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Conserved domains on  [gi|315707006|ref|NP_001186846|]
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phosphoacetylglucosamine mutase isoform 1 [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 ...
 50-555 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: 895.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006  50 QYGTAGFRTKAEHLDHVMFRMGLLAVLRSKQTKS-TIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLANAEEQ 128
Cdd:cd03086    1 SYGTAGFRTKAELLDSVVFRVGILAALRSKKLGGkTIGVMITASHNPVEDNGVKIVDPDGEMLEESWEPYATQLANASDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 129 DMQRVLIDI--SEKEAVNLQQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNTGGRYGKA 206
Cdd:cd03086   81 ELLVLVLMLisVKELNIDLSVPANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYLVRAANTEGAYGEP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 207 TIEGYYQKLSKAFVELTKQASCSGDEYRSLKVDCANGIGALKLREMEHYFSQGLSVQLFNDGSKG--KLNHLCGADFVKS 284
Cdd:cd03086  161 TEEGYYEKLSKAFNELYNLLQDGGDEPEKLVVDCANGVGALKLKELLKRLKKGLSVKIINDGEEGpeLLNDGCGADYVKT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 285 HQKPPQGMEIK-SNERCCSFDGDADRIVYYYHDADGHFHLIDGDKIATLISSFLKELL--VEIGESLNIGVVQTAYANGS 361
Cdd:cd03086  241 KQKPPRGFELKpPGVRCCSFDGDADRLVYFYPDSSNKFHLLDGDKIATLFAKFIKELLkkAGEELKLTIGVVQTAYANGA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 362 STRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFSTAVEMKIKqSAEQLEDKKRKAAKMLENIIDLFN 441
Cdd:cd03086  321 STKYLEDVLKVPVVCTPTGVKHLHHAAEEFDIGVYFEANGHGTVLFSESALAKIE-ENSSLSDEQEKAAKTLLAFSRLIN 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 442 QAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQVADRRVISTTDAERQAVTPPGLQEAINDLVKKYKLSRA 521
Cdd:cd03086  400 QTVGDAISDMLAVELILAALGWSPQDWDNLYTDLPNRQLKVKVPDRSVIKTTDAERRLVEPKGLQDKIDAIVAKYNNGRA 479

                        490       500       510
                 ....*....|....*....|....*....|....
gi 315707006 522 FVRPSGTEDVVRVYAEADSQESADHLAHEVSLAV 555
Cdd:cd03086  480 FVRPSGTEDVVRVYAEAATQEEADELANEVAELV 513
 
Name Accession Description Interval E-value
PGM3 cd03086
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ...
 50-555 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: 895.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006  50 QYGTAGFRTKAEHLDHVMFRMGLLAVLRSKQTKS-TIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLANAEEQ 128
Cdd:cd03086    1 SYGTAGFRTKAELLDSVVFRVGILAALRSKKLGGkTIGVMITASHNPVEDNGVKIVDPDGEMLEESWEPYATQLANASDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 129 DMQRVLIDI--SEKEAVNLQQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNTGGRYGKA 206
Cdd:cd03086   81 ELLVLVLMLisVKELNIDLSVPANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYLVRAANTEGAYGEP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 207 TIEGYYQKLSKAFVELTKQASCSGDEYRSLKVDCANGIGALKLREMEHYFSQGLSVQLFNDGSKG--KLNHLCGADFVKS 284
Cdd:cd03086  161 TEEGYYEKLSKAFNELYNLLQDGGDEPEKLVVDCANGVGALKLKELLKRLKKGLSVKIINDGEEGpeLLNDGCGADYVKT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 285 HQKPPQGMEIK-SNERCCSFDGDADRIVYYYHDADGHFHLIDGDKIATLISSFLKELL--VEIGESLNIGVVQTAYANGS 361
Cdd:cd03086  241 KQKPPRGFELKpPGVRCCSFDGDADRLVYFYPDSSNKFHLLDGDKIATLFAKFIKELLkkAGEELKLTIGVVQTAYANGA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 362 STRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFSTAVEMKIKqSAEQLEDKKRKAAKMLENIIDLFN 441
Cdd:cd03086  321 STKYLEDVLKVPVVCTPTGVKHLHHAAEEFDIGVYFEANGHGTVLFSESALAKIE-ENSSLSDEQEKAAKTLLAFSRLIN 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 442 QAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQVADRRVISTTDAERQAVTPPGLQEAINDLVKKYKLSRA 521
Cdd:cd03086  400 QTVGDAISDMLAVELILAALGWSPQDWDNLYTDLPNRQLKVKVPDRSVIKTTDAERRLVEPKGLQDKIDAIVAKYNNGRA 479

                        490       500       510
                 ....*....|....*....|....*....|....
gi 315707006 522 FVRPSGTEDVVRVYAEADSQESADHLAHEVSLAV 555
Cdd:cd03086  480 FVRPSGTEDVVRVYAEAATQEEADELANEVAELV 513
PLN02895 PLN02895
phosphoacetylglucosamine mutase
 28-566 0e+00

phosphoacetylglucosamine mutase


Pssm-ID: 215485  Cd Length: 562  Bit Score: 679.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006  28 DMDLGAITKYSALHAKPNGLILQYGTAGFRTKAEHLDHVMFRMGLLAVLRSKQTKSTIGVMVTASHNPEEDNGVKLVDPL 107
Cdd:PLN02895   3 EIQRASLLAASSRFPPPQGVRFSYGTAGFRTDASLLESTVFRVGILAALRSLKTGAATGLMITASHNPVSDNGVKIVDPS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 108 GEMLAPSWEEHATCLANAE-EQDMQRVLIDISEKEAVNL---QQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYG 183
Cdd:PLN02895  83 GGMLPQAWEPFADALANAPdPDALVQLIREFVKKENIPAvggNPPAEVLLGRDTRPSGPALLAAALKGVRAIGARAVDMG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 184 LLTTPQLHYMVYCRNTGGrygKATIEGYYQKLSKAF---VELTKQASCSGDEYRSLKVDCANGIGALKLREMEHYFSqGL 260
Cdd:PLN02895 163 ILTTPQLHWMVRAANKGM---KATESDYFEQLSSSFralLDLIPNGSGDDRADDKLVVDGANGVGAEKLETLKKALG-GL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 261 SVQLFNDG--SKGKLNHLCGADFVKSHQKPPQGMEIK-SNERCCSFDGDADRIVYYYHDADG-HFHLIDGDKIATLISSF 336
Cdd:PLN02895 239 DLEVRNSGkeGEGVLNEGVGADFVQKEKVPPTGFASKdVGLRCASLDGDADRLVYFYVSSAGsKIDLLDGDKIASLFALF 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 337 LKELLVEIGES---------LNIGVVQTAYANGSSTRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALF 407
Cdd:PLN02895 319 IKEQLRILNGNgnekpeellVRLGVVQTAYANGASTAYLKQVLGLEVVCTPTGVKYLHEAAAEFDIGVYFEANGHGTVLF 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 408 STAVEMKIKQSAEQLEDKKR-----KAAKMLENIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKV 482
Cdd:PLN02895 399 SERFLDWLEAAAAELSSKAKgseahKAARRLLAVSRLINQAVGDALSGLLLVEAILQYRGWSLAEWNALYQDLPSRQLKV 478

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 483 QVADRRVISTTDAERQAVTPPGLQEAINDLVKKYKLSRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSLAVFQLAGGI 562
Cdd:PLN02895 479 KVADRTAITTTDAETVVVRPAGLQDAIDAEVAKYPRGRAFVRPSGTEDVVRVYAEASTQEAADSLAREVARLVYDLLGGV 558


                 ....
gi 315707006 563 GERP 566
Cdd:PLN02895 559 GPPP 562
ManB COG1109
Phosphomannomutase [Carbohydrate transport and metabolism];
151-551 2.52e-31

Phosphomannomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440726 [Multi-domain]  Cd Length: 456  Bit Score: 126.85  E-value: 2.52e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 151 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNTGG--------------------RYGK----- 205
Cdd:COG1109   44 VVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVPTPALAFAVRHLGADGgimitashnppeyngikffdADGGklspe 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 206 --ATIEGYYQKLSKAFVELTKQASCS-----GDEY--------------RSLKV--DCANGIGALK----LREMehyfsq 258
Cdd:COG1109  124 eeKEIEALIEKEDFRRAEAEEIGKVTriedvLEAYiealkslvdealrlRGLKVvvDCGNGAAGGVaprlLREL------ 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 259 GLSVQLFN---DGSKGklNHLCG---------ADFVKSHqkppqGMEIksnerCCSFDGDADRI--VyyyhDADGHFhlI 324
Cdd:COG1109  198 GAEVIVLNaepDGNFP--NHNPNpepenledlIEAVKET-----GADL-----GIAFDGDADRLgvV----DEKGRF--L 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 325 DGDKIATLISSFLKEllveigESLNIGVVQTAyangSSTRYLEEVMK---VPVYCTKTGVKHLHHKAQEFD--IGvyFEA 399
Cdd:COG1109  260 DGDQLLALLARYLLE------KGPGGTVVVTV----MSSLALEDIAEkhgGEVVRTKVGFKYIKEKMRETGavLG--GEE 327

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 400 NGHgtalfstavemkikqsaeqledkkrkaakmlenIIDLFNQAAGDAI-SDMLVIEaILALKGLTVQQWDALYTDLPNR 478
Cdd:COG1109  328 SGG---------------------------------IIFPDFVPTDDGIlAALLLLE-LLAKQGKSLSELLAELPRYPQP 373

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 315707006 479 QLKVQVADRRVISTTDAE-RQAVTPPGLQEAINDLvkKYKL---SRAFVRPSGTEDVVRVYAEADSQESADHLAHEV 551
Cdd:COG1109  374 EINVRVPDEEKIGAVMEKlREAVEDKEELDTIDGV--KVDLedgGWVLVRPSGTEPLLRVYAEAKDEEEAEELLAEL 448
glmM TIGR01455
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ...
 85-555 2.97e-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: 108.61  E-value: 2.97e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006   85 IGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEhatclanaeeqdmqrvlidisEKEAVNLQQDAFvvigrdTRPSSEKL 164
Cdd:TIGR01455  91 AGVMISASHNPYEDNGIKFFGPGGFKLDDATEA---------------------AIEALLDEADPL------PRPESEGL 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006  165 SQSVidgvtvlggqfhdygllttpqlhymvycrntggRYGKATieGYYQKLSKAfvELTKQASCSGdeyrsLKV--DCAN 242
Cdd:TIGR01455 144 GRVK---------------------------------RYPDAV--GRYIEFLKS--TLPRGLTLSG-----LKVvlDCAN 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006  243 GiGALKLREMEhYFSQGLSVQLFNDGSKG-KLNHLCGADFVKSHQKP--PQGMEIKsnercCSFDGDADRIVYYyhDADG 319
Cdd:TIGR01455 182 G-AAYKVAPHV-FRELGAEVIAIGVEPDGlNINDGCGSTHLDALQKAvrEHGADLG-----IAFDGDADRVLAV--DANG 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006  320 hfHLIDGDKIATLISSFLKELlveiGESLNIGVVQTAYANGSSTRYLEEvMKVPVYCTKTGVKHLHHKAQEFDIGVYFEA 399
Cdd:TIGR01455 253 --RIVDGDQILYIIARALKES----GELAGNTVVATVMSNLGLERALEK-LGLTLIRTAVGDRYVLEEMRESGYNLGGEQ 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006  400 NGHgtalfstavemkikqsaeqledkkrkaakmlenIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQ 479
Cdd:TIGR01455 326 SGH---------------------------------IILLDYSTTGDGIVSALQVLTIMKKSGSTLSELAAEFVPYPQTL 372

