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Conserved domains on  [gi|7661568|ref|NP_056414|]
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phosphoacetylglucosamine mutase isoform 2 [Homo sapiens]

Protein Classification

phosphoacetylglucosamine mutase( domain architecture ID 10122986)

phosphoacetylglucosamine mutase (PAGM) catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, a sugar nucleotide critical to multiple glycosylation pathways including protein N- and O-glycosylation

EC:  5.4.2.3
Gene Ontology:  GO:0004610

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PGM3 cd03086
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ...
 22-527 0e+00

PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 (N-acetylglucosamine-phosphate mutase), is an essential enzyme found in eukaryotes that reversibly catalyzes the conversion of GlcNAc-6-phosphate into GlcNAc-1-phosphate as part of the UDP-N-acetylglucosamine (UDP-GlcNAc) biosynthetic pathway. UDP-GlcNAc is an essential metabolite that serves as the biosynthetic precursor of many glycoproteins and mucopolysaccharides. AGM1 is a member of the alpha-D-phosphohexomutase superfamily, which catalyzes the intramolecular phosphoryl transfer of sugar substrates. The alpha-D-phosphohexomutases have four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


:

Pssm-ID: 100088  Cd Length: 513  Bit Score: 892.33  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   22 QYGTAGFRTKAEHLDHVMFRMGLLAVLRSKQTKS-TIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLANAEEQ 100
Cdd:cd03086   1 SYGTAGFRTKAELLDSVVFRVGILAALRSKKLGGkTIGVMITASHNPVEDNGVKIVDPDGEMLEESWEPYATQLANASDD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  101 DMQRVLIDI--SEKEAVNLQQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNTGGRYGKA 178
Cdd:cd03086  81 ELLVLVLMLisVKELNIDLSVPANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYLVRAANTEGAYGEP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  179 TIEGYYQKLSKAFVELTKQASCSGDEYRSLKVDCANGIGALKLREMEHYFSQGLSVQLFNDGSKG--KLNHLCGADFVKS 256
Cdd:cd03086 161 TEEGYYEKLSKAFNELYNLLQDGGDEPEKLVVDCANGVGALKLKELLKRLKKGLSVKIINDGEEGpeLLNDGCGADYVKT 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  257 HQKPPQGMEIK-SNERCCSFDGDADRIVYYYHDADGHFHLIDGDKIATLISSFLKELL--VEIGESLNIGVVQTAYANGS 333
Cdd:cd03086 241 KQKPPRGFELKpPGVRCCSFDGDADRLVYFYPDSSNKFHLLDGDKIATLFAKFIKELLkkAGEELKLTIGVVQTAYANGA 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  334 STRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFSTAVEMKIKqSAEQLEDKKRKAAKMLENIIDLFN 413
Cdd:cd03086 321 STKYLEDVLKVPVVCTPTGVKHLHHAAEEFDIGVYFEANGHGTVLFSESALAKIE-ENSSLSDEQEKAAKTLLAFSRLIN 399

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  414 QAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQVADRRVISTTDAERQAVTPPGLQEAINDLVKKYKLSRA 493
Cdd:cd03086 400 QTVGDAISDMLAVELILAALGWSPQDWDNLYTDLPNRQLKVKVPDRSVIKTTDAERRLVEPKGLQDKIDAIVAKYNNGRA 479

                       490       500       510
                ....*....|....*....|....*....|....
gi 7661568  494 FVRPSGTEDVVRVYAEADSQESADHLAHEVSLAV 527
Cdd:cd03086 480 FVRPSGTEDVVRVYAEAATQEEADELANEVAELV 513
 
Name Accession Description Interval E-value
PGM3 cd03086
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ...
 22-527 0e+00

PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 (N-acetylglucosamine-phosphate mutase), is an essential enzyme found in eukaryotes that reversibly catalyzes the conversion of GlcNAc-6-phosphate into GlcNAc-1-phosphate as part of the UDP-N-acetylglucosamine (UDP-GlcNAc) biosynthetic pathway. UDP-GlcNAc is an essential metabolite that serves as the biosynthetic precursor of many glycoproteins and mucopolysaccharides. AGM1 is a member of the alpha-D-phosphohexomutase superfamily, which catalyzes the intramolecular phosphoryl transfer of sugar substrates. The alpha-D-phosphohexomutases have four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100088  Cd Length: 513  Bit Score: 892.33  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   22 QYGTAGFRTKAEHLDHVMFRMGLLAVLRSKQTKS-TIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLANAEEQ 100
Cdd:cd03086   1 SYGTAGFRTKAELLDSVVFRVGILAALRSKKLGGkTIGVMITASHNPVEDNGVKIVDPDGEMLEESWEPYATQLANASDD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  101 DMQRVLIDI--SEKEAVNLQQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNTGGRYGKA 178
Cdd:cd03086  81 ELLVLVLMLisVKELNIDLSVPANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYLVRAANTEGAYGEP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  179 TIEGYYQKLSKAFVELTKQASCSGDEYRSLKVDCANGIGALKLREMEHYFSQGLSVQLFNDGSKG--KLNHLCGADFVKS 256
Cdd:cd03086 161 TEEGYYEKLSKAFNELYNLLQDGGDEPEKLVVDCANGVGALKLKELLKRLKKGLSVKIINDGEEGpeLLNDGCGADYVKT 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  257 HQKPPQGMEIK-SNERCCSFDGDADRIVYYYHDADGHFHLIDGDKIATLISSFLKELL--VEIGESLNIGVVQTAYANGS 333
Cdd:cd03086 241 KQKPPRGFELKpPGVRCCSFDGDADRLVYFYPDSSNKFHLLDGDKIATLFAKFIKELLkkAGEELKLTIGVVQTAYANGA 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  334 STRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFSTAVEMKIKqSAEQLEDKKRKAAKMLENIIDLFN 413
Cdd:cd03086 321 STKYLEDVLKVPVVCTPTGVKHLHHAAEEFDIGVYFEANGHGTVLFSESALAKIE-ENSSLSDEQEKAAKTLLAFSRLIN 399

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  414 QAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQVADRRVISTTDAERQAVTPPGLQEAINDLVKKYKLSRA 493
Cdd:cd03086 400 QTVGDAISDMLAVELILAALGWSPQDWDNLYTDLPNRQLKVKVPDRSVIKTTDAERRLVEPKGLQDKIDAIVAKYNNGRA 479

