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Conserved domains on  [gi|1277125586|gb|PIR27579|]
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phosphoglycerate mutase (2,3-diphosphoglycerate-independent) [Candidatus Berkelbacteria bacterium CG11_big_fil_rev_8_21_14_0_20_42_15]

Protein Classification

2,3-bisphosphoglycerate-independent phosphoglycerate mutase( domain architecture ID 10887757)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
iPGM cd16010
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ...
 6-513 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: 766.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586   6 RVALIVLDGWGLGPPWGGNAITAAKTSNMDYFWRNYCRTTLVACGEAVGLPSGTSGNSETGHLNIGAGRIVPQDLPYINT 85
Cdd:cd16010     2 PVVLIILDGWGIRPEDEGNAIALAKTPNLDRLWATYPHTLLKASGEAVGLPDGQMGNSEVGHLNIGAGRIVYQDLTRINK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586  86 LIKDGQFFKNPRILAAFEQVKKNNSRLHLMGLVGFGRVHSDMSHLFALLKMARDNDLQQVYLDLFTDGRDSDPSSALSVL 165
Cdd:cd16010    82 AIEDGSFFKNEALLKAIEHAKKNNSTLHLMGLLSDGGVHSHIDHLFALLELAKKEGVKKVYVHAFTDGRDTPPKSALKYL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 166 ELITNRIQEIGIGRITTICGRYFAMDRDRNWGRTSRAYNALTKGEAEVSPSIRDVISRAYLRNITDEYIKPHLIVGAGQe 245
Cdd:cd16010   162 KELEEKLKELGVGKIASVSGRYYAMDRDKRWDRTEKAYDALVLGEGEKAESAEEAIEASYAKGITDEFIPPTVIGDEGG- 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 246 kvLVGDNDAVIFFNFRPDRARQITRAFTtvrMPELP--DRKILSNLYFLTFVNREPNPLGTPAFEPHIIKNTLAEVVSHA 323
Cdd:cd16010   241 --TIKDGDAVIFFNFRADRARQITRAFT---DPDFDgfDRKKPKNLYFVTMTEYDKDLPVPVAFPPPKIKNTLGEVLSKA 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 324 GLRQFHIAETEKYAHVTYFINGGCEEPFPGELQYMVPSPKVPTYDFTPAMSAAKITAKIVSVVWEN-FDLIIGNYANADM 402
Cdd:cd16010   316 GLKQLRIAETEKYAHVTYFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLIEAIKSGkYDFIVVNFANPDM 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 403 VGHVGNFYAAVQAIEFVDLCLGKITNALLKNNYVVFITADHGNAEEMLNPRTNQPQTEHTSNPVPLVIVSKDIsvaRLKL 482
Cdd:cd16010   396 VGHTGNLEAAVKAVEAVDECLGRIVEAVLENGGTLLITADHGNAEEMIDPETGGPHTAHTTNPVPFIIVDPGL---KRKL 472

                         490       500       510
                  ....*....|....*....|....*....|.
gi 1277125586 483 KPGGALSNIAPTILEIMGLEKPPEMTAISLI 513
Cdd:cd16010   473 LKDGGLADVAPTILDLLGIEKPKEMTGKSLI 503
 
Name Accession Description Interval E-value
iPGM cd16010
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ...
 6-513 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: 766.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586   6 RVALIVLDGWGLGPPWGGNAITAAKTSNMDYFWRNYCRTTLVACGEAVGLPSGTSGNSETGHLNIGAGRIVPQDLPYINT 85
Cdd:cd16010     2 PVVLIILDGWGIRPEDEGNAIALAKTPNLDRLWATYPHTLLKASGEAVGLPDGQMGNSEVGHLNIGAGRIVYQDLTRINK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586  86 LIKDGQFFKNPRILAAFEQVKKNNSRLHLMGLVGFGRVHSDMSHLFALLKMARDNDLQQVYLDLFTDGRDSDPSSALSVL 165
Cdd:cd16010    82 AIEDGSFFKNEALLKAIEHAKKNNSTLHLMGLLSDGGVHSHIDHLFALLELAKKEGVKKVYVHAFTDGRDTPPKSALKYL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 166 ELITNRIQEIGIGRITTICGRYFAMDRDRNWGRTSRAYNALTKGEAEVSPSIRDVISRAYLRNITDEYIKPHLIVGAGQe 245
Cdd:cd16010   162 KELEEKLKELGVGKIASVSGRYYAMDRDKRWDRTEKAYDALVLGEGEKAESAEEAIEASYAKGITDEFIPPTVIGDEGG- 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 246 kvLVGDNDAVIFFNFRPDRARQITRAFTtvrMPELP--DRKILSNLYFLTFVNREPNPLGTPAFEPHIIKNTLAEVVSHA 323
Cdd:cd16010   241 --TIKDGDAVIFFNFRADRARQITRAFT---DPDFDgfDRKKPKNLYFVTMTEYDKDLPVPVAFPPPKIKNTLGEVLSKA 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 324 GLRQFHIAETEKYAHVTYFINGGCEEPFPGELQYMVPSPKVPTYDFTPAMSAAKITAKIVSVVWEN-FDLIIGNYANADM 402
Cdd:cd16010   316 GLKQLRIAETEKYAHVTYFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLIEAIKSGkYDFIVVNFANPDM 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 403 VGHVGNFYAAVQAIEFVDLCLGKITNALLKNNYVVFITADHGNAEEMLNPRTNQPQTEHTSNPVPLVIVSKDIsvaRLKL 482
Cdd:cd16010   396 VGHTGNLEAAVKAVEAVDECLGRIVEAVLENGGTLLITADHGNAEEMIDPETGGPHTAHTTNPVPFIIVDPGL---KRKL 472

                         490       500       510
                  ....*....|....*....|....*....|.
gi 1277125586 483 KPGGALSNIAPTILEIMGLEKPPEMTAISLI 513
Cdd:cd16010   473 LKDGGLADVAPTILDLLGIEKPKEMTGKSLI 503
GpmI COG0696
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ...
 4-513 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: 756.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586   4 KARVALIVLDGWGLGPPWGGNAITAAKTSNMDYFWRNYCRTTLVACGEAVGLPSGTSGNSETGHLNIGAGRIVPQDLPYI 83
Cdd:COG0696     2 KKPVVLIILDGWGIREETEGNAIALANTPNLDRLWATYPHTLLRASGEAVGLPDGQMGNSEVGHLNIGAGRVVYQDLTRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586  84 NTLIKDGQFFKNPRILAAFEQVKKNNSRLHLMGLVGFGRVHSDMSHLFALLKMARDNDLQQVYLDLFTDGRDSDPSSALS 163
Cdd:COG0696    82 NKAIEDGSFFENPVLLDAIDKAKENGGALHLMGLLSDGGVHSHIDHLKALLELAKEEGVKKVYVHAFLDGRDTPPKSALG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 164 VLELITNRIQEIGIGRITTICGRYFAMDRDRNWGRTSRAYNALTKGEAEVSPSIRDVISRAYLRNITDEYIKPHLIVGAG 243
Cdd:COG0696   162 YLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVNGEGETAASAVEAIEASYARGETDEFVKPTVIVDYG 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 244 QEKVLVGDNDAVIFFNFRPDRARQITRAFTTVRMPELPDRKILSNLYFLTFVNREPNPLGTPAFEPHIIKNTLAEVVSHA 323
Cdd:COG0696   242 KPVATIEDGDAVIFFNFRADRARQLTRAFTDPDFDGFDRGKRPKLLYFVTMTEYDETFDVPVAFPPENLKNTLGEVLAKA 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 324 GLRQFHIAETEKYAHVTYFINGGCEEPFPGELQYMVPSPKVPTYDFTPAMSAAKITAKIVSVVWEN-FDLIIGNYANADM 402
Cdd:COG0696   322 GLKQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGkYDFIVLNFANPDM 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 403 VGHVGNFYAAVQAIEFVDLCLGKITNALLKNNYVVFITADHGNAEEMLNPRTNQPQTEHTSNPVPLVIVSKDISVarlKL 482
Cdd:COG0696   402 VGHTGVLEAAIKAVEAVDECLGRVVDAVLAAGGTLLITADHGNAEQMIDPDTGGPHTAHTTNPVPFILVGGDKGV---KL 478

                         490       500       510
                  ....*....|....*....|....*....|.
gi 1277125586 483 KPGGALSNIAPTILEIMGLEKPPEMTAISLI 513
Cdd:COG0696   479 REDGRLADIAPTILELMGLPQPAEMTGKSLI 509
PRK05434 PRK05434
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
1-513 0e+00

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


Pssm-ID: 235463  Cd Length: 507  Bit Score: 737.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586   1 MREKARVALIVLDGWGLGPPWGGNAITAAKTSNMDYFWRNYCRTTLVACGEAVGLPSGTSGNSETGHLNIGAGRIVPQDL 80
Cdd:PRK05434    1 MMMKKPVVLIILDGWGYREETEGNAIALAKTPNLDRLWANYPHTLLSASGLAVGLPDGQMGNSEVGHLNIGAGRIVYQDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586  81 PYINTLIKDGQFFKNPRILAAFEQVKKNNSRLHLMGLVGFGRVHSDMSHLFALLKMARDNDLQQVYLDLFTDGRDSDPSS 160
Cdd:PRK05434   81 TRINKAIEDGSFFENPALLDAIDKAKKNGGALHLMGLLSDGGVHSHIDHLFALLELAKEEGVKKVYVHAFLDGRDTPPKS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 161 ALSVLELITNRIQEIGIGRITTICGRYFAMDRDRNWGRTSRAYNALTKGEAEV-SPSIRDVISRAYLRNITDEYIKPhlI 239
Cdd:PRK05434  161 ALGYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVLGEGPFtAESAVEALEASYARGETDEFVKP--T 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 240 VGAGQEKVLVGDNDAVIFFNFRPDRARQITRAFTtvrMPELP--DRKIlSNLYFLTFVNREPNpLGTP-AFEPHIIKNTL 316
Cdd:PRK05434  239 VIGGEPVAGIEDGDAVIFFNFRADRARQITRAFT---DPDFDgfDRVP-KLLNFVTMTQYDAD-LKVPvAFPPESLKNTL 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 317 AEVVSHAGLRQFHIAETEKYAHVTYFINGGCEEPFPGELQYMVPSPKVPTYDFTPAMSAAKITAKIVSVVWEN-FDLIIG 395
Cdd:PRK05434  314 GEVLAKAGLTQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGkYDFIIL 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 396 NYANADMVGHVGNFYAAVQAIEFVDLCLGKITNALLKNNYVVFITADHGNAEEMLNPRTNQPQTEHTSNPVPLVIVSKDI 475
Cdd:PRK05434  394 NFANPDMVGHTGNLEAAVKAVEAVDECLGRVVDAVLKVGGTLLITADHGNAEQMIDPETGQPHTAHTTNPVPFILVGGKA 473

                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 1277125586 476 svarlKLKPGGALSNIAPTILEIMGLEKPPEMTAISLI 513
Cdd:PRK05434  474 -----LRLEGGKLADIAPTILDLLGLEQPAEMTGKSLI 506
pgm_bpd_ind TIGR01307
phosphoglycerate mutase (2,3-diphosphoglycerate-independent); This protein is about double in ...
 5-513 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: 605.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586   5 ARVALIVLDGWGLGPPWGGNAITAAKTSNMDYFWRNYCRTTLVACGEAVGLPSGTSGNSETGHLNIGAGRIVPQDLPYIN 84
Cdd:TIGR01307   1 KKVVLVILDGWGYRNDDDGNAIFAAKTPTMDELIAAYPYSLLDASGLDVGLPDGQMGNSEVGHLNIGAGRVVYQDLVRIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586  85 TLIKDGQFFKNPRILAAFEQVKKNNSRLHLMGLVGFGRVHSDMSHLFALLKMARDNDLQQVYLDLFTDGRDSDPSSALSV 164
Cdd:TIGR01307  81 QAIKDGEFFANPALLGAIDRAKDNNGKLHLMGLVSDGGVHSHIDHLIALIELAAERGIEKVVLHAFTDGRDTAPKSAESY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 165 LELITNRIQEIGIGRITTICGRYFAMDRDRNWGRTSRAYNALTKGEAEVSPSIRDVISRAYLRNITDEYIKPHLIVGAGQ 244
Cdd:TIGR01307 161 LEQLQAFLKEIGNGRIATISGRYYAMDRDQRWDRVEIAYKAITGGDGFEFSDPVAYIQDAYARDITDEFIKPTIIGNGGA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 245 ekvlVGDNDAVIFFNFRPDRARQITRAFTTVRMPELPdRKILSNLYFLTFVNREPNPLGTPAFEPHIIKNTLAEVVSHAG 324
Cdd:TIGR01307 241 ----LKDGDAVIFFNFRADRAREITRALVNSDFDGFP-REKNPKLDFVTMTQYDGTFPSPVAFPPQSLTNTLGEVLAKHD 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 325 LRQFHIAETEKYAHVTYFINGGCEEPFPGELQYMVPSPKVPTYDFTPAMSAAKITAKIVSVVWE-NFDLIIGNYANADMV 403
Cdd:TIGR01307 316 LTQLRIAETEKYAHVTFFFNGGVEVPFAGETRTLIPSPKVATYDLQPEMSAKAVTDAVLEAIAQgKFDLIVVNFANPDMV 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 404 GHVGNFYAAVQAIEFVDLCLGKITNALLKNNYVVFITADHGNAEEMLNPrTNQPQTEHTSNPVPLVIVSKDisvARLKLK 483
Cdd:TIGR01307 396 GHTGNFEAAIKAVEALDVCLGRIVEACKKVGGTLFLTADHGNAEEMIDE-NGNPHTAHTTNPVPFVCVGAK---NVKLIR 471

