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Conserved domains on  [gi|581387295|gb|EVN98337|]
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2,3-bisphosphoglycerate-independent phosphoglycerate mutase [Staphylococcus aureus M1022]

Protein Classification

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

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

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

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK05434 PRK05434
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
1-504 0e+00

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


:

Pssm-ID: 235463  Cd Length: 507  Bit Score: 921.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295   1 MAKKPTALIILDGFANRESEHGNAVKLANKPNFDRYYNKYPTTQIEASGLDVGLPEGQMGNSEVGHMNIGAGRIVYQSLT 80
Cdd:PRK05434   2 MMKKPVVLIILDGWGYREETEGNAIALAKTPNLDRLWANYPHTLLSASGLAVGLPDGQMGNSEVGHLNIGAGRIVYQDLT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  81 RINKSIEDGDFFENDVLNNAIAHVNSHDSALHIFGLLSDGGVHSHYKHLFALLELAKKQGVEKVYVHAFLDGRDVDQKSA 160
Cdd:PRK05434  82 RINKAIEDGSFFENPALLDAIDKAKKNGGALHLMGLLSDGGVHSHIDHLFALLELAKEEGVKKVYVHAFLDGRDTPPKSA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 161 LKYIEETEAKFNELGIGQFASVSGRYYAMDRDKRWEREEKAYNAIRNFDAPTYA-TAKEGVEASYNEGLTDEFVVPFIVE 239
Cdd:PRK05434 162 LGYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVLGEGPFTAeSAVEALEASYARGETDEFVKPTVIG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 240 NQNDG-VNDGDAVIFYNFRPDRAAQLSEIFANRAFEGFKvEQVKDLFYATFTKYNDNIDAAIVFEKVDLNNTIGEIAQNN 318
Cdd:PRK05434 242 GEPVAgIEDGDAVIFFNFRADRARQITRAFTDPDFDGFD-RVPKLLNFVTMTQYDADLKVPVAFPPESLKNTLGEVLAKA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 319 NLTQLRIAETEKYPHVTYFMSGGRNEEFKGERRRLIDSPKVATYDLKPEMSAYEVKDALLEELNKGDLDLIILNFANPDM 398
Cdd:PRK05434 321 GLTQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIILNFANPDM 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 399 VGHSGMLEPTIKAIEAVDECLGEVVDKILDMDGYAIITADHGNSDQVLTDDD-QPMTTHTTNPVPVIVTKEGVTLRETGR 477
Cdd:PRK05434 401 VGHTGNLEAAVKAVEAVDECLGRVVDAVLKVGGTLLITADHGNAEQMIDPETgQPHTAHTTNPVPFILVGGKALRLEGGK 480

                        490       500
                 ....*....|....*....|....*..
gi 581387295 478 LGDLAPTLLDLLNVEQPEDMTGESLIK 504
Cdd:PRK05434 481 LADIAPTILDLLGLEQPAEMTGKSLIE 507
 
Name Accession Description Interval E-value
PRK05434 PRK05434
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
1-504 0e+00

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


Pssm-ID: 235463  Cd Length: 507  Bit Score: 921.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295   1 MAKKPTALIILDGFANRESEHGNAVKLANKPNFDRYYNKYPTTQIEASGLDVGLPEGQMGNSEVGHMNIGAGRIVYQSLT 80
Cdd:PRK05434   2 MMKKPVVLIILDGWGYREETEGNAIALAKTPNLDRLWANYPHTLLSASGLAVGLPDGQMGNSEVGHLNIGAGRIVYQDLT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  81 RINKSIEDGDFFENDVLNNAIAHVNSHDSALHIFGLLSDGGVHSHYKHLFALLELAKKQGVEKVYVHAFLDGRDVDQKSA 160
Cdd:PRK05434  82 RINKAIEDGSFFENPALLDAIDKAKKNGGALHLMGLLSDGGVHSHIDHLFALLELAKEEGVKKVYVHAFLDGRDTPPKSA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 161 LKYIEETEAKFNELGIGQFASVSGRYYAMDRDKRWEREEKAYNAIRNFDAPTYA-TAKEGVEASYNEGLTDEFVVPFIVE 239
Cdd:PRK05434 162 LGYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVLGEGPFTAeSAVEALEASYARGETDEFVKPTVIG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 240 NQNDG-VNDGDAVIFYNFRPDRAAQLSEIFANRAFEGFKvEQVKDLFYATFTKYNDNIDAAIVFEKVDLNNTIGEIAQNN 318
Cdd:PRK05434 242 GEPVAgIEDGDAVIFFNFRADRARQITRAFTDPDFDGFD-RVPKLLNFVTMTQYDADLKVPVAFPPESLKNTLGEVLAKA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 319 NLTQLRIAETEKYPHVTYFMSGGRNEEFKGERRRLIDSPKVATYDLKPEMSAYEVKDALLEELNKGDLDLIILNFANPDM 398
Cdd:PRK05434 321 GLTQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIILNFANPDM 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 399 VGHSGMLEPTIKAIEAVDECLGEVVDKILDMDGYAIITADHGNSDQVLTDDD-QPMTTHTTNPVPVIVTKEGVTLRETGR 477
Cdd:PRK05434 401 VGHTGNLEAAVKAVEAVDECLGRVVDAVLKVGGTLLITADHGNAEQMIDPETgQPHTAHTTNPVPFILVGGKALRLEGGK 480

                        490       500
                 ....*....|....*....|....*..
gi 581387295 478 LGDLAPTLLDLLNVEQPEDMTGESLIK 504
Cdd:PRK05434 481 LADIAPTILDLLGLEQPAEMTGKSLIE 507
GpmI COG0696
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ...
 2-504 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: 919.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295   2 AKKPTALIILDGFANRESEHGNAVKLANKPNFDRYYNKYPTTQIEASGLDVGLPEGQMGNSEVGHMNIGAGRIVYQSLTR 81
Cdd:COG0696    1 RKKPVVLIILDGWGIREETEGNAIALANTPNLDRLWATYPHTLLRASGEAVGLPDGQMGNSEVGHLNIGAGRVVYQDLTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  82 INKSIEDGDFFENDVLNNAIAHVNSHDSALHIFGLLSDGGVHSHYKHLFALLELAKKQGVEKVYVHAFLDGRDVDQKSAL 161
Cdd:COG0696   81 INKAIEDGSFFENPVLLDAIDKAKENGGALHLMGLLSDGGVHSHIDHLKALLELAKEEGVKKVYVHAFLDGRDTPPKSAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 162 KYIEETEAKFNELGIGQFASVSGRYYAMDRDKRWEREEKAYNAIRNFDAPTYATAKEGVEASYNEGLTDEFVVPFIVENQ 241
Cdd:COG0696  161 GYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVNGEGETAASAVEAIEASYARGETDEFVKPTVIVDY 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 242 ND---GVNDGDAVIFYNFRPDRAAQLSEIFANRAFEGFKVEQV-KDLFYATFTKYNDNIDAAIVFEKVDLNNTIGEIAQN 317
Cdd:COG0696  241 GKpvaTIEDGDAVIFFNFRADRARQLTRAFTDPDFDGFDRGKRpKLLYFVTMTEYDETFDVPVAFPPENLKNTLGEVLAK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 318 NNLTQLRIAETEKYPHVTYFMSGGRNEEFKGERRRLIDSPKVATYDLKPEMSAYEVKDALLEELNKGDLDLIILNFANPD 397
Cdd:COG0696  321 AGLKQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIVLNFANPD 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 398 MVGHSGMLEPTIKAIEAVDECLGEVVDKILDMDGYAIITADHGNSDQVLTDD-DQPMTTHTTNPVPVIVT--KEGVTLRE 474
Cdd:COG0696  401 MVGHTGVLEAAIKAVEAVDECLGRVVDAVLAAGGTLLITADHGNAEQMIDPDtGGPHTAHTTNPVPFILVggDKGVKLRE 480

                        490       500       510
                 ....*....|....*....|....*....|
gi 581387295 475 TGRLGDLAPTLLDLLNVEQPEDMTGESLIK 504
Cdd:COG0696  481 DGRLADIAPTILELMGLPQPAEMTGKSLIE 510
iPGM cd16010
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ...
 4-503 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: 864.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295   4 KPTALIILDGFANRESEHGNAVKLANKPNFDRYYNKYPTTQIEASGLDVGLPEGQMGNSEVGHMNIGAGRIVYQSLTRIN 83
Cdd:cd16010    1 KPVVLIILDGWGIRPEDEGNAIALAKTPNLDRLWATYPHTLLKASGEAVGLPDGQMGNSEVGHLNIGAGRIVYQDLTRIN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  84 KSIEDGDFFENDVLNNAIAHVNSHDSALHIFGLLSDGGVHSHYKHLFALLELAKKQGVEKVYVHAFLDGRDVDQKSALKY 163
Cdd:cd16010   81 KAIEDGSFFKNEALLKAIEHAKKNNSTLHLMGLLSDGGVHSHIDHLFALLELAKKEGVKKVYVHAFTDGRDTPPKSALKY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 164 IEETEAKFNELGIGQFASVSGRYYAMDRDKRWEREEKAYNAIRNFDAPTYATAKEGVEASYNEGLTDEFVVPFIVENQND 243
Cdd:cd16010  161 LKELEEKLKELGVGKIASVSGRYYAMDRDKRWDRTEKAYDALVLGEGEKAESAEEAIEASYAKGITDEFIPPTVIGDEGG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 244 GVNDGDAVIFYNFRPDRAAQLSEIFANRAFEGFKVEQVKDLFYATFTKYNDNIDAAIVFEKVDLNNTIGEIAQNNNLTQL 323
Cdd:cd16010  241 TIKDGDAVIFFNFRADRARQITRAFTDPDFDGFDRKKPKNLYFVTMTEYDKDLPVPVAFPPPKIKNTLGEVLSKAGLKQL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 324 RIAETEKYPHVTYFMSGGRNEEFKGERRRLIDSPKVATYDLKPEMSAYEVKDALLEELNKGDLDLIILNFANPDMVGHSG 403
Cdd:cd16010  321 RIAETEKYAHVTYFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLIEAIKSGKYDFIVVNFANPDMVGHTG 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 404 MLEPTIKAIEAVDECLGEVVDKILDMDGYAIITADHGNSDQVLTDDD-QPMTTHTTNPVPVIVTKEGV--TLRETGRLGD 480
Cdd:cd16010  401 NLEAAVKAVEAVDECLGRIVEAVLENGGTLLITADHGNAEEMIDPETgGPHTAHTTNPVPFIIVDPGLkrKLLKDGGLAD 480

                        490       500
                 ....*....|....*....|...
gi 581387295 481 LAPTLLDLLNVEQPEDMTGESLI 503
Cdd:cd16010  481 VAPTILDLLGIEKPKEMTGKSLI 503
pgm_bpd_ind TIGR01307
phosphoglycerate mutase (2,3-diphosphoglycerate-independent); This protein is about double in ...
 4-503 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: 694.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295    4 KPTALIILDGFANRESEHGNAVKLANKPNFDRYYNKYPTTQIEASGLDVGLPEGQMGNSEVGHMNIGAGRIVYQSLTRIN 83
Cdd:TIGR01307   1 KKVVLVILDGWGYRNDDDGNAIFAAKTPTMDELIAAYPYSLLDASGLDVGLPDGQMGNSEVGHLNIGAGRVVYQDLVRIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295   84 KSIEDGDFFENDVLNNAIAHVNSHDSALHIFGLLSDGGVHSHYKHLFALLELAKKQGVEKVYVHAFLDGRDVDQKSALKY 163
Cdd:TIGR01307  81 QAIKDGEFFANPALLGAIDRAKDNNGKLHLMGLVSDGGVHSHIDHLIALIELAAERGIEKVVLHAFTDGRDTAPKSAESY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  164 IEETEAKFNELGIGQFASVSGRYYAMDRDKRWEREEKAYNAIRNFDAPTYATAKEGVEASYNEGLTDEFVVPFIVENQNd 243
Cdd:TIGR01307 161 LEQLQAFLKEIGNGRIATISGRYYAMDRDQRWDRVEIAYKAITGGDGFEFSDPVAYIQDAYARDITDEFIKPTIIGNGG- 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  244 GVNDGDAVIFYNFRPDRAAQLSEIFANRAFEGFKVEQVKDLFYATFTKYNDNIDAAIVFEKVDLNNTIGEIAQNNNLTQL 323
Cdd:TIGR01307 240 ALKDGDAVIFFNFRADRAREITRALVNSDFDGFPREKNPKLDFVTMTQYDGTFPSPVAFPPQSLTNTLGEVLAKHDLTQL 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  324 RIAETEKYPHVTYFMSGGRNEEFKGERRRLIDSPKVATYDLKPEMSAYEVKDALLEELNKGDLDLIILNFANPDMVGHSG 403
Cdd:TIGR01307 320 RIAETEKYAHVTFFFNGGVEVPFAGETRTLIPSPKVATYDLQPEMSAKAVTDAVLEAIAQGKFDLIVVNFANPDMVGHTG 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  404 MLEPTIKAIEAVDECLGEVVDKILDMDGYAIITADHGNSDQVLTDDDQPMTTHTTNPVPVIVT--KEGVTLRETGRLGDL 481
Cdd:TIGR01307 400 NFEAAIKAVEALDVCLGRIVEACKKVGGTLFLTADHGNAEEMIDENGNPHTAHTTNPVPFVCVgaKNVKLIREGGVLADI 479

