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Conserved domains on  [gi|446038710|ref|WP_000116565|]
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MULTISPECIES: 2,3-bisphosphoglycerate-independent phosphoglycerate mutase [Enterobacteriaceae]

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK05434 PRK05434
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
2-512 0e+00

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


:

Pssm-ID: 235463  Cd Length: 507  Bit Score: 982.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710   2 SVSKKPMVLVILDGYGYREEQQDNAIFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDL 81
Cdd:PRK05434   1 MMMKKPVVLIILDGWGYREETEGNAIALAKTPNLDRLWANYPHTLLSASGLAVGLPDGQMGNSEVGHLNIGAGRIVYQDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710  82 TRLDVEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRS 161
Cdd:PRK05434  81 TRINKAIEDGSFFENPALLDAIDKAKKNGGALHLMGLLSDGGVHSHIDHLFALLELAKEEGVKKVYVHAFLDGRDTPPKS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 162 AESSLKKFEEKFAALGKGRVASIIGRYYAMDRDNRWDRVEKAYDLLTLAQGEFQADTAVAGLQAAYARDENDEFVKATVI 241
Cdd:PRK05434 161 ALGYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVLGEGPFTAESAVEALEASYARGETDEFVKPTVI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 242 raEGQPDAAMEDGDALIFMNFRADRAREITRAFVNADFDGFARkKVVNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWM 321
Cdd:PRK05434 241 --GGEPVAGIEDGDAVIFFNFRADRARQITRAFTDPDFDGFDR-VPKLLNFVTMTQYDADLKVPVAFPPESLKNTLGEVL 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 322 AKNDKTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKSGKYDTIICNYPN 401
Cdd:PRK05434 318 AKAGLTQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIILNFAN 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 402 GDMVGHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDPATGQAHTAHTNLPVPLIYVGDKNVKAv 481
Cdd:PRK05434 398 PDMVGHTGNLEAAVKAVEAVDECLGRVVDAVLKVGGTLLITADHGNAEQMIDPETGQPHTAHTTNPVPFILVGGKALRL- 476
                        490       500       510
                 ....*....|....*....|....*....|.
gi 446038710 482 AGGKLSDIAPTMLSLMGMEIPQEMTGKPLFI 512
Cdd:PRK05434 477 EGGKLADIAPTILDLLGLEQPAEMTGKSLIE 507
 
Name Accession Description Interval E-value
PRK05434 PRK05434
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
2-512 0e+00

