|
Name |
Accession |
Description |
Interval |
E-value |
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
22-527 |
0e+00 |
|
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 (N-acetylglucosamine-phosphate mutase), is an essential enzyme found in eukaryotes that reversibly catalyzes the conversion of GlcNAc-6-phosphate into GlcNAc-1-phosphate as part of the UDP-N-acetylglucosamine (UDP-GlcNAc) biosynthetic pathway. UDP-GlcNAc is an essential metabolite that serves as the biosynthetic precursor of many glycoproteins and mucopolysaccharides. AGM1 is a member of the alpha-D-phosphohexomutase superfamily, which catalyzes the intramolecular phosphoryl transfer of sugar substrates. The alpha-D-phosphohexomutases have four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100088 Cd Length: 513 Bit Score: 891.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 22 QYGTAGFRTKAEHLDHVMFRMGLLAVLRSKQTKS-TIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLANAEEQ 100
Cdd:cd03086 1 SYGTAGFRTKAELLDSVVFRVGILAALRSKKLGGkTIGVMITASHNPVEDNGVKIVDPDGEMLEESWEPYATQLANASDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 101 DMQRVLIDI--SEKEAVNLQQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNTGGRYGKA 178
Cdd:cd03086 81 ELLVLVLMLisVKELNIDLSVPANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYLVRAANTEGAYGEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 179 TIEGYYQKLSKAFVELTKQASCSGDEYRSLKVDCANGIGALKLREMEHYFSQGLSVQLFNDGSKG--KLNHLCGADFVKS 256
Cdd:cd03086 161 TEEGYYEKLSKAFNELYNLLQDGGDEPEKLVVDCANGVGALKLKELLKRLKKGLSVKIINDGEEGpeLLNDGCGADYVKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 257 HQKPPQGMEIK-SNERCCSFDGDADRIVYYYHDADGHFHLIDGDKIATLISSFLKELL--VEIGESLNIGVVQTAYANGS 333
Cdd:cd03086 241 KQKPPRGFELKpPGVRCCSFDGDADRLVYFYPDSSNKFHLLDGDKIATLFAKFIKELLkkAGEELKLTIGVVQTAYANGA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 334 STRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFSTAVEMKIKqSAEQLEDKKRKAAKMLENIIDLFN 413
Cdd:cd03086 321 STKYLEDVLKVPVVCTPTGVKHLHHAAEEFDIGVYFEANGHGTVLFSESALAKIE-ENSSLSDEQEKAAKTLLAFSRLIN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 414 QAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQVADRRVISTTDAERQAVTPPGLQEAINDLVKKYKLSRA 493
Cdd:cd03086 400 QTVGDAISDMLAVELILAALGWSPQDWDNLYTDLPNRQLKVKVPDRSVIKTTDAERRLVEPKGLQDKIDAIVAKYNNGRA 479
|
490 500 510
....*....|....*....|....*....|....
gi 315707010 494 FVRPSGTEDVVRVYAEADSQESADHLAHEVSLAV 527
Cdd:cd03086 480 FVRPSGTEDVVRVYAEAATQEEADELANEVAELV 513
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
1-538 |
0e+00 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 677.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 1 MDLGAITKYSALHAKPNGLILQYGTAGFRTKAEHLDHVMFRMGLLAVLRSKQTKSTIGVMVTASHNPEEDNGVKLVDPLG 80
Cdd:PLN02895 4 IQRASLLAASSRFPPPQGVRFSYGTAGFRTDASLLESTVFRVGILAALRSLKTGAATGLMITASHNPVSDNGVKIVDPSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 81 EMLAPSWEEHATCLANAE-EQDMQRVLIDISEKEAVNL---QQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGL 156
Cdd:PLN02895 84 GMLPQAWEPFADALANAPdPDALVQLIREFVKKENIPAvggNPPAEVLLGRDTRPSGPALLAAALKGVRAIGARAVDMGI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 157 LTTPQLHYMVYCRNTGGrygKATIEGYYQKLSKAF---VELTKQASCSGDEYRSLKVDCANGIGALKLREMEHYFSqGLS 233
Cdd:PLN02895 164 LTTPQLHWMVRAANKGM---KATESDYFEQLSSSFralLDLIPNGSGDDRADDKLVVDGANGVGAEKLETLKKALG-GLD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 234 VQLFNDG--SKGKLNHLCGADFVKSHQKPPQGMEIK-SNERCCSFDGDADRIVYYYHDADG-HFHLIDGDKIATLISSFL 309
Cdd:PLN02895 240 LEVRNSGkeGEGVLNEGVGADFVQKEKVPPTGFASKdVGLRCASLDGDADRLVYFYVSSAGsKIDLLDGDKIASLFALFI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 310 KELLVEIGES---------LNIGVVQTAYANGSSTRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFS 380
Cdd:PLN02895 320 KEQLRILNGNgnekpeellVRLGVVQTAYANGASTAYLKQVLGLEVVCTPTGVKYLHEAAAEFDIGVYFEANGHGTVLFS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 381 TAVEMKIKQSAEQLEDKKR-----KAAKMLENIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQ 455
Cdd:PLN02895 400 ERFLDWLEAAAAELSSKAKgseahKAARRLLAVSRLINQAVGDALSGLLLVEAILQYRGWSLAEWNALYQDLPSRQLKVK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 456 VADRRVISTTDAERQAVTPPGLQEAINDLVKKYKLSRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSLAVFQLAGGIG 535
Cdd:PLN02895 480 VADRTAITTTDAETVVVRPAGLQDAIDAEVAKYPRGRAFVRPSGTEDVVRVYAEASTQEAADSLAREVARLVYDLLGGVG 559
|
...