                       490       500       510
                ....*....|....*....|....*....|....
gi 7661568  494 FVRPSGTEDVVRVYAEADSQESADHLAHEVSLAV 527
Cdd:cd03086 480 FVRPSGTEDVVRVYAEAATQEEADELANEVAELV 513
PLN02895 PLN02895
phosphoacetylglucosamine mutase
 1-538 0e+00

phosphoacetylglucosamine mutase


Pssm-ID: 215485  Cd Length: 562  Bit Score: 677.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568     1 MDLGAITKYSALHAKPNGLILQYGTAGFRTKAEHLDHVMFRMGLLAVLRSKQTKSTIGVMVTASHNPEEDNGVKLVDPLG 80
Cdd:PLN02895   4 IQRASLLAASSRFPPPQGVRFSYGTAGFRTDASLLESTVFRVGILAALRSLKTGAATGLMITASHNPVSDNGVKIVDPSG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568    81 EMLAPSWEEHATCLANAE-EQDMQRVLIDISEKEAVNL---QQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGL 156
Cdd:PLN02895  84 GMLPQAWEPFADALANAPdPDALVQLIREFVKKENIPAvggNPPAEVLLGRDTRPSGPALLAAALKGVRAIGARAVDMGI 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   157 LTTPQLHYMVYCRNTGGrygKATIEGYYQKLSKAF---VELTKQASCSGDEYRSLKVDCANGIGALKLREMEHYFSqGLS 233
Cdd:PLN02895 164 LTTPQLHWMVRAANKGM---KATESDYFEQLSSSFralLDLIPNGSGDDRADDKLVVDGANGVGAEKLETLKKALG-GLD 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   234 VQLFNDG--SKGKLNHLCGADFVKSHQKPPQGMEIK-SNERCCSFDGDADRIVYYYHDADG-HFHLIDGDKIATLISSFL 309
Cdd:PLN02895 240 LEVRNSGkeGEGVLNEGVGADFVQKEKVPPTGFASKdVGLRCASLDGDADRLVYFYVSSAGsKIDLLDGDKIASLFALFI 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   310 KELLVEIGES---------LNIGVVQTAYANGSSTRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFS 380
Cdd:PLN02895 320 KEQLRILNGNgnekpeellVRLGVVQTAYANGASTAYLKQVLGLEVVCTPTGVKYLHEAAAEFDIGVYFEANGHGTVLFS 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   381 TAVEMKIKQSAEQLEDKKR-----KAAKMLENIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQ 455
Cdd:PLN02895 400 ERFLDWLEAAAAELSSKAKgseahKAARRLLAVSRLINQAVGDALSGLLLVEAILQYRGWSLAEWNALYQDLPSRQLKVK 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   456 VADRRVISTTDAERQAVTPPGLQEAINDLVKKYKLSRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSLAVFQLAGGIG 535
Cdd:PLN02895 480 VADRTAITTTDAETVVVRPAGLQDAIDAEVAKYPRGRAFVRPSGTEDVVRVYAEASTQEAADSLAREVARLVYDLLGGVG 559


                 ...
gi 7661568   536 ERP 538
Cdd:PLN02895 560 PPP 562
ManB COG1109
Phosphomannomutase [Carbohydrate transport and metabolism];
123-523 4.39e-31

Phosphomannomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440726 [Multi-domain]  Cd Length: 456  Bit Score: 125.70  E-value: 4.39e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  123 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNTGG--------------------RYGK----- 177
Cdd:COG1109  44 VVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVPTPALAFAVRHLGADGgimitashnppeyngikffdADGGklspe 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  178 --ATIEGYYQKLSKAFVELTKQASCS-----GDEY--------------RSLKV--DCANGIGALK----LREMehyfsq 230
Cdd:COG1109 124 eeKEIEALIEKEDFRRAEAEEIGKVTriedvLEAYiealkslvdealrlRGLKVvvDCGNGAAGGVaprlLREL------ 197

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  231 GLSVQLFN---DGSKGklNHLCG---------ADFVKSHqkppqGMEIksnerCCSFDGDADRI--VyyyhDADGHFhlI 296
Cdd:COG1109 198 GAEVIVLNaepDGNFP--NHNPNpepenledlIEAVKET-----GADL-----GIAFDGDADRLgvV----DEKGRF--L 259

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  297 DGDKIATLISSFLKEllveigESLNIGVVQTAyangSSTRYLEEVMK---VPVYCTKTGVKHLHHKAQEFD--IGvyFEA 371
Cdd:COG1109 260 DGDQLLALLARYLLE------KGPGGTVVVTV----MSSLALEDIAEkhgGEVVRTKVGFKYIKEKMRETGavLG--GEE 327

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  372 NGHgtalfstavemkikqsaeqledkkrkaakmlenIIDLFNQAAGDAI-SDMLVIEaILALKGLTVQQWDALYTDLPNR 450
Cdd:COG1109 328 SGG---------------------------------IIFPDFVPTDDGIlAALLLLE-LLAKQGKSLSELLAELPRYPQP 373

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7661568  451 QLKVQVADRRVISTTDAE-RQAVTPPGLQEAINDLvkKYKL---SRAFVRPSGTEDVVRVYAEADSQESADHLAHEV 523
Cdd:COG1109 374 EINVRVPDEEKIGAVMEKlREAVEDKEELDTIDGV--KVDLedgGWVLVRPSGTEPLLRVYAEAKDEEEAEELLAEL 448
glmM TIGR01455
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ...
 57-527 3.04e-25

phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also designated in MrsA and YhbF E. coli, UreC in Helicobacter pylori, and femR315 or FemD in Staphlococcus aureus. It converts glucosamine-6-phosphate to glucosamine-1-phosphate as part of the pathway toward UDP-N-acetylglucosamine for peptidoglycan and lipopolysaccharides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]


Pssm-ID: 130522  Cd Length: 443  Bit Score: 108.22  E-value: 3.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568     57 IGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEhatclanaeeqdmqrvlidisEKEAVNLQQDAFvvigrdTRPSSEKL 136
Cdd:TIGR01455  91 AGVMISASHNPYEDNGIKFFGPGGFKLDDATEA---------------------AIEALLDEADPL------PRPESEGL 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568    137 SQSVidgvtvlggqfhdygllttpqlhymvycrntggRYGKATieGYYQKLSKAfvELTKQASCSGdeyrsLKV--DCAN 214
Cdd:TIGR01455 144 GRVK---------------------------------RYPDAV--GRYIEFLKS--TLPRGLTLSG-----LKVvlDCAN 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568    215 GiGALKLREMEhYFSQGLSVQLFNDGSKG-KLNHLCGADFVKSHQKP--PQGMEIKsnercCSFDGDADRIVYYyhDADG 291
Cdd:TIGR01455 182 G-AAYKVAPHV-FRELGAEVIAIGVEPDGlNINDGCGSTHLDALQKAvrEHGADLG-----IAFDGDADRVLAV--DANG 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568    292 hfHLIDGDKIATLISSFLKELlveiGESLNIGVVQTAYANGSSTRYLEEvMKVPVYCTKTGVKHLHHKAQEFDIGVYFEA 371
Cdd:TIGR01455 253 --RIVDGDQILYIIARALKES----GELAGNTVVATVMSNLGLERALEK-LGLTLIRTAVGDRYVLEEMRESGYNLGGEQ 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568    372 NGHgtalfstavemkikqsaeqledkkrkaakmlenIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQ 451
Cdd:TIGR01455 326 SGH---------------------------------IILLDYSTTGDGIVSALQVLTIMKKSGSTLSELAAEFVPYPQTL 372

