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Conserved domains on  [gi|255522941|ref|NP_001157218|]
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phosphoacetylglucosamine mutase isoform 2 [Mus musculus]

Protein Classification

phosphoacetylglucosamine mutase( domain architecture ID 10122986)

phosphoacetylglucosamine mutase 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

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 ...
 22-486 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: 751.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  22 QYGTAGFRTNAQHLDHIMFRMGLLAVLRSKQTRS-TIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLASAEEQ 100
Cdd:cd03086    1 SYGTAGFRTKAELLDSVVFRVGILAALRSKKLGGkTIGVMITASHNPVEDNGVKIVDPDGEMLEESWEPYATQLANASDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 101 DVRQVLAAI--VEKEAVDLTQTAFVVIARDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNSGGRYGQA 178
Cdd:cd03086   81 ELLVLVLMLisVKELNIDLSVPANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYLVRAANTEGAYGEP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 179 TVEGYCQKLSKAFVDLTNQVSCSGDVKRSVKVDCANGIGALKLREMEHYFSRGLSVLLFNDG--TQGRLNHLCGADFVKS 256
Cdd:cd03086  161 TEEGYYEKLSKAFNELYNLLQDGGDEPEKLVVDCANGVGALKLKELLKRLKKGLSVKIINDGeeGPELLNDGCGADYVKT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 257 QQKPPQGIEMK-SGERCCSFDGDADRIVYYYCDADGHFHLIDGDKIATLISSFLKELL--LEIGESVNLGVVQTAYANGS 333
Cdd:cd03086  241 KQKPPRGFELKpPGVRCCSFDGDADRLVYFYPDSSNKFHLLDGDKIATLFAKFIKELLkkAGEELKLTIGVVQTAYANGA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 334 STRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFSEAVEVKIKRlAQELDDGKGKAARTLASIIDLFN 413
Cdd:cd03086  321 STKYLEDVLKVPVVCTPTGVKHLHHAAEEFDIGVYFEANGHGTVLFSESALAKIEE-NSSLSDEQEKAAKTLLAFSRLIN 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 414 Q-----------------------------------------VADRRVISTTDAERQAVTPPGLQEAINDLVKKYTLARA 452
Cdd:cd03086  400 QtvgdaisdmlavelilaalgwspqdwdnlytdlpnrqlkvkVPDRSVIKTTDAERRLVEPKGLQDKIDAIVAKYNNGRA 479

                        490       500       510
                 ....*....|....*....|....*....|....
gi 255522941 453 FVRPSGTEDIVRVYAEANSQESADRLAYEVSLLV 486
Cdd:cd03086  480 FVRPSGTEDVVRVYAEAATQEEADELANEVAELV 513
 
Name Accession Description Interval E-value
PGM3 cd03086
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ...
 22-486 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: 751.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  22 QYGTAGFRTNAQHLDHIMFRMGLLAVLRSKQTRS-TIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLASAEEQ 100
Cdd:cd03086    1 SYGTAGFRTKAELLDSVVFRVGILAALRSKKLGGkTIGVMITASHNPVEDNGVKIVDPDGEMLEESWEPYATQLANASDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 101 DVRQVLAAI--VEKEAVDLTQTAFVVIARDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNSGGRYGQA 178
Cdd:cd03086   81 ELLVLVLMLisVKELNIDLSVPANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYLVRAANTEGAYGEP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 179 TVEGYCQKLSKAFVDLTNQVSCSGDVKRSVKVDCANGIGALKLREMEHYFSRGLSVLLFNDG--TQGRLNHLCGADFVKS 256
Cdd:cd03086  161 TEEGYYEKLSKAFNELYNLLQDGGDEPEKLVVDCANGVGALKLKELLKRLKKGLSVKIINDGeeGPELLNDGCGADYVKT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 257 QQKPPQGIEMK-SGERCCSFDGDADRIVYYYCDADGHFHLIDGDKIATLISSFLKELL--LEIGESVNLGVVQTAYANGS 333
Cdd:cd03086  241 KQKPPRGFELKpPGVRCCSFDGDADRLVYFYPDSSNKFHLLDGDKIATLFAKFIKELLkkAGEELKLTIGVVQTAYANGA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 334 STRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFSEAVEVKIKRlAQELDDGKGKAARTLASIIDLFN 413
Cdd:cd03086  321 STKYLEDVLKVPVVCTPTGVKHLHHAAEEFDIGVYFEANGHGTVLFSESALAKIEE-NSSLSDEQEKAAKTLLAFSRLIN 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 414 Q-----------------------------------------VADRRVISTTDAERQAVTPPGLQEAINDLVKKYTLARA 452
Cdd:cd03086  400 QtvgdaisdmlavelilaalgwspqdwdnlytdlpnrqlkvkVPDRSVIKTTDAERRLVEPKGLQDKIDAIVAKYNNGRA 479

                        490       500       510
                 ....*....|....*....|....*....|....
gi 255522941 453 FVRPSGTEDIVRVYAEANSQESADRLAYEVSLLV 486
Cdd:cd03086  480 FVRPSGTEDVVRVYAEAATQEEADELANEVAELV 513
PLN02895 PLN02895
phosphoacetylglucosamine mutase
 1-497 0e+00

phosphoacetylglucosamine mutase


Pssm-ID: 215485  Cd Length: 562  Bit Score: 588.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941   1 MDLEAVCKRSALHAKPQGLILQYGTAGFRTNAQHLDHIMFRMGLLAVLRSKQTRSTIGVMVTASHNPEEDNGVKLVDPLG 80
Cdd:PLN02895   4 IQRASLLAASSRFPPPQGVRFSYGTAGFRTDASLLESTVFRVGILAALRSLKTGAATGLMITASHNPVSDNGVKIVDPSG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  81 EMLAPSWEEHATCLASAE-EQDVRQVLAAIVEKEAVDL---TQTAFVVIARDTRPSSEKLSQSVIDGVTVLGGQFHDYGL 156
Cdd:PLN02895  84 GMLPQAWEPFADALANAPdPDALVQLIREFVKKENIPAvggNPPAEVLLGRDTRPSGPALLAAALKGVRAIGARAVDMGI 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 157 LTTPQLHYMVYCRNSGGRygqATVEGYCQKLSKAFVDLTNQVSCSGDVKRSVK---VDCANGIGALKLREMEHYFSrGLS 233
Cdd:PLN02895 164 LTTPQLHWMVRAANKGMK---ATESDYFEQLSSSFRALLDLIPNGSGDDRADDklvVDGANGVGAEKLETLKKALG-GLD 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 234 VLLFNDGTQGR--LNHLCGADFVKSQQKPPQGIEMK-SGERCCSFDGDADRIVYYYCDADG-HFHLIDGDKIATLISSFL 309
Cdd:PLN02895 240 LEVRNSGKEGEgvLNEGVGADFVQKEKVPPTGFASKdVGLRCASLDGDADRLVYFYVSSAGsKIDLLDGDKIASLFALFI 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 310 KELLLEIGES---------VNLGVVQTAYANGSSTRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFS 380
Cdd:PLN02895 320 KEQLRILNGNgnekpeellVRLGVVQTAYANGASTAYLKQVLGLEVVCTPTGVKYLHEAAAEFDIGVYFEANGHGTVLFS 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 381 EAVEVKIKRLAQELDDGKG-----KAARTLASIIDLFNQ----------------------------------------- 414
Cdd:PLN02895 400 ERFLDWLEAAAAELSSKAKgseahKAARRLLAVSRLINQavgdalsglllveailqyrgwslaewnalyqdlpsrqlkvk 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 415 VADRRVISTTDAERQAVTPPGLQEAINDLVKKYTLARAFVRPSGTEDIVRVYAEANSQESADRLAYEVSLLVFQLAGGIG 494
Cdd:PLN02895 480 VADRTAITTTDAETVVVRPAGLQDAIDAEVAKYPRGRAFVRPSGTEDVVRVYAEASTQEAADSLAREVARLVYDLLGGVG 559


                 ...
gi 255522941 495 ERP 497
Cdd:PLN02895 560 PPP 562
ManB COG1109
Phosphomannomutase [Carbohydrate transport and metabolism];
58-486 3.65e-26

Phosphomannomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440726 [Multi-domain]  Cd Length: 456  Bit Score: 110.68  E-value: 3.65e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  58 GVMVTASHNPEEDNGVKLVDPLGEMLAPSWEehatclasaeeqdvrQVLAAIVEKEAVDltqtafvviardtRPSSEKLs 137
Cdd:COG1109   95 GIMITASHNPPEYNGIKFFDADGGKLSPEEE---------------KEIEALIEKEDFR-------------RAEAEEI- 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 138 qsvidgvtvlggqfhdyGLLTTPQlhymvycrnsggrygqATVEGYCQKLSKAFVDLTNqvscsgdvKRSVKV--DCANG 215
Cdd:COG1109  146 -----------------GKVTRIE----------------DVLEAYIEALKSLVDEALR--------LRGLKVvvDCGNG 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 216 IGALKLREMehyFSR-GLSVLLFN---DGTQGrlNHLC-----------------GADFvksqqkppqGIemksgerccS 274
Cdd:COG1109  185 AAGGVAPRL---LRElGAEVIVLNaepDGNFP--NHNPnpepenledlieavketGADL---------GI---------A 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 275 FDGDADRIVYyyCDADGHFhlIDGDKIATLISsflkELLLEIGEsvNLGVVQTAyangSSTRYLEEVMK---VPVYCTKT 351
Cdd:COG1109  242 FDGDADRLGV--VDEKGRF--LDGDQLLALLA----RYLLEKGP--GGTVVVTV----MSSLALEDIAEkhgGEVVRTKV 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 352 GVKHLHHKAQEFD--IGvyFEANGHgtALFSEAVEVK-----IKRLAQELDdgkgKAARTLASIIDLFNQVADRRV-IST 423
Cdd:COG1109  308 GFKYIKEKMRETGavLG--GEESGG--IIFPDFVPTDdgilaALLLLELLA----KQGKSLSELLAELPRYPQPEInVRV 379

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255522941 424 TDAE---------RQAVTPPGLQEAINDLvkKYTLA---RAFVRPSGTEDIVRVYAEANSQESADRLAYEVSLLV 486
Cdd:COG1109  380 PDEEkigavmeklREAVEDKEELDTIDGV--KVDLEdggWVLVRPSGTEPLLRVYAEAKDEEEAEELLAELAELV 452
glmM TIGR01455
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ...
 53-479 2.21e-23

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: 102.44  E-value: 2.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941   53 TRSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLASAEEQdvrqvlaaivekeavdltqtafvviarDTRPS 132
Cdd:TIGR01455  87 LRADAGVMISASHNPYEDNGIKFFGPGGFKLDDATEAAIEALLDEADP---------------------------LPRPE 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  133 SEKLsqsvidgvtvlggqfhdygllttpqlhymvycrnsGGRYGQATVEGYCQKLSKAfvDLTNQVSCSGdvkRSVKVDC 212
Cdd:TIGR01455 140 SEGL-----------------------------------GRVKRYPDAVGRYIEFLKS--TLPRGLTLSG---LKVVLDC 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  213 ANGiGALKLREMEhYFSRGLSVLLFNDGTQGR-LNHLCGADFVKSQQKPPQGIEMKSGercCSFDGDADRIVyyYCDADG 291
Cdd:TIGR01455 180 ANG-AAYKVAPHV-FRELGAEVIAIGVEPDGLnINDGCGSTHLDALQKAVREHGADLG---IAFDGDADRVL--AVDANG 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  292 hfHLIDGDKIATLISSFLKELlleiGESVNLGVVQTAYANGSSTRYLEEvMKVPVYCTKTGVKHLHHKAQEFDIGVYFEA 371
Cdd:TIGR01455 253 --RIVDGDQILYIIARALKES----GELAGNTVVATVMSNLGLERALEK-LGLTLIRTAVGDRYVLEEMRESGYNLGGEQ 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  372 NGH---------G----TALFSEAVEVKIKRLAQELDDGKGKAARTLASIidlfnQVADRRvisttdaeRQAVTPPGLQE 438
Cdd:TIGR01455 326 SGHiilldysttGdgivSALQVLTIMKKSGSTLSELAAEFVPYPQTLVNV-----RVADRK--------LAAAEAPAVKA 392

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 255522941  439 AINDLVKKY-TLARAFVRPSGTEDIVRVYAEANSQESADRLA 479
Cdd:TIGR01455 393 AIEDAEAELgGTGRILLRPSGTEPLIRVMVEAADEELVQQLA 434
PGM_PMM_IV pfam00408
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
434-486 4.13e-08

Phosphoglucomutase/phosphomannomutase, C-terminal domain;


Pssm-ID: 425666  Cd Length: 71  Bit Score: 49.96  E-value: 4.13e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 255522941  434 PGLQEAINDLVKKYTL--ARAFVRPSGTEDIVRVYAEANSQESADRLAYEVSLLV 486
Cdd:pfam00408  16 AAILKVFADAEKILGEdgRRLDVRPSGTEPVLRVMVEGDSDEELARLADEIADLL 70
 
Name Accession Description Interval E-value
PGM3 cd03086
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ...
 22-486 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: 751.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  22 QYGTAGFRTNAQHLDHIMFRMGLLAVLRSKQTRS-TIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLASAEEQ 100
Cdd:cd03086    1 SYGTAGFRTKAELLDSVVFRVGILAALRSKKLGGkTIGVMITASHNPVEDNGVKIVDPDGEMLEESWEPYATQLANASDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 101 DVRQVLAAI--VEKEAVDLTQTAFVVIARDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNSGGRYGQA 178
Cdd:cd03086   81 ELLVLVLMLisVKELNIDLSVPANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYLVRAANTEGAYGEP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 179 TVEGYCQKLSKAFVDLTNQVSCSGDVKRSVKVDCANGIGALKLREMEHYFSRGLSVLLFNDG--TQGRLNHLCGADFVKS 256
Cdd:cd03086  161 TEEGYYEKLSKAFNELYNLLQDGGDEPEKLVVDCANGVGALKLKELLKRLKKGLSVKIINDGeeGPELLNDGCGADYVKT 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 257 QQKPPQGIEMK-SGERCCSFDGDADRIVYYYCDADGHFHLIDGDKIATLISSFLKELL--LEIGESVNLGVVQTAYANGS 333
Cdd:cd03086  241 KQKPPRGFELKpPGVRCCSFDGDADRLVYFYPDSSNKFHLLDGDKIATLFAKFIKELLkkAGEELKLTIGVVQTAYANGA 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 334 STRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFSEAVEVKIKRlAQELDDGKGKAARTLASIIDLFN 413
Cdd:cd03086  321 STKYLEDVLKVPVVCTPTGVKHLHHAAEEFDIGVYFEANGHGTVLFSESALAKIEE-NSSLSDEQEKAAKTLLAFSRLIN 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 414 Q-----------------------------------------VADRRVISTTDAERQAVTPPGLQEAINDLVKKYTLARA 452
Cdd:cd03086  400 QtvgdaisdmlavelilaalgwspqdwdnlytdlpnrqlkvkVPDRSVIKTTDAERRLVEPKGLQDKIDAIVAKYNNGRA 479

                        490       500       510
                 ....*....|....*....|....*....|....
gi 255522941 453 FVRPSGTEDIVRVYAEANSQESADRLAYEVSLLV 486
Cdd:cd03086  480 FVRPSGTEDVVRVYAEAATQEEADELANEVAELV 513
PLN02895 PLN02895
phosphoacetylglucosamine mutase
 1-497 0e+00

phosphoacetylglucosamine mutase


Pssm-ID: 215485  Cd Length: 562  Bit Score: 588.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941   1 MDLEAVCKRSALHAKPQGLILQYGTAGFRTNAQHLDHIMFRMGLLAVLRSKQTRSTIGVMVTASHNPEEDNGVKLVDPLG 80
Cdd:PLN02895   4 IQRASLLAASSRFPPPQGVRFSYGTAGFRTDASLLESTVFRVGILAALRSLKTGAATGLMITASHNPVSDNGVKIVDPSG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  81 EMLAPSWEEHATCLASAE-EQDVRQVLAAIVEKEAVDL---TQTAFVVIARDTRPSSEKLSQSVIDGVTVLGGQFHDYGL 156
Cdd:PLN02895  84 GMLPQAWEPFADALANAPdPDALVQLIREFVKKENIPAvggNPPAEVLLGRDTRPSGPALLAAALKGVRAIGARAVDMGI 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 157 LTTPQLHYMVYCRNSGGRygqATVEGYCQKLSKAFVDLTNQVSCSGDVKRSVK---VDCANGIGALKLREMEHYFSrGLS 233
Cdd:PLN02895 164 LTTPQLHWMVRAANKGMK---ATESDYFEQLSSSFRALLDLIPNGSGDDRADDklvVDGANGVGAEKLETLKKALG-GLD 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 234 VLLFNDGTQGR--LNHLCGADFVKSQQKPPQGIEMK-SGERCCSFDGDADRIVYYYCDADG-HFHLIDGDKIATLISSFL 309
Cdd:PLN02895 240 LEVRNSGKEGEgvLNEGVGADFVQKEKVPPTGFASKdVGLRCASLDGDADRLVYFYVSSAGsKIDLLDGDKIASLFALFI 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 310 KELLLEIGES---------VNLGVVQTAYANGSSTRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFS 380
Cdd:PLN02895 320 KEQLRILNGNgnekpeellVRLGVVQTAYANGASTAYLKQVLGLEVVCTPTGVKYLHEAAAEFDIGVYFEANGHGTVLFS 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 381 EAVEVKIKRLAQELDDGKG-----KAARTLASIIDLFNQ----------------------------------------- 414
Cdd:PLN02895 400 ERFLDWLEAAAAELSSKAKgseahKAARRLLAVSRLINQavgdalsglllveailqyrgwslaewnalyqdlpsrqlkvk 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 415 VADRRVISTTDAERQAVTPPGLQEAINDLVKKYTLARAFVRPSGTEDIVRVYAEANSQESADRLAYEVSLLVFQLAGGIG 494
Cdd:PLN02895 480 VADRTAITTTDAETVVVRPAGLQDAIDAEVAKYPRGRAFVRPSGTEDVVRVYAEASTQEAADSLAREVARLVYDLLGGVG 559