                         490       500       510
                  ....*....|....*....|....*....|
gi 1277125586 484 PGGALSNIAPTILEIMGLEKPPEMTAISLI 513
Cdd:TIGR01307 472 EGGVLADIAPTILDLMGLEQPAEMTGKSLL 501
Metalloenzyme pfam01676
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ...
 5-503 9.41e-106

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: 322.04  E-value: 9.41e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586   5 ARVALIVLDGWGLGPPWGGNAIT---AAKTSNMDYFWRNYCRTTLVACGEAVGLPSGTSGNSETGHLNIGAGRIVPQDLP 81
Cdd:pfam01676   1 KKVVLIVLDGWGDRPAEDLNAKTplhIAKTPNMDKLAKEYPEQLIGASGLAVGLPEGQMGGSDVGHLEIGGGRIVYQYLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586  82 YINTLIKDGQFFKNPRILAAFEQVKKNNSRLHLMGLVGFGRVHSDMSHLFALLKMARDNDLQQVYLDLFTDGRDsdpssa 161
Cdd:pfam01676  81 RGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHSHIEHLLALIALAKEAGAIKVHLLGDGDDRP------ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 162 lsvlelitnriqeigigritticgryfamdrdrnwgrtsraynaltkgeaevspsirdvisraylrnitdeyikphlivg 241
Cdd:pfam01676     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 242 agQEKVLVGDNDAVIFFNFRPDRARQITRA------FTTVRMPELPDRKILSNLYfltfvnrePNPLGTP-AFEPHIIKN 314
Cdd:pfam01676 155 --VGYILDGDAVITINFRFDRRRARILRLFlldpdfFDRDRVRHDALHVPTKTLY--------ELKLPSAgAFVPEEGKN 224

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 315 TLAEVVSHAGLRQFHIAETEKYAHVTYFINGGCEEPFPGELQYMVPSPKVPTYDFTPAMSAAKITAKIVSVVWENFDLII 394
Cdd:pfam01676 225 TDGEVLEGHGLKQLRIAETEKYAHVTFFWGGGREPPFPGEERYLIPSPKVATYDLQPEMSAMEITDKLLEALKEKYDFVF 304

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 395 GNYANADMVGHVGNFYAAVQAIEFVDLCLGKITNALLKNNYVVFITADHGNAEEMLNprtnqpqTEHTSNPVPLVIVSKD 474
Cdd:pfam01676 305 VNFANTDMVGHTGDVEGKVKAIEAVDERLGELLDALEEDDGLLIITADHGNPEEMKD-------TDHTREPVPILIYGKG 377

                         490       500       510
                  ....*....|....*....|....*....|...
gi 1277125586 475 ISVAR----LKLKPGGALSNIAPTILEIMGLEK 503
Cdd:pfam01676 378 VRPDQvlfgEKFRERGGLADIAATILMLLGLKK 410
 
Name Accession Description Interval E-value
iPGM cd16010
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ...
 6-513 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: 766.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586   6 RVALIVLDGWGLGPPWGGNAITAAKTSNMDYFWRNYCRTTLVACGEAVGLPSGTSGNSETGHLNIGAGRIVPQDLPYINT 85
Cdd:cd16010     2 PVVLIILDGWGIRPEDEGNAIALAKTPNLDRLWATYPHTLLKASGEAVGLPDGQMGNSEVGHLNIGAGRIVYQDLTRINK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586  86 LIKDGQFFKNPRILAAFEQVKKNNSRLHLMGLVGFGRVHSDMSHLFALLKMARDNDLQQVYLDLFTDGRDSDPSSALSVL 165
Cdd:cd16010    82 AIEDGSFFKNEALLKAIEHAKKNNSTLHLMGLLSDGGVHSHIDHLFALLELAKKEGVKKVYVHAFTDGRDTPPKSALKYL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 166 ELITNRIQEIGIGRITTICGRYFAMDRDRNWGRTSRAYNALTKGEAEVSPSIRDVISRAYLRNITDEYIKPHLIVGAGQe 245
Cdd:cd16010   162 KELEEKLKELGVGKIASVSGRYYAMDRDKRWDRTEKAYDALVLGEGEKAESAEEAIEASYAKGITDEFIPPTVIGDEGG- 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 246 kvLVGDNDAVIFFNFRPDRARQITRAFTtvrMPELP--DRKILSNLYFLTFVNREPNPLGTPAFEPHIIKNTLAEVVSHA 323
Cdd:cd16010   241 --TIKDGDAVIFFNFRADRARQITRAFT---DPDFDgfDRKKPKNLYFVTMTEYDKDLPVPVAFPPPKIKNTLGEVLSKA 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 324 GLRQFHIAETEKYAHVTYFINGGCEEPFPGELQYMVPSPKVPTYDFTPAMSAAKITAKIVSVVWEN-FDLIIGNYANADM 402
Cdd:cd16010   316 GLKQLRIAETEKYAHVTYFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLIEAIKSGkYDFIVVNFANPDM 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 403 VGHVGNFYAAVQAIEFVDLCLGKITNALLKNNYVVFITADHGNAEEMLNPRTNQPQTEHTSNPVPLVIVSKDIsvaRLKL 482
Cdd:cd16010   396 VGHTGNLEAAVKAVEAVDECLGRIVEAVLENGGTLLITADHGNAEEMIDPETGGPHTAHTTNPVPFIIVDPGL---KRKL 472

                         490       500       510
                  ....*....|....*....|....*....|.
gi 1277125586 483 KPGGALSNIAPTILEIMGLEKPPEMTAISLI 513
Cdd:cd16010   473 LKDGGLADVAPTILDLLGIEKPKEMTGKSLI 503
GpmI COG0696
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ...
 4-513 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: 756.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586   4 KARVALIVLDGWGLGPPWGGNAITAAKTSNMDYFWRNYCRTTLVACGEAVGLPSGTSGNSETGHLNIGAGRIVPQDLPYI 83
Cdd:COG0696     2 KKPVVLIILDGWGIREETEGNAIALANTPNLDRLWATYPHTLLRASGEAVGLPDGQMGNSEVGHLNIGAGRVVYQDLTRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586  84 NTLIKDGQFFKNPRILAAFEQVKKNNSRLHLMGLVGFGRVHSDMSHLFALLKMARDNDLQQVYLDLFTDGRDSDPSSALS 163
Cdd:COG0696    82 NKAIEDGSFFENPVLLDAIDKAKENGGALHLMGLLSDGGVHSHIDHLKALLELAKEEGVKKVYVHAFLDGRDTPPKSALG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 164 VLELITNRIQEIGIGRITTICGRYFAMDRDRNWGRTSRAYNALTKGEAEVSPSIRDVISRAYLRNITDEYIKPHLIVGAG 243
Cdd:COG0696   162 YLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVNGEGETAASAVEAIEASYARGETDEFVKPTVIVDYG 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 244 QEKVLVGDNDAVIFFNFRPDRARQITRAFTTVRMPELPDRKILSNLYFLTFVNREPNPLGTPAFEPHIIKNTLAEVVSHA 323
Cdd:COG0696   242 KPVATIEDGDAVIFFNFRADRARQLTRAFTDPDFDGFDRGKRPKLLYFVTMTEYDETFDVPVAFPPENLKNTLGEVLAKA 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 324 GLRQFHIAETEKYAHVTYFINGGCEEPFPGELQYMVPSPKVPTYDFTPAMSAAKITAKIVSVVWEN-FDLIIGNYANADM 402
Cdd:COG0696   322 GLKQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGkYDFIVLNFANPDM 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 403 VGHVGNFYAAVQAIEFVDLCLGKITNALLKNNYVVFITADHGNAEEMLNPRTNQPQTEHTSNPVPLVIVSKDISVarlKL 482
Cdd:COG0696   402 VGHTGVLEAAIKAVEAVDECLGRVVDAVLAAGGTLLITADHGNAEQMIDPDTGGPHTAHTTNPVPFILVGGDKGV---KL 478

