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Conserved domains on  [gi|499656130|ref|WP_011336864|]
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phosphopentomutase [Cereibacter sphaeroides]

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];
1-395 0e+00

Phosphopentomutase [Carbohydrate transport and metabolism];


:

Pssm-ID: 440639  Cd Length: 385  Bit Score: 625.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130   1 MPRAFLIVMDSVGCGGAPDAAAFGDAGSNTLGHIAEAcaagraeegrSGPLRLPVLDALGLGRAIELAsGLTAPglgAEP 80
Cdd:COG1015    1 MKRAILIVLDSVGIGEAPDAAKFGDEGANTLGHIAEA----------VGGLNLPNLARLGLGNIAPLA-GLPPV---EEP 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130  81 SGRWGAATEVSKGKDTPSGHWELAGVPVPWDWHYFPDrcpAFPDDLTAEICRRAGTeGILGNRHASGTAVIEELGAEHVR 160
Cdd:COG1015   67 LGAYGKMAEVSAGKDTTTGHWEIAGLPVEFPFPTFPD---GFPEELIDEFEERTGR-GVLGNKPASGTEIIEELGEEHMR 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 161 TGWPICYTSADSVLQIAAHEEAFGLDRLLALCAGLAPTLH-AMRVGRVIARPFTGAPGSFARTPNRRDYAIAPPAPTLLD 239
Cdd:COG1015  143 TGKPIVYTSADSVFQIAAHEEVFPLEELYRLCEIARELLDgEYAVGRVIARPFVGEPGNFVRTANRHDYALKPPGPTLLD 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 240 IAAAAGRATHAIGKIGDIFSHRGIGQLHKGRDDAALFDRLDALADTAEEGaLTFANFVEFDSLYGHRRDVSGYARALEWF 319
Cdd:COG1015  223 RLKEAGGDVIAVGKISDIFAGRGITESVKTKGNADGMDKTLEAMDEAFGG-LIFTNLVDFDSLYGHRRDVAGYAKALEEF 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 320 DGRAGAFLARLRPGDMALFTADHGNDPTFRGTEHTRERVPVLIAG---TGEGPLGLCA-YADVAATVAAHLGLSNPGPGR 395
Cdd:COG1015  302 DARLPELLAALRPDDLLIITADHGNDPTWPGTDHTREYVPLLVYGpglKPGGNLGTREtFADIGATIADHFGVPPPGHGT 381
 
Name Accession Description Interval E-value
DeoB COG1015
Phosphopentomutase [Carbohydrate transport and metabolism];
1-395 0e+00

Phosphopentomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440639  Cd Length: 385  Bit Score: 625.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130   1 MPRAFLIVMDSVGCGGAPDAAAFGDAGSNTLGHIAEAcaagraeegrSGPLRLPVLDALGLGRAIELAsGLTAPglgAEP 80
Cdd:COG1015    1 MKRAILIVLDSVGIGEAPDAAKFGDEGANTLGHIAEA----------VGGLNLPNLARLGLGNIAPLA-GLPPV---EEP 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130  81 SGRWGAATEVSKGKDTPSGHWELAGVPVPWDWHYFPDrcpAFPDDLTAEICRRAGTeGILGNRHASGTAVIEELGAEHVR 160
Cdd:COG1015   67 LGAYGKMAEVSAGKDTTTGHWEIAGLPVEFPFPTFPD---GFPEELIDEFEERTGR-GVLGNKPASGTEIIEELGEEHMR 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 161 TGWPICYTSADSVLQIAAHEEAFGLDRLLALCAGLAPTLH-AMRVGRVIARPFTGAPGSFARTPNRRDYAIAPPAPTLLD 239
Cdd:COG1015  143 TGKPIVYTSADSVFQIAAHEEVFPLEELYRLCEIARELLDgEYAVGRVIARPFVGEPGNFVRTANRHDYALKPPGPTLLD 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 240 IAAAAGRATHAIGKIGDIFSHRGIGQLHKGRDDAALFDRLDALADTAEEGaLTFANFVEFDSLYGHRRDVSGYARALEWF 319
Cdd:COG1015  223 RLKEAGGDVIAVGKISDIFAGRGITESVKTKGNADGMDKTLEAMDEAFGG-LIFTNLVDFDSLYGHRRDVAGYAKALEEF 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 320 DGRAGAFLARLRPGDMALFTADHGNDPTFRGTEHTRERVPVLIAG---TGEGPLGLCA-YADVAATVAAHLGLSNPGPGR 395
Cdd:COG1015  302 DARLPELLAALRPDDLLIITADHGNDPTWPGTDHTREYVPLLVYGpglKPGGNLGTREtFADIGATIADHFGVPPPGHGT 381
PRK05362 PRK05362
phosphopentomutase; Provisional
 1-396 0e+00

