|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
1-556 |
0e+00 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 967.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 1 MDEIQIASILKSSELFPIPQGVKLSYGTAGFRGDAKLLESTVYRVGILSALRSLKLGsATVGLMITASHNKVSDNGIKVS 80
Cdd:PLN02895 1 MDEIQRASLLAASSRFPPPQGVRFSYGTAGFRTDASLLESTVFRVGILAALRSLKTG-AATGLMITASHNPVSDNGVKIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 81 DPSGFMLSQEWEPFADQIANASSPEELVSLIRKFMEKEEIAIGENNKGAEVWLGRDTRPSGESLLRAGEIGVGSIlGSVA 160
Cdd:PLN02895 80 DPSGGMLPQAWEPFADALANAPDPDALVQLIREFVKKENIPAVGGNPPAEVLLGRDTRPSGPALLAAALKGVRAI-GARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 161 IDIGILTTPQLHWMVRAKNKGLKATENDYFENLSTSFRCLIDLIPSSGNDKLEISKLLVDGANGVGGQKIEKLRGSLSNL 240
Cdd:PLN02895 159 VDMGILTTPQLHWMVRAANKGMKATESDYFEQLSSSFRALLDLIPNGSGDDRADDKLVVDGANGVGAEKLETLKKALGGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 241 DVEIRNTGRDG-GVLNEGVGADFVQKEKVLPVGFGFKDVGMRCASLDGDADRLVYFYIPSDSSeKVELLDGDKILSLFAL 319
Cdd:PLN02895 239 DLEVRNSGKEGeGVLNEGVGADFVQKEKVPPTGFASKDVGLRCASLDGDADRLVYFYVSSAGS-KIDLLDGDKIASLFAL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 320 FIKEQLNALEDDEERK----QSRLGVVQTAYANGASTDYLKH-LGLDVVFAKTGVKHLHEKAAEFDIGIYFEANGHGTIL 394
Cdd:PLN02895 318 FIKEQLRILNGNGNEKpeelLVRLGVVQTAYANGASTAYLKQvLGLEVVCTPTGVKYLHEAAAEFDIGVYFEANGHGTVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 395 FSESFLSWLVSKQKDLTAKGQGgSEEHKAVSRLMAVSNLINQAVGDALSGVLLVEVILQHLGWSIEKWNELYKDLPSRQI 474
Cdd:PLN02895 398 FSERFLDWLEAAAAELSSKAKG-SEAHKAARRLLAVSRLINQAVGDALSGLLLVEAILQYRGWSLAEWNALYQDLPSRQL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 475 KVEVPDRTAVVTTSEETEALRPMGIQDAINSEIKKYSRGRAFIRPSGTEDVVRVYAEASTQEDADSLANSVAQLVKSFLG 554
Cdd:PLN02895 477 KVKVADRTAITTTDAETVVVRPAGLQDAIDAEVAKYPRGRAFVRPSGTEDVVRVYAEASTQEAADSLAREVARLVYDLLG 556
|
..
gi 19715620 555 SS 556
Cdd:PLN02895 557 GV 558
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
25-549 |
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: 782.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 25 SYGTAGFRGDAKLLESTVYRVGILSALRSLKLGSATVGLMITASHNKVSDNGIKVSDPSGFMLSQEWEPFADQIANASSP 104
Cdd:cd03086 1 SYGTAGFRTKAELLDSVVFRVGILAALRSKKLGGKTIGVMITASHNPVEDNGVKIVDPDGEMLEESWEPYATQLANASDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 105 EELVSLIRKFMEKEEIAIgeNNKGAEVWLGRDTRPSGESLLRAGEIGVGSiLGSVAIDIGILTTPQLHWMVRAKNKGL-- 182
Cdd:cd03086 81 ELLVLVLMLISVKELNID--LSVPANVFVGRDTRPSGPALLQALLDGLKA-LGGNVIDYGLVTTPQLHYLVRAANTEGay 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 183 -KATENDYFENLSTSFRCLIDLIPSSGNdklEISKLLVDGANGVGGQKIEKLRGSLS-NLDVEIRNTGRDG-GVLNEGVG 259
Cdd:cd03086 158 gEPTEEGYYEKLSKAFNELYNLLQDGGD---EPEKLVVDCANGVGALKLKELLKRLKkGLSVKIINDGEEGpELLNDGCG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 260 ADFVQKEKVLPVGFGFKDVGMRCASLDGDADRLVYFYIpsDSSEKVELLDGDKILSLFALFIKEQLnalEDDEERKQSRL 339
Cdd:cd03086 235 ADYVKTKQKPPRGFELKPPGVRCCSFDGDADRLVYFYP--DSSNKFHLLDGDKIATLFAKFIKELL---KKAGEELKLTI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 340 GVVQTAYANGASTDYLKH-LGLDVVFAKTGVKHLHEKAAEFDIGIYFEANