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Conserved domains on  [gi|1708852043|ref|XP_029890182|]
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phosphoacetylglucosamine mutase isoform X3 [Aquila chrysaetos chrysaetos]

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 ...
 22-528 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: 868.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043  22 QYGTAGFRTKAEQLDHVMFRMGLLAVLRSKAVVS-TIGVMVTASHNPEEDNGVKLVDPLGEMLHPSWEEYATQLANAEEE 100
Cdd:cd03086     1 SYGTAGFRTKAELLDSVVFRVGILAALRSKKLGGkTIGVMITASHNPVEDNGVKIVDPDGEMLEESWEPYATQLANASDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 101 ELQKIIIDIC--QKAAVNQHKDALVFIGRDTRPSSEKLSQSVIDGISVLGGQYHDYGLVTTPQLHYMVCCQNTQGQYGKA 178
Cdd:cd03086    81 ELLVLVLMLIsvKELNIDLSVPANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYLVRAANTEGAYGEP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 179 MLEGYYEKLSKAFTELIKQSPSAGESQRHLKIDCANGIGALKLSEMEPYFPKEVIIHLFNDGTK--EKLNHLCGADFVKV 256
Cdd:cd03086   161 TEEGYYEKLSKAFNELYNLLQDGGDEPEKLVVDCANGVGALKLKELLKRLKKGLSVKIINDGEEgpELLNDGCGADYVKT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 257 HQKPPRGLDMK-PNERCCSFDGDADRIVYYYKDATGHFHLIDGDKIATLISIFLKELLAKVGE--TLHMAVVQTAYANGS 333
Cdd:cd03086   241 KQKPPRGFELKpPGVRCCSFDGDADRLVYFYPDSSNKFHLLDGDKIATLFAKFIKELLKKAGEelKLTIGVVQTAYANGA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 334 STRYLEETLKVPVHCVKTGVKHLHHKAQEFDVGVYFEANGHGTVLFSKAAETKIRQlaKEGKDDEKREAAKVLENMIDLI 413
Cdd:cd03086   321 STKYLEDVLKVPVVCTPTGVKHLHHAAEEFDIGVYFEANGHGTVLFSESALAKIEE--NSSLSDEQEKAAKTLLAFSRLI 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 414 NQTVGDAISDMLVIEAILALKGLTVQQWDAIYADLPNRLLKVQVADRRVIVTTDAERCVVTPPGLQEKIDALVKKYKLSR 493
Cdd:cd03086   399 NQTVGDAISDMLAVELILAALGWSPQDWDNLYTDLPNRQLKVKVPDRSVIKTTDAERRLVEPKGLQDKIDAIVAKYNNGR 478

                         490       500       510
                  ....*....|....*....|....*....|....*
gi 1708852043 494 AFVRPSGTEDVVRIYAEADTQENTDALAHEVSLAV 528
Cdd:cd03086   479 AFVRPSGTEDVVRVYAEAATQEEADELANEVAELV 513
 
Name Accession Description Interval E-value
PGM3 cd03086
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ...
 22-528 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: 868.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043  22 QYGTAGFRTKAEQLDHVMFRMGLLAVLRSKAVVS-TIGVMVTASHNPEEDNGVKLVDPLGEMLHPSWEEYATQLANAEEE 100
Cdd:cd03086     1 SYGTAGFRTKAELLDSVVFRVGILAALRSKKLGGkTIGVMITASHNPVEDNGVKIVDPDGEMLEESWEPYATQLANASDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 101 ELQKIIIDIC--QKAAVNQHKDALVFIGRDTRPSSEKLSQSVIDGISVLGGQYHDYGLVTTPQLHYMVCCQNTQGQYGKA 178
Cdd:cd03086    81 ELLVLVLMLIsvKELNIDLSVPANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYLVRAANTEGAYGEP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 179 MLEGYYEKLSKAFTELIKQSPSAGESQRHLKIDCANGIGALKLSEMEPYFPKEVIIHLFNDGTK--EKLNHLCGADFVKV 256
Cdd:cd03086   161 TEEGYYEKLSKAFNELYNLLQDGGDEPEKLVVDCANGVGALKLKELLKRLKKGLSVKIINDGEEgpELLNDGCGADYVKT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 257 HQKPPRGLDMK-PNERCCSFDGDADRIVYYYKDATGHFHLIDGDKIATLISIFLKELLAKVGE--TLHMAVVQTAYANGS 333
Cdd:cd03086   241 KQKPPRGFELKpPGVRCCSFDGDADRLVYFYPDSSNKFHLLDGDKIATLFAKFIKELLKKAGEelKLTIGVVQTAYANGA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 334 STRYLEETLKVPVHCVKTGVKHLHHKAQEFDVGVYFEANGHGTVLFSKAAETKIRQlaKEGKDDEKREAAKVLENMIDLI 413
Cdd:cd03086   321 STKYLEDVLKVPVVCTPTGVKHLHHAAEEFDIGVYFEANGHGTVLFSESALAKIEE--NSSLSDEQEKAAKTLLAFSRLI 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 414 NQTVGDAISDMLVIEAILALKGLTVQQWDAIYADLPNRLLKVQVADRRVIVTTDAERCVVTPPGLQEKIDALVKKYKLSR 493
Cdd:cd03086   399 NQTVGDAISDMLAVELILAALGWSPQDWDNLYTDLPNRQLKVKVPDRSVIKTTDAERRLVEPKGLQDKIDAIVAKYNNGR 478

                         490       500       510
                  ....*....|....*....|....*....|....*
gi 1708852043 494 AFVRPSGTEDVVRIYAEADTQENTDALAHEVSLAV 528
Cdd:cd03086   479 AFVRPSGTEDVVRVYAEAATQEEADELANEVAELV 513
PLN02895 PLN02895
phosphoacetylglucosamine mutase
 1-539 0e+00