                         490       500
                  ....*....|....*....|..
gi 581387295  482 APTLLDLLNVEQPEDMTGESLI 503
Cdd:TIGR01307 480 APTILDLMGLEQPAEMTGKSLL 501
Metalloenzyme pfam01676
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ...
 4-492 8.37e-123

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: 365.57  E-value: 8.37e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295    4 KPTALIILDGFANRESEHGNA---VKLANKPNFDRYYNKYPTTQIEASGLDVGLPEGQMGNSEVGHMNIGAGRIVYQSLT 80
Cdd:pfam01676   1 KKVVLIVLDGWGDRPAEDLNAktpLHIAKTPNMDKLAKEYPEQLIGASGLAVGLPEGQMGGSDVGHLEIGGGRIVYQYLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295   81 RINKSIEDGDFFENDVLNNAIAHVNSHDSALHIFGLLSDGGVHSHYKHLFALLELAKKQGVEKVYVHAFLDGRDVdqksa 160
Cdd:pfam01676  81 RGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHSHIEHLLALIALAKEAGAIKVHLLGDGDDRPV----- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  161 lkyieeteakfnelgigqfasvsgrYYAMDrdkrwereekaynairnfdaptyatakegveasynegltdefvvpfiven 240
Cdd:pfam01676 156 -------------------------GYILD-------------------------------------------------- 160

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  241 qndgvNDGDAVIFYNFRPDRAAQLSEIFANRAFEGFKVEQVKDLFYATFTKYNDNIDAAIVFEKVDLNNTIGEIAQNNNL 320
Cdd:pfam01676 161 -----GDAVITINFRFDRRRARILRLFLLDPDFFDRDRVRHDALHVPTKTLYELKLPSAGAFVPEEGKNTDGEVLEGHGL 235

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  321 TQLRIAETEKYPHVTYFMSGGRNEEFKGERRRLIDSPKVATYDLKPEMSAYEVKDALLEELnKGDLDLIILNFANPDMVG 400
Cdd:pfam01676 236 KQLRIAETEKYAHVTFFWGGGREPPFPGEERYLIPSPKVATYDLQPEMSAMEITDKLLEAL-KEKYDFVFVNFANTDMVG 314

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  401 HSGMLEPTIKAIEAVDECLGEVVDKILDMDGYAIITADHGNSDQVLTDDdqpmttHTTNPVPVIVTKEGV---------T 471
Cdd:pfam01676 315 HTGDVEGKVKAIEAVDERLGELLDALEEDDGLLIITADHGNPEEMKDTD------HTREPVPILIYGKGVrpdqvlfgeK 388

                         490       500
                  ....*....|....*....|.
gi 581387295  472 LRETGRLGDLAPTLLDLLNVE 492
Cdd:pfam01676 389 FRERGGLADIAATILMLLGLK 409
 
Name Accession Description Interval E-value
PRK05434 PRK05434
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
1-504 0e+00

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


Pssm-ID: 235463  Cd Length: 507  Bit Score: 921.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295   1 MAKKPTALIILDGFANRESEHGNAVKLANKPNFDRYYNKYPTTQIEASGLDVGLPEGQMGNSEVGHMNIGAGRIVYQSLT 80
Cdd:PRK05434   2 MMKKPVVLIILDGWGYREETEGNAIALAKTPNLDRLWANYPHTLLSASGLAVGLPDGQMGNSEVGHLNIGAGRIVYQDLT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  81 RINKSIEDGDFFENDVLNNAIAHVNSHDSALHIFGLLSDGGVHSHYKHLFALLELAKKQGVEKVYVHAFLDGRDVDQKSA 160
Cdd:PRK05434  82 RINKAIEDGSFFENPALLDAIDKAKKNGGALHLMGLLSDGGVHSHIDHLFALLELAKEEGVKKVYVHAFLDGRDTPPKSA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 161 LKYIEETEAKFNELGIGQFASVSGRYYAMDRDKRWEREEKAYNAIRNFDAPTYA-TAKEGVEASYNEGLTDEFVVPFIVE 239
Cdd:PRK05434 162 LGYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVLGEGPFTAeSAVEALEASYARGETDEFVKPTVIG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 240 NQNDG-VNDGDAVIFYNFRPDRAAQLSEIFANRAFEGFKvEQVKDLFYATFTKYNDNIDAAIVFEKVDLNNTIGEIAQNN 318
Cdd:PRK05434 242 GEPVAgIEDGDAVIFFNFRADRARQITRAFTDPDFDGFD-RVPKLLNFVTMTQYDADLKVPVAFPPESLKNTLGEVLAKA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 319 NLTQLRIAETEKYPHVTYFMSGGRNEEFKGERRRLIDSPKVATYDLKPEMSAYEVKDALLEELNKGDLDLIILNFANPDM 398
Cdd:PRK05434 321 GLTQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIILNFANPDM 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 399 VGHSGMLEPTIKAIEAVDECLGEVVDKILDMDGYAIITADHGNSDQVLTDDD-QPMTTHTTNPVPVIVTKEGVTLRETGR 477
Cdd:PRK05434 401 VGHTGNLEAAVKAVEAVDECLGRVVDAVLKVGGTLLITADHGNAEQMIDPETgQPHTAHTTNPVPFILVGGKALRLEGGK 480