                         490       500       510
                  ....*....|....*....|....*....|.
gi 1277125586 483 KPGGALSNIAPTILEIMGLEKPPEMTAISLI 513
Cdd:COG0696   479 REDGRLADIAPTILELMGLPQPAEMTGKSLI 509
PRK05434 PRK05434
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
1-513 0e+00

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


Pssm-ID: 235463  Cd Length: 507  Bit Score: 737.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586   1 MREKARVALIVLDGWGLGPPWGGNAITAAKTSNMDYFWRNYCRTTLVACGEAVGLPSGTSGNSETGHLNIGAGRIVPQDL 80
Cdd:PRK05434    1 MMMKKPVVLIILDGWGYREETEGNAIALAKTPNLDRLWANYPHTLLSASGLAVGLPDGQMGNSEVGHLNIGAGRIVYQDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586  81 PYINTLIKDGQFFKNPRILAAFEQVKKNNSRLHLMGLVGFGRVHSDMSHLFALLKMARDNDLQQVYLDLFTDGRDSDPSS 160
Cdd:PRK05434   81 TRINKAIEDGSFFENPALLDAIDKAKKNGGALHLMGLLSDGGVHSHIDHLFALLELAKEEGVKKVYVHAFLDGRDTPPKS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 161 ALSVLELITNRIQEIGIGRITTICGRYFAMDRDRNWGRTSRAYNALTKGEAEV-SPSIRDVISRAYLRNITDEYIKPhlI 239
Cdd:PRK05434  161 ALGYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVLGEGPFtAESAVEALEASYARGETDEFVKP--T 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 240 VGAGQEKVLVGDNDAVIFFNFRPDRARQITRAFTtvrMPELP--DRKIlSNLYFLTFVNREPNpLGTP-AFEPHIIKNTL 316
Cdd:PRK05434  239 VIGGEPVAGIEDGDAVIFFNFRADRARQITRAFT---DPDFDgfDRVP-KLLNFVTMTQYDAD-LKVPvAFPPESLKNTL 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 317 AEVVSHAGLRQFHIAETEKYAHVTYFINGGCEEPFPGELQYMVPSPKVPTYDFTPAMSAAKITAKIVSVVWEN-FDLIIG 395
Cdd:PRK05434  314 GEVLAKAGLTQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGkYDFIIL 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 396 NYANADMVGHVGNFYAAVQAIEFVDLCLGKITNALLKNNYVVFITADHGNAEEMLNPRTNQPQTEHTSNPVPLVIVSKDI 475
Cdd:PRK05434  394 NFANPDMVGHTGNLEAAVKAVEAVDECLGRVVDAVLKVGGTLLITADHGNAEQMIDPETGQPHTAHTTNPVPFILVGGKA 473

                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 1277125586 476 svarlKLKPGGALSNIAPTILEIMGLEKPPEMTAISLI 513
Cdd:PRK05434  474 -----LRLEGGKLADIAPTILDLLGLEQPAEMTGKSLI 506
pgm_bpd_ind TIGR01307
phosphoglycerate mutase (2,3-diphosphoglycerate-independent); This protein is about double in ...
 5-513 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: 605.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586   5 ARVALIVLDGWGLGPPWGGNAITAAKTSNMDYFWRNYCRTTLVACGEAVGLPSGTSGNSETGHLNIGAGRIVPQDLPYIN 84
Cdd:TIGR01307   1 KKVVLVILDGWGYRNDDDGNAIFAAKTPTMDELIAAYPYSLLDASGLDVGLPDGQMGNSEVGHLNIGAGRVVYQDLVRIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586  85 TLIKDGQFFKNPRILAAFEQVKKNNSRLHLMGLVGFGRVHSDMSHLFALLKMARDNDLQQVYLDLFTDGRDSDPSSALSV 164
Cdd:TIGR01307  81 QAIKDGEFFANPALLGAIDRAKDNNGKLHLMGLVSDGGVHSHIDHLIALIELAAERGIEKVVLHAFTDGRDTAPKSAESY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 165 LELITNRIQEIGIGRITTICGRYFAMDRDRNWGRTSRAYNALTKGEAEVSPSIRDVISRAYLRNITDEYIKPHLIVGAGQ 244
Cdd:TIGR01307 161 LEQLQAFLKEIGNGRIATISGRYYAMDRDQRWDRVEIAYKAITGGDGFEFSDPVAYIQDAYARDITDEFIKPTIIGNGGA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 245 ekvlVGDNDAVIFFNFRPDRARQITRAFTTVRMPELPdRKILSNLYFLTFVNREPNPLGTPAFEPHIIKNTLAEVVSHAG 324
Cdd:TIGR01307 241 ----LKDGDAVIFFNFRADRAREITRALVNSDFDGFP-REKNPKLDFVTMTQYDGTFPSPVAFPPQSLTNTLGEVLAKHD 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 325 LRQFHIAETEKYAHVTYFINGGCEEPFPGELQYMVPSPKVPTYDFTPAMSAAKITAKIVSVVWE-NFDLIIGNYANADMV 403
Cdd:TIGR01307 316 LTQLRIAETEKYAHVTFFFNGGVEVPFAGETRTLIPSPKVATYDLQPEMSAKAVTDAVLEAIAQgKFDLIVVNFANPDMV 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 404 GHVGNFYAAVQAIEFVDLCLGKITNALLKNNYVVFITADHGNAEEMLNPrTNQPQTEHTSNPVPLVIVSKDisvARLKLK 483
Cdd:TIGR01307 396 GHTGNFEAAIKAVEALDVCLGRIVEACKKVGGTLFLTADHGNAEEMIDE-NGNPHTAHTTNPVPFVCVGAK---NVKLIR 471

                         490       500       510
                  ....*....|....*....|....*....|
gi 1277125586 484 PGGALSNIAPTILEIMGLEKPPEMTAISLI 513
Cdd:TIGR01307 472 EGGVLADIAPTILDLMGLEQPAEMTGKSLL 501
Metalloenzyme pfam01676
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ...
 5-503 9.41e-106

