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Conserved domains on  [gi|872705949|ref|WP_048557389|]
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MULTISPECIES: 2,3-bisphosphoglycerate-independent phosphoglycerate mutase [Bacillus]

Protein Classification

2,3-bisphosphoglycerate-independent phosphoglycerate mutase( domain architecture ID 11430849)

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

CATH:  3.40.1450.10|3.40.720.10
EC:  5.4.2.12
Gene Ontology:  GO:0030145|GO:0006007|GO:0046537|GO:0006096
PubMed:  10958932|2543188
SCOP:  4003438

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GpmI COG0696
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ...
 2-509 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: 983.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949   2 RKPTALIILDGFGLREETYGNAVAQAKKPNFDGYWNKFPHTTLTACGEAVGLPEGQMGNSEVGHLNIGAGRIVYQSLTRV 81
Cdd:COG0696    2 KKPVVLIILDGWGIREETEGNAIALANTPNLDRLWATYPHTLLRASGEAVGLPDGQMGNSEVGHLNIGAGRVVYQDLTRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  82 NVAIREGEFDKNETFQSAIKSVKEKGTALHLFGLLSDGGVHSHMNHMFALLRLAAKEGVEKVYIHAFLDGRDVGPKTAQS 161
Cdd:COG0696   82 NKAIEDGSFFENPVLLDAIDKAKENGGALHLMGLLSDGGVHSHIDHLKALLELAKEEGVKKVYVHAFLDGRDTPPKSALG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 162 YIDATNEVIKETGVGQFATISGRYYSMDRDKRWDRVEKCYRAMVNGEGPTYKSAEECVEDSYANGIYDEFVLPSVIVNED 241
Cdd:COG0696  162 YLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVNGEGETAASAVEAIEASYARGETDEFVKPTVIVDYG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 242 NtPVATINDDDAVIFYNFRPDRAIQIARVFTNEDFREFDRGeKVPHIPEFVCMTHFSETVDGYVAFKPMNLDNTLGEVVA 321
Cdd:COG0696  242 K-PVATIEDGDAVIFFNFRADRARQLTRAFTDPDFDGFDRG-KRPKLLYFVTMTEYDETFDVPVAFPPENLKNTLGEVLA 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 322 QAGLKQLRIAETEKYPHVTFFFSGGREAEFPGEERILINSPKVATYDLKPEMSIYEVTDALVNEIENDKHDVIILNFANC 401
Cdd:COG0696  320 KAGLKQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIVLNFANP 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 402 DMVGHSGMMEPTIKAVEATDECLGKVVEAILAKDGVALITADHGNADEELTSE-GEPMTAHTTNPVPFIVT--KNDVELR 478
Cdd:COG0696  400 DMVGHTGVLEAAIKAVEAVDECLGRVVDAVLAAGGTLLITADHGNAEQMIDPDtGGPHTAHTTNPVPFILVggDKGVKLR 479

                        490       500       510
                 ....*....|....*....|....*....|.
gi 872705949 479 EGGILGDIAPTMLTLLGVEQPKEMTGKTIIK 509
Cdd:COG0696  480 EDGRLADIAPTILELMGLPQPAEMTGKSLIE 510
 
Name Accession Description Interval E-value
GpmI COG0696
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ...
 2-509 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: 983.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949   2 RKPTALIILDGFGLREETYGNAVAQAKKPNFDGYWNKFPHTTLTACGEAVGLPEGQMGNSEVGHLNIGAGRIVYQSLTRV 81
Cdd:COG0696    2 KKPVVLIILDGWGIREETEGNAIALANTPNLDRLWATYPHTLLRASGEAVGLPDGQMGNSEVGHLNIGAGRVVYQDLTRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  82 NVAIREGEFDKNETFQSAIKSVKEKGTALHLFGLLSDGGVHSHMNHMFALLRLAAKEGVEKVYIHAFLDGRDVGPKTAQS 161
Cdd:COG0696   82 NKAIEDGSFFENPVLLDAIDKAKENGGALHLMGLLSDGGVHSHIDHLKALLELAKEEGVKKVYVHAFLDGRDTPPKSALG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 162 YIDATNEVIKETGVGQFATISGRYYSMDRDKRWDRVEKCYRAMVNGEGPTYKSAEECVEDSYANGIYDEFVLPSVIVNED 241
Cdd:COG0696  162 YLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVNGEGETAASAVEAIEASYARGETDEFVKPTVIVDYG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 242 NtPVATINDDDAVIFYNFRPDRAIQIARVFTNEDFREFDRGeKVPHIPEFVCMTHFSETVDGYVAFKPMNLDNTLGEVVA 321
Cdd:COG0696  242 K-PVATIEDGDAVIFFNFRADRARQLTRAFTDPDFDGFDRG-KRPKLLYFVTMTEYDETFDVPVAFPPENLKNTLGEVLA 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 322 QAGLKQLRIAETEKYPHVTFFFSGGREAEFPGEERILINSPKVATYDLKPEMSIYEVTDALVNEIENDKHDVIILNFANC 401
Cdd:COG0696  320 KAGLKQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIVLNFANP 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 402 DMVGHSGMMEPTIKAVEATDECLGKVVEAILAKDGVALITADHGNADEELTSE-GEPMTAHTTNPVPFIVT--KNDVELR 478
Cdd:COG0696  400 DMVGHTGVLEAAIKAVEAVDECLGRVVDAVLAAGGTLLITADHGNAEQMIDPDtGGPHTAHTTNPVPFILVggDKGVKLR 479

                        490       500       510
                 ....*....|....*....|....*....|.
gi 872705949 479 EGGILGDIAPTMLTLLGVEQPKEMTGKTIIK 509
Cdd:COG0696  480 EDGRLADIAPTILELMGLPQPAEMTGKSLIE 510
PRK05434 PRK05434
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
1-509 0e+00