phosphoacetylglucosamine mutase


Pssm-ID: 215485  Cd Length: 562  Bit Score: 666.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043   1 MDSEALKKYSALHPKPPGLTLQYGTAGFRTKAEQLDHVMFRMGLLAVLRSKAVVSTIGVMVTASHNPEEDNGVKLVDPLG 80
Cdd:PLN02895    4 IQRASLLAASSRFPPPQGVRFSYGTAGFRTDASLLESTVFRVGILAALRSLKTGAATGLMITASHNPVSDNGVKIVDPSG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043  81 EMLHPSWEEYATQLANAE-EEELQKIIIDICQKAAVNQHKD---ALVFIGRDTRPSSEKLSQSVIDGISVLGGQYHDYGL 156
Cdd:PLN02895   84 GMLPQAWEPFADALANAPdPDALVQLIREFVKKENIPAVGGnppAEVLLGRDTRPSGPALLAAALKGVRAIGARAVDMGI 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 157 VTTPQLHYMVCCQNtQGQygKAMLEGYYEKLSKAFTELIKQSPSAGESQRHLK---IDCANGIGALKLSEMEPYFPkEVI 233
Cdd:PLN02895  164 LTTPQLHWMVRAAN-KGM--KATESDYFEQLSSSFRALLDLIPNGSGDDRADDklvVDGANGVGAEKLETLKKALG-GLD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 234 IHLFNDGTKEK--LNHLCGADFVKVHQKPPRGLDMKP-NERCCSFDGDADRIVYYYKDATG-HFHLIDGDKIATLISIFL 309
Cdd:PLN02895  240 LEVRNSGKEGEgvLNEGVGADFVQKEKVPPTGFASKDvGLRCASLDGDADRLVYFYVSSAGsKIDLLDGDKIASLFALFI 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 310 KELLAKVGET---------LHMAVVQTAYANGSSTRYLEETLKVPVHCVKTGVKHLHHKAQEFDVGVYFEANGHGTVLFS 380
Cdd:PLN02895  320 KEQLRILNGNgnekpeellVRLGVVQTAYANGASTAYLKQVLGLEVVCTPTGVKYLHEAAAEFDIGVYFEANGHGTVLFS 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 381 KAA----ETKIRQLAKEGKDDEKREAAKVLENMIDLINQTVGDAISDMLVIEAILALKGLTVQQWDAIYADLPNRLLKVQ 456
Cdd:PLN02895  400 ERFldwlEAAAAELSSKAKGSEAHKAARRLLAVSRLINQAVGDALSGLLLVEAILQYRGWSLAEWNALYQDLPSRQLKVK 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 457 VADRRVIVTTDAERCVVTPPGLQEKIDALVKKYKLSRAFVRPSGTEDVVRIYAEADTQENTDALAHEVSLAVYHLAGGKG 536
Cdd:PLN02895  480 VADRTAITTTDAETVVVRPAGLQDAIDAEVAKYPRGRAFVRPSGTEDVVRVYAEASTQEAADSLAREVARLVYDLLGGVG 559


                  ...
gi 1708852043 537 APP 539
Cdd:PLN02895  560 PPP 562
ManB COG1109
Phosphomannomutase [Carbohydrate transport and metabolism];
58-524 4.13e-30

Phosphomannomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440726 [Multi-domain]  Cd Length: 456  Bit Score: 123.00  E-value: 4.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043  58 GVMVTASHNPEEDNGVKLVDplgemlhpsweEYATQLANAEEEELQKIIidicqkaavnqhkdalvFIGRDTRPSSEKLs 137
Cdd:COG1109    95 GIMITASHNPPEYNGIKFFD-----------ADGGKLSPEEEKEIEALI-----------------EKEDFRRAEAEEI- 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 138 qsvidgisvlggqyhdyGLVTTPQlhymvccqntqgqygkAMLEGYYEKLSKAFTELIKQSPsagesqrhLKI--DCANG 215
Cdd:COG1109   146 -----------------GKVTRIE----------------DVLEAYIEALKSLVDEALRLRG--------LKVvvDCGNG 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 216 IGAlklsemePYFPK-------EVI-IHLFNDGTKekLNHLCG---------ADFVKVHqkpprGLDMkpnerCCSFDGD 278
Cdd:COG1109   185 AAG-------GVAPRllrelgaEVIvLNAEPDGNF--PNHNPNpepenledlIEAVKET-----GADL-----GIAFDGD 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 279 ADRI--VyyykDATGHFhlIDGDKIatlISIFLKELLAKvgeTLHMAVVQTAyangSSTRYLEETLK---VPVHCVKTGV 353
Cdd:COG1109   246 ADRLgvV----DEKGRF--LDGDQL---LALLARYLLEK---GPGGTVVVTV----MSSLALEDIAEkhgGEVVRTKVGF 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 354 KHLHHKAQEFDVGVYFEANGHgtVLFSKaaetkirqlakegkddekreaakvlenmidliNQTVGDAI-SDMLVIEaILA 432
Cdd:COG1109   310 KYIKEKMRETGAVLGGEESGG--IIFPD--------------------------------FVPTDDGIlAALLLLE-LLA 354

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 433 LKGLTVQQWDAIYADLPNRLLKVQVADRRVIVTTDAE-RCVVTPPGLQEKIDALvkKYKL---SRAFVRPSGTEDVVRIY 508
Cdd:COG1109   355 KQGKSLSELLAELPRYPQPEINVRVPDEEKIGAVMEKlREAVEDKEELDTIDGV--KVDLedgGWVLVRPSGTEPLLRVY 432

                         490
                  ....*....|....*.
gi 1708852043 509 AEADTQENTDALAHEV 524
Cdd:COG1109   433 AEAKDEEEAEELLAEL 448
glmM TIGR01455
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ...
 57-528 8.40e-24

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: 103.99  E-value: 8.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043  57 IGVMVTASHNPEEDNGVKLVDPLGEmlhpsweeyatQLANAEEEELQKIIIDICQKAAVNQHKdalvfIGRDTRpssekl 136
Cdd:TIGR01455  91 AGVMISASHNPYEDNGIKFFGPGGF-----------KLDDATEAAIEALLDEADPLPRPESEG-----LGRVKR------ 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 137 sqsVIDGIsvlggqyhdyglvttpqlhymvccqntqgqygkamleGYYeklskafTELIKQSPSAGESQRHLKI--DCAN 214
Cdd:TIGR01455 149 ---YPDAV-------------------------------------GRY-------IEFLKSTLPRGLTLSGLKVvlDCAN 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 215 GiGALKLSemepyfPK-------EVI-IHLFNDGTkeKLNHLCGADFVKVHQKPPR--GLDMKpnercCSFDGDADRIVY 284
Cdd:TIGR01455 182 G-AAYKVA------PHvfrelgaEVIaIGVEPDGL--NINDGCGSTHLDALQKAVRehGADLG-----IAFDGDADRVLA 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 285 YykDATGhfHLIDGDKIATLISIFLKEllakVGETLHMAVVQTAYANGSSTRYLEEtLKVPVHCVKTGVKHLHHKAQEFD 364
Cdd:TIGR01455 248 V--DANG--RIVDGDQILYIIARALKE----SGELAGNTVVATVMSNLGLERALEK-LGLTLIRTAVGDRYVLEEMRESG 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 365 VGVYFEANGHgtvlfskaaetkirqlakegkddekreaakvlenMIDLINQTVGDAISDMLVIEAILALKGLTVQQWDAI 444
Cdd:TIGR01455 319 YNLGGEQSGH----------------------------------IILLDYSTTGDGIVSALQVLTIMKKSGSTLSELAAE 364

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 445 YADLPNRLLKVQVADRRvivttdaeRCVVTPPGLQEKI----DALVKKyklSRAFVRPSGTEDVVRIYAEADTQENTDAL 520
Cdd:TIGR01455 365 FVPYPQTLVNVRVADRK--------LAAAEAPAVKAAIedaeAELGGT---GRILLRPSGTEPLIRVMVEAADEELVQQL 433


                  ....*...
gi 1708852043 521 AHEVSLAV 528
Cdd:TIGR01455 434 ADTLADVV 441
PGM_PMM_I pfam02878
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
116-166 2.32e-07

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


Pssm-ID: 427032  Cd Length: 138  Bit Score: 49.92  E-value: 2.32e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1708852043 116 NQHKDALVFIGRDTRPSSEKLSQSVIDGISVLGGQYHDYGLVTTPQLHYMV 166
Cdd:pfam02878  36 AQGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTPAVSFAT 86
 
Name Accession Description Interval E-value
PGM3 cd03086
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ...
 22-528 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: 868.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043  22 QYGTAGFRTKAEQLDHVMFRMGLLAVLRSKAVVS-TIGVMVTASHNPEEDNGVKLVDPLGEMLHPSWEEYATQLANAEEE 100
Cdd:cd03086     1 SYGTAGFRTKAELLDSVVFRVGILAALRSKKLGGkTIGVMITASHNPVEDNGVKIVDPDGEMLEESWEPYATQLANASDD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 101 ELQKIIIDIC--QKAAVNQHKDALVFIGRDTRPSSEKLSQSVIDGISVLGGQYHDYGLVTTPQLHYMVCCQNTQGQYGKA 178
Cdd:cd03086    81 ELLVLVLMLIsvKELNIDLSVPANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYLVRAANTEGAYGEP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 179 MLEGYYEKLSKAFTELIKQSPSAGESQRHLKIDCANGIGALKLSEMEPYFPKEVIIHLFNDGTK--EKLNHLCGADFVKV 256
Cdd:cd03086   161 TEEGYYEKLSKAFNELYNLLQDGGDEPEKLVVDCANGVGALKLKELLKRLKKGLSVKIINDGEEgpELLNDGCGADYVKT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 257 HQKPPRGLDMK-PNERCCSFDGDADRIVYYYKDATGHFHLIDGDKIATLISIFLKELLAKVGE--TLHMAVVQTAYANGS 333
Cdd:cd03086   241 KQKPPRGFELKpPGVRCCSFDGDADRLVYFYPDSSNKFHLLDGDKIATLFAKFIKELLKKAGEelKLTIGVVQTAYANGA 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 334 STRYLEETLKVPVHCVKTGVKHLHHKAQEFDVGVYFEANGHGTVLFSKAAETKIRQlaKEGKDDEKREAAKVLENMIDLI 413
Cdd:cd03086   321 STKYLEDVLKVPVVCTPTGVKHLHHAAEEFDIGVYFEANGHGTVLFSESALAKIEE--NSSLSDEQEKAAKTLLAFSRLI 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 414 NQTVGDAISDMLVIEAILALKGLTVQQWDAIYADLPNRLLKVQVADRRVIVTTDAERCVVTPPGLQEKIDALVKKYKLSR 493
Cdd:cd03086   399 NQTVGDAISDMLAVELILAALGWSPQDWDNLYTDLPNRQLKVKVPDRSVIKTTDAERRLVEPKGLQDKIDAIVAKYNNGR 478

                         490       500       510
                  ....*....|....*....|....*....|....*
gi 1708852043 494 AFVRPSGTEDVVRIYAEADTQENTDALAHEVSLAV 528
Cdd:cd03086   479 AFVRPSGTEDVVRVYAEAATQEEADELANEVAELV 513
PLN02895 PLN02895
phosphoacetylglucosamine mutase
 1-539 0e+00

phosphoacetylglucosamine mutase


Pssm-ID: 215485  Cd Length: 562  Bit Score: 666.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043   1 MDSEALKKYSALHPKPPGLTLQYGTAGFRTKAEQLDHVMFRMGLLAVLRSKAVVSTIGVMVTASHNPEEDNGVKLVDPLG 80
Cdd:PLN02895    4 IQRASLLAASSRFPPPQGVRFSYGTAGFRTDASLLESTVFRVGILAALRSLKTGAATGLMITASHNPVSDNGVKIVDPSG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043  81 EMLHPSWEEYATQLANAE-EEELQKIIIDICQKAAVNQHKD---ALVFIGRDTRPSSEKLSQSVIDGISVLGGQYHDYGL 156
Cdd:PLN02895   84 GMLPQAWEPFADALANAPdPDALVQLIREFVKKENIPAVGGnppAEVLLGRDTRPSGPALLAAALKGVRAIGARAVDMGI 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 157 VTTPQLHYMVCCQNtQGQygKAMLEGYYEKLSKAFTELIKQSPSAGESQRHLK---IDCANGIGALKLSEMEPYFPkEVI 233
Cdd:PLN02895  164 LTTPQLHWMVRAAN-KGM--KATESDYFEQLSSSFRALLDLIPNGSGDDRADDklvVDGANGVGAEKLETLKKALG-GLD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 234 IHLFNDGTKEK--LNHLCGADFVKVHQKPPRGLDMKP-NERCCSFDGDADRIVYYYKDATG-HFHLIDGDKIATLISIFL 309
Cdd:PLN02895  240 LEVRNSGKEGEgvLNEGVGADFVQKEKVPPTGFASKDvGLRCASLDGDADRLVYFYVSSAGsKIDLLDGDKIASLFALFI 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 310 KELLAKVGET---------LHMAVVQTAYANGSSTRYLEETLKVPVHCVKTGVKHLHHKAQEFDVGVYFEANGHGTVLFS 380
Cdd:PLN02895  320 KEQLRILNGNgnekpeellVRLGVVQTAYANGASTAYLKQVLGLEVVCTPTGVKYLHEAAAEFDIGVYFEANGHGTVLFS 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 381 KAA----ETKIRQLAKEGKDDEKREAAKVLENMIDLINQTVGDAISDMLVIEAILALKGLTVQQWDAIYADLPNRLLKVQ 456
Cdd:PLN02895  400 ERFldwlEAAAAELSSKAKGSEAHKAARRLLAVSRLINQAVGDALSGLLLVEAILQYRGWSLAEWNALYQDLPSRQLKVK 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 457 VADRRVIVTTDAERCVVTPPGLQEKIDALVKKYKLSRAFVRPSGTEDVVRIYAEADTQENTDALAHEVSLAVYHLAGGKG 536
Cdd:PLN02895  480 VADRTAITTTDAETVVVRPAGLQDAIDAEVAKYPRGRAFVRPSGTEDVVRVYAEASTQEAADSLAREVARLVYDLLGGVG 559


                  ...
gi 1708852043 537 APP 539
Cdd:PLN02895  560 PPP 562
PTZ00302 PTZ00302
N-acetylglucosamine-phosphate mutase; Provisional
 2-534 0e+00

N-acetylglucosamine-phosphate mutase; Provisional


Pssm-ID: 240352 [Multi-domain]  Cd Length: 585  Bit Score: 592.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043   2 DSEALKKYSALHPKppgltLQYGTAGFRTKAE--QLDHVMFRMGLLAVLRS--------KAVVSTIGVMVTASHNPEEDN 71
Cdd:PTZ00302   17 GSKFPLRHSAIENP-----LTYGTAGFRTKAElpPLEPVAYRVGILAALRSflyggkraKRGNKSVGVMITASHNPIQDN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043  72 GVKLVDPLGEMLHPSWEEYATQLANAE-EEELQKIIIDICQKAAVN-----------QHKDALVFIGRDTRPSSEKLSQS 139
Cdd:PTZ00302   92 GVKIIDPDGGMLEESWEKICTDFANARtGEDLVSVLMDCLTEHGIKlsnlkldlnksNCSKAKVHVGRDTRPSSPELVSA 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 140 VIDGISVLGGQYH-DYGLVTTPQLHYMVCCQNTQGQ-YGKAMLEGYYEKLSKAFTEL------IKQSPSAGESQRHLKID 211
Cdd:PTZ00302  172 LLRGLKLLIGSNVrNFGIVTTPQLHFLVAFANGLGVdVVESSDELYYAYLLAAFKELyrtlqeGGPVDLTQNNSKILVVD 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 212 CANGIGALKLSEMEPYFPK---EVIIHLFNDGTKEKLNHLCGADFVKVHQKPPRGLDMKPN---ERCCSFDGDADRIVYY 285
Cdd:PTZ00302  252 CANGVGGYKIKRFFEALKQlgiEIIPININCDEEELLNDKCGADYVQKTRKPPRAMKEWPGdeeTRVASFDGDADRLVYF 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 286 YKDATGH--FHLIDGDKIATLISIFLKELLAK--VGETLHMAVVQTAYANGSSTRYLEETLK-VPVHCVKTGVKHLHHKA 360
Cdd:PTZ00302  332 FPDKDGDdkWVLLDGDRIAILYAMLIKKLLGKiqLKKKLDIGVVQTAYANGASTNYLNELLGrLRVYCAPTGVKNLHPKA 411

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 361 QEFDVGVYFEANGHGTVLFSkaaETKIRQLAKEGKD-DEKREAAKVLENMIDLINQTVGDAISDMLVIEAILALKGLTVQ 439
Cdd:PTZ00302  412 HKYDIGIYFEANGHGTVLFN---EKALAEWAKFLAKqNALNSACRQLEKFLRLFNQTIGDAISDLLAVELALAFLGLSFQ 488

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 440 QWDAIYADLPNRLLKVQVADRRVIVTTDAERCVVTPPGLQEKIDALVKKYK-LSRAFVRPSGTEDVVRIYAEADTQENTD 518
Cdd:PTZ00302  489 DWLNLYTDLPSRQDKVTVKDRTLITNTEDETRLLEPKGLQDKIDAIVSKYDnAARAFIRPSGTEPVVRVYAEAPTLEQAD 568

                         570
                  ....*....|....*.
gi 1708852043 519 ALAHEVSLAVYHLAGG 534
Cdd:PTZ00302  569 ELANEVKGLVLRYCSG 584
phosphohexomutase cd03084
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ...
 23-525 1.11e-49

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: 174.85  E-value: 1.11e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043  23 YGTAGFRTKA--EQLDHVMFRMGllavlrsKAVVSTIGVMVTASHNPEEDNGVKLVDPLGEMLHPSWEEYATQLANAEEE 100
Cdd:cd03084     2 FGTSGVRGVVgdDITPETAVALG-------QAIGSTGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 101 elqkiiidicqkaavnqhkdalvfigrdTRPSSEKLSQSVidgisvlggqyhdyglvttpqlhymvccqntqgqYGKAML 180
Cdd:cd03084    75 ----------------------------PSAVAYELGGSV----------------------------------KAVDIL 92

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 181 EGYYEKLSKAFTELIKQspsagESQRHLKIDCANGIGALKLSEM-EPYFPKEVIIHLFNDGTKEKLNHLCGADfvKVHQK 259
Cdd:cd03084    93 QRYFEALKKLFDVAALS-----NKKFKVVVDSVNGVGGPIAPQLlEKLGAEVIPLNCEPDGNFGNINPDPGSE--TNLKQ 165

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 260 PPRGLDMKPNERCCSFDGDADRIVYYYKDATghfhLIDGDKIATLISIFLKELLAKVGetlhmAVVQTAYANGSSTRYLE 339
Cdd:cd03084   166 LLAVVKAEKADFGVAFDGDADRLIVVDENGG----FLDGDELLALLAVELFLTFNPRG-----GVVKTVVSSGALDKVAK 236

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 340 EtLKVPVHCVKTGVKHLHHKAQEFDVGVYFEANGHGTVLFskaaetkirqlakegkddekreaakvlenmidliNQTVGD 419
Cdd:cd03084   237 K-LGIKVIRTKTGFKWVGEAMQEGDVVLGGEESGGVIFPE----------------------------------FHPGRD 281

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 420 AISDMLVIEAILALKGLTVQQWDAIYADLPNRLLKVQvadrrvivttdaercvvtppglqekidalvkkyklSRAFVRPS 499
Cdd:cd03084   282 GISAALLLLEILANLGKSLSELFSELPRYYYIRLKVR-----------------------------------GWVLVRAS 326

                         490       500
                  ....*....|....*....|....*.
gi 1708852043 500 GTEDVVRIYAEADTQENTDALAHEVS 525
Cdd:cd03084   327 GTEPAIRIYAEADTQEDVEQIKKEAR 352
ManB COG1109
Phosphomannomutase [Carbohydrate transport and metabolism];
58-524 4.13e-30

Phosphomannomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440726 [Multi-domain]  Cd Length: 456  Bit Score: 123.00  E-value: 4.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043  58 GVMVTASHNPEEDNGVKLVDplgemlhpsweEYATQLANAEEEELQKIIidicqkaavnqhkdalvFIGRDTRPSSEKLs 137
Cdd:COG1109    95 GIMITASHNPPEYNGIKFFD-----------ADGGKLSPEEEKEIEALI-----------------EKEDFRRAEAEEI- 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 138 qsvidgisvlggqyhdyGLVTTPQlhymvccqntqgqygkAMLEGYYEKLSKAFTELIKQSPsagesqrhLKI--DCANG 215
Cdd:COG1109   146 -----------------GKVTRIE----------------DVLEAYIEALKSLVDEALRLRG--------LKVvvDCGNG 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 216 IGAlklsemePYFPK-------EVI-IHLFNDGTKekLNHLCG---------ADFVKVHqkpprGLDMkpnerCCSFDGD 278
Cdd:COG1109   185 AAG-------GVAPRllrelgaEVIvLNAEPDGNF--PNHNPNpepenledlIEAVKET-----GADL-----GIAFDGD 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 279 ADRI--VyyykDATGHFhlIDGDKIatlISIFLKELLAKvgeTLHMAVVQTAyangSSTRYLEETLK---VPVHCVKTGV 353
Cdd:COG1109   246 ADRLgvV----DEKGRF--LDGDQL---LALLARYLLEK---GPGGTVVVTV----MSSLALEDIAEkhgGEVVRTKVGF 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 354 KHLHHKAQEFDVGVYFEANGHgtVLFSKaaetkirqlakegkddekreaakvlenmidliNQTVGDAI-SDMLVIEaILA 432
Cdd:COG1109   310 KYIKEKMRETGAVLGGEESGG--IIFPD--------------------------------FVPTDDGIlAALLLLE-LLA 354

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 433 LKGLTVQQWDAIYADLPNRLLKVQVADRRVIVTTDAE-RCVVTPPGLQEKIDALvkKYKL---SRAFVRPSGTEDVVRIY 508
Cdd:COG1109   355 KQGKSLSELLAELPRYPQPEINVRVPDEEKIGAVMEKlREAVEDKEELDTIDGV--KVDLedgGWVLVRPSGTEPLLRVY 432

                         490
                  ....*....|....*.
gi 1708852043 509 AEADTQENTDALAHEV 524
Cdd:COG1109   433 AEAKDEEEAEELLAEL 448
GlmM cd05802
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ...
 57-525 4.59e-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: 4.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043  57 IGVMVTASHNPEEDNGVKLVDPLGemlhpsweeyaTQLANAEEEELQKIIIDicqkaavnqhkdalvfiGRDTRPSSEKL 136
Cdd:cd05802    90 AGVVISASHNPFEDNGIKFFSSDG-----------YKLPDEVEEEIEALIDK-----------------ELELPPTGEKI 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 137 SQSVIdgISVLGGQYHDYglvttpqlhymvcCQNTqgqYGKAMLEGyyeklskaftelikqspsagesqrhLKI--DCAN 214
Cdd:cd05802   142 GRVYR--IDDARGRYIEF-------------LKST---FPKDLLSG-------------------------LKIvlDCAN 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 215 G----IGALKLSEMEpyfpKEVIIhLFN--DGTKekLNHLCGADFVKVHQKP--PRGLDMKpnercCSFDGDADRIVYYy 286
Cdd:cd05802   179 GaaykVAPEVFRELG----AEVIV-INNapDGLN--INVNCGSTHPESLQKAvlENGADLG-----IAFDGDADRVIAV- 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 287 kDATGhfHLIDGDKIATLISIFLKELlakvGETLHMAVVQTAYANGSSTRYLEEtLKVPVHCVKTGVKHLHHKAQEFDVG 366
Cdd:cd05802   246 -DEKG--NIVDGDQILAICARDLKER----GRLKGNTVVGTVMSNLGLEKALKE-LGIKLVRTKVGDRYVLEEMLKHGAN 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 367 VYFEANGHgtvlfskaaetkirqlakegkddekreaakvlenMIDLINQTVGDAISDMLVIEAILALKGLTVQQWDAIYA 446
Cdd:cd05802   318 LGGEQSGH----------------------------------IIFLDHSTTGDGLLTALQLLAIMKRSGKSLSELASDMK 363

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 447 DLPNRLLKVQVADRRVIvttdaercvVTPPGLQEKIDALVKKYKLS-RAFVRPSGTEDVVRIYAEADTQENTDALAHEVS 525
Cdd:cd05802   364 LYPQVLVNVRVKDKKAL---------LENPRVQAAIAEAEKELGGEgRVLVRPSGTEPLIRVMVEGEDEELVEKLAEELA 434
glmM TIGR01455
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ...
 57-528 8.40e-24

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: 103.99  E-value: 8.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043  57 IGVMVTASHNPEEDNGVKLVDPLGEmlhpsweeyatQLANAEEEELQKIIIDICQKAAVNQHKdalvfIGRDTRpssekl 136
Cdd:TIGR01455  91 AGVMISASHNPYEDNGIKFFGPGGF-----------KLDDATEAAIEALLDEADPLPRPESEG-----LGRVKR------ 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 137 sqsVIDGIsvlggqyhdyglvttpqlhymvccqntqgqygkamleGYYeklskafTELIKQSPSAGESQRHLKI--DCAN 214
Cdd:TIGR01455 149 ---YPDAV-------------------------------------GRY-------IEFLKSTLPRGLTLSGLKVvlDCAN 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 215 GiGALKLSemepyfPK-------EVI-IHLFNDGTkeKLNHLCGADFVKVHQKPPR--GLDMKpnercCSFDGDADRIVY 284
Cdd:TIGR01455 182 G-AAYKVA------PHvfrelgaEVIaIGVEPDGL--NINDGCGSTHLDALQKAVRehGADLG-----IAFDGDADRVLA 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 285 YykDATGhfHLIDGDKIATLISIFLKEllakVGETLHMAVVQTAYANGSSTRYLEEtLKVPVHCVKTGVKHLHHKAQEFD 364
Cdd:TIGR01455 248 V--DANG--RIVDGDQILYIIARALKE----SGELAGNTVVATVMSNLGLERALEK-LGLTLIRTAVGDRYVLEEMRESG 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 365 VGVYFEANGHgtvlfskaaetkirqlakegkddekreaakvlenMIDLINQTVGDAISDMLVIEAILALKGLTVQQWDAI 444
Cdd:TIGR01455 319 YNLGGEQSGH----------------------------------IILLDYSTTGDGIVSALQVLTIMKKSGSTLSELAAE 364