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: 322.04  E-value: 9.41e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586   5 ARVALIVLDGWGLGPPWGGNAIT---AAKTSNMDYFWRNYCRTTLVACGEAVGLPSGTSGNSETGHLNIGAGRIVPQDLP 81
Cdd:pfam01676   1 KKVVLIVLDGWGDRPAEDLNAKTplhIAKTPNMDKLAKEYPEQLIGASGLAVGLPEGQMGGSDVGHLEIGGGRIVYQYLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586  82 YINTLIKDGQFFKNPRILAAFEQVKKNNSRLHLMGLVGFGRVHSDMSHLFALLKMARDNDLQQVYLDLFTDGRDsdpssa 161
Cdd:pfam01676  81 RGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHSHIEHLLALIALAKEAGAIKVHLLGDGDDRP------ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 162 lsvlelitnriqeigigritticgryfamdrdrnwgrtsraynaltkgeaevspsirdvisraylrnitdeyikphlivg 241
Cdd:pfam01676     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 242 agQEKVLVGDNDAVIFFNFRPDRARQITRA------FTTVRMPELPDRKILSNLYfltfvnrePNPLGTP-AFEPHIIKN 314
Cdd:pfam01676 155 --VGYILDGDAVITINFRFDRRRARILRLFlldpdfFDRDRVRHDALHVPTKTLY--------ELKLPSAgAFVPEEGKN 224

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 315 TLAEVVSHAGLRQFHIAETEKYAHVTYFINGGCEEPFPGELQYMVPSPKVPTYDFTPAMSAAKITAKIVSVVWENFDLII 394
Cdd:pfam01676 225 TDGEVLEGHGLKQLRIAETEKYAHVTFFWGGGREPPFPGEERYLIPSPKVATYDLQPEMSAMEITDKLLEALKEKYDFVF 304

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 395 GNYANADMVGHVGNFYAAVQAIEFVDLCLGKITNALLKNNYVVFITADHGNAEEMLNprtnqpqTEHTSNPVPLVIVSKD 474
Cdd:pfam01676 305 VNFANTDMVGHTGDVEGKVKAIEAVDERLGELLDALEEDDGLLIITADHGNPEEMKD-------TDHTREPVPILIYGKG 377

                         490       500       510
                  ....*....|....*....|....*....|...
gi 1277125586 475 ISVAR----LKLKPGGALSNIAPTILEIMGLEK 503
Cdd:pfam01676 378 VRPDQvlfgEKFRERGGLADIAATILMLLGLKK 410
iPGM_N pfam06415
BPG-independent PGAM N-terminus (iPGM_N); This family represents the N-terminal region of the ...
 83-294 1.18e-101

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: 304.33  E-value: 1.18e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586  83 INTLIKDGQFFKNPRILAAFEQVKKNNSRLHLMGLVGFGRVHSDMSHLFALLKMARDNDLQQVYLDLFTDGRDSDPSSAL 162
Cdd:pfam06415   1 INKAIEDGSFFENPALLKAIENAKANGGALHLMGLLSDGGVHSHIDHLFALLELAKEEGVKKVYVHAFLDGRDTPPKSAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 163 SVLELITNRIQEIGIGRITTICGRYFAMDRDRNWGRTSRAYNALTKGEAEVSPSIRDVISRAYLRNITDEYIKPHLIVGA 242
Cdd:pfam06415  81 GYLEQLEAKLAELGVGKIATVSGRYYAMDRDKRWDRVEKAYDALVLGEGESAADAVEAIEASYARGETDEFVKPTVIVDD 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1277125586 243 GQEKVLVGDNDAVIFFNFRPDRARQITRAFTTVRMPELPDRKILSNLYFLTF 294
Cdd:pfam06415 161 GKPVGTIKDGDSVIFFNFRPDRAREITRAFTDPDFDGFERRKRPKDLHFVTM 212
PLN02538 PLN02538
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
 7-507 1.67e-83

2,3-bisphosphoglycerate-independent phosphoglycerate mutase


Pssm-ID: 215295  Cd Length: 558  Bit Score: 269.24  E-value: 1.67e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586   7 VALIVLDGWGLGPPWGGNAITAAKTSNMDYF-------WRnycrtTLVACGEAVGLPSGTS-GNSETGHLNIGAGRIVPQ 78
Cdd:PLN02538   23 LLLIVLDGWGENAPDEFNAIHVAPTPTMDSLkagaperWR-----LVKAHGTAVGLPSDDDmGNSEVGHNALGAGRIFAQ 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586  79 DLPYINTLIKDGQFFKNPrilaAFEQVKK--NNSRLHLMGLVGFGRVHSDMSHLFALLKMARDNDLQQVYLDLFTDGRDS 156
Cdd:PLN02538   98 GAKLVDLALASGKIFEGE----GFKYIKEafATGTLHLIGLLSDGGVHSRLDQLQLLLKGAAERGAKRIRVHVLTDGRDV 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 157 DPSSALSVLELITNRIQEI---GI-GRITTICGR-YFAMDR-DRNWGRTSRAYNALTKGEA--EVSPSIRDVIS-RAYLR 227
Cdd:PLN02538  174 PDGSSVGFVETLEKDLAELrekGCdARIASGGGRmYVTMDRyENDWNVVKRGWDAHVLGEAphKFKSALEAVKKlREEPP 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 228 NITDEYIKPHLIVGAGQEKV-LVGDNDAVIFFNFRPDRARQITRA--------FTTVRMPELP---------DRKILSNl 289
Cdd:PLN02538  254 PANDQYLPPFVIVDEDGKPVgPIEDGDAVVTFNFRADRMVMIAKAleyedfdkFDRVRVPKIRyagmlqydgELKLPSH- 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 290 YFLTfvnrepnplgtpafePHIIKNTLAEVVSHAGLRQFHIAETEKYAHVTYFINGGCEEPFPGEL-QYM-VPSPKVPTY 367
Cdd:PLN02538  333 YLVS---------------PPLIERTSGEYLVANGVRTFACSETVKFGHVTFFWNGNRSGYFNEKLeEYVeIPSDNGIPF 397

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 368 DFTPAMSAAKITAKIVSVVWE-NFDLIIGNYANADMVGHVGNFYAAVQAIEFVDLCLGKITNALLKNNYVVFITADHGNA 446
Cdd:PLN02538  398 NVQPKMKALEIAEKARDALLSgKFDQVRVNLANGDMVGHTGDLEATIVACEAVDAAVKEILDAVEQVGGIYLVTADHGNA 477

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277125586 447 EEML------NPRTN-----QPQTEHTSNPVPLVIVSKDISvARLKLK---PGGALSNIAPTILEIMGLEKPPEM 507
Cdd:PLN02538  478 EDMVkrdksgKPLLDkdgnpQILTSHTLAPVPVAIGGPGLP-PGVRFRddlPTAGLANVAATVMNLHGFEAPADY 551
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 391-499 8.74e-11