                        490       500
                 ....*....|....*....|....*..
gi 581387295 478 LGDLAPTLLDLLNVEQPEDMTGESLIK 504
Cdd:PRK05434 481 LADIAPTILDLLGLEQPAEMTGKSLIE 507
GpmI COG0696
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ...
 2-504 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: 919.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295   2 AKKPTALIILDGFANRESEHGNAVKLANKPNFDRYYNKYPTTQIEASGLDVGLPEGQMGNSEVGHMNIGAGRIVYQSLTR 81
Cdd:COG0696    1 RKKPVVLIILDGWGIREETEGNAIALANTPNLDRLWATYPHTLLRASGEAVGLPDGQMGNSEVGHLNIGAGRVVYQDLTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  82 INKSIEDGDFFENDVLNNAIAHVNSHDSALHIFGLLSDGGVHSHYKHLFALLELAKKQGVEKVYVHAFLDGRDVDQKSAL 161
Cdd:COG0696   81 INKAIEDGSFFENPVLLDAIDKAKENGGALHLMGLLSDGGVHSHIDHLKALLELAKEEGVKKVYVHAFLDGRDTPPKSAL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 162 KYIEETEAKFNELGIGQFASVSGRYYAMDRDKRWEREEKAYNAIRNFDAPTYATAKEGVEASYNEGLTDEFVVPFIVENQ 241
Cdd:COG0696  161 GYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVNGEGETAASAVEAIEASYARGETDEFVKPTVIVDY 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 242 ND---GVNDGDAVIFYNFRPDRAAQLSEIFANRAFEGFKVEQV-KDLFYATFTKYNDNIDAAIVFEKVDLNNTIGEIAQN 317
Cdd:COG0696  241 GKpvaTIEDGDAVIFFNFRADRARQLTRAFTDPDFDGFDRGKRpKLLYFVTMTEYDETFDVPVAFPPENLKNTLGEVLAK 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 318 NNLTQLRIAETEKYPHVTYFMSGGRNEEFKGERRRLIDSPKVATYDLKPEMSAYEVKDALLEELNKGDLDLIILNFANPD 397
Cdd:COG0696  321 AGLKQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIVLNFANPD 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 398 MVGHSGMLEPTIKAIEAVDECLGEVVDKILDMDGYAIITADHGNSDQVLTDD-DQPMTTHTTNPVPVIVT--KEGVTLRE 474
Cdd:COG0696  401 MVGHTGVLEAAIKAVEAVDECLGRVVDAVLAAGGTLLITADHGNAEQMIDPDtGGPHTAHTTNPVPFILVggDKGVKLRE 480

                        490       500       510
                 ....*....|....*....|....*....|
gi 581387295 475 TGRLGDLAPTLLDLLNVEQPEDMTGESLIK 504
Cdd:COG0696  481 DGRLADIAPTILELMGLPQPAEMTGKSLIE 510
iPGM cd16010
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ...
 4-503 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: 864.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295   4 KPTALIILDGFANRESEHGNAVKLANKPNFDRYYNKYPTTQIEASGLDVGLPEGQMGNSEVGHMNIGAGRIVYQSLTRIN 83
Cdd:cd16010    1 KPVVLIILDGWGIRPEDEGNAIALAKTPNLDRLWATYPHTLLKASGEAVGLPDGQMGNSEVGHLNIGAGRIVYQDLTRIN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  84 KSIEDGDFFENDVLNNAIAHVNSHDSALHIFGLLSDGGVHSHYKHLFALLELAKKQGVEKVYVHAFLDGRDVDQKSALKY 163
Cdd:cd16010   81 KAIEDGSFFKNEALLKAIEHAKKNNSTLHLMGLLSDGGVHSHIDHLFALLELAKKEGVKKVYVHAFTDGRDTPPKSALKY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 164 IEETEAKFNELGIGQFASVSGRYYAMDRDKRWEREEKAYNAIRNFDAPTYATAKEGVEASYNEGLTDEFVVPFIVENQND 243
Cdd:cd16010  161 LKELEEKLKELGVGKIASVSGRYYAMDRDKRWDRTEKAYDALVLGEGEKAESAEEAIEASYAKGITDEFIPPTVIGDEGG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 244 GVNDGDAVIFYNFRPDRAAQLSEIFANRAFEGFKVEQVKDLFYATFTKYNDNIDAAIVFEKVDLNNTIGEIAQNNNLTQL 323
Cdd:cd16010  241 TIKDGDAVIFFNFRADRARQITRAFTDPDFDGFDRKKPKNLYFVTMTEYDKDLPVPVAFPPPKIKNTLGEVLSKAGLKQL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 324 RIAETEKYPHVTYFMSGGRNEEFKGERRRLIDSPKVATYDLKPEMSAYEVKDALLEELNKGDLDLIILNFANPDMVGHSG 403
Cdd:cd16010  321 RIAETEKYAHVTYFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLIEAIKSGKYDFIVVNFANPDMVGHTG 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 404 MLEPTIKAIEAVDECLGEVVDKILDMDGYAIITADHGNSDQVLTDDD-QPMTTHTTNPVPVIVTKEGV--TLRETGRLGD 480
Cdd:cd16010  401 NLEAAVKAVEAVDECLGRIVEAVLENGGTLLITADHGNAEEMIDPETgGPHTAHTTNPVPFIIVDPGLkrKLLKDGGLAD 480

                        490       500
                 ....*....|....*....|...
gi 581387295 481 LAPTLLDLLNVEQPEDMTGESLI 503
Cdd:cd16010  481 VAPTILDLLGIEKPKEMTGKSLI 503
pgm_bpd_ind TIGR01307
phosphoglycerate mutase (2,3-diphosphoglycerate-independent); This protein is about double in ...
 4-503 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: 694.12  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295    4 KPTALIILDGFANRESEHGNAVKLANKPNFDRYYNKYPTTQIEASGLDVGLPEGQMGNSEVGHMNIGAGRIVYQSLTRIN 83
Cdd:TIGR01307   1 KKVVLVILDGWGYRNDDDGNAIFAAKTPTMDELIAAYPYSLLDASGLDVGLPDGQMGNSEVGHLNIGAGRVVYQDLVRIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295   84 KSIEDGDFFENDVLNNAIAHVNSHDSALHIFGLLSDGGVHSHYKHLFALLELAKKQGVEKVYVHAFLDGRDVDQKSALKY 163
Cdd:TIGR01307  81 QAIKDGEFFANPALLGAIDRAKDNNGKLHLMGLVSDGGVHSHIDHLIALIELAAERGIEKVVLHAFTDGRDTAPKSAESY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  164 IEETEAKFNELGIGQFASVSGRYYAMDRDKRWEREEKAYNAIRNFDAPTYATAKEGVEASYNEGLTDEFVVPFIVENQNd 243
Cdd:TIGR01307 161 LEQLQAFLKEIGNGRIATISGRYYAMDRDQRWDRVEIAYKAITGGDGFEFSDPVAYIQDAYARDITDEFIKPTIIGNGG- 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  244 GVNDGDAVIFYNFRPDRAAQLSEIFANRAFEGFKVEQVKDLFYATFTKYNDNIDAAIVFEKVDLNNTIGEIAQNNNLTQL 323
Cdd:TIGR01307 240 ALKDGDAVIFFNFRADRAREITRALVNSDFDGFPREKNPKLDFVTMTQYDGTFPSPVAFPPQSLTNTLGEVLAKHDLTQL 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  324 RIAETEKYPHVTYFMSGGRNEEFKGERRRLIDSPKVATYDLKPEMSAYEVKDALLEELNKGDLDLIILNFANPDMVGHSG 403
Cdd:TIGR01307 320 RIAETEKYAHVTFFFNGGVEVPFAGETRTLIPSPKVATYDLQPEMSAKAVTDAVLEAIAQGKFDLIVVNFANPDMVGHTG 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  404 MLEPTIKAIEAVDECLGEVVDKILDMDGYAIITADHGNSDQVLTDDDQPMTTHTTNPVPVIVT--KEGVTLRETGRLGDL 481
Cdd:TIGR01307 400 NFEAAIKAVEALDVCLGRIVEACKKVGGTLFLTADHGNAEEMIDENGNPHTAHTTNPVPFVCVgaKNVKLIREGGVLADI 479

                         490       500
                  ....*....|....*....|..
gi 581387295  482 APTLLDLLNVEQPEDMTGESLI 503
Cdd:TIGR01307 480 APTILDLMGLEQPAEMTGKSLL 501
Metalloenzyme pfam01676
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ...
 4-492 8.37e-123

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: 365.57  E-value: 8.37e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295    4 KPTALIILDGFANRESEHGNA---VKLANKPNFDRYYNKYPTTQIEASGLDVGLPEGQMGNSEVGHMNIGAGRIVYQSLT 80
Cdd:pfam01676   1 KKVVLIVLDGWGDRPAEDLNAktpLHIAKTPNMDKLAKEYPEQLIGASGLAVGLPEGQMGGSDVGHLEIGGGRIVYQYLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295   81 RINKSIEDGDFFENDVLNNAIAHVNSHDSALHIFGLLSDGGVHSHYKHLFALLELAKKQGVEKVYVHAFLDGRDVdqksa 160
Cdd:pfam01676  81 RGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHSHIEHLLALIALAKEAGAIKVHLLGDGDDRPV----- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  161 lkyieeteakfnelgigqfasvsgrYYAMDrdkrwereekaynairnfdaptyatakegveasynegltdefvvpfiven 240
Cdd:pfam01676 156 -------------------------GYILD-------------------------------------------------- 160

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  241 qndgvNDGDAVIFYNFRPDRAAQLSEIFANRAFEGFKVEQVKDLFYATFTKYNDNIDAAIVFEKVDLNNTIGEIAQNNNL 320
Cdd:pfam01676 161 -----GDAVITINFRFDRRRARILRLFLLDPDFFDRDRVRHDALHVPTKTLYELKLPSAGAFVPEEGKNTDGEVLEGHGL 235

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  321 TQLRIAETEKYPHVTYFMSGGRNEEFKGERRRLIDSPKVATYDLKPEMSAYEVKDALLEELnKGDLDLIILNFANPDMVG 400
Cdd:pfam01676 236 KQLRIAETEKYAHVTFFWGGGREPPFPGEERYLIPSPKVATYDLQPEMSAMEITDKLLEAL-KEKYDFVFVNFANTDMVG 314

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  401 HSGMLEPTIKAIEAVDECLGEVVDKILDMDGYAIITADHGNSDQVLTDDdqpmttHTTNPVPVIVTKEGV---------T 471
Cdd:pfam01676 315 HTGDVEGKVKAIEAVDERLGELLDALEEDDGLLIITADHGNPEEMKDTD------HTREPVPILIYGKGVrpdqvlfgeK 388

                         490       500
                  ....*....|....*....|.
gi 581387295  472 LRETGRLGDLAPTLLDLLNVE 492
Cdd:pfam01676 389 FRERGGLADIAATILMLLGLK 409
iPGM_N pfam06415
BPG-independent PGAM N-terminus (iPGM_N); This family represents the N-terminal region of the ...
 82-294 2.36e-121

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: 354.40  E-value: 2.36e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295   82 INKSIEDGDFFENDVLNNAIAHVNSHDSALHIFGLLSDGGVHSHYKHLFALLELAKKQGVEKVYVHAFLDGRDVDQKSAL 161
Cdd:pfam06415   1 INKAIEDGSFFENPALLKAIENAKANGGALHLMGLLSDGGVHSHIDHLFALLELAKEEGVKKVYVHAFLDGRDTPPKSAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  162 KYIEETEAKFNELGIGQFASVSGRYYAMDRDKRWEREEKAYNAIRNFDAPTYATAKEGVEASYNEGLTDEFVVPFIVENQ 241
Cdd:pfam06415  81 GYLEQLEAKLAELGVGKIATVSGRYYAMDRDKRWDRVEKAYDALVLGEGESAADAVEAIEASYARGETDEFVKPTVIVDD 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 581387295  242 ND---GVNDGDAVIFYNFRPDRAAQLSEIFANRAFEGFKVEQV-KDLFYATFTKYND 294
Cdd:pfam06415 161 GKpvgTIKDGDSVIFFNFRPDRAREITRAFTDPDFDGFERRKRpKDLHFVTMTQYDA 217
PLN02538 PLN02538
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
 3-497 2.82e-104

2,3-bisphosphoglycerate-independent phosphoglycerate mutase


Pssm-ID: 215295  Cd Length: 558  Bit Score: 322.78  E-value: 2.82e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295   3 KKPTALIILDGFANRESEHGNAVKLANKPNFDRYYNKYPTT--QIEASGLDVGLP-EGQMGNSEVGHMNIGAGRIVYQSL 79
Cdd:PLN02538  20 GKPLLLIVLDGWGENAPDEFNAIHVAPTPTMDSLKAGAPERwrLVKAHGTAVGLPsDDDMGNSEVGHNALGAGRIFAQGA 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  80 TRINKSIEDGDFFENDVLNNAIAHVNSHdsALHIFGLLSDGGVHSHYKHLFALLELAKKQGVEKVYVHAFLDGRDVDQKS 159
Cdd:PLN02538 100 KLVDLALASGKIFEGEGFKYIKEAFATG--TLHLIGLLSDGGVHSRLDQLQLLLKGAAERGAKRIRVHVLTDGRDVPDGS 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 160 ALKYIEETEAKFNEL---GI-GQFASVSGRYY-AMDR-DKRWEREEKAYNAIRNFDAP-TYATAKEGVEA--SYNEGLTD 230
Cdd:PLN02538 178 SVGFVETLEKDLAELrekGCdARIASGGGRMYvTMDRyENDWNVVKRGWDAHVLGEAPhKFKSALEAVKKlrEEPPPAND 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 231 EFVVPF-IVENQNDGVN---DGDAVIFYNFRPDRAAQLSEIFANRAFEGFKVEQVKDLFYATFTKYND--NIDAAIVFEK 304
Cdd:PLN02538 258 QYLPPFvIVDEDGKPVGpieDGDAVVTFNFRADRMVMIAKALEYEDFDKFDRVRVPKIRYAGMLQYDGelKLPSHYLVSP 337