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


Pssm-ID: 235463  Cd Length: 507  Bit Score: 969.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949   1 MRKPTALIILDGFGLREETYGNAVAQAKKPNFDGYWNKFPHTTLTACGEAVGLPEGQMGNSEVGHLNIGAGRIVYQSLTR 80
Cdd:PRK05434   3 MKKPVVLIILDGWGYREETEGNAIALAKTPNLDRLWANYPHTLLSASGLAVGLPDGQMGNSEVGHLNIGAGRIVYQDLTR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  81 VNVAIREGEFDKNETFQSAIKSVKEKGTALHLFGLLSDGGVHSHMNHMFALLRLAAKEGVEKVYIHAFLDGRDVGPKTAQ 160
Cdd:PRK05434  83 INKAIEDGSFFENPALLDAIDKAKKNGGALHLMGLLSDGGVHSHIDHLFALLELAKEEGVKKVYVHAFLDGRDTPPKSAL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 161 SYIDATNEVIKETGVGQFATISGRYYSMDRDKRWDRVEKCYRAMVNGEGP-TYKSAEECVEDSYANGIYDEFVLPSVIVN 239
Cdd:PRK05434 163 GYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVLGEGPfTAESAVEALEASYARGETDEFVKPTVIGG 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 240 EdntPVATINDDDAVIFYNFRPDRAIQIARVFTNEDFREFDRgekVPHIPEFVCMTHFSETVDGYVAFKPMNLDNTLGEV 319
Cdd:PRK05434 243 E---PVAGIEDGDAVIFFNFRADRARQITRAFTDPDFDGFDR---VPKLLNFVTMTQYDADLKVPVAFPPESLKNTLGEV 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 320 VAQAGLKQLRIAETEKYPHVTFFFSGGREAEFPGEERILINSPKVATYDLKPEMSIYEVTDALVNEIENDKHDVIILNFA 399
Cdd:PRK05434 317 LAKAGLTQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIILNFA 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 400 NCDMVGHSGMMEPTIKAVEATDECLGKVVEAILAKDGVALITADHGNADEELTSE-GEPMTAHTTNPVPFIVTKNDVELR 478
Cdd:PRK05434 397 NPDMVGHTGNLEAAVKAVEAVDECLGRVVDAVLKVGGTLLITADHGNAEQMIDPEtGQPHTAHTTNPVPFILVGGKALRL 476

                        490       500       510
                 ....*....|....*....|....*....|.
gi 872705949 479 EGGILGDIAPTMLTLLGVEQPKEMTGKTIIK 509
Cdd:PRK05434 477 EGGKLADIAPTILDLLGLEQPAEMTGKSLIE 507
iPGM cd16010
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ...
 3-508 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: 915.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949   3 KPTALIILDGFGLREETYGNAVAQAKKPNFDGYWNKFPHTTLTACGEAVGLPEGQMGNSEVGHLNIGAGRIVYQSLTRVN 82
Cdd:cd16010    1 KPVVLIILDGWGIRPEDEGNAIALAKTPNLDRLWATYPHTLLKASGEAVGLPDGQMGNSEVGHLNIGAGRIVYQDLTRIN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  83 VAIREGEFDKNETFQSAIKSVKEKGTALHLFGLLSDGGVHSHMNHMFALLRLAAKEGVEKVYIHAFLDGRDVGPKTAQSY 162
Cdd:cd16010   81 KAIEDGSFFKNEALLKAIEHAKKNNSTLHLMGLLSDGGVHSHIDHLFALLELAKKEGVKKVYVHAFTDGRDTPPKSALKY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 163 IDATNEVIKETGVGQFATISGRYYSMDRDKRWDRVEKCYRAMVNGEGPTYKSAEECVEDSYANGIYDEFVLPSVIVNEDN 242
Cdd:cd16010  161 LKELEEKLKELGVGKIASVSGRYYAMDRDKRWDRTEKAYDALVLGEGEKAESAEEAIEASYAKGITDEFIPPTVIGDEGG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 243 tpvaTINDDDAVIFYNFRPDRAIQIARVFTNEDFREFDRgeKVPHIPEFVCMTHFSETVDGYVAFKPMNLDNTLGEVVAQ 322
Cdd:cd16010  241 ----TIKDGDAVIFFNFRADRARQITRAFTDPDFDGFDR--KKPKNLYFVTMTEYDKDLPVPVAFPPPKIKNTLGEVLSK 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 323 AGLKQLRIAETEKYPHVTFFFSGGREAEFPGEERILINSPKVATYDLKPEMSIYEVTDALVNEIENDKHDVIILNFANCD 402
Cdd:cd16010  315 AGLKQLRIAETEKYAHVTYFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLIEAIKSGKYDFIVVNFANPD 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 403 MVGHSGMMEPTIKAVEATDECLGKVVEAILAKDGVALITADHGNADEELTSE-GEPMTAHTTNPVPFIVTKNDVE--LRE 479
Cdd:cd16010  395 MVGHTGNLEAAVKAVEAVDECLGRIVEAVLENGGTLLITADHGNAEEMIDPEtGGPHTAHTTNPVPFIIVDPGLKrkLLK 474

                        490       500
                 ....*....|....*....|....*....
gi 872705949 480 GGILGDIAPTMLTLLGVEQPKEMTGKTII 508
Cdd:cd16010  475 DGGLADVAPTILDLLGIEKPKEMTGKSLI 503
pgm_bpd_ind TIGR01307
phosphoglycerate mutase (2,3-diphosphoglycerate-independent); This protein is about double in ...
 3-508 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: 721.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949    3 KPTALIILDGFGLREETYGNAVAQAKKPNFDGYWNKFPHTTLTACGEAVGLPEGQMGNSEVGHLNIGAGRIVYQSLTRVN 82
Cdd:TIGR01307   1 KKVVLVILDGWGYRNDDDGNAIFAAKTPTMDELIAAYPYSLLDASGLDVGLPDGQMGNSEVGHLNIGAGRVVYQDLVRIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949   83 VAIREGEFDKNETFQSAIKSVKEKGTALHLFGLLSDGGVHSHMNHMFALLRLAAKEGVEKVYIHAFLDGRDVGPKTAQSY 162
Cdd:TIGR01307  81 QAIKDGEFFANPALLGAIDRAKDNNGKLHLMGLVSDGGVHSHIDHLIALIELAAERGIEKVVLHAFTDGRDTAPKSAESY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  163 IDATNEVIKETGVGQFATISGRYYSMDRDKRWDRVEKCYRAMVNGEGPTYKSAEECVEDSYANGIYDEFVLPSVIVNEDn 242
Cdd:TIGR01307 161 LEQLQAFLKEIGNGRIATISGRYYAMDRDQRWDRVEIAYKAITGGDGFEFSDPVAYIQDAYARDITDEFIKPTIIGNGG- 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  243 tpvaTINDDDAVIFYNFRPDRAIQIARVFTNEDFREFDRgEKVPHIpEFVCMTHFSETVDGYVAFKPMNLDNTLGEVVAQ 322
Cdd:TIGR01307 240 ----ALKDGDAVIFFNFRADRAREITRALVNSDFDGFPR-EKNPKL-DFVTMTQYDGTFPSPVAFPPQSLTNTLGEVLAK 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  323 AGLKQLRIAETEKYPHVTFFFSGGREAEFPGEERILINSPKVATYDLKPEMSIYEVTDALVNEIENDKHDVIILNFANCD 402
Cdd:TIGR01307 314 HDLTQLRIAETEKYAHVTFFFNGGVEVPFAGETRTLIPSPKVATYDLQPEMSAKAVTDAVLEAIAQGKFDLIVVNFANPD 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  403 MVGHSGMMEPTIKAVEATDECLGKVVEAILAKDGVALITADHGNADEELTSEGEPMTAHTTNPVPFIVT--KNDVELREG 480
Cdd:TIGR01307 394 MVGHTGNFEAAIKAVEALDVCLGRIVEACKKVGGTLFLTADHGNAEEMIDENGNPHTAHTTNPVPFVCVgaKNVKLIREG 473