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7661568    452 LKVQVADRRvisttdaeRQAVTPPGLQEAINDLVKKY-KLSRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSLAV 527
Cdd:TIGR01455 373 VNVRVADRK--------LAAAEAPAVKAAIEDAEAELgGTGRILLRPSGTEPLIRVMVEAADEELVQQLADTLADVV 441
PGM_PMM_IV pfam00408
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
475-527 1.51e-10

Phosphoglucomutase/phosphomannomutase, C-terminal domain;


Pssm-ID: 425666  Cd Length: 71  Bit Score: 57.28  E-value: 1.51e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 7661568    475 PGLQEAINDLVKKYKL--SRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSLAV 527
Cdd:pfam00408  16 AAILKVFADAEKILGEdgRRLDVRPSGTEPVLRVMVEGDSDEELARLADEIADLL 70
 
Name Accession Description Interval E-value
PGM3 cd03086
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ...
 22-527 0e+00

PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 (N-acetylglucosamine-phosphate mutase), is an essential enzyme found in eukaryotes that reversibly catalyzes the conversion of GlcNAc-6-phosphate into GlcNAc-1-phosphate as part of the UDP-N-acetylglucosamine (UDP-GlcNAc) biosynthetic pathway. UDP-GlcNAc is an essential metabolite that serves as the biosynthetic precursor of many glycoproteins and mucopolysaccharides. AGM1 is a member of the alpha-D-phosphohexomutase superfamily, which catalyzes the intramolecular phosphoryl transfer of sugar substrates. The alpha-D-phosphohexomutases have four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100088  Cd Length: 513  Bit Score: 892.33  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   22 QYGTAGFRTKAEHLDHVMFRMGLLAVLRSKQTKS-TIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLANAEEQ 100
Cdd:cd03086   1 SYGTAGFRTKAELLDSVVFRVGILAALRSKKLGGkTIGVMITASHNPVEDNGVKIVDPDGEMLEESWEPYATQLANASDD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  101 DMQRVLIDI--SEKEAVNLQQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNTGGRYGKA 178
Cdd:cd03086  81 ELLVLVLMLisVKELNIDLSVPANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYLVRAANTEGAYGEP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  179 TIEGYYQKLSKAFVELTKQASCSGDEYRSLKVDCANGIGALKLREMEHYFSQGLSVQLFNDGSKG--KLNHLCGADFVKS 256
Cdd:cd03086 161 TEEGYYEKLSKAFNELYNLLQDGGDEPEKLVVDCANGVGALKLKELLKRLKKGLSVKIINDGEEGpeLLNDGCGADYVKT 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  257 HQKPPQGMEIK-SNERCCSFDGDADRIVYYYHDADGHFHLIDGDKIATLISSFLKELL--VEIGESLNIGVVQTAYANGS 333
Cdd:cd03086 241 KQKPPRGFELKpPGVRCCSFDGDADRLVYFYPDSSNKFHLLDGDKIATLFAKFIKELLkkAGEELKLTIGVVQTAYANGA 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  334 STRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFSTAVEMKIKqSAEQLEDKKRKAAKMLENIIDLFN 413
Cdd:cd03086 321 STKYLEDVLKVPVVCTPTGVKHLHHAAEEFDIGVYFEANGHGTVLFSESALAKIE-ENSSLSDEQEKAAKTLLAFSRLIN 399

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  414 QAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQVADRRVISTTDAERQAVTPPGLQEAINDLVKKYKLSRA 493
Cdd:cd03086 400 QTVGDAISDMLAVELILAALGWSPQDWDNLYTDLPNRQLKVKVPDRSVIKTTDAERRLVEPKGLQDKIDAIVAKYNNGRA 479

                       490       500       510
                ....*....|....*....|....*....|....
gi 7661568  494 FVRPSGTEDVVRVYAEADSQESADHLAHEVSLAV 527
Cdd:cd03086 480 FVRPSGTEDVVRVYAEAATQEEADELANEVAELV 513
PLN02895 PLN02895
phosphoacetylglucosamine mutase
 1-538 0e+00

phosphoacetylglucosamine mutase


Pssm-ID: 215485  Cd Length: 562  Bit Score: 677.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568     1 MDLGAITKYSALHAKPNGLILQYGTAGFRTKAEHLDHVMFRMGLLAVLRSKQTKSTIGVMVTASHNPEEDNGVKLVDPLG 80
Cdd:PLN02895   4 IQRASLLAASSRFPPPQGVRFSYGTAGFRTDASLLESTVFRVGILAALRSLKTGAATGLMITASHNPVSDNGVKIVDPSG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568    81 EMLAPSWEEHATCLANAE-EQDMQRVLIDISEKEAVNL---QQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGL 156
Cdd:PLN02895  84 GMLPQAWEPFADALANAPdPDALVQLIREFVKKENIPAvggNPPAEVLLGRDTRPSGPALLAAALKGVRAIGARAVDMGI 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   157 LTTPQLHYMVYCRNTGGrygKATIEGYYQKLSKAF---VELTKQASCSGDEYRSLKVDCANGIGALKLREMEHYFSqGLS 233
Cdd:PLN02895 164 LTTPQLHWMVRAANKGM---KATESDYFEQLSSSFralLDLIPNGSGDDRADDKLVVDGANGVGAEKLETLKKALG-GLD 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   234 VQLFNDG--SKGKLNHLCGADFVKSHQKPPQGMEIK-SNERCCSFDGDADRIVYYYHDADG-HFHLIDGDKIATLISSFL 309
Cdd:PLN02895 240 LEVRNSGkeGEGVLNEGVGADFVQKEKVPPTGFASKdVGLRCASLDGDADRLVYFYVSSAGsKIDLLDGDKIASLFALFI 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   310 KELLVEIGES---------LNIGVVQTAYANGSSTRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFS 380
Cdd:PLN02895 320 KEQLRILNGNgnekpeellVRLGVVQTAYANGASTAYLKQVLGLEVVCTPTGVKYLHEAAAEFDIGVYFEANGHGTVLFS 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   381 TAVEMKIKQSAEQLEDKKR-----KAAKMLENIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQ 455
Cdd:PLN02895 400 ERFLDWLEAAAAELSSKAKgseahKAARRLLAVSRLINQAVGDALSGLLLVEAILQYRGWSLAEWNALYQDLPSRQLKVK 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   456 VADRRVISTTDAERQAVTPPGLQEAINDLVKKYKLSRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSLAVFQLAGGIG 535
Cdd:PLN02895 480 VADRTAITTTDAETVVVRPAGLQDAIDAEVAKYPRGRAFVRPSGTEDVVRVYAEASTQEAADSLAREVARLVYDLLGGVG 559


                 ...
gi 7661568   536 ERP 538
Cdd:PLN02895 560 PPP 562
PTZ00302 PTZ00302
N-acetylglucosamine-phosphate mutase; Provisional
 5-533 0e+00

