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Conserved domains on  [gi|226735912|sp|B5FFX7|]
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RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase; Short=BPG-independent PGAM; Short=Phosphoglyceromutase; Short=iPGM

Protein Classification

2,3-bisphosphoglycerate-independent phosphoglycerate mutase( domain architecture ID 11480953)

2,3-bisphosphoglycerate-independent phosphoglycerate mutase catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate

EC:  5.4.2.12
Gene Ontology:  GO:0030145|GO:0006007|GO:0005737|GO:0046537|GO:0006096
PubMed:  10958932|2543188

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK05434 PRK05434
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
1-510 0e+00

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


:

Pssm-ID: 235463  Cd Length: 507  Bit Score: 955.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912   1 MSAKKPMALVILDGYGHRETQADNAITNANTPVLDGLMANQPNTLISASGMDVGLPDGQMGNSEVGHTNIGAGRVVYQDL 80
Cdd:PRK05434   1 MMMKKPVVLIILDGWGYREETEGNAIALAKTPNLDRLWANYPHTLLSASGLAVGLPDGQMGNSEVGHLNIGAGRIVYQDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  81 TRITKAISDGEFQQNETLVNAIDKAVKAGKAVHIMGLMSPGGVHSHEDHIYAAVEMAAARGAEKIYLHCFLDGRDTPPRS 160
Cdd:PRK05434  81 TRINKAIEDGSFFENPALLDAIDKAKKNGGALHLMGLLSDGGVHSHIDHLFALLELAKEEGVKKVYVHAFLDGRDTPPKS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 161 AENSLKNFQELFAKLGKGRIASLVGRYYAMDRDNNWERVQKAYDLMTEAKAEFTFATAVEGLEAAYAREENDEFVQATEI 240
Cdd:PRK05434 161 ALGYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVLGEGPFTAESAVEALEASYARGETDEFVKPTVI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 241 kaEGEESAAIVDGDAVIFMNYRADRARQITRTFV-PSFDGFTRnVFPAIDFVMLTQYAADIPLLCAFAPASLENTYGEWL 319
Cdd:PRK05434 241 --GGEPVAGIEDGDAVIFFNFRADRARQITRAFTdPDFDGFDR-VPKLLNFVTMTQYDADLKVPVAFPPESLKNTLGEVL 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 320 SKEGKTQLRISETEKYAHVTFFFNGGIEDEFEGEERQLVASPKVATYDLQPEMSAPELTEKLVAAIKSGKYDAIVCNFPN 399
Cdd:PRK05434 318 AKAGLTQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIILNFAN 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 400 CDMVGHTGVYDATVKAVESLDECIGKVVEAIKEVDGQLLITADHGNAEMMIDPETGGVHTAHTNLPVPLIYVGSKAIeFK 479
Cdd:PRK05434 398 PDMVGHTGNLEAAVKAVEAVDECLGRVVDAVLKVGGTLLITADHGNAEQMIDPETGQPHTAHTTNPVPFILVGGKAL-RL 476

                        490       500       510
                 ....*....|....*....|....*....|.
gi 226735912 480 EGGKLSDLAPTMLALTDTAIPAEMSGEVLFK 510
Cdd:PRK05434 477 EGGKLADIAPTILDLLGLEQPAEMTGKSLIE 507
 
Name Accession Description Interval E-value
PRK05434 PRK05434
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
1-510 0e+00

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


Pssm-ID: 235463  Cd Length: 507  Bit Score: 955.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912   1 MSAKKPMALVILDGYGHRETQADNAITNANTPVLDGLMANQPNTLISASGMDVGLPDGQMGNSEVGHTNIGAGRVVYQDL 80
Cdd:PRK05434   1 MMMKKPVVLIILDGWGYREETEGNAIALAKTPNLDRLWANYPHTLLSASGLAVGLPDGQMGNSEVGHLNIGAGRIVYQDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  81 TRITKAISDGEFQQNETLVNAIDKAVKAGKAVHIMGLMSPGGVHSHEDHIYAAVEMAAARGAEKIYLHCFLDGRDTPPRS 160
Cdd:PRK05434  81 TRINKAIEDGSFFENPALLDAIDKAKKNGGALHLMGLLSDGGVHSHIDHLFALLELAKEEGVKKVYVHAFLDGRDTPPKS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 161 AENSLKNFQELFAKLGKGRIASLVGRYYAMDRDNNWERVQKAYDLMTEAKAEFTFATAVEGLEAAYAREENDEFVQATEI 240
Cdd:PRK05434 161 ALGYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVLGEGPFTAESAVEALEASYARGETDEFVKPTVI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 241 kaEGEESAAIVDGDAVIFMNYRADRARQITRTFV-PSFDGFTRnVFPAIDFVMLTQYAADIPLLCAFAPASLENTYGEWL 319
Cdd:PRK05434 241 --GGEPVAGIEDGDAVIFFNFRADRARQITRAFTdPDFDGFDR-VPKLLNFVTMTQYDADLKVPVAFPPESLKNTLGEVL 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 320 SKEGKTQLRISETEKYAHVTFFFNGGIEDEFEGEERQLVASPKVATYDLQPEMSAPELTEKLVAAIKSGKYDAIVCNFPN 399
Cdd:PRK05434 318 AKAGLTQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIILNFAN 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 400 CDMVGHTGVYDATVKAVESLDECIGKVVEAIKEVDGQLLITADHGNAEMMIDPETGGVHTAHTNLPVPLIYVGSKAIeFK 479
Cdd:PRK05434 398 PDMVGHTGNLEAAVKAVEAVDECLGRVVDAVLKVGGTLLITADHGNAEQMIDPETGQPHTAHTTNPVPFILVGGKAL-RL 476

