|
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: 795.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 22 QYGTAGFRTKAEHLDHVMFRMGLLAVLRSKQTKS-TIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLANAEEQ 100
Cdd:cd03086 1 SYGTAGFRTKAELLDSVVFRVGILAALRSKKLGGkTIGVMITASHNPVEDNGVKIVDPDGEMLEESWEPYATQLANASDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 101 DMQRVLIDI--SEKEAVNLQQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNTGGRYGKA 178
Cdd:cd03086 81 ELLVLVLMLisVKELNIDLSVPANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYLVRAANTEGAYGEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 179 TIEGYYQKLSKAFVELTKQASCSGDEYRSLKVDCANGIGALKLREMEHYFSQGLSVQLFNDGSKG--KLNHLCGADFVKS 256
Cdd:cd03086 161 TEEGYYEKLSKAFNELYNLLQDGGDEPEKLVVDCANGVGALKLKELLKRLKKGLSVKIINDGEEGpeLLNDGCGADYVKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 257 HQKPPQGMEIK-SNERCCSFDGDADRIVYYYHDADGHFHLIDGDKIATLISSFLKELL--VEIGESLNIGVVQTAYANGS 333
Cdd:cd03086 241 KQKPPRGFELKpPGVRCCSFDGDADRLVYFYPDSSNKFHLLDGDKIATLFAKFIKELLkkAGEELKLTIGVVQTAYANGA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 334 STRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFSTAVEMKIKqSAEQLEDKKRKAAKMLENIIDLFN 413
Cdd:cd03086 321 STKYLEDVLKVPVVCTPTGVKHLHHAAEEFDIGVYFEANGHGTVLFSESALAKIE-ENSSLSDEQEKAAKTLLAFSRLIN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 414 Q-----------------------------------------VADRRVISTTDAERQAVTPPGLQEAINDLVKKYKLSRA 452
Cdd:cd03086 400 QtvgdaisdmlavelilaalgwspqdwdnlytdlpnrqlkvkVPDRSVIKTTDAERRLVEPKGLQDKIDAIVAKYNNGRA 479
|
490 500 510
....*....|....*....|....*....|....
gi 1516481958 453 FVRPSGTEDVVRVYAEADSQESADHLAHEVSLAV 486
Cdd:cd03086 480 FVRPSGTEDVVRVYAEAATQEEADELANEVAELV 513
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
1-497 |
0e+00 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 589.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 1 MDLGAITKYSALHAKPNGLILQYGTAGFRTKAEHLDHVMFRMGLLAVLRSKQTKSTIGVMVTASHNPEEDNGVKLVDPLG 80
Cdd:PLN02895 4 IQRASLLAASSRFPPPQGVRFSYGTAGFRTDASLLESTVFRVGILAALRSLKTGAATGLMITASHNPVSDNGVKIVDPSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 81 EMLAPSWEEHATCLANAE-EQDMQRVLIDISEKEAVNL---QQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGL 156
Cdd:PLN02895 84 GMLPQAWEPFADALANAPdPDALVQLIREFVKKENIPAvggNPPAEVLLGRDTRPSGPALLAAALKGVRAIGARAVDMGI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 157 LTTPQLHYMVYCRNTGgryGKATIEGYYQKLSKAF---VELTKQASCSGDEYRSLKVDCANGIGALKLREMEHYFSqGLS 233
Cdd:PLN02895 164 LTTPQLHWMVRAANKG---MKATESDYFEQLSSSFralLDLIPNGSGDDRADDKLVVDGANGVGAEKLETLKKALG-GLD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 234 VQLFNDG--SKGKLNHLCGADFVKSHQKPPQGMEIK-SNERCCSFDGDADRIVYYYHDADG-HFHLIDGDKIATLISSFL 309
Cdd:PLN02895 240 LEVRNSGkeGEGVLNEGVGADFVQKEKVPPTGFASKdVGLRCASLDGDADRLVYFYVSSAGsKIDLLDGDKIASLFALFI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 310 KELLVEIGES---------LNIGVVQTAYANGSSTRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFS 380
Cdd:PLN02895 320 KEQLRILNGNgnekpeellVRLGVVQTAYANGASTAYLKQVLGLEVVCTPTGVKYLHEAAAEFDIGVYFEANGHGTVLFS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 381 TAVEMKIKQSAEQLEDKKR-----KAAKMLENIIDLFNQ----------------------------------------- 414
Cdd:PLN02895 400 ERFLDWLEAAAAELSSKAKgseahKAARRLLAVSRLINQavgdalsglllveailqyrgwslaewnalyqdlpsrqlkvk 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 415 VADRRVISTTDAERQAVTPPGLQEAINDLVKKYKLSRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSLAVFQLAGGIG 494
Cdd:PLN02895 480 VADRTAITTTDAETVVVRPAGLQDAIDAEVAKYPRGRAFVRPSGTEDVVRVYAEASTQEAADSLAREVARLVYDLLGGVG 559
|
...