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: 62.05  E-value: 8.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 391 DLIIGNYANADMVGH-----VGNFYAAVQAIefvDLCLGKITNALLK----NNYVVFITADHGNAEEMLNPRTN---QPQ 458
Cdd:cd00016   121 FVLFLHFDGPDGPGHaygpnTPEYYDAVEEI---DERIGKVLDALKKagdaDDTVIIVTADHGGIDKGHGGDPKadgKAD 197

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1277125586 459 TEHTSNPVPLVIVSKDISVARlKLKPGGALSNIAPTILEIM 499
Cdd:cd00016   198 KSHTGMRVPFIAYGPGVKKGG-VKHELISQYDIAPTLADLL 237
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 410-512 5.69e-10

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: 60.25  E-value: 5.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 410 YAAvqAIEFVDLCLGKITNAL----LKNNYVVFITADHGnaEEM----LNPRTNQPQTEHTSNpVPLVIvskdisvARLK 481
Cdd:cd16148   165 YDA--EVRYVDEQIGRLLDKLkelgLLEDTLVIVTSDHG--EEFgehgLYWGHGSNLYDEQLH-VPLII-------RWPG 232

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1277125586 482 LKPGGALSN------IAPTILEIMGLEKPPEMTAISL 512
Cdd:cd16148   233 KEPGKRVDAlvshidIAPTLLDLLGVEPPDYSDGRSL 269
PRK04024 PRK04024
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
366-477 1.54e-09

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


Pssm-ID: 235203  Cd Length: 412  Bit Score: 59.93  E-value: 1.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 366 TYDfTPAMSAAKitaKIVSVVwENFDLIIGNYANADMVGHVGNFYAAVQAIEFVDLCLGKITNALLKNNYVVFITADHGN 445
Cdd:PRK04024  275 GKD-TNYMAKAK---AAVELL-KEYDFVLLNIKGTDEAGHDGDFEGKVEVIEKIDKMLGYILDNLDLDEVYIAVTGDHST 349

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1277125586 446 AEEMLnprtnqpqtEHTSNPVPLVIVSKDISV 477
Cdd:PRK04024  350 PVEVK---------DHSGDPVPILIYGPGVRV 372
PPM cd16009
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ...
 410-510 4.87e-08

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: 55.15  E-value: 4.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 410 YAavQAIEFVDLCLGKITNaLLKNNYVVFITADHGNaeemlNPRTnqPQTEHTSNPVPLVIVSKDISVARLKLKPGgaLS 489
Cdd:cd16009   294 YA--EALEEFDRRLPELLA-KLKEDDLLIITADHGN-----DPTI--GGTDHTREYVPLLVYGKGLKGVNLGTRET--FA 361

                          90       100
                  ....*....|....*....|.
gi 1277125586 490 NIAPTILEIMGLEKPPEMTAI 510
Cdd:cd16009   362 DIGATIADNFGVEPPENGTSF 382
PRK05362 PRK05362
phosphopentomutase; Provisional
 410-505 5.58e-08

phosphopentomutase; Provisional


Pssm-ID: 235430  Cd Length: 394  Bit Score: 54.74  E-value: 5.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 410 YAavQAIEFVDLCLGKITnALLKNNYVVFITADHGNaeemlNPRTnqPQTEHTSNPVPLVIVSKDISVARLKLKpgGALS 489
Cdd:PRK05362  301 YA--AALEEFDARLPELL-AALKEDDLLIITADHGN-----DPTW--PGTDHTREYVPLLVYGPKFKGGSLGHR--ETFA 368

                          90
                  ....*....|....*.
gi 1277125586 490 NIAPTILEIMGLEKPP 505
Cdd:PRK05362  369 DIGATIADNFGVEPME 384
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 405-512 2.13e-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: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 52.95  E-value: 2.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 405 HVGNFYAAvqaIEFVDLCLGKITNAL-----LKNNYVVFiTADHGNA--EEMLNPRTNQpqTEHTSNpVPLVIVSKDIsv 477
Cdd:cd16155   190 HLAEYYAM---ITHLDAQIGRILDALeasgeLDNTIIVF-TSDHGLAvgSHGLMGKQNL--YEHSMR-VPLIISGPGI-- 260

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1277125586 478 arlklKPGGA------LSNIAPTILEIMGLEKPPEMTAISL 512
Cdd:cd16155   261 -----PKGKRrdalvyLQDVFPTLCELAGIEIPESVEGKSL 296
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 409-513 2.71e-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: 52.55  E-value: 2.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 409 FYAAVqaiEFVDLCLGKITNAL----LKNNYVVFITADHGnaeEMLNPRTN-QPQT--EHtSNPVPLVIVSKDISVARLK 481
Cdd:cd16037   164 YYGLV---EFLDENIGRVLDALeelgLLDNTLIIYTSDHG---DMLGERGLwGKSTmyEE-SVRVPMIISGPGIPAGKRV 236

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1277125586 482 LKPGGALsNIAPTILEIMGLEKPPEMTAISLI 513
Cdd:cd16037   237 KTPVSLV-DLAPTILEAAGAPPPPDLDGRSLL 267
DeoB COG1015
Phosphopentomutase [Carbohydrate transport and metabolism];
401-505 3.31e-07

Phosphopentomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440639  Cd Length: 385  Bit Score: 52.36  E-value: 3.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 401 DMV-GH----VGnfYAavQAIEFVDLCLGKITnALLKNNYVVFITADHGNaeemlNPRTnqPQTEHTSNPVPLVIVSKdi 475
Cdd:COG1015   282 DSLyGHrrdvAG--YA--KALEEFDARLPELL-AALRPDDLLIITADHGN-----DPTW--PGTDHTREYVPLLVYGP-- 347

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1277125586 476 svarlKLKPGGAL------SNIAPTILEIMGLEKPP 505
Cdd:COG1015   348 -----GLKPGGNLgtretfADIGATIADHFGVPPPG 378
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 408-507 8.05e-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: 293758 [Multi-domain]  Cd Length: 399  Bit Score: 51.42  E-value: 8.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 408 NFYAAVQAIefvDLCLGKI-----TNALLKNNYVVFiTADHGnaeEML----NPRTNQPQTEhtSNPVPLVIvskdisva 478
Cdd:cd16034   228 GYYAMITAL---DDNIGRLldalkELGLLENTIVVF-TSDHG---DMLgshgLMNKQVPYEE--SIRVPFII-------- 290

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1277125586 479 RL--KLKPGG----ALSN--IAPTILEIMGLEKPPEM 507
Cdd:cd16034   291 RYpgKIKAGRvvdlLINTvdIMPTLLGLCGLPIPDTV 327
apgM TIGR00306
phosphoglycerate mutase (2,3-diphosphoglycerate-independent), archaeal form; Experimentally ...
 388-481 1.03e-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: 50.93  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 388 ENFDLIIGNYANADMVGHVGNFYAAVQAIEFVDLCLGKITNALLKNNYVVFITADHGNAEEMLNprtnqpqteHTSNPVP 467
Cdd:TIGR00306 286 EEYDFVLVHTKGPDEAGHDGDPELKVRAIEKIDSKIVGPLLALDLDETRLILTADHSTPVEVKD---------HSADPVP 356