phosphopentomutase; Provisional


Pssm-ID: 235430  Cd Length: 394  Bit Score: 610.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130   1 MPRAFLIVMDSVGCGGAPDAAAFGDAGSNTLGHIAEAcaagraeegRSGPLRLPVLDALGLGRAIELAsglTAPGLGA-- 78
Cdd:PRK05362   1 MKRVFLIVLDSVGIGAAPDAAKFGDEGADTLGHIAEA---------RKGGLKLPNLAKLGLGNIATGT---PIAGVPAna 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130  79 EPSGRWGAATEVSKGKDTPSGHWELAGVPVPWDWHYFPDrcpAFPDDLTAEICRRAGTEGILGNRHASGTAVIEELGAEH 158
Cdd:PRK05362  69 EPIGYYGKAQEVSSGKDTPTGHWEIMGVPVLFPFGYFPN---GFPQELIDEIEERAGRPGILGNKHASGTEIIDELGEEH 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 159 VRTGWPICYTSADSVLQIAAHEEAFGLDRLLALCAGLAPTLHAM--RVGRVIARPFTGAPGSFARTPNRRDYAIAPPAPT 236
Cdd:PRK05362 146 MKTGKPIVYTSADSVFQIAAHEEVFGLEELYRICEIAREILLDRpyNVGRVIARPFVGEPGNFTRTGNRHDYALKPPAPT 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 237 LLDIAAAAGRATHAIGKIGDIFSHRGIGQLHKGRDDAALFDRLDALADTAEEGALTFANFVEFDSLYGHRRDVSGYARAL 316
Cdd:PRK05362 226 VLDKLKEAGGEVIAVGKIADIFAGQGITEKVKTKSNMDGMDATIEEMKEAGDNGLVFTNLVDFDSLYGHRRDVAGYAAAL 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 317 EWFDGRAGAFLARLRPGDMALFTADHGNDPTFRGTEHTRERVPVLIAGTG--EGPLGLC-AYADVAATVAAHLGLSNPGP 393
Cdd:PRK05362 306 EEFDARLPELLAALKEDDLLIITADHGNDPTWPGTDHTREYVPLLVYGPKfkGGSLGHReTFADIGATIADNFGVEPMEY 385


                 ...
gi 499656130 394 GRA 396
Cdd:PRK05362 386 GKS 388
PPM cd16009
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ...
 3-394 2.35e-180

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: 506.22  E-value: 2.35e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130   3 RAFLIVMDSVGCGGAPDAAAFGDAGSNTLGHIAEACaagraeegrsGPLRLPVLDALGLGRAIELASGLTAPglgaEPSG 82
Cdd:cd16009    2 RVILIVLDSFGIGAMPDAAKFGDEGANTLGHIAEAV----------PGLNLPNLEKLGLGNIVGIEGGPPKE----NPIA 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130  83 RWGAATEVSKGKDTPSGHWELAGVPVPWDWHYFPDrcpAFPDDLTAEICRRAGTEGIlGNRHASGTAVIEELGAEHVRTG 162
Cdd:cd16009   68 AYGKMREASAGKDTTTGHWEIMGLKPKKPFPTFPN---GFPKELIDEFEKATGRKGL-GNKPASGTEIIKELGEEHLKTG 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 163 WPICYTSADSVLQIAAHEEAFGLDRLLALCAGLAPTLHAM-RVGRVIARPFTGAPGS-FARTPNRRDYAIAPPAPTLLDI 240
Cdd:cd16009  144 APIVYTSADSVFQIAAHEEVIPLEELYRICEIAREILDGEyKVGRVIARPFVGETGVyFKRTSNRHDYALVPPGKTVLDI 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 241 AAAAGRATHAIGKIGDIFSHRGIGQLHKGRDDAALFDRLDALADTAEEGaLTFANFVEFDSLYGHRRDVSGYARALEWFD 320
Cdd:cd16009  224 LKEAGIPVIGIGKIADIFAGRGITESIHTKSNADGMEKTLEALKEDFNG-LIFTNLVDFDMLYGHRRDPEGYAEALEEFD 302