                 ...
gi 255522941 495 ERP 497
Cdd:PLN02895 560 PPP 562
PTZ00302 PTZ00302
N-acetylglucosamine-phosphate mutase; Provisional
 21-492 5.51e-172

N-acetylglucosamine-phosphate mutase; Provisional


Pssm-ID: 240352 [Multi-domain]  Cd Length: 585  Bit Score: 497.25  E-value: 5.51e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  21 LQYGTAGFRTNAQ--HLDHIMFRMGLLAVLRS--------KQTRSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEH 90
Cdd:PTZ00302  31 LTYGTAGFRTKAElpPLEPVAYRVGILAALRSflyggkraKRGNKSVGVMITASHNPIQDNGVKIIDPDGGMLEESWEKI 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  91 ATCLASAE-EQDVRQVLAAIVEKEAVDLTQ-----------TAFVVIARDTRPSSEKLSQSVIDGVTVLGGQFH-DYGLL 157
Cdd:PTZ00302 111 CTDFANARtGEDLVSVLMDCLTEHGIKLSNlkldlnksncsKAKVHVGRDTRPSSPELVSALLRGLKLLIGSNVrNFGIV 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 158 TTPQLHYMVYCRNSGGR-YGQATVEGYCQKLSKAFVDLTN------QVSCSGDVKRSVKVDCANGIGALKLREMEHYF-- 228
Cdd:PTZ00302 191 TTPQLHFLVAFANGLGVdVVESSDELYYAYLLAAFKELYRtlqeggPVDLTQNNSKILVVDCANGVGGYKIKRFFEALkq 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 229 -SRGLSVLLFNDGTQGRLNHLCGADFVKSQQKPPQGIEMK---SGERCCSFDGDADRIVYYY--CDADGHFHLIDGDKIA 302
Cdd:PTZ00302 271 lGIEIIPININCDEEELLNDKCGADYVQKTRKPPRAMKEWpgdEETRVASFDGDADRLVYFFpdKDGDDKWVLLDGDRIA 350

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 303 TLISSFLKELLLEIGESVNL--GVVQTAYANGSSTRYLEEVMK-VPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALF 379
Cdd:PTZ00302 351 ILYAMLIKKLLGKIQLKKKLdiGVVQTAYANGASTNYLNELLGrLRVYCAPTGVKNLHPKAHKYDIGIYFEANGHGTVLF 430

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 380 SEAVevkIKRLAQELDD--GKGKAARTLASIIDLFNQ-----------------------------------------VA 416
Cdd:PTZ00302 431 NEKA---LAEWAKFLAKqnALNSACRQLEKFLRLFNQtigdaisdllavelalaflglsfqdwlnlytdlpsrqdkvtVK 507

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255522941 417 DRRVISTTDAERQAVTPPGLQEAINDLVKKY-TLARAFVRPSGTEDIVRVYAEANSQESADRLAYEVSLLVFQLAGG 492
Cdd:PTZ00302 508 DRTLITNTEDETRLLEPKGLQDKIDAIVSKYdNAARAFIRPSGTEPVVRVYAEAPTLEQADELANEVKGLVLRYCSG 584
phosphohexomutase cd03084
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ...
 23-486 1.05e-42

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: 155.21  E-value: 1.05e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  23 YGTAGFR--TNAQHLDHIMFRMGLLAVlrskqtrSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLASAEEQ 100
Cdd:cd03084    2 FGTSGVRgvVGDDITPETAVALGQAIG-------STGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 101 DVRQVLAAIVEKEAVDltqtafvviardtrpsseklsqsvidgvtvlggqfhdygllttpqlhymvycrnsggrygqaTV 180
Cdd:cd03084   75 PSAVAYELGGSVKAVD--------------------------------------------------------------IL 92

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 181 EGYCQKL-SKAFVDLTNQVscsgdvKRSVKVDCANGIGALKLREM-EHYfsrGLSVLLFN---DGTQGRLNHLCGAD--- 252
Cdd:cd03084   93 QRYFEALkKLFDVAALSNK------KFKVVVDSVNGVGGPIAPQLlEKL---GAEVIPLNcepDGNFGNINPDPGSEtnl 163

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 253 ----FVKSQQKPPQGIemksgerccSFDGDADRIVYYycdaDGHFHLIDGDKIATLISsflKELLLEIGEsvNLGVVQTA 328
Cdd:cd03084  164 kqllAVVKAEKADFGV---------AFDGDADRLIVV----DENGGFLDGDELLALLA---VELFLTFNP--RGGVVKTV 225

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 329 YANGSSTRYLEEvMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTalFSEAVEVKikrlaqeldDGKGKAARTLA-- 406
Cdd:cd03084  226 VSSGALDKVAKK-LGIKVIRTKTGFKWVGEAMQEGDVVLGGEESGGVI--FPEFHPGR---------DGISAALLLLEil 293

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 407 -----SIIDLFNQVADRrvisttdaerqavtppglqeaINDLVKKYtlARAFVRPSGTEDIVRVYAEANSQESADRLAYE 481
Cdd:cd03084  294 anlgkSLSELFSELPRY---------------------YYIRLKVR--GWVLVRASGTEPAIRIYAEADTQEDVEQIKKE 350


                 ....*
gi 255522941 482 VSLLV 486
Cdd:cd03084  351 ARELV 355
GlmM cd05802
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ...
 51-483 3.13e-26

