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Conserved domains on  [gi|489523593|ref|WP_003428374|]
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phosphopentomutase [Clostridioides difficile]

Protein Classification

phosphopentomutase( domain architecture ID 18492003)

phosphopentomutase catalyzes the interconversion of alpha-D-ribose 5-phosphate and alpha-D-ribose 1-phosphate

CATH:  3.30.70.1250
Gene Ontology:  GO:0008973|GO:0030145|GO:0006015
PubMed:  21193409
SCOP:  4003235

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DeoB COG1015
Phosphopentomutase [Carbohydrate transport and metabolism];
1-387 0e+00

Phosphopentomutase [Carbohydrate transport and metabolism];


:

Pssm-ID: 440639  Cd Length: 385  Bit Score: 731.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593   1 MSRVIWIVIDSVGIGALPDAENFGDsKDVSTLGNIFKKHPDIQIPNMRKLGIGNIDGVDFFESIKEPIGCFGKCKEMSQG 80
Cdd:COG1015    1 MKRAILIVLDSVGIGEAPDAAKFGD-EGANTLGHIAEAVGGLNLPNLARLGLGNIAPLAGLPPVEEPLGAYGKMAEVSAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593  81 KDTTTGHWEMTGIIVDKPFKTFEDGFSKEIIEEFEKKTGRKVVGNKPASGTVIIDEYGEHQIETGDVIVYTSADSVFQIA 160
Cdd:COG1015   80 KDTTTGHWEIAGLPVEFPFPTFPDGFPEELIDEFEERTGRGVLGNKPASGTEIIEELGEEHMRTGKPIVYTSADSVFQIA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593 161 ANEEVIPLEELYNMCKIAREIMMGDNAVARVIARPFIGKKkGEFVRTSNRRDYSLDPFEPTVLDNIKESGLDVLAVGKIE 240
Cdd:COG1015  160 AHEEVFPLEELYRLCEIARELLDGEYAVGRVIARPFVGEP-GNFVRTANRHDYALKPPGPTLLDRLKEAGGDVIAVGKIS 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593 241 DIFNGKGITDAIHTKSNMDGVDETLNYMKQDNKGLIYSNLVDFDSKYGHRRDPEGYKKALEEFDSRLPEIMANMRKDDIL 320
Cdd:COG1015  239 DIFAGRGITESVKTKGNADGMDKTLEAMDEAFGGLIFTNLVDFDSLYGHRRDVAGYAKALEEFDARLPELLAALRPDDLL 318

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489523593 321 IINADHGNDPTYKGTDHTREYIPVMIYGNKIKKGFNLGVKDTFADIGATVADILNVKLPKHGSSFKE 387
Cdd:COG1015  319 IITADHGNDPTWPGTDHTREYVPLLVYGPGLKPGGNLGTRETFADIGATIADHFGVPPPGHGTSFLS 385
 
Name Accession Description Interval E-value
DeoB COG1015
Phosphopentomutase [Carbohydrate transport and metabolism];
1-387 0e+00

Phosphopentomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440639  Cd Length: 385  Bit Score: 731.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593   1 MSRVIWIVIDSVGIGALPDAENFGDsKDVSTLGNIFKKHPDIQIPNMRKLGIGNIDGVDFFESIKEPIGCFGKCKEMSQG 80
Cdd:COG1015    1 MKRAILIVLDSVGIGEAPDAAKFGD-EGANTLGHIAEAVGGLNLPNLARLGLGNIAPLAGLPPVEEPLGAYGKMAEVSAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593  81 KDTTTGHWEMTGIIVDKPFKTFEDGFSKEIIEEFEKKTGRKVVGNKPASGTVIIDEYGEHQIETGDVIVYTSADSVFQIA 160
Cdd:COG1015   80 KDTTTGHWEIAGLPVEFPFPTFPDGFPEELIDEFEERTGRGVLGNKPASGTEIIEELGEEHMRTGKPIVYTSADSVFQIA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593 161 ANEEVIPLEELYNMCKIAREIMMGDNAVARVIARPFIGKKkGEFVRTSNRRDYSLDPFEPTVLDNIKESGLDVLAVGKIE 240
Cdd:COG1015  160 AHEEVFPLEELYRLCEIARELLDGEYAVGRVIARPFVGEP-GNFVRTANRHDYALKPPGPTLLDRLKEAGGDVIAVGKIS 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593 241 DIFNGKGITDAIHTKSNMDGVDETLNYMKQDNKGLIYSNLVDFDSKYGHRRDPEGYKKALEEFDSRLPEIMANMRKDDIL 320
Cdd:COG1015  239 DIFAGRGITESVKTKGNADGMDKTLEAMDEAFGGLIFTNLVDFDSLYGHRRDVAGYAKALEEFDARLPELLAALRPDDLL 318