N-acetylglucosamine-phosphate mutase; Provisional


Pssm-ID: 240352 [Multi-domain]  Cd Length: 585  Bit Score: 608.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568     5 AITKYSALH-AKPNGLIlqYGTAGFRTKAE--HLDHVMFRMGLLAVLRSKQTKS--------TIGVMVTASHNPEEDNGV 73
Cdd:PTZ00302  16 CGSKFPLRHsAIENPLT--YGTAGFRTKAElpPLEPVAYRVGILAALRSFLYGGkrakrgnkSVGVMITASHNPIQDNGV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568    74 KLVDPLGEMLAPSWEEHATCLANAE-EQDMQRVLIDISEKEAVNLQQD-----------AFVVIGRDTRPSSEKLSQSVI 141
Cdd:PTZ00302  94 KIIDPDGGMLEESWEKICTDFANARtGEDLVSVLMDCLTEHGIKLSNLkldlnksncskAKVHVGRDTRPSSPELVSALL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   142 DGVTVLGGQFH-DYGLLTTPQLHYMVYCRNTGGR-YGKATIEGYYQKLSKAFVELTKQASCSGDEYRS------LKVDCA 213
Cdd:PTZ00302 174 RGLKLLIGSNVrNFGIVTTPQLHFLVAFANGLGVdVVESSDELYYAYLLAAFKELYRTLQEGGPVDLTqnnskiLVVDCA 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   214 NGIGALKLREMEHYFSQ---GLSVQLFNDGSKGKLNHLCGADFVKSHQKPPQGMEIK---SNERCCSFDGDADRIVYYYH 287
Cdd:PTZ00302 254 NGVGGYKIKRFFEALKQlgiEIIPININCDEEELLNDKCGADYVQKTRKPPRAMKEWpgdEETRVASFDGDADRLVYFFP 333

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   288 DADGH--FHLIDGDKIATLISSFLKELLVEIG--ESLNIGVVQTAYANGSSTRYLEEVMK-VPVYCTKTGVKHLHHKAQE 362
Cdd:PTZ00302 334 DKDGDdkWVLLDGDRIAILYAMLIKKLLGKIQlkKKLDIGVVQTAYANGASTNYLNELLGrLRVYCAPTGVKNLHPKAHK 413

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   363 FDIGVYFEANGHGTALFStavEMKIKQSAEQLEDK--KRKAAKMLENIIDLFNQAAGDAISDMLVIEAILALKGLTVQQW 440
Cdd:PTZ00302 414 YDIGIYFEANGHGTVLFN---EKALAEWAKFLAKQnaLNSACRQLEKFLRLFNQTIGDAISDLLAVELALAFLGLSFQDW 490

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   441 DALYTDLPNRQLKVQVADRRVISTTDAERQAVTPPGLQEAINDLVKKYK-LSRAFVRPSGTEDVVRVYAEADSQESADHL 519
Cdd:PTZ00302 491 LNLYTDLPSRQDKVTVKDRTLITNTEDETRLLEPKGLQDKIDAIVSKYDnAARAFIRPSGTEPVVRVYAEAPTLEQADEL 570

                        570
                 ....*....|....
gi 7661568   520 AHEVSLAVFQLAGG 533
Cdd:PTZ00302 571 ANEVKGLVLRYCSG 584
phosphohexomutase cd03084
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ...
 23-524 1.34e-46

The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this family include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). These enzymes play important and diverse roles in carbohydrate metabolism in organisms from bacteria to humans. Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100086 [Multi-domain]  Cd Length: 355  Bit Score: 166.38  E-value: 1.34e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   23 YGTAGFRTKA--EHLDHVMFRMGLLAVlrskqtkSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLANAEEQ 100
Cdd:cd03084   2 FGTSGVRGVVgdDITPETAVALGQAIG-------STGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDE 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  101 DmqrvlidisekeavnlqqdafvvigrdtRPSSEKLSQSVidgvtvlggqfhdygllttpqlhymvycrntggrYGKATI 180
Cdd:cd03084  75 P----------------------------SAVAYELGGSV----------------------------------KAVDIL 92

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  181 EGYYQKL-SKAFVELTKQAScsgdeyRSLKVDCANGIGALKLREM-EHYfsqGLSVQLFN---DGSKGKLNHLCGADfvK 255
Cdd:cd03084  93 QRYFEALkKLFDVAALSNKK------FKVVVDSVNGVGGPIAPQLlEKL---GAEVIPLNcepDGNFGNINPDPGSE--T 161

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  256 SHQKPPQGMEIKSNERCCSFDGDADRIVYYYHDadghFHLIDGDKIATLISsflKELLVEIGesLNIGVVQTAYANGSST 335
Cdd:cd03084 162 NLKQLLAVVKAEKADFGVAFDGDADRLIVVDEN----GGFLDGDELLALLA---VELFLTFN--PRGGVVKTVVSSGALD 232

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  336 RYLEEvMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGtalfstavemkikqsaeqledkkrkaakmleniIDLFNQA 415
Cdd:cd03084 233 KVAKK-LGIKVIRTKTGFKWVGEAMQEGDVVLGGEESGGV---------------------------------IFPEFHP 278

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  416 AGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQvadrrvisttdaerqavtppglqeaindlvkkyklSRAFV 495
Cdd:cd03084 279 GRDGISAALLLLEILANLGKSLSELFSELPRYYYIRLKVR-----------------------------------GWVLV 323

                       490       500
                ....*....|....*....|....*....
gi 7661568  496 RPSGTEDVVRVYAEADSQESADHLAHEVS 524
Cdd:cd03084 324 RASGTEPAIRIYAEADTQEDVEQIKKEAR 352
ManB COG1109
Phosphomannomutase [Carbohydrate transport and metabolism];
123-523 4.39e-31

Phosphomannomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440726 [Multi-domain]  Cd Length: 456  Bit Score: 125.70  E-value: 4.39e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  123 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNTGG--------------------RYGK----- 177
Cdd:COG1109  44 VVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVPTPALAFAVRHLGADGgimitashnppeyngikffdADGGklspe 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  178 --ATIEGYYQKLSKAFVELTKQASCS-----GDEY--------------RSLKV--DCANGIGALK----LREMehyfsq 230
Cdd:COG1109 124 eeKEIEALIEKEDFRRAEAEEIGKVTriedvLEAYiealkslvdealrlRGLKVvvDCGNGAAGGVaprlLREL------ 197

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  231 GLSVQLFN---DGSKGklNHLCG---------ADFVKSHqkppqGMEIksnerCCSFDGDADRI--VyyyhDADGHFhlI 296
Cdd:COG1109 198 GAEVIVLNaepDGNFP--NHNPNpepenledlIEAVKET-----GADL-----GIAFDGDADRLgvV----DEKGRF--L 259