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499656130 321 GRAGAFLARLRPGDMALFTADHGNDPTFRGTEHTRERVPVLIAGTG--EGPLGLCA-YADVAATVAAHLGLSNPGPG 394
Cdd:cd16009  303 RRLPELLAKLKEDDLLIITADHGNDPTIGGTDHTREYVPLLVYGKGlkGVNLGTREtFADIGATIADNFGVEPPENG 379
deoB TIGR01696
phosphopentomutase; This protein is involved in the purine and pyrimidine salvage pathway. It ...
 3-396 2.03e-130

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: 379.62  E-value: 2.03e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130    3 RAFLIVMDSVGCGGAPDAAAFGDAGSNTLGHIAEACAAgraeegrsgpLRLPVLDALGLGRAIELAsGLTApglGAEPSG 82
Cdd:TIGR01696   1 RVFLIVMDSVGIGEAPDAADFGDEGAHTLGHIAEACAK----------LNLPNLTKLGLGKIHEPA-GVDG---NEEPIA 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130   83 RWGAATEVSKGKDTPSGHWELAGVPVPWDWHYFPDrcpAFPDDLTAEICRRAGTEgILGNRHASGTAVIEELGAEHVRTG 162
Cdd:TIGR01696  67 YYAKAHEASSGKDTMTGHWEIMGLPILFPFKVFPN---GFPQELLQKLEERAGRK-YLGNKPASGTVILDELGEEHMKTG 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130  163 WPICYTSADSVLQIAAHEEAFGLDRLLALC--AGLAPTLHAMRVGRVIARPFTGAPGSFARTPNRRDYAIAPPAPTLLDI 240
Cdd:TIGR01696 143 KLIVYTSADSVLQIAAHEETFPLEELYEICeiARELTTDPKYNIGRIIARPFVGEPGNFQRTGNRHDYALKPFAPTVLQK 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130  241 AAAAGRATHAIGKIGDIFSHRGIGqlhKGRDDAALFDRLDALADTAEEG--ALTFANFVEFDSLYGHRRDVSGYARALEW 318
Cdd:TIGR01696 223 LKDEGHDVISIGKIADIYDGEGIT---KKVRTTSNMDGMDATIKEMKEDftGISFTNLVDFDALWGHRRDVAGYAAALEL 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130  319 FDGRAGAFLARLRPGDMALFTADHGNDPTFRGTEHTRERVPVLIAGTGEGP---LGLC-AYADVAATVAAHLGLSNPGPG 394
Cdd:TIGR01696 300 FDRRLPELFSLLREDDLLIITADHGNDPTWTGTDHTREYIPVLVYSPKVKPghsLGHReTFADIGATIADNFGTSDPEYG 379


                  ..
gi 499656130  395 RA 396
Cdd:TIGR01696 380 KS 381
Metalloenzyme pfam01676
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ...
 3-390 3.81e-37

