvegG 484
Cdd:cd16027 194 EIERLDQQVGEILDELEEDG--LLdntiviFTSDHGMP-FPRakgtlyDSGLR----------VPLIVRWPGKIKP---G 257
|
90 100 110
....*....|....*....|....*....|....
gi 485719030 485 KLS-------DIAPTMLSLMGMEIPQEMTGKPLF 511
Cdd:cd16027 258 SVSdalvsfiDLAPTLLDLAGIEPPEYLQGRSFL 291
|
|
| GPI_EPT_2 |
cd16024 |
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ... |
403-510 |
1.53e-04 |
|
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.
Pssm-ID: 293748 [Multi-domain] Cd Length: 274 Bit Score: 43.71 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 403 DMVGHTG---VMEAAVKAVEaLDHCVEEVAKAVESVGGQ----LLITADHGnaeqMRDPAT-GQAHTAHTNlpVPLIYVG 474
Cdd:cd16024 156 DHIGHLEgpkSPLMPPKLKE-MDDVIKRIYESLEEQSSNnptlLVVCGDHG----MTDAGNhGGSSPGETS--VPLLFIS 228
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 485719030 475 ----DKNVKAVEGGKLS------DIAPTMLSLMGMEIPQEMTGKPL 510
Cdd:cd16024 229 pkfsSKPSNADGELSYYetvqqvDLAPTLALLLGLPIPKNSVGVLI 274
|
|
| PRK04024 |
PRK04024 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
381-498 |
2.86e-04 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235203 Cd Length: 412 Bit Score: 43.36 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 381 EKLVAAIKsgKYDTIICNYPNGDMVGHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDpatgqah 460
Cdd:PRK04024 285 KAAVELLK--EYDFVLLNIKGTDEAGHDGDFEGKVEVIEKIDKMLGYILDNLDLDEVYIAVTGDHSTPVEVKD------- 355
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 485719030 461 taHTNLPVP-LIYVGDKNVKAVE---------GG----KLSDIAPTMLSLMG 498
Cdd:PRK04024 356 --HSGDPVPiLIYGPGVRVDDVEkfnelsaakGGlgriRGLDVMPILLDLMN 405
|
|
| PRK05362 |
PRK05362 |
phosphopentomutase; Provisional |
375-511 |
4.79e-04 |
|
phosphopentomutase; Provisional
Pssm-ID: 235430 Cd Length: 394 Bit Score: 42.41 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 375 SSAELTEKLVAAIKSGKYDTII-CNYPNGDMV-GHTGVMEAAVKAVEALDHCVEEVAKAVESvGGQLLITADHGNaeqmr 452
Cdd:PRK05362 260 SNMDGMDATIEEMKEAGDNGLVfTNLVDFDSLyGHRRDVAGYAAALEEFDARLPELLAALKE-DDLLIITADHGN----- 333
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 485719030 453 DPAT-GqahTAHTNLPVPLIYVGdKNVKAVEGGK---LSDIAPTMLSLMGMEIPqeMTGKPLF 511
Cdd:PRK05362 334 DPTWpG---TDHTREYVPLLVYG-PKFKGGSLGHretFADIGATIADNFGVEPM--EYGKSFL 390
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
417-508 |
6.09e-04 |
|
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: 293758 [Multi-domain] Cd Length: 399 Bit Score: 42.17 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 417 AVEALDHCVEEVAKAVESVGgqLL------ITADHGnaEQMrdpatGQAHTAHTNLP------VPLIyVGDKnvKAVEGG 484
Cdd:cd16034 232 MITALDDNIGRLLDALKELG--LLentivvFTSDHG--DML-----GSHGLMNKQVPyeesirVPFI-IRYP--GKIKAG 299
|
90 100 110
....*....|....*....|....*....|.