gi 1516481958 495 ERP 497
Cdd:PLN02895 560 PPP 562
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
5-492 |
0e+00 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 524.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 5 AITKYSALH-AKPNGLIlqYGTAGFRTKAE--HLDHVMFRMGLLAVLRSKQTKS--------TIGVMVTASHNPEEDNGV 73
Cdd:PTZ00302 16 CGSKFPLRHsAIENPLT--YGTAGFRTKAElpPLEPVAYRVGILAALRSFLYGGkrakrgnkSVGVMITASHNPIQDNGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 74 KLVDPLGEMLAPSWEEHATCLANAE-EQDMQRVLIDISEKEAVNLQQD-----------AFVVIGRDTRPSSEKLSQSVI 141
Cdd:PTZ00302 94 KIIDPDGGMLEESWEKICTDFANARtGEDLVSVLMDCLTEHGIKLSNLkldlnksncskAKVHVGRDTRPSSPELVSALL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 142 DGVTVLGGQFH-DYGLLTTPQLHYMVYCRNTGGR-YGKATIEGYYQKLSKAFVELTKQASCSGDEYRS------LKVDCA 213
Cdd:PTZ00302 174 RGLKLLIGSNVrNFGIVTTPQLHFLVAFANGLGVdVVESSDELYYAYLLAAFKELYRTLQEGGPVDLTqnnskiLVVDCA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 214 NGIGALKLREMEHYFSQ---GLSVQLFNDGSKGKLNHLCGADFVKSHQKPPQGMEIK---SNERCCSFDGDADRIVYYYH 287
Cdd:PTZ00302 254 NGVGGYKIKRFFEALKQlgiEIIPININCDEEELLNDKCGADYVQKTRKPPRAMKEWpgdEETRVASFDGDADRLVYFFP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 288 DADGH--FHLIDGDKIATLISSFLKELLVEIG--ESLNIGVVQTAYANGSSTRYLEEVMK-VPVYCTKTGVKHLHHKAQE 362
Cdd:PTZ00302 334 DKDGDdkWVLLDGDRIAILYAMLIKKLLGKIQlkKKLDIGVVQTAYANGASTNYLNELLGrLRVYCAPTGVKNLHPKAHK 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 363 FDIGVYFEANGHGTALFStavEMKIKQSAEQLEDK--KRKAAKMLENIIDLFNQ-------------------------- 414
Cdd:PTZ00302 414 YDIGIYFEANGHGTVLFN---EKALAEWAKFLAKQnaLNSACRQLEKFLRLFNQtigdaisdllavelalaflglsfqdw 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 415 ---------------VADRRVISTTDAERQAVTPPGLQEAINDLVKKYK-LSRAFVRPSGTEDVVRVYAEADSQESADHL 478
Cdd:PTZ00302 491 lnlytdlpsrqdkvtVKDRTLITNTEDETRLLEPKGLQDKIDAIVSKYDnAARAFIRPSGTEPVVRVYAEAPTLEQADEL 570
|
570
....*....|....
gi 1516481958 479 AHEVSLAVFQLAGG 492
Cdd:PTZ00302 571 ANEVKGLVLRYCSG 584
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
23-483 |
2.96e-44 |
|
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: 159.44 E-value: 2.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 23 YGTAGFRTKA--EHLDHVMFRMGLLAVlrskqtkSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLANAEEQ 100
Cdd:cd03084 2 FGTSGVRGVVgdDITPETAVALGQAIG-------STGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 101 DmqrvlidisekeavnlqqdafvvigrdtRPSSEKLSQSVidgvtvlggqfhdygllttpqlhymvycrntggrYGKATI 180
Cdd:cd03084 75 P----------------------------SAVAYELGGSV----------------------------------KAVDIL 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 181 EGYYQKL-SKAFVELTKQAScsgdeyRSLKVDCANGIGALKLREM-EHYfsqGLSVQLFN---DGSKGKLNHLCGADfvK 255
Cdd:cd03084 93 QRYFEALkKLFDVAALSNKK------FKVVVDSVNGVGGPIAPQLlEKL---GAEVIPLNcepDGNFGNINPDPGSE--T 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 256 SHQKPPQGMEIKSNERCCSFDGDADRIVYYYHDadghFHLIDGDKIATLISsflKELLVEIGesLNIGVVQTAYANGSST 335
Cdd:cd03084 162 NLKQLLAVVKAEKADFGVAFDGDADRLIVVDEN----GGFLDGDELLALLA---VELFLTFN--PRGGVVKTVVSSGALD 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 336 RYLEEvMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFSTAVEMKIKQSAEQLEdkkrKAAKMLENIIDLFNQV 415
Cdd:cd03084 233 KVAKK-LGIKVIRTKTGFKWVGEAMQEGDVVLGGEESGGVIFPEFHPGRDGISAALLLLE----ILANLGKSLSELFSEL 307
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1516481958 416 ADRrvisttdaerqavtppglqeaINDLVKKYklSRAFVRPSGTEDVVRVYAEADSQESADHLAHEVS 483
Cdd:cd03084 308 PRY---------------------YYIRLKVR--GWVLVRASGTEPAIRIYAEADTQEDVEQIKKEAR 352
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
123-482 |
3.70e-27 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 113.76 E-value: 3.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 123 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNTGG--------------------RYGK----- 177
Cdd:COG1109 44 VVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVPTPALAFAVRHLGADGgimitashnppeyngikffdADGGklspe 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 178 --ATIEGYYQKLSKAFVELTKQASCS-----GDEY--------------RSLKV--DCANGIGALK----LREMehyfsq 230
Cdd:COG1109 124 eeKEIEALIEKEDFRRAEAEEIGKVTriedvLEAYiealkslvdealrlRGLKVvvDCGNGAAGGVaprlLREL------ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 231 GLSVQLFN---DGSKGklNHLCG---------ADFVKSHqkppqGMEIksnerCCSFDGDADRI--VyyyhDADGHFhlI 296
Cdd:COG1109 198 GAEVIVLNaepDGNFP--NHNPNpepenledlIEAVKET-----GADL-----GIAFDGDADRLgvV----DEKGRF--L 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 297 DGDKIATLISSFLKEllveigESLNIGVVQTAyangSSTRYLEEVMK---VPVYCTKTGVKHLHHKAQEFD--IGvyFEA 371
Cdd:COG1109 260 DGDQLLALLARYLLE------KGPGGTVVVTV----MSSLALEDIAEkhgGEVVRTKVGFKYIKEKMRETGavLG--GEE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 372 NGH---------GTALFSTAvemkikQSAEQLEDKKRKAAKMLENIIDLFN-----QVADRRVISTTDAE-RQAVTPPGL 436
Cdd:COG1109 328 SGGiifpdfvptDDGILAAL------LLLELLAKQGKSLSELLAELPRYPQpeinvRVPDEEKIGAVMEKlREAVEDKEE 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1516481958 437 QEAINDLvkKYKL---SRAFVRPSGTEDVVRVYAEADSQESADHLAHEV 482
Cdd:COG1109 402 LDTIDGV--KVDLedgGWVLVRPSGTEPLLRVYAEAKDEEEAEELLAEL 448
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
57-486 |
1.19e-26 |
|
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: 112.07 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 57 IGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEhatclanaeeqdmqrvlidisEKEAVNLQQDAFvvigrdTRPSSEKL 136