                        490       500       510
                 ....*....|....*....|....*....|.
gi 226735912 480 EGGKLSDLAPTMLALTDTAIPAEMSGEVLFK 510
Cdd:PRK05434 477 EGGKLADIAPTILDLLGLEQPAEMTGKSLIE 507
GpmI COG0696
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ...
 3-510 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: 949.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912   3 AKKPMALVILDGYGHRETQADNAITNANTPVLDGLMANQPNTLISASGMDVGLPDGQMGNSEVGHTNIGAGRVVYQDLTR 82
Cdd:COG0696    1 RKKPVVLIILDGWGIREETEGNAIALANTPNLDRLWATYPHTLLRASGEAVGLPDGQMGNSEVGHLNIGAGRVVYQDLTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  83 ITKAISDGEFQQNETLVNAIDKAVKAGKAVHIMGLMSPGGVHSHEDHIYAAVEMAAARGAEKIYLHCFLDGRDTPPRSAE 162
Cdd:COG0696   81 INKAIEDGSFFENPVLLDAIDKAKENGGALHLMGLLSDGGVHSHIDHLKALLELAKEEGVKKVYVHAFLDGRDTPPKSAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 163 NSLKNFQELFAKLGKGRIASLVGRYYAMDRDNNWERVQKAYDLMTEAKAEfTFATAVEGLEAAYAREENDEFVQATEIKA 242
Cdd:COG0696  161 GYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVNGEGE-TAASAVEAIEASYARGETDEFVKPTVIVD 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 243 EGEESAAIVDGDAVIFMNYRADRARQITRTFV-PSFDGFTRNVFPA-IDFVMLTQYAADIPLLCAFAPASLENTYGEWLS 320
Cdd:COG0696  240 YGKPVATIEDGDAVIFFNFRADRARQLTRAFTdPDFDGFDRGKRPKlLYFVTMTEYDETFDVPVAFPPENLKNTLGEVLA 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 321 KEGKTQLRISETEKYAHVTFFFNGGIEDEFEGEERQLVASPKVATYDLQPEMSAPELTEKLVAAIKSGKYDAIVCNFPNC 400
Cdd:COG0696  320 KAGLKQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIVLNFANP 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 401 DMVGHTGVYDATVKAVESLDECIGKVVEAIKEVDGQLLITADHGNAEMMIDPETGGVHTAHTNLPVPLIYVG-SKAIEFK 479
Cdd:COG0696  400 DMVGHTGVLEAAIKAVEAVDECLGRVVDAVLAAGGTLLITADHGNAEQMIDPDTGGPHTAHTTNPVPFILVGgDKGVKLR 479

                        490       500       510
                 ....*....|....*....|....*....|.
gi 226735912 480 EGGKLSDLAPTMLALTDTAIPAEMSGEVLFK 510
Cdd:COG0696  480 EDGRLADIAPTILELMGLPQPAEMTGKSLIE 510
iPGM cd16010
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ...
 5-508 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: 874.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912   5 KPMALVILDGYGHRETQADNAITNANTPVLDGLMANQPNTLISASGMDVGLPDGQMGNSEVGHTNIGAGRVVYQDLTRIT 84
Cdd:cd16010    1 KPVVLIILDGWGIRPEDEGNAIALAKTPNLDRLWATYPHTLLKASGEAVGLPDGQMGNSEVGHLNIGAGRIVYQDLTRIN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  85 KAISDGEFQQNETLVNAIDKAVKAGKAVHIMGLMSPGGVHSHEDHIYAAVEMAAARGAEKIYLHCFLDGRDTPPRSAENS 164
Cdd:cd16010   81 KAIEDGSFFKNEALLKAIEHAKKNNSTLHLMGLLSDGGVHSHIDHLFALLELAKKEGVKKVYVHAFTDGRDTPPKSALKY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 165 LKNFQELFAKLGKGRIASLVGRYYAMDRDNNWERVQKAYDLMTEAKAEfTFATAVEGLEAAYAREENDEFVQATEIkaeG 244
Cdd:cd16010  161 LKELEEKLKELGVGKIASVSGRYYAMDRDKRWDRTEKAYDALVLGEGE-KAESAEEAIEASYAKGITDEFIPPTVI---G 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 245 EESAAIVDGDAVIFMNYRADRARQITRTFV-PSFDGFTRNVFPAIDFVMLTQYAADIPLLCAFAPASLENTYGEWLSKEG 323
Cdd:cd16010  237 DEGGTIKDGDAVIFFNFRADRARQITRAFTdPDFDGFDRKKPKNLYFVTMTEYDKDLPVPVAFPPPKIKNTLGEVLSKAG 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 324 KTQLRISETEKYAHVTFFFNGGIEDEFEGEERQLVASPKVATYDLQPEMSAPELTEKLVAAIKSGKYDAIVCNFPNCDMV 403
Cdd:cd16010  317 LKQLRIAETEKYAHVTYFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLIEAIKSGKYDFIVVNFANPDMV 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 404 GHTGVYDATVKAVESLDECIGKVVEAIKEVDGQLLITADHGNAEMMIDPETGGVHTAHTNLPVPLIYVG-SKAIEFKEGG 482
Cdd:cd16010  397 GHTGNLEAAVKAVEAVDECLGRIVEAVLENGGTLLITADHGNAEEMIDPETGGPHTAHTTNPVPFIIVDpGLKRKLLKDG 476

                        490       500
                 ....*....|....*....|....*.
gi 226735912 483 KLSDLAPTMLALTDTAIPAEMSGEVL 508
Cdd:cd16010  477 GLADVAPTILDLLGIEKPKEMTGKSL 502
pgm_bpd_ind TIGR01307
phosphoglycerate mutase (2,3-diphosphoglycerate-independent); This protein is about double in ...
 5-509 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: 773.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912    5 KPMALVILDGYGHRETQADNAITNANTPVLDGLMANQPNTLISASGMDVGLPDGQMGNSEVGHTNIGAGRVVYQDLTRIT 84
Cdd:TIGR01307   1 KKVVLVILDGWGYRNDDDGNAIFAAKTPTMDELIAAYPYSLLDASGLDVGLPDGQMGNSEVGHLNIGAGRVVYQDLVRIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912   85 KAISDGEFQQNETLVNAIDKAVKAGKAVHIMGLMSPGGVHSHEDHIYAAVEMAAARGAEKIYLHCFLDGRDTPPRSAENS 164
Cdd:TIGR01307  81 QAIKDGEFFANPALLGAIDRAKDNNGKLHLMGLVSDGGVHSHIDHLIALIELAAERGIEKVVLHAFTDGRDTAPKSAESY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  165 LKNFQELFAKLGKGRIASLVGRYYAMDRDNNWERVQKAYDLMTEAKAeFTFATAVEGLEAAYAREENDEFVQATEIKAEG 244
Cdd:TIGR01307 161 LEQLQAFLKEIGNGRIATISGRYYAMDRDQRWDRVEIAYKAITGGDG-FEFSDPVAYIQDAYARDITDEFIKPTIIGNGG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  245 eesaAIVDGDAVIFMNYRADRARQITRTFV-PSFDGFTRNVFPAIDFVMLTQYAADIPLLCAFAPASLENTYGEWLSKEG 323
Cdd:TIGR01307 240 ----ALKDGDAVIFFNFRADRAREITRALVnSDFDGFPREKNPKLDFVTMTQYDGTFPSPVAFPPQSLTNTLGEVLAKHD 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  324 KTQLRISETEKYAHVTFFFNGGIEDEFEGEERQLVASPKVATYDLQPEMSAPELTEKLVAAIKSGKYDAIVCNFPNCDMV 403
Cdd:TIGR01307 316 LTQLRIAETEKYAHVTFFFNGGVEVPFAGETRTLIPSPKVATYDLQPEMSAKAVTDAVLEAIAQGKFDLIVVNFANPDMV 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  404 GHTGVYDATVKAVESLDECIGKVVEAIKEVDGQLLITADHGNAEMMIDpETGGVHTAHTNLPVPLIYVGSKAIEF-KEGG 482
Cdd:TIGR01307 396 GHTGNFEAAIKAVEALDVCLGRIVEACKKVGGTLFLTADHGNAEEMID-ENGNPHTAHTTNPVPFVCVGAKNVKLiREGG 474