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489523593 321 IINADHGNDPTYKGTDHTREYIPVMIYGNKIKKGFNLGVKDTFADIGATVADILNVKLPKHGSSFKE 387
Cdd:COG1015  319 IITADHGNDPTWPGTDHTREYVPLLVYGPGLKPGGNLGTRETFADIGATIADHFGVPPPGHGTSFLS 385
PRK05362 PRK05362
phosphopentomutase; Provisional
 1-389 0e+00

phosphopentomutase; Provisional


Pssm-ID: 235430  Cd Length: 394  Bit Score: 674.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593   1 MSRVIWIVIDSVGIGALPDAENFGDsKDVSTLGNI--FKKHPdIQIPNMRKLGIGNIDGVDFFESI---KEPIGCFGKCK 75
Cdd:PRK05362   1 MKRVFLIVLDSVGIGAAPDAAKFGD-EGADTLGHIaeARKGG-LKLPNLAKLGLGNIATGTPIAGVpanAEPIGYYGKAQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593  76 EMSQGKDTTTGHWEMTGIIVDKPFKTFEDGFSKEIIEEFEKKTGR-KVVGNKPASGTVIIDEYGEHQIETGDVIVYTSAD 154
Cdd:PRK05362  79 EVSSGKDTPTGHWEIMGVPVLFPFGYFPNGFPQELIDEIEERAGRpGILGNKHASGTEIIDELGEEHMKTGKPIVYTSAD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593 155 SVFQIAANEEVIPLEELYNMCKIAREIMMGD-NAVARVIARPFIGKKkGEFVRTSNRRDYSLDPFEPTVLDNIKESGLDV 233
Cdd:PRK05362 159 SVFQIAAHEEVFGLEELYRICEIAREILLDRpYNVGRVIARPFVGEP-GNFTRTGNRHDYALKPPAPTVLDKLKEAGGEV 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593 234 LAVGKIEDIFNGKGITDAIHTKSNMDGVDETLNYMKQ-DNKGLIYSNLVDFDSKYGHRRDPEGYKKALEEFDSRLPEIMA 312
Cdd:PRK05362 238 IAVGKIADIFAGQGITEKVKTKSNMDGMDATIEEMKEaGDNGLVFTNLVDFDSLYGHRRDVAGYAAALEEFDARLPELLA 317

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489523593 313 NMRKDDILIINADHGNDPTYKGTDHTREYIPVMIYGNKIKKGfNLGVKDTFADIGATVADILNVKLPKHGSSFKEDL 389
Cdd:PRK05362 318 ALKEDDLLIITADHGNDPTWPGTDHTREYVPLLVYGPKFKGG-SLGHRETFADIGATIADNFGVEPMEYGKSFLDEL 393
PPM cd16009
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ...
 3-385 0e+00

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: 660.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593   3 RVIWIVIDSVGIGALPDAENFGDsKDVSTLGNIFKKHPDIQIPNMRKLGIGNIDGVDFFESIKEPIGCFGKCKEMSQGKD 82
Cdd:cd16009    2 RVILIVLDSFGIGAMPDAAKFGD-EGANTLGHIAEAVPGLNLPNLEKLGLGNIVGIEGGPPKENPIAAYGKMREASAGKD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593  83 TTTGHWEMTGIIVDKPFKTFEDGFSKEIIEEFEKKTGRKVVGNKPASGTVIIDEYGEHQIETGDVIVYTSADSVFQIAAN 162
Cdd:cd16009   81 TTTGHWEIMGLKPKKPFPTFPNGFPKELIDEFEKATGRKGLGNKPASGTEIIKELGEEHLKTGAPIVYTSADSVFQIAAH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593 163 EEVIPLEELYNMCKIAREIMMGDNAVARVIARPFIGKKKGEFVRTSNRRDYSLDPFEPTVLDNIKESGLDVLAVGKIEDI 242
Cdd:cd16009  161 EEVIPLEELYRICEIAREILDGEYKVGRVIARPFVGETGVYFKRTSNRHDYALVPPGKTVLDILKEAGIPVIGIGKIADI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593 243 FNGKGITDAIHTKSNMDGVDETLNYMKQDNKGLIYSNLVDFDSKYGHRRDPEGYKKALEEFDSRLPEIMANMRKDDILII 322
Cdd:cd16009  241 FAGRGITESIHTKSNADGMEKTLEALKEDFNGLIFTNLVDFDMLYGHRRDPEGYAEALEEFDRRLPELLAKLKEDDLLII 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489523593 323 NADHGNDPTYKGTDHTREYIPVMIYGNKIkKGFNLGVKDTFADIGATVADILNVKLPKHGSSF 385
Cdd:cd16009  321 TADHGNDPTIGGTDHTREYVPLLVYGKGL-KGVNLGTRETFADIGATIADNFGVEPPENGTSF 382
deoB TIGR01696
phosphopentomutase; This protein is involved in the purine and pyrimidine salvage pathway. It ...
 3-384 2.30e-180

phosphopentomutase; This protein is involved in the purine and pyrimidine salvage pathway. It catalyzes the conversion of D-ribose 1-phosphate to D-ribose 5-phosphate and the conversion of 2-deoxy-D-ribose 1-phosphate to 2-deoxy-D-ribose 5-phosphate. The seed members of this protein are characterized deoB proteins from E.Coli(SP:P07651) and Bacillus (SP:P46353). This model matches pfam01676 for Metalloenzyme superfamily. [Purines, pyrimidines, nucleosides, and nucleotides, Other]


Pssm-ID: 162494  Cd Length: 381  Bit Score: 506.35  E-value: 2.30e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593    3 RVIWIVIDSVGIGALPDAENFGDsKDVSTLGNIFKKHPDIQIPNMRKLGIGNIDGVDFFESIKEPIGCFGKCKEMSQGKD 82
Cdd:TIGR01696   1 RVFLIVMDSVGIGEAPDAADFGD-EGAHTLGHIAEACAKLNLPNLTKLGLGKIHEPAGVDGNEEPIAYYAKAHEASSGKD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593   83 TTTGHWEMTGIIVDKPFKTFEDGFSKEIIEEFEKKTGRKVVGNKPASGTVIIDEYGEHQIETGDVIVYTSADSVFQIAAN 162
Cdd:TIGR01696  80 TMTGHWEIMGLPILFPFKVFPNGFPQELLQKLEERAGRKYLGNKPASGTVILDELGEEHMKTGKLIVYTSADSVLQIAAH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593  163 EEVIPLEELYNMCKIAREIMM-GDNAVARVIARPFIGKKkGEFVRTSNRRDYSLDPFEPTVLDNIKESGLDVLAVGKIED 241
Cdd:TIGR01696 160 EETFPLEELYEICEIARELTTdPKYNIGRIIARPFVGEP-GNFQRTGNRHDYALKPFAPTVLQKLKDEGHDVISIGKIAD 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593  242 IFNGKGITDAIHTKSNMDGVDETLNYMKQDNKGLIYSNLVDFDSKYGHRRDPEGYKKALEEFDSRLPEIMANMRKDDILI 321
Cdd:TIGR01696 239 IYDGEGITKKVRTTSNMDGMDATIKEMKEDFTGISFTNLVDFDALWGHRRDVAGYAAALELFDRRLPELFSLLREDDLLI 318

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489523593  322 INADHGNDPTYKGTDHTREYIPVMIYGNKIKKGFNLGVKDTFADIGATVADILNVKLPKHGSS 384
Cdd:TIGR01696 319 ITADHGNDPTWTGTDHTREYIPVLVYSPKVKPGHSLGHRETFADIGATIADNFGTSDPEYGKS 381
Metalloenzyme pfam01676
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ...
 2-378 2.03e-54

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: 184.91  E-value: 2.03e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593    2 SRVIWIVIDSVGIGALPDAenfgdskDVSTLGNIFKKhpdiqiPNMRKLgIGNIDGVdffeSIKEPIGCFGKCKEMSQGK 81
Cdd:pfam01676   1 KKVVLIVLDGWGDRPAEDL-------NAKTPLHIAKT------PNMDKL-AKEYPEQ----LIGASGLAVGLPEGQMGGS 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593   82 DTttGHWEMTGIIVDKPFKTFEDGFSKEIIEEFEKKTGRKVVGNKPASGTVIIDEYGEHQIETGDVIVYTSADSVFQIAA 161
Cdd:pfam01676  63 DV--GHLEIGGGRIVYQYLGRGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHSHIEHLLALIALAKEAG 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593  162 NEEVIPLEEL----YNMCKIAR-EIMMGDNAVARVIARPFI-GKKKGEFVRTSNRRDYSLDPFEPTVLDNIKESGLDVLA 235
Cdd:pfam01676 141 AIKVHLLGDGddrpVGYILDGDaVITINFRFDRRRARILRLfLLDPDFFDRDRVRHDALHVPTKTLYELKLPSAGAFVPE 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593  236 VGKIEDI-------------------------FNG-----------------KGIT-DAIHTKSNMDGVDETLNYMKqDN 272
Cdd:pfam01676 221 EGKNTDGevleghglkqlriaetekyahvtffWGGgreppfpgeerylipspKVATyDLQPEMSAMEITDKLLEALK-EK 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593  273 KGLIYSNLVDFDSkYGHRRDPEGYKKALEEFDSRLPEIMANMRKDD-ILIINADHGNDPTYKGTDHTREYIPVMIYGNKI 351
Cdd:pfam01676 300 YDFVFVNFANTDM-VGHTGDVEGKVKAIEAVDERLGELLDALEEDDgLLIITADHGNPEEMKDTDHTREPVPILIYGKGV 378

                         410       420       430
                  ....*....|....*....|....*....|..
gi 489523593  352 KKGFNLGV-----KDTFADIGATVADILNVKL 378
Cdd:pfam01676 379 RPDQVLFGekfreRGGLADIAATILMLLGLKK 410
 
Name Accession Description Interval E-value
DeoB COG1015
Phosphopentomutase [Carbohydrate transport and metabolism];
1-387 0e+00

Phosphopentomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440639  Cd Length: 385  Bit Score: 731.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593   1 MSRVIWIVIDSVGIGALPDAENFGDsKDVSTLGNIFKKHPDIQIPNMRKLGIGNIDGVDFFESIKEPIGCFGKCKEMSQG 80
Cdd:COG1015    1 MKRAILIVLDSVGIGEAPDAAKFGD-EGANTLGHIAEAVGGLNLPNLARLGLGNIAPLAGLPPVEEPLGAYGKMAEVSAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593  81 KDTTTGHWEMTGIIVDKPFKTFEDGFSKEIIEEFEKKTGRKVVGNKPASGTVIIDEYGEHQIETGDVIVYTSADSVFQIA 160
Cdd:COG1015   80 KDTTTGHWEIAGLPVEFPFPTFPDGFPEELIDEFEERTGRGVLGNKPASGTEIIEELGEEHMRTGKPIVYTSADSVFQIA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593 161 ANEEVIPLEELYNMCKIAREIMMGDNAVARVIARPFIGKKkGEFVRTSNRRDYSLDPFEPTVLDNIKESGLDVLAVGKIE 240
Cdd:COG1015  160 AHEEVFPLEELYRLCEIARELLDGEYAVGRVIARPFVGEP-GNFVRTANRHDYALKPPGPTLLDRLKEAGGDVIAVGKIS 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593 241 DIFNGKGITDAIHTKSNMDGVDETLNYMKQDNKGLIYSNLVDFDSKYGHRRDPEGYKKALEEFDSRLPEIMANMRKDDIL 320
Cdd:COG1015  239 DIFAGRGITESVKTKGNADGMDKTLEAMDEAFGGLIFTNLVDFDSLYGHRRDVAGYAKALEEFDARLPELLAALRPDDLL 318

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489523593 321 IINADHGNDPTYKGTDHTREYIPVMIYGNKIKKGFNLGVKDTFADIGATVADILNVKLPKHGSSFKE 387
Cdd:COG1015  319 IITADHGNDPTWPGTDHTREYVPLLVYGPGLKPGGNLGTRETFADIGATIADHFGVPPPGHGTSFLS 385
PRK05362 PRK05362
phosphopentomutase; Provisional
 1-389 0e+00

phosphopentomutase; Provisional


Pssm-ID: 235430  Cd Length: 394  Bit Score: 674.14  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593   1 MSRVIWIVIDSVGIGALPDAENFGDsKDVSTLGNI--FKKHPdIQIPNMRKLGIGNIDGVDFFESI---KEPIGCFGKCK 75
Cdd:PRK05362   1 MKRVFLIVLDSVGIGAAPDAAKFGD-EGADTLGHIaeARKGG-LKLPNLAKLGLGNIATGTPIAGVpanAEPIGYYGKAQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593  76 EMSQGKDTTTGHWEMTGIIVDKPFKTFEDGFSKEIIEEFEKKTGR-KVVGNKPASGTVIIDEYGEHQIETGDVIVYTSAD 154
Cdd:PRK05362  79 EVSSGKDTPTGHWEIMGVPVLFPFGYFPNGFPQELIDEIEERAGRpGILGNKHASGTEIIDELGEEHMKTGKPIVYTSAD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593 155 SVFQIAANEEVIPLEELYNMCKIAREIMMGD-NAVARVIARPFIGKKkGEFVRTSNRRDYSLDPFEPTVLDNIKESGLDV 233
Cdd:PRK05362 159 SVFQIAAHEEVFGLEELYRICEIAREILLDRpYNVGRVIARPFVGEP-GNFTRTGNRHDYALKPPAPTVLDKLKEAGGEV 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593 234 LAVGKIEDIFNGKGITDAIHTKSNMDGVDETLNYMKQ-DNKGLIYSNLVDFDSKYGHRRDPEGYKKALEEFDSRLPEIMA 312
Cdd:PRK05362 238 IAVGKIADIFAGQGITEKVKTKSNMDGMDATIEEMKEaGDNGLVFTNLVDFDSLYGHRRDVAGYAAALEEFDARLPELLA 317

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489523593 313 NMRKDDILIINADHGNDPTYKGTDHTREYIPVMIYGNKIKKGfNLGVKDTFADIGATVADILNVKLPKHGSSFKEDL 389
Cdd:PRK05362 318 ALKEDDLLIITADHGNDPTWPGTDHTREYVPLLVYGPKFKGG-SLGHRETFADIGATIADNFGVEPMEYGKSFLDEL 393
PPM cd16009
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ...
 3-385 0e+00

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: 660.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593   3 RVIWIVIDSVGIGALPDAENFGDsKDVSTLGNIFKKHPDIQIPNMRKLGIGNIDGVDFFESIKEPIGCFGKCKEMSQGKD 82
Cdd:cd16009    2 RVILIVLDSFGIGAMPDAAKFGD-EGANTLGHIAEAVPGLNLPNLEKLGLGNIVGIEGGPPKENPIAAYGKMREASAGKD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593  83 TTTGHWEMTGIIVDKPFKTFEDGFSKEIIEEFEKKTGRKVVGNKPASGTVIIDEYGEHQIETGDVIVYTSADSVFQIAAN 162
Cdd:cd16009   81 TTTGHWEIMGLKPKKPFPTFPNGFPKELIDEFEKATGRKGLGNKPASGTEIIKELGEEHLKTGAPIVYTSADSVFQIAAH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593 163 EEVIPLEELYNMCKIAREIMMGDNAVARVIARPFIGKKKGEFVRTSNRRDYSLDPFEPTVLDNIKESGLDVLAVGKIEDI 242
Cdd:cd16009  161 EEVIPLEELYRICEIAREILDGEYKVGRVIARPFVGETGVYFKRTSNRHDYALVPPGKTVLDILKEAGIPVIGIGKIADI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593 243 FNGKGITDAIHTKSNMDGVDETLNYMKQDNKGLIYSNLVDFDSKYGHRRDPEGYKKALEEFDSRLPEIMANMRKDDILII 322
Cdd:cd16009  241 FAGRGITESIHTKSNADGMEKTLEALKEDFNGLIFTNLVDFDMLYGHRRDPEGYAEALEEFDRRLPELLAKLKEDDLLII 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489523593 323 NADHGNDPTYKGTDHTREYIPVMIYGNKIkKGFNLGVKDTFADIGATVADILNVKLPKHGSSF 385
Cdd:cd16009  321 TADHGNDPTIGGTDHTREYVPLLVYGKGL-KGVNLGTRETFADIGATIADNFGVEPPENGTSF 382
deoB TIGR01696
phosphopentomutase; This protein is involved in the purine and pyrimidine salvage pathway. It ...
 3-384 2.30e-180

phosphopentomutase; This protein is involved in the purine and pyrimidine salvage pathway. It catalyzes the conversion of D-ribose 1-phosphate to D-ribose 5-phosphate and the conversion of 2-deoxy-D-ribose 1-phosphate to 2-deoxy-D-ribose 5-phosphate. The seed members of this protein are characterized deoB proteins from E.Coli(SP:P07651) and Bacillus (SP:P46353). This model matches pfam01676 for Metalloenzyme superfamily. [Purines, pyrimidines, nucleosides, and nucleotides, Other]