gi 315707010 536 ERP 538
Cdd:PLN02895 560 PPP 562
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
5-533 |
0e+00 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 608.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 5 AITKYSALH-AKPNGLIlqYGTAGFRTKAE--HLDHVMFRMGLLAVLRSKQTKS--------TIGVMVTASHNPEEDNGV 73
Cdd:PTZ00302 16 CGSKFPLRHsAIENPLT--YGTAGFRTKAElpPLEPVAYRVGILAALRSFLYGGkrakrgnkSVGVMITASHNPIQDNGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 74 KLVDPLGEMLAPSWEEHATCLANAE-EQDMQRVLIDISEKEAVNLQQD-----------AFVVIGRDTRPSSEKLSQSVI 141
Cdd:PTZ00302 94 KIIDPDGGMLEESWEKICTDFANARtGEDLVSVLMDCLTEHGIKLSNLkldlnksncskAKVHVGRDTRPSSPELVSALL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 142 DGVTVLGGQFH-DYGLLTTPQLHYMVYCRNTGGR-YGKATIEGYYQKLSKAFVELTKQASCSGDEYRS------LKVDCA 213
Cdd:PTZ00302 174 RGLKLLIGSNVrNFGIVTTPQLHFLVAFANGLGVdVVESSDELYYAYLLAAFKELYRTLQEGGPVDLTqnnskiLVVDCA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 214 NGIGALKLREMEHYFSQ---GLSVQLFNDGSKGKLNHLCGADFVKSHQKPPQGMEIK---SNERCCSFDGDADRIVYYYH 287
Cdd:PTZ00302 254 NGVGGYKIKRFFEALKQlgiEIIPININCDEEELLNDKCGADYVQKTRKPPRAMKEWpgdEETRVASFDGDADRLVYFFP 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 288 DADGH--FHLIDGDKIATLISSFLKELLVEIG--ESLNIGVVQTAYANGSSTRYLEEVMK-VPVYCTKTGVKHLHHKAQE 362
Cdd:PTZ00302 334 DKDGDdkWVLLDGDRIAILYAMLIKKLLGKIQlkKKLDIGVVQTAYANGASTNYLNELLGrLRVYCAPTGVKNLHPKAHK 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 363 FDIGVYFEANGHGTALFStavEMKIKQSAEQLEDK--KRKAAKMLENIIDLFNQAAGDAISDMLVIEAILALKGLTVQQW 440
Cdd:PTZ00302 414 YDIGIYFEANGHGTVLFN---EKALAEWAKFLAKQnaLNSACRQLEKFLRLFNQTIGDAISDLLAVELALAFLGLSFQDW 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 441 DALYTDLPNRQLKVQVADRRVISTTDAERQAVTPPGLQEAINDLVKKYK-LSRAFVRPSGTEDVVRVYAEADSQESADHL 519
Cdd:PTZ00302 491 LNLYTDLPSRQDKVTVKDRTLITNTEDETRLLEPKGLQDKIDAIVSKYDnAARAFIRPSGTEPVVRVYAEAPTLEQADEL 570
|
570
....*....|....