                         490       500
                  ....*....|....*....|....*...
gi 872705949  481 GILGDIAPTMLTLLGVEQPKEMTGKTII 508
Cdd:TIGR01307 474 GVLADIAPTILDLMGLEQPAEMTGKSLL 501
Metalloenzyme pfam01676
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ...
 3-497 1.53e-133

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: 392.92  E-value: 1.53e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949    3 KPTALIILDGFGLREETYGNA---VAQAKKPNFDGYWNKFPHTTLTACGEAVGLPEGQMGNSEVGHLNIGAGRIVYQSLT 79
Cdd:pfam01676   1 KKVVLIVLDGWGDRPAEDLNAktpLHIAKTPNMDKLAKEYPEQLIGASGLAVGLPEGQMGGSDVGHLEIGGGRIVYQYLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949   80 RVNVAIREGEFDKNETFQSAIKSVKEKGTALHLFGLLSDGGVHSHMNHMFALLRLAAKEGVEKVYIHAFLDGRDVGPkta 159
Cdd:pfam01676  81 RGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHSHIEHLLALIALAKEAGAIKVHLLGDGDDRPVGY--- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  160 qsyidatneviketgvgqfatisgryysmdrdkrwdrvekcyramvngegptyksaeecvedsyangiydefvlpsvivn 239
Cdd:pfam01676     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  240 edntpvatINDDDAVIFYNFRPDRAIQIARVFTNEDFREFDRGEKVPHIPEFVCMTHFSETVDGYVAFKPMNLDNTLGEV 319
Cdd:pfam01676 158 --------ILDGDAVITINFRFDRRRARILRLFLLDPDFFDRDRVRHDALHVPTKTLYELKLPSAGAFVPEEGKNTDGEV 229

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  320 VAQAGLKQLRIAETEKYPHVTFFFSGGREAEFPGEERILINSPKVATYDLKPEMSIYEVTDALVNEIEnDKHDVIILNFA 399
Cdd:pfam01676 230 LEGHGLKQLRIAETEKYAHVTFFWGGGREPPFPGEERYLIPSPKVATYDLQPEMSAMEITDKLLEALK-EKYDFVFVNFA 308

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  400 NCDMVGHSGMMEPTIKAVEATDECLGKVVEAILAKDGVALITADHGNADEELTsegepmTAHTTNPVPFIVTKNDV---- 475
Cdd:pfam01676 309 NTDMVGHTGDVEGKVKAIEAVDERLGELLDALEEDDGLLIITADHGNPEEMKD------TDHTREPVPILIYGKGVrpdq 382

                         490       500
                  ....*....|....*....|....*..
gi 872705949  476 -----ELREGGILGDIAPTMLTLLGVE 497
Cdd:pfam01676 383 vlfgeKFRERGGLADIAATILMLLGLK 409
 
Name Accession Description Interval E-value
GpmI COG0696
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ...
 2-509 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: 983.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949   2 RKPTALIILDGFGLREETYGNAVAQAKKPNFDGYWNKFPHTTLTACGEAVGLPEGQMGNSEVGHLNIGAGRIVYQSLTRV 81
Cdd:COG0696    2 KKPVVLIILDGWGIREETEGNAIALANTPNLDRLWATYPHTLLRASGEAVGLPDGQMGNSEVGHLNIGAGRVVYQDLTRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  82 NVAIREGEFDKNETFQSAIKSVKEKGTALHLFGLLSDGGVHSHMNHMFALLRLAAKEGVEKVYIHAFLDGRDVGPKTAQS 161
Cdd:COG0696   82 NKAIEDGSFFENPVLLDAIDKAKENGGALHLMGLLSDGGVHSHIDHLKALLELAKEEGVKKVYVHAFLDGRDTPPKSALG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 162 YIDATNEVIKETGVGQFATISGRYYSMDRDKRWDRVEKCYRAMVNGEGPTYKSAEECVEDSYANGIYDEFVLPSVIVNED 241
Cdd:COG0696  162 YLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVNGEGETAASAVEAIEASYARGETDEFVKPTVIVDYG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 242 NtPVATINDDDAVIFYNFRPDRAIQIARVFTNEDFREFDRGeKVPHIPEFVCMTHFSETVDGYVAFKPMNLDNTLGEVVA 321
Cdd:COG0696  242 K-PVATIEDGDAVIFFNFRADRARQLTRAFTDPDFDGFDRG-KRPKLLYFVTMTEYDETFDVPVAFPPENLKNTLGEVLA 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 322 QAGLKQLRIAETEKYPHVTFFFSGGREAEFPGEERILINSPKVATYDLKPEMSIYEVTDALVNEIENDKHDVIILNFANC 401
Cdd:COG0696  320 KAGLKQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIVLNFANP 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 402 DMVGHSGMMEPTIKAVEATDECLGKVVEAILAKDGVALITADHGNADEELTSE-GEPMTAHTTNPVPFIVT--KNDVELR 478
Cdd:COG0696  400 DMVGHTGVLEAAIKAVEAVDECLGRVVDAVLAAGGTLLITADHGNAEQMIDPDtGGPHTAHTTNPVPFILVggDKGVKLR 479

                        490       500       510
                 ....*....|....*....|....*....|.
gi 872705949 479 EGGILGDIAPTMLTLLGVEQPKEMTGKTIIK 509
Cdd:COG0696  480 EDGRLADIAPTILELMGLPQPAEMTGKSLIE 510
PRK05434 PRK05434
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
1-509 0e+00

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


Pssm-ID: 235463  Cd Length: 507  Bit Score: 969.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949   1 MRKPTALIILDGFGLREETYGNAVAQAKKPNFDGYWNKFPHTTLTACGEAVGLPEGQMGNSEVGHLNIGAGRIVYQSLTR 80
Cdd:PRK05434   3 MKKPVVLIILDGWGYREETEGNAIALAKTPNLDRLWANYPHTLLSASGLAVGLPDGQMGNSEVGHLNIGAGRIVYQDLTR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  81 VNVAIREGEFDKNETFQSAIKSVKEKGTALHLFGLLSDGGVHSHMNHMFALLRLAAKEGVEKVYIHAFLDGRDVGPKTAQ 160
Cdd:PRK05434  83 INKAIEDGSFFENPALLDAIDKAKKNGGALHLMGLLSDGGVHSHIDHLFALLELAKEEGVKKVYVHAFLDGRDTPPKSAL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 161 SYIDATNEVIKETGVGQFATISGRYYSMDRDKRWDRVEKCYRAMVNGEGP-TYKSAEECVEDSYANGIYDEFVLPSVIVN 239
Cdd:PRK05434 163 GYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVLGEGPfTAESAVEALEASYARGETDEFVKPTVIGG 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 240 EdntPVATINDDDAVIFYNFRPDRAIQIARVFTNEDFREFDRgekVPHIPEFVCMTHFSETVDGYVAFKPMNLDNTLGEV 319
Cdd:PRK05434 243 E---PVAGIEDGDAVIFFNFRADRARQITRAFTDPDFDGFDR---VPKLLNFVTMTQYDADLKVPVAFPPESLKNTLGEV 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 320 VAQAGLKQLRIAETEKYPHVTFFFSGGREAEFPGEERILINSPKVATYDLKPEMSIYEVTDALVNEIENDKHDVIILNFA 399
Cdd:PRK05434 317 LAKAGLTQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIILNFA 396

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 400 NCDMVGHSGMMEPTIKAVEATDECLGKVVEAILAKDGVALITADHGNADEELTSE-GEPMTAHTTNPVPFIVTKNDVELR 478
Cdd:PRK05434 397 NPDMVGHTGNLEAAVKAVEAVDECLGRVVDAVLKVGGTLLITADHGNAEQMIDPEtGQPHTAHTTNPVPFILVGGKALRL 476

                        490       500       510
                 ....*....|....*....|....*....|.
gi 872705949 479 EGGILGDIAPTMLTLLGVEQPKEMTGKTIIK 509
Cdd:PRK05434 477 EGGKLADIAPTILDLLGLEQPAEMTGKSLIE 507
iPGM cd16010
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ...
 3-508 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: 915.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949   3 KPTALIILDGFGLREETYGNAVAQAKKPNFDGYWNKFPHTTLTACGEAVGLPEGQMGNSEVGHLNIGAGRIVYQSLTRVN 82
Cdd:cd16010    1 KPVVLIILDGWGIRPEDEGNAIALAKTPNLDRLWATYPHTLLKASGEAVGLPDGQMGNSEVGHLNIGAGRIVYQDLTRIN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  83 VAIREGEFDKNETFQSAIKSVKEKGTALHLFGLLSDGGVHSHMNHMFALLRLAAKEGVEKVYIHAFLDGRDVGPKTAQSY 162
Cdd:cd16010   81 KAIEDGSFFKNEALLKAIEHAKKNNSTLHLMGLLSDGGVHSHIDHLFALLELAKKEGVKKVYVHAFTDGRDTPPKSALKY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 163 IDATNEVIKETGVGQFATISGRYYSMDRDKRWDRVEKCYRAMVNGEGPTYKSAEECVEDSYANGIYDEFVLPSVIVNEDN 242
Cdd:cd16010  161 LKELEEKLKELGVGKIASVSGRYYAMDRDKRWDRTEKAYDALVLGEGEKAESAEEAIEASYAKGITDEFIPPTVIGDEGG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 243 tpvaTINDDDAVIFYNFRPDRAIQIARVFTNEDFREFDRgeKVPHIPEFVCMTHFSETVDGYVAFKPMNLDNTLGEVVAQ 322
Cdd:cd16010  241 ----TIKDGDAVIFFNFRADRARQITRAFTDPDFDGFDR--KKPKNLYFVTMTEYDKDLPVPVAFPPPKIKNTLGEVLSK 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 323 AGLKQLRIAETEKYPHVTFFFSGGREAEFPGEERILINSPKVATYDLKPEMSIYEVTDALVNEIENDKHDVIILNFANCD 402
Cdd:cd16010  315 AGLKQLRIAETEKYAHVTYFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLIEAIKSGKYDFIVVNFANPD 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 403 MVGHSGMMEPTIKAVEATDECLGKVVEAILAKDGVALITADHGNADEELTSE-GEPMTAHTTNPVPFIVTKNDVE--LRE 479
Cdd:cd16010  395 MVGHTGNLEAAVKAVEAVDECLGRIVEAVLENGGTLLITADHGNAEEMIDPEtGGPHTAHTTNPVPFIIVDPGLKrkLLK 474