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  297 DGDKIATLISSFLKEllveigESLNIGVVQTAyangSSTRYLEEVMK---VPVYCTKTGVKHLHHKAQEFD--IGvyFEA 371
Cdd:COG1109 260 DGDQLLALLARYLLE------KGPGGTVVVTV----MSSLALEDIAEkhgGEVVRTKVGFKYIKEKMRETGavLG--GEE 327

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  372 NGHgtalfstavemkikqsaeqledkkrkaakmlenIIDLFNQAAGDAI-SDMLVIEaILALKGLTVQQWDALYTDLPNR 450
Cdd:COG1109 328 SGG---------------------------------IIFPDFVPTDDGIlAALLLLE-LLAKQGKSLSELLAELPRYPQP 373

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7661568  451 QLKVQVADRRVISTTDAE-RQAVTPPGLQEAINDLvkKYKL---SRAFVRPSGTEDVVRVYAEADSQESADHLAHEV 523
Cdd:COG1109 374 EINVRVPDEEKIGAVMEKlREAVEDKEELDTIDGV--KVDLedgGWVLVRPSGTEPLLRVYAEAKDEEEAEELLAEL 448
glmM TIGR01455
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ...
 57-527 3.04e-25

phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also designated in MrsA and YhbF E. coli, UreC in Helicobacter pylori, and femR315 or FemD in Staphlococcus aureus. It converts glucosamine-6-phosphate to glucosamine-1-phosphate as part of the pathway toward UDP-N-acetylglucosamine for peptidoglycan and lipopolysaccharides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]


Pssm-ID: 130522  Cd Length: 443  Bit Score: 108.22  E-value: 3.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568     57 IGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEhatclanaeeqdmqrvlidisEKEAVNLQQDAFvvigrdTRPSSEKL 136
Cdd:TIGR01455  91 AGVMISASHNPYEDNGIKFFGPGGFKLDDATEA---------------------AIEALLDEADPL------PRPESEGL 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568    137 SQSVidgvtvlggqfhdygllttpqlhymvycrntggRYGKATieGYYQKLSKAfvELTKQASCSGdeyrsLKV--DCAN 214
Cdd:TIGR01455 144 GRVK---------------------------------RYPDAV--GRYIEFLKS--TLPRGLTLSG-----LKVvlDCAN 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568    215 GiGALKLREMEhYFSQGLSVQLFNDGSKG-KLNHLCGADFVKSHQKP--PQGMEIKsnercCSFDGDADRIVYYyhDADG 291
Cdd:TIGR01455 182 G-AAYKVAPHV-FRELGAEVIAIGVEPDGlNINDGCGSTHLDALQKAvrEHGADLG-----IAFDGDADRVLAV--DANG 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568    292 hfHLIDGDKIATLISSFLKELlveiGESLNIGVVQTAYANGSSTRYLEEvMKVPVYCTKTGVKHLHHKAQEFDIGVYFEA 371
Cdd:TIGR01455 253 --RIVDGDQILYIIARALKES----GELAGNTVVATVMSNLGLERALEK-LGLTLIRTAVGDRYVLEEMRESGYNLGGEQ 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568    372 NGHgtalfstavemkikqsaeqledkkrkaakmlenIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQ 451
Cdd:TIGR01455 326 SGH---------------------------------IILLDYSTTGDGIVSALQVLTIMKKSGSTLSELAAEFVPYPQTL 372

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7661568    452 LKVQVADRRvisttdaeRQAVTPPGLQEAINDLVKKY-KLSRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSLAV 527
Cdd:TIGR01455 373 VNVRVADRK--------LAAAEAPAVKAAIEDAEAELgGTGRILLRPSGTEPLIRVMVEAADEELVQQLADTLADVV 441
GlmM cd05802
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ...
 51-524 4.14e-24

GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the alpha-D-phosphohexomutase superfamily. It is required for the interconversion of glucosamine-6-phosphate and glucosamine-1-phosphate in the biosynthetic pathway of UDP-N-acetylglucosamine, an essential precursor to components of the cell envelope. In order to be active, GlmM must be phosphorylated, which can occur via autophosphorylation or by the Ser/Thr kinase StkP. GlmM functions in a classical ping-pong bi-bi mechanism with glucosamine-1,6-diphosphate as an intermediate. Other members of the alpha-D-phosphohexomutase superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100095  Cd Length: 434  Bit Score: 104.87  E-value: 4.14e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   51 KQTKSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEhatclanaeeqdmqrvlidisEKEAVNLQqdafvviGRDTR 130
Cdd:cd05802  84 RKLRADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVEE---------------------EIEALIDK-------ELELP 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  131 PSSEKLsqsvidgvtvlgGQFHDYgllTTPQLHYMVYCRNTGGRygkatiegyyQKLSKafveltkqascsgdeyrsLKV 210
Cdd:cd05802 136 PTGEKI------------GRVYRI---DDARGRYIEFLKSTFPK----------DLLSG------------------LKI 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  211 --DCANG----IGALKLREMehyfsqGLSVQLFNDGSKG-KLNHLCGADFVKSHQKppqgmEIKSNERCC--SFDGDADR 281
Cdd:cd05802 173 vlDCANGaaykVAPEVFREL------GAEVIVINNAPDGlNINVNCGSTHPESLQK-----AVLENGADLgiAFDGDADR 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  282 IVYYyhDADGHfhLIDGDKIATLISSFLKELlveiGESLNIGVVQTAYANGSSTRYLEEvMKVPVYCTKTGVKHLHHKAQ 361
Cdd:cd05802 242 VIAV--DEKGN--IVDGDQILAICARDLKER----GRLKGNTVVGTVMSNLGLEKALKE-LGIKLVRTKVGDRYVLEEML 312

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  362 EFDIGVYFEANGHgtalfstavemkikqsaeqledkkrkaakmlenIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWD 441
Cdd:cd05802 313 KHGANLGGEQSGH---------------------------------IIFLDHSTTGDGLLTALQLLAIMKRSGKSLSELA 359

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  442 ALYTDLPNRQLKVQVADRRVISTtdaerqavtPPGLQEAINDLVKKYKLS-RAFVRPSGTEDVVRVYAEADSQESADHLA 520
Cdd:cd05802 360 SDMKLYPQVLVNVRVKDKKALLE---------NPRVQAAIAEAEKELGGEgRVLVRPSGTEPLIRVMVEGEDEELVEKLA 430


                ....
gi 7661568  521 HEVS 524
Cdd:cd05802 431 EELA 434
Arch_GlmM TIGR03990
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ...
 58-523 1.55e-17

phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been characterized as the archaeal protein responsible for the second step of UDP-GlcNAc biosynthesis. This GlmM protein catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. The first-characterized bacterial GlmM protein is modeled by TIGR01455. These two families are members of the larger phosphoglucomutase/phosphomannomutase family (characterized by three domains: pfam02878, pfam02879 and pfam02880), but are not nearest neighbors to each other. This model also includes a number of sequences from non-archaea in the Bacteroides, Chlorobi, Chloroflexi, Planctomycetes and Spirochaetes lineages. Evidence supporting their inclusion in this equivalog as having the same activity comes from genomic context and phylogenetic profiling. A large number of these organisms are known to produce exo-polysaccharide and yet only appeared to contain the GlmS enzyme of the GlmSMU pathway for UDP-GlcNAc biosynthesis (GenProp0750). In some organisms including Leptospira, this archaeal GlmM is found adjacent to the GlmS as well as a putative GlmU non-orthologous homolog. Phylogenetic profiling of the GlmS-only pattern using PPP identifies members of this archaeal GlmM family as the highest-scoring result. [Central intermediary metabolism, Amino sugars]