                         490       500
                  ....*....|....*....|....*..
gi 226735912  483 KLSDLAPTMLALTDTAIPAEMSGEVLF 509
Cdd:TIGR01307 475 VLADIAPTILDLMGLEQPAEMTGKSLL 501
Metalloenzyme pfam01676
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ...
 5-494 5.34e-132

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: 389.07  E-value: 5.34e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912    5 KPMALVILDGYGHRETQADNAIT---NANTPVLDGLMANQPNTLISASGMDVGLPDGQMGNSEVGHTNIGAGRVVYQDLT 81
Cdd:pfam01676   1 KKVVLIVLDGWGDRPAEDLNAKTplhIAKTPNMDKLAKEYPEQLIGASGLAVGLPEGQMGGSDVGHLEIGGGRIVYQYLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912   82 RITKAISDGEFQQNETLVNAIDKAVKAGKAVHIMGLMSPGGVHSHEDHIYAAVEMAAARGAEKIYLHCFLDGRDTPPrsa 161
Cdd:pfam01676  81 RGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHSHIEHLLALIALAKEAGAIKVHLLGDGDDRPVGY--- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  162 enslknfqelfaklgkgriaslvgryyamdrdnnwervqkaydlmteakaeftfatavegleaayareendefvqateik 241
Cdd:pfam01676     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  242 aegeesAAIVDGDAVIFMNYRADRARQITRTFV-PSFDGFTRNVFPAIDFVMLTQYAADIPLLCAFAPASLENTYGEWLS 320
Cdd:pfam01676 158 ------ILDGDAVITINFRFDRRRARILRLFLLdPDFFDRDRVRHDALHVPTKTLYELKLPSAGAFVPEEGKNTDGEVLE 231

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  321 KEGKTQLRISETEKYAHVTFFFNGGIEDEFEGEERQLVASPKVATYDLQPEMSAPELTEKLVAAIKsGKYDAIVCNFPNC 400
Cdd:pfam01676 232 GHGLKQLRIAETEKYAHVTFFWGGGREPPFPGEERYLIPSPKVATYDLQPEMSAMEITDKLLEALK-EKYDFVFVNFANT 310

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  401 DMVGHTGVYDATVKAVESLDECIGKVVEAIKEVDGQLLITADHGNAEMMIDpetggvhTAHTNLPVPLIYVG-------- 472
Cdd:pfam01676 311 DMVGHTGDVEGKVKAIEAVDERLGELLDALEEDDGLLIITADHGNPEEMKD-------TDHTREPVPILIYGkgvrpdqv 383

                         490       500
                  ....*....|....*....|..
gi 226735912  473 SKAIEFKEGGKLSDLAPTMLAL 494
Cdd:pfam01676 384 LFGEKFRERGGLADIAATILML 405
 
Name Accession Description Interval E-value
PRK05434 PRK05434
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
1-510 0e+00

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


Pssm-ID: 235463  Cd Length: 507  Bit Score: 955.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912   1 MSAKKPMALVILDGYGHRETQADNAITNANTPVLDGLMANQPNTLISASGMDVGLPDGQMGNSEVGHTNIGAGRVVYQDL 80
Cdd:PRK05434   1 MMMKKPVVLIILDGWGYREETEGNAIALAKTPNLDRLWANYPHTLLSASGLAVGLPDGQMGNSEVGHLNIGAGRIVYQDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  81 TRITKAISDGEFQQNETLVNAIDKAVKAGKAVHIMGLMSPGGVHSHEDHIYAAVEMAAARGAEKIYLHCFLDGRDTPPRS 160
Cdd:PRK05434  81 TRINKAIEDGSFFENPALLDAIDKAKKNGGALHLMGLLSDGGVHSHIDHLFALLELAKEEGVKKVYVHAFLDGRDTPPKS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 161 AENSLKNFQELFAKLGKGRIASLVGRYYAMDRDNNWERVQKAYDLMTEAKAEFTFATAVEGLEAAYAREENDEFVQATEI 240
Cdd:PRK05434 161 ALGYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVLGEGPFTAESAVEALEASYARGETDEFVKPTVI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 241 kaEGEESAAIVDGDAVIFMNYRADRARQITRTFV-PSFDGFTRnVFPAIDFVMLTQYAADIPLLCAFAPASLENTYGEWL 319
Cdd:PRK05434 241 --GGEPVAGIEDGDAVIFFNFRADRARQITRAFTdPDFDGFDR-VPKLLNFVTMTQYDADLKVPVAFPPESLKNTLGEVL 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 320 SKEGKTQLRISETEKYAHVTFFFNGGIEDEFEGEERQLVASPKVATYDLQPEMSAPELTEKLVAAIKSGKYDAIVCNFPN 399
Cdd:PRK05434 318 AKAGLTQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIILNFAN 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 400 CDMVGHTGVYDATVKAVESLDECIGKVVEAIKEVDGQLLITADHGNAEMMIDPETGGVHTAHTNLPVPLIYVGSKAIeFK 479
Cdd:PRK05434 398 PDMVGHTGNLEAAVKAVEAVDECLGRVVDAVLKVGGTLLITADHGNAEQMIDPETGQPHTAHTTNPVPFILVGGKAL-RL 476