                          90
                  ....*....|....
gi 1277125586 468 LVIVSKDISVARLK 481
Cdd:TIGR00306 357 IVIVGPGVRVDEVK 370
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
410-512 1.28e-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: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 410 YAAvqAIEFVDLCLGKITNAL----LKNNYVVFITADHGnaeEMLNPRTNQPQ----TEHTSNpVPLVIVSKDisvarlK 481
Cdd:COG3119   202 YAA--MIEEVDDQVGRLLDALeelgLADNTIVVFTSDNG---PSLGEHGLRGGkgtlYEGGIR-VPLIVRWPG------K 269

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1277125586 482 LKPGG---ALSN---IAPTILEIMGLEKPPEMTAISL 512
Cdd:COG3119   270 IKAGSvsdALVSlidLLPTLLDLAGVPIPEDLDGRSL 306
Sulfatase pfam00884
Sulfatase;
414-501 1.29e-06

Sulfatase;


Pssm-ID: 459979 [Multi-domain]  Cd Length: 298  Bit Score: 50.11  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 414 QAIEFVDLCLGKITNALLKN----NYVVFITADHGnaeEMLNPRTNQPQTEHTSNP------VPLVIVSKDISVARLKLK 483
Cdd:pfam00884 204 NTLLYTDDAIGRVLDKLEENglldNTLVVYTSDHG---ESLGEGGGYLHGGKYDNApeggyrVPLLIWSPGGKAKGQKSE 280

                          90
                  ....*....|....*...
gi 1277125586 484 PGGALSNIAPTILEIMGL 501
Cdd:pfam00884 281 ALVSHVDLFPTILDLAGI 298
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
 410-511 6.26e-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: 47.43  E-value: 6.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 410 YAAVqaIEFVDLCLGKITNAL-----LKNNYVVFiTADHGnaeEMLNPRTNQpqTEHTSNP-----VPLVIVSKDIsvar 479
Cdd:cd16022   133 YYAM--VSAIDDQIGRILDALeelglLDNTLIVF-TSDHG---DMLGDHGLR--GKKGSLYeggirVPFIVRWPGK---- 200

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1277125586 480 lklKPGGALSN-------IAPTILEIMGLEKPPEMTAIS 511
Cdd:cd16022   201 ---IPAGQVSDalvslldLLPTLLDLAGIEPPEGLDGRS 236
iPGM_like cd16011
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate ...
 401-475 7.13e-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: 48.24  E-value: 7.13e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277125586 401 DMVGHVGNFYAAVQAIEFVDLCLGKITNALLK-NNYVVFITADHGNAEEMLnprtnqpqtEHTSNPVPLVIVSKDI 475
Cdd:cd16011   268 DEAGHDGDPEAKVKAIERIDKAIVGPLLELLDgEDFVIVVTPDHSTPCSLK---------THSGDPVPFLIYGPGV 334
PRK12383 PRK12383
putative mutase; Provisional
 379-504 7.84e-06

putative mutase; Provisional


Pssm-ID: 237085  Cd Length: 406  Bit Score: 48.04  E-value: 7.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 379 TAKIVSVVWENFD-----LIIGNYANADMVGHVGNFYAAVQAIEFVDLCLGKITnALLKNNYVVFITADHGNaeemlNPR 453
Cdd:PRK12383  271 TQRVMDITLDEFNthptaFICTNIQETDLAGHAEDVARYAERLEVVDRNLARLL-EAMTPDDCLVVMADHGN-----DPT 344

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1277125586 454 TNQPQteHTSNPVPLVIVSKDISVARLKLKPggALSNIAPTILEIMGLEKP 504
Cdd:PRK12383  345 IGHSH--HTREVVPLLVYQKGLQATQLGVRT--TLSDVGATVCEFFGAPPP 391
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
 408-514 8.70e-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: 8.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 408 NFYAAvqaIEFVDLCLGKITNAL----LKNNYVVFITADHGnaeeMLNPRTNQPQTEHtSNPVPLVIVSKDisvarlKLK 483
Cdd:cd16027   190 DYYDE---IERLDQQVGEILDELeedgLLDNTIVIFTSDHG----MPFPRAKGTLYDS-GLRVPLIVRWPG------KIK 255

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1277125586 484 PGG---AL-SNI--APTILEIMGLEKPPEMTAISLIG 514
Cdd:cd16027   256 PGSvsdALvSFIdlAPTLLDLAGIEPPEYLQGRSFLP 292
LTA_synthase cd16015
Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer ...
 413-500 2.00e-05

Lipoteichoic acid synthase like; Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.


Pssm-ID: 293739 [Multi-domain]  Cd Length: 283  Bit Score: 46.52  E-value: 2.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 413 VQAIEFVDLCLGKITNAL----LKNNYVVFITADHG-NAEEMLNPRTNQPQTEHTsnpVPLVIVSKDISVARLKLKPGGA 487
Cdd:cd16015   195 LNAIHYTDKALGEFIEKLkksgLYENTIIVIYGDHLpSLGSDYDETDEDPLDLYR---TPLLIYSPGLKKPKKIDRVGSQ 271

                          90
                  ....*....|...
gi 1277125586 488 LsNIAPTILEIMG 500
Cdd:cd16015   272 I-DIAPTLLDLLG 283
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
 413-508 2.05e-05

Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 47.34  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 413 VQAIEFVDLCLGKITNAL----LKNNYVVFITADHGNAEEMLNPRTNQPQTEHtsnpVPLVIVSKDISVARLKLKPGGAL 488
Cdd:COG1368   420 LNAVRYADQALGEFIEKLkksgWYDNTIFVIYGDHGPRSPGKTDYENPLERYR----VPLLIYSPGLKKPKVIDTVGSQI 495

                          90       100
                  ....*....|....*....|
gi 1277125586 489 sNIAPTILEIMGLEKPPEMT 508
Cdd:COG1368   496 -DIAPTLLDLLGIDYPSYYA 514
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 315-444 5.33e-05

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 45.51  E-value: 5.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 315 TLAEVVSHAGLR--QFHIAETEKYAhvtyFINGGCEEPFPGELQYMvpspKVPTYDFTPAMSAAKITAKivsvvwENFDL 392
Cdd:COG1524   120 TIFERARAAGLTtaAVFWPSFEGSG----LIDAARPYPYDGRKPLL----GNPAADRWIAAAALELLRE------GRPDL 185

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1277125586 393 IIGNYANADMVGHV-GNFYAAV-QAIEFVDLCLGKITNAL----LKNNYVVFITADHG 444
Cdd:COG1524   186 LLVYLPDLDYAGHRyGPDSPEYrAALREVDAALGRLLDALkargLYEGTLVIVTADHG 243
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 391-444 3.27e-04

Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of phosphodiesterases, including human plasma-cell membrane glycoprotein PC-1 / alkaline phosphodiesterase i / nucleotide pyrophosphatase (nppase). These enzymes catalyze the cleavage of phosphodiester and phosphosulfate bonds in NAD, deoxynucleotides and nucleotide sugars. Also in this family is ATX an autotaxin, tumour cell motility-stimulating protein which exhibits type I phosphodiesterases activity. The alignment encompasses the active site. Also present with in this family is 60-kDa Ca2+-ATPase form F. odoratum.