Cdd:TIGR01455 91 AGVMISASHNPYEDNGIKFFGPGGFKLDDATEA---------------------AIEALLDEADPL------PRPESEGL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 137 SQSVidgvtvlggqfhdygllttpqlhymvycrntggRYGKATieGYYQKLSKAfvELTKQASCSGdeyrsLKV--DCAN 214
Cdd:TIGR01455 144 GRVK---------------------------------RYPDAV--GRYIEFLKS--TLPRGLTLSG-----LKVvlDCAN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 215 GiGALKLREMEhYFSQGLSVQLFNDGSKG-KLNHLCGADFVKSHQKP--PQGMEIKsnercCSFDGDADRIVYYyhDADG 291
Cdd:TIGR01455 182 G-AAYKVAPHV-FRELGAEVIAIGVEPDGlNINDGCGSTHLDALQKAvrEHGADLG-----IAFDGDADRVLAV--DANG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 292 hfHLIDGDKIATLISSFLKELlveiGESLNIGVVQTAYANGSSTRYLEEvMKVPVYCTKTGVKHLHHKAQEFDIGVYFEA 371
Cdd:TIGR01455 253 --RIVDGDQILYIIARALKES----GELAGNTVVATVMSNLGLERALEK-LGLTLIRTAVGDRYVLEEMRESGYNLGGEQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 372 NGH---------G----TALFSTAVEMKIKQSAEQLEDKKRKAAKMLENIidlfnQVADRRvisttdaeRQAVTPPGLQE 438
Cdd:TIGR01455 326 SGHiilldysttGdgivSALQVLTIMKKSGSTLSELAAEFVPYPQTLVNV-----RVADRK--------LAAAEAPAVKA 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1516481958 439 AINDLVKKY-KLSRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSLAV 486
Cdd:TIGR01455 393 AIEDAEAELgGTGRILLRPSGTEPLIRVMVEAADEELVQQLADTLADVV 441
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
51-483 |
9.29e-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: 103.33 E-value: 9.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 51 KQTKSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEhatclanaeeqdmqrvlidisEKEAVNLQqdafvviGRDTR 130
Cdd:cd05802 84 RKLRADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVEE---------------------EIEALIDK-------ELELP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 131 PSSEKLsqsvidgvtvlgGQFHDYgllTTPQLHYMVYCRNTGGRygkatiegyyQKLSKafveltkqascsgdeyrsLKV 210
Cdd:cd05802 136 PTGEKI------------GRVYRI---DDARGRYIEFLKSTFPK----------DLLSG------------------LKI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 211 --DCANG----IGALKLREMehyfsqGLSVQLFNDGSKG-KLNHLCGADFVKSHQKppqgmEIKSNERCC--SFDGDADR 281
Cdd:cd05802 173 vlDCANGaaykVAPEVFREL------GAEVIVINNAPDGlNINVNCGSTHPESLQK-----AVLENGADLgiAFDGDADR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 282 IVYYyhDADGhfHLIDGDKIATLISSFLKELlveiGESLNIGVVQTAYANGSSTRYLEEvMKVPVYCTKTGVKHLHHKAQ 361
Cdd:cd05802 242 VIAV--DEKG--NIVDGDQILAICARDLKER----GRLKGNTVVGTVMSNLGLEKALKE-LGIKLVRTKVGDRYVLEEML 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 362 EFDIGVYFEANGH---------G----TALfstavemkikQSAEQLEDKKRKAAKMLeNIIDLFNQV-ADRRVISTTDAE 427
Cdd:cd05802 313 KHGANLGGEQSGHiifldhsttGdgllTAL----------QLLAIMKRSGKSLSELA-SDMKLYPQVlVNVRVKDKKALL 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1516481958 428 rqavTPPGLQEAINDLVKKYKLS-RAFVRPSGTEDVVRVYAEADSQESADHLAHEVS 483
Cdd:cd05802 382 ----ENPRVQAAIAEAEKELGGEgRVLVRPSGTEPLIRVMVEGEDEELVEKLAEELA 434
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
58-482 |
6.56e-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: 91.86 E-value: 6.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 58 GVMVTASHNPEEDNGVKLVDPLG-EMlapsweehatclanaeEQDMQRVLIDISEKEAVNLQqdAFVVIGRDTRPSsekl 136
Cdd:cd03087 86 GVMITASHNPPEYNGIKLVNPDGtEF----------------SREQEEEIEEIIFSERFRRV--AWDEVGSVRRED---- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 137 sqSVIDgvtvlggqfhDYgllttpqlhymvycrntggrygkatIEGYYQKLSKafveltkqascsgDEYRSLKV--DCAN 214
Cdd:cd03087 144 --SAID----------EY-------------------------IEAILDKVDI-------------DGGKGLKVvvDCGN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 215 GIGALK----LREMehyfsqGLSVQLFN---DG---------SKGKLNHLC------GADFVKSHqkppqgmeiksnerc 272
Cdd:cd03087 174 GAGSLTtpylLREL------GCKVITLNanpDGffpgrppepTPENLSELMelvratGADLGIAH--------------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 273 csfDGDADRIVYYyhDADGHFhlIDGDKIATLISsflKELLVEIGeslniGVVQTAYangSSTRYLEEVMK---VPVYCT 349
Cdd:cd03087 233 ---DGDADRAVFV--DEKGRF--IDGDKLLALLA---KYLLEEGG-----GKVVTPV---DASMLVEDVVEeagGEVIRT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 350 KTGVKHLHHKAQEFDIGVYFEANGH-----------GTALFSTAVEMKikqsaeqleDKKRKAAKMLENIIDLFNqvaDR 418
Cdd:cd03087 295 PVGDVHVAEEMIENGAVFGGEPNGGwifpdhqlcrdGIMTAALLLELL---------AEEKPLSELLDELPKYPL---LR 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1516481958 419 RVISTTDAERQAVtPPGLQEAINDLVKK------YKLSR----AFVRPSGTEDVVRVYAEADSQESADHLAHEV 482
Cdd:cd03087 363 EKVECPDEKKEEV-MEAVEEELSDADEDvdtidgVRIEYedgwVLIRPSGTEPKIRITAEAKTEERAKELLEEG 435
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
58-482 |
4.16e-19 |
|
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: 89.49 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 58 GVMVTASHNPEEDNGVKLVDPLGEMLAPsweehatclanaeeqDMQRVLIDISEKEavnlqqDAFVV----IGRDTRPSS 133
Cdd:TIGR03990 89 GIMITASHNPPEYNGIKLLNSDGTELSR---------------EQEEEIEEIAESG------DFERAdwdeIGTVTSDED 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 134 ekLSQSVIDGVtvlggqfhdygllttpqlhymvycrntggrygkatiegyyqklsKAFVELTKQAScsgdeyRSLKV--D 211
Cdd:TIGR03990 148 --AIDDYIEAI--------------------------------------------LDKVDVEAIRK------KGFKVvvD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 212 CANGIGALK----LREMehyfsqGLSVQLFNDGSKGK------------LNHLC------GADFVKSHqkppqgmeiksn 269
Cdd:TIGR03990 176 CGNGAGSLTtpylLREL------GCKVITLNCQPDGTfpgrnpeptpenLKDLSalvkatGADLGIAH------------ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 270 erccsfDGDADRIVYYyhDADGHFhlIDGDKIATLissFLKELLVEIGESLnigVVqtayaNGSSTRYLEEVMK---VPV 346
Cdd:TIGR03990 238 ------DGDADRLVFI--DEKGRF--IGGDYTLAL---FAKYLLEHGGGKV---VT-----NVSSSRAVEDVAErhgGEV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 347 YCTKTGVKHLHHKAQEFDIGVYFEANGH--------------GTALFstaVEMkikqsaeqLEDKKRKAAKMLENIIDLF 412
Cdd:TIGR03990 297 IRTKVGEVNVAEKMKEEGAVFGGEGNGGwifpdhhycrdglmAAALF---LEL--------LAEEGKPLSELLAELPKYP 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1516481958 413 NQvadRRVISTTDAERQAVTpPGLQEAINDL----VKKYKLSR----AFVRPSGTEDVVRVYAEADSQESADHLAHEV 482
Cdd:TIGR03990 366 MS---KEKVELPDEDKEEVM-EAVEEEFADAeidtIDGVRIDFedgwVLVRPSGTEPIVRIYAEAKTEERAEELLEEG 439
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
52-479 |
6.40e-13 |
|
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: 70.41 E-value: 6.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 52 QTKSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSweehatclanaeeqDMQRVLIDISEKEAVNLQQDAfvvIGRDTrp 131
Cdd:cd05803 85 QSQASGGIIITASHNPPQWNGLKFIGPDGEFLTPD--------------EGEEVLSCAEAGSAQKAGYDQ---LGEVT-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 132 SSEKLSQSVIDGVtvlggqfhdygllttpqlhymvycrntggrygkatiegyyqkLSKAFVELTKQAScsgdeyRSLKV- 210
Cdd:cd05803 146 FSEDAIAEHIDKV------------------------------------------LALVDVDVIKIRE------RNFKVa 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 211 -DCANGIGALKLREMEHyfSQGLSVQLFNDGSKGKLNHlcgadfvkshqkPPQgmEIKSN---------ERCCSF----D 276
Cdd:cd05803 178 vDSVNGAGGLLIPRLLE--KLGCEVIVLNCEPTGLFPH------------TPE--PLPENltqlcaavkESGADVgfavD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 277 GDADRIVyyyhdadghfhLIDGDKIA-----TLISSFLkELLVEIGESLNIGVvqtayaNGSSTRYLEEVMK---VPVYC 348
Cdd:cd05803 242 PDADRLA-----------LVDEDGRPigeeyTLALAVD-YVLKYGGRKGPVVV------NLSTSRALEDIARkhgVPVFR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 349 TKTGVKHLHHKAQEFDIGVYFEANG-------H-------GTALFSTAVEM---KIKQSAEQLEDK---KRK---AAKML 405
Cdd:cd05803 304 SAVGEANVVEKMKEVDAVIGGEGNGgvilpdvHygrdslvGIALVLQLLAAsgkPLSEIVDELPQYyisKTKvtiAGEAL 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1516481958 406 ENIIDLFNQVADRRVISTTDaerqavtppGLQEAINDlvkkyklSRAFVRPSGTEDVVRVYAEADSQESADHLA 479
Cdd:cd05803 384 ERLLKKLEAYFKDAEASTLD---------GLRLDSED-------SWVHVRPSNTEPIVRIIAEAPTQDEAEALA 441
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
434-486 |
1.13e-10 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 57.28 E-value: 1.13e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1516481958 434 PGLQEAINDLVKKYKL--SRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSLAV 486
Cdd:pfam00408 16 AAILKVFADAEKILGEdgRRLDVRPSGTEPVLRVMVEGDSDEELARLADEIADLL 70
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
123-482 |
1.38e-09 |
|
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars (e.g. between mannose-1-phosphate and mannose-6-phosphate or glucose-1-phosphate and glucose-6-phosphate) via a bisphosphorylated sugar intermediate. The reaction involves two phosphoryl transfers, with an intervening 180 degree reorientation of the reaction intermediate during catalysis. Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is thus, a simple example of processivity, as defined by multiple rounds of catalysis without release of substrate. Glucose-6-phosphate and glucose-1-phosphate are known to be utilized for energy metabolism and cell surface construction, respectively. PMM/PGM belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the phosphoglucomutases (PGM1 and PGM2). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100091 Cd Length: 443 Bit Score: 60.22 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 123 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHY-----------MV--------Y-----CRNTGGRYG-- 176
Cdd:cd03089 39 VVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPVLYFatfhldadggvMItashnppeYngfkiVIGGGPLSGed 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 177 ----KATIEGYYQKLSKAFVELTKQasCSGDEY------------RSLK--VDCANGIGALKLREMEhyfsQGL---SVQ 235
Cdd:cd03089 119 iqalRERAEKGDFAAATGRGSVEKV--DILPDYidrllsdiklgkRPLKvvVDAGNGAAGPIAPQLL----EALgceVIP 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 236 LFN--DGS----------KGKLNHLC------GADFvkshqkppqGMeiksnerccSFDGDADRIVYYyhDADGHFhlID 297
Cdd:cd03089 193 LFCepDGTfpnhhpdptdPENLEDLIaavkenGADL---------GI---------AFDGDGDRLGVV--DEKGEI--IW 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 298 GDKIATLISsflKELLVEIGESLNIGVVQTayangssTRYLEEVMK----VPVYCtKTGVKHLHHKAQEFDIGVYFEANG 373
Cdd:cd03089 251 GDRLLALFA---RDILKRNPGATIVYDVKC-------SRNLYDFIEeaggKPIMW-KTGHSFIKAKMKETGALLAGEMSG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 374 HG----------TALFSTAvemKIkqsAEQLEDKKRKAAKMLENIIDLFNQVADRrvISTTDAERQAVTpPGLQEAINDL 443
Cdd:cd03089 320 HIffkdrwygfdDGIYAAL---RL---LELLSKSGKTLSELLADLPKYFSTPEIR--IPVTEEDKFAVI-ERLKEHFEFP 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1516481958 444 VKK----------YKLSRAFVRPSGTEDVVRVYAEADSQESADHLAHEV 482
Cdd:cd03089 391 GAEiididgvrvdFEDGWGLVRASNTEPVLVLRFEADTEEGLEEIKAEL 439
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
123-166 |
1.75e-07 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 50.30 E-value: 1.75e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1516481958 123 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMV 166
Cdd:pfam02878 43 VVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTPAVSFAT 86
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
58-100 |
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 40
....*....|....*....|....*....|....*....|...
gi 1516481958 58 GVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLANAEEQ 100
Cdd:pfam02878 94 GIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKEDF 136
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
58-486 |
1.90e-06 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 50.13 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 58 GVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEhatcLANAE-EQDMQRVlidisekEAVNLqqdafvviGRDTRpssekl 136
Cdd:PRK10887 93 GIVISASHNPYYDNGIKFFSADGTKLPDEVEL----AIEAElDKPLTCV-------ESAEL--------GKASR------ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 137 sqsvIDGVTvlggqfhdygllttpqlhymvycrntgGRYgkatIEgyyqklskaFVELTKQASCSgdeYRSLK--VDCAN 214
Cdd:PRK10887 148 ----INDAA---------------------------GRY----IE---------FCKSTFPNELS---LRGLKivVDCAN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 215 G----IGALKLREMehyfsqglsvqlfndgskgklnhlcGADFVKSHQKpPQGMEIksNERCCS---------------- 274
Cdd:PRK10887 181 GatyhIAPNVFREL-------------------------GAEVIAIGCE-PNGLNI--NDECGAtdpealqaavlaekad 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 275 ----FDGDADRIVYyyhdADGHFHLIDGDKIATLISsflKELLVEiGEsLNIGVVQTAYANGSSTRYLEEvMKVPVYCTK 350
Cdd:PRK10887 233 lgiaFDGDGDRVIM----VDHLGNLVDGDQLLYIIA---RDRLRR-GQ-LRGGVVGTLMSNMGLELALKQ-LGIPFVRAK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 351 TGVKHLHHKAQEFD--IGVyfEANGH---------GTALFST-AVEMKIKQSAEQLEDkkrkaakmLENIIDLFNQV-AD 417
Cdd:PRK10887 303 VGDRYVLEKLQEKGwrLGG--ENSGHilcldktttGDGIVAAlQVLAAMVRSGMSLAD--------LCSGMKLFPQVlIN 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1516481958 418 RRVISTTDAERQAvtpPGLQEAINDlVKKyKL---SRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSLAV 486
Cdd:PRK10887 373 VRFKPGADDPLES---EAVKAALAE-VEA-ELggrGRVLLRKSGTEPLIRVMVEGEDEAQVTALAERIADAV 439
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
275-478 |
2.57e-06 |
|
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: 49.86 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 275 FDGDADRI--VyyyhDADGHFhlIDGDKIATLISSFLKELLVEIGeslniGVVQTAyangSSTRYLEEVMK---VPVYCT 349
Cdd:cd05800 241 TDGDADRIgaV----DEKGNF--LDPNQILALLLDYLLENKGLRG-----PVVKTV----STTHLIDRIAEkhgLPVYET 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 350 KTGVKHLHHKAQEFD--IGVYfEANGHG------------TALFstAVEMkikqsaeqLEDKKRKAAKMLENIIDLFNQV 415
Cdd:cd05800 306 PVGFKYIAEKMLEEDvlIGGE-ESGGLGirghiperdgilAGLL--LLEA--------VAKTGKPLSELVAELEEEYGPS 374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1516481958 416 A-DRRVISTTDAERQAVT-----PPGLQEAINDLVK-------KYKL---SRAFVRPSGTEDVVRVYAEADSQESADHL 478