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 445 YADLPNRLLKVQVADRRvivttdaeRCVVTPPGLQEKI----DALVKKyklSRAFVRPSGTEDVVRIYAEADTQENTDAL 520
Cdd:TIGR01455 365 FVPYPQTLVNVRVADRK--------LAAAEAPAVKAAIedaeAELGGT---GRILLRPSGTEPLIRVMVEAADEELVQQL 433


                  ....*...
gi 1708852043 521 AHEVSLAV 528
Cdd:TIGR01455 434 ADTLADVV 441
Arch_GlmM TIGR03990
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ...
 46-524 4.34e-21

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: 96.04  E-value: 4.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043  46 AVLRSKAVVstiGVMVTASHNPEEDNGVKLVDPLGEMLHPsweeyatqlanAEEEELQKIIIDIC-QKAAVNQhkdalvf 124
Cdd:TIGR03990  80 AVRELGADG---GIMITASHNPPEYNGIKLLNSDGTELSR-----------EQEEEIEEIAESGDfERADWDE------- 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 125 IGRDTRPSS--EKLSQSVIDGISVlggqyhdyglvttpqlhymvccqntqgqygkamlegyyeklskaftELIKqspsag 202
Cdd:TIGR03990 139 IGTVTSDEDaiDDYIEAILDKVDV----------------------------------------------EAIR------ 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 203 esQRHLK--IDCANGIGALKLsemePYFPKE--VIIHLFN---DG---------TKEKLNHLC------GADFVKVHqkp 260
Cdd:TIGR03990 167 --KKGFKvvVDCGNGAGSLTT----PYLLRElgCKVITLNcqpDGtfpgrnpepTPENLKDLSalvkatGADLGIAH--- 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 261 prgldmkpnerccsfDGDADRIVYYykDATGHFhlIDGDKiatLISIFLKELLAKVGETLhmaVVqtayaNGSSTRYLEE 340
Cdd:TIGR03990 238 ---------------DGDADRLVFI--DEKGRF--IGGDY---TLALFAKYLLEHGGGKV---VT-----NVSSSRAVED 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 341 TLK---VPVHCVKTGVKHLHHKAQEFDVGVYFEANGHgtVLFSKaaetkiRQLAkegkDDEKREAAKVLEnMIDLINQTV 417
Cdd:TIGR03990 288 VAErhgGEVIRTKVGEVNVAEKMKEEGAVFGGEGNGG--WIFPD------HHYC----RDGLMAAALFLE-LLAEEGKPL 354

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 418 GDAISDM----LVIEAIlalkGLTVQQWDAIYadlpnRLLKVQVADRRVIvTTDaercvvtppGLqeKIDalvkkYKLSR 493
Cdd:TIGR03990 355 SELLAELpkypMSKEKV----ELPDEDKEEVM-----EAVEEEFADAEID-TID---------GV--RID-----FEDGW 408

                         490       500       510
                  ....*....|....*....|....*....|.
gi 1708852043 494 AFVRPSGTEDVVRIYAEADTQENTDALAHEV 524
Cdd:TIGR03990 409 VLVRPSGTEPIVRIYAEAKTEERAEELLEEG 439
PGM_like1 cd03087
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ...
 58-524 1.86e-20

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: 93.79  E-value: 1.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043  58 GVMVTASHNPEEDNGVKLVDPLGemlhpsweeyaTQLANAEEEELQKIIIDicqkaavnqhkdalvfigRDTRPSSekls 137
Cdd:cd03087    86 GVMITASHNPPEYNGIKLVNPDG-----------TEFSREQEEEIEEIIFS------------------ERFRRVA---- 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 138 qsvidgisvlggqYHDYGLVTTPqlhymvccqntqgqygKAMLEGYYEKLSKAFTElikqspsagESQRHLK--IDCANG 215
Cdd:cd03087   133 -------------WDEVGSVRRE----------------DSAIDEYIEAILDKVDI---------DGGKGLKvvVDCGNG 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 216 IGALklseMEPYFPKE--VIIHLFN---DG---------TKEKLNHLC------GADFVKVHqkpprgldmkpnerccsf 275
Cdd:cd03087   175 AGSL----TTPYLLRElgCKVITLNanpDGffpgrppepTPENLSELMelvratGADLGIAH------------------ 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 276 DGDADRIVYYykDATGHFhlIDGDKIATLISiflKELLAKVGETLHMAVvqtayangSSTRYLEETLK---VPVHCVKTG 352
Cdd:cd03087   233 DGDADRAVFV--DEKGRF--IDGDKLLALLA---KYLLEEGGGKVVTPV--------DASMLVEDVVEeagGEVIRTPVG 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 353 VKHLHHKAQEFDVGVYFEANghGTVLFSKaaetkiRQLAKEGkddeKREAAKVLENMIDliNQTVGDAISDmlvIEAILA 432
Cdd:cd03087   298 DVHVAEEMIENGAVFGGEPN--GGWIFPD------HQLCRDG----IMTAALLLELLAE--EKPLSELLDE---LPKYPL 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 433 LKG---LTVQQWDAIYADLPNRLLKvqvADRRVIvTTDaercvvtppGLqeKIDalvkkYKLSRAFVRPSGTEDVVRIYA 509
Cdd:cd03087   361 LREkveCPDEKKEEVMEAVEEELSD---ADEDVD-TID---------GV--RIE-----YEDGWVLIRPSGTEPKIRITA 420

                         490
                  ....*....|....*
gi 1708852043 510 EADTQENTDALAHEV 524
Cdd:cd03087   421 EAKTEERAKELLEEG 435
PMM_PGM cd03089
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ...
 123-524 2.28e-11

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: 66.00  E-value: 2.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 123 VFIGRDTRPSSEKLSQSVIDGISVLGGQYHDYGLVTTPQLHY-----------MVC-------------CQNTQGQYG-- 176
Cdd:cd03089    39 VVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPVLYFatfhldadggvMITashnppeyngfkiVIGGGPLSGed 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 177 ----KAMLEGYYEKLSKAFTELIKQSPSA----------GESQRHLKI--DCANGIGALKLSEMEPYFPKEVIIhLFN-- 238
Cdd:cd03089   119 iqalRERAEKGDFAAATGRGSVEKVDILPdyidrllsdiKLGKRPLKVvvDAGNGAAGPIAPQLLEALGCEVIP-LFCep 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 239 DGT----------KEKLNHLC------GADFvkvhqkpprGLdmkpnerccSFDGDADRIVYYykDATGHFhlIDGDKia 302
Cdd:cd03089   198 DGTfpnhhpdptdPENLEDLIaavkenGADL---------GI---------AFDGDGDRLGVV--DEKGEI--IWGDR-- 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 303 tLISIFLKELLAKV-GETlhmaVVqtayANGSSTRYLEETLK----VPVHCvKTGVKHLHHKAQEFDVGVYFEANGHgtV 377
Cdd:cd03089   254 -LLALFARDILKRNpGAT----IV----YDVKCSRNLYDFIEeaggKPIMW-KTGHSFIKAKMKETGALLAGEMSGH--I 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 378 LFskaaetkirqlaKE---GKDDEKREAAKVLEnmidlinqtvgdaisdmlvieaILALKGLTVqqwDAIYADLPNRL-- 452
Cdd:cd03089   322 FF------------KDrwyGFDDGIYAALRLLE----------------------LLSKSGKTL---SELLADLPKYFst 364

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1708852043 453 --LKVQVAD---RRVI--VTTDAERCVVTPpglqEKIDALVKKYKLSRAFVRPSGTEDVVRIYAEADTQENTDALAHEV 524
Cdd:cd03089   365 peIRIPVTEedkFAVIerLKEHFEFPGAEI----IDIDGVRVDFEDGWGLVRASNTEPVLVLRFEADTEEGLEEIKAEL 439
PGM_like4 cd05803
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ...
 45-521 6.64e-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: 58.09  E-value: 6.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043  45 LAVLRSKAVVstiGVMVTASHNPEEDNGVKLVDPLGEMLHPswEEYATQLANAEEEELQKIiidicqkaavnqhkdalvf 124
Cdd:cd05803    81 VLVRQSQASG---GIIITASHNPPQWNGLKFIGPDGEFLTP--DEGEEVLSCAEAGSAQKA------------------- 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 125 igrdtrpsseklsqsvidgisvlggQYHDYGLVTTpqlhymvcCQNTQGQYGKAMlegyyekLSKAFTELIKQspsageS 204
Cdd:cd05803   137 -------------------------GYDQLGEVTF--------SEDAIAEHIDKV-------LALVDVDVIKI------R 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 205 QRHLK--IDCANGIGALKLSEM-EPYFPKEVIIHLFNDG--------TKEKLNHLCGAdfVKvhqkpprgldmkpnERCC 273
Cdd:cd05803   171 ERNFKvaVDSVNGAGGLLIPRLlEKLGCEVIVLNCEPTGlfphtpepLPENLTQLCAA--VK--------------ESGA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 274 SF----DGDADRIVyyykdatghfhLIDGDKIAtlisiflkellakVGE--TLHMAVVQ-TAYA--------NGSSTRYL 338
Cdd:cd05803   235 DVgfavDPDADRLA-----------LVDEDGRP-------------IGEeyTLALAVDYvLKYGgrkgpvvvNLSTSRAL 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 339 EETLK---VPVHCVKTGVKHLHHKAQEFDVGVYFEANGhGTVLFSkaaetkirqlAKEGKddekreaakvlenmidlinq 415
Cdd:cd05803   291 EDIARkhgVPVFRSAVGEANVVEKMKEVDAVIGGEGNG-GVILPD----------VHYGR-------------------- 339

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 416 tvgDAISDMLVIEAILALKGLTVQQWDAIYADLPNRLLKVQVA--DRRVIVTTDAERcvvTPPGLQEKIDALVKKYKLSR 493
Cdd:cd05803   340 ---DSLVGIALVLQLLAASGKPLSEIVDELPQYYISKTKVTIAgeALERLLKKLEAY---FKDAEASTLDGLRLDSEDSW 413

                         490       500
                  ....*....|....*....|....*...
gi 1708852043 494 AFVRPSGTEDVVRIYAEADTQENTDALA 521
Cdd:cd05803   414 VHVRPSNTEPIVRIIAEAPTQDEAEALA 441
PGM_like2 cd05800
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ...
 58-520 2.08e-07

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: 53.32  E-value: 2.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043  58 GVMVTASHNPEEDNGVKLVDPLGEMLHPSWeeyatqlANAEEEELQKIIIDICQKAAvnqhkdalvfigrdtrpssekls 137
Cdd:cd05800    94 GVMITASHNPPEYNGVKVKPAFGGSALPEI-------TAAIEARLASGEPPGLEARA----------------------- 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 138 qsvidgisvlggqyhdYGLVTTPQLhymvccqntqgqygkamLEGYYEKLSKAF-TELIKqspsagESQRHLKIDCANGI 216
Cdd:cd05800   144 ----------------EGLIETIDP-----------------KPDYLEALRSLVdLEAIR------EAGLKVVVDPMYGA 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 217 GALKLSEMEPYFPKEVI-IH-----LFNDGTKEKLNHLCGADFVKVHQKPPR-GLdmkpnerccSFDGDADRI--Vyyyk 287
Cdd:cd05800   185 GAGYLEELLRGAGVDVEeIRaerdpLFGGIPPEPIEKNLGELAEAVKEGGADlGL---------ATDGDADRIgaV---- 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 288 DATGHFhlIDGDKIatlISIFLKELLAKVGetLHMAVVQTAyangSSTRYLE---ETLKVPVHCVKTGVKHLHHKAQEFD 364
Cdd:cd05800   252 DEKGNF--LDPNQI---LALLLDYLLENKG--LRGPVVKTV----STTHLIDriaEKHGLPVYETPVGFKYIAEKMLEED 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 365 V--GVYfEANGHGtvlfskaaetkIRQLAKEGkddekreaakvlenmidlinqtvgDAI-SDMLVIEAIlALKGLTVqqw 441
Cdd:cd05800   321 VliGGE-ESGGLG-----------IRGHIPER------------------------DGIlAGLLLLEAV-AKTGKPL--- 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 442 DAIYADLPNRLLKVqVADRRVIVTTDAERCVVT--PPGLQEKIDALVK----------KYKL---SRAFVRPSGTEDVVR 506
Cdd:cd05800   361 SELVAELEEEYGPS-YYDRIDLRLTPAQKEAILekLKNEPPLSIAGGKvdevntidgvKLVLedgSWLLIRPSGTEPLLR 439

                         490
                  ....*....|....
gi 1708852043 507 IYAEADTQENTDAL 520
Cdd:cd05800   440 IYAEAPSPEKVEAL 453
PGM_PMM_I pfam02878
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
116-166 2.32e-07

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


Pssm-ID: 427032  Cd Length: 138  Bit Score: 49.92  E-value: 2.32e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1708852043 116 NQHKDALVFIGRDTRPSSEKLSQSVIDGISVLGGQYHDYGLVTTPQLHYMV 166
Cdd:pfam02878  36 AQGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTPAVSFAT 86
PGM_PMM_I pfam02878
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
58-100 2.66e-07

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


Pssm-ID: 427032  Cd Length: 138  Bit Score: 49.92  E-value: 2.66e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1708852043  58 GVMVTASHNPEEDNGVKLVDPLGEMLHPSWEEYATQLANAEEE 100
Cdd:pfam02878  94 GIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKEDF 136
PGM_PMM_IV pfam00408
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
476-528 3.18e-07

Phosphoglucomutase/phosphomannomutase, C-terminal domain;


Pssm-ID: 425666  Cd Length: 71  Bit Score: 47.65  E-value: 3.18e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1708852043 476 PGLQEKIDALVKKYKL--SRAFVRPSGTEDVVRIYAEADTQENTDALAHEVSLAV 528
Cdd:pfam00408  16 AAILKVFADAEKILGEdgRRLDVRPSGTEPVLRVMVEGDSDEELARLADEIADLL 70
glmM PRK10887
phosphoglucosamine mutase; Provisional
 58-532 3.47e-06

phosphoglucosamine mutase; Provisional


Pssm-ID: 236787  Cd Length: 443  Bit Score: 49.36  E-value: 3.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043  58 GVMVTASHNPEEDNGVKLVDPLGEMLHPSWEEyatqlanAEEEELQKIIidICQKAAvnqhkdalvFIGRDTRpssekls 137
Cdd:PRK10887   93 GIVISASHNPYYDNGIKFFSADGTKLPDEVEL-------AIEAELDKPL--TCVESA---------ELGKASR------- 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 138 qsvIDGisvlggqyhdyglvttpqlhymvccqnTQGQYgkamlegyyeklskafTELIKQSPSAGESQRHLKI--DCANG 215
Cdd:PRK10887  148 ---IND---------------------------AAGRY----------------IEFCKSTFPNELSLRGLKIvvDCANG 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 216 ----IGALKLSEMEpyfpKEVI-IHLFNDGTkeKLNHLCGADFVK------VHQKPPRGLdmkpnerccSFDGDADRIVY 284
Cdd:PRK10887  182 atyhIAPNVFRELG----AEVIaIGCEPNGL--NINDECGATDPEalqaavLAEKADLGI---------AFDGDGDRVIM 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 285 YykDATGhfHLIDGDKIATLISiflKELLAKvGEtLHMAVVQTAYANGSSTRYLEEtLKVPVHCVKTGVKHLHHKAQEFD 364
Cdd:PRK10887  247 V--DHLG--NLVDGDQLLYIIA---RDRLRR-GQ-LRGGVVGTLMSNMGLELALKQ-LGIPFVRAKVGDRYVLEKLQEKG 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 365 VGVYFEANGHgtvlfskaaetkirqlakegkddekreaakvlenMIDLINQTVGDAI-SDMLVIEAiLALKGLTVQQWDA 443
Cdd:PRK10887  317 WRLGGENSGH----------------------------------ILCLDKTTTGDGIvAALQVLAA-MVRSGMSLADLCS 361

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708852043 444 IYADLPNRLLKVQVADRRVIVTTDaercvvtpPGLQEKIDAlVKKyKL---SRAFVRPSGTEDVVRIYAEADTQENTDAL 520
Cdd:PRK10887  362 GMKLFPQVLINVRFKPGADDPLES--------EAVKAALAE-VEA-ELggrGRVLLRKSGTEPLIRVMVEGEDEAQVTAL 431

                         490
                  ....*....|..
gi 1708852043 521 AHEVSLAVYHLA 532
Cdd:PRK10887  432 AERIADAVKAAA 443
PGM2 cd05799
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ...
 58-74 5.10e-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: 45.96  E-value: 5.10e-05
                          10
                  ....*....|....*..
gi 1708852043  58 GVMVTASHNPEEDNGVK 74
Cdd:cd05799   100 GIMITASHNPKEYNGYK 116
PTZ00150 PTZ00150
phosphoglucomutase-2-like protein; Provisional
 57-74 1.46e-04

phosphoglucomutase-2-like protein; Provisional


Pssm-ID: 240294  Cd Length: 584  Bit Score: 44.67  E-value: 1.46e-04
                          10
                  ....*....|....*...
gi 1708852043  57 IGVMVTASHNPEEDNGVK 74
Cdd:PTZ00150  143 AGVMVTASHNPKEDNGYK 160
ManB cd03088
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ...
 123-164 4.95e-04

ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose 6-phosphate to mannose-1-phosphate in the second of three steps in the GDP-mannose pathway, in which GDP-D-mannose is synthesized from fructose-6-phosphate. In Mycobacterium tuberculosis, the causative agent of tuberculosis, PMM is involved in the biosynthesis of mannosylated lipoglycans that participate in the association of mycobacteria with host macrophage phagocytic receptors. ManB belongs to the 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 the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), 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: 100090  Cd Length: 459  Bit Score: 42.57  E-value: 4.95e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1708852043 123 VFIGRDTRPSSEKLSQSVIDGISVLGGQYHDYGLVTTPQLHY 164
Cdd:cd03088    39 VAVGRDLRPSSPRIAAACAAALRDAGFRVVDCGAVPTPALAL 80
PLN02371 PLN02371
phosphoglucosamine mutase family protein
 123-160 7.37e-04

phosphoglucosamine mutase family protein


Pssm-ID: 215211 [Multi-domain]  Cd Length: 583  Bit Score: 42.35  E-value: 7.37e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1708852043 123 VFIGRDTRPSSEKLSQSVIDGISVLGGQYHDYGLVTTP 160
Cdd:PLN02371  118 VSVGRDPRISGPRLADAVFAGLASAGLDVVDMGLATTP 155
 
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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