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: 139.07  E-value: 3.81e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130    3 RAFLIVMDSVGcggapDAAAfGDAGSNTLGHIAEacaagraeegrsgplrLPVLDALglgraIElasglTAPGLGAEPSG 82
Cdd:pfam01676   2 KVVLIVLDGWG-----DRPA-EDLNAKTPLHIAK----------------TPNMDKL-----AK-----EYPEQLIGASG 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130   83 RW-GAATEVSKGKDTpsGHWELAGVPVPWDWHYFPDRCPAFP-----DDLTAEICRragteGILGNRHASGTAVIEELGA 156
Cdd:pfam01676  50 LAvGLPEGQMGGSDV--GHLEIGGGRIVYQYLGRGDLEIAGGgfflkPADLAARIN-----FATGNGHLHGLGLDSGGGV 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130  157 EHVRTGWPICYTSADSVLQIAAHEEAFGLDRLLALCAGLAPTL----HAMRVGRVIARPFTGAPGSFARTPNRRDYAIAP 232
Cdd:pfam01676 123 HSHIEHLLALIALAKEAGAIKVHLLGDGDDRPVGYILDGDAVItinfRFDRRRARILRLFLLDPDFFDRDRVRHDALHVP 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130  233 PAPTLLDIAAAAGRATHAIGKIGDIFSHRGIGQ-------------------------------------------LHKG 269
Cdd:pfam01676 203 TKTLYELKLPSAGAFVPEEGKNTDGEVLEGHGLkqlriaetekyahvtffwgggreppfpgeerylipspkvatydLQPE 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130  270 RDDAALFDRL-DALAdtaEEGALTFANFVEFDSLyGHRRDVSGYARALEWFDGRAGAFLARLRPGDMALF-TADHGNDPT 347
Cdd:pfam01676 283 MSAMEITDKLlEALK---EKYDFVFVNFANTDMV-GHTGDVEGKVKAIEAVDERLGELLDALEEDDGLLIiTADHGNPEE 358

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 499656130  348 FRGTEHTRERVPVLIAGTG------EGPLGLCA---YADVAATVAAHLGLSN 390
Cdd:pfam01676 359 MKDTDHTREPVPILIYGKGvrpdqvLFGEKFRErggLADIAATILMLLGLKK 410
 
Name Accession Description Interval E-value
DeoB COG1015
Phosphopentomutase [Carbohydrate transport and metabolism];
1-395 0e+00

Phosphopentomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440639  Cd Length: 385  Bit Score: 625.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130   1 MPRAFLIVMDSVGCGGAPDAAAFGDAGSNTLGHIAEAcaagraeegrSGPLRLPVLDALGLGRAIELAsGLTAPglgAEP 80
Cdd:COG1015    1 MKRAILIVLDSVGIGEAPDAAKFGDEGANTLGHIAEA----------VGGLNLPNLARLGLGNIAPLA-GLPPV---EEP 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130  81 SGRWGAATEVSKGKDTPSGHWELAGVPVPWDWHYFPDrcpAFPDDLTAEICRRAGTeGILGNRHASGTAVIEELGAEHVR 160
Cdd:COG1015   67 LGAYGKMAEVSAGKDTTTGHWEIAGLPVEFPFPTFPD---GFPEELIDEFEERTGR-GVLGNKPASGTEIIEELGEEHMR 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 161 TGWPICYTSADSVLQIAAHEEAFGLDRLLALCAGLAPTLH-AMRVGRVIARPFTGAPGSFARTPNRRDYAIAPPAPTLLD 239
Cdd:COG1015  143 TGKPIVYTSADSVFQIAAHEEVFPLEELYRLCEIARELLDgEYAVGRVIARPFVGEPGNFVRTANRHDYALKPPGPTLLD 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 240 IAAAAGRATHAIGKIGDIFSHRGIGQLHKGRDDAALFDRLDALADTAEEGaLTFANFVEFDSLYGHRRDVSGYARALEWF 319
Cdd:COG1015  223 RLKEAGGDVIAVGKISDIFAGRGITESVKTKGNADGMDKTLEAMDEAFGG-LIFTNLVDFDSLYGHRRDVAGYAKALEEF 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 320 DGRAGAFLARLRPGDMALFTADHGNDPTFRGTEHTRERVPVLIAG---TGEGPLGLCA-YADVAATVAAHLGLSNPGPGR 395
Cdd:COG1015  302 DARLPELLAALRPDDLLIITADHGNDPTWPGTDHTREYVPLLVYGpglKPGGNLGTREtFADIGATIADHFGVPPPGHGT 381
PRK05362 PRK05362
phosphopentomutase; Provisional
 1-396 0e+00