                        490       500
                 ....*....|....*....|....*....
gi 872705949 480 GGILGDIAPTMLTLLGVEQPKEMTGKTII 508
Cdd:cd16010  475 DGGLADVAPTILDLLGIEKPKEMTGKSLI 503
pgm_bpd_ind TIGR01307
phosphoglycerate mutase (2,3-diphosphoglycerate-independent); This protein is about double in ...
 3-508 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: 721.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949    3 KPTALIILDGFGLREETYGNAVAQAKKPNFDGYWNKFPHTTLTACGEAVGLPEGQMGNSEVGHLNIGAGRIVYQSLTRVN 82
Cdd:TIGR01307   1 KKVVLVILDGWGYRNDDDGNAIFAAKTPTMDELIAAYPYSLLDASGLDVGLPDGQMGNSEVGHLNIGAGRVVYQDLVRIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949   83 VAIREGEFDKNETFQSAIKSVKEKGTALHLFGLLSDGGVHSHMNHMFALLRLAAKEGVEKVYIHAFLDGRDVGPKTAQSY 162
Cdd:TIGR01307  81 QAIKDGEFFANPALLGAIDRAKDNNGKLHLMGLVSDGGVHSHIDHLIALIELAAERGIEKVVLHAFTDGRDTAPKSAESY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  163 IDATNEVIKETGVGQFATISGRYYSMDRDKRWDRVEKCYRAMVNGEGPTYKSAEECVEDSYANGIYDEFVLPSVIVNEDn 242
Cdd:TIGR01307 161 LEQLQAFLKEIGNGRIATISGRYYAMDRDQRWDRVEIAYKAITGGDGFEFSDPVAYIQDAYARDITDEFIKPTIIGNGG- 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  243 tpvaTINDDDAVIFYNFRPDRAIQIARVFTNEDFREFDRgEKVPHIpEFVCMTHFSETVDGYVAFKPMNLDNTLGEVVAQ 322
Cdd:TIGR01307 240 ----ALKDGDAVIFFNFRADRAREITRALVNSDFDGFPR-EKNPKL-DFVTMTQYDGTFPSPVAFPPQSLTNTLGEVLAK 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  323 AGLKQLRIAETEKYPHVTFFFSGGREAEFPGEERILINSPKVATYDLKPEMSIYEVTDALVNEIENDKHDVIILNFANCD 402
Cdd:TIGR01307 314 HDLTQLRIAETEKYAHVTFFFNGGVEVPFAGETRTLIPSPKVATYDLQPEMSAKAVTDAVLEAIAQGKFDLIVVNFANPD 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  403 MVGHSGMMEPTIKAVEATDECLGKVVEAILAKDGVALITADHGNADEELTSEGEPMTAHTTNPVPFIVT--KNDVELREG 480
Cdd:TIGR01307 394 MVGHTGNFEAAIKAVEALDVCLGRIVEACKKVGGTLFLTADHGNAEEMIDENGNPHTAHTTNPVPFVCVgaKNVKLIREG 473

                         490       500
                  ....*....|....*....|....*...
gi 872705949  481 GILGDIAPTMLTLLGVEQPKEMTGKTII 508
Cdd:TIGR01307 474 GVLADIAPTILDLMGLEQPAEMTGKSLL 501
Metalloenzyme pfam01676
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ...
 3-497 1.53e-133

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: 392.92  E-value: 1.53e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949    3 KPTALIILDGFGLREETYGNA---VAQAKKPNFDGYWNKFPHTTLTACGEAVGLPEGQMGNSEVGHLNIGAGRIVYQSLT 79
Cdd:pfam01676   1 KKVVLIVLDGWGDRPAEDLNAktpLHIAKTPNMDKLAKEYPEQLIGASGLAVGLPEGQMGGSDVGHLEIGGGRIVYQYLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949   80 RVNVAIREGEFDKNETFQSAIKSVKEKGTALHLFGLLSDGGVHSHMNHMFALLRLAAKEGVEKVYIHAFLDGRDVGPkta 159
Cdd:pfam01676  81 RGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHSHIEHLLALIALAKEAGAIKVHLLGDGDDRPVGY--- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  160 qsyidatneviketgvgqfatisgryysmdrdkrwdrvekcyramvngegptyksaeecvedsyangiydefvlpsvivn 239
Cdd:pfam01676     --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  240 edntpvatINDDDAVIFYNFRPDRAIQIARVFTNEDFREFDRGEKVPHIPEFVCMTHFSETVDGYVAFKPMNLDNTLGEV 319
Cdd:pfam01676 158 --------ILDGDAVITINFRFDRRRARILRLFLLDPDFFDRDRVRHDALHVPTKTLYELKLPSAGAFVPEEGKNTDGEV 229

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  320 VAQAGLKQLRIAETEKYPHVTFFFSGGREAEFPGEERILINSPKVATYDLKPEMSIYEVTDALVNEIEnDKHDVIILNFA 399
Cdd:pfam01676 230 LEGHGLKQLRIAETEKYAHVTFFWGGGREPPFPGEERYLIPSPKVATYDLQPEMSAMEITDKLLEALK-EKYDFVFVNFA 308

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  400 NCDMVGHSGMMEPTIKAVEATDECLGKVVEAILAKDGVALITADHGNADEELTsegepmTAHTTNPVPFIVTKNDV---- 475
Cdd:pfam01676 309 NTDMVGHTGDVEGKVKAIEAVDERLGELLDALEEDDGLLIITADHGNPEEMKD------TDHTREPVPILIYGKGVrpdq 382

                         490       500
                  ....*....|....*....|....*..
gi 872705949  476 -----ELREGGILGDIAPTMLTLLGVE 497
Cdd:pfam01676 383 vlfgeKFRERGGLADIAATILMLLGLK 409
iPGM_N pfam06415
BPG-independent PGAM N-terminus (iPGM_N); This family represents the N-terminal region of the ...
 81-299 2.41e-128

BPG-independent PGAM N-terminus (iPGM_N); This family represents the N-terminal region of the 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (or phosphoglyceromutase or BPG-independent PGAM) protein (EC:5.4.2.1). The family is found in conjunction with pfam01676 (located in the C-terminal region of the protein).


Pssm-ID: 461901  Cd Length: 217  Bit Score: 372.12  E-value: 2.41e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949   81 VNVAIREGEFDKNETFQSAIKSVKEKGTALHLFGLLSDGGVHSHMNHMFALLRLAAKEGVEKVYIHAFLDGRDVGPKTAQ 160
Cdd:pfam06415   1 INKAIEDGSFFENPALLKAIENAKANGGALHLMGLLSDGGVHSHIDHLFALLELAKEEGVKKVYVHAFLDGRDTPPKSAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  161 SYIDATNEVIKETGVGQFATISGRYYSMDRDKRWDRVEKCYRAMVNGEGPTYKSAEECVEDSYANGIYDEFVLPSVIVnE 240
Cdd:pfam06415  81 GYLEQLEAKLAELGVGKIATVSGRYYAMDRDKRWDRVEKAYDALVLGEGESAADAVEAIEASYARGETDEFVKPTVIV-D 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 872705949  241 DNTPVATINDDDAVIFYNFRPDRAIQIARVFTNEDFREFDRGeKVPHIPEFVCMTHFSE 299
Cdd:pfam06415 160 DGKPVGTIKDGDSVIFFNFRPDRAREITRAFTDPDFDGFERR-KRPKDLHFVTMTQYDA 217
PLN02538 PLN02538
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
 3-502 9.47e-120