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: 110.65  E-value: 3.13e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  51 KQTRSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHatclasaeeqdvrqvLAAIVEKEavdltqtafvviaRDTR 130
Cdd:cd05802   84 RKLRADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVEEE---------------IEALIDKE-------------LELP 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 131 PSSEKLsqsvidgvtvlgGQFHDYgllTTPQLHYMVYCRNSggrygqatvegycqkLSKAFVDltnqvscsgDVKrsVKV 210
Cdd:cd05802  136 PTGEKI------------GRVYRI---DDARGRYIEFLKST---------------FPKDLLS---------GLK--IVL 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 211 DCANG----IGALKLREMehyfsrGLSVLLFN---DGTqgRLNHLCGADFVKSQQKppqgiEMKSgERC---CSFDGDAD 280
Cdd:cd05802  175 DCANGaaykVAPEVFREL------GAEVIVINnapDGL--NINVNCGSTHPESLQK-----AVLE-NGAdlgIAFDGDAD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 281 RIVYyyCDADGHfhLIDGDKIATLISSFLKELlleiGESVNLGVVQTAYANGSSTRYLEEvMKVPVYCTKTGVKHLHHKA 360
Cdd:cd05802  241 RVIA--VDEKGN--IVDGDQILAICARDLKER----GRLKGNTVVGTVMSNLGLEKALKE-LGIKLVRTKVGDRYVLEEM 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 361 QEFDIGVYFEANGH---------GTALFSeAVEVkIKRLAQElddgkGKAARTLASIIDLFNQV-ADRRVISTTDAErqa 430
Cdd:cd05802  312 LKHGANLGGEQSGHiifldhsttGDGLLT-ALQL-LAIMKRS-----GKSLSELASDMKLYPQVlVNVRVKDKKALL--- 381

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 255522941 431 vTPPGLQEAINDLVKKytLA---RAFVRPSGTEDIVRVYAEANSQESADRLAYEVS 483
Cdd:cd05802  382 -ENPRVQAAIAEAEKE--LGgegRVLVRPSGTEPLIRVMVEGEDEELVEKLAEELA 434
ManB COG1109
Phosphomannomutase [Carbohydrate transport and metabolism];
58-486 3.65e-26

Phosphomannomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440726 [Multi-domain]  Cd Length: 456  Bit Score: 110.68  E-value: 3.65e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  58 GVMVTASHNPEEDNGVKLVDPLGEMLAPSWEehatclasaeeqdvrQVLAAIVEKEAVDltqtafvviardtRPSSEKLs 137
Cdd:COG1109   95 GIMITASHNPPEYNGIKFFDADGGKLSPEEE---------------KEIEALIEKEDFR-------------RAEAEEI- 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 138 qsvidgvtvlggqfhdyGLLTTPQlhymvycrnsggrygqATVEGYCQKLSKAFVDLTNqvscsgdvKRSVKV--DCANG 215
Cdd:COG1109  146 -----------------GKVTRIE----------------DVLEAYIEALKSLVDEALR--------LRGLKVvvDCGNG 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 216 IGALKLREMehyFSR-GLSVLLFN---DGTQGrlNHLC-----------------GADFvksqqkppqGIemksgerccS 274
Cdd:COG1109  185 AAGGVAPRL---LRElGAEVIVLNaepDGNFP--NHNPnpepenledlieavketGADL---------GI---------A 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 275 FDGDADRIVYyyCDADGHFhlIDGDKIATLISsflkELLLEIGEsvNLGVVQTAyangSSTRYLEEVMK---VPVYCTKT 351
Cdd:COG1109  242 FDGDADRLGV--VDEKGRF--LDGDQLLALLA----RYLLEKGP--GGTVVVTV----MSSLALEDIAEkhgGEVVRTKV 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 352 GVKHLHHKAQEFD--IGvyFEANGHgtALFSEAVEVK-----IKRLAQELDdgkgKAARTLASIIDLFNQVADRRV-IST 423
Cdd:COG1109  308 GFKYIKEKMRETGavLG--GEESGG--IIFPDFVPTDdgilaALLLLELLA----KQGKSLSELLAELPRYPQPEInVRV 379

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255522941 424 TDAE---------RQAVTPPGLQEAINDLvkKYTLA---RAFVRPSGTEDIVRVYAEANSQESADRLAYEVSLLV 486
Cdd:COG1109  380 PDEEkigavmeklREAVEDKEELDTIDGV--KVDLEdggWVLVRPSGTEPLLRVYAEAKDEEEAEELLAELAELV 452
glmM TIGR01455
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ...
 53-479 2.21e-23

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: 102.44  E-value: 2.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941   53 TRSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLASAEEQdvrqvlaaivekeavdltqtafvviarDTRPS 132
Cdd:TIGR01455  87 LRADAGVMISASHNPYEDNGIKFFGPGGFKLDDATEAAIEALLDEADP---------------------------LPRPE 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  133 SEKLsqsvidgvtvlggqfhdygllttpqlhymvycrnsGGRYGQATVEGYCQKLSKAfvDLTNQVSCSGdvkRSVKVDC 212
Cdd:TIGR01455 140 SEGL-----------------------------------GRVKRYPDAVGRYIEFLKS--TLPRGLTLSG---LKVVLDC 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  213 ANGiGALKLREMEhYFSRGLSVLLFNDGTQGR-LNHLCGADFVKSQQKPPQGIEMKSGercCSFDGDADRIVyyYCDADG 291
Cdd:TIGR01455 180 ANG-AAYKVAPHV-FRELGAEVIAIGVEPDGLnINDGCGSTHLDALQKAVREHGADLG---IAFDGDADRVL--AVDANG 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  292 hfHLIDGDKIATLISSFLKELlleiGESVNLGVVQTAYANGSSTRYLEEvMKVPVYCTKTGVKHLHHKAQEFDIGVYFEA 371
Cdd:TIGR01455 253 --RIVDGDQILYIIARALKES----GELAGNTVVATVMSNLGLERALEK-LGLTLIRTAVGDRYVLEEMRESGYNLGGEQ 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  372 NGH---------G----TALFSEAVEVKIKRLAQELDDGKGKAARTLASIidlfnQVADRRvisttdaeRQAVTPPGLQE 438
Cdd:TIGR01455 326 SGHiilldysttGdgivSALQVLTIMKKSGSTLSELAAEFVPYPQTLVNV-----RVADRK--------LAAAEAPAVKA 392