phosphopentomutase; Provisional


Pssm-ID: 235430  Cd Length: 394  Bit Score: 610.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130   1 MPRAFLIVMDSVGCGGAPDAAAFGDAGSNTLGHIAEAcaagraeegRSGPLRLPVLDALGLGRAIELAsglTAPGLGA-- 78
Cdd:PRK05362   1 MKRVFLIVLDSVGIGAAPDAAKFGDEGADTLGHIAEA---------RKGGLKLPNLAKLGLGNIATGT---PIAGVPAna 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130  79 EPSGRWGAATEVSKGKDTPSGHWELAGVPVPWDWHYFPDrcpAFPDDLTAEICRRAGTEGILGNRHASGTAVIEELGAEH 158
Cdd:PRK05362  69 EPIGYYGKAQEVSSGKDTPTGHWEIMGVPVLFPFGYFPN---GFPQELIDEIEERAGRPGILGNKHASGTEIIDELGEEH 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 159 VRTGWPICYTSADSVLQIAAHEEAFGLDRLLALCAGLAPTLHAM--RVGRVIARPFTGAPGSFARTPNRRDYAIAPPAPT 236
Cdd:PRK05362 146 MKTGKPIVYTSADSVFQIAAHEEVFGLEELYRICEIAREILLDRpyNVGRVIARPFVGEPGNFTRTGNRHDYALKPPAPT 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 237 LLDIAAAAGRATHAIGKIGDIFSHRGIGQLHKGRDDAALFDRLDALADTAEEGALTFANFVEFDSLYGHRRDVSGYARAL 316
Cdd:PRK05362 226 VLDKLKEAGGEVIAVGKIADIFAGQGITEKVKTKSNMDGMDATIEEMKEAGDNGLVFTNLVDFDSLYGHRRDVAGYAAAL 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 317 EWFDGRAGAFLARLRPGDMALFTADHGNDPTFRGTEHTRERVPVLIAGTG--EGPLGLC-AYADVAATVAAHLGLSNPGP 393
Cdd:PRK05362 306 EEFDARLPELLAALKEDDLLIITADHGNDPTWPGTDHTREYVPLLVYGPKfkGGSLGHReTFADIGATIADNFGVEPMEY 385


                 ...
gi 499656130 394 GRA 396
Cdd:PRK05362 386 GKS 388
PPM cd16009
Bacterial phosphopentomutase; Bacterial phosphopentomutases (PPMs) are alkaline phosphatase ...
 3-394 2.35e-180

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: 506.22  E-value: 2.35e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130   3 RAFLIVMDSVGCGGAPDAAAFGDAGSNTLGHIAEACaagraeegrsGPLRLPVLDALGLGRAIELASGLTAPglgaEPSG 82
Cdd:cd16009    2 RVILIVLDSFGIGAMPDAAKFGDEGANTLGHIAEAV----------PGLNLPNLEKLGLGNIVGIEGGPPKE----NPIA 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130  83 RWGAATEVSKGKDTPSGHWELAGVPVPWDWHYFPDrcpAFPDDLTAEICRRAGTEGIlGNRHASGTAVIEELGAEHVRTG 162
Cdd:cd16009   68 AYGKMREASAGKDTTTGHWEIMGLKPKKPFPTFPN---GFPKELIDEFEKATGRKGL-GNKPASGTEIIKELGEEHLKTG 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 163 WPICYTSADSVLQIAAHEEAFGLDRLLALCAGLAPTLHAM-RVGRVIARPFTGAPGS-FARTPNRRDYAIAPPAPTLLDI 240
Cdd:cd16009  144 APIVYTSADSVFQIAAHEEVIPLEELYRICEIAREILDGEyKVGRVIARPFVGETGVyFKRTSNRHDYALVPPGKTVLDI 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 241 AAAAGRATHAIGKIGDIFSHRGIGQLHKGRDDAALFDRLDALADTAEEGaLTFANFVEFDSLYGHRRDVSGYARALEWFD 320
Cdd:cd16009  224 LKEAGIPVIGIGKIADIFAGRGITESIHTKSNADGMEKTLEALKEDFNG-LIFTNLVDFDMLYGHRRDPEGYAEALEEFD 302