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 315707006  480 LKVQVADRRvisttdaeRQAVTPPGLQEAINDLVKKY-KLSRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSLAV 555
Cdd:TIGR01455 373 VNVRVADRK--------LAAAEAPAVKAAIEDAEAELgGTGRILLRPSGTEPLIRVMVEAADEELVQQLADTLADVV 441
PGM_PMM_IV pfam00408
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
503-555 1.05e-10

Phosphoglucomutase/phosphomannomutase, C-terminal domain;


Pssm-ID: 425666  Cd Length: 71  Bit Score: 57.66  E-value: 1.05e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 315707006  503 PGLQEAINDLVKKYKL--SRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSLAV 555
Cdd:pfam00408  16 AAILKVFADAEKILGEdgRRLDVRPSGTEPVLRVMVEGDSDEELARLADEIADLL 70
 
Name Accession Description Interval E-value
PGM3 cd03086
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ...
 50-555 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: 895.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006  50 QYGTAGFRTKAEHLDHVMFRMGLLAVLRSKQTKS-TIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLANAEEQ 128
Cdd:cd03086    1 SYGTAGFRTKAELLDSVVFRVGILAALRSKKLGGkTIGVMITASHNPVEDNGVKIVDPDGEMLEESWEPYATQLANASDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 129 DMQRVLIDI--SEKEAVNLQQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNTGGRYGKA 206
Cdd:cd03086   81 ELLVLVLMLisVKELNIDLSVPANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYLVRAANTEGAYGEP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 207 TIEGYYQKLSKAFVELTKQASCSGDEYRSLKVDCANGIGALKLREMEHYFSQGLSVQLFNDGSKG--KLNHLCGADFVKS 284
Cdd:cd03086  161 TEEGYYEKLSKAFNELYNLLQDGGDEPEKLVVDCANGVGALKLKELLKRLKKGLSVKIINDGEEGpeLLNDGCGADYVKT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 285 HQKPPQGMEIK-SNERCCSFDGDADRIVYYYHDADGHFHLIDGDKIATLISSFLKELL--VEIGESLNIGVVQTAYANGS 361
Cdd:cd03086  241 KQKPPRGFELKpPGVRCCSFDGDADRLVYFYPDSSNKFHLLDGDKIATLFAKFIKELLkkAGEELKLTIGVVQTAYANGA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 362 STRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFSTAVEMKIKqSAEQLEDKKRKAAKMLENIIDLFN 441
Cdd:cd03086  321 STKYLEDVLKVPVVCTPTGVKHLHHAAEEFDIGVYFEANGHGTVLFSESALAKIE-ENSSLSDEQEKAAKTLLAFSRLIN 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 442 QAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQVADRRVISTTDAERQAVTPPGLQEAINDLVKKYKLSRA 521
Cdd:cd03086  400 QTVGDAISDMLAVELILAALGWSPQDWDNLYTDLPNRQLKVKVPDRSVIKTTDAERRLVEPKGLQDKIDAIVAKYNNGRA 479

                        490       500       510
                 ....*....|....*....|....*....|....
gi 315707006 522 FVRPSGTEDVVRVYAEADSQESADHLAHEVSLAV 555
Cdd:cd03086  480 FVRPSGTEDVVRVYAEAATQEEADELANEVAELV 513
PLN02895 PLN02895
phosphoacetylglucosamine mutase
 28-566 0e+00

phosphoacetylglucosamine mutase


Pssm-ID: 215485  Cd Length: 562  Bit Score: 679.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006  28 DMDLGAITKYSALHAKPNGLILQYGTAGFRTKAEHLDHVMFRMGLLAVLRSKQTKSTIGVMVTASHNPEEDNGVKLVDPL 107
Cdd:PLN02895   3 EIQRASLLAASSRFPPPQGVRFSYGTAGFRTDASLLESTVFRVGILAALRSLKTGAATGLMITASHNPVSDNGVKIVDPS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 108 GEMLAPSWEEHATCLANAE-EQDMQRVLIDISEKEAVNL---QQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYG 183
Cdd:PLN02895  83 GGMLPQAWEPFADALANAPdPDALVQLIREFVKKENIPAvggNPPAEVLLGRDTRPSGPALLAAALKGVRAIGARAVDMG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 184 LLTTPQLHYMVYCRNTGGrygKATIEGYYQKLSKAF---VELTKQASCSGDEYRSLKVDCANGIGALKLREMEHYFSqGL 260
Cdd:PLN02895 163 ILTTPQLHWMVRAANKGM---KATESDYFEQLSSSFralLDLIPNGSGDDRADDKLVVDGANGVGAEKLETLKKALG-GL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 261 SVQLFNDG--SKGKLNHLCGADFVKSHQKPPQGMEIK-SNERCCSFDGDADRIVYYYHDADG-HFHLIDGDKIATLISSF 336
Cdd:PLN02895 239 DLEVRNSGkeGEGVLNEGVGADFVQKEKVPPTGFASKdVGLRCASLDGDADRLVYFYVSSAGsKIDLLDGDKIASLFALF 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 337 LKELLVEIGES---------LNIGVVQTAYANGSSTRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALF 407
Cdd:PLN02895 319 IKEQLRILNGNgnekpeellVRLGVVQTAYANGASTAYLKQVLGLEVVCTPTGVKYLHEAAAEFDIGVYFEANGHGTVLF 398

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 408 STAVEMKIKQSAEQLEDKKR-----KAAKMLENIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKV 482
Cdd:PLN02895 399 SERFLDWLEAAAAELSSKAKgseahKAARRLLAVSRLINQAVGDALSGLLLVEAILQYRGWSLAEWNALYQDLPSRQLKV 478

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 483 QVADRRVISTTDAERQAVTPPGLQEAINDLVKKYKLSRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSLAVFQLAGGI 562
Cdd:PLN02895 479 KVADRTAITTTDAETVVVRPAGLQDAIDAEVAKYPRGRAFVRPSGTEDVVRVYAEASTQEAADSLAREVARLVYDLLGGV 558