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 305 VDLNNTIGEIAQNNNLTQLRIAETEKYPHVTYFMSGGRNEEF--KGERRRLIDSPKVATYDLKPEMSAYEVKDALLEELN 382
Cdd:PLN02538 338 PLIERTSGEYLVANGVRTFACSETVKFGHVTFFWNGNRSGYFneKLEEYVEIPSDNGIPFNVQPKMKALEIAEKARDALL 417

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 383 KGDLDLIILNFANPDMVGHSGMLEPTIKAIEAVDECLGEVVDKILDMDGYAIITADHGNSD---------QVLTDDD--- 450
Cdd:PLN02538 418 SGKFDQVRVNLANGDMVGHTGDLEATIVACEAVDAAVKEILDAVEQVGGIYLVTADHGNAEdmvkrdksgKPLLDKDgnp 497

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....
gi 581387295 451 QPMTTHTTNPVPVIV----TKEGVTLR---ETGRLGDLAPTLLDLLNVEQPEDM 497
Cdd:PLN02538 498 QILTSHTLAPVPVAIggpgLPPGVRFRddlPTAGLANVAATVMNLHGFEAPADY 551
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 378-489 2.67e-17

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: 81.31  E-value: 2.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 378 LEELNKGDLDLIILNFANPDMVGHS--GMLEPTIKAIEAVDECLGEVVDKIL---DMDGYAII-TADHGNSDQVLT---- 447
Cdd:cd00016  112 IDETSKEKPFVLFLHFDGPDGPGHAygPNTPEYYDAVEEIDERIGKVLDALKkagDADDTVIIvTADHGGIDKGHGgdpk 191

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 581387295 448 DDDQPMTTHTTNPVPVIVTKEGV----TLRETGRLGDLAPTLLDLL 489
Cdd:cd00016  192 ADGKADKSHTGMRVPFIAYGPGVkkggVKHELISQYDIAPTLADLL 237
PPM cd16009
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ...
 372-498 8.05e-11

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: 63.62  E-value: 8.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 372 EVKDALLEELNKGDLDLIILNFANPDMV-GHS----GMleptIKAIEAVDECLGEVVDKiLDMDGYAIITADHGNsdqvl 446
Cdd:cd16009  257 DGMEKTLEALKEDFNGLIFTNLVDFDMLyGHRrdpeGY----AEALEEFDRRLPELLAK-LKEDDLLIITADHGN----- 326

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 581387295 447 tddDQ--PMTTHTTNPVPVIVTKEGVT-----LRETgrLGDLAPTLLDLLNVEQPEDMT 498
Cdd:cd16009  327 ---DPtiGGTDHTREYVPLLVYGKGLKgvnlgTRET--FADIGATIADNFGVEPPENGT 380
PRK05362 PRK05362
phosphopentomutase; Provisional
 375-504 1.45e-10

phosphopentomutase; Provisional


Pssm-ID: 235430  Cd Length: 394  Bit Score: 62.83  E-value: 1.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 375 DALLEEL-NKGDLDLIILNFANPDMV-GH----SGMleptIKAIEAVDECLGEVVDKILDmDGYAIITADHGNsdqvltD 448
Cdd:PRK05362 266 DATIEEMkEAGDNGLVFTNLVDFDSLyGHrrdvAGY----AAALEEFDARLPELLAALKE-DDLLIITADHGN------D 334

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 581387295 449 DDQPMTTHTTNPVPVIVTKEGVT-----LRETgrLGDLAPTLLDLLNVEQPEdmTGESLIK 504
Cdd:PRK05362 335 PTWPGTDHTREYVPLLVYGPKFKggslgHRET--FADIGATIADNFGVEPME--YGKSFLD 391
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 411-502 2.39e-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: 61.41  E-value: 2.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 411 AIEAVDECLGEVVDKILDMDGYA----IITADHG---NSDQVLTDDDQPMTTHTTNpVPVIV----TKEGVTLRETGRLG 479
Cdd:cd16148  168 EVRYVDEQIGRLLDKLKELGLLEdtlvIVTSDHGeefGEHGLYWGHGSNLYDEQLH-VPLIIrwpgKEPGKRVDALVSHI 246

                         90       100
                 ....*....|....*....|...
gi 581387295 480 DLAPTLLDLLNVEQPEDMTGESL 502
Cdd:cd16148  247 DIAPTLLDLLGVEPPDYSDGRSL 269
DeoB COG1015
Phosphopentomutase [Carbohydrate transport and metabolism];
375-504 3.33e-10

Phosphopentomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440639  Cd Length: 385  Bit Score: 61.61  E-value: 3.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 375 DALLEELNKGDLDLIILNFANPDMV-GH----SGMleptIKAIEAVDECLGEVVDKILDmDGYAIITADHGNsdqvltDD 449
Cdd:COG1015  260 DKTLEAMDEAFGGLIFTNLVDFDSLyGHrrdvAGY----AKALEEFDARLPELLAALRP-DDLLIITADHGN------DP 328

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 581387295 450 DQPMTTHTTNPVPVIVT----KEGVTL--RETgrLGDLAPTLLDLLNVEQPEDmtGESLIK 504
Cdd:COG1015  329 TWPGTDHTREYVPLLVYgpglKPGGNLgtRET--FADIGATIADHFGVPPPGH--GTSFLS 385
iPGM_like cd16011
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate ...
 371-470 7.27e-10

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: 60.56  E-value: 7.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 371 YEVK-DALLEELNKGDLdlIILNFANPDMVGHSGMLEPTIKAIEAVDECLGEVVDKILDMDGYAI-ITADHgnsdqvLTd 448
Cdd:cd16011  243 YEGKaEAALEALKDYDF--VFVHVKAPDEAGHDGDPEAKVKAIERIDKAIVGPLLELLDGEDFVIvVTPDH------ST- 313

                         90       100
                 ....*....|....*....|....
gi 581387295 449 ddqPMT--THTTNPVPVIVTKEGV 470
Cdd:cd16011  314 ---PCSlkTHSGDPVPFLIYGPGV 334
Enpp cd16018
Ectonucleotide pyrophosphatase/phosphodiesterase, also called autotaxin; Ecto-nucleotide ...
 367-490 6.80e-09