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499656130 321 GRAGAFLARLRPGDMALFTADHGNDPTFRGTEHTRERVPVLIAGTG--EGPLGLCA-YADVAATVAAHLGLSNPGPG 394
Cdd:cd16009  303 RRLPELLAKLKEDDLLIITADHGNDPTIGGTDHTREYVPLLVYGKGlkGVNLGTREtFADIGATIADNFGVEPPENG 379
deoB TIGR01696
phosphopentomutase; This protein is involved in the purine and pyrimidine salvage pathway. It ...
 3-396 2.03e-130

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: 379.62  E-value: 2.03e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130    3 RAFLIVMDSVGCGGAPDAAAFGDAGSNTLGHIAEACAAgraeegrsgpLRLPVLDALGLGRAIELAsGLTApglGAEPSG 82
Cdd:TIGR01696   1 RVFLIVMDSVGIGEAPDAADFGDEGAHTLGHIAEACAK----------LNLPNLTKLGLGKIHEPA-GVDG---NEEPIA 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130   83 RWGAATEVSKGKDTPSGHWELAGVPVPWDWHYFPDrcpAFPDDLTAEICRRAGTEgILGNRHASGTAVIEELGAEHVRTG 162
Cdd:TIGR01696  67 YYAKAHEASSGKDTMTGHWEIMGLPILFPFKVFPN---GFPQELLQKLEERAGRK-YLGNKPASGTVILDELGEEHMKTG 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130  163 WPICYTSADSVLQIAAHEEAFGLDRLLALC--AGLAPTLHAMRVGRVIARPFTGAPGSFARTPNRRDYAIAPPAPTLLDI 240
Cdd:TIGR01696 143 KLIVYTSADSVLQIAAHEETFPLEELYEICeiARELTTDPKYNIGRIIARPFVGEPGNFQRTGNRHDYALKPFAPTVLQK 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130  241 AAAAGRATHAIGKIGDIFSHRGIGqlhKGRDDAALFDRLDALADTAEEG--ALTFANFVEFDSLYGHRRDVSGYARALEW 318
Cdd:TIGR01696 223 LKDEGHDVISIGKIADIYDGEGIT---KKVRTTSNMDGMDATIKEMKEDftGISFTNLVDFDALWGHRRDVAGYAAALEL 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130  319 FDGRAGAFLARLRPGDMALFTADHGNDPTFRGTEHTRERVPVLIAGTGEGP---LGLC-AYADVAATVAAHLGLSNPGPG 394
Cdd:TIGR01696 300 FDRRLPELFSLLREDDLLIITADHGNDPTWTGTDHTREYIPVLVYSPKVKPghsLGHReTFADIGATIADNFGTSDPEYG 379


                  ..
gi 499656130  395 RA 396
Cdd:TIGR01696 380 KS 381
Metalloenzyme pfam01676
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ...
 3-390 3.81e-37

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: 139.07  E-value: 3.81e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130    3 RAFLIVMDSVGcggapDAAAfGDAGSNTLGHIAEacaagraeegrsgplrLPVLDALglgraIElasglTAPGLGAEPSG 82
Cdd:pfam01676   2 KVVLIVLDGWG-----DRPA-EDLNAKTPLHIAK----------------TPNMDKL-----AK-----EYPEQLIGASG 49