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


Pssm-ID: 235463  Cd Length: 507  Bit Score: 982.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710   2 SVSKKPMVLVILDGYGYREEQQDNAIFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDL 81
Cdd:PRK05434   1 MMMKKPVVLIILDGWGYREETEGNAIALAKTPNLDRLWANYPHTLLSASGLAVGLPDGQMGNSEVGHLNIGAGRIVYQDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710  82 TRLDVEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRS 161
Cdd:PRK05434  81 TRINKAIEDGSFFENPALLDAIDKAKKNGGALHLMGLLSDGGVHSHIDHLFALLELAKEEGVKKVYVHAFLDGRDTPPKS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 162 AESSLKKFEEKFAALGKGRVASIIGRYYAMDRDNRWDRVEKAYDLLTLAQGEFQADTAVAGLQAAYARDENDEFVKATVI 241
Cdd:PRK05434 161 ALGYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVLGEGPFTAESAVEALEASYARGETDEFVKPTVI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 242 raEGQPDAAMEDGDALIFMNFRADRAREITRAFVNADFDGFARkKVVNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWM 321
Cdd:PRK05434 241 --GGEPVAGIEDGDAVIFFNFRADRARQITRAFTDPDFDGFDR-VPKLLNFVTMTQYDADLKVPVAFPPESLKNTLGEVL 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 322 AKNDKTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKSGKYDTIICNYPN 401
Cdd:PRK05434 318 AKAGLTQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIILNFAN 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 402 GDMVGHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDPATGQAHTAHTNLPVPLIYVGDKNVKAv 481
Cdd:PRK05434 398 PDMVGHTGNLEAAVKAVEAVDECLGRVVDAVLKVGGTLLITADHGNAEQMIDPETGQPHTAHTTNPVPFILVGGKALRL- 476
                        490       500       510
                 ....*....|....*....|....*....|.
gi 446038710 482 AGGKLSDIAPTMLSLMGMEIPQEMTGKPLFI 512
Cdd:PRK05434 477 EGGKLADIAPTILDLLGLEQPAEMTGKSLIE 507
GpmI COG0696
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ...
4-512 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: 971.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710   4 SKKPMVLVILDGYGYREEQQDNAIFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDLTR 83
Cdd:COG0696    1 RKKPVVLIILDGWGIREETEGNAIALANTPNLDRLWATYPHTLLRASGEAVGLPDGQMGNSEVGHLNIGAGRVVYQDLTR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710  84 LDVEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRSAE 163
Cdd:COG0696   81 INKAIEDGSFFENPVLLDAIDKAKENGGALHLMGLLSDGGVHSHIDHLKALLELAKEEGVKKVYVHAFLDGRDTPPKSAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 164 SSLKKFEEKFAALGKGRVASIIGRYYAMDRDNRWDRVEKAYDLLTLAQGEfQADTAVAGLQAAYARDENDEFVKATVIRA 243
Cdd:COG0696  161 GYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVNGEGE-TAASAVEAIEASYARGETDEFVKPTVIVD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 244 EGQPDAAMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKV-VNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWMA 322
Cdd:COG0696  240 YGKPVATIEDGDAVIFFNFRADRARQLTRAFTDPDFDGFDRGKRpKLLYFVTMTEYDETFDVPVAFPPENLKNTLGEVLA 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 323 KNDKTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKSGKYDTIICNYPNG 402
Cdd:COG0696  320 KAGLKQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIVLNFANP 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 403 DMVGHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDPATGQAHTAHTNLPVPLIYVG-DKNVKAV 481
Cdd:COG0696  400 DMVGHTGVLEAAIKAVEAVDECLGRVVDAVLAAGGTLLITADHGNAEQMIDPDTGGPHTAHTTNPVPFILVGgDKGVKLR 479
                        490       500       510
                 ....*....|....*....|....*....|.
gi 446038710 482 AGGKLSDIAPTMLSLMGMEIPQEMTGKPLFI 512
Cdd:COG0696  480 EDGRLADIAPTILELMGLPQPAEMTGKSLIE 510
iPGM cd16010
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ...
6-510 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: 899.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710   6 KPMVLVILDGYGYREEQQDNAIFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDLTRLD 85
Cdd:cd16010    1 KPVVLIILDGWGIRPEDEGNAIALAKTPNLDRLWATYPHTLLKASGEAVGLPDGQMGNSEVGHLNIGAGRIVYQDLTRIN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710  86 VEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRSAESS 165
Cdd:cd16010   81 KAIEDGSFFKNEALLKAIEHAKKNNSTLHLMGLLSDGGVHSHIDHLFALLELAKKEGVKKVYVHAFTDGRDTPPKSALKY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 166 LKKFEEKFAALGKGRVASIIGRYYAMDRDNRWDRVEKAYDLLTLAQGEfQADTAVAGLQAAYARDENDEFVKATVIRAEG 245
Cdd:cd16010  161 LKELEEKLKELGVGKIASVSGRYYAMDRDKRWDRTEKAYDALVLGEGE-KAESAEEAIEASYAKGITDEFIPPTVIGDEG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 246 QPdaaMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKVVNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWMAKND 325
Cdd:cd16010  240 GT---IKDGDAVIFFNFRADRARQITRAFTDPDFDGFDRKKPKNLYFVTMTEYDKDLPVPVAFPPPKIKNTLGEVLSKAG 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 326 KTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKSGKYDTIICNYPNGDMV 405
Cdd:cd16010  317 LKQLRIAETEKYAHVTYFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLIEAIKSGKYDFIVVNFANPDMV 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 406 GHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDPATGQAHTAHTNLPVPLIYVG-DKNVKAVAGG 484
Cdd:cd16010  397 GHTGNLEAAVKAVEAVDECLGRIVEAVLENGGTLLITADHGNAEEMIDPETGGPHTAHTTNPVPFIIVDpGLKRKLLKDG 476
                        490       500
                 ....*....|....*....|....*.
gi 446038710 485 KLSDIAPTMLSLMGMEIPQEMTGKPL 510
Cdd:cd16010  477 GLADVAPTILDLLGIEKPKEMTGKSL 502
pgm_bpd_ind TIGR01307
phosphoglycerate mutase (2,3-diphosphoglycerate-independent); This protein is about double in ...
6-511 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: 879.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710    6 KPMVLVILDGYGYREEQQDNAIFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDLTRLD 85
Cdd:TIGR01307   1 KKVVLVILDGWGYRNDDDGNAIFAAKTPTMDELIAAYPYSLLDASGLDVGLPDGQMGNSEVGHLNIGAGRVVYQDLVRIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710   86 VEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRSAESS 165
Cdd:TIGR01307  81 QAIKDGEFFANPALLGAIDRAKDNNGKLHLMGLVSDGGVHSHIDHLIALIELAAERGIEKVVLHAFTDGRDTAPKSAESY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710  166 LKKFEEKFAALGKGRVASIIGRYYAMDRDNRWDRVEKAYDLLTLAQGeFQADTAVAGLQAAYARDENDEFVKATVIRAEG 245
Cdd:TIGR01307 161 LEQLQAFLKEIGNGRIATISGRYYAMDRDQRWDRVEIAYKAITGGDG-FEFSDPVAYIQDAYARDITDEFIKPTIIGNGG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710  246 qpdaAMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKVVNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWMAKND 325
Cdd:TIGR01307 240 ----ALKDGDAVIFFNFRADRAREITRALVNSDFDGFPREKNPKLDFVTMTQYDGTFPSPVAFPPQSLTNTLGEVLAKHD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710  326 KTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKSGKYDTIICNYPNGDMV 405
Cdd:TIGR01307 316 LTQLRIAETEKYAHVTFFFNGGVEVPFAGETRTLIPSPKVATYDLQPEMSAKAVTDAVLEAIAQGKFDLIVVNFANPDMV 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710  406 GHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDPAtGQAHTAHTNLPVPLIYVGDKNVKAVA-GG 484
Cdd:TIGR01307 396 GHTGNFEAAIKAVEALDVCLGRIVEACKKVGGTLFLTADHGNAEEMIDEN-GNPHTAHTTNPVPFVCVGAKNVKLIReGG 474
                         490       500
                  ....*....|....*....|....*..
gi 446038710  485 KLSDIAPTMLSLMGMEIPQEMTGKPLF 511
Cdd:TIGR01307 475 VLADIAPTILDLMGLEQPAEMTGKSLL 501
Metalloenzyme pfam01676
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ...
6-501 5.16e-151

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: 437.60  E-value: 5.16e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710    6 KPMVLVILDGYGYREEQQDNA---IFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDLT 82
Cdd:pfam01676   1 KKVVLIVLDGWGDRPAEDLNAktpLHIAKTPNMDKLAKEYPEQLIGASGLAVGLPEGQMGGSDVGHLEIGGGRIVYQYLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710   83 RLDVEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPrsa 162
Cdd:pfam01676  81 RGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHSHIEHLLALIALAKEAGAIKVHLLGDGDDRPVGY--- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710  163 esslkkfeekfaalgkgrvasiigryyamdrdnrwdrvekaydlltlaqgefqadtavaglqaayardendefvkatvir 242
Cdd:pfam01676     --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710  243 aegqpdAAMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKVVNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWMA 322
Cdd:pfam01676 158 ------ILDGDAVITINFRFDRRRARILRLFLLDPDFFDRDRVRHDALHVPTKTLYELKLPSAGAFVPEEGKNTDGEVLE 231
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710  323 KNDKTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKsGKYDTIICNYPNG 402
Cdd:pfam01676 232 GHGLKQLRIAETEKYAHVTFFWGGGREPPFPGEERYLIPSPKVATYDLQPEMSAMEITDKLLEALK-EKYDFVFVNFANT 310
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710  403 DMVGHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDpatgqahTAHTNLPVPLIYVGDK------ 476
Cdd:pfam01676 311 DMVGHTGDVEGKVKAIEAVDERLGELLDALEEDDGLLIITADHGNPEEMKD-------TDHTREPVPILIYGKGvrpdqv 383
                         490       500
                  ....*....|....*....|....*..
gi 446038710  477 --NVKAVAGGKLSDIAPTMLSLMGMEI 501
Cdd:pfam01676 384 lfGEKFRERGGLADIAATILMLLGLKK 410
 
Name Accession Description Interval E-value
PRK05434 PRK05434
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
2-512 0e+00