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: 56.82  E-value: 6.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 367 EMSAYEVKDALLEELNKGDLDLIILNFANPDMVGHS-GMLEP-TIKAIEAVDECLGEVVDKILDMDGYA----IITADHG 440
Cdd:cd16018  138 SFPFEERVDTILEWLDLERPDLILLYFEEPDSAGHKyGPDSPeVNEALKRVDRRLGYLIEALKERGLLDdtniIVVSDHG 217

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 581387295 441 nsdqvltdddqpMT---THTTNPV-----PVIV-----TKEGVTLrETGRLGDLAPTLLDLLN 490
Cdd:cd16018  218 ------------MTdvgTHGYDNElpdmrAIFIargpaFKKGKKL-GPFRNVDIYPLMCNLLG 267
ApgM COG3635
2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type [Carbohydrate ...
 371-470 7.32e-09

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: 57.85  E-value: 7.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 371 YEVK-DALLEELNkgDLDLIILNFANPDMVGHSGMLEPTIKAIEAVDE-CLGEVVDKILDMDGYAI-ITADHgnsdqvLT 447
Cdd:COG3635  274 YAGKaEAALEALK--DYDFVYVHVEAPDEAGHDGDLEEKVKAIERIDRrVVGPLLEGLEKFEDYRIlVTPDH------PT 345

                         90       100
                 ....*....|....*....|....*
gi 581387295 448 dddqP--MTTHTTNPVPVIVTKEGV 470
Cdd:COG3635  346 ----PisLRTHSGDPVPFLIYGPGV 366
apgM TIGR00306
phosphoglycerate mutase (2,3-diphosphoglycerate-independent), archaeal form; Experimentally ...
 366-470 1.01e-08

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: 57.09  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  366 PEMSAYEVKDALLEELNkgDLDLIILNFANPDMVGHSGMLEPTIKAIEAVDECLGEVVDKILDMDGYAIITADHGNSDQV 445
Cdd:TIGR00306 270 IDTDYRGKVRALILALE--EYDFVLVHTKGPDEAGHDGDPELKVRAIEKIDSKIVGPLLALDLDETRLILTADHSTPVEV 347

                          90       100
                  ....*....|....*....|....*
gi 581387295  446 LtdddqpmtTHTTNPVPVIVTKEGV 470
Cdd:TIGR00306 348 K--------DHSADPVPIVIVGPGV 364
PRK04024 PRK04024
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
375-490 1.15e-08

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


Pssm-ID: 235203  Cd Length: 412  Bit Score: 57.23  E-value: 1.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 375 DALLEELNkgDLDLIILNFANPDMVGHSGMLEPTIKAIEAVDECLGEVVDKILDMDGYAIITADHgnSDQVLTDDdqpmt 454
Cdd:PRK04024 285 KAAVELLK--EYDFVLLNIKGTDEAGHDGDFEGKVEVIEKIDKMLGYILDNLDLDEVYIAVTGDH--STPVEVKD----- 355

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 581387295 455 tHTTNPVPVIVTKEGVTLRETGRLG---------------DLAPTLLDLLN 490
Cdd:PRK04024 356 -HSGDPVPILIYGPGVRVDDVEKFNelsaakgglgrirglDVMPILLDLMN 405
PRK12383 PRK12383
putative mutase; Provisional
 372-501 1.85e-07

putative mutase; Provisional


Pssm-ID: 237085  Cd Length: 406  Bit Score: 53.43  E-value: 1.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 372 EVKDALLEELNKGDLDLIILNFANPDMVGHSGMLEPTIKAIEAVDECLGEVVDKiLDMDGYAIITADHGNsdqvltDDDQ 451
Cdd:PRK12383 273 RVMDITLDEFNTHPTAFICTNIQETDLAGHAEDVARYAERLEVVDRNLARLLEA-MTPDDCLVVMADHGN------DPTI 345

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 581387295 452 PMTTHTTNPVPVIVTKEGVT-----LRETgrLGDLAPTLLDLLNVEQPEdmTGES 501
Cdd:PRK12383 346 GHSHHTREVVPLLVYQKGLQatqlgVRTT--LSDVGATVCEFFGAPPPQ--NGRS 396
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
 375-443 3.89e-07

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 52.06  E-value: 3.89e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 581387295 375 DALLEELNKGDLDLIILNFANPDMVGH-----SgmlEPTIKAIEAVDECLGEVVDKILDMDGYA----IITADHGNSD 443
Cdd:COG1524  172 AAALELLREGRPDLLLVYLPDLDYAGHrygpdS---PEYRAALREVDAALGRLLDALKARGLYEgtlvIVTADHGMVD 246
PRK04200 PRK04200
cofactor-independent phosphoglycerate mutase; Provisional
 371-471 1.92e-06

cofactor-independent phosphoglycerate mutase; Provisional


Pssm-ID: 179781  Cd Length: 395  Bit Score: 49.87  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 371 YEVK-DALLEELnkGDLDLIILNFANPDMVGHSGMLEPTIKAIEAVDE-CLGEVVDKILDMDGYAI-ITADHgnsdqvlt 447
Cdd:PRK04200 270 YEGKaEAALEAL--KTHDFVFVHVEAPDEAGHEGDLEAKIKAIEDIDErVVGPILEALKKYEDYRIlVLPDH-------- 339

                         90       100
                 ....*....|....*....|....*...
gi 581387295 448 dddqP----MTTHTTNPVPVIVTKEGVT 471
Cdd:PRK04200 340 ----PtpieLKTHTADPVPFLIYGEGIE 363
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
411-502 1.93e-06

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 49.88  E-value: 1.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 411 AIEAVDECLGEVVDKiLDMDGYA-----IITADHGNSdqvLTDDDQPMT--------THttnpVPVIV-----TKEGVTL 472
Cdd:COG3119  205 MIEEVDDQVGRLLDA-LEELGLAdntivVFTSDNGPS---LGEHGLRGGkgtlyeggIR----VPLIVrwpgkIKAGSVS 276

                         90       100       110
                 ....*....|....*....|....*....|
gi 581387295 473 RETGRLGDLAPTLLDLLNVEQPEDMTGESL 502
Cdd:COG3119  277 DALVSLIDLLPTLLDLAGVPIPEDLDGRSL 306
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
 411-502 9.64e-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: 9.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 411 AIEAVDECLGEVVDKiLDMDGYA-----IITADHGNsdqvltdddqPMTTHTTNP------VPVIV-----TKEGvtlRE 474
Cdd:cd16027  194 EIERLDQQVGEILDE-LEEDGLLdntivIFTSDHGM----------PFPRAKGTLydsglrVPLIVrwpgkIKPG---SV 259