Pssm-ID: 162494  Cd Length: 381  Bit Score: 506.35  E-value: 2.30e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593    3 RVIWIVIDSVGIGALPDAENFGDsKDVSTLGNIFKKHPDIQIPNMRKLGIGNIDGVDFFESIKEPIGCFGKCKEMSQGKD 82
Cdd:TIGR01696   1 RVFLIVMDSVGIGEAPDAADFGD-EGAHTLGHIAEACAKLNLPNLTKLGLGKIHEPAGVDGNEEPIAYYAKAHEASSGKD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593   83 TTTGHWEMTGIIVDKPFKTFEDGFSKEIIEEFEKKTGRKVVGNKPASGTVIIDEYGEHQIETGDVIVYTSADSVFQIAAN 162
Cdd:TIGR01696  80 TMTGHWEIMGLPILFPFKVFPNGFPQELLQKLEERAGRKYLGNKPASGTVILDELGEEHMKTGKLIVYTSADSVLQIAAH 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593  163 EEVIPLEELYNMCKIAREIMM-GDNAVARVIARPFIGKKkGEFVRTSNRRDYSLDPFEPTVLDNIKESGLDVLAVGKIED 241
Cdd:TIGR01696 160 EETFPLEELYEICEIARELTTdPKYNIGRIIARPFVGEP-GNFQRTGNRHDYALKPFAPTVLQKLKDEGHDVISIGKIAD 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593  242 IFNGKGITDAIHTKSNMDGVDETLNYMKQDNKGLIYSNLVDFDSKYGHRRDPEGYKKALEEFDSRLPEIMANMRKDDILI 321
Cdd:TIGR01696 239 IYDGEGITKKVRTTSNMDGMDATIKEMKEDFTGISFTNLVDFDALWGHRRDVAGYAAALELFDRRLPELFSLLREDDLLI 318

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489523593  322 INADHGNDPTYKGTDHTREYIPVMIYGNKIKKGFNLGVKDTFADIGATVADILNVKLPKHGSS 384
Cdd:TIGR01696 319 ITADHGNDPTWTGTDHTREYIPVLVYSPKVKPGHSLGHRETFADIGATIADNFGTSDPEYGKS 381
PRK12383 PRK12383
putative mutase; Provisional
 1-385 1.18e-65

putative mutase; Provisional


Pssm-ID: 237085  Cd Length: 406  Bit Score: 214.06  E-value: 1.18e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593   1 MSRVIWIVIDSVGIGALPDAENFgDSKDV--STLGNIFKKHPDIQIPNMRKLGIGNIDGVDFFESIKEPIGCFGKCKEMS 78
Cdd:PRK12383   1 MARFVVLVIDSFGVGAMKDVTLV-RPQDAgaNTCGHILSQLPHLQLPTLEKLGLINALGYAPGDMQPSPSATWGVAELQH 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593  79 QGKDTTTGHWEMTGiivDKPFKTFEDGFSkEIIEEFE---KKTGRKVvgNKPASGT--VIIDeygeHQIETGDVIvytSA 153
Cdd:PRK12383  80 EGADTFMGHQEIMG---TRPLPPLRMPFS-DVIDRVEqalESAGYQV--ERRGDGLqfLLVN----QAVAIGDNL---EA 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593 154 D--SVFQIAANEEVIPLEELYNMCKIAREImmgdNAVARVIArpFIGK-------------KKGEFVRTSNRRD------ 212
Cdd:PRK12383 147 DlgQVYNVTANLSVISFDDALKIGRIVREQ----VQVGRVIV--FGGLltdsqrildaaesKEGRFIGINAPKSgvydng 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593 213 -------YSLDPFE--PTVLdniKESGLDVLAVGKIEDIFN---GKGITDAIHTKSNMDgvdETLNYMKQDNKGLIYSNL 280
Cdd:PRK12383 221 yqvvhlgYGVDPKVqvPQKL---YEAGVPVVLVGKVADIVNnpyGVSWQNLVDTQRVMD---ITLDEFNTHPTAFICTNI 294

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593 281 VDFDSKyGHRRDPEGYKKALEEFDSRLPEIMANMRKDDILIINADHGNDPTYKGTDHTREYIPVMIYGNKIkKGFNLGVK 360
Cdd:PRK12383 295 QETDLA-GHAEDVARYAERLEVVDRNLARLLEAMTPDDCLVVMADHGNDPTIGHSHHTREVVPLLVYQKGL-QATQLGVR 372

                        410       420
                 ....*....|....*....|....*
gi 489523593 361 DTFADIGATVADILNVKLPKHGSSF 385
Cdd:PRK12383 373 TTLSDVGATVCEFFGAPPPQNGRSF 397
Metalloenzyme pfam01676
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ...
 2-378 2.03e-54