Pssm-ID: 274906  Cd Length: 443  Bit Score: 84.87  E-value: 1.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568     58 GVMVTASHNPEEDNGVKLVDPLGEMLAPsweehatclanaeeqDMQRVLIDISEKEavnlqqDAFVV----IGRDTRPSS 133
Cdd:TIGR03990  89 GIMITASHNPPEYNGIKLLNSDGTELSR---------------EQEEEIEEIAESG------DFERAdwdeIGTVTSDED 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568    134 ekLSQSVIDGVtvlggqfhdygllttpqlhymvycrntggrygkatiegyyqklsKAFVELTKQAScsgdeyRSLKV--D 211
Cdd:TIGR03990 148 --AIDDYIEAI--------------------------------------------LDKVDVEAIRK------KGFKVvvD 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568    212 CANGIGALK----LREMehyfsqGLSVQLFNDGSKGK------------LNHLC------GADFVKSHqkppqgmeiksn 269
Cdd:TIGR03990 176 CGNGAGSLTtpylLREL------GCKVITLNCQPDGTfpgrnpeptpenLKDLSalvkatGADLGIAH------------ 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568    270 erccsfDGDADRIVYYyhDADGHFhlIDGDKIATLissFLKELLVEIGESLnigVVqtayaNGSSTRYLEEVMK---VPV 346
Cdd:TIGR03990 238 ------DGDADRLVFI--DEKGRF--IGGDYTLAL---FAKYLLEHGGGKV---VT-----NVSSSRAVEDVAErhgGEV 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568    347 YCTKTGVKHLHHKAQEFDIGVYFEANGHgtalfstavemkikqsaeqledkkrkaakmlenIIDLFNQAAGDAISDMLVI 426
Cdd:TIGR03990 297 IRTKVGEVNVAEKMKEEGAVFGGEGNGG---------------------------------WIFPDHHYCRDGLMAAALF 343

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568    427 EAILALKGLTVQQWDALYTDLPNRQLKVQVADRRVISTTDAERQAVTppglQEAINDL--VK-KYKLSRAFVRPSGTEDV 503
Cdd:TIGR03990 344 LELLAEEGKPLSELLAELPKYPMSKEKVELPDEDKEEVMEAVEEEFA----DAEIDTIdgVRiDFEDGWVLVRPSGTEPI 419

                         490       500
                  ....*....|....*....|
gi 7661568    504 VRVYAEADSQESADHLAHEV 523
Cdd:TIGR03990 420 VRIYAEAKTEERAEELLEEG 439
PGM_like1 cd03087
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ...
 58-523 3.02e-16

This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100089  Cd Length: 439  Bit Score: 81.08  E-value: 3.02e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   58 GVMVTASHNPEEDNGVKLVDPLG-EMlapsweehatclanaeEQDMQRVLIDISEKEAVNLQqdAFVVIGRDTRPSsekl 136
Cdd:cd03087  86 GVMITASHNPPEYNGIKLVNPDGtEF----------------SREQEEEIEEIIFSERFRRV--AWDEVGSVRRED---- 143

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  137 sqSVIDgvtvlggqfhDYgllttpqlhymvycrntggrygkatIEGYYQKLSKafveltkqascsgDEYRSLKV--DCAN 214
Cdd:cd03087 144 --SAID----------EY-------------------------IEAILDKVDI-------------DGGKGLKVvvDCGN 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  215 GIGALK----LREMehyfsqGLSVQLFN---DG---------SKGKLNHLC------GADFVKSHqkppqgmeiksnerc 272
Cdd:cd03087 174 GAGSLTtpylLREL------GCKVITLNanpDGffpgrppepTPENLSELMelvratGADLGIAH--------------- 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  273 csfDGDADRIVYYyhDADGHFhlIDGDKIATLISsflKELLVEIGeslniGVVQTAYangSSTRYLEEVMK---VPVYCT 349
Cdd:cd03087 233 ---DGDADRAVFV--DEKGRF--IDGDKLLALLA---KYLLEEGG-----GKVVTPV---DASMLVEDVVEeagGEVIRT 294

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  350 KTGVKHLHHKAQEFDIGVYFEANGHG-TALFSTAVemkikqsaeqleDKKRKAAKMLEniidlfnqaagdaisdmLVIEA 428
Cdd:cd03087 295 PVGDVHVAEEMIENGAVFGGEPNGGWiFPDHQLCR------------DGIMTAALLLE-----------------LLAEE 345

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  429 ilalKGLtvqqwDALYTDLPNRQLKvqvadRRVISTTDAERQAVtPPGLQEAINDLVKK------YKLSR----AFVRPS 498
Cdd:cd03087 346 ----KPL-----SELLDELPKYPLL-----REKVECPDEKKEEV-MEAVEEELSDADEDvdtidgVRIEYedgwVLIRPS 410

                       490       500
                ....*....|....*....|....*
gi 7661568  499 GTEDVVRVYAEADSQESADHLAHEV 523
Cdd:cd03087 411 GTEPKIRITAEAKTEERAKELLEEG 435
PGM_PMM_IV pfam00408
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
475-527 1.51e-10

Phosphoglucomutase/phosphomannomutase, C-terminal domain;


Pssm-ID: 425666  Cd Length: 71  Bit Score: 57.28  E-value: 1.51e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 7661568    475 PGLQEAINDLVKKYKL--SRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSLAV 527
Cdd:pfam00408  16 AAILKVFADAEKILGEdgRRLDVRPSGTEPVLRVMVEGDSDEELARLADEIADLL 70
PGM_like4 cd05803
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ...
 52-520 2.96e-09

This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate guanyltransferase domain in a protein of unknown function that is found in both prokaryotes and eukaryotes. This domain belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100096  Cd Length: 445  Bit Score: 59.24  E-value: 2.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   52 QTKSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSweehatclanaeeqDMQRVLIDISEKEAVNLQQDAfvvIGRDTrp 131
Cdd:cd05803  85 QSQASGGIIITASHNPPQWNGLKFIGPDGEFLTPD--------------EGEEVLSCAEAGSAQKAGYDQ---LGEVT-- 145

