|
Name |
Accession |
Description |
Interval |
E-value |
| pgm_bpd_ind |
TIGR01307 |
phosphoglycerate mutase (2,3-diphosphoglycerate-independent); This protein is about double in ... |
3-504 |
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: 890.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 3 KKVLLAILDGYGISNKQHGNAVYHAKTPALDSLIKDYPCVMLEASGEAVGLPQGQIGNSEVGHLNIGAGRIVYTGLSLIN 82
Cdd:TIGR01307 1 KKVVLVILDGWGYRNDDDGNAIFAAKTPTMDELIAAYPYSLLDASGLDVGLPDGQMGNSEVGHLNIGAGRVVYQDLVRIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 83 QNIKTGAFHHNQVLLEAIARAKANNAKLHLIGLFSHGGVHSHMDHLYALIKLAAPQ--VKMVLHLFGDGRDVAPCTMKSD 160
Cdd:TIGR01307 81 QAIKDGEFFANPALLGAIDRAKDNNGKLHLMGLVSDGGVHSHIDHLIALIELAAERgiEKVVLHAFTDGRDTAPKSAESY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 161 LEAFMVFLKDYHNVIIGTLGGRYYGMDRDQRWDREEIAYNAILGNSKASFTDPVAYVQSAYDQKVTDEFLYPAVNGNVDk 240
Cdd:TIGR01307 161 LEQLQAFLKEIGNGRIATISGRYYAMDRDQRWDRVEIAYKAITGGDGFEFSDPVAYIQDAYARDITDEFIKPTIIGNGG- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 241 eqfALKDHDSVIFFNFRPDRARQMSHMLFQTDYYDYTPKAGRKYNlfFVTMMNYEGIKPSAVVFPPETIPNTFGEVIAHN 320
Cdd:TIGR01307 240 ---ALKDGDAVIFFNFRADRAREITRALVNSDFDGFPREKNPKLD--FVTMTQYDGTFPSPVAFPPQSLTNTLGEVLAKH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 321 KLKQLRIAETEKYAHVTFFFDGGVEVDLPNETKCMVPSLKVATYDLAPEMACKGITDQLLNQINQ--FDLTVLNFANPDM 398
Cdd:TIGR01307 315 DLTQLRIAETEKYAHVTFFFNGGVEVPFAGETRTLIPSPKVATYDLQPEMSAKAVTDAVLEAIAQgkFDLIVVNFANPDM 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 399 VGHTGNYAACVQGLEALDVQIQRIIDFCKANHITLFLTADHGNAEEMIDSNNNPVTKHTVNKVPFVCTD-TNIDLQQDSA 477
Cdd:TIGR01307 395 VGHTGNFEAAIKAVEALDVCLGRIVEACKKVGGTLFLTADHGNAEEMIDENGNPHTAHTTNPVPFVCVGaKNVKLIREGG 474
|
490 500
....*....|....*....|....*..
gi 1802581430 478 SLANIAPTILAYLGLKQPAEMTANSLL 504
Cdd:TIGR01307 475 VLADIAPTILDLMGLEQPAEMTGKSLL 501
|
|
| PRK05434 |
PRK05434 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
1-505 |
0e+00 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235463 Cd Length: 507 Bit Score: 776.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 1 MHKKVLLAILDGYGISNKQHGNAVYHAKTPALDSLIKDYPCVMLEASGEAVGLPQGQIGNSEVGHLNIGAGRIVYTGLSL 80
Cdd:PRK05434 3 MKKPVVLIILDGWGYREETEGNAIALAKTPNLDRLWANYPHTLLSASGLAVGLPDGQMGNSEVGHLNIGAGRIVYQDLTR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 81 INQNIKTGAFHHNQVLLEAIARAKANNAKLHLIGLFSHGGVHSHMDHLYALIKLAAPQ--VKMVLHLFGDGRDVAPCTMK 158
Cdd:PRK05434 83 INKAIEDGSFFENPALLDAIDKAKKNGGALHLMGLLSDGGVHSHIDHLFALLELAKEEgvKKVYVHAFLDGRDTPPKSAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 159 SDLEAFMVFLKDYHNVIIGTLGGRYYGMDRDQRWDREEIAYNAI-LGNSKASFTDPVAYVQSAYDQKVTDEFLYPAVNGN 237
Cdd:PRK05434 163 GYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALvLGEGPFTAESAVEALEASYARGETDEFVKPTVIGG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 238 vdKEQFALKDHDSVIFFNFRPDRARQMSHMLFQTDYYDYTPKagrKYNLFFVTMMNYEGIKPSAVVFPPETIPNTFGEVI 317
Cdd:PRK05434 243 --EPVAGIEDGDAVIFFNFRADRARQITRAFTDPDFDGFDRV---PKLLNFVTMTQYDADLKVPVAFPPESLKNTLGEVL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 318 AHNKLKQLRIAETEKYAHVTFFFDGGVEVDLPNETKCMVPSLKVATYDLAPEMACKGITDQLLNQIN--QFDLTVLNFAN 395
Cdd:PRK05434 318 AKAGLTQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIEsgKYDFIILNFAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 396 PDMVGHTGNYAACVQGLEALDVQIQRIIDFCKANHITLFLTADHGNAEEMID-SNNNPVTKHTVNKVPFVCTDtNIDLQQ 474
Cdd:PRK05434 398 PDMVGHTGNLEAAVKAVEAVDECLGRVVDAVLKVGGTLLITADHGNAEQMIDpETGQPHTAHTTNPVPFILVG-GKALRL 476
|
490 500 510
....*....|....*....|....*....|.
gi 1802581430 475 DSASLANIAPTILAYLGLKQPAEMTANSLLI 505
Cdd:PRK05434 477 EGGKLADIAPTILDLLGLEQPAEMTGKSLIE 507
|
|
| iPGM |
cd16010 |
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
3-504 |
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: 772.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 3 KKVLLAILDGYGISNKQHGNAVYHAKTPALDSLIKDYPCVMLEASGEAVGLPQGQIGNSEVGHLNIGAGRIVYTGLSLIN 82
Cdd:cd16010 1 KPVVLIILDGWGIRPEDEGNAIALAKTPNLDRLWATYPHTLLKASGEAVGLPDGQMGNSEVGHLNIGAGRIVYQDLTRIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 83 QNIKTGAFHHNQVLLEAIARAKANNAKLHLIGLFSHGGVHSHMDHLYALIKLAAPQ--VKMVLHLFGDGRDVAPCTMKSD 160
Cdd:cd16010 81 KAIEDGSFFKNEALLKAIEHAKKNNSTLHLMGLLSDGGVHSHIDHLFALLELAKKEgvKKVYVHAFTDGRDTPPKSALKY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 161 LEAFMVFLKDYHNVIIGTLGGRYYGMDRDQRWDREEIAYNAILGNSKASFTDPVAYVQSAYDQKVTDEFLYPAVNGNVDK 240
Cdd:cd16010 161 LKELEEKLKELGVGKIASVSGRYYAMDRDKRWDRTEKAYDALVLGEGEKAESAEEAIEASYAKGITDEFIPPTVIGDEGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 241 eqfALKDHDSVIFFNFRPDRARQMSHMLFQTDYYDYTPKagRKYNLFFVTMMNYEGIKPSAVVFPPETIPNTFGEVIAHN 320
Cdd:cd16010 241 ---TIKDGDAVIFFNFRADRARQITRAFTDPDFDGFDRK--KPKNLYFVTMTEYDKDLPVPVAFPPPKIKNTLGEVLSKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 321 KLKQLRIAETEKYAHVTFFFDGGVEVDLPNETKCMVPSLKVATYDLAPEMACKGITDQLLNQIN--QFDLTVLNFANPDM 398
Cdd:cd16010 316 GLKQLRIAETEKYAHVTYFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLIEAIKsgKYDFIVVNFANPDM 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 399 VGHTGNYAACVQGLEALDVQIQRIIDFCKANHITLFLTADHGNAEEMID-SNNNPVTKHTVNKVPFVCTDTNIDLQQ-DS 476
Cdd:cd16010 396 VGHTGNLEAAVKAVEAVDECLGRIVEAVLENGGTLLITADHGNAEEMIDpETGGPHTAHTTNPVPFIIVDPGLKRKLlKD 475
|
490 500
....*....|....*....|....*...
gi 1802581430 477 ASLANIAPTILAYLGLKQPAEMTANSLL 504
Cdd:cd16010 476 GGLADVAPTILDLLGIEKPKEMTGKSLI 503
|
|
| GpmI |
COG0696 |
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ... |
2-505 |
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: 757.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 2 HKKVLLAILDGYGISNKQHGNAVYHAKTPALDSLIKDYPCVMLEASGEAVGLPQGQIGNSEVGHLNIGAGRIVYTGLSLI 81
Cdd:COG0696 2 KKPVVLIILDGWGIREETEGNAIALANTPNLDRLWATYPHTLLRASGEAVGLPDGQMGNSEVGHLNIGAGRVVYQDLTRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 82 NQNIKTGAFHHNQVLLEAIARAKANNAKLHLIGLFSHGGVHSHMDHLYALIKLAAPQ--VKMVLHLFGDGRDVAPCTMKS 159
Cdd:COG0696 82 NKAIEDGSFFENPVLLDAIDKAKENGGALHLMGLLSDGGVHSHIDHLKALLELAKEEgvKKVYVHAFLDGRDTPPKSALG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 160 DLEAFMVFLKDYHNVIIGTLGGRYYGMDRDQRWDREEIAYNAILGNSKASFTDPVAYVQSAYDQKVTDEFLYPAVNGNVD 239
Cdd:COG0696 162 YLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVNGEGETAASAVEAIEASYARGETDEFVKPTVIVDYG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 240 KEQFALKDHDSVIFFNFRPDRARQMSHMLFQTDYYDYTPKAGRKyNLFFVTMMNYEGIKPSAVVFPPETIPNTFGEVIAH 319
Cdd:COG0696 242 KPVATIEDGDAVIFFNFRADRARQLTRAFTDPDFDGFDRGKRPK-LLYFVTMTEYDETFDVPVAFPPENLKNTLGEVLAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 320 NKLKQLRIAETEKYAHVTFFFDGGVEVDLPNETKCMVPSLKVATYDLAPEMACKGITDQLLNQIN--QFDLTVLNFANPD 397
Cdd:COG0696 321 AGLKQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIEsgKYDFIVLNFANPD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 398 MVGHTGNYAACVQGLEALDVQIQRIIDFCKANHITLFLTADHGNAEEMIDSN-NNPVTKHTVNKVPFVCTDTNIDLQ-QD 475
Cdd:COG0696 401 MVGHTGVLEAAIKAVEAVDECLGRVVDAVLAAGGTLLITADHGNAEQMIDPDtGGPHTAHTTNPVPFILVGGDKGVKlRE 480
|
490 500 510
....*....|....*....|....*....|
gi 1802581430 476 SASLANIAPTILAYLGLKQPAEMTANSLLI 505
Cdd:COG0696 481 DGRLADIAPTILELMGLPQPAEMTGKSLIE 510
|
|
| Metalloenzyme |
pfam01676 |
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ... |
3-493 |
2.02e-149 |
|
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: 433.36 E-value: 2.02e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 3 KKVLLAILDGYGISNKQHGNA---VYHAKTPALDSLIKDYPCVMLEASGEAVGLPQGQIGNSEVGHLNIGAGRIVYTGLS 79
Cdd:pfam01676 1 KKVVLIVLDGWGDRPAEDLNAktpLHIAKTPNMDKLAKEYPEQLIGASGLAVGLPEGQMGGSDVGHLEIGGGRIVYQYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 80 LINQNIKTGAFHHNQVLLEAIARAKANNAKLHLIGLFSHGGVHSHMDHLYALIKLAAPQVKMVLHLFGDGRDVApctmks 159
Cdd:pfam01676 81 RGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHSHIEHLLALIALAKEAGAIKVHLLGDGDDRP------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 160 dleafmvflkdyhnviigtlggryygmdrdqrwdreeiaynailgnskasftdpvayvqsaydqkvtdeflypavngnvd 239
Cdd:pfam01676 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 240 keQFALKDHDSVIFFNFRPDRARQMSHMLFQTDYYDYTPKAGRKYNLFFVTMMNYEGIKPSAVVFPPETIPNTFGEVIAH 319
Cdd:pfam01676 155 --VGYILDGDAVITINFRFDRRRARILRLFLLDPDFFDRDRVRHDALHVPTKTLYELKLPSAGAFVPEEGKNTDGEVLEG 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 320 NKLKQLRIAETEKYAHVTFFFDGGVEVDLPNETKCMVPSLKVATYDLAPEMACKGITDQLLNQINQ-FDLTVLNFANPDM 398
Cdd:pfam01676 233 HGLKQLRIAETEKYAHVTFFWGGGREPPFPGEERYLIPSPKVATYDLQPEMSAMEITDKLLEALKEkYDFVFVNFANTDM 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 399 VGHTGNYAACVQGLEALDVQIQRIIDFCKANHITLFLTADHGNAEEMIDsnnnpvTKHTVNKVPFVCTDTNIDLQQDS-- 476
Cdd:pfam01676 313 VGHTGDVEGKVKAIEAVDERLGELLDALEEDDGLLIITADHGNPEEMKD------TDHTREPVPILIYGKGVRPDQVLfg 386
|
490 500
....*....|....*....|...
gi 1802581430 477 ------ASLANIAPTILAYLGLK 493
Cdd:pfam01676 387 ekfrerGGLADIAATILMLLGLK 409
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| pgm_bpd_ind |
TIGR01307 |
phosphoglycerate mutase (2,3-diphosphoglycerate-independent); This protein is about double in ... |
3-504 |
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: 890.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 3 KKVLLAILDGYGISNKQHGNAVYHAKTPALDSLIKDYPCVMLEASGEAVGLPQGQIGNSEVGHLNIGAGRIVYTGLSLIN 82
Cdd:TIGR01307 1 KKVVLVILDGWGYRNDDDGNAIFAAKTPTMDELIAAYPYSLLDASGLDVGLPDGQMGNSEVGHLNIGAGRVVYQDLVRIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 83 QNIKTGAFHHNQVLLEAIARAKANNAKLHLIGLFSHGGVHSHMDHLYALIKLAAPQ--VKMVLHLFGDGRDVAPCTMKSD 160
Cdd:TIGR01307 81 QAIKDGEFFANPALLGAIDRAKDNNGKLHLMGLVSDGGVHSHIDHLIALIELAAERgiEKVVLHAFTDGRDTAPKSAESY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 161 LEAFMVFLKDYHNVIIGTLGGRYYGMDRDQRWDREEIAYNAILGNSKASFTDPVAYVQSAYDQKVTDEFLYPAVNGNVDk 240
Cdd:TIGR01307 161 LEQLQAFLKEIGNGRIATISGRYYAMDRDQRWDRVEIAYKAITGGDGFEFSDPVAYIQDAYARDITDEFIKPTIIGNGG- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 241 eqfALKDHDSVIFFNFRPDRARQMSHMLFQTDYYDYTPKAGRKYNlfFVTMMNYEGIKPSAVVFPPETIPNTFGEVIAHN 320
Cdd:TIGR01307 240 ---ALKDGDAVIFFNFRADRAREITRALVNSDFDGFPREKNPKLD--FVTMTQYDGTFPSPVAFPPQSLTNTLGEVLAKH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 321 KLKQLRIAETEKYAHVTFFFDGGVEVDLPNETKCMVPSLKVATYDLAPEMACKGITDQLLNQINQ--FDLTVLNFANPDM 398
Cdd:TIGR01307 315 DLTQLRIAETEKYAHVTFFFNGGVEVPFAGETRTLIPSPKVATYDLQPEMSAKAVTDAVLEAIAQgkFDLIVVNFANPDM 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 399 VGHTGNYAACVQGLEALDVQIQRIIDFCKANHITLFLTADHGNAEEMIDSNNNPVTKHTVNKVPFVCTD-TNIDLQQDSA 477
Cdd:TIGR01307 395 VGHTGNFEAAIKAVEALDVCLGRIVEACKKVGGTLFLTADHGNAEEMIDENGNPHTAHTTNPVPFVCVGaKNVKLIREGG 474
|
490 500
....*....|....*....|....*..
gi 1802581430 478 SLANIAPTILAYLGLKQPAEMTANSLL 504
Cdd:TIGR01307 475 VLADIAPTILDLMGLEQPAEMTGKSLL 501
|
|
| PRK05434 |
PRK05434 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
1-505 |
0e+00 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235463 Cd Length: 507 Bit Score: 776.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 1 MHKKVLLAILDGYGISNKQHGNAVYHAKTPALDSLIKDYPCVMLEASGEAVGLPQGQIGNSEVGHLNIGAGRIVYTGLSL 80
Cdd:PRK05434 3 MKKPVVLIILDGWGYREETEGNAIALAKTPNLDRLWANYPHTLLSASGLAVGLPDGQMGNSEVGHLNIGAGRIVYQDLTR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 81 INQNIKTGAFHHNQVLLEAIARAKANNAKLHLIGLFSHGGVHSHMDHLYALIKLAAPQ--VKMVLHLFGDGRDVAPCTMK 158
Cdd:PRK05434 83 INKAIEDGSFFENPALLDAIDKAKKNGGALHLMGLLSDGGVHSHIDHLFALLELAKEEgvKKVYVHAFLDGRDTPPKSAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 159 SDLEAFMVFLKDYHNVIIGTLGGRYYGMDRDQRWDREEIAYNAI-LGNSKASFTDPVAYVQSAYDQKVTDEFLYPAVNGN 237
Cdd:PRK05434 163 GYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALvLGEGPFTAESAVEALEASYARGETDEFVKPTVIGG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 238 vdKEQFALKDHDSVIFFNFRPDRARQMSHMLFQTDYYDYTPKagrKYNLFFVTMMNYEGIKPSAVVFPPETIPNTFGEVI 317
Cdd:PRK05434 243 --EPVAGIEDGDAVIFFNFRADRARQITRAFTDPDFDGFDRV---PKLLNFVTMTQYDADLKVPVAFPPESLKNTLGEVL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 318 AHNKLKQLRIAETEKYAHVTFFFDGGVEVDLPNETKCMVPSLKVATYDLAPEMACKGITDQLLNQIN--QFDLTVLNFAN 395
Cdd:PRK05434 318 AKAGLTQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIEsgKYDFIILNFAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 396 PDMVGHTGNYAACVQGLEALDVQIQRIIDFCKANHITLFLTADHGNAEEMID-SNNNPVTKHTVNKVPFVCTDtNIDLQQ 474
Cdd:PRK05434 398 PDMVGHTGNLEAAVKAVEAVDECLGRVVDAVLKVGGTLLITADHGNAEQMIDpETGQPHTAHTTNPVPFILVG-GKALRL 476
|
490 500 510
....*....|....*....|....*....|.
gi 1802581430 475 DSASLANIAPTILAYLGLKQPAEMTANSLLI 505
Cdd:PRK05434 477 EGGKLADIAPTILDLLGLEQPAEMTGKSLIE 507
|
|
| iPGM |
cd16010 |
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ... |
3-504 |
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: 772.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 3 KKVLLAILDGYGISNKQHGNAVYHAKTPALDSLIKDYPCVMLEASGEAVGLPQGQIGNSEVGHLNIGAGRIVYTGLSLIN 82
Cdd:cd16010 1 KPVVLIILDGWGIRPEDEGNAIALAKTPNLDRLWATYPHTLLKASGEAVGLPDGQMGNSEVGHLNIGAGRIVYQDLTRIN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 83 QNIKTGAFHHNQVLLEAIARAKANNAKLHLIGLFSHGGVHSHMDHLYALIKLAAPQ--VKMVLHLFGDGRDVAPCTMKSD 160
Cdd:cd16010 81 KAIEDGSFFKNEALLKAIEHAKKNNSTLHLMGLLSDGGVHSHIDHLFALLELAKKEgvKKVYVHAFTDGRDTPPKSALKY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 161 LEAFMVFLKDYHNVIIGTLGGRYYGMDRDQRWDREEIAYNAILGNSKASFTDPVAYVQSAYDQKVTDEFLYPAVNGNVDK 240
Cdd:cd16010 161 LKELEEKLKELGVGKIASVSGRYYAMDRDKRWDRTEKAYDALVLGEGEKAESAEEAIEASYAKGITDEFIPPTVIGDEGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 241 eqfALKDHDSVIFFNFRPDRARQMSHMLFQTDYYDYTPKagRKYNLFFVTMMNYEGIKPSAVVFPPETIPNTFGEVIAHN 320
Cdd:cd16010 241 ---TIKDGDAVIFFNFRADRARQITRAFTDPDFDGFDRK--KPKNLYFVTMTEYDKDLPVPVAFPPPKIKNTLGEVLSKA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 321 KLKQLRIAETEKYAHVTFFFDGGVEVDLPNETKCMVPSLKVATYDLAPEMACKGITDQLLNQIN--QFDLTVLNFANPDM 398
Cdd:cd16010 316 GLKQLRIAETEKYAHVTYFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLIEAIKsgKYDFIVVNFANPDM 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 399 VGHTGNYAACVQGLEALDVQIQRIIDFCKANHITLFLTADHGNAEEMID-SNNNPVTKHTVNKVPFVCTDTNIDLQQ-DS 476
Cdd:cd16010 396 VGHTGNLEAAVKAVEAVDECLGRIVEAVLENGGTLLITADHGNAEEMIDpETGGPHTAHTTNPVPFIIVDPGLKRKLlKD 475
|
490 500
....*....|....*....|....*...
gi 1802581430 477 ASLANIAPTILAYLGLKQPAEMTANSLL 504
Cdd:cd16010 476 GGLADVAPTILDLLGIEKPKEMTGKSLI 503
|
|
| GpmI |
COG0696 |
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ... |
2-505 |
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: 757.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 2 HKKVLLAILDGYGISNKQHGNAVYHAKTPALDSLIKDYPCVMLEASGEAVGLPQGQIGNSEVGHLNIGAGRIVYTGLSLI 81
Cdd:COG0696 2 KKPVVLIILDGWGIREETEGNAIALANTPNLDRLWATYPHTLLRASGEAVGLPDGQMGNSEVGHLNIGAGRVVYQDLTRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 82 NQNIKTGAFHHNQVLLEAIARAKANNAKLHLIGLFSHGGVHSHMDHLYALIKLAAPQ--VKMVLHLFGDGRDVAPCTMKS 159
Cdd:COG0696 82 NKAIEDGSFFENPVLLDAIDKAKENGGALHLMGLLSDGGVHSHIDHLKALLELAKEEgvKKVYVHAFLDGRDTPPKSALG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 160 DLEAFMVFLKDYHNVIIGTLGGRYYGMDRDQRWDREEIAYNAILGNSKASFTDPVAYVQSAYDQKVTDEFLYPAVNGNVD 239
Cdd:COG0696 162 YLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVNGEGETAASAVEAIEASYARGETDEFVKPTVIVDYG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 240 KEQFALKDHDSVIFFNFRPDRARQMSHMLFQTDYYDYTPKAGRKyNLFFVTMMNYEGIKPSAVVFPPETIPNTFGEVIAH 319
Cdd:COG0696 242 KPVATIEDGDAVIFFNFRADRARQLTRAFTDPDFDGFDRGKRPK-LLYFVTMTEYDETFDVPVAFPPENLKNTLGEVLAK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 320 NKLKQLRIAETEKYAHVTFFFDGGVEVDLPNETKCMVPSLKVATYDLAPEMACKGITDQLLNQIN--QFDLTVLNFANPD 397
Cdd:COG0696 321 AGLKQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIEsgKYDFIVLNFANPD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 398 MVGHTGNYAACVQGLEALDVQIQRIIDFCKANHITLFLTADHGNAEEMIDSN-NNPVTKHTVNKVPFVCTDTNIDLQ-QD 475
Cdd:COG0696 401 MVGHTGVLEAAIKAVEAVDECLGRVVDAVLAAGGTLLITADHGNAEQMIDPDtGGPHTAHTTNPVPFILVGGDKGVKlRE 480
|
490 500 510
....*....|....*....|....*....|
gi 1802581430 476 SASLANIAPTILAYLGLKQPAEMTANSLLI 505
Cdd:COG0696 481 DGRLADIAPTILELMGLPQPAEMTGKSLIE 510
|
|
| Metalloenzyme |
pfam01676 |
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ... |
3-493 |
2.02e-149 |
|
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: 433.36 E-value: 2.02e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 3 KKVLLAILDGYGISNKQHGNA---VYHAKTPALDSLIKDYPCVMLEASGEAVGLPQGQIGNSEVGHLNIGAGRIVYTGLS 79
Cdd:pfam01676 1 KKVVLIVLDGWGDRPAEDLNAktpLHIAKTPNMDKLAKEYPEQLIGASGLAVGLPEGQMGGSDVGHLEIGGGRIVYQYLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 80 LINQNIKTGAFHHNQVLLEAIARAKANNAKLHLIGLFSHGGVHSHMDHLYALIKLAAPQVKMVLHLFGDGRDVApctmks 159
Cdd:pfam01676 81 RGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHSHIEHLLALIALAKEAGAIKVHLLGDGDDRP------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 160 dleafmvflkdyhnviigtlggryygmdrdqrwdreeiaynailgnskasftdpvayvqsaydqkvtdeflypavngnvd 239
Cdd:pfam01676 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 240 keQFALKDHDSVIFFNFRPDRARQMSHMLFQTDYYDYTPKAGRKYNLFFVTMMNYEGIKPSAVVFPPETIPNTFGEVIAH 319
Cdd:pfam01676 155 --VGYILDGDAVITINFRFDRRRARILRLFLLDPDFFDRDRVRHDALHVPTKTLYELKLPSAGAFVPEEGKNTDGEVLEG 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 320 NKLKQLRIAETEKYAHVTFFFDGGVEVDLPNETKCMVPSLKVATYDLAPEMACKGITDQLLNQINQ-FDLTVLNFANPDM 398
Cdd:pfam01676 233 HGLKQLRIAETEKYAHVTFFWGGGREPPFPGEERYLIPSPKVATYDLQPEMSAMEITDKLLEALKEkYDFVFVNFANTDM 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 399 VGHTGNYAACVQGLEALDVQIQRIIDFCKANHITLFLTADHGNAEEMIDsnnnpvTKHTVNKVPFVCTDTNIDLQQDS-- 476
Cdd:pfam01676 313 VGHTGDVEGKVKAIEAVDERLGELLDALEEDDGLLIITADHGNPEEMKD------TDHTREPVPILIYGKGVRPDQVLfg 386
|
490 500
....*....|....*....|...
gi 1802581430 477 ------ASLANIAPTILAYLGLK 493
Cdd:pfam01676 387 ekfrerGGLADIAATILMLLGLK 409
|
|
| iPGM_N |
pfam06415 |
BPG-independent PGAM N-terminus (iPGM_N); This family represents the N-terminal region of the ... |
81-296 |
6.77e-99 |
|
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: 297.01 E-value: 6.77e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 81 INQNIKTGAFHHNQVLLEAIARAKANNAKLHLIGLFSHGGVHSHMDHLYALIKLAAPQ-VKMV-LHLFGDGRDVAPCTMK 158
Cdd:pfam06415 1 INKAIEDGSFFENPALLKAIENAKANGGALHLMGLLSDGGVHSHIDHLFALLELAKEEgVKKVyVHAFLDGRDTPPKSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 159 SDLEAFMVFLKDYHNVIIGTLGGRYYGMDRDQRWDREEIAYNAILGNSKASFTDPVAYVQSAYDQKVTDEFLYPAVNGNV 238
Cdd:pfam06415 81 GYLEQLEAKLAELGVGKIATVSGRYYAMDRDKRWDRVEKAYDALVLGEGESAADAVEAIEASYARGETDEFVKPTVIVDD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1802581430 239 DKEQFALKDHDSVIFFNFRPDRARQMSHMLFQTDYYDYTPKAGRKyNLFFVTMMNYEG 296
Cdd:pfam06415 161 GKPVGTIKDGDSVIFFNFRPDRAREITRAFTDPDFDGFERRKRPK-DLHFVTMTQYDA 217
|
|
| PLN02538 |
PLN02538 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase |
3-498 |
2.70e-94 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
Pssm-ID: 215295 Cd Length: 558 Bit Score: 296.97 E-value: 2.70e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 3 KKVLLAILDGYGISNKQHGNAVYHAKTPALDSLIKDYPCV--MLEASGEAVGLP-QGQIGNSEVGHLNIGAGRIVYTGLS 79
Cdd:PLN02538 21 KPLLLIVLDGWGENAPDEFNAIHVAPTPTMDSLKAGAPERwrLVKAHGTAVGLPsDDDMGNSEVGHNALGAGRIFAQGAK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 80 LINQNIKTGAFHHNQVLLeAIARAKANNAkLHLIGLFSHGGVHSHMDHLYALIKLAAPQ--VKMVLHLFGDGRDVAPCT- 156
Cdd:PLN02538 101 LVDLALASGKIFEGEGFK-YIKEAFATGT-LHLIGLLSDGGVHSRLDQLQLLLKGAAERgaKRIRVHVLTDGRDVPDGSs 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 157 --MKSDLEAFMVFLKDYH-NVIIGTLGGRYY-GMDR-DQRWDREEIAYNA-ILGNSKASFTDPVAYVQS--AYDQKVTDE 228
Cdd:PLN02538 179 vgFVETLEKDLAELREKGcDARIASGGGRMYvTMDRyENDWNVVKRGWDAhVLGEAPHKFKSALEAVKKlrEEPPPANDQ 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 229 FLYPAVNgnVDKEQFA---LKDHDSVIFFNFRPDRARQMSHMLfqtDYYDYTP-KAGRKYNLFFVTMMNYEG-IK-PSAV 302
Cdd:PLN02538 259 YLPPFVI--VDEDGKPvgpIEDGDAVVTFNFRADRMVMIAKAL---EYEDFDKfDRVRVPKIRYAGMLQYDGeLKlPSHY 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 303 VFPPETIPNTFGEVIAHNKLKQLRIAETEKYAHVTFFFDGGVE--VDLPNETKCMVPSLKVATYDLAPEMACKGIT---- 376
Cdd:PLN02538 334 LVSPPLIERTSGEYLVANGVRTFACSETVKFGHVTFFWNGNRSgyFNEKLEEYVEIPSDNGIPFNVQPKMKALEIAekar 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 377 DQLLNqiNQFDLTVLNFANPDMVGHTGNYAACVQGLEALDVQIQRIIDFCKANHITLFLTADHGNAEEMI---------- 446
Cdd:PLN02538 414 DALLS--GKFDQVRVNLANGDMVGHTGDLEATIVACEAVDAAVKEILDAVEQVGGIYLVTADHGNAEDMVkrdksgkpll 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 447 --DSNNNPVTKHTVNKVPFVC----TDTNIDLQQD--SASLANIAPTILAYLGLKQPAEM 498
Cdd:PLN02538 492 dkDGNPQILTSHTLAPVPVAIggpgLPPGVRFRDDlpTAGLANVAATVMNLHGFEAPADY 551
|
|
| sulfatase_like |
cd16148 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
405-504 |
6.86e-07 |
|
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: 50.62 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 405 YAACVqglEALDVQIQRIIDFCKANHI---TLF-LTADHGnaEEM-----IDSNNNPVTKHTVNkVPFV------CTDTN 469
Cdd:cd16148 165 YDAEV---RYVDEQIGRLLDKLKELGLledTLViVTSDHG--EEFgehglYWGHGSNLYDEQLH-VPLIirwpgkEPGKR 238
|
90 100 110
....*....|....*....|....*....|....*
gi 1802581430 470 IDLQqdsASLANIAPTILAYLGLKQPAEMTANSLL 504
Cdd:cd16148 239 VDAL---VSHIDIAPTLLDLLGVEPPDYSDGRSLL 270
|
|
| PPM |
cd16009 |
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ... |
371-499 |
1.47e-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: 50.53 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 371 ACKGIT------------DQLLNQ-INQF-DLTVLNFANPDMV-GHTGN---YAACvqgLEALDVQIQRIIDFCKANHIt 432
Cdd:cd16009 242 AGRGITesihtksnadgmEKTLEAlKEDFnGLIFTNLVDFDMLyGHRRDpegYAEA---LEEFDRRLPELLAKLKEDDL- 317
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1802581430 433 LFLTADHGNaeemiDsnnnPV---TKHTVNKVPFVCTDTNIDLQQ--DSASLANIAPTILAYLGLKQPAEMT 499
Cdd:cd16009 318 LIITADHGN-----D----PTiggTDHTREYVPLLVYGKGLKGVNlgTRETFADIGATIADNFGVEPPENGT 380
|
|
| DeoB |
COG1015 |
Phosphopentomutase [Carbohydrate transport and metabolism]; |
377-496 |
2.12e-06 |
|
Phosphopentomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440639 Cd Length: 385 Bit Score: 50.05 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 377 DQLLNQINQF--DLTVLNFANPDMV-GHTGN---YAACvqgLEALDVQIQRIIDFCKANHItLFLTADHGNaeemiDsnn 450
Cdd:COG1015 260 DKTLEAMDEAfgGLIFTNLVDFDSLyGHRRDvagYAKA---LEEFDARLPELLAALRPDDL-LIITADHGN-----D--- 327
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1802581430 451 nPVTK---HTVNKVPFVCTDTNIDLQQD---SASLANIAPTILAYLGLKQPA 496
Cdd:COG1015 328 -PTWPgtdHTREYVPLLVYGPGLKPGGNlgtRETFADIGATIADHFGVPPPG 378
|
|
| ALP_like |
cd00016 |
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ... |
387-488 |
4.26e-06 |
|
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: 48.19 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 387 DLTVLNFANPDMVGHTGNYAACVQG--LEALDVQIQRIIDFCKANHI---TLFL-TADHGNAEE----MIDSNNNPVTKH 456
Cdd:cd00016 121 FVLFLHFDGPDGPGHAYGPNTPEYYdaVEEIDERIGKVLDALKKAGDaddTVIIvTADHGGIDKghggDPKADGKADKSH 200
|
90 100 110
....*....|....*....|....*....|....*
gi 1802581430 457 TVNKVPFVCTDTNIDLQQ---DSASLANIAPTILA 488
Cdd:cd00016 201 TGMRVPFIAYGPGVKKGGvkhELISQYDIAPTLAD 235
|
|
| AtaC |
COG1524 |
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ... |
387-447 |
1.59e-05 |
|
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];
Pssm-ID: 441133 [Multi-domain] Cd Length: 370 Bit Score: 47.05 E-value: 1.59e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1802581430 387 DLTVLNFANPDMVGHT--GNYAACVQGLEALDVQIQRIIDFCKANHI----TLFLTADHGnaeeMID 447
Cdd:COG1524 184 DLLLVYLPDLDYAGHRygPDSPEYRAALREVDAALGRLLDALKARGLyegtLVIVTADHG----MVD 246
|
|
| PRK04024 |
PRK04024 |
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; |
373-464 |
2.33e-05 |
|
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
Pssm-ID: 235203 Cd Length: 412 Bit Score: 46.83 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 373 KGITDQLLNQINQFDLTVLNFANPDMVGHTGNYAACVQGLEALDVQIQRIIDFCKANHITLFLTADHGNAEEMIDsnnnp 452
Cdd:PRK04024 281 MAKAKAAVELLKEYDFVLLNIKGTDEAGHDGDFEGKVEVIEKIDKMLGYILDNLDLDEVYIAVTGDHSTPVEVKD----- 355
|
90
....*....|..
gi 1802581430 453 vtkHTVNKVPFV 464
Cdd:PRK04024 356 ---HSGDPVPIL 364
|
|
| AslA |
COG3119 |
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism]; |
403-504 |
2.92e-05 |
|
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
Pssm-ID: 442353 [Multi-domain] Cd Length: 393 Bit Score: 46.41 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 403 GNYAACVqglEALDVQIQRIIDFCKANHI---TL-FLTADHGnaeEMIDSNNNPVTKHTV----NKVPFVCTDTN-IDLQ 473
Cdd:COG3119 200 AAYAAMI---EEVDDQVGRLLDALEELGLadnTIvVFTSDNG---PSLGEHGLRGGKGTLyeggIRVPLIVRWPGkIKAG 273
|
90 100 110
....*....|....*....|....*....|....
gi 1802581430 474 QDSASLAN---IAPTILAYLGLKQPAEMTANSLL 504
Cdd:COG3119 274 SVSDALVSlidLLPTLLDLAGVPIPEDLDGRSLL 307
|
|
| PRK05362 |
PRK05362 |
phosphopentomutase; Provisional |
371-495 |
5.43e-05 |
|
phosphopentomutase; Provisional
Pssm-ID: 235430 Cd Length: 394 Bit Score: 45.49 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 371 ACKGIT------------DQLLNQINQFDLTVLNFANP---DMV-GHTGN---YAACvqgLEALDVQIQRIIDFCKANHI 431
Cdd:PRK05362 248 AGQGITekvktksnmdgmDATIEEMKEAGDNGLVFTNLvdfDSLyGHRRDvagYAAA---LEEFDARLPELLAALKEDDL 324
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1802581430 432 tLFLTADHGnaeemidsnNNPVTK---HTVNKVPFVCTDTNIDLQQ--DSASLANIAPTILAYLGLKQP 495
Cdd:PRK05362 325 -LIITADHG---------NDPTWPgtdHTREYVPLLVYGPKFKGGSlgHRETFADIGATIADNFGVEPM 383
|
|
| apgM |
TIGR00306 |
phosphoglycerate mutase (2,3-diphosphoglycerate-independent), archaeal form; Experimentally ... |
374-474 |
2.82e-04 |
|
phosphoglycerate mutase (2,3-diphosphoglycerate-independent), archaeal form; Experimentally characterized in archaea as 2,3-bisphosphoglycerate-independent phosphoglycerate mutase. This model describes a set of proteins in the Archaea (two each in Methanococcus jannaschii, Methanobacterium thermoautotrophicum, and Archaeoglobus fulgidus) and in Aquifex aeolicus (1 member). [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 273005 Cd Length: 396 Bit Score: 43.23 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 374 GITDQLLNQINQFDLTVLNFANPDMVGHTGNYAACVQGLEALDVQIQRIIDFCKANHITLFLTADHGNAEEMIDsnnnpv 453
Cdd:TIGR00306 276 GKVRALILALEEYDFVLVHTKGPDEAGHDGDPELKVRAIEKIDSKIVGPLLALDLDETRLILTADHSTPVEVKD------ 349
|
90 100
....*....|....*....|.
gi 1802581430 454 tkHTVNKVPFVCTDTNIDLQQ 474
Cdd:TIGR00306 350 --HSADPVPIVIVGPGVRVDE 368
|
|
| sulfatase_like |
cd16022 |
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ... |
390-498 |
1.90e-03 |
|
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: 40.11 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 390 VLNFANPdmvgHTG-NYAACVqglEALDVQIQRIIDFCKANHI---TLFL-TADHGnaeEMIDSNNNPVTKHT----VNK 460
Cdd:cd16022 121 YVSFNAP----HPPfAYYAMV---SAIDDQIGRILDALEELGLldnTLIVfTSDHG---DMLGDHGLRGKKGSlyegGIR 190
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1802581430 461 VPF-------VCTDTNIDlqqDSASLANIAPTILAYLGLKQPAEM 498
Cdd:cd16022 191 VPFivrwpgkIPAGQVSD---ALVSLLDLLPTLLDLAGIEPPEGL 232
|
|
| sulfatase_like |
cd16155 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
396-504 |
2.61e-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: 40.24 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 396 PDMVG-HTGNYAACVqglEALDVQIQRIIDFCKA-----NHITLFlTADHG------------NAEEmidsnnnpvtkHT 457
Cdd:cd16155 184 PEAVRqHLAEYYAMI---THLDAQIGRILDALEAsgeldNTIIVF-TSDHGlavgshglmgkqNLYE-----------HS 248
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1802581430 458 VnKVPFVCTDTNIDLQQDSAS---LANIAPTILAYLGLKQPAEMTANSLL 504
Cdd:cd16155 249 M-RVPLIISGPGIPKGKRRDAlvyLQDVFPTLCELAGIEIPESVEGKSLL 297
|
|
| sulfatase_like |
cd16034 |
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ... |
405-498 |
4.95e-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: 293758 [Multi-domain] Cd Length: 399 Bit Score: 39.09 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 405 YAACvqglEALDVQIQRIIDFCKANHI---TLF-LTADHGnaeEMIDSNNNpVTKHTVN----KVPFVC-------TDTN 469
Cdd:cd16034 230 YAMI----TALDDNIGRLLDALKELGLlenTIVvFTSDHG---DMLGSHGL-MNKQVPYeesiRVPFIIrypgkikAGRV 301
|
90 100
....*....|....*....|....*....
gi 1802581430 470 IDLQqdsASLANIAPTILAYLGLKQPAEM 498
Cdd:cd16034 302 VDLL---INTVDIMPTLLGLCGLPIPDTV 327
|
|
| PRK12383 |
PRK12383 |
putative mutase; Provisional |
373-496 |
6.53e-03 |
|
putative mutase; Provisional
Pssm-ID: 237085 Cd Length: 406 Bit Score: 38.80 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802581430 373 KGITDQLLNQINQFD--LTVLNFANPDMVGHTGNYAACVQGLEALDVQIQRIIDFCKANHItLFLTADHGnaeemidsnN 450
Cdd:PRK12383 272 QRVMDITLDEFNTHPtaFICTNIQETDLAGHAEDVARYAERLEVVDRNLARLLEAMTPDDC-LVVMADHG---------N 341
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1802581430 451 NPV---TKHTVNKVPFVCTDTNIDLQQ--DSASLANIAPTILAYLGLKQPA 496
Cdd:PRK12383 342 DPTighSHHTREVVPLLVYQKGLQATQlgVRTTLSDVGATVCEFFGAPPPQ 392
|
|
| |