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: 184.91  E-value: 2.03e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593    2 SRVIWIVIDSVGIGALPDAenfgdskDVSTLGNIFKKhpdiqiPNMRKLgIGNIDGVdffeSIKEPIGCFGKCKEMSQGK 81
Cdd:pfam01676   1 KKVVLIVLDGWGDRPAEDL-------NAKTPLHIAKT------PNMDKL-AKEYPEQ----LIGASGLAVGLPEGQMGGS 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593   82 DTttGHWEMTGIIVDKPFKTFEDGFSKEIIEEFEKKTGRKVVGNKPASGTVIIDEYGEHQIETGDVIVYTSADSVFQIAA 161
Cdd:pfam01676  63 DV--GHLEIGGGRIVYQYLGRGDLEIAGGGFFLKPADLAARINFATGNGHLHGLGLDSGGGVHSHIEHLLALIALAKEAG 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593  162 NEEVIPLEEL----YNMCKIAR-EIMMGDNAVARVIARPFI-GKKKGEFVRTSNRRDYSLDPFEPTVLDNIKESGLDVLA 235
Cdd:pfam01676 141 AIKVHLLGDGddrpVGYILDGDaVITINFRFDRRRARILRLfLLDPDFFDRDRVRHDALHVPTKTLYELKLPSAGAFVPE 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593  236 VGKIEDI-------------------------FNG-----------------KGIT-DAIHTKSNMDGVDETLNYMKqDN 272
Cdd:pfam01676 221 EGKNTDGevleghglkqlriaetekyahvtffWGGgreppfpgeerylipspKVATyDLQPEMSAMEITDKLLEALK-EK 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593  273 KGLIYSNLVDFDSkYGHRRDPEGYKKALEEFDSRLPEIMANMRKDD-ILIINADHGNDPTYKGTDHTREYIPVMIYGNKI 351
Cdd:pfam01676 300 YDFVFVNFANTDM-VGHTGDVEGKVKAIEAVDERLGELLDALEEDDgLLIITADHGNPEEMKDTDHTREPVPILIYGKGV 378

                         410       420       430
                  ....*....|....*....|....*....|..
gi 489523593  352 KKGFNLGV-----KDTFADIGATVADILNVKL 378
Cdd:pfam01676 379 RPDQVLFGekfreRGGLADIAATILMLLGLKK 410
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 202-374 2.47e-14

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: 72.07  E-value: 2.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593 202 GEFVRTSNRRDYSLDPFEPTVLDNIKESGLDVLAVGkiedifngkgitdaihtksnmdgVDETLNYMKQDNKGLIYSNLV 281
Cdd:cd00016   72 GSADPELPSRAAGKDEDGPTIPELLKQAGYRTGVIG-----------------------LLKAIDETSKEKPFVLFLHFD 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593 282 DFD-SKYGHRRDPEGYKKALEEFDSRLPEIM-----ANMRKDDILIINADHGNDP----------TYKGTDHTREYIPVM 345
Cdd:cd00016  129 GPDgPGHAYGPNTPEYYDAVEEIDERIGKVLdalkkAGDADDTVIIVTADHGGIDkghggdpkadGKADKSHTGMRVPFI 208

                        170       180
                 ....*....|....*....|....*....
gi 489523593 346 IYGNKIKKGFNLGVKDTFADIGATVADIL 374
Cdd:cd00016  209 AYGPGVKKGGVKHELISQYDIAPTLADLL 237
iPGM_like cd16011
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate ...
 288-354 1.70e-08

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: 55.94  E-value: 1.70e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489523593 288 GHRRDPEGYKKALEEFDSRLPEIMAN--MRKDDILIINADHgndPT---YKgtDHTREYIPVMIYGNKIKKG 354
Cdd:cd16011  271 GHDGDPEAKVKAIERIDKAIVGPLLEllDGEDFVIVVTPDH---STpcsLK--THSGDPVPFLIYGPGVRRD 337
ApgM COG3635
2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type [Carbohydrate ...
 288-353 9.78e-07

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: 50.53  E-value: 9.78e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593 288 GHRRDPEGYKKALEEFDSR-LPEIMANMRKDD--ILIINADHgndPT-YKGTDHTREYIPVMIYGNKIKK 353
Cdd:COG3635  302 GHDGDLEEKVKAIERIDRRvVGPLLEGLEKFEdyRILVTPDH---PTpISLRTHSGDPVPFLIYGPGVRP 368
apgM TIGR00306
phosphoglycerate mutase (2,3-diphosphoglycerate-independent), archaeal form; Experimentally ...
 288-356 4.56e-05

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: 45.15  E-value: 4.56e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489523593  288 GHRRDPEGYKKALEEFDSRLPEIMANMRKDDI-LIINADHgndPT-YKGTDHTREYIPVMIYGNKIK----KGFN 356
Cdd:TIGR00306 302 GHDGDPELKVRAIEKIDSKIVGPLLALDLDETrLILTADH---STpVEVKDHSADPVPIVIVGPGVRvdevKSFN 373
PRK04135 PRK04135
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
284-354 6.42e-05