2,3-bisphosphoglycerate-independent phosphoglycerate mutase


Pssm-ID: 215295  Cd Length: 558  Bit Score: 362.84  E-value: 9.47e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949   3 KPTALIILDGFGLREETYGNAVAQAKKPNFDGYWNKFPHT--TLTACGEAVGLP-EGQMGNSEVGHLNIGAGRIVYQSLT 79
Cdd:PLN02538  21 KPLLLIVLDGWGENAPDEFNAIHVAPTPTMDSLKAGAPERwrLVKAHGTAVGLPsDDDMGNSEVGHNALGAGRIFAQGAK 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  80 RVNVAIREGEFDKNETFQSaIKSVKEKGTaLHLFGLLSDGGVHSHMNHMFALLRLAAKEGVEKVYIHAFLDGRDVGPKTA 159
Cdd:PLN02538 101 LVDLALASGKIFEGEGFKY-IKEAFATGT-LHLIGLLSDGGVHSRLDQLQLLLKGAAERGAKRIRVHVLTDGRDVPDGSS 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 160 QSYIDATNEV---IKETGV-GQFATISGRYY-SMDR-DKRWDRVEKCYRAMVNGEGP-TYKSAEECVEDSYANG--IYDE 230
Cdd:PLN02538 179 VGFVETLEKDlaeLREKGCdARIASGGGRMYvTMDRyENDWNVVKRGWDAHVLGEAPhKFKSALEAVKKLREEPppANDQ 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 231 FVLPSVIVNEDNTPVATINDDDAVIFYNFRPDRAIQIARVFTNEDFREFDRGeKVPHIpEFVCMTHFsetvDG------- 303
Cdd:PLN02538 259 YLPPFVIVDEDGKPVGPIEDGDAVVTFNFRADRMVMIAKALEYEDFDKFDRV-RVPKI-RYAGMLQY----DGelklpsh 332

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 304 YVAfKPMNLDNTLGEVVAQAGLKQLRIAETEKYPHVTFFFSGGREAEFPG--EERILINSPKVATYDLKPEMSIYEVTDA 381
Cdd:PLN02538 333 YLV-SPPLIERTSGEYLVANGVRTFACSETVKFGHVTFFWNGNRSGYFNEklEEYVEIPSDNGIPFNVQPKMKALEIAEK 411

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 382 LVNEIENDKHDVIILNFANCDMVGHSGMMEPTIKAVEATDECLGKVVEAILAKDGVALITADHGNADE----------EL 451
Cdd:PLN02538 412 ARDALLSGKFDQVRVNLANGDMVGHTGDLEATIVACEAVDAAVKEILDAVEQVGGIYLVTADHGNAEDmvkrdksgkpLL 491

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 872705949 452 TSEGEP--MTAHTTNPVPF----------IVTKNDveLREGGiLGDIAPTMLTLLGVEQPKEM 502
Cdd:PLN02538 492 DKDGNPqiLTSHTLAPVPVaiggpglppgVRFRDD--LPTAG-LANVAATVMNLHGFEAPADY 551
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 383-494 3.65e-19

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: 86.71  E-value: 3.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 383 VNEIENDKHDVIILNFANCDMVGHS--GMMEPTIKAVEATDECLGKVVEAI----LAKDGVALITADHGNADEELT---- 452
Cdd:cd00016  112 IDETSKEKPFVLFLHFDGPDGPGHAygPNTPEYYDAVEEIDERIGKVLDALkkagDADDTVIIVTADHGGIDKGHGgdpk 191

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 872705949 453 SEGEPMTAHTTNPVPFIVT----KNDVELREGGILGDIAPTMLTLL 494
Cdd:cd00016  192 ADGKADKSHTGMRVPFIAYgpgvKKGGVKHELISQYDIAPTLADLL 237
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 3-116 1.11e-08

alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.


Pssm-ID: 293732 [Multi-domain]  Cd Length: 237  Bit Score: 55.89  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949   3 KPTALIILDGFGLREETYGNAVAQAkKPNFDGYWNKFPHTTLTACgeavglpeGQMGNSEVGHLNIGAGRIVYQSLTRVN 82
Cdd:cd00016    1 KHVVLIVLDGLGADDLGKAGNPAPT-TPNLKRLASEGATFNFRSV--------SPPTSSAPNHAALLTGAYPTLHGYTGN 71

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 872705949  83 VAIREG----EFDKNETFQSAIKSVKEKGTALHLFGLL 116
Cdd:cd00016   72 GSADPElpsrAAGKDEDGPTIPELLKQAGYRTGVIGLL 109
PPM cd16009
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ...
 377-503 1.47e-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: 56.69  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 377 EVTDALVNEIENDKHDVIILNFANCDMV-GHS----GMmeptIKAVEATDECLGKVVEAiLAKDGVALITADHGNaDEel 451
Cdd:cd16009  257 DGMEKTLEALKEDFNGLIFTNLVDFDMLyGHRrdpeGY----AEALEEFDRRLPELLAK-LKEDDLLIITADHGN-DP-- 328

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 872705949 452 TSEGepmTAHTTNPVPFIVTKNDVELREGGI---LGDIAPTMLTLLGVEQPKEMT 503
Cdd:cd16009  329 TIGG---TDHTREYVPLLVYGKGLKGVNLGTretFADIGATIADNFGVEPPENGT 380
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 420-505 1.74e-07

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


Pssm-ID: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 52.55  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 420 TDECLGKVVEAI----LAKDGVALITADHGnadEEL------TSEGEPMTAHTTNpVPFIVTKNDVE--LREGGILG--D 485
Cdd:cd16148  172 VDEQIGRLLDKLkelgLLEDTLVIVTSDHG---EEFgehglyWGHGSNLYDEQLH-VPLIIRWPGKEpgKRVDALVShiD 247

                         90       100
                 ....*....|....*....|
gi 872705949 486 IAPTMLTLLGVEQPKEMTGK 505
Cdd:cd16148  248 IAPTLLDLLGVEPPDYSDGR 267
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
 421-509 4.89e-07

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: 52.00  E-value: 4.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 421 DECLGKVVEAI--LAKDGVALITADHGNA--DEELTSEGEPMTAHTTNpVPFIVTKNDVELREGGI-----LGDIAPTML 491
Cdd:cd16156  251 DYEIGRVLDAAdeIAEDAWVIYTSDHGDMlgAHKLWAKGPAVYDEITN-IPLIIRGKGGEKAGTVTdtpvsHIDLAPTIL 329

                         90
                 ....*....|....*...
gi 872705949 492 TLLGVEQPKEMTGKTIIK 509
Cdd:cd16156  330 DYAGIPQPKVLEGESILA 347
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
 416-505 7.43e-07