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  132 SSEKLSQSVIDGVtvlggqfhdygllttpqlhymvycrntggrygkatiegyyqkLSKAFVELTKQAScsgdeyRSLKV- 210
Cdd:cd05803 146 FSEDAIAEHIDKV------------------------------------------LALVDVDVIKIRE------RNFKVa 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  211 -DCANGIGALKLREMEHyfSQGLSVQLFNDGSKGKLNHlcgadfvkshqkPPQgmEIKSN---------ERCCSF----D 276
Cdd:cd05803 178 vDSVNGAGGLLIPRLLE--KLGCEVIVLNCEPTGLFPH------------TPE--PLPENltqlcaavkESGADVgfavD 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  277 GDADRIVyyyhdadghfhLIDGDKIA-----TLISSFLkELLVEIGESLNIGVvqtayaNGSSTRYLEEVMK---VPVYC 348
Cdd:cd05803 242 PDADRLA-----------LVDEDGRPigeeyTLALAVD-YVLKYGGRKGPVVV------NLSTSRALEDIARkhgVPVFR 303

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  349 TKTGVKHLHHKAQEFDIGVYFEANGhgtalfstavemkikqsaeqledkkrkaakmleNIIDLFNQAAGDAISDMLVIEA 428
Cdd:cd05803 304 SAVGEANVVEKMKEVDAVIGGEGNG---------------------------------GVILPDVHYGRDSLVGIALVLQ 350

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  429 ILALKGLTVQQWDALYTDLPNRQLKVQVADR---RVISTTDAE---RQAVTPPGLQEAINDlvkkyklSRAFVRPSGTED 502
Cdd:cd05803 351 LLAASGKPLSEIVDELPQYYISKTKVTIAGEaleRLLKKLEAYfkdAEASTLDGLRLDSED-------SWVHVRPSNTEP 423

                       490
                ....*....|....*...
gi 7661568  503 VVRVYAEADSQESADHLA 520
Cdd:cd05803 424 IVRIIAEAPTQDEAEALA 441
PMM_PGM cd03089
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ...
 123-523 1.26e-08

The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars (e.g. between mannose-1-phosphate and mannose-6-phosphate or glucose-1-phosphate and glucose-6-phosphate) via a bisphosphorylated sugar intermediate. The reaction involves two phosphoryl transfers, with an intervening 180 degree reorientation of the reaction intermediate during catalysis. Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is thus, a simple example of processivity, as defined by multiple rounds of catalysis without release of substrate. Glucose-6-phosphate and glucose-1-phosphate are known to be utilized for energy metabolism and cell surface construction, respectively. PMM/PGM belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the phosphoglucomutases (PGM1 and PGM2). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100091  Cd Length: 443  Bit Score: 57.14  E-value: 1.26e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  123 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHY-----------MV--------Y-----CRNTGGRYG-- 176
Cdd:cd03089  39 VVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPVLYFatfhldadggvMItashnppeYngfkiVIGGGPLSGed 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  177 ----KATIEGYYQKLSKAFVELTKQasCSGDEY------------RSLK--VDCANGIGALKLREMEhyfsQGL---SVQ 235
Cdd:cd03089 119 iqalRERAEKGDFAAATGRGSVEKV--DILPDYidrllsdiklgkRPLKvvVDAGNGAAGPIAPQLL----EALgceVIP 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  236 LFN--DGS----------KGKLNHLC------GADFvkshqkppqGMeiksnerccSFDGDADRIVYYyhDADGHFhlID 297
Cdd:cd03089 193 LFCepDGTfpnhhpdptdPENLEDLIaavkenGADL---------GI---------AFDGDGDRLGVV--DEKGEI--IW 250

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  298 GDKIATLISsflKELLVEIGESLNIGVVQTayangssTRYLEEVMK----VPVYCtKTGVKHLHHKAQEFDIGVYFEANG 373
Cdd:cd03089 251 GDRLLALFA---RDILKRNPGATIVYDVKC-------SRNLYDFIEeaggKPIMW-KTGHSFIKAKMKETGALLAGEMSG 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  374 HgtaLFstavemkikqsaeqledkkrkaakmleniidlFNQA---AGDAISDMLVIEAILALKGLTVqqwDALYTDLPNR 450
Cdd:cd03089 320 H---IF--------------------------------FKDRwygFDDGIYAALRLLELLSKSGKTL---SELLADLPKY 361

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  451 ----QLKVQVADRRVISTTDAERQAVTPPGLQeaINDL--VK-KYKLSRAFVRPSGTEDVVRVYAEADSQESADHLAHEV 523
Cdd:cd03089 362 fstpEIRIPVTEEDKFAVIERLKEHFEFPGAE--IIDIdgVRvDFEDGWGLVRASNTEPVLVLRFEADTEEGLEEIKAEL 439
PGM_PMM_I pfam02878
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
123-166 1.88e-07

Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;


Pssm-ID: 427032  Cd Length: 138  Bit Score: 50.30  E-value: 1.88e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 7661568    123 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMV 166
Cdd:pfam02878  43 VVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTPAVSFAT 86
PGM_PMM_I pfam02878
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
58-89 2.76e-07

Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;


Pssm-ID: 427032  Cd Length: 138  Bit Score: 49.92  E-value: 2.76e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 7661568     58 GVMVTASHNPEEDNGVKLVDPLGEMLAPSWEE 89
Cdd:pfam02878  94 GIMITASHNPPEYNGIKVFDSNGGPIPPEVEK 125
glmM PRK10887
phosphoglucosamine mutase; Provisional
 58-527 5.79e-07

phosphoglucosamine mutase; Provisional


Pssm-ID: 236787  Cd Length: 443  Bit Score: 52.06  E-value: 5.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568    58 GVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEhatcLANAE-EQDMQRVlidisekEAVNLqqdafvviGRDTRpssekl 136
Cdd:PRK10887  93 GIVISASHNPYYDNGIKFFSADGTKLPDEVEL----AIEAElDKPLTCV-------ESAEL--------GKASR------ 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   137 sqsvIDGVTvlggqfhdygllttpqlhymvycrntgGRYgkatIEgyyqklskaFVELTKQASCSgdeYRSLK--VDCAN 214
Cdd:PRK10887 148 ----INDAA---------------------------GRY----IE---------FCKSTFPNELS---LRGLKivVDCAN 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   215 G----IGALKLREMehyfsqglsvqlfndgskgklnhlcGADFVKSHQKpPQGMEIksNERCCS---------------- 274
Cdd:PRK10887 181 GatyhIAPNVFREL-------------------------GAEVIAIGCE-PNGLNI--NDECGAtdpealqaavlaekad 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   275 ----FDGDADRIVYyyhdADGHFHLIDGDKIATLISsflKELLVEiGEsLNIGVVQTAYANGSSTRYLEEvMKVPVYCTK 350
Cdd:PRK10887 233 lgiaFDGDGDRVIM----VDHLGNLVDGDQLLYIIA---RDRLRR-GQ-LRGGVVGTLMSNMGLELALKQ-LGIPFVRAK 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   351 TGVKHLHHKAQEFD--IGVyfEANGHgtalfstavemkikqsaeqledkkrkaakmlenIIDLFNQAAGDAI-SDMLVIE 427
Cdd:PRK10887 303 VGDRYVLEKLQEKGwrLGG--ENSGH---------------------------------ILCLDKTTTGDGIvAALQVLA 347

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568   428 AiLALKGLTVQQWDALYTDLPNRQLKVQVADRRVISTTDAERQAVtppgLQEAINDLVKKyklSRAFVRPSGTEDVVRVY 507
Cdd:PRK10887 348 A-MVRSGMSLADLCSGMKLFPQVLINVRFKPGADDPLESEAVKAA----LAEVEAELGGR---GRVLLRKSGTEPLIRVM 419

                        490       500
                 ....*....|....*....|
gi 7661568   508 AEADSQESADHLAHEVSLAV 527
Cdd:PRK10887 420 VEGEDEAQVTALAERIADAV 439
PGM_like2 cd05800
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ...
 418-519 3.56e-05

This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily and is found in both archaea and bacteria. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four structural domains (subdomains) with a centrally located active site formed by four loops, one from each subdomain. All four subdomains are included in this alignment model.