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


Pssm-ID: 235463  Cd Length: 507  Bit Score: 982.67  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710   2 SVSKKPMVLVILDGYGYREEQQDNAIFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDL 81
Cdd:PRK05434   1 MMMKKPVVLIILDGWGYREETEGNAIALAKTPNLDRLWANYPHTLLSASGLAVGLPDGQMGNSEVGHLNIGAGRIVYQDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710  82 TRLDVEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRS 161
Cdd:PRK05434  81 TRINKAIEDGSFFENPALLDAIDKAKKNGGALHLMGLLSDGGVHSHIDHLFALLELAKEEGVKKVYVHAFLDGRDTPPKS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 162 AESSLKKFEEKFAALGKGRVASIIGRYYAMDRDNRWDRVEKAYDLLTLAQGEFQADTAVAGLQAAYARDENDEFVKATVI 241
Cdd:PRK05434 161 ALGYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVLGEGPFTAESAVEALEASYARGETDEFVKPTVI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 242 raEGQPDAAMEDGDALIFMNFRADRAREITRAFVNADFDGFARkKVVNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWM 321
Cdd:PRK05434 241 --GGEPVAGIEDGDAVIFFNFRADRARQITRAFTDPDFDGFDR-VPKLLNFVTMTQYDADLKVPVAFPPESLKNTLGEVL 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 322 AKNDKTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKSGKYDTIICNYPN 401
Cdd:PRK05434 318 AKAGLTQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIILNFAN 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 402 GDMVGHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDPATGQAHTAHTNLPVPLIYVGDKNVKAv 481
Cdd:PRK05434 398 PDMVGHTGNLEAAVKAVEAVDECLGRVVDAVLKVGGTLLITADHGNAEQMIDPETGQPHTAHTTNPVPFILVGGKALRL- 476
                        490       500       510
                 ....*....|....*....|....*....|.
gi 446038710 482 AGGKLSDIAPTMLSLMGMEIPQEMTGKPLFI 512
Cdd:PRK05434 477 EGGKLADIAPTILDLLGLEQPAEMTGKSLIE 507
GpmI COG0696
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ...
4-512 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: 971.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710   4 SKKPMVLVILDGYGYREEQQDNAIFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDLTR 83
Cdd:COG0696    1 RKKPVVLIILDGWGIREETEGNAIALANTPNLDRLWATYPHTLLRASGEAVGLPDGQMGNSEVGHLNIGAGRVVYQDLTR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710  84 LDVEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRSAE 163
Cdd:COG0696   81 INKAIEDGSFFENPVLLDAIDKAKENGGALHLMGLLSDGGVHSHIDHLKALLELAKEEGVKKVYVHAFLDGRDTPPKSAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 164 SSLKKFEEKFAALGKGRVASIIGRYYAMDRDNRWDRVEKAYDLLTLAQGEfQADTAVAGLQAAYARDENDEFVKATVIRA 243
Cdd:COG0696  161 GYLEELEAKLAELGVGRIASVSGRYYAMDRDKRWDRVEKAYDALVNGEGE-TAASAVEAIEASYARGETDEFVKPTVIVD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 244 EGQPDAAMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKV-VNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWMA 322
Cdd:COG0696  240 YGKPVATIEDGDAVIFFNFRADRARQLTRAFTDPDFDGFDRGKRpKLLYFVTMTEYDETFDVPVAFPPENLKNTLGEVLA 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 323 KNDKTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKSGKYDTIICNYPNG 402
Cdd:COG0696  320 KAGLKQLRIAETEKYAHVTFFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLVEAIESGKYDFIVLNFANP 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 403 DMVGHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDPATGQAHTAHTNLPVPLIYVG-DKNVKAV 481
Cdd:COG0696  400 DMVGHTGVLEAAIKAVEAVDECLGRVVDAVLAAGGTLLITADHGNAEQMIDPDTGGPHTAHTTNPVPFILVGgDKGVKLR 479
                        490       500       510
                 ....*....|....*....|....*....|.
gi 446038710 482 AGGKLSDIAPTMLSLMGMEIPQEMTGKPLFI 512
Cdd:COG0696  480 EDGRLADIAPTILELMGLPQPAEMTGKSLIE 510
iPGM cd16010
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ...
6-510 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: 899.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710   6 KPMVLVILDGYGYREEQQDNAIFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDLTRLD 85
Cdd:cd16010    1 KPVVLIILDGWGIRPEDEGNAIALAKTPNLDRLWATYPHTLLKASGEAVGLPDGQMGNSEVGHLNIGAGRIVYQDLTRIN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710  86 VEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRSAESS 165
Cdd:cd16010   81 KAIEDGSFFKNEALLKAIEHAKKNNSTLHLMGLLSDGGVHSHIDHLFALLELAKKEGVKKVYVHAFTDGRDTPPKSALKY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 166 LKKFEEKFAALGKGRVASIIGRYYAMDRDNRWDRVEKAYDLLTLAQGEfQADTAVAGLQAAYARDENDEFVKATVIRAEG 245
Cdd:cd16010  161 LKELEEKLKELGVGKIASVSGRYYAMDRDKRWDRTEKAYDALVLGEGE-KAESAEEAIEASYAKGITDEFIPPTVIGDEG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 246 QPdaaMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKVVNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWMAKND 325
Cdd:cd16010  240 GT---IKDGDAVIFFNFRADRARQITRAFTDPDFDGFDRKKPKNLYFVTMTEYDKDLPVPVAFPPPKIKNTLGEVLSKAG 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 326 KTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKSGKYDTIICNYPNGDMV 405
Cdd:cd16010  317 LKQLRIAETEKYAHVTYFFNGGREEPFPGEDRILIPSPKVATYDLKPEMSAYEVTDKLIEAIKSGKYDFIVVNFANPDMV 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 406 GHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDPATGQAHTAHTNLPVPLIYVG-DKNVKAVAGG 484
Cdd:cd16010  397 GHTGNLEAAVKAVEAVDECLGRIVEAVLENGGTLLITADHGNAEEMIDPETGGPHTAHTTNPVPFIIVDpGLKRKLLKDG 476
                        490       500
                 ....*....|....*....|....*.
gi 446038710 485 KLSDIAPTMLSLMGMEIPQEMTGKPL 510
Cdd:cd16010  477 GLADVAPTILDLLGIEKPKEMTGKSL 502
pgm_bpd_ind TIGR01307
phosphoglycerate mutase (2,3-diphosphoglycerate-independent); This protein is about double in ...
6-511 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: 879.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710    6 KPMVLVILDGYGYREEQQDNAIFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDLTRLD 85
Cdd:TIGR01307   1 KKVVLVILDGWGYRNDDDGNAIFAAKTPTMDELIAAYPYSLLDASGLDVGLPDGQMGNSEVGHLNIGAGRVVYQDLVRIS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710   86 VEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRSAESS 165
Cdd:TIGR01307  81 QAIKDGEFFANPALLGAIDRAKDNNGKLHLMGLVSDGGVHSHIDHLIALIELAAERGIEKVVLHAFTDGRDTAPKSAESY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710  166 LKKFEEKFAALGKGRVASIIGRYYAMDRDNRWDRVEKAYDLLTLAQGeFQADTAVAGLQAAYARDENDEFVKATVIRAEG 245
Cdd:TIGR01307 161 LEQLQAFLKEIGNGRIATISGRYYAMDRDQRWDRVEIAYKAITGGDG-FEFSDPVAYIQDAYARDITDEFIKPTIIGNGG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710  246 qpdaAMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKVVNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWMAKND 325
Cdd:TIGR01307 240 ----ALKDGDAVIFFNFRADRAREITRALVNSDFDGFPREKNPKLDFVTMTQYDGTFPSPVAFPPQSLTNTLGEVLAKHD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710  326 KTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKSGKYDTIICNYPNGDMV 405
Cdd:TIGR01307 316 LTQLRIAETEKYAHVTFFFNGGVEVPFAGETRTLIPSPKVATYDLQPEMSAKAVTDAVLEAIAQGKFDLIVVNFANPDMV 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710  406 GHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDPAtGQAHTAHTNLPVPLIYVGDKNVKAVA-GG 484
Cdd:TIGR01307 396 GHTGNFEAAIKAVEALDVCLGRIVEACKKVGGTLFLTADHGNAEEMIDEN-GNPHTAHTTNPVPFVCVGAKNVKLIReGG 474
                         490       500
                  ....*....|....*....|....*..
gi 446038710  485 KLSDIAPTMLSLMGMEIPQEMTGKPLF 511
Cdd:TIGR01307 475 VLADIAPTILDLMGLEQPAEMTGKSLL 501
Metalloenzyme pfam01676
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ...
6-501 5.16e-151