gi 315707010 520 AHEVSLAVFQLAGG 533
Cdd:PTZ00302 571 ANEVKGLVLRYCSG 584
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
23-524 |
2.13e-46 |
|
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this family include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). These enzymes play important and diverse roles in carbohydrate metabolism in organisms from bacteria to humans. Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100086 [Multi-domain] Cd Length: 355 Bit Score: 166.38 E-value: 2.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 23 YGTAGFRTKA--EHLDHVMFRMGLLAVlrskqtkSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLANAEEQ 100
Cdd:cd03084 2 FGTSGVRGVVgdDITPETAVALGQAIG-------STGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 101 DmqrvlidisekeavnlqqdafvvigrdtRPSSEKLSQSVidgvtvlggqfhdygllttpqlhymvycrntggrYGKATI 180
Cdd:cd03084 75 P----------------------------SAVAYELGGSV----------------------------------KAVDIL 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 181 EGYYQKL-SKAFVELTKQAScsgdeyRSLKVDCANGIGALKLREM-EHYfsqGLSVQLFN---DGSKGKLNHLCGADfvK 255
Cdd:cd03084 93 QRYFEALkKLFDVAALSNKK------FKVVVDSVNGVGGPIAPQLlEKL---GAEVIPLNcepDGNFGNINPDPGSE--T 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 256 SHQKPPQGMEIKSNERCCSFDGDADRIVYYYHDadghFHLIDGDKIATLISsflKELLVEIGesLNIGVVQTAYANGSST 335
Cdd:cd03084 162 NLKQLLAVVKAEKADFGVAFDGDADRLIVVDEN----GGFLDGDELLALLA---VELFLTFN--PRGGVVKTVVSSGALD 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 336 RYLEEvMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGtalfstavemkikqsaeqledkkrkaakmleniIDLFNQA 415
Cdd:cd03084 233 KVAKK-LGIKVIRTKTGFKWVGEAMQEGDVVLGGEESGGV---------------------------------IFPEFHP 278
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 416 AGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQvadrrvisttdaerqavtppglqeaindlvkkyklSRAFV 495
Cdd:cd03084 279 GRDGISAALLLLEILANLGKSLSELFSELPRYYYIRLKVR-----------------------------------GWVLV 323
|
490 500
....*....|....*....|....*....
gi 315707010 496 RPSGTEDVVRVYAEADSQESADHLAHEVS 524
Cdd:cd03084 324 RASGTEPAIRIYAEADTQEDVEQIKKEAR 352
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
123-523 |
4.32e-31 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 126.08 E-value: 4.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 123 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNTGG--------------------RYGK----- 177
Cdd:COG1109 44 VVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVPTPALAFAVRHLGADGgimitashnppeyngikffdADGGklspe 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 178 --ATIEGYYQKLSKAFVELTKQASCS-----GDEY--------------RSLKV--DCANGIGALK----LREMehyfsq 230
Cdd:COG1109 124 eeKEIEALIEKEDFRRAEAEEIGKVTriedvLEAYiealkslvdealrlRGLKVvvDCGNGAAGGVaprlLREL------ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 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 315707010 297 DGDKIATLISSFLKEllveigESLNIGVVQTAyangSSTRYLEEVMK---VPVYCTKTGVKHLHHKAQEFD--IGvyFEA 371
Cdd:COG1109 260 DGDQLLALLARYLLE------KGPGGTVVVTV----MSSLALEDIAEkhgGEVVRTKVGFKYIKEKMRETGavLG--GEE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 372 NGHgtalfstavemkikqsaeqledkkrkaakmlenIIDLFNQAAGDAI-SDMLVIEaILALKGLTVQQWDALYTDLPNR 450
Cdd:COG1109 328 SGG---------------------------------IIFPDFVPTDDGIlAALLLLE-LLAKQGKSLSELLAELPRYPQP 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 315707010 451 QLKVQVADRRVISTTDAE-RQAVTPPGLQEAINDLvkKYKL---SRAFVRPSGTEDVVRVYAEADSQESADHLAHEV 523
Cdd:COG1109 374 EINVRVPDEEKIGAVMEKlREAVEDKEELDTIDGV--KVDLedgGWVLVRPSGTEPLLRVYAEAKDEEEAEELLAEL 448
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
57-527 |
3.66e-25 |
|
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also designated in MrsA and YhbF E. coli, UreC in Helicobacter pylori, and femR315 or FemD in Staphlococcus aureus. It converts glucosamine-6-phosphate to glucosamine-1-phosphate as part of the pathway toward UDP-N-acetylglucosamine for peptidoglycan and lipopolysaccharides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]
Pssm-ID: 130522 Cd Length: 443 Bit Score: 108.22 E-value: 3.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 57 IGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEhatclanaeeqdmqrvlidisEKEAVNLQQDAFvvigrdTRPSSEKL 136
Cdd:TIGR01455 91 AGVMISASHNPYEDNGIKFFGPGGFKLDDATEA---------------------AIEALLDEADPL------PRPESEGL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 137 SQSVidgvtvlggqfhdygllttpqlhymvycrntggRYGKATieGYYQKLSKAfvELTKQASCSGdeyrsLKV--DCAN 214
Cdd:TIGR01455 144 GRVK---------------------------------RYPDAV--GRYIEFLKS--TLPRGLTLSG-----LKVvlDCAN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 215 GiGALKLREMEhYFSQGLSVQLFNDGSKG-KLNHLCGADFVKSHQKP--PQGMEIKsnercCSFDGDADRIVYYyhDADG 291
Cdd:TIGR01455 182 G-AAYKVAPHV-FRELGAEVIAIGVEPDGlNINDGCGSTHLDALQKAvrEHGADLG-----IAFDGDADRVLAV--DANG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 292 hfHLIDGDKIATLISSFLKELlveiGESLNIGVVQTAYANGSSTRYLEEvMKVPVYCTKTGVKHLHHKAQEFDIGVYFEA 371
Cdd:TIGR01455 253 --RIVDGDQILYIIARALKES----GELAGNTVVATVMSNLGLERALEK-LGLTLIRTAVGDRYVLEEMRESGYNLGGEQ 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 372 NGHgtalfstavemkikqsaeqledkkrkaakmlenIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQ 451
Cdd:TIGR01455 326 SGH---------------------------------IILLDYSTTGDGIVSALQVLTIMKKSGSTLSELAAEFVPYPQTL 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 315707010 452 LKVQVADRRvisttdaeRQAVTPPGLQEAINDLVKKY-KLSRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSLAV 527
Cdd:TIGR01455 373 VNVRVADRK--------LAAAEAPAVKAAIEDAEAELgGTGRILLRPSGTEPLIRVMVEAADEELVQQLADTLADVV 441
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
51-524 |
4.25e-24 |
|
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the alpha-D-phosphohexomutase superfamily. It is required for the interconversion of glucosamine-6-phosphate and glucosamine-1-phosphate in the biosynthetic pathway of UDP-N-acetylglucosamine, an essential precursor to components of the cell envelope. In order to be active, GlmM must be phosphorylated, which can occur via autophosphorylation or by the Ser/Thr kinase StkP. GlmM functions in a classical ping-pong bi-bi mechanism with glucosamine-1,6-diphosphate as an intermediate. Other members of the alpha-D-phosphohexomutase superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100095 Cd Length: 434 Bit Score: 104.87 E-value: 4.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 51 KQTKSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEhatclanaeeqdmqrvlidisEKEAVNLQqdafvviGRDTR 130
Cdd:cd05802 84 RKLRADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVEE---------------------EIEALIDK-------ELELP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 131 PSSEKLsqsvidgvtvlgGQFHDYgllTTPQLHYMVYCRNTGGRygkatiegyyQKLSKafveltkqascsgdeyrsLKV 210
Cdd:cd05802 136 PTGEKI------------GRVYRI---DDARGRYIEFLKSTFPK----------DLLSG------------------LKI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 211 --DCANG----IGALKLREMehyfsqGLSVQLFNDGSKG-KLNHLCGADFVKSHQKppqgmEIKSNERCC--SFDGDADR 281
Cdd:cd05802 173 vlDCANGaaykVAPEVFREL------GAEVIVINNAPDGlNINVNCGSTHPESLQK-----AVLENGADLgiAFDGDADR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 282 IVYYyhDADGHfhLIDGDKIATLISSFLKELlveiGESLNIGVVQTAYANGSSTRYLEEvMKVPVYCTKTGVKHLHHKAQ 361
Cdd:cd05802 242 VIAV--DEKGN--IVDGDQILAICARDLKER----GRLKGNTVVGTVMSNLGLEKALKE-LGIKLVRTKVGDRYVLEEML 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 362 EFDIGVYFEANGHgtalfstavemkikqsaeqledkkrkaakmlenIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWD 441
Cdd:cd05802 313 KHGANLGGEQSGH---------------------------------IIFLDHSTTGDGLLTALQLLAIMKRSGKSLSELA 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 442 ALYTDLPNRQLKVQVADRRVISTtdaerqavtPPGLQEAINDLVKKYKLS-RAFVRPSGTEDVVRVYAEADSQESADHLA 520
Cdd:cd05802 360 SDMKLYPQVLVNVRVKDKKALLE---------NPRVQAAIAEAEKELGGEgRVLVRPSGTEPLIRVMVEGEDEELVEKLA 430
|
....