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 255522941  439 AINDLVKKY-TLARAFVRPSGTEDIVRVYAEANSQESADRLA 479
Cdd:TIGR01455 393 AIEDAEAELgGTGRILLRPSGTEPLIRVMVEAADEELVQQLA 434
Arch_GlmM TIGR03990
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ...
 58-486 2.09e-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: 96.43  E-value: 2.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941   58 GVMVTASHNPEEDNGVKLVDPLGEMLAPsweehatclasAEEQDVRQvlaaIVEKEAVDltqtafvviardtRPSSEKLS 137
Cdd:TIGR03990  89 GIMITASHNPPEYNGIKLLNSDGTELSR-----------EQEEEIEE----IAESGDFE-------------RADWDEIG 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  138 QSVIDgvtvlggqfHDYgllttpqlhymvycrnsggrygqatVEGYCQKLsKAFVDltnqVSCSGDVKRSVKVDCANGIG 217
Cdd:TIGR03990 141 TVTSD---------EDA-------------------------IDDYIEAI-LDKVD----VEAIRKKGFKVVVDCGNGAG 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  218 ALK----LREMehyfsrGLSVLLFN---DGT-QGR--------LNHLC------GADFvksqqkppqGIemksgerccSF 275
Cdd:TIGR03990 182 SLTtpylLREL------GCKVITLNcqpDGTfPGRnpeptpenLKDLSalvkatGADL---------GI---------AH 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  276 DGDADRIVYYycDADGHFhlIDGDKIATLissFLKELLLEIGESVnlgVVqtayaNGSSTRYLEEVMK---VPVYCTKTG 352
Cdd:TIGR03990 238 DGDADRLVFI--DEKGRF--IGGDYTLAL---FAKYLLEHGGGKV---VT-----NVSSSRAVEDVAErhgGEVIRTKVG 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  353 VKHLHHKAQEFDIGVYFEANGH--------------GTALFSEAVEVKIKRLAQELDD-------------GKGKAARTL 405
Cdd:TIGR03990 303 EVNVAEKMKEEGAVFGGEGNGGwifpdhhycrdglmAAALFLELLAEEGKPLSELLAElpkypmskekvelPDEDKEEVM 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  406 ASIIDLFnqvADRRVIsTTDaerqavtppGLQEAINDlvkkytlARAFVRPSGTEDIVRVYAEANSQESADRLAYEVSLL 485
Cdd:TIGR03990 383 EAVEEEF---ADAEID-TID---------GVRIDFED-------GWVLVRPSGTEPIVRIYAEAKTEERAEELLEEGRSL 442


                  .
gi 255522941  486 V 486
Cdd:TIGR03990 443 V 443
PGM_like1 cd03087
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ...
 58-482 2.19e-21

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: 96.49  E-value: 2.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  58 GVMVTASHNPEEDNGVKLVDPLGemlapsweehatclaSAEEQDVRQVLAAIVEKEAVDLTqtAFVVIARDTRPSSekls 137
Cdd:cd03087   86 GVMITASHNPPEYNGIKLVNPDG---------------TEFSREQEEEIEEIIFSERFRRV--AWDEVGSVRREDS---- 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 138 qsVIDgvtvlggqfhdygllttpqlhymvycrnsggRYGQATVEGYCQKLSKAFvdltnqvscsgdvkrSVKVDCANGIG 217
Cdd:cd03087  145 --AID-------------------------------EYIEAILDKVDIDGGKGL---------------KVVVDCGNGAG 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 218 ALK----LREMehyfsrGLSVLLFN---DGT-QGR--------LNHLC------GADFvksqqkppqGIemksgerccSF 275
Cdd:cd03087  177 SLTtpylLREL------GCKVITLNanpDGFfPGRppeptpenLSELMelvratGADL---------GI---------AH 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 276 DGDADRIVyyYCDADGHFhlIDGDKIATLISsflKELLLEIGesvnlGVVQTAYangSSTRYLEEVMK---VPVYCTKTG 352
Cdd:cd03087  233 DGDADRAV--FVDEKGRF--IDGDKLLALLA---KYLLEEGG-----GKVVTPV---DASMLVEDVVEeagGEVIRTPVG 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 353 VKHLHHKAQEFDIGVYFEANG------HG--------TALFSEAVEvKIKRLAQELDD-------------GKGKAARTL 405
Cdd:cd03087  298 DVHVAEEMIENGAVFGGEPNGgwifpdHQlcrdgimtAALLLELLA-EEKPLSELLDElpkypllrekvecPDEKKEEVM 376

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255522941 406 ASIIDLFNQVADRrvISTTDaerqavtppGLQEAINDlvkkytlARAFVRPSGTEDIVRVYAEANSQESADRLAYEV 482
Cdd:cd03087  377 EAVEEELSDADED--VDTID---------GVRIEYED-------GWVLIRPSGTEPKIRITAEAKTEERAKELLEEG 435
PGM_like4 cd05803
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ...
 52-479 6.37e-12