                         90       100       110
                 ....*....|....*....|....*....|.
gi 581387295 475 TGRLG---DLAPTLLDLLNVEQPEDMTGESL 502
Cdd:cd16027  260 SDALVsfiDLAPTLLDLAGIEPPEYLQGRSF 290
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 412-503 2.44e-05

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


Pssm-ID: 293760 [Multi-domain]  Cd Length: 321  Bit Score: 46.38  E-value: 2.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 412 IEAVDECLGEVVDKI----LDMDGYAIITADHGnsDQV----------LTDDdqpmTTHttnpVPVIVTKEGVtlrETGR 477
Cdd:cd16037  168 VEFLDENIGRVLDALeelgLLDNTLIIYTSDHG--DMLgerglwgkstMYEE----SVR----VPMIISGPGI---PAGK 234

                         90       100       110
                 ....*....|....*....|....*....|...
gi 581387295 478 -------LGDLAPTLLDLLNVEQPEDMTGESLI 503
Cdd:cd16037  235 rvktpvsLVDLAPTILEAAGAPPPPDLDGRSLL 267
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 393-502 1.90e-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: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 43.71  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 393 FANPDMVGHSGMLEP------TIKA--------IEAVDECLGEVVDKILDM----DGYAIITADHGNS--------DQVL 446
Cdd:cd16155  165 FDNGEGTVRDEQLAPfprtpeAVRQhlaeyyamITHLDAQIGRILDALEASgeldNTIIVFTSDHGLAvgshglmgKQNL 244

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 447 TDddqpmttHTTNpVPVIVTKEGVTLRETGR----LGDLAPTLLDLLNVEQPEDMTGESL 502
Cdd:cd16155  245 YE-------HSMR-VPLIISGPGIPKGKRRDalvyLQDVFPTLCELAGIEIPESVEGKSL 296
sulfatase_like cd16156
uncharacterized sulfatase subfamily; includes Escherichia coli YidJ; Sulfatases catalyze the ...
 415-504 1.92e-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: 43.91  E-value: 1.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 415 VDECLGEVVDKILDM--DGYAIITADHGNSDQV--LTDDDQPMTTHTTNpVPVIV-----TKEGVTLRETGRLGDLAPTL 485
Cdd:cd16156  250 VDYEIGRVLDAADEIaeDAWVIYTSDHGDMLGAhkLWAKGPAVYDEITN-IPLIIrgkggEKAGTVTDTPVSHIDLAPTI 328

                         90
                 ....*....|....*....
gi 581387295 486 LDLLNVEQPEDMTGESLIK 504
Cdd:cd16156  329 LDYAGIPQPKVLEGESILA 347
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
 402-502 3.01e-04

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 43.49  E-value: 3.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 402 SGMLEPTIKAIEAVDECLGEVVDKILDMDGYA----IITADHGNSDQVLTDDDQPMTTHTtnpVP-VIVTKEGVTLRETG 476
Cdd:COG1368  413 KTTLNNYLNAVRYADQALGEFIEKLKKSGWYDntifVIYGDHGPRSPGKTDYENPLERYR---VPlLIYSPGLKKPKVID 489

                         90       100       110
                 ....*....|....*....|....*....|
gi 581387295 477 RLG---DLAPTLLDLLNVEQPED-MTGESL 502
Cdd:COG1368  490 TVGsqiDIAPTLLDLLGIDYPSYyAFGRDL 519
sulfatase_like cd16033
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 412-503 9.28e-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: 41.44  E-value: 9.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 412 IEAVDECLGEVVDKI----LDMDGYAIITADHGNS--DQVLTDDDQPMTTHTTNpVPVIV-----TKEGVTLRETGRLGD 480
Cdd:cd16033  223 ITLIDDAIGRILDALeelgLADDTLVIFTSDHGDAlgAHRLWDKGPFMYEETYR-IPLIIkwpgvIAAGQVVDEFVSLLD 301

                         90       100
                 ....*....|....*....|...
gi 581387295 481 LAPTLLDLLNVEQPEDMTGESLI 503
Cdd:cd16033  302 LAPTILDLAGVDVPPKVDGRSLL 324
PglZ pfam08665
PglZ domain; This family is a member of the Alkaline phosphatase clan.
 374-441 1.81e-03

PglZ domain; This family is a member of the Alkaline phosphatase clan.


Pssm-ID: 430139 [Multi-domain]  Cd Length: 176  Bit Score: 39.26  E-value: 1.81e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 581387295  374 KDALLEELNKGDLDLIILNFAnpDMVGHSGMLEPtiKAIEAVDECLGEV---VDKILDMDGYAII-TADHGN 441
Cdd:pfam08665 102 GDERRELVRDKEVVYIYHNKI--DALGDKQSTEQ--KSFEAVEEALVELsdlVRRLLNRLGYRVYlTADHGF 169
Phosphodiest pfam01663
Type I phosphodiesterase / nucleotide pyrophosphatase; This family consists of ...
 387-440 2.02e-03

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: 40.48  E-value: 2.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295  387 DLIILNFANPDMVGHS-GMLEPTI-KAIEAVDECLGEVVDKILDMDGYA----IITADHG 440
Cdd:pfam01663 164 DLLLVYLEEPDYAGHRyGPDSPEVeDALRRVDRAIGDLLEALDERGLFEdtnvIVVSDHG 223
ARSK cd16171
arylsulfatase family, member K ....arylsulfatase k short ask flags precursor; ARSK is a ...
 416-503 2.64e-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: 40.22  E-value: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 581387295 416 DECLGEVVDKILDMD----GYAIITADHGnsdQVLTDDDQ--PMTTH-TTNPVPVIVT----KEGVTLRETGRLGDLAPT 484
Cdd:cd16171  206 DAMLGEIISALKDTGlldkTYVFFTSDHG---ELAMEHRQfyKMSMYeGSSHVPLLIMgpgiKAGQQVSDVVSLVDIYPT 282

                         90
                 ....*....|....*....
gi 581387295 485 LLDLLNVEQPEDMTGESLI 503
Cdd:cd16171  283 MLDIAGVPQPQNLSGYSLL 301
G6S_like cd16031
unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); ...
 480-502 4.25e-03

unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS); N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficiency of N-acetylglucosamine-6-sulfatase results in the disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease.


Pssm-ID: 293755 [Multi-domain]  Cd Length: 429  Bit Score: 39.43  E-value: 4.25e-03
                         10        20
                 ....*....|....*....|...
gi 581387295 480 DLAPTLLDLLNVEQPEDMTGESL 502
Cdd:cd16031  320 DFAPTILDLAGVPIPEDMQGRSL 342
 
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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