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130   83 RW-GAATEVSKGKDTpsGHWELAGVPVPWDWHYFPDRCPAFP-----DDLTAEICRragteGILGNRHASGTAVIEELGA 156
Cdd:pfam01676  50 LAvGLPEGQMGGSDV--GHLEIGGGRIVYQYLGRGDLEIAGGgfflkPADLAARIN-----FATGNGHLHGLGLDSGGGV 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130  157 EHVRTGWPICYTSADSVLQIAAHEEAFGLDRLLALCAGLAPTL----HAMRVGRVIARPFTGAPGSFARTPNRRDYAIAP 232
Cdd:pfam01676 123 HSHIEHLLALIALAKEAGAIKVHLLGDGDDRPVGYILDGDAVItinfRFDRRRARILRLFLLDPDFFDRDRVRHDALHVP 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130  233 PAPTLLDIAAAAGRATHAIGKIGDIFSHRGIGQ-------------------------------------------LHKG 269
Cdd:pfam01676 203 TKTLYELKLPSAGAFVPEEGKNTDGEVLEGHGLkqlriaetekyahvtffwgggreppfpgeerylipspkvatydLQPE 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130  270 RDDAALFDRL-DALAdtaEEGALTFANFVEFDSLyGHRRDVSGYARALEWFDGRAGAFLARLRPGDMALF-TADHGNDPT 347
Cdd:pfam01676 283 MSAMEITDKLlEALK---EKYDFVFVNFANTDMV-GHTGDVEGKVKAIEAVDERLGELLDALEEDDGLLIiTADHGNPEE 358

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 499656130  348 FRGTEHTRERVPVLIAGTG------EGPLGLCA---YADVAATVAAHLGLSN 390
Cdd:pfam01676 359 MKDTDHTREPVPILIYGKGvrpdqvLFGEKFRErggLADIAATILMLLGLKK 410
PRK12383 PRK12383
putative mutase; Provisional
 1-395 8.80e-32

putative mutase; Provisional


Pssm-ID: 237085  Cd Length: 406  Bit Score: 124.31  E-value: 8.80e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130   1 MPRAFLIVMDSVGCGGAPDAAAF--GDAGSNTLGHIAEAcaagraeegrSGPLRLPVLDALGLGRAIELASGLTAPglga 78
Cdd:PRK12383   1 MARFVVLVIDSFGVGAMKDVTLVrpQDAGANTCGHILSQ----------LPHLQLPTLEKLGLINALGYAPGDMQP---- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130  79 EPSGRWGAATEVSKGKDTPSGHWELAGV-PVPWDWHYFPDRCPAFPDDLTAEicrragteGILGNRHASGTAV------- 150
Cdd:PRK12383  67 SPSATWGVAELQHEGADTFMGHQEIMGTrPLPPLRMPFSDVIDRVEQALESA--------GYQVERRGDGLQFllvnqav 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 151 -----IE-ELGAEHVRTGwPICYTSADSVLQIAaheeafgldRLLALCAGlaptlhamrVGRVIARPFTGAP----GSFA 220
Cdd:PRK12383 139 aigdnLEaDLGQVYNVTA-NLSVISFDDALKIG---------RIVREQVQ---------VGRVIVFGGLLTDsqriLDAA 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 221 RTPNRRDYAIAPP-----------------------APTLLdiaAAAGRATHAIGKIGDIFSHRGigqlhkGRDDAALFD 277
Cdd:PRK12383 200 ESKEGRFIGINAPksgvydngyqvvhlgygvdpkvqVPQKL---YEAGVPVVLVGKVADIVNNPY------GVSWQNLVD 270

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 278 RLDALADTAEE-----GALTFANFVEFDsLYGHRRDVSGYARALEWFDGRAGAFLARLRPGDMALFTADHGNDPTFRGTE 352
Cdd:PRK12383 271 TQRVMDITLDEfnthpTAFICTNIQETD-LAGHAEDVARYAERLEVVDRNLARLLEAMTPDDCLVVMADHGNDPTIGHSH 349

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 499656130 353 HTRERVPVLIAGTGEGP--LGLCA-YADVAATVAAHLGLSNPGPGR 395
Cdd:PRK12383 350 HTREVVPLLVYQKGLQAtqLGVRTtLSDVGATVCEFFGAPPPQNGR 395
ALP_like cd00016
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
 188-384 1.87e-05