                        490       500       510
                 ....*....|....*....|....*....|.
gi 226735912 480 EGGKLSDLAPTMLALTDTAIPAEMSGEVLFK 510
Cdd:PRK05434 477 EGGKLADIAPTILDLLGLEQPAEMTGKSLIE 507
GpmI COG0696
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ...
 3-510 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: 949.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912   3 AKKPMALVILDGYGHRETQADNAITNANTPVLDGLMANQPNTLISASGMDVGLPDGQMGNSEVGHTNIGAGRVVYQDLTR 82
Cdd:COG0696    1 RKKPVVLIILDGWGIREETEGNAIALANTPNLDRLWATYPHTLLRASGEAVGLPDGQMGNSEVGHLNIGAGRVVYQDLTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  83 ITKAISDGEFQQNETLVNAIDKAVKAGKAVHIMGLMSPGGVHSHEDHIYAAVEMAAARGAEKIYLHCFLDGRDTPPRSAE 162
Cdd:COG0696   81 INKAIEDGSFFENPVLLDAIDKAKENGGALHLMGLLSDGGVHSHIDHLKALLELAKEEGVKKVYVHAFLDGRDTPPKSAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 163 NSLKNFQELFAKLGKGRIASLVGRYYAMDRDNNWERVQKAYDLMTEAKAEfTFATAVEGLEAAYAREENDEFVQATEIKA 242
Cdd:COG0696  161 GYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVNGEGE-TAASAVEAIEASYARGETDEFVKPTVIVD 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 243 EGEESAAIVDGDAVIFMNYRADRARQITRTFV-PSFDGFTRNVFPA-IDFVMLTQYAADIPLLCAFAPASLENTYGEWLS 320
Cdd:COG0696  240 YGKPVATIEDGDAVIFFNFRADRARQLTRAFTdPDFDGFDRGKRPKlLYFVTMTEYDETFDVPVAFPPENLKNTLGEVLA 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 321 KEGKTQLRISETEKYAHVTFFFNGGIEDEFEGEERQLVASPKVATYDLQPEMSAPELTEKLVAAIKSGKYDAIVCNFPNC 400
Cdd:COG0696  320 KAGLKQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIVLNFANP 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 401 DMVGHTGVYDATVKAVESLDECIGKVVEAIKEVDGQLLITADHGNAEMMIDPETGGVHTAHTNLPVPLIYVG-SKAIEFK 479
Cdd:COG0696  400 DMVGHTGVLEAAIKAVEAVDECLGRVVDAVLAAGGTLLITADHGNAEQMIDPDTGGPHTAHTTNPVPFILVGgDKGVKLR 479

                        490       500       510
                 ....*....|....*....|....*....|.
gi 226735912 480 EGGKLSDLAPTMLALTDTAIPAEMSGEVLFK 510
Cdd:COG0696  480 EDGRLADIAPTILELMGLPQPAEMTGKSLIE 510
iPGM cd16010
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ...
 5-508 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: 874.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912   5 KPMALVILDGYGHRETQADNAITNANTPVLDGLMANQPNTLISASGMDVGLPDGQMGNSEVGHTNIGAGRVVYQDLTRIT 84
Cdd:cd16010    1 KPVVLIILDGWGIRPEDEGNAIALAKTPNLDRLWATYPHTLLKASGEAVGLPDGQMGNSEVGHLNIGAGRIVYQDLTRIN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  85 KAISDGEFQQNETLVNAIDKAVKAGKAVHIMGLMSPGGVHSHEDHIYAAVEMAAARGAEKIYLHCFLDGRDTPPRSAENS 164
Cdd:cd16010   81 KAIEDGSFFKNEALLKAIEHAKKNNSTLHLMGLLSDGGVHSHIDHLFALLELAKKEGVKKVYVHAFTDGRDTPPKSALKY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 165 LKNFQELFAKLGKGRIASLVGRYYAMDRDNNWERVQKAYDLMTEAKAEfTFATAVEGLEAAYAREENDEFVQATEIkaeG 244
Cdd:cd16010  161 LKELEEKLKELGVGKIASVSGRYYAMDRDKRWDRTEKAYDALVLGEGE-KAESAEEAIEASYAKGITDEFIPPTVI---G 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 245 EESAAIVDGDAVIFMNYRADRARQITRTFV-PSFDGFTRNVFPAIDFVMLTQYAADIPLLCAFAPASLENTYGEWLSKEG 323
Cdd:cd16010  237 DEGGTIKDGDAVIFFNFRADRARQITRAFTdPDFDGFDRKKPKNLYFVTMTEYDKDLPVPVAFPPPKIKNTLGEVLSKAG 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 324 KTQLRISETEKYAHVTFFFNGGIEDEFEGEERQLVASPKVATYDLQPEMSAPELTEKLVAAIKSGKYDAIVCNFPNCDMV 403
Cdd:cd16010  317 LKQLRIAETEKYAHVTYFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLIEAIKSGKYDFIVVNFANPDMV 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 404 GHTGVYDATVKAVESLDECIGKVVEAIKEVDGQLLITADHGNAEMMIDPETGGVHTAHTNLPVPLIYVG-SKAIEFKEGG 482
Cdd:cd16010  397 GHTGNLEAAVKAVEAVDECLGRIVEAVLENGGTLLITADHGNAEEMIDPETGGPHTAHTTNPVPFIIVDpGLKRKLLKDG 476

                        490       500
                 ....*....|....*....|....*.
gi 226735912 483 KLSDLAPTMLALTDTAIPAEMSGEVL 508
Cdd:cd16010  477 GLADVAPTILDLLGIEKPKEMTGKSL 502
pgm_bpd_ind TIGR01307
phosphoglycerate mutase (2,3-diphosphoglycerate-independent); This protein is about double in ...
 5-509 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: 773.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912    5 KPMALVILDGYGHRETQADNAITNANTPVLDGLMANQPNTLISASGMDVGLPDGQMGNSEVGHTNIGAGRVVYQDLTRIT 84
Cdd:TIGR01307   1 KKVVLVILDGWGYRNDDDGNAIFAAKTPTMDELIAAYPYSLLDASGLDVGLPDGQMGNSEVGHLNIGAGRVVYQDLVRIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912   85 KAISDGEFQQNETLVNAIDKAVKAGKAVHIMGLMSPGGVHSHEDHIYAAVEMAAARGAEKIYLHCFLDGRDTPPRSAENS 164
Cdd:TIGR01307  81 QAIKDGEFFANPALLGAIDRAKDNNGKLHLMGLVSDGGVHSHIDHLIALIELAAERGIEKVVLHAFTDGRDTAPKSAESY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  165 LKNFQELFAKLGKGRIASLVGRYYAMDRDNNWERVQKAYDLMTEAKAeFTFATAVEGLEAAYAREENDEFVQATEIKAEG 244
Cdd:TIGR01307 161 LEQLQAFLKEIGNGRIATISGRYYAMDRDQRWDRVEIAYKAITGGDG-FEFSDPVAYIQDAYARDITDEFIKPTIIGNGG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  245 eesaAIVDGDAVIFMNYRADRARQITRTFV-PSFDGFTRNVFPAIDFVMLTQYAADIPLLCAFAPASLENTYGEWLSKEG 323
Cdd:TIGR01307 240 ----ALKDGDAVIFFNFRADRAREITRALVnSDFDGFPREKNPKLDFVTMTQYDGTFPSPVAFPPQSLTNTLGEVLAKHD 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  324 KTQLRISETEKYAHVTFFFNGGIEDEFEGEERQLVASPKVATYDLQPEMSAPELTEKLVAAIKSGKYDAIVCNFPNCDMV 403
Cdd:TIGR01307 316 LTQLRIAETEKYAHVTFFFNGGVEVPFAGETRTLIPSPKVATYDLQPEMSAKAVTDAVLEAIAQGKFDLIVVNFANPDMV 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  404 GHTGVYDATVKAVESLDECIGKVVEAIKEVDGQLLITADHGNAEMMIDpETGGVHTAHTNLPVPLIYVGSKAIEF-KEGG 482
Cdd:TIGR01307 396 GHTGNFEAAIKAVEALDVCLGRIVEACKKVGGTLFLTADHGNAEEMID-ENGNPHTAHTTNPVPFVCVGAKNVKLiREGG 474