gi 315707010 521 HEVS 524
Cdd:cd05802 431 EELA 434
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
58-523 |
1.85e-17 |
|
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been characterized as the archaeal protein responsible for the second step of UDP-GlcNAc biosynthesis. This GlmM protein catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. The first-characterized bacterial GlmM protein is modeled by TIGR01455. These two families are members of the larger phosphoglucomutase/phosphomannomutase family (characterized by three domains: pfam02878, pfam02879 and pfam02880), but are not nearest neighbors to each other. This model also includes a number of sequences from non-archaea in the Bacteroides, Chlorobi, Chloroflexi, Planctomycetes and Spirochaetes lineages. Evidence supporting their inclusion in this equivalog as having the same activity comes from genomic context and phylogenetic profiling. A large number of these organisms are known to produce exo-polysaccharide and yet only appeared to contain the GlmS enzyme of the GlmSMU pathway for UDP-GlcNAc biosynthesis (GenProp0750). In some organisms including Leptospira, this archaeal GlmM is found adjacent to the GlmS as well as a putative GlmU non-orthologous homolog. Phylogenetic profiling of the GlmS-only pattern using PPP identifies members of this archaeal GlmM family as the highest-scoring result. [Central intermediary metabolism, Amino sugars]
Pssm-ID: 274906 Cd Length: 443 Bit Score: 84.87 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 58 GVMVTASHNPEEDNGVKLVDPLGEMLAPsweehatclanaeeqDMQRVLIDISEKEavnlqqDAFVV----IGRDTRPSS 133
Cdd:TIGR03990 89 GIMITASHNPPEYNGIKLLNSDGTELSR---------------EQEEEIEEIAESG------DFERAdwdeIGTVTSDED 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 134 ekLSQSVIDGVtvlggqfhdygllttpqlhymvycrntggrygkatiegyyqklsKAFVELTKQAScsgdeyRSLKV--D 211
Cdd:TIGR03990 148 --AIDDYIEAI--------------------------------------------LDKVDVEAIRK------KGFKVvvD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 212 CANGIGALK----LREMehyfsqGLSVQLFNDGSKGK------------LNHLC------GADFVKSHqkppqgmeiksn 269
Cdd:TIGR03990 176 CGNGAGSLTtpylLREL------GCKVITLNCQPDGTfpgrnpeptpenLKDLSalvkatGADLGIAH------------ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 270 erccsfDGDADRIVYYyhDADGHFhlIDGDKIATLissFLKELLVEIGESLnigVVqtayaNGSSTRYLEEVMK---VPV 346
Cdd:TIGR03990 238 ------DGDADRLVFI--DEKGRF--IGGDYTLAL---FAKYLLEHGGGKV---VT-----NVSSSRAVEDVAErhgGEV 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 347 YCTKTGVKHLHHKAQEFDIGVYFEANGHgtalfstavemkikqsaeqledkkrkaakmlenIIDLFNQAAGDAISDMLVI 426
Cdd:TIGR03990 297 IRTKVGEVNVAEKMKEEGAVFGGEGNGG---------------------------------WIFPDHHYCRDGLMAAALF 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 427 EAILALKGLTVQQWDALYTDLPNRQLKVQVADRRVISTTDAERQAVTppglQEAINDL--VK-KYKLSRAFVRPSGTEDV 503
Cdd:TIGR03990 344 LELLAEEGKPLSELLAELPKYPMSKEKVELPDEDKEEVMEAVEEEFA----DAEIDTIdgVRiDFEDGWVLVRPSGTEPI 419
|
490 500
....*....|....*....|
gi 315707010 504 VRVYAEADSQESADHLAHEV 523
Cdd:TIGR03990 420 VRIYAEAKTEERAEELLEEG 439
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
58-523 |
3.68e-16 |
|
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100089 Cd Length: 439 Bit Score: 81.08 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 58 GVMVTASHNPEEDNGVKLVDPLG-EMlapsweehatclanaeEQDMQRVLIDISEKEAVNLQqdAFVVIGRDTRPSsekl 136
Cdd:cd03087 86 GVMITASHNPPEYNGIKLVNPDGtEF----------------SREQEEEIEEIIFSERFRRV--AWDEVGSVRRED---- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 137 sqSVIDgvtvlggqfhDYgllttpqlhymvycrntggrygkatIEGYYQKLSKafveltkqascsgDEYRSLKV--DCAN 214
Cdd:cd03087 144 --SAID----------EY-------------------------IEAILDKVDI-------------DGGKGLKVvvDCGN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 215 GIGALK----LREMehyfsqGLSVQLFN---DG---------SKGKLNHLC------GADFVKSHqkppqgmeiksnerc 272
Cdd:cd03087 174 GAGSLTtpylLREL------GCKVITLNanpDGffpgrppepTPENLSELMelvratGADLGIAH--------------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 273 csfDGDADRIVYYyhDADGHFhlIDGDKIATLISsflKELLVEIGeslniGVVQTAYangSSTRYLEEVMK---VPVYCT 349
Cdd:cd03087 233 ---DGDADRAVFV--DEKGRF--IDGDKLLALLA---KYLLEEGG-----GKVVTPV---DASMLVEDVVEeagGEVIRT 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 350 KTGVKHLHHKAQEFDIGVYFEANGHG-TALFSTAVemkikqsaeqleDKKRKAAKMLEniidlfnqaagdaisdmLVIEA 428
Cdd:cd03087 295 PVGDVHVAEEMIENGAVFGGEPNGGWiFPDHQLCR------------DGIMTAALLLE-----------------LLAEE 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 429 ilalKGLtvqqwDALYTDLPNRQLKvqvadRRVISTTDAERQAVtPPGLQEAINDLVKK------YKLSR----AFVRPS 498
Cdd:cd03087 346 ----KPL-----SELLDELPKYPLL-----REKVECPDEKKEEV-MEAVEEELSDADEDvdtidgVRIEYedgwVLIRPS 410
|
490 500
....*....|....*....|....*
gi 315707010 499 GTEDVVRVYAEADSQESADHLAHEV 523
Cdd:cd03087 411 GTEPKIRITAEAKTEERAKELLEEG 435
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
475-527 |
1.29e-10 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 57.28 E-value: 1.29e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 315707010 475 PGLQEAINDLVKKYKL--SRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSLAV 527
Cdd:pfam00408 16 AAILKVFADAEKILGEdgRRLDVRPSGTEPVLRVMVEGDSDEELARLADEIADLL 70
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
52-520 |
3.32e-09 |
|
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate guanyltransferase domain in a protein of unknown function that is found in both prokaryotes and eukaryotes. This domain belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100096 Cd Length: 445 Bit Score: 59.24 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 52 QTKSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSweehatclanaeeqDMQRVLIDISEKEAVNLQQDAfvvIGRDTrp 131
Cdd:cd05803 85 QSQASGGIIITASHNPPQWNGLKFIGPDGEFLTPD--------------EGEEVLSCAEAGSAQKAGYDQ---LGEVT-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 132 SSEKLSQSVIDGVtvlggqfhdygllttpqlhymvycrntggrygkatiegyyqkLSKAFVELTKQAScsgdeyRSLKV- 210
Cdd:cd05803 146 FSEDAIAEHIDKV------------------------------------------LALVDVDVIKIRE------RNFKVa 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 211 -DCANGIGALKLREMEHyfSQGLSVQLFNDGSKGKLNHlcgadfvkshqkPPQgmEIKSN---------ERCCSF----D 276
Cdd:cd05803 178 vDSVNGAGGLLIPRLLE--KLGCEVIVLNCEPTGLFPH------------TPE--PLPENltqlcaavkESGADVgfavD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 277 GDADRIVyyyhdadghfhLIDGDKIA-----TLISSFLkELLVEIGESLNIGVvqtayaNGSSTRYLEEVMK---VPVYC 348
Cdd:cd05803 242 PDADRLA-----------LVDEDGRPigeeyTLALAVD-YVLKYGGRKGPVVV------NLSTSRALEDIARkhgVPVFR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 349 TKTGVKHLHHKAQEFDIGVYFEANGhgtalfstavemkikqsaeqledkkrkaakmleNIIDLFNQAAGDAISDMLVIEA 428
Cdd:cd05803 304 SAVGEANVVEKMKEVDAVIGGEGNG---------------------------------GVILPDVHYGRDSLVGIALVLQ 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 429 ILALKGLTVQQWDALYTDLPNRQLKVQVADR---RVISTTDAE---RQAVTPPGLQEAINDlvkkyklSRAFVRPSGTED 502
Cdd:cd05803 351 LLAASGKPLSEIVDELPQYYISKTKVTIAGEaleRLLKKLEAYfkdAEASTLDGLRLDSED-------SWVHVRPSNTEP 423
|
490
....*....|....*...