Pssm-ID: 100093  Cd Length: 461  Bit Score: 46.39  E-value: 3.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568  418 DAI-SDMLVIEAIlALKGLTVqqwDALYTDLpnrQLKVQVA--DRRVISTTDAERQAVT-----PPGLQEAINDLVK--- 486
Cdd:cd05800 341 DGIlAGLLLLEAV-AKTGKPL---SELVAEL---EEEYGPSyyDRIDLRLTPAQKEAILeklknEPPLSIAGGKVDEvnt 413

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 7661568  487 ----KYKL---SRAFVRPSGTEDVVRVYAEADSQESADHL 519
Cdd:cd05800 414 idgvKLVLedgSWLLIRPSGTEPLLRIYAEAPSPEKVEAL 453
PGM2 cd05799
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ...
 51-74 3.83e-05

This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The mammalian PGM2 is thought to be a phosphopentomutase that catalyzes the conversion of the nucleoside breakdown products, ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. PGM2L1 is thought to catalyze the 1,3-bisphosphoglycerate-dependent synthesis of glucose 1,6-bisphosphate and other aldose-bisphosphates that serve as cofactors for several sugar phosphomutases and possibly also as regulators of glycolytic enzymes. PGM2 and PGM2L1 belong to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100092  Cd Length: 487  Bit Score: 46.35  E-value: 3.83e-05
                        10        20
                ....*....|....*....|....
gi 7661568   51 KQTKSTIGVMVTASHNPEEDNGVK 74
Cdd:cd05799  93 RHLGADAGIMITASHNPKEYNGYK 116
PMM_PGM cd03089
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ...
 58-76 7.04e-05

The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars (e.g. between mannose-1-phosphate and mannose-6-phosphate or glucose-1-phosphate and glucose-6-phosphate) via a bisphosphorylated sugar intermediate. The reaction involves two phosphoryl transfers, with an intervening 180 degree reorientation of the reaction intermediate during catalysis. Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is thus, a simple example of processivity, as defined by multiple rounds of catalysis without release of substrate. Glucose-6-phosphate and glucose-1-phosphate are known to be utilized for energy metabolism and cell surface construction, respectively. PMM/PGM belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the phosphoglucomutases (PGM1 and PGM2). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100091  Cd Length: 443  Bit Score: 45.20  E-value: 7.04e-05
                        10
                ....*....|....*....
gi 7661568   58 GVMVTASHNPEEDNGVKLV 76
Cdd:cd03089  90 GVMITASHNPPEYNGFKIV 108
PTZ00150 PTZ00150
phosphoglucomutase-2-like protein; Provisional
 54-74 9.54e-05

phosphoglucomutase-2-like protein; Provisional


Pssm-ID: 240294  Cd Length: 584  Bit Score: 45.06  E-value: 9.54e-05
                         10        20
                 ....*....|....*....|.
gi 7661568    54 KSTIGVMVTASHNPEEDNGVK 74
Cdd:PTZ00150 140 KCLAGVMVTASHNPKEDNGYK 160
PRK07564 PRK07564
phosphoglucomutase; Validated
 495-521 5.19e-04

phosphoglucomutase; Validated


Pssm-ID: 236050  Cd Length: 543  Bit Score: 42.82  E-value: 5.19e-04
                         10        20
                 ....*....|....*....|....*..
gi 7661568   495 VRPSGTEDVVRVYAEadSQESADHLAH 521
Cdd:PRK07564 504 ARPSGTETTYKIYAE--SFEGDEHLHQ 528
manB PRK09542
phosphomannomutase/phosphoglucomutase; Reviewed
 123-164 5.80e-04

phosphomannomutase/phosphoglucomutase; Reviewed


Pssm-ID: 236557  Cd Length: 445  Bit Score: 42.28  E-value: 5.80e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 7661568   123 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHY 164
Cdd:PRK09542  38 VVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIGLASTDQLYF 79
PLN02371 PLN02371
phosphoglucosamine mutase family protein
 111-160 8.83e-04

phosphoglucosamine mutase family protein


Pssm-ID: 215211 [Multi-domain]  Cd Length: 583  Bit Score: 41.97  E-value: 8.83e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 7661568   111 EKEAVNLQQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTP 160
Cdd:PLN02371 106 EKKKADGSGELRVSVGRDPRISGPRLADAVFAGLASAGLDVVDMGLATTP 155
PGM_like2 cd05800
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ...
 58-74 1.90e-03

This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily and is found in both archaea and bacteria. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four structural domains (subdomains) with a centrally located active site formed by four loops, one from each subdomain. All four subdomains are included in this alignment model.


Pssm-ID: 100093  Cd Length: 461  Bit Score: 41.00  E-value: 1.90e-03
                        10
                ....*....|....*..
gi 7661568   58 GVMVTASHNPEEDNGVK 74
Cdd:cd05800  94 GVMITASHNPPEYNGVK 110
PGM_PMM_III pfam02880
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
297-375 4.64e-03

Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;


Pssm-ID: 460733  Cd Length: 115  Bit Score: 37.04  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7661568    297 DGDKIATLISSFLKELLVEIGeslNIGVVQTAyangSSTRYLEEVMK---VPVYCTKTGVKHLHHKAQEFDIGVYFEANG 373
Cdd:pfam02880   1 DGDQILALLAKYLLEQGKLPP---GAGVVKTV----MSSLGLDRVAKklgGKLVRTPVGDKYVKEKMREEGALFGGEESG 73


                  ..
gi 7661568    374 HG 375
Cdd:pfam02880  74 HI 75
PGM_like3 cd05801
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ...
 496-520 7.97e-03

This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100094 [Multi-domain]  Cd Length: 522  Bit Score: 38.77  E-value: 7.97e-03
                        10        20
                ....*....|....*....|....*
gi 7661568  496 RPSGTEDVVRVYAEadSQESADHLA 520
Cdd:cd05801 490 RPSGTEDVYKIYAE--SFLSEEHLK 512
 
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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