                         490       500
                  ....*....|....*....|....*..
gi 226735912  483 KLSDLAPTMLALTDTAIPAEMSGEVLF 509
Cdd:TIGR01307 475 VLADIAPTILDLMGLEQPAEMTGKSLL 501
Metalloenzyme pfam01676
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ...
 5-494 5.34e-132

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: 389.07  E-value: 5.34e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912    5 KPMALVILDGYGHRETQADNAIT---NANTPVLDGLMANQPNTLISASGMDVGLPDGQMGNSEVGHTNIGAGRVVYQDLT 81
Cdd:pfam01676   1 KKVVLIVLDGWGDRPAEDLNAKTplhIAKTPNMDKLAKEYPEQLIGASGLAVGLPEGQMGGSDVGHLEIGGGRIVYQYLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912   82 RITKAISDGEFQQNETLVNAIDKAVKAGKAVHIMGLMSPGGVHSHEDHIYAAVEMAAARGAEKIYLHCFLDGRDTPPrsa 161
Cdd:pfam01676  81 RGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHSHIEHLLALIALAKEAGAIKVHLLGDGDDRPVGY--- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  162 enslknfqelfaklgkgriaslvgryyamdrdnnwervqkaydlmteakaeftfatavegleaayareendefvqateik 241
Cdd:pfam01676     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  242 aegeesAAIVDGDAVIFMNYRADRARQITRTFV-PSFDGFTRNVFPAIDFVMLTQYAADIPLLCAFAPASLENTYGEWLS 320
Cdd:pfam01676 158 ------ILDGDAVITINFRFDRRRARILRLFLLdPDFFDRDRVRHDALHVPTKTLYELKLPSAGAFVPEEGKNTDGEVLE 231

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  321 KEGKTQLRISETEKYAHVTFFFNGGIEDEFEGEERQLVASPKVATYDLQPEMSAPELTEKLVAAIKsGKYDAIVCNFPNC 400
Cdd:pfam01676 232 GHGLKQLRIAETEKYAHVTFFWGGGREPPFPGEERYLIPSPKVATYDLQPEMSAMEITDKLLEALK-EKYDFVFVNFANT 310

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  401 DMVGHTGVYDATVKAVESLDECIGKVVEAIKEVDGQLLITADHGNAEMMIDpetggvhTAHTNLPVPLIYVG-------- 472
Cdd:pfam01676 311 DMVGHTGDVEGKVKAIEAVDERLGELLDALEEDDGLLIITADHGNPEEMKD-------TDHTREPVPILIYGkgvrpdqv 383

                         490       500
                  ....*....|....*....|..
gi 226735912  473 SKAIEFKEGGKLSDLAPTMLAL 494
Cdd:pfam01676 384 LFGEKFRERGGLADIAATILML 405
iPGM_N pfam06415
BPG-independent PGAM N-terminus (iPGM_N); This family represents the N-terminal region of the ...
 83-298 6.42e-123

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: 358.64  E-value: 6.42e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912   83 ITKAISDGEFQQNETLVNAIDKAVKAGKAVHIMGLMSPGGVHSHEDHIYAAVEMAAARGAEKIYLHCFLDGRDTPPRSAE 162
Cdd:pfam06415   1 INKAIEDGSFFENPALLKAIENAKANGGALHLMGLLSDGGVHSHIDHLFALLELAKEEGVKKVYVHAFLDGRDTPPKSAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  163 NSLKNFQELFAKLGKGRIASLVGRYYAMDRDNNWERVQKAYDLMTEAKAEFtFATAVEGLEAAYAREENDEFVQATEIKA 242
Cdd:pfam06415  81 GYLEQLEAKLAELGVGKIATVSGRYYAMDRDKRWDRVEKAYDALVLGEGES-AADAVEAIEASYARGETDEFVKPTVIVD 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 226735912  243 EGEESAAIVDGDAVIFMNYRADRARQITRTFV-PSFDGFTRNVFPA-IDFVMLTQYAA 298
Cdd:pfam06415 160 DGKPVGTIKDGDSVIFFNFRPDRAREITRAFTdPDFDGFERRKRPKdLHFVTMTQYDA 217
PLN02538 PLN02538
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
 4-503 1.99e-121

2,3-bisphosphoglycerate-independent phosphoglycerate mutase


Pssm-ID: 215295  Cd Length: 558  Bit Score: 367.08  E-value: 1.99e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912   4 KKPMALVILDGYGHRETQADNAITNANTPVLDGLMANQPNT--LISASGMDVGLP-DGQMGNSEVGHTNIGAGRVVYQDL 80
Cdd:PLN02538  20 GKPLLLIVLDGWGENAPDEFNAIHVAPTPTMDSLKAGAPERwrLVKAHGTAVGLPsDDDMGNSEVGHNALGAGRIFAQGA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  81 TRITKAISDGEFQQNETLvNAIDKAVKAGkAVHIMGLMSPGGVHSHEDHIYAAVEMAAARGAEKIYLHCFLDGRDTPPRS 160
Cdd:PLN02538 100 KLVDLALASGKIFEGEGF-KYIKEAFATG-TLHLIGLLSDGGVHSRLDQLQLLLKGAAERGAKRIRVHVLTDGRDVPDGS 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 161 AENSLKNFQELFAKL-GKG---RIASLVGRYY-AMDR-DNNWERVQKAYDLMTEAKAEFTFATAVEGLEAAyaREE---- 230
Cdd:PLN02538 178 SVGFVETLEKDLAELrEKGcdaRIASGGGRMYvTMDRyENDWNVVKRGWDAHVLGEAPHKFKSALEAVKKL--REEpppa 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 231 NDEFVQATEI-KAEGEESAAIVDGDAVIFMNYRADRARQITRTFV-PSFDGFTRNVFPAIDFVMLTQYAAD--IPLLCAF 306
Cdd:PLN02538 256 NDQYLPPFVIvDEDGKPVGPIEDGDAVVTFNFRADRMVMIAKALEyEDFDKFDRVRVPKIRYAGMLQYDGElkLPSHYLV 335