Cdd:cd05800 375 YyDRIDLRLTPAQKEAILeklknEPPLSIAGGKVDEvntidgvKLVLedgSWLLIRPSGTEPLLRIYAEAPSPEKVEAL 453
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
51-74 |
3.46e-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: 3.46e-05
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
58-76 |
6.27e-05 |
|
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars (e.g. between mannose-1-phosphate and mannose-6-phosphate or glucose-1-phosphate and glucose-6-phosphate) via a bisphosphorylated sugar intermediate. The reaction involves two phosphoryl transfers, with an intervening 180 degree reorientation of the reaction intermediate during catalysis. Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is thus, a simple example of processivity, as defined by multiple rounds of catalysis without release of substrate. Glucose-6-phosphate and glucose-1-phosphate are known to be utilized for energy metabolism and cell surface construction, respectively. PMM/PGM belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the phosphoglucomutases (PGM1 and PGM2). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100091 Cd Length: 443 Bit Score: 45.20 E-value: 6.27e-05
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
54-74 |
8.49e-05 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 45.06 E-value: 8.49e-05
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
454-480 |
4.44e-04 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 42.82 E-value: 4.44e-04
10 20
....*....|....*....|....*..
gi 1516481958 454 VRPSGTEDVVRVYAEadSQESADHLAH 480
Cdd:PRK07564 504 ARPSGTETTYKIYAE--SFEGDEHLHQ 528
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
123-164 |
5.15e-04 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 42.28 E-value: 5.15e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1516481958 123 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHY 164
Cdd:PRK09542 38 VVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIGLASTDQLYF 79
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
111-160 |
7.90e-04 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 41.97 E-value: 7.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1516481958 111 EKEAVNLQQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTP 160
Cdd:PLN02371 106 EKKKADGSGELRVSVGRDPRISGPRLADAVFAGLASAGLDVVDMGLATTP 155
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
297-375 |
4.01e-03 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 37.04 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1516481958 297 DGDKIATLISSFLKELLVEIGeslNIGVVQTAyangSSTRYLEEVMK---VPVYCTKTGVKHLHHKAQEFDIGVYFEANG 373
Cdd:pfam02880 1 DGDQILALLAKYLLEQGKLPP---GAGVVKTV----MSSLGLDRVAKklgGKLVRTPVGDKYVKEKMREEGALFGGEESG 73
|
..
gi 1516481958 374 HG 375
Cdd:pfam02880 74 HI 75
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
455-479 |
7.16e-03 |
|
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100094 [Multi-domain] Cd Length: 522 Bit Score: 38.77 E-value: 7.16e-03
10 20
....*....|....*....|....*
gi 1516481958 455 RPSGTEDVVRVYAEadSQESADHLA 479
Cdd:cd05801 490 RPSGTEDVYKIYAE--SFLSEEHLK 512
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
123-164 |
9.43e-03 |
|
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: 38.34 E-value: 9.43e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1516481958 123 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHY 164
Cdd:cd03088 39 VAVGRDLRPSSPRIAAACAAALRDAGFRVVDCGAVPTPALAL 80
|
|
| |