Pssm-ID: 396300 [Multi-domain]  Cd Length: 343  Bit Score: 42.79  E-value: 3.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 391 DLIIGNYANADMVGH-VGNFYAAV-QAIEFVDLCLGKITNAL----LKNNYVVFITADHG 444
Cdd:pfam01663 164 DLLLVYLEEPDYAGHrYGPDSPEVeDALRRVDRAIGDLLEALdergLFEDTNVIVVSDHG 223
ApgM COG3635
2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type [Carbohydrate ...
 387-475 3.28e-04

2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type [Carbohydrate transport and metabolism]; 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 442852  Cd Length: 398  Bit Score: 43.21  E-value: 3.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 387 WENFDLIIGNYANADMVGHVGNFYAAVQAIEFVD-LCLGKITNALLKNN-YVVFITADHgnaeemlnP-----RTnqpqt 459
Cdd:COG3635   285 LKDYDFVYVHVEAPDEAGHDGDLEEKVKAIERIDrRVVGPLLEGLEKFEdYRILVTPDH--------PtpislRT----- 351

                          90
                  ....*....|....*.
gi 1277125586 460 eHTSNPVPLVIVSKDI 475
Cdd:COG3635   352 -HSGDPVPFLIYGPGV 366
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
 418-513 4.04e-04

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: 42.75  E-value: 4.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 418 FVDLCLGKITNALLKN--NYVVFITADHGnaeEMLNPRT----NQPQTEHTSNpVPLVIVSKDISVARLKLKPGGALSNI 491
Cdd:cd16156   249 FVDYEIGRVLDAADEIaeDAWVIYTSDHG---DMLGAHKlwakGPAVYDEITN-IPLIIRGKGGEKAGTVTDTPVSHIDL 324

                          90       100
                  ....*....|....*....|..
gi 1277125586 492 APTILEIMGLEKPPEMTAISLI 513
Cdd:cd16156   325 APTILDYAGIPQPKVLEGESIL 346
PRK04135 PRK04135
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
386-473 7.13e-04

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


Pssm-ID: 179745 [Multi-domain]  Cd Length: 395  Bit Score: 41.83  E-value: 7.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 386 VWENFDLIIGNYANADMVGHVGNFYAAVQAIEFVDLCLGKITNalLKNNyVVFITADHGnaeemlnprTNQPQTEHTSNP 465
Cdd:PRK04135  276 NWNDYDFFFLHVKKTDSYGEDGNFEEKVKVIEEVDALLPEILA--LKPD-VLVITGDHS---------TPAVLKGHSWHP 343


                  ....*...
gi 1277125586 466 VPLVIVSK 473
Cdd:PRK04135  344 VPLLLYSK 351
sulfatase_like cd16035
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 408-509 1.56e-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: 293759 [Multi-domain]  Cd Length: 311  Bit Score: 40.65  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 408 NFYAavQAIEFVDLCLGKITNAL-----LKNNYVVFiTADHG-------------NA-EEMLNprtnqpqtehtsnpVPL 468
Cdd:cd16035   167 NFYY--NLIRDVDRQIGRVLDALdasglADNTIVVF-TSDHGemggahglrgkgfNAyEEALH--------------VPL 229

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1277125586 469 VIVSKDisvarlkLKPGG----ALSN---IAPTILEIMGLEKPPEMTA 509
Cdd:cd16035   230 IISHPD-------LFGTGqttdALTShidLLPTLLGLAGVDAEARATE 270
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
 409-513 4.05e-03

arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a lysosomal sulfatase which exhibits an acidic pH optimum for catalytic activity against arylsulfate substrates. Other names for ARSK include arylsulfatase K and TSULF. 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: 293781 [Multi-domain]  Cd Length: 366  Bit Score: 39.45  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 409 FYAAVQAIefVDLCLGKITNAL-----LKNNYVVFiTADHGNAEeMLNPRTNQPQTEHTSNPVPLVIVSKDISvARLKLK 483
Cdd:cd16171   197 FYYAMCAE--TDAMLGEIISALkdtglLDKTYVFF-TSDHGELA-MEHRQFYKMSMYEGSSHVPLLIMGPGIK-AGQQVS 271

                          90       100       110
                  ....*....|....*....|....*....|
gi 1277125586 484 PGGALSNIAPTILEIMGLEKPPEMTAISLI 513
Cdd:cd16171   272 DVVSLVDIYPTMLDIAGVPQPQNLSGYSLL 301
choline-sulfatase cd16032
choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from ...
 415-510 8.30e-03

choline-sulfatase; Choline-sulphatase is involved in the synthesis of glycine betaine from choline. The symbiotic soil bacterium Rhizobium meliloti can synthesize glycine betaine from choline-O-sulphate and choline to protect itself from osmotic stress. This biosynthetic pathway is encoded by the betICBA locus, which comprises a regulatory gene, betI, and three structural genes, betC (choline sulfatase), betB (betaine aldehyde dehydrogenase), and betA (choline dehydrogenase). betICBA genes constitute a single operon.


Pssm-ID: 293756 [Multi-domain]  Cd Length: 327  Bit Score: 38.33  E-value: 8.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277125586 415 AIEFVDLCLGKITNAL----LKNNYVVFITADHGnaeEMLNPRT---NQPQTEHTSNpVPLVIVSKDISVARLKLKPgGA 487
Cdd:cd16032   169 MVSYVDDKVGQLLDTLertgLADDTIVIFTSDHG---DMLGERGlwyKMSFFEGSAR-VPLIISAPGRFAPRRVAEP-VS 243

                          90       100
                  ....*....|....*....|...
gi 1277125586 488 LSNIAPTILEIMGLEKPPEMTAI 510
Cdd:cd16032   244 LVDLLPTLVDLAGGGTAPHVPPL 266
PRK04200 PRK04200
cofactor-independent phosphoglycerate mutase; Provisional
 401-475 9.09e-03

cofactor-independent phosphoglycerate mutase; Provisional


Pssm-ID: 179781  Cd Length: 395  Bit Score: 38.32  E-value: 9.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277125586 401 DMVGHVGNFYAAVQAIEFVD-LCLGKITNALLK-NNYVVFITADHGNAEEMlnpRTnqpqteHTSNPVPLVIVSKDI 475
Cdd:PRK04200  295 DEAGHEGDLEAKIKAIEDIDeRVVGPILEALKKyEDYRILVLPDHPTPIEL---KT------HTADPVPFLIYGEGI 362
 
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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