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 307 APASLENTYGEWLSKEGKTQLRISETEKYAHVTFFFNGGIEDEF--EGEERQLVASPKVATYDLQPEMSAPELTEKLVAA 384
Cdd:PLN02538 336 SPPLIERTSGEYLVANGVRTFACSETVKFGHVTFFWNGNRSGYFneKLEEYVEIPSDNGIPFNVQPKMKALEIAEKARDA 415

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 385 IKSGKYDAIVCNFPNCDMVGHTGVYDATVKAVESLDECIGKVVEAIKEVDGQLLITADHGNAEMMIDPETGG-------- 456
Cdd:PLN02538 416 LLSGKFDQVRVNLANGDMVGHTGDLEATIVACEAVDAAVKEILDAVEQVGGIYLVTADHGNAEDMVKRDKSGkplldkdg 495

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 226735912 457 ---VHTAHTNLPVPLIYVG---SKAIEFKEG---GKLSDLAPTMLALTDTAIPAEM 503
Cdd:PLN02538 496 npqILTSHTLAPVPVAIGGpglPPGVRFRDDlptAGLANVAATVMNLHGFEAPADY 551
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 388-494 6.53e-10

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: 59.36  E-value: 6.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 388 GKYDAIVCNFPNCDMVGHT--GVYDATVKAVESLDECIGKVVEAIKEV----DGQLLITADHGNAEMMIDPETGGVHTA- 460
Cdd:cd00016  118 EKPFVLFLHFDGPDGPGHAygPNTPEYYDAVEEIDERIGKVLDALKKAgdadDTVIIVTADHGGIDKGHGGDPKADGKAd 197

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 226735912 461 --HTNLPVPLIYVGSKAiefKEGGKLS------DLAPTMLAL 494
Cdd:cd00016  198 ksHTGMRVPFIAYGPGV---KKGGVKHelisqyDIAPTLADL 236
sulfatase_like cd16152
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 415-508 8.91e-08

uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.


Pssm-ID: 293771 [Multi-domain]  Cd Length: 373  Bit Score: 54.16  E-value: 8.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 415 AVESLDECIGKVVEAIKEV----DGQLLITADHG------NAEMMIDPETGGVHtahtnlpVPLIYVGSKaieFKEGGK- 483
Cdd:cd16152  180 CCERLDENVGRIRDALKELglydNTIIVFTSDHGchfrtrNAEYKRSCHESSIR-------VPLVIYGPG---FNGGGRv 249

                         90       100       110
                 ....*....|....*....|....*....|
gi 226735912 484 -----LSDLAPTMLALTDTAIPAEMSGEVL 508
Cdd:cd16152  250 eelvsLIDLPPTLLDAAGIDVPEEMQGRSL 279
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 377-451 1.48e-07

c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal transduction mechanisms];


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 53.60  E-value: 1.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 377 LTEKLVAAIKSGKYDAIVCNFPNCDMVGH-TGV-YDATVKAVESLDECIGKVVEAIKEVDG----QLLITADHGnaemMI 450
Cdd:COG1524  170 IAAAALELLREGRPDLLLVYLPDLDYAGHrYGPdSPEYRAALREVDAALGRLLDALKARGLyegtLVIVTADHG----MV 245


                 .
gi 226735912 451 D 451
Cdd:COG1524  246 D 246
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 416-509 2.08e-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: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 52.93  E-value: 2.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 416 VESLDECIGKVVEAIKEV----DGQLLITADHGnaEMMidpetgGVH-----------TAHtnlpVPLIYVGSKaieFKE 480
Cdd:cd16037  168 VEFLDENIGRVLDALEELglldNTLIIYTSDHG--DML------GERglwgkstmyeeSVR----VPMIISGPG---IPA 232

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 226735912 481 GGK------LSDLAPTMLALTDTAIPAEMSGEVLF 509
Cdd:cd16037  233 GKRvktpvsLVDLAPTILEAAGAPPPPDLDGRSLL 267
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
407-506 1.27e-06

Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 50.65  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 407 GVYDAtvkAVESLDECIGKVVEAIKEvDGQL-----LITADHGnaEMMIDP----------EtGGVHtahtnlpVPLIYV 471
Cdd:COG3119  200 AAYAA---MIEEVDDQVGRLLDALEE-LGLAdntivVFTSDNG--PSLGEHglrggkgtlyE-GGIR-------VPLIVR 265

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 226735912 472 GSKAIefKEGGK------LSDLAPTMLALTDTAIPAEMSGE 506
Cdd:COG3119  266 WPGKI--KAGSVsdalvsLIDLLPTLLDLAGVPIPEDLDGR 304
apgM TIGR00306
phosphoglycerate mutase (2,3-diphosphoglycerate-independent), archaeal form; Experimentally ...
 390-472 1.89e-06

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: 50.16  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  390 YDAIVCNFPNCDMVGHTGVYDATVKAVESLDECIGKVVEAIKEVDGQLLITADHGN-AEMMIdpetggvhtaHTNLPVPL 468
Cdd:TIGR00306 288 YDFVLVHTKGPDEAGHDGDPELKVRAIEKIDSKIVGPLLALDLDETRLILTADHSTpVEVKD----------HSADPVPI 357


                  ....
gi 226735912  469 IYVG 472
Cdd:TIGR00306 358 VIVG 361
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
 416-506 4.78e-06

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: 47.82  E-value: 4.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 416 VESLDECIGKVVEAIKEvDGQL-----LITADHGnaEMMIDPET---------GGVHtahtnlpVPLIYVGSKAIEfkeG 481
Cdd:cd16022  137 VSAIDDQIGRILDALEE-LGLLdntliVFTSDHG--DMLGDHGLrgkkgslyeGGIR-------VPFIVRWPGKIP---A 203