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: 437.60  E-value: 5.16e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710    6 KPMVLVILDGYGYREEQQDNA---IFSAKTPVMDALWANRPHTLIDASGLEVGLPDRQMGNSEVGHVNLGAGRIVYQDLT 82
Cdd:pfam01676   1 KKVVLIVLDGWGDRPAEDLNAktpLHIAKTPNMDKLAKEYPEQLIGASGLAVGLPEGQMGGSDVGHLEIGGGRIVYQYLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710   83 RLDVEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPrsa 162
Cdd:pfam01676  81 RGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHSHIEHLLALIALAKEAGAIKVHLLGDGDDRPVGY--- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710  163 esslkkfeekfaalgkgrvasiigryyamdrdnrwdrvekaydlltlaqgefqadtavaglqaayardendefvkatvir 242
Cdd:pfam01676     --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710  243 aegqpdAAMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKVVNVDFVMLTEYAADIKTAVAYPPASLVNTFGEWMA 322
Cdd:pfam01676 158 ------ILDGDAVITINFRFDRRRARILRLFLLDPDFFDRDRVRHDALHVPTKTLYELKLPSAGAFVPEEGKNTDGEVLE 231
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710  323 KNDKTQLRISETEKYAHVTFFFNGGVEESFKGEDRILINSPKVATYDLQPEMSSAELTEKLVAAIKsGKYDTIICNYPNG 402
Cdd:pfam01676 232 GHGLKQLRIAETEKYAHVTFFWGGGREPPFPGEERYLIPSPKVATYDLQPEMSAMEITDKLLEALK-EKYDFVFVNFANT 310
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710  403 DMVGHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDpatgqahTAHTNLPVPLIYVGDK------ 476
Cdd:pfam01676 311 DMVGHTGDVEGKVKAIEAVDERLGELLDALEEDDGLLIITADHGNPEEMKD-------TDHTREPVPILIYGKGvrpdqv 383
                         490       500
                  ....*....|....*....|....*..
gi 446038710  477 --NVKAVAGGKLSDIAPTMLSLMGMEI 501
Cdd:pfam01676 384 lfGEKFRERGGLADIAATILMLLGLKK 410
PLN02538 PLN02538
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
5-505 2.93e-128

2,3-bisphosphoglycerate-independent phosphoglycerate mutase


Pssm-ID: 215295  Cd Length: 558  Bit Score: 384.80  E-value: 2.93e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710   5 KKPMVLVILDGYGYREEQQDNAIFSAKTPVMDALWANRPHT--LIDASGLEVGLP-DRQMGNSEVGHVNLGAGRIVYQDL 81
Cdd:PLN02538  20 GKPLLLIVLDGWGENAPDEFNAIHVAPTPTMDSLKAGAPERwrLVKAHGTAVGLPsDDDMGNSEVGHNALGAGRIFAQGA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710  82 TRLDVEIKDRAFFANPVLTGAvdKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRS 161
Cdd:PLN02538 100 KLVDLALASGKIFEGEGFKYI--KEAFATGTLHLIGLLSDGGVHSRLDQLQLLLKGAAERGAKRIRVHVLTDGRDVPDGS 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 162 AESSLKKFEEKFAAL-GKG---RVASIIGRYY-AMDR-DNRWDRVEKAYD--LLTLAQGEFQ-ADTAVAGLQAAyARDEN 232
Cdd:PLN02538 178 SVGFVETLEKDLAELrEKGcdaRIASGGGRMYvTMDRyENDWNVVKRGWDahVLGEAPHKFKsALEAVKKLREE-PPPAN 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 233 DEFVKATVI-RAEGQPDAAMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKVVNVDFVMLTEYAADIKTAVAY--P 309
Cdd:PLN02538 257 DQYLPPFVIvDEDGKPVGPIEDGDAVVTFNFRADRMVMIAKALEYEDFDKFDRVRVPKIRYAGMLQYDGELKLPSHYlvS 336
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 310 PASLVNTFGEWMAKNDKTQLRISETEKYAHVTFFFNGGVEESF--KGEDRILINSPKVATYDLQPEMSSAELTEKLVAAI 387
Cdd:PLN02538 337 PPLIERTSGEYLVANGVRTFACSETVKFGHVTFFWNGNRSGYFneKLEEYVEIPSDNGIPFNVQPKMKALEIAEKARDAL 416
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 388 KSGKYDTIICNYPNGDMVGHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQM--RD----PATG---- 457
Cdd:PLN02538 417 LSGKFDQVRVNLANGDMVGHTGDLEATIVACEAVDAAVKEILDAVEQVGGIYLVTADHGNAEDMvkRDksgkPLLDkdgn 496
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446038710 458 -QAHTAHTNLPVPLIYVG---DKNVK---AVAGGKLSDIAPTMLSLMGMEIPQEM 505
Cdd:PLN02538 497 pQILTSHTLAPVPVAIGGpglPPGVRfrdDLPTAGLANVAATVMNLHGFEAPADY 551
iPGM_N pfam06415
BPG-independent PGAM N-terminus (iPGM_N); This family represents the N-terminal region of the ...
85-300 3.89e-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: 371.74  E-value: 3.89e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710   85 DVEIKDRAFFANPVLTGAVDKAKNAGKAVHIMGLLSAGGVHSHEDHIMAMVELAAERGAEKIYLHAFLDGRDTPPRSAES 164
Cdd:pfam06415   2 NKAIEDGSFFENPALLKAIENAKANGGALHLMGLLSDGGVHSHIDHLFALLELAKEEGVKKVYVHAFLDGRDTPPKSALG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710  165 SLKKFEEKFAALGKGRVASIIGRYYAMDRDNRWDRVEKAYDLLTLAQGEFqADTAVAGLQAAYARDENDEFVKATVIRAE 244
Cdd:pfam06415  82 YLEQLEAKLAELGVGKIATVSGRYYAMDRDKRWDRVEKAYDALVLGEGES-AADAVEAIEASYARGETDEFVKPTVIVDD 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446038710  245 GQPDAAMEDGDALIFMNFRADRAREITRAFVNADFDGFARKKVV-NVDFVMLTEYAA 300
Cdd:pfam06415 161 GKPVGTIKDGDSVIFFNFRPDRAREITRAFTDPDFDGFERRKRPkDLHFVTMTQYDA 217
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
390-497 2.28e-07