gi 315707010 503 VVRVYAEADSQESADHLA 520
Cdd:cd05803 424 IVRIIAEAPTQDEAEALA 441
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
123-523 |
1.26e-08 |
|
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars (e.g. between mannose-1-phosphate and mannose-6-phosphate or glucose-1-phosphate and glucose-6-phosphate) via a bisphosphorylated sugar intermediate. The reaction involves two phosphoryl transfers, with an intervening 180 degree reorientation of the reaction intermediate during catalysis. Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is thus, a simple example of processivity, as defined by multiple rounds of catalysis without release of substrate. Glucose-6-phosphate and glucose-1-phosphate are known to be utilized for energy metabolism and cell surface construction, respectively. PMM/PGM belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the phosphoglucomutases (PGM1 and PGM2). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100091 Cd Length: 443 Bit Score: 57.52 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 123 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHY-----------MV--------Y-----CRNTGGRYG-- 176
Cdd:cd03089 39 VVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPVLYFatfhldadggvMItashnppeYngfkiVIGGGPLSGed 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 177 ----KATIEGYYQKLSKAFVELTKQasCSGDEY------------RSLK--VDCANGIGALKLREMEhyfsQGL---SVQ 235
Cdd:cd03089 119 iqalRERAEKGDFAAATGRGSVEKV--DILPDYidrllsdiklgkRPLKvvVDAGNGAAGPIAPQLL----EALgceVIP 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 236 LFN--DGS----------KGKLNHLC------GADFvkshqkppqGMeiksnerccSFDGDADRIVYYyhDADGHFhlID 297
Cdd:cd03089 193 LFCepDGTfpnhhpdptdPENLEDLIaavkenGADL---------GI---------AFDGDGDRLGVV--DEKGEI--IW 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 298 GDKIATLISsflKELLVEIGESLNIGVVQTayangssTRYLEEVMK----VPVYCtKTGVKHLHHKAQEFDIGVYFEANG 373
Cdd:cd03089 251 GDRLLALFA---RDILKRNPGATIVYDVKC-------SRNLYDFIEeaggKPIMW-KTGHSFIKAKMKETGALLAGEMSG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 374 HgtaLFstavemkikqsaeqledkkrkaakmleniidlFNQA---AGDAISDMLVIEAILALKGLTVqqwDALYTDLPNR 450
Cdd:cd03089 320 H---IF--------------------------------FKDRwygFDDGIYAALRLLELLSKSGKTL---SELLADLPKY 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 451 ----QLKVQVADRRVISTTDAERQAVTPPGLQeaINDL--VK-KYKLSRAFVRPSGTEDVVRVYAEADSQESADHLAHEV 523
Cdd:cd03089 362 fstpEIRIPVTEEDKFAVIERLKEHFEFPGAE--IIDIdgVRvDFEDGWGLVRASNTEPVLVLRFEADTEEGLEEIKAEL 439
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
123-166 |
2.28e-07 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 50.30 E-value: 2.28e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 315707010 123 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMV 166
Cdd:pfam02878 43 VVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTPAVSFAT 86
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
58-100 |
3.23e-07 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 49.53 E-value: 3.23e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 315707010 58 GVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLANAEEQ 100
Cdd:pfam02878 94 GIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKEDF 136
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
58-527 |
5.48e-07 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 52.06 E-value: 5.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 58 GVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEhatcLANAE-EQDMQRVlidisekEAVNLqqdafvviGRDTRpssekl 136
Cdd:PRK10887 93 GIVISASHNPYYDNGIKFFSADGTKLPDEVEL----AIEAElDKPLTCV-------ESAEL--------GKASR------ 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 137 sqsvIDGVTvlggqfhdygllttpqlhymvycrntgGRYgkatIEgyyqklskaFVELTKQASCSgdeYRSLK--VDCAN 214
Cdd:PRK10887 148 ----INDAA---------------------------GRY----IE---------FCKSTFPNELS---LRGLKivVDCAN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 215 G----IGALKLREMehyfsqglsvqlfndgskgklnhlcGADFVKSHQKpPQGMEIksNERCCS---------------- 274
Cdd:PRK10887 181 GatyhIAPNVFREL-------------------------GAEVIAIGCE-PNGLNI--NDECGAtdpealqaavlaekad 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 275 ----FDGDADRIVYyyhdADGHFHLIDGDKIATLISsflKELLVEiGEsLNIGVVQTAYANGSSTRYLEEvMKVPVYCTK 350
Cdd:PRK10887 233 lgiaFDGDGDRVIM----VDHLGNLVDGDQLLYIIA---RDRLRR-GQ-LRGGVVGTLMSNMGLELALKQ-LGIPFVRAK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 351 TGVKHLHHKAQEFD--IGVyfEANGHgtalfstavemkikqsaeqledkkrkaakmlenIIDLFNQAAGDAI-SDMLVIE 427
Cdd:PRK10887 303 VGDRYVLEKLQEKGwrLGG--ENSGH---------------------------------ILCLDKTTTGDGIvAALQVLA 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 428 AiLALKGLTVQQWDALYTDLPNRQLKVQVADRRVISTTDAERQAVtppgLQEAINDLVKKyklSRAFVRPSGTEDVVRVY 507
Cdd:PRK10887 348 A-MVRSGMSLADLCSGMKLFPQVLINVRFKPGADDPLESEAVKAA----LAEVEAELGGR---GRVLLRKSGTEPLIRVM 419
|
490 500
....*....|....*....|
gi 315707010 508 AEADSQESADHLAHEVSLAV 527
Cdd:PRK10887 420 VEGEDEAQVTALAERIADAV 439
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
418-519 |
3.63e-05 |
|
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily and is found in both archaea and bacteria. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four structural domains (subdomains) with a centrally located active site formed by four loops, one from each subdomain. All four subdomains are included in this alignment model.