                         90       100       110
                 ....*....|....*....|....*....|..
gi 226735912 482 GKLS-------DLAPTMLALTDTAIPAEMSGE 506
Cdd:cd16022  204 GQVSdalvsllDLLPTLLDLAGIEPPEGLDGR 235
iPGM_like cd16011
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate ...
 377-473 4.90e-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: 48.62  E-value: 4.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 377 LTEKLVAAIKS-GKYDAIVCNFPNCDMVGHTGVYDATVKAVESLDECIGK-VVEAIKEVDGQLLITADHGNaemmidPET 454
Cdd:cd16011  243 YEGKAEAALEAlKDYDFVFVHVKAPDEAGHDGDPEAKVKAIERIDKAIVGpLLELLDGEDFVIVVTPDHST------PCS 316

                         90
                 ....*....|....*....
gi 226735912 455 GGVHTAHtnlPVPLIYVGS 473
Cdd:cd16011  317 LKTHSGD---PVPFLIYGP 332
PPM cd16009
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ...
 378-492 7.12e-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: 48.22  E-value: 7.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 378 TEKLVAAIKSGKYDAIVCNFPNCDMV-GH----TGvYdatVKAVESLDECIGKVVEAIKEvDGQLLITADHGNaemmiDP 452
Cdd:cd16009  259 MEKTLEALKEDFNGLIFTNLVDFDMLyGHrrdpEG-Y---AEALEEFDRRLPELLAKLKE-DDLLIITADHGN-----DP 328

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 226735912 453 ETGgvHTAHT--NLPVpLIYvgSKAIEFKEGGK---LSDLAPTML 492
Cdd:cd16009  329 TIG--GTDHTreYVPL-LVY--GKGLKGVNLGTretFADIGATIA 368
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
 415-509 8.20e-06

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: 47.89  E-value: 8.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 415 AVESLDECIGKVVEAIKEvDGQL-----LITADHGNA---------EmmidpetGGVHtahtnlpVPLI-YVGSKaieFK 479
Cdd:cd16027  194 EIERLDQQVGEILDELEE-DGLLdntivIFTSDHGMPfprakgtlyD-------SGLR-------VPLIvRWPGK---IK 255

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 226735912 480 EGGK------LSDLAPTMLALTDTAIPAEMSGEVLF 509
Cdd:cd16027  256 PGSVsdalvsFIDLAPTLLDLAGIEPPEYLQGRSFL 291
DeoB COG1015
Phosphopentomutase [Carbohydrate transport and metabolism];
376-494 9.09e-06

Phosphopentomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440639  Cd Length: 385  Bit Score: 47.74  E-value: 9.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 376 ELTEKLVAAIKSGKYDAIVCNFPNCDMV-GH----TGvYdatVKAVESLDECIGKVVEAIKEvDGQLLITADHGNaemmi 450
Cdd:COG1015  257 DGMDKTLEAMDEAFGGLIFTNLVDFDSLyGHrrdvAG-Y---AKALEEFDARLPELLAALRP-DDLLIITADHGN----- 326

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 226735912 451 DPETGGvhTAHTNLPVPLIYVGSKaieFKEGGKL------SDLAPTMLAL 494
Cdd:COG1015  327 DPTWPG--TDHTREYVPLLVYGPG---LKPGGNLgtretfADIGATIADH 371
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 415-505 9.94e-06

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: 47.95  E-value: 9.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 415 AVESLDECIGKVVEAIKE---VDGQLLI-TADHGnaEMMidpetgGVH-TAHTNLP------VPLIYVGSKAIefKEGGK 483
Cdd:cd16034  232 MITALDDNIGRLLDALKElglLENTIVVfTSDHG--DML------GSHgLMNKQVPyeesirVPFIIRYPGKI--KAGRV 301

                         90       100
                 ....*....|....*....|....*...
gi 226735912 484 LS------DLAPTMLALTDTAIPAEMSG 505
Cdd:cd16034  302 VDllintvDIMPTLLGLCGLPIPDTVEG 329
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 409-510 1.27e-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: 46.77  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 409 YDATVKAVeslDECIGKVVEAIKEvDGQL-----LITADHGnaEMMIDPETGGVHTAH---TNLPVPLIYVGSKaieFKE 480
Cdd:cd16148  165 YDAEVRYV---DEQIGRLLDKLKE-LGLLedtlvIVTSDHG--EEFGEHGLYWGHGSNlydEQLHVPLIIRWPG---KEP 235

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 226735912 481 GGKLS------DLAPTMLALTDTAIPAEMSGEVLFK 510
Cdd:cd16148  236 GKRVDalvshiDIAPTLLDLLGVEPPDYSDGRSLLP 271
PRK04024 PRK04024
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
379-472 1.58e-05

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


Pssm-ID: 235203  Cd Length: 412  Bit Score: 47.21  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 379 EKLVAAIKsgKYDAIVCNFPNCDMVGHTGVYDATVKAVESLDECIGKVVEAIKEVDGQLLITADHGNAEMMIDpetggvh 458
Cdd:PRK04024 285 KAAVELLK--EYDFVLLNIKGTDEAGHDGDFEGKVEVIEKIDKMLGYILDNLDLDEVYIAVTGDHSTPVEVKD------- 355

                         90
                 ....*....|....
gi 226735912 459 taHTNLPVPLIYVG 472
Cdd:PRK04024 356 --HSGDPVPILIYG 367
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
 420-510 2.85e-05

uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; 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: 293775 [Multi-domain]  Cd Length: 468  Bit Score: 46.61  E-value: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 420 DECIGKVVEAIKEV--DGQLLITADHGnaEMMidpetgGVHTAHTNLP--------VPLIyvgskaIEFKEGGKLS---- 485
Cdd:cd16156  251 DYEIGRVLDAADEIaeDAWVIYTSDHG--DML------GAHKLWAKGPavydeitnIPLI------IRGKGGEKAGtvtd 316

                         90       100       110
                 ....*....|....*....|....*....|.
gi 226735912 486 ------DLAPTMLALTDTAIPAEMSGEVLFK 510
Cdd:cd16156  317 tpvshiDLAPTILDYAGIPQPKVLEGESILA 347
PRK05362 PRK05362
phosphopentomutase; Provisional
 376-470 3.95e-05

phosphopentomutase; Provisional


Pssm-ID: 235430  Cd Length: 394  Bit Score: 45.88  E-value: 3.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 376 ELTEKLVAAIKSGKYDAIV-CNFPNCDMV-GH----TGvYdatVKAVESLDECIGKVVEAIKEvDGQLLITADHGNaemm 449
Cdd:PRK05362 263 DGMDATIEEMKEAGDNGLVfTNLVDFDSLyGHrrdvAG-Y---AAALEEFDARLPELLAALKE-DDLLIITADHGN---- 333