                 ....
gi 315707006 563 GERP 566
Cdd:PLN02895 559 GPPP 562
PTZ00302 PTZ00302
N-acetylglucosamine-phosphate mutase; Provisional
 33-561 0e+00

N-acetylglucosamine-phosphate mutase; Provisional


Pssm-ID: 240352 [Multi-domain]  Cd Length: 585  Bit Score: 610.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006  33 AITKYSALH-AKPNGLIlqYGTAGFRTKAE--HLDHVMFRMGLLAVLRSKQTKS--------TIGVMVTASHNPEEDNGV 101
Cdd:PTZ00302  16 CGSKFPLRHsAIENPLT--YGTAGFRTKAElpPLEPVAYRVGILAALRSFLYGGkrakrgnkSVGVMITASHNPIQDNGV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 102 KLVDPLGEMLAPSWEEHATCLANAE-EQDMQRVLIDISEKEAVNLQQD-----------AFVVIGRDTRPSSEKLSQSVI 169
Cdd:PTZ00302  94 KIIDPDGGMLEESWEKICTDFANARtGEDLVSVLMDCLTEHGIKLSNLkldlnksncskAKVHVGRDTRPSSPELVSALL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 170 DGVTVLGGQFH-DYGLLTTPQLHYMVYCRNTGGR-YGKATIEGYYQKLSKAFVELTKQASCSGDEYRS------LKVDCA 241
Cdd:PTZ00302 174 RGLKLLIGSNVrNFGIVTTPQLHFLVAFANGLGVdVVESSDELYYAYLLAAFKELYRTLQEGGPVDLTqnnskiLVVDCA 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 242 NGIGALKLREMEHYFSQ---GLSVQLFNDGSKGKLNHLCGADFVKSHQKPPQGMEIK---SNERCCSFDGDADRIVYYYH 315
Cdd:PTZ00302 254 NGVGGYKIKRFFEALKQlgiEIIPININCDEEELLNDKCGADYVQKTRKPPRAMKEWpgdEETRVASFDGDADRLVYFFP 333

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 316 DADGH--FHLIDGDKIATLISSFLKELLVEIG--ESLNIGVVQTAYANGSSTRYLEEVMK-VPVYCTKTGVKHLHHKAQE 390
Cdd:PTZ00302 334 DKDGDdkWVLLDGDRIAILYAMLIKKLLGKIQlkKKLDIGVVQTAYANGASTNYLNELLGrLRVYCAPTGVKNLHPKAHK 413

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 391 FDIGVYFEANGHGTALFStavEMKIKQSAEQLEDK--KRKAAKMLENIIDLFNQAAGDAISDMLVIEAILALKGLTVQQW 468
Cdd:PTZ00302 414 YDIGIYFEANGHGTVLFN---EKALAEWAKFLAKQnaLNSACRQLEKFLRLFNQTIGDAISDLLAVELALAFLGLSFQDW 490

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 469 DALYTDLPNRQLKVQVADRRVISTTDAERQAVTPPGLQEAINDLVKKYK-LSRAFVRPSGTEDVVRVYAEADSQESADHL 547
Cdd:PTZ00302 491 LNLYTDLPSRQDKVTVKDRTLITNTEDETRLLEPKGLQDKIDAIVSKYDnAARAFIRPSGTEPVVRVYAEAPTLEQADEL 570

                        570
                 ....*....|....
gi 315707006 548 AHEVSLAVFQLAGG 561
Cdd:PTZ00302 571 ANEVKGLVLRYCSG 584
phosphohexomutase cd03084
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ...
 51-552 2.11e-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: 2.11e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006  51 YGTAGFRTKA--EHLDHVMFRMGLLAVlrskqtkSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLANAEEQ 128
Cdd:cd03084    2 FGTSGVRGVVgdDITPETAVALGQAIG-------STGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 129 DmqrvlidisekeavnlqqdafvvigrdtRPSSEKLSQSVidgvtvlggqfhdygllttpqlhymvycrntggrYGKATI 208
Cdd:cd03084   75 P----------------------------SAVAYELGGSV----------------------------------KAVDIL 92

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 209 EGYYQKL-SKAFVELTKQAScsgdeyRSLKVDCANGIGALKLREM-EHYfsqGLSVQLFN---DGSKGKLNHLCGADfvK 283
Cdd:cd03084   93 QRYFEALkKLFDVAALSNKK------FKVVVDSVNGVGGPIAPQLlEKL---GAEVIPLNcepDGNFGNINPDPGSE--T 161

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 284 SHQKPPQGMEIKSNERCCSFDGDADRIVYYYHDadghFHLIDGDKIATLISsflKELLVEIGesLNIGVVQTAYANGSST 363
Cdd:cd03084  162 NLKQLLAVVKAEKADFGVAFDGDADRLIVVDEN----GGFLDGDELLALLA---VELFLTFN--PRGGVVKTVVSSGALD 232

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 364 RYLEEvMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGtalfstavemkikqsaeqledkkrkaakmleniIDLFNQA 443
Cdd:cd03084  233 KVAKK-LGIKVIRTKTGFKWVGEAMQEGDVVLGGEESGGV---------------------------------IFPEFHP 278

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 444 AGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQvadrrvisttdaerqavtppglqeaindlvkkyklSRAFV 523
Cdd:cd03084  279 GRDGISAALLLLEILANLGKSLSELFSELPRYYYIRLKVR-----------------------------------GWVLV 323

                        490       500
                 ....*....|....*....|....*....
gi 315707006 524 RPSGTEDVVRVYAEADSQESADHLAHEVS 552
Cdd:cd03084  324 RASGTEPAIRIYAEADTQEDVEQIKKEAR 352
ManB COG1109
Phosphomannomutase [Carbohydrate transport and metabolism];
151-551 2.52e-31

Phosphomannomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440726 [Multi-domain]  Cd Length: 456  Bit Score: 126.85  E-value: 2.52e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 151 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNTGG--------------------RYGK----- 205
Cdd:COG1109   44 VVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVPTPALAFAVRHLGADGgimitashnppeyngikffdADGGklspe 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 206 --ATIEGYYQKLSKAFVELTKQASCS-----GDEY--------------RSLKV--DCANGIGALK----LREMehyfsq 258
Cdd:COG1109  124 eeKEIEALIEKEDFRRAEAEEIGKVTriedvLEAYiealkslvdealrlRGLKVvvDCGNGAAGGVaprlLREL------ 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 259 GLSVQLFN---DGSKGklNHLCG---------ADFVKSHqkppqGMEIksnerCCSFDGDADRI--VyyyhDADGHFhlI 324
Cdd:COG1109  198 GAEVIVLNaepDGNFP--NHNPNpepenledlIEAVKET-----GADL-----GIAFDGDADRLgvV----DEKGRF--L 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 325 DGDKIATLISSFLKEllveigESLNIGVVQTAyangSSTRYLEEVMK---VPVYCTKTGVKHLHHKAQEFD--IGvyFEA 399
Cdd:COG1109  260 DGDQLLALLARYLLE------KGPGGTVVVTV----MSSLALEDIAEkhgGEVVRTKVGFKYIKEKMRETGavLG--GEE 327

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 400 NGHgtalfstavemkikqsaeqledkkrkaakmlenIIDLFNQAAGDAI-SDMLVIEaILALKGLTVQQWDALYTDLPNR 478
Cdd:COG1109  328 SGG---------------------------------IIFPDFVPTDDGIlAALLLLE-LLAKQGKSLSELLAELPRYPQP 373

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 315707006 479 QLKVQVADRRVISTTDAE-RQAVTPPGLQEAINDLvkKYKL---SRAFVRPSGTEDVVRVYAEADSQESADHLAHEV 551
Cdd:COG1109  374 EINVRVPDEEKIGAVMEKlREAVEDKEELDTIDGV--KVDLedgGWVLVRPSGTEPLLRVYAEAKDEEEAEELLAEL 448
glmM TIGR01455
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ...
 85-555 2.97e-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: 108.61  E-value: 2.97e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006   85 IGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEhatclanaeeqdmqrvlidisEKEAVNLQQDAFvvigrdTRPSSEKL 164
Cdd:TIGR01455  91 AGVMISASHNPYEDNGIKFFGPGGFKLDDATEA---------------------AIEALLDEADPL------PRPESEGL 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006  165 SQSVidgvtvlggqfhdygllttpqlhymvycrntggRYGKATieGYYQKLSKAfvELTKQASCSGdeyrsLKV--DCAN 242
Cdd:TIGR01455 144 GRVK---------------------------------RYPDAV--GRYIEFLKS--TLPRGLTLSG-----LKVvlDCAN 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006  243 GiGALKLREMEhYFSQGLSVQLFNDGSKG-KLNHLCGADFVKSHQKP--PQGMEIKsnercCSFDGDADRIVYYyhDADG 319
Cdd:TIGR01455 182 G-AAYKVAPHV-FRELGAEVIAIGVEPDGlNINDGCGSTHLDALQKAvrEHGADLG-----IAFDGDADRVLAV--DANG 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006  320 hfHLIDGDKIATLISSFLKELlveiGESLNIGVVQTAYANGSSTRYLEEvMKVPVYCTKTGVKHLHHKAQEFDIGVYFEA 399
Cdd:TIGR01455 253 --RIVDGDQILYIIARALKES----GELAGNTVVATVMSNLGLERALEK-LGLTLIRTAVGDRYVLEEMRESGYNLGGEQ 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006  400 NGHgtalfstavemkikqsaeqledkkrkaakmlenIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQ 479
Cdd:TIGR01455 326 SGH---------------------------------IILLDYSTTGDGIVSALQVLTIMKKSGSTLSELAAEFVPYPQTL 372

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 315707006  480 LKVQVADRRvisttdaeRQAVTPPGLQEAINDLVKKY-KLSRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSLAV 555
Cdd:TIGR01455 373 VNVRVADRK--------LAAAEAPAVKAAIEDAEAELgGTGRILLRPSGTEPLIRVMVEAADEELVQQLADTLADVV 441
GlmM cd05802
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ...
 79-552 2.44e-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: 105.64  E-value: 2.44e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006  79 KQTKSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEhatclanaeeqdmqrvlidisEKEAVNLQqdafvviGRDTR 158
Cdd:cd05802   84 RKLRADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVEE---------------------EIEALIDK-------ELELP 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 159 PSSEKLsqsvidgvtvlgGQFHDYgllTTPQLHYMVYCRNTGGRygkatiegyyQKLSKafveltkqascsgdeyrsLKV 238
Cdd:cd05802  136 PTGEKI------------GRVYRI---DDARGRYIEFLKSTFPK----------DLLSG------------------LKI 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 239 --DCANG----IGALKLREMehyfsqGLSVQLFNDGSKG-KLNHLCGADFVKSHQKppqgmEIKSNERCC--SFDGDADR 309
Cdd:cd05802  173 vlDCANGaaykVAPEVFREL------GAEVIVINNAPDGlNINVNCGSTHPESLQK-----AVLENGADLgiAFDGDADR 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 310 IVYYyhDADGHfhLIDGDKIATLISSFLKELlveiGESLNIGVVQTAYANGSSTRYLEEvMKVPVYCTKTGVKHLHHKAQ 389
Cdd:cd05802  242 VIAV--DEKGN--IVDGDQILAICARDLKER----GRLKGNTVVGTVMSNLGLEKALKE-LGIKLVRTKVGDRYVLEEML 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 390 EFDIGVYFEANGHgtalfstavemkikqsaeqledkkrkaakmlenIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWD 469
Cdd:cd05802  313 KHGANLGGEQSGH---------------------------------IIFLDHSTTGDGLLTALQLLAIMKRSGKSLSELA 359

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 470 ALYTDLPNRQLKVQVADRRVISTtdaerqavtPPGLQEAINDLVKKYKLS-RAFVRPSGTEDVVRVYAEADSQESADHLA 548
Cdd:cd05802  360 SDMKLYPQVLVNVRVKDKKALLE---------NPRVQAAIAEAEKELGGEgRVLVRPSGTEPLIRVMVEGEDEELVEKLA 430


                 ....
gi 315707006 549 HEVS 552
Cdd:cd05802  431 EELA 434
Arch_GlmM TIGR03990
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ...
 86-551 1.21e-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: 85.64  E-value: 1.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006   86 GVMVTASHNPEEDNGVKLVDPLGEMLAPsweehatclanaeeqDMQRVLIDISEKEavnlqqDAFVV----IGRDTRPSS 161
Cdd:TIGR03990  89 GIMITASHNPPEYNGIKLLNSDGTELSR---------------EQEEEIEEIAESG------DFERAdwdeIGTVTSDED 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006  162 ekLSQSVIDGVtvlggqfhdygllttpqlhymvycrntggrygkatiegyyqklsKAFVELTKQAScsgdeyRSLKV--D 239
Cdd:TIGR03990 148 --AIDDYIEAI--------------------------------------------LDKVDVEAIRK------KGFKVvvD 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006  240 CANGIGALK----LREMehyfsqGLSVQLFNDGSKGK------------LNHLC------GADFVKSHqkppqgmeiksn 297
Cdd:TIGR03990 176 CGNGAGSLTtpylLREL------GCKVITLNCQPDGTfpgrnpeptpenLKDLSalvkatGADLGIAH------------ 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006  298 erccsfDGDADRIVYYyhDADGHFhlIDGDKIATLissFLKELLVEIGESLnigVVqtayaNGSSTRYLEEVMK---VPV 374
Cdd:TIGR03990 238 ------DGDADRLVFI--DEKGRF--IGGDYTLAL---FAKYLLEHGGGKV---VT-----NVSSSRAVEDVAErhgGEV 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006  375 YCTKTGVKHLHHKAQEFDIGVYFEANGHgtalfstavemkikqsaeqledkkrkaakmlenIIDLFNQAAGDAISDMLVI 454
Cdd:TIGR03990 297 IRTKVGEVNVAEKMKEEGAVFGGEGNGG---------------------------------WIFPDHHYCRDGLMAAALF 343

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006  455 EAILALKGLTVQQWDALYTDLPNRQLKVQVADRRVISTTDAERQAVTppglQEAINDL--VK-KYKLSRAFVRPSGTEDV 531
Cdd:TIGR03990 344 LELLAEEGKPLSELLAELPKYPMSKEKVELPDEDKEEVMEAVEEEFA----DAEIDTIdgVRiDFEDGWVLVRPSGTEPI 419

                         490       500
                  ....*....|....*....|
gi 315707006  532 VRVYAEADSQESADHLAHEV 551
Cdd:TIGR03990 420 VRIYAEAKTEERAEELLEEG 439
PGM_like1 cd03087
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ...
 86-551 2.47e-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: 81.46  E-value: 2.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006  86 GVMVTASHNPEEDNGVKLVDPLG-EMlapsweehatclanaeEQDMQRVLIDISEKEAVNLQqdAFVVIGRDTRPSsekl 164
Cdd:cd03087   86 GVMITASHNPPEYNGIKLVNPDGtEF----------------SREQEEEIEEIIFSERFRRV--AWDEVGSVRRED---- 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 165 sqSVIDgvtvlggqfhDYgllttpqlhymvycrntggrygkatIEGYYQKLSKafveltkqascsgDEYRSLKV--DCAN 242
Cdd:cd03087  144 --SAID----------EY-------------------------IEAILDKVDI-------------DGGKGLKVvvDCGN 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 243 GIGALK----LREMehyfsqGLSVQLFN---DG---------SKGKLNHLC------GADFVKSHqkppqgmeiksnerc 300
Cdd:cd03087  174 GAGSLTtpylLREL------GCKVITLNanpDGffpgrppepTPENLSELMelvratGADLGIAH--------------- 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 301 csfDGDADRIVYYyhDADGHFhlIDGDKIATLISsflKELLVEIGeslniGVVQTAYangSSTRYLEEVMK---VPVYCT 377
Cdd:cd03087  233 ---DGDADRAVFV--DEKGRF--IDGDKLLALLA---KYLLEEGG-----GKVVTPV---DASMLVEDVVEeagGEVIRT 294

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 378 KTGVKHLHHKAQEFDIGVYFEANGHG-TALFSTAVemkikqsaeqleDKKRKAAKMLEniidlfnqaagdaisdmLVIEA 456
Cdd:cd03087  295 PVGDVHVAEEMIENGAVFGGEPNGGWiFPDHQLCR------------DGIMTAALLLE-----------------LLAEE 345

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 457 ilalKGLtvqqwDALYTDLPNRQLKvqvadRRVISTTDAERQAVtPPGLQEAINDLVKK------YKLSR----AFVRPS 526
Cdd:cd03087  346 ----KPL-----SELLDELPKYPLL-----REKVECPDEKKEEV-MEAVEEELSDADEDvdtidgVRIEYedgwVLIRPS 410

                        490       500
                 ....*....|....*....|....*
gi 315707006 527 GTEDVVRVYAEADSQESADHLAHEV 551
Cdd:cd03087  411 GTEPKIRITAEAKTEERAKELLEEG 435
PGM_PMM_IV pfam00408
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
503-555 1.05e-10

Phosphoglucomutase/phosphomannomutase, C-terminal domain;