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: 52.04  E-value: 2.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 390 GKYDTIICNYPNGDMVGHT--GVMEAAVKAVEALDHCVEEVAKAVESVG----GQLLITADHGNAEQ---MRDPATGQAH 460
Cdd:cd00016  118 EKPFVLFLHFDGPDGPGHAygPNTPEYYDAVEEIDERIGKVLDALKKAGdaddTVIIVTADHGGIDKghgGDPKADGKAD 197
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446038710 461 TAHTNLPVPLIYVGD---KNVKAVAGGKLSDIAPTMLSLM 497
Cdd:cd00016  198 KSHTGMRVPFIAYGPgvkKGGVKHELISQYDIAPTLADLL 237
PRK12383 PRK12383
putative mutase; Provisional
371-503 5.83e-07

putative mutase; Provisional


Pssm-ID: 237085  Cd Length: 406  Bit Score: 51.89  E-value: 5.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 371 QPEMSSAELTEKLVAAIKSGKYDTIICNYPNGDMVGHTGVMEAAVKAVEALDHCVEEVAKAVESvGGQLLITADHGNaeq 450
Cdd:PRK12383 266 QNLVDTQRVMDITLDEFNTHPTAFICTNIQETDLAGHAEDVARYAERLEVVDRNLARLLEAMTP-DDCLVVMADHGN--- 341
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446038710 451 mrDPATGqaHTAHTNLPVPLIYVGdKNVKAVAGGK---LSDIAPTMLSLMGMEIPQ 503
Cdd:PRK12383 342 --DPTIG--HSHHTREVVPLLVYQ-KGLQATQLGVrttLSDVGATVCEFFGAPPPQ 392
PPM cd16009
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ...
439-506 3.04e-06

Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase superfamily members that interconvert alpha-D-ribose 5-phosphate (ribose 5-phosphate) and alpha-D-ribose 1-phosphate (ribose 1-phosphate). This reaction bridges glucose metabolism and RNA biosynthesis. PPM is a Mn(2+)-dependent enzyme and protein phosphorylation activates the enzyme.


Pssm-ID: 293733  Cd Length: 382  Bit Score: 49.37  E-value: 3.04e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446038710 439 LLITADHGNaeqmrDPATGqaHTAHTNLPVPLIYVGdKNVKAVAGGK---LSDIAPTMLSLMGMEIPQEMT 506
Cdd:cd16009  318 LIITADHGN-----DPTIG--GTDHTREYVPLLVYG-KGLKGVNLGTretFADIGATIADNFGVEPPENGT 380
sulfatase_like cd16037
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
418-511 1.60e-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: 46.77  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 418 VEALDHCVEEVAKAVESVG----GQLLITADHGnaEQMRDPATGQAHT-----AHtnlpVPLIYVGDKnvkaVAGGK--- 485
Cdd:cd16037  168 VEFLDENIGRVLDALEELGlldnTLIIYTSDHG--DMLGERGLWGKSTmyeesVR----VPMIISGPG----IPAGKrvk 237
                         90       100       110
                 ....*....|....*....|....*....|
gi 446038710 486 ----LSDIAPTMLSLMGMEIPQEMTGKPLF 511
Cdd:cd16037  238 tpvsLVDLAPTILEAAGAPPPPDLDGRSLL 267
AtaC COG1524
c-di-AMP phosphodiesterase AtaC or nucleotide pyrophosphatase, AlkP superfamily [Signal ...
375-446 3.77e-05

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


Pssm-ID: 441133 [Multi-domain]  Cd Length: 370  Bit Score: 45.89  E-value: 3.77e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446038710 375 SSAELTEKLVAAIKSGKYDTIICNYPNGDMVGH-TGVM-EAAVKAVEALDHCVEEVAKAVESVGG----QLLITADHG 446
Cdd:COG1524  166 ADRWIAAAALELLREGRPDLLLVYLPDLDYAGHrYGPDsPEYRAALREVDAALGRLLDALKARGLyegtLVIVTADHG 243
SGSH cd16027
N-sulfoglucosamine sulfohydrolase (SGSH; sulfamidase); N-sulfoglucosamine sulfohydrolase (SGSH) ...
417-511 1.42e-04