                         90       100
                 ....*....|....*....|...
gi 226735912 450 iDPETGGvhTAHT--NLPVpLIY 470
Cdd:PRK05362 334 -DPTWPG--TDHTreYVPL-LVY 352
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 416-508 5.35e-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: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 45.63  E-value: 5.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 416 VESLDECIGKVVEAIKEvDGQL-----LITADHGNA-------------EmmidpetggvHTAHtnlpVPLIYVGsKAIe 477
Cdd:cd16155  198 ITHLDAQIGRILDALEA-SGELdntiiVFTSDHGLAvgshglmgkqnlyE----------HSMR----VPLIISG-PGI- 260

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 226735912 478 fKEGGK------LSDLAPTMLALTDTAIPAEMSGEVL 508
Cdd:cd16155  261 -PKGKRrdalvyLQDVFPTLCELAGIEIPESVEGKSL 296
PRK12383 PRK12383
putative mutase; Provisional
 369-491 5.44e-05

putative mutase; Provisional


Pssm-ID: 237085  Cd Length: 406  Bit Score: 45.34  E-value: 5.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 369 QPEMSAPELTEKLVAAIKSGKYDAIVCNFPNCDMVGH---TGVYdatVKAVESLDECIGKVVEAIKEVDgQLLITADHGN 445
Cdd:PRK12383 266 QNLVDTQRVMDITLDEFNTHPTAFICTNIQETDLAGHaedVARY---AERLEVVDRNLARLLEAMTPDD-CLVVMADHGN 341

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 226735912 446 aemmiDPETGgvHTAHTNLPVPLIYV--GSKAIEFKEGGKLSDLAPTM 491
Cdd:PRK12383 342 -----DPTIG--HSHHTREVVPLLVYqkGLQATQLGVRTTLSDVGATV 382
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 397-496 9.64e-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: 9.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 397 FPNCDMVGHT-GVY-DATVKAVESLDECIGKVVEAIKEVDGQ----LLITADHGnaemMIDPETGGVHTAHTNLPVPLIY 470
Cdd:cd16018  164 FEEPDSAGHKyGPDsPEVNEALKRVDRRLGYLIEALKERGLLddtnIIVVSDHG----MTDVGTHGYDNELPDMRAIFIA 239

                         90       100       110
                 ....*....|....*....|....*....|.
gi 226735912 471 VGSKaieFKEGGKLS-----DLAPTMLALTD 496
Cdd:cd16018  240 RGPA---FKKGKKLGpfrnvDIYPLMCNLLG 267
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
 416-505 4.03e-04

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: 43.02  E-value: 4.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 416 VESLDECIGKVVEAIKEvDGQL---LI--TADHGnaEMMIDP---ETGGVHTA--HtnlpVPLI----------YVGSKA 475
Cdd:cd16028  244 IAEVDDHLGRLFDYLKE-TGQWddtLIvfTSDHG--EQLGDHwlwGKDGFFDQayR----VPLIvrdprreadaTRGQVV 316

                         90       100       110
                 ....*....|....*....|....*....|
gi 226735912 476 IEFKEggkLSDLAPTMLALTDTAIPAEMSG 505
Cdd:cd16028  317 DAFTE---SVDVMPTILDWLGGEIPHQCDG 343
sulfatase_like cd16153
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 419-510 4.31e-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: 293772 [Multi-domain]  Cd Length: 282  Bit Score: 42.36  E-value: 4.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 419 LDECIGKVVEAIK---EVDGQ----LLITADHGnAEMMIDpetgGVHTAHTNLP----VPLIYVGSKAIEFKEGGKLS-- 485
Cdd:cd16153  177 GDAQVGRAVEAFKaysLKQDRdytiVYVTGDHG-WHLGEQ----GILAKFTFWPqshrVPLIVVSSDKLKAPAGKVRHdf 251

                         90       100       110
                 ....*....|....*....|....*....|.
gi 226735912 486 ----DLAPTMLALT--DTAIPAEMSGEVLFK 510
Cdd:cd16153  252 vefvDLAPTLLAAAgvDVDAPDYLDGRDLFE 282
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 419-508 1.01e-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: 293757 [Multi-domain]  Cd Length: 411  Bit Score: 41.44  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 419 LDECIGKVVEAIKEVdGQ-----LLITADHGnaEMMidpetgGVHTAHTNLP--------VPLIYVGSKAIEfkEGGK-- 483
Cdd:cd16033  226 IDDAIGRILDALEEL-GLaddtlVIFTSDHG--DAL------GAHRLWDKGPfmyeetyrIPLIIKWPGVIA--AGQVvd 294

                         90       100
                 ....*....|....*....|....*....
gi 226735912 484 ----LSDLAPTMLALTDTAIPAEMSGEVL 508
Cdd:cd16033  295 efvsLLDLAPTILDLAGVDVPPKVDGRSL 323
ALP cd16012
Alkaline Phosphatase; Alkaline phosphatases are non-specific membrane-bound ...
 401-479 1.31e-03

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: 40.87  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912 401 DMVGHTGVYDATVKAVESLDECIGKVVEAIKEVDGQLLI-TADHGnaemmidpetggvhTAHTNLPVPLIYVGSKAIEFK 479
Cdd:cd16012  201 DWAGHANDAARAIEETLAFDKAVKVALDFAKKDGDTLVIvTADHE--------------TGHTGEDVPVFAYGPGAELFG 266
Sulfatase pfam00884
Sulfatase;
399-496 2.33e-03

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 40.10  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226735912  399 NCDMVGHTGVYDATVkavESLDECIGKVVEAIKEvDGQ-----LLITADHGnaEMMIDPETGGVHTAHTNLP-----VPL 468
Cdd:pfam00884 192 SCSEEQLLNSYDNTL---LYTDDAIGRVLDKLEE-NGLldntlVVYTSDHG--ESLGEGGGYLHGGKYDNAPeggyrVPL 265

                          90       100       110
                  ....*....|....*....|....*....|....
gi 226735912  469 IYVGSKAIefKEGGK------LSDLAPTMLALTD 496
Cdd:pfam00884 266 LIWSPGGK--AKGQKsealvsHVDLFPTILDLAG 297
PRK04200 PRK04200
cofactor-independent phosphoglycerate mutase; Provisional
 401-470 8.59e-03

cofactor-independent phosphoglycerate mutase; Provisional


Pssm-ID: 179781  Cd Length: 395  Bit Score: 38.70  E-value: 8.59e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226735912 401 DMVGHTGVYDATVKAVESLDECI-GKVVEAIKEV-DGQLLITADHgnaemmidPETGGVHTaHTNLPVP-LIY 470
Cdd:PRK04200 295 DEAGHEGDLEAKIKAIEDIDERVvGPILEALKKYeDYRILVLPDH--------PTPIELKT-HTADPVPfLIY 358
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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