gi 485719030 485 KLS-------DIAPTMLSLMGMEIPQEMTGK 508
Cdd:cd16034 300 RVVdllintvDIMPTLLGLCGLPIPDTVEGR 330
|
|
| iPGM_like |
cd16011 |
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate ... |
379-474 |
1.68e-03 |
|
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: 40.53 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 379 LTEKLVAAIKS-GKYDTIICNYPNGDMVGHTGVMEAAVKAVEALDHCVeeVAKAVESVGGQ---LLITADHgnaeqmRDP 454
Cdd:cd16011 243 YEGKAEAALEAlKDYDFVFVHVKAPDEAGHDGDPEAKVKAIERIDKAI--VGPLLELLDGEdfvIVVTPDH------STP 314
|
90 100
....*....|....*....|
gi 485719030 455 ATGQAHTAHtnlPVPLIYVG 474
Cdd:cd16011 315 CSLKTHSGD---PVPFLIYG 331
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
417-510 |
3.11e-03 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 39.86 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 417 AVEALDHCVEEVAKAVESvGGQL-----LITADHGnaEQMRDPA-TGQAHTAH---TNlpVPLIYVGDKNVKAvegGKLS 487
Cdd:COG3119 205 MIEEVDDQVGRLLDALEE-LGLAdntivVFTSDNG--PSLGEHGlRGGKGTLYeggIR--VPLIVRWPGKIKA---GSVS 276
|
90 100 110
....*....|....*....|....*....|
gi 485719030 488 -------DIAPTMLSLMGMEIPQEMTGKPL 510
Cdd:COG3119 277 dalvsliDLLPTLLDLAGVPIPEDLDGRSL 306
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
418-510 |
3.33e-03 |
|
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: 293774 [Multi-domain] Cd Length: 372 Bit Score: 39.86 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 418 VEALDHCVEEVAKAVESVGgQL-----LITADHGnaeqmrdPATGQ----------AHTAHtnlpVPLIYVGdKNVKAve 482
Cdd:cd16155 198 ITHLDAQIGRILDALEASG-ELdntiiVFTSDHG-------LAVGShglmgkqnlyEHSMR----VPLIISG-PGIPK-- 262
|
90 100 110
....*....|....*....|....*....|....
gi 485719030 483 GGK------LSDIAPTMLSLMGMEIPQEMTGKPL 510
Cdd:cd16155 263 GKRrdalvyLQDVFPTLCELAGIEIPESVEGKSL 296
|
|
| DeoB |
COG1015 |
Phosphopentomutase [Carbohydrate transport and metabolism]; |
375-502 |
4.57e-03 |
|
Phosphopentomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440639 Cd Length: 385 Bit Score: 39.27 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 375 SSAELTEKLVAAIKSGKYDTIICNYPNGDMV-GHTGVMEAAVKAVEALDHCVEEVAKAVESvGGQLLITADHGNaeqmrD 453
Cdd:COG1015 254 GNADGMDKTLEAMDEAFGGLIFTNLVDFDSLyGHRRDVAGYAKALEEFDARLPELLAALRP-DDLLIITADHGN-----D 327
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 485719030 454 PATgqAHTAHTNLPVPLIYVGdKNVKAveGGKL------SDIAPTMLSLMGMEIP 502
Cdd:COG1015 328 PTW--PGTDHTREYVPLLVYG-PGLKP--GGNLgtretfADIGATIADHFGVPPP 377
|
|
| PMH |
cd16028 |
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ... |
418-510 |
5.67e-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: 39.16 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485719030 418 VEALDHCVEEVAKAVESVG---GQLLI-TADHGnaEQMRDP-ATGQAHTAHTNLPVPLIyVGD--KNVKAVEGGKLS--- 487
Cdd:cd16028 244 IAEVDDHLGRLFDYLKETGqwdDTLIVfTSDHG--EQLGDHwLWGKDGFFDQAYRVPLI-VRDprREADATRGQVVDaft 320
|
90 100
....*....|....*....|....*.
gi 485719030 488 ---DIAPTMLSLMGMEIPQEMTGKPL 510
Cdd:cd16028 321 esvDVMPTILDWLGGEIPHQCDGRSL 346
|
|
| |