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: 44.04  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 417 AVEALDHCVEEVAKAVESVGgqLL------ITADHGNAeQMR------DPATGqahtahtnlpVPLIYVGDKNVKAvagG 484
Cdd:cd16027  194 EIERLDQQVGEILDELEEDG--LLdntiviFTSDHGMP-FPRakgtlyDSGLR----------VPLIVRWPGKIKP---G 257
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446038710 485 KLS-------DIAPTMLSLMGMEIPQEMTGKPLF 511
Cdd:cd16027  258 SVSdalvsfiDLAPTLLDLAGIEPPEYLQGRSFL 291
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
421-511 2.29e-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: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 42.92  E-value: 2.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 421 LDHCVEEVAKAVESVGgqLL------ITADHGnaEQM--RDPATGQAHTAH-TNLPVPLIYVGDKNVKAVAGGKLS---D 488
Cdd:cd16148  172 VDEQIGRLLDKLKELG--LLedtlviVTSDHG--EEFgeHGLYWGHGSNLYdEQLHVPLIIRWPGKEPGKRVDALVshiD 247
                         90       100
                 ....*....|....*....|...
gi 446038710 489 IAPTMLSLMGMEIPQEMTGKPLF 511
Cdd:cd16148  248 IAPTLLDLLGVEPPDYSDGRSLL 270
GPI_EPT_2 cd16024
GPI ethanolamine phosphate transferase 2; PIG-G; Ethanolamine phosphate transferase is ...
403-510 2.70e-04

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: 42.94  E-value: 2.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 403 DMVGHTG---VMEAAVKAVEaLDHCVEEVAKAVESVGGQ----LLITADHGnaeqMRDPAT-GQAHTAHTNlpVPLIYVG 474
Cdd:cd16024  156 DHIGHLEgpkSPLMPPKLKE-MDDVIKRIYESLEEQSSNnptlLVVCGDHG----MTDAGNhGGSSPGETS--VPLLFIS 228
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446038710 475 ----DKNVKAVAGGKLS------DIAPTMLSLMGMEIPQEMTGKPL 510
Cdd:cd16024  229 pkfsSKPSNADGELSYYetvqqvDLAPTLALLLGLPIPKNSVGVLI 274
PRK04024 PRK04024
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
381-498 3.59e-04

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


Pssm-ID: 235203  Cd Length: 412  Bit Score: 42.98  E-value: 3.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 381 EKLVAAIKsgKYDTIICNYPNGDMVGHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLITADHGNAEQMRDpatgqah 460
Cdd:PRK04024 285 KAAVELLK--EYDFVLLNIKGTDEAGHDGDFEGKVEVIEKIDKMLGYILDNLDLDEVYIAVTGDHSTPVEVKD------- 355
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446038710 461 taHTNLPVP-LIY--------VGDKNVKAVAGGKL-----SDIAPTMLSLMG 498
Cdd:PRK04024 356 --HSGDPVPiLIYgpgvrvddVEKFNELSAAKGGLgrirgLDVMPILLDLMN 405
sulfatase_like cd16034
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
417-508 9.84e-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: 293758 [Multi-domain]  Cd Length: 399  Bit Score: 41.40  E-value: 9.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 417 AVEALDHCVEEVAKAVESVGgqLL------ITADHGnaEQMrdpatGQAHTAHTNLP------VPLIYVGDKNVKAvaGG 484
Cdd:cd16034  232 MITALDDNIGRLLDALKELG--LLentivvFTSDHG--DML-----GSHGLMNKQVPyeesirVPFIIRYPGKIKA--GR 300
                         90       100       110
                 ....*....|....*....|....*....|
gi 446038710 485 KLS------DIAPTMLSLMGMEIPQEMTGK 508
Cdd:cd16034  301 VVDllintvDIMPTLLGLCGLPIPDTVEGR 330
PRK05362 PRK05362
phosphopentomutase; Provisional
375-511 1.03e-03

phosphopentomutase; Provisional


Pssm-ID: 235430  Cd Length: 394  Bit Score: 41.25  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 375 SSAELTEKLVAAIKSGKYDTII-CNYPNGDMV-GHTGVMEAAVKAVEALDHCVEEVAKAVESvGGQLLITADHGNaeqmr 452
Cdd:PRK05362 260 SNMDGMDATIEEMKEAGDNGLVfTNLVDFDSLyGHRRDVAGYAAALEEFDARLPELLAALKE-DDLLIITADHGN----- 333
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446038710 453 DPAT-GqahTAHTNLPVPLIYVGdKNVKAVAGGK---LSDIAPTMLSLMGMEIPqeMTGKPLF 511
Cdd:PRK05362 334 DPTWpG---TDHTREYVPLLVYG-PKFKGGSLGHretFADIGATIADNFGVEPM--EYGKSFL 390
iPGM_like cd16011
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate ...
379-497 1.33e-03

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: 40.92  E-value: 1.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 379 LTEKLVAAIKS-GKYDTIICNYPNGDMVGHTGVMEAAVKAVEALDHCVeeVAKAVESVGGQ---LLITADHgnaeqmRDP 454
Cdd:cd16011  243 YEGKAEAALEAlKDYDFVFVHVKAPDEAGHDGDPEAKVKAIERIDKAI--VGPLLELLDGEdfvIVVTPDH------STP 314
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446038710 455 ATGQAHTAHtnlPVPLIYVG-----DKNV----KAVAGGKL-----SDIAPTMLSLM 497
Cdd:cd16011  315 CSLKTHSGD---PVPFLIYGpgvrrDGVTrfdeISAAAGGLgrirgHELMPLLLNYA 368
AslA COG3119
Arylsulfatase A or related enzyme, AlkP superfamily [Inorganic ion transport and metabolism];
417-510 3.14e-03