Pssm-ID: 100093 Cd Length: 461 Bit Score: 46.39 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 418 DAI-SDMLVIEAIlALKGLTVqqwDALYTDLpnrQLKVQVA--DRRVISTTDAERQAVT-----PPGLQEAINDLVK--- 486
Cdd:cd05800 341 DGIlAGLLLLEAV-AKTGKPL---SELVAEL---EEEYGPSyyDRIDLRLTPAQKEAILeklknEPPLSIAGGKVDEvnt 413
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 315707010 487 ----KYKL---SRAFVRPSGTEDVVRVYAEADSQESADHL 519
Cdd:cd05800 414 idgvKLVLedgSWLLIRPSGTEPLLRIYAEAPSPEKVEAL 453
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
51-74 |
4.29e-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: 4.29e-05
10 20
....*....|....*....|....
gi 315707010 51 KQTKSTIGVMVTASHNPEEDNGVK 74
Cdd:cd05799 93 RHLGADAGIMITASHNPKEYNGYK 116
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
58-76 |
7.36e-05 |
|
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars (e.g. between mannose-1-phosphate and mannose-6-phosphate or glucose-1-phosphate and glucose-6-phosphate) via a bisphosphorylated sugar intermediate. The reaction involves two phosphoryl transfers, with an intervening 180 degree reorientation of the reaction intermediate during catalysis. Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is thus, a simple example of processivity, as defined by multiple rounds of catalysis without release of substrate. Glucose-6-phosphate and glucose-1-phosphate are known to be utilized for energy metabolism and cell surface construction, respectively. PMM/PGM belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the phosphoglucomutases (PGM1 and PGM2). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100091 Cd Length: 443 Bit Score: 45.20 E-value: 7.36e-05
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
54-74 |
1.01e-04 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 45.06 E-value: 1.01e-04
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
495-521 |
5.91e-04 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 42.82 E-value: 5.91e-04
10 20
....*....|....*....|....*..
gi 315707010 495 VRPSGTEDVVRVYAEadSQESADHLAH 521
Cdd:PRK07564 504 ARPSGTETTYKIYAE--SFEGDEHLHQ 528
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|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
123-164 |
6.49e-04 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 42.28 E-value: 6.49e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 315707010 123 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHY 164
Cdd:PRK09542 38 VVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIGLASTDQLYF 79
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
111-160 |
9.63e-04 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 41.97 E-value: 9.63e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 315707010 111 EKEAVNLQQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTP 160
Cdd:PLN02371 106 EKKKADGSGELRVSVGRDPRISGPRLADAVFAGLASAGLDVVDMGLATTP 155
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
58-74 |
2.00e-03 |
|
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily and is found in both archaea and bacteria. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four structural domains (subdomains) with a centrally located active site formed by four loops, one from each subdomain. All four subdomains are included in this alignment model.
Pssm-ID: 100093 Cd Length: 461 Bit Score: 41.00 E-value: 2.00e-03
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
297-375 |
4.55e-03 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 37.04 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707010 297 DGDKIATLISSFLKELLVEIGeslNIGVVQTAyangSSTRYLEEVMK---VPVYCTKTGVKHLHHKAQEFDIGVYFEANG 373
Cdd:pfam02880 1 DGDQILALLAKYLLEQGKLPP---GAGVVKTV----MSSLGLDRVAKklgGKLVRTPVGDKYVKEKMREEGALFGGEESG 73
|
..
gi 315707010 374 HG 375
Cdd:pfam02880 74 HI 75
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
496-520 |
8.44e-03 |
|
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100094 [Multi-domain] Cd Length: 522 Bit Score: 38.77 E-value: 8.44e-03
10 20
....*....|....*....|....*
gi 315707010 496 RPSGTEDVVRVYAEadSQESADHLA 520
Cdd:cd05801 490 RPSGTEDVYKIYAE--SFLSEEHLK 512
|
|
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