Pssm-ID: 425666  Cd Length: 71  Bit Score: 57.66  E-value: 1.05e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 315707006  503 PGLQEAINDLVKKYKL--SRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSLAV 555
Cdd:pfam00408  16 AAILKVFADAEKILGEdgRRLDVRPSGTEPVLRVMVEGDSDEELARLADEIADLL 70
PGM_like4 cd05803
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ...
 80-548 2.72e-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: 59.63  E-value: 2.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006  80 QTKSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSweehatclanaeeqDMQRVLIDISEKEAVNLQQDAfvvIGRDTrp 159
Cdd:cd05803   85 QSQASGGIIITASHNPPQWNGLKFIGPDGEFLTPD--------------EGEEVLSCAEAGSAQKAGYDQ---LGEVT-- 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 160 SSEKLSQSVIDGVtvlggqfhdygllttpqlhymvycrntggrygkatiegyyqkLSKAFVELTKQAScsgdeyRSLKV- 238
Cdd:cd05803  146 FSEDAIAEHIDKV------------------------------------------LALVDVDVIKIRE------RNFKVa 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 239 -DCANGIGALKLREMEHyfSQGLSVQLFNDGSKGKLNHlcgadfvkshqkPPQgmEIKSN---------ERCCSF----D 304
Cdd:cd05803  178 vDSVNGAGGLLIPRLLE--KLGCEVIVLNCEPTGLFPH------------TPE--PLPENltqlcaavkESGADVgfavD 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 305 GDADRIVyyyhdadghfhLIDGDKIA-----TLISSFLkELLVEIGESLNIGVvqtayaNGSSTRYLEEVMK---VPVYC 376
Cdd:cd05803  242 PDADRLA-----------LVDEDGRPigeeyTLALAVD-YVLKYGGRKGPVVV------NLSTSRALEDIARkhgVPVFR 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 377 TKTGVKHLHHKAQEFDIGVYFEANGhgtalfstavemkikqsaeqledkkrkaakmleNIIDLFNQAAGDAISDMLVIEA 456
Cdd:cd05803  304 SAVGEANVVEKMKEVDAVIGGEGNG---------------------------------GVILPDVHYGRDSLVGIALVLQ 350

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 457 ILALKGLTVQQWDALYTDLPNRQLKVQVADR---RVISTTDAE---RQAVTPPGLQEAINDlvkkyklSRAFVRPSGTED 530
Cdd:cd05803  351 LLAASGKPLSEIVDELPQYYISKTKVTIAGEaleRLLKKLEAYfkdAEASTLDGLRLDSED-------SWVHVRPSNTEP 423

                        490
                 ....*....|....*...
gi 315707006 531 VVRVYAEADSQESADHLA 548
Cdd:cd05803  424 IVRIIAEAPTQDEAEALA 441
PMM_PGM cd03089
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ...
 151-551 6.70e-09

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: 58.29  E-value: 6.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 151 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHY-----------MV--------Y-----CRNTGGRYG-- 204
Cdd:cd03089   39 VVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPVLYFatfhldadggvMItashnppeYngfkiVIGGGPLSGed 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 205 ----KATIEGYYQKLSKAFVELTKQasCSGDEY------------RSLK--VDCANGIGALKLREMEhyfsQGL---SVQ 263
Cdd:cd03089  119 iqalRERAEKGDFAAATGRGSVEKV--DILPDYidrllsdiklgkRPLKvvVDAGNGAAGPIAPQLL----EALgceVIP 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 264 LFN--DGS----------KGKLNHLC------GADFvkshqkppqGMeiksnerccSFDGDADRIVYYyhDADGHFhlID 325
Cdd:cd03089  193 LFCepDGTfpnhhpdptdPENLEDLIaavkenGADL---------GI---------AFDGDGDRLGVV--DEKGEI--IW 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 326 GDKIATLISsflKELLVEIGESLNIGVVQTayangssTRYLEEVMK----VPVYCtKTGVKHLHHKAQEFDIGVYFEANG 401
Cdd:cd03089  251 GDRLLALFA---RDILKRNPGATIVYDVKC-------SRNLYDFIEeaggKPIMW-KTGHSFIKAKMKETGALLAGEMSG 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 402 HG----------TALFStavemkikqsaeqledkkrkAAKMLEniidlfnqaagdaisdmlvieaILALKGLTVqqwDAL 471
Cdd:cd03089  320 HIffkdrwygfdDGIYA--------------------ALRLLE----------------------LLSKSGKTL---SEL 354

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 472 YTDLPNR----QLKVQVADRRVISTTDAERQAVTPPGLQeaINDL--VK-KYKLSRAFVRPSGTEDVVRVYAEADSQESA 544
Cdd:cd03089  355 LADLPKYfstpEIRIPVTEEDKFAVIERLKEHFEFPGAE--IIDIdgVRvDFEDGWGLVRASNTEPVLVLRFEADTEEGL 432


                 ....*..
gi 315707006 545 DHLAHEV 551
Cdd:cd03089  433 EEIKAEL 439
PGM_PMM_I pfam02878
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
151-194 1.99e-07

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


Pssm-ID: 427032  Cd Length: 138  Bit Score: 50.30  E-value: 1.99e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 315707006  151 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMV 194
Cdd:pfam02878  43 VVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTPAVSFAT 86
PGM_PMM_I pfam02878
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
86-117 2.93e-07

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


Pssm-ID: 427032  Cd Length: 138  Bit Score: 49.92  E-value: 2.93e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 315707006   86 GVMVTASHNPEEDNGVKLVDPLGEMLAPSWEE 117
Cdd:pfam02878  94 GIMITASHNPPEYNGIKVFDSNGGPIPPEVEK 125
glmM PRK10887
phosphoglucosamine mutase; Provisional
 86-555 4.69e-07

phosphoglucosamine mutase; Provisional


Pssm-ID: 236787  Cd Length: 443  Bit Score: 52.45  E-value: 4.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006  86 GVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEhatcLANAE-EQDMQRVlidisekEAVNLqqdafvviGRDTRpssekl 164
Cdd:PRK10887  93 GIVISASHNPYYDNGIKFFSADGTKLPDEVEL----AIEAElDKPLTCV-------ESAEL--------GKASR------ 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 165 sqsvIDGVTvlggqfhdygllttpqlhymvycrntgGRYgkatIEgyyqklskaFVELTKQASCSgdeYRSLK--VDCAN 242
Cdd:PRK10887 148 ----INDAA---------------------------GRY----IE---------FCKSTFPNELS---LRGLKivVDCAN 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 243 G----IGALKLREMehyfsqglsvqlfndgskgklnhlcGADFVKSHQKpPQGMEIksNERCCS---------------- 302
Cdd:PRK10887 181 GatyhIAPNVFREL-------------------------GAEVIAIGCE-PNGLNI--NDECGAtdpealqaavlaekad 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 303 ----FDGDADRIVYyyhdADGHFHLIDGDKIATLISsflKELLVEiGEsLNIGVVQTAYANGSSTRYLEEvMKVPVYCTK 378
Cdd:PRK10887 233 lgiaFDGDGDRVIM----VDHLGNLVDGDQLLYIIA---RDRLRR-GQ-LRGGVVGTLMSNMGLELALKQ-LGIPFVRAK 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 379 TGVKHLHHKAQEFD--IGVyfEANGHgtalfstavemkikqsaeqledkkrkaakmlenIIDLFNQAAGDAI-SDMLVIE 455
Cdd:PRK10887 303 VGDRYVLEKLQEKGwrLGG--ENSGH---------------------------------ILCLDKTTTGDGIvAALQVLA 347

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 456 AiLALKGLTVQQWDALYTDLPNRQLKVQVADRRVISTTDAERQAVtppgLQEAINDLVKKyklSRAFVRPSGTEDVVRVY 535
Cdd:PRK10887 348 A-MVRSGMSLADLCSGMKLFPQVLINVRFKPGADDPLESEAVKAA----LAEVEAELGGR---GRVLLRKSGTEPLIRVM 419

                        490       500
                 ....*....|....*....|
gi 315707006 536 AEADSQESADHLAHEVSLAV 555
Cdd:PRK10887 420 VEGEDEAQVTALAERIADAV 439
PGM_like2 cd05800
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ...
 446-547 3.22e-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: 3.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006 446 DAI-SDMLVIEAIlALKGLTVqqwDALYTDLpnrQLKVQVA--DRRVISTTDAERQAVT-----PPGLQEAINDLVK--- 514
Cdd:cd05800  341 DGIlAGLLLLEAV-AKTGKPL---SELVAEL---EEEYGPSyyDRIDLRLTPAQKEAILeklknEPPLSIAGGKVDEvnt 413

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 315707006 515 ----KYKL---SRAFVRPSGTEDVVRVYAEADSQESADHL 547
Cdd:cd05800  414 idgvKLVLedgSWLLIRPSGTEPLLRIYAEAPSPEKVEAL 453
PGM2 cd05799
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ...
 79-102 3.65e-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: 3.65e-05
                         10        20
                 ....*....|....*....|....
gi 315707006  79 KQTKSTIGVMVTASHNPEEDNGVK 102
Cdd:cd05799   93 RHLGADAGIMITASHNPKEYNGYK 116
PMM_PGM cd03089
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ...
 86-104 6.81e-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: 45.58  E-value: 6.81e-05
                         10
                 ....*....|....*....
gi 315707006  86 GVMVTASHNPEEDNGVKLV 104
Cdd:cd03089   90 GVMITASHNPPEYNGFKIV 108
PTZ00150 PTZ00150
phosphoglucomutase-2-like protein; Provisional
 82-102 1.03e-04

phosphoglucomutase-2-like protein; Provisional


Pssm-ID: 240294  Cd Length: 584  Bit Score: 45.06  E-value: 1.03e-04
                         10        20
                 ....*....|....*....|.
gi 315707006  82 KSTIGVMVTASHNPEEDNGVK 102
Cdd:PTZ00150 140 KCLAGVMVTASHNPKEDNGYK 160
PRK07564 PRK07564
phosphoglucomutase; Validated
 523-549 5.33e-04

phosphoglucomutase; Validated


Pssm-ID: 236050  Cd Length: 543  Bit Score: 42.82  E-value: 5.33e-04
                         10        20
                 ....*....|....*....|....*..
gi 315707006 523 VRPSGTEDVVRVYAEadSQESADHLAH 549
Cdd:PRK07564 504 ARPSGTETTYKIYAE--SFEGDEHLHQ 528
manB PRK09542
phosphomannomutase/phosphoglucomutase; Reviewed
 151-192 5.95e-04

phosphomannomutase/phosphoglucomutase; Reviewed


Pssm-ID: 236557  Cd Length: 445  Bit Score: 42.66  E-value: 5.95e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 315707006 151 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHY 192
Cdd:PRK09542  38 VVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIGLASTDQLYF 79
PLN02371 PLN02371
phosphoglucosamine mutase family protein
 139-188 9.47e-04

phosphoglucosamine mutase family protein


Pssm-ID: 215211 [Multi-domain]  Cd Length: 583  Bit Score: 41.97  E-value: 9.47e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 315707006 139 EKEAVNLQQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTP 188
Cdd:PLN02371 106 EKKKADGSGELRVSVGRDPRISGPRLADAVFAGLASAGLDVVDMGLATTP 155
PGM_like2 cd05800
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ...
 86-102 1.88e-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: 1.88e-03
                         10
                 ....*....|....*..
gi 315707006  86 GVMVTASHNPEEDNGVK 102
Cdd:cd05800   94 GVMITASHNPPEYNGVK 110
PGM_PMM_III pfam02880
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
325-403 4.63e-03

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


Pssm-ID: 460733  Cd Length: 115  Bit Score: 37.04  E-value: 4.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707006  325 DGDKIATLISSFLKELLVEIGeslNIGVVQTAyangSSTRYLEEVMK---VPVYCTKTGVKHLHHKAQEFDIGVYFEANG 401
Cdd:pfam02880   1 DGDQILALLAKYLLEQGKLPP---GAGVVKTV----MSSLGLDRVAKklgGKLVRTPVGDKYVKEKMREEGALFGGEESG 73


                  ..
gi 315707006  402 HG 403
Cdd:pfam02880  74 HI 75
PGM_like3 cd05801
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ...
 524-548 8.52e-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: 8.52e-03
                         10        20
                 ....*....|....*....|....*
gi 315707006 524 RPSGTEDVVRVYAEadSQESADHLA 548
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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