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


Pssm-ID: 442353 [Multi-domain]  Cd Length: 393  Bit Score: 39.86  E-value: 3.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 417 AVEALDHCVEEVAKAVESvGGQL-----LITADHGnaEQMRDPA-TGQAHTAH---TNlpVPLIYVGDKNVKAvagGKLS 487
Cdd:COG3119  205 MIEEVDDQVGRLLDALEE-LGLAdntivVFTSDNG--PSLGEHGlRGGKGTLYeggIR--VPLIVRWPGKIKA---GSVS 276
                         90       100       110
                 ....*....|....*....|....*....|
gi 446038710 488 -------DIAPTMLSLMGMEIPQEMTGKPL 510
Cdd:COG3119  277 dalvsliDLLPTLLDLAGVPIPEDLDGRSL 306
sulfatase_like cd16155
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
418-510 3.36e-03

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


Pssm-ID: 293774 [Multi-domain]  Cd Length: 372  Bit Score: 39.86  E-value: 3.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 418 VEALDHCVEEVAKAVESVGgQL-----LITADHGnaeqmrdPATGQ----------AHTAHtnlpVPLIYVGdKNVKAva 482
Cdd:cd16155  198 ITHLDAQIGRILDALEASG-ELdntiiVFTSDHG-------LAVGShglmgkqnlyEHSMR----VPLIISG-PGIPK-- 262
                         90       100       110
                 ....*....|....*....|....*....|....
gi 446038710 483 GGK------LSDIAPTMLSLMGMEIPQEMTGKPL 510
Cdd:cd16155  263 GKRrdalvyLQDVFPTLCELAGIEIPESVEGKSL 296
DeoB COG1015
Phosphopentomutase [Carbohydrate transport and metabolism];
375-502 4.49e-03

Phosphopentomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440639  Cd Length: 385  Bit Score: 39.27  E-value: 4.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 375 SSAELTEKLVAAIKSGKYDTIICNYPNGDMV-GHTGVMEAAVKAVEALDHCVEEVAKAVESvGGQLLITADHGNaeqmrD 453
Cdd:COG1015  254 GNADGMDKTLEAMDEAFGGLIFTNLVDFDSLyGHRRDVAGYAKALEEFDARLPELLAALRP-DDLLIITADHGN-----D 327
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446038710 454 PATgqAHTAHTNLPVPLIYVGdKNVKavAGGKL------SDIAPTMLSLMGMEIP 502
Cdd:COG1015  328 PTW--PGTDHTREYVPLLVYG-PGLK--PGGNLgtretfADIGATIADHFGVPPP 377
PMH cd16028
Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase ...
418-510 6.02e-03

Phosphonate monoester hydrolase/phosphodiesterase; Phosphonate monoester hydrolase/phosphodiesterase hydrolyses phosphonate monoesters or phosphate diesters using a posttranslationally formed formylglycine as the catalytic nucleophile. PMH is the member of the alkaline phosphatase superfamily. The structure of PMH is more homologous to arylsulfatase than alkaline phosphatase. Sulfatases also use formylglycine as catalytic nucleophile.


Pssm-ID: 293752 [Multi-domain]  Cd Length: 449  Bit Score: 39.16  E-value: 6.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 418 VEALDHCVEEVAKAVESVG---GQLLI-TADHGnaEQMRDP-ATGQAHTAHTNLPVPLIyVGD--KNVKAVAGGKLS--- 487
Cdd:cd16028  244 IAEVDDHLGRLFDYLKETGqwdDTLIVfTSDHG--EQLGDHwLWGKDGFFDQAYRVPLI-VRDprREADATRGQVVDaft 320
                         90       100
                 ....*....|....*....|....*.
gi 446038710 488 ---DIAPTMLSLMGMEIPQEMTGKPL 510
Cdd:cd16028  321 esvDVMPTILDWLGGEIPHQCDGRSL 346
ALP cd16012
Alkaline Phosphatase; Alkaline phosphatases are non-specific membrane-bound ...
403-498 6.48e-03

Alkaline Phosphatase; Alkaline phosphatases are non-specific membrane-bound phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Mammalian alkaline phosphatase is divided into four isozymes depending upon the site of tissue expression. They are Intestinal ALP, Placental ALP, Germ cell ALP and tissue nonspecific alkaline phosphatase or liver/bone/kidney (L/B/K) ALP.


Pssm-ID: 293736  Cd Length: 283  Bit Score: 38.56  E-value: 6.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446038710 403 DMVGHTGVMEAAVKAVEALDHCVEEVAKAVESVGGQLLI-TADHGnaeqmrdpatgqahTAHTNLPVPLIYVGdknvkav 481
Cdd:cd16012  201 DWAGHANDAARAIEETLAFDKAVKVALDFAKKDGDTLVIvTADHE--------------TGHTGEDVPVFAYG------- 259
                         90       100
                 ....*....|....*....|....
gi 446038710 482 AGGKL-------SDIAPTMLSLMG 498
Cdd:cd16012  260 PGAELfggvydnTDIFHKIAEALG 283
 
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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