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: 51.35  E-value: 7.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 416 AVEATDECLGKVVEAiLAKDGVA-----LITADHGNadeeltsegePMTAHTTNP------VPFIV---------TKND- 474
Cdd:cd16027  194 EIERLDQQVGEILDE-LEEDGLLdntivIFTSDHGM----------PFPRAKGTLydsglrVPLIVrwpgkikpgSVSDa 262

                         90       100       110
                 ....*....|....*....|....*....|..
gi 872705949 475 -VELreggIlgDIAPTMLTLLGVEQPKEMTGK 505
Cdd:cd16027  263 lVSF----I--DLAPTLLDLAGIEPPEYLQGR 288
PRK05362 PRK05362
phosphopentomutase; Provisional
 380-509 7.63e-07

phosphopentomutase; Provisional


Pssm-ID: 235430  Cd Length: 394  Bit Score: 51.27  E-value: 7.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 380 DALVNEIENDKHDVII-LNFANCDMV-GH----SGMMeptiKAVEATDECLGKVVEAiLAKDGVALITADHGNaDEelTS 453
Cdd:PRK05362 266 DATIEEMKEAGDNGLVfTNLVDFDSLyGHrrdvAGYA----AALEEFDARLPELLAA-LKEDDLLIITADHGN-DP--TW 337

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 872705949 454 EGepmTAHTTNPVPFIV-----TKNDVELREGgiLGDIAPTMLTLLGVEQPKemTGKTIIK 509
Cdd:PRK05362 338 PG---TDHTREYVPLLVygpkfKGGSLGHRET--FADIGATIADNFGVEPME--YGKSFLD 391
PRK04024 PRK04024
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
389-495 1.33e-06

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


Pssm-ID: 235203  Cd Length: 412  Bit Score: 50.68  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 389 DKHDVIILNFANCDMVGHSGMMEPTIKAVEATDECLGKVVEAILAKDGVALITADHGNADEELTsegepmtaHTTNPVPF 468
Cdd:PRK04024 292 KEYDFVLLNIKGTDEAGHDGDFEGKVEVIEKIDKMLGYILDNLDLDEVYIAVTGDHSTPVEVKD--------HSGDPVPI 363

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 872705949 469 IVTKNDV-----------ELREGG---ILG-DIAPTMLTLLG 495
Cdd:PRK04024 364 LIYGPGVrvddvekfnelSAAKGGlgrIRGlDVMPILLDLMN 405
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 378-448 2.24e-06

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 49.75  E-value: 2.24e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 872705949 378 VTDALVNEIENDKHDVIILNFANCDMVGHS-GMM-EPTIKAVEATDECLGKVVEAILA---KDGVALI-TADHGNAD 448
Cdd:COG1524  170 IAAAALELLREGRPDLLLVYLPDLDYAGHRyGPDsPEYRAALREVDAALGRLLDALKArglYEGTLVIvTADHGMVD 246
DeoB COG1015
Phosphopentomutase [Carbohydrate transport and metabolism];
380-500 3.51e-06

Phosphopentomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440639  Cd Length: 385  Bit Score: 49.28  E-value: 3.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 380 DALVNEIENDKHDVIILNFANCDMV-GH----SGMMeptiKAVEATDECLGKVVEAiLAKDGVALITADHGNaDEelTSE 454
Cdd:COG1015  260 DKTLEAMDEAFGGLIFTNLVDFDSLyGHrrdvAGYA----KALEEFDARLPELLAA-LRPDDLLIITADHGN-DP--TWP 331

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 872705949 455 GepmTAHTTNPVPFIVTKNDVelREGGILG------DIAPTMLTLLGVEQPK 500
Cdd:COG1015  332 G---TDHTREYVPLLVYGPGL--KPGGNLGtretfaDIGATIADHFGVPPPG 378
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 372-495 4.38e-06

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: 48.35  E-value: 4.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 372 EMSIYEVTDALVNEIENDKHDVIILNFANCDMVGHS-GMMEP-TIKAVEATDECLGKVVEAILAK---DGVALI-TADHG 445
Cdd:cd16018  138 SFPFEERVDTILEWLDLERPDLILLYFEEPDSAGHKyGPDSPeVNEALKRVDRRLGYLIEALKERgllDDTNIIvVSDHG 217

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 872705949 446 nadeeltsegepMTA---HTTNP------VPFIVTKNDVelREGGILG-----DIAPTMLTLLG 495
Cdd:cd16018  218 ------------MTDvgtHGYDNelpdmrAIFIARGPAF--KKGKKLGpfrnvDIYPLMCNLLG 267
apgM TIGR00306
phosphoglycerate mutase (2,3-diphosphoglycerate-independent), archaeal form; Experimentally ...
 371-475 5.79e-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: 48.62  E-value: 5.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949  371 PEMSIYEVTDALVNEIEndKHDVIILNFANCDMVGHSGMMEPTIKAVEATDECLGKVVEAILAKDGVALITADHGNADEE 450
Cdd:TIGR00306 270 IDTDYRGKVRALILALE--EYDFVLVHTKGPDEAGHDGDPELKVRAIEKIDSKIVGPLLALDLDETRLILTADHSTPVEV 347

                          90       100
                  ....*....|....*....|....*
gi 872705949  451 LTsegepmtaHTTNPVPFIVTKNDV 475
Cdd:TIGR00306 348 KD--------HSADPVPIVIVGPGV 364
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 416-505 2.81e-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: 293758 [Multi-domain]  Cd Length: 399  Bit Score: 46.41  E-value: 2.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 416 AVEATDECLGKVVEAI----LAKDGVALITADHGnadeeltsegEPMTAH----TTNP------VPFIVTKNDVeLREGG 481
Cdd:cd16034  232 MITALDDNIGRLLDALkelgLLENTIVVFTSDHG----------DMLGSHglmnKQVPyeesirVPFIIRYPGK-IKAGR 300

                         90       100       110
                 ....*....|....*....|....*....|
gi 872705949 482 I----LG--DIAPTMLTLLGVEQPKEMTGK 505
Cdd:cd16034  301 VvdllINtvDIMPTLLGLCGLPIPDTVEGR 330
sulfatase_like cd16022
sulfatase; Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, ...
 417-505 2.85e-05

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: 45.51  E-value: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 417 VEATDECLGKVVEAiLAKDGVA-----LITADHGnadeELTSEGEPMTAHTTNP-----VPFIVT-----KNDVELREGG 481
Cdd:cd16022  137 VSAIDDQIGRILDA-LEELGLLdntliVFTSDHG----DMLGDHGLRGKKGSLYeggirVPFIVRwpgkiPAGQVSDALV 211