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


Pssm-ID: 179745 [Multi-domain]  Cd Length: 395  Bit Score: 44.53  E-value: 6.42e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489523593 284 DSkYGHRRDPEGYKKALEEFDSRLPEIMAnmRKDDILIINADHGNDPTYKGtdHTREYIPVMIYGNKIKKG 354
Cdd:PRK04135 291 DS-YGEDGNFEEKVKVIEEVDALLPEILA--LKPDVLVITGDHSTPAVLKG--HSWHPVPLLLYSKYCRPD 356
PRK05434 PRK05434
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
297-384 2.00e-04

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


Pssm-ID: 235463  Cd Length: 507  Bit Score: 43.17  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593 297 KKALEEFDSRLPEIMANMRKDD-ILIINADHGN-----DPTYKG--TDHTREYIPVMIYGNKIKKGFNlGvkdTFADIGA 368
Cdd:PRK05434 411 VKAVEAVDECLGRVVDAVLKVGgTLLITADHGNaeqmiDPETGQphTAHTTNPVPFILVGGKALRLEG-G---KLADIAP 486

                         90
                 ....*....|....*...
gi 489523593 369 TVADILNVKLPK--HGSS 384
Cdd:PRK05434 487 TILDLLGLEQPAemTGKS 504
PRK04024 PRK04024
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
287-351 2.99e-04

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


Pssm-ID: 235203  Cd Length: 412  Bit Score: 42.59  E-value: 2.99e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489523593 287 YGHRRDPEGYKKALEEFDSRLPEIMANMRKDDILI-INADHGNDPTYKgtDHTREYIPVMIYGNKI 351
Cdd:PRK04024 307 AGHDGDFEGKVEVIEKIDKMLGYILDNLDLDEVYIaVTGDHSTPVEVK--DHSGDPVPILIYGPGV 370
MdoB COG1368
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ...
 298-390 7.04e-04

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


Pssm-ID: 440979 [Multi-domain]  Cd Length: 576  Bit Score: 41.56  E-value: 7.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593 298 KALEEFdsrlpeiMANMRKDD-----ILIINADHG---NDPTYKGTDHTREYIPVMIYGNKIKKGfnlGVKDTFA---DI 366
Cdd:COG1368  428 QALGEF-------IEKLKKSGwydntIFVIYGDHGprsPGKTDYENPLERYRVPLLIYSPGLKKP---KVIDTVGsqiDI 497

                         90       100
                 ....*....|....*....|....
gi 489523593 367 GATVADILNVKLPkHGSSFKEDLF 390
Cdd:COG1368  498 APTLLDLLGIDYP-SYYAFGRDLL 520
iPGM cd16010
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ...
 297-380 1.00e-03

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: 41.25  E-value: 1.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593 297 KKALEEFDSRLPEIMANMRKDD-ILIINADHGN-----DPTYKG--TDHTREYIPVMIYGNKIKKgfNLGVKDTFADIGA 368
Cdd:cd16010  406 VKAVEAVDECLGRIVEAVLENGgTLLITADHGNaeemiDPETGGphTAHTTNPVPFIIVDPGLKR--KLLKDGGLADVAP 483

                         90
                 ....*....|..
gi 489523593 369 TVADILNVKLPK 380
Cdd:cd16010  484 TILDLLGIEKPK 495
GpmI COG0696
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ...
 298-380 1.22e-03

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: 40.81  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593 298 KALEEFDSRLPEIMANMRKDD-ILIINADHGN-----DPTYKG--TDHTREYIPVMIYGNkiKKGFNLGVKDTFADIGAT 369
Cdd:COG0696  413 KAVEAVDECLGRVVDAVLAAGgTLLITADHGNaeqmiDPDTGGphTAHTTNPVPFILVGG--DKGVKLREDGRLADIAPT 490

                         90
                 ....*....|.
gi 489523593 370 VADILNVKLPK 380
Cdd:COG0696  491 ILELMGLPQPA 501
sulfatase_like cd16148
uncharacterized sulfatase subfamily; Sulfatases catalyze the hydrolysis of sulfate esters from ...
 293-385 4.20e-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: 293767 [Multi-domain]  Cd Length: 271  Bit Score: 38.68  E-value: 4.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489523593 293 PEGYKKALEEFDSRLPEIMA-----NMRKDDILIINADHG------------NDPTYKGTDHtreyIPVMIYGNKIKKGf 355
Cdd:cd16148  162 PYLYDAEVRYVDEQIGRLLDklkelGLLEDTLVIVTSDHGeefgehglywghGSNLYDEQLH----VPLIIRWPGKEPG- 236

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 489523593 356 nlGVKDTF---ADIGATVADILNVKLPK--HGSSF 385
Cdd:cd16148  237 --KRVDALvshIDIAPTLLDLLGVEPPDysDGRSL 269
 
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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