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: 67.33  E-value: 6.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  52 QTRSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSweehatclasaeeqDVRQVLAAIVEKEAVDLTQTAFVVIARDTRP 131
Cdd:cd05803   85 QSQASGGIIITASHNPPQWNGLKFIGPDGEFLTPD--------------EGEEVLSCAEAGSAQKAGYDQLGEVTFSEDA 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 132 SSEKlsqsvIDGVtvlggqfhdygllttpqlhymvycrnsggrygqatvegycqkLSKAFVDltnqVSCSGDVKRSVKVD 211
Cdd:cd05803  151 IAEH-----IDKV------------------------------------------LALVDVD----VIKIRERNFKVAVD 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 212 CANGIGALKLREMEHyfSRGLSVLLFNDGTQGRLNHlcgadfvksqqkPPQGIEMKSGERC-------CSF----DGDAD 280
Cdd:cd05803  180 SVNGAGGLLIPRLLE--KLGCEVIVLNCEPTGLFPH------------TPEPLPENLTQLCaavkesgADVgfavDPDAD 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 281 RIVyyycdadghfhLIDGDKIA-----TLISSFLkELLLEIGESVNlgVVqtayANGSSTRYLEEVMK---VPVYCTKTG 352
Cdd:cd05803  246 RLA-----------LVDEDGRPigeeyTLALAVD-YVLKYGGRKGP--VV----VNLSTSRALEDIARkhgVPVFRSAVG 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 353 VKHLHHKAQEFDIGVYFEANG-------H-------GTALFSEAV---EVKIKRLAQELDD---GKGK---AARTLASII 409
Cdd:cd05803  308 EANVVEKMKEVDAVIGGEGNGgvilpdvHygrdslvGIALVLQLLaasGKPLSEIVDELPQyyiSKTKvtiAGEALERLL 387

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 410 DLFNQVADRRVISTTDaerqavtppGLQEAINDlvkkytlARAFVRPSGTEDIVRVYAEANSQESADRLA 479
Cdd:cd05803  388 KKLEAYFKDAEASTLD---------GLRLDSED-------SWVHVRPSNTEPIVRIIAEAPTQDEAEALA 441
PMM_PGM cd03089
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ...
 123-486 3.84e-10

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: 61.76  E-value: 3.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 123 VVIARDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHY-----------MV--------Y-----CRNSGGRYGQ- 177
Cdd:cd03089   39 VVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPVLYFatfhldadggvMItashnppeYngfkiVIGGGPLSGEd 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 178 ---------------ATVEGYCQKLS--KAFVD-LTNQVSCSgdvKRSVK--VDCANGIGALKLREMEhyfsRGL---SV 234
Cdd:cd03089  119 iqalreraekgdfaaATGRGSVEKVDilPDYIDrLLSDIKLG---KRPLKvvVDAGNGAAGPIAPQLL----EALgceVI 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 235 LLFN--DGTqgRLNH------------LC------GADFvksqqkppqGIemksgerccSFDGDADRIVYYycDADGHFh 294
Cdd:cd03089  192 PLFCepDGT--FPNHhpdptdpenledLIaavkenGADL---------GI---------AFDGDGDRLGVV--DEKGEI- 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 295 lIDGDKIATLISsflKELLLE------IGESVnlgvvqtayangsSTRYLEEVMK----VPVYCtKTGVKHLHHKAQEFD 364
Cdd:cd03089  249 -IWGDRLLALFA---RDILKRnpgatiVYDVK-------------CSRNLYDFIEeaggKPIMW-KTGHSFIKAKMKETG 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 365 IGVYFEANGHGtaLFSE-----------AVevkikRLAQELDDGKGKAARTLASIIDLFNQVADRrvISTTDAERQAVTp 433
Cdd:cd03089  311 ALLAGEMSGHI--FFKDrwygfddgiyaAL-----RLLELLSKSGKTLSELLADLPKYFSTPEIR--IPVTEEDKFAVI- 380

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255522941 434 PGLQEAINDLVKK----------YTLARAFVRPSGTEDIVRVYAEANSQESADRLAYEVSLLV 486
Cdd:cd03089  381 ERLKEHFEFPGAEiididgvrvdFEDGWGLVRASNTEPVLVLRFEADTEEGLEEIKAELRKLL 443
PGM_like2 cd05800
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ...
 58-478 1.78e-08

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: 56.79  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  58 GVMVTASHNPEEDNGVKLVDPLGemlapsweehatclASAEEQDVRQV---LAAIVEKEAVDLTQTAFVVIarDTRPsse 134
Cdd:cd05800   94 GVMITASHNPPEYNGVKVKPAFG--------------GSALPEITAAIearLASGEPPGLEARAEGLIETI--DPKP--- 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 135 klsqsvidgvtvlggqfhdygllttpqlhymvycrnsggrygqatveGYCQKLSKaFVDLtnqvscsgDVKRS----VKV 210
Cdd:cd05800  155 -----------------------------------------------DYLEALRS-LVDL--------EAIREaglkVVV 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 211 DCANG--IGALK--LREmehyfsRGLSVLLFNDG------------TQGRLNHLcgADFVKsQQKPPQGIemksgerccS 274
Cdd:cd05800  179 DPMYGagAGYLEelLRG------AGVDVEEIRAErdplfggippepIEKNLGEL--AEAVK-EGGADLGL---------A 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 275 FDGDADRI--VyyycDADGHFhlIDGDKIATLissflkeLLLEIGESVNL--GVVQTAyangSSTRYLEEVMK---VPVY 347
Cdd:cd05800  241 TDGDADRIgaV----DEKGNF--LDPNQILAL-------LLDYLLENKGLrgPVVKTV----STTHLIDRIAEkhgLPVY 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 348 CTKTGVKHLHHKAQEFD--IGVYfEANGHG-------------TALFSEAVEVKIKRLAQelddgkgkaarTLASIIDLF 412
Cdd:cd05800  304 ETPVGFKYIAEKMLEEDvlIGGE-ESGGLGirghiperdgilaGLLLLEAVAKTGKPLSE-----------LVAELEEEY 371

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 413 NQVA-DRRVISTTDAERQAVT-----PPGLQEAINDLVK-------KYTLARAF---VRPSGTEDIVRVYAEANSQESAD 476
Cdd:cd05800  372 GPSYyDRIDLRLTPAQKEAILeklknEPPLSIAGGKVDEvntidgvKLVLEDGSwllIRPSGTEPLLRIYAEAPSPEKVE 451


                 ..
gi 255522941 477 RL 478
Cdd:cd05800  452 AL 453
PGM_PMM_IV pfam00408
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
434-486 4.13e-08

Phosphoglucomutase/phosphomannomutase, C-terminal domain;