                         90       100
                 ....*....|....*....|....
gi 872705949 482 ILGDIAPTMLTLLGVEQPKEMTGK 505
Cdd:cd16022  212 SLLDLLPTLLDLAGIEPPEGLDGR 235
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 417-505 4.12e-05

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


Pssm-ID: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 45.61  E-value: 4.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 417 VEATDECLGKVVEAI----LAKDGVALITADHGnadEELTSEG--------EPmTAHttnpVPFIVTKNDVElrEGGI-- 482
Cdd:cd16037  168 VEFLDENIGRVLDALeelgLLDNTLIIYTSDHG---DMLGERGlwgkstmyEE-SVR----VPMIISGPGIP--AGKRvk 237

                         90       100
                 ....*....|....*....|....*..
gi 872705949 483 ----LGDIAPTMLTLLGVEQPKEMTGK 505
Cdd:cd16037  238 tpvsLVDLAPTILEAAGAPPPPDLDGR 264
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
416-505 5.79e-05

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 45.25  E-value: 5.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 416 AVEATDECLGKVVEAiLAKDGVA-----LITADHGNADEELTSEGEPMTAH--TTNpVPFIV---------TKND--VEL 477
Cdd:COG3119  205 MIEEVDDQVGRLLDA-LEELGLAdntivVFTSDNGPSLGEHGLRGGKGTLYegGIR-VPLIVrwpgkikagSVSDalVSL 282

                         90       100
                 ....*....|....*....|....*...
gi 872705949 478 ReggilgDIAPTMLTLLGVEQPKEMTGK 505
Cdd:COG3119  283 I------DLLPTLLDLAGVPIPEDLDGR 304
iPGM_like cd16011
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate ...
 389-475 1.03e-04

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: 44.38  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 389 DKHDVIILNFANCDMVGHSGMMEPTIKAVEATDECLGKVVEAILAKDGVAL-ITADHgnadeeLTsegePMT--AHTTNP 465
Cdd:cd16011  255 KDYDFVFVHVKAPDEAGHDGDPEAKVKAIERIDKAIVGPLLELLDGEDFVIvVTPDH------ST----PCSlkTHSGDP 324

                         90
                 ....*....|
gi 872705949 466 VPFIVTKNDV 475
Cdd:cd16011  325 VPFLIYGPGV 334
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
 414-503 1.17e-04

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 44.64  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 414 IKAVEATDECLGKVVEAI----LAKDGVALITADHGNADEELTSEGEPMTAHTtnpVPFIVTKNDV-ELREGGILG---D 485
Cdd:COG1368  420 LNAVRYADQALGEFIEKLkksgWYDNTIFVIYGDHGPRSPGKTDYENPLERYR---VPLLIYSPGLkKPKVIDTVGsqiD 496

                         90
                 ....*....|....*...
gi 872705949 486 IAPTMLTLLGVEQPKEMT 503
Cdd:COG1368  497 IAPTLLDLLGIDYPSYYA 514
PRK12383 PRK12383
putative mutase; Provisional
 377-499 2.98e-04

putative mutase; Provisional


Pssm-ID: 237085  Cd Length: 406  Bit Score: 43.03  E-value: 2.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 377 EVTDALVNEIENDKHDVIILNFANCDMVGHSGMMEPTIKAVEATDECLGKVVEAiLAKDGVALITADHGNadeeltsegE 456
Cdd:PRK12383 273 RVMDITLDEFNTHPTAFICTNIQETDLAGHAEDVARYAERLEVVDRNLARLLEA-MTPDDCLVVMADHGN---------D 342

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 872705949 457 PM---TAHTTNPVPFIVTKND---VELREGGILGDIAPTMLTLLGVEQP 499
Cdd:PRK12383 343 PTighSHHTREVVPLLVYQKGlqaTQLGVRTTLSDVGATVCEFFGAPPP 391
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 421-508 8.02e-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: 293757 [Multi-domain]  Cd Length: 411  Bit Score: 41.82  E-value: 8.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 421 DECLGKVVEAI----LAKDGVALITADHGNA--DEELTSEGEPMTAHTTNpVPFIVtKNDVELREGGI------LGDIAP 488
Cdd:cd16033  227 DDAIGRILDALeelgLADDTLVIFTSDHGDAlgAHRLWDKGPFMYEETYR-IPLII-KWPGVIAAGQVvdefvsLLDLAP 304

                         90       100
                 ....*....|....*....|
gi 872705949 489 TMLTLLGVEQPKEMTGKTII 508
Cdd:cd16033  305 TILDLAGVDVPPKVDGRSLL 324
PRK04200 PRK04200
cofactor-independent phosphoglycerate mutase; Provisional
 391-476 4.23e-03

cofactor-independent phosphoglycerate mutase; Provisional


Pssm-ID: 179781  Cd Length: 395  Bit Score: 39.47  E-value: 4.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 391 HDVIILNFANCDMVGHSGMMEPTIKAVEATDE-CLGKVVEAILAKDGVA-LITADHgnadeeltsegeP-----MTaHTT 463
Cdd:PRK04200 284 HDFVFVHVEAPDEAGHEGDLEAKIKAIEDIDErVVGPILEALKKYEDYRiLVLPDH------------PtpielKT-HTA 350

                         90
                 ....*....|...
gi 872705949 464 NPVPFIVTKNDVE 476
Cdd:PRK04200 351 DPVPFLIYGEGIE 363
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
 378-507 5.25e-03

GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is involved in glycosylphosphatidylinositol-anchor biosynthesis. It catalyzes the transfer of ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. It may act as suppressor of replication stress and chromosome missegregation.


Pssm-ID: 293748 [Multi-domain]  Cd Length: 274  Bit Score: 38.70  E-value: 5.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872705949 378 VTDALVNEIENDKHDVIILNFANCDMVGHSG-----MMEPtiKAVEaTDECLGKVVEAILA----KDGVALITADHGNAD 448
Cdd:cd16024  132 VTRHLDSELSRDDWDVLILHYLGLDHIGHLEgpkspLMPP--KLKE-MDDVIKRIYESLEEqssnNPTLLVVCGDHGMTD 208

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 872705949 449 eeLTSEGEPMTAHTTNPVPFIVTK----NDVELREGGILG-----DIAPTMLTLLGVEQPKEMTGKTI 507
Cdd:cd16024  209 --AGNHGGSSPGETSVPLLFISPKfsskPSNADGELSYYEtvqqvDLAPTLALLLGLPIPKNSVGVLI 274
 
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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