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: 45.49  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 188 LLALCAGLAPTLHAMRVgrviarpftgaPGSFARTPNRRDYAIAPPAPTLLDIaaaagrathaigkigdifshrgigqLH 267
Cdd:cd00016   54 HAALLTGAYPTLHGYTG-----------NGSADPELPSRAAGKDEDGPTIPEL-------------------------LK 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 268 KGRDDAALFDRLDAL-ADTAEEGALTFANFVEFD-SLYGHRRDVSGYARALEWFDGRAGAFLARLRPGDMA-----LFTA 340
Cdd:cd00016   98 QAGYRTGVIGLLKAIdETSKEKPFVLFLHFDGPDgPGHAYGPNTPEYYDAVEEIDERIGKVLDALKKAGDAddtviIVTA 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499656130 341 DHGNDPTFRG----------TEHTRERVPVLIAGTG-----EGPLGLCAYaDVAATVAA 384
Cdd:cd00016  178 DHGGIDKGHGgdpkadgkadKSHTGMRVPFIAYGPGvkkggVKHELISQY-DIAPTLAD 235
ApgM COG3635
2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type [Carbohydrate ...
 304-380 3.31e-05

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: 45.52  E-value: 3.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 304 GHRRDVSGYARALEWFDGRA-GAFLARLRPGDMA--LFTADHgndPTF-RGTEHTRERVPVLIAGTGEGPLGLCAYADVA 379
Cdd:COG3635  302 GHDGDLEEKVKAIERIDRRVvGPLLEGLEKFEDYriLVTPDH---PTPiSLRTHSGDPVPFLIYGPGVRPDDVTRFDERS 378


                 .
gi 499656130 380 A 380
Cdd:COG3635  379 A 379
iPGM_like cd16011
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate ...
 304-380 1.91e-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: 40.15  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499656130 304 GHRRDVSGYARALEWFDGRAGAFLARL--RPGDMALFTADHgndPTF-RGTEHTRERVPVLIAGTGEGPLGLCAYADVAA 380
Cdd:cd16011  271 GHDGDPEAKVKAIERIDKAIVGPLLELldGEDFVIVVTPDH---STPcSLKTHSGDPVPFLIYGPGVRRDGVTRFDEISA 347
GpmI COG0696
Phosphoglycerate mutase (BPG-independent), AlkP superfamily [Carbohydrate transport and ...
 336-391 2.82e-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: 39.65  E-value: 2.82e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499656130 336 ALFTADHGN-----DPTFRG--TEHTRERVPVLIAGTGEG-----PLGLcayADVAATVAAHLGLSNP 391
Cdd:COG0696  436 LLITADHGNaeqmiDPDTGGphTAHTTNPVPFILVGGDKGvklreDGRL---ADIAPTILELMGLPQP 500
PRK05434 PRK05434
2,3-bisphosphoglycerate-independent phosphoglycerate mutase;
336-391 3.30e-03

2,3-bisphosphoglycerate-independent phosphoglycerate mutase;


Pssm-ID: 235463  Cd Length: 507  Bit Score: 39.31  E-value: 3.30e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499656130 336 ALFTADHGN-----DPTFRG--TEHTRERVPVLIAGTGEGPLGLCAYADVAATVAAHLGLSNP 391
Cdd:PRK05434 435 LLITADHGNaeqmiDPETGQphTAHTTNPVPFILVGGKALRLEGGKLADIAPTILDLLGLEQP 497
iPGM cd16010
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ...
 336-391 3.48e-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: 39.32  E-value: 3.48e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499656130 336 ALFTADHGN-----DPTFRG--TEHTRERVP-VLIAGTGEGPL----GLCayaDVAATVAAHLGLSNP 391
Cdd:cd16010  430 LLITADHGNaeemiDPETGGphTAHTTNPVPfIIVDPGLKRKLlkdgGLA---DVAPTILDLLGIEKP 494
 
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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