Pssm-ID: 425666  Cd Length: 71  Bit Score: 49.96  E-value: 4.13e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 255522941  434 PGLQEAINDLVKKYTL--ARAFVRPSGTEDIVRVYAEANSQESADRLAYEVSLLV 486
Cdd:pfam00408  16 AAILKVFADAEKILGEdgRRLDVRPSGTEPVLRVMVEGDSDEELARLADEIADLL 70
PGM_PMM_I pfam02878
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
58-89 2.52e-07

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


Pssm-ID: 427032  Cd Length: 138  Bit Score: 49.92  E-value: 2.52e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 255522941   58 GVMVTASHNPEEDNGVKLVDPLGEMLAPSWEE 89
Cdd:pfam02878  94 GIMITASHNPPEYNGIKVFDSNGGPIPPEVEK 125
PGM_PMM_I pfam02878
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
123-166 1.07e-06

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


Pssm-ID: 427032  Cd Length: 138  Bit Score: 47.99  E-value: 1.07e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 255522941  123 VVIARDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMV 166
Cdd:pfam02878  43 VVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTPAVSFAT 86
glmM PRK10887
phosphoglucosamine mutase; Provisional
 54-479 2.50e-05

phosphoglucosamine mutase; Provisional


Pssm-ID: 236787  Cd Length: 443  Bit Score: 46.67  E-value: 2.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  54 RSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEhatclasaeeqdvrqvlaAIvEKEavdLTQTAFVViardtrpSS 133
Cdd:PRK10887  89 RAEAGIVISASHNPYYDNGIKFFSADGTKLPDEVEL------------------AI-EAE---LDKPLTCV-------ES 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 134 EKLSQSV-IDGvtvlggqfhdygllttpqlhymvycrnSGGRYgqatVEgYCqklsKAFVDltNQVSCSGdVKrsVKVDC 212
Cdd:PRK10887 140 AELGKASrIND---------------------------AAGRY----IE-FC----KSTFP--NELSLRG-LK--IVVDC 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 213 ANG----IGALKLREMehyfsrGLSVLLFNDGTQGR-LNHLCGADFVKS------QQKPPQGIemksgerccSFDGDADR 281
Cdd:PRK10887 179 ANGatyhIAPNVFREL------GAEVIAIGCEPNGLnINDECGATDPEAlqaavlAEKADLGI---------AFDGDGDR 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 282 IVYyycdADGHFHLIDGDKIATLISsflKELLLEiGESVNlGVVQTAYANGSSTRYLEEvMKVPVYCTKTGVKHLHHKAQ 361
Cdd:PRK10887 244 VIM----VDHLGNLVDGDQLLYIIA---RDRLRR-GQLRG-GVVGTLMSNMGLELALKQ-LGIPFVRAKVGDRYVLEKLQ 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 362 EFDIGVYFEANGH---------GTALFSeAVEV--KIKRLAQELDDgkgkaartLASIIDLFNQV-ADRRVISTTDAERQ 429
Cdd:PRK10887 314 EKGWRLGGENSGHilcldktttGDGIVA-ALQVlaAMVRSGMSLAD--------LCSGMKLFPQVlINVRFKPGADDPLE 384

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 255522941 430 AvtpPGLQEAINDlVKKyTLA---RAFVRPSGTEDIVRVYAEANSQESADRLA 479
Cdd:PRK10887 385 S---EAVKAALAE-VEA-ELGgrgRVLLRKSGTEPLIRVMVEGEDEAQVTALA 432
PGM2 cd05799
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ...
 58-74 3.38e-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: 3.38e-05
                         10
                 ....*....|....*..
gi 255522941  58 GVMVTASHNPEEDNGVK 74
Cdd:cd05799  100 GIMITASHNPKEYNGYK 116
PTZ00150 PTZ00150
phosphoglucomutase-2-like protein; Provisional
 57-74 1.30e-04

phosphoglucomutase-2-like protein; Provisional


Pssm-ID: 240294  Cd Length: 584  Bit Score: 44.67  E-value: 1.30e-04
                         10
                 ....*....|....*...
gi 255522941  57 IGVMVTASHNPEEDNGVK 74
Cdd:PTZ00150 143 AGVMVTASHNPKEDNGYK 160
PLN02371 PLN02371
phosphoglucosamine mutase family protein
 101-160 1.80e-04

phosphoglucosamine mutase family protein


Pssm-ID: 215211 [Multi-domain]  Cd Length: 583  Bit Score: 44.28  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941 101 DVRQVLAAIVEKEAVDLTQ-------TAF-----------------VVIARDTRPSSEKLSQSVIDGVTVLGGQFHDYGL 156
Cdd:PLN02371  72 DIRGVAVEGVEGEPVTLTPpaveaigAAFaewllekkkadgsgelrVSVGRDPRISGPRLADAVFAGLASAGLDVVDMGL 151


                 ....
gi 255522941 157 LTTP 160
Cdd:PLN02371 152 ATTP 155
manB PRK09542
phosphomannomutase/phosphoglucomutase; Reviewed
 101-164 2.61e-04

phosphomannomutase/phosphoglucomutase; Reviewed


Pssm-ID: 236557  Cd Length: 445  Bit Score: 43.43  E-value: 2.61e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255522941 101 DVRQVLAAIVEKEAVDLTQTAF-----------VVIARDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHY 164
Cdd:PRK09542   5 DVRGVVGEQIDEDLVRDVGAAFarlmraegattVVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIGLASTDQLYF 79
PGM_PMM_III pfam02880
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
297-375 4.33e-03

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


Pssm-ID: 460733  Cd Length: 115  Bit Score: 37.04  E-value: 4.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255522941  297 DGDKIATLISSFLKELLLEIGesvNLGVVQTAyangSSTRYLEEVMK---VPVYCTKTGVKHLHHKAQEFDIGVYFEANG 373
Cdd:pfam02880   1 DGDQILALLAKYLLEQGKLPP---GAGVVKTV----MSSLGLDRVAKklgGKLVRTPVGDKYVKEKMREEGALFGGEESG 73


                  ..
gi 255522941  374 HG 375
Cdd:pfam02880  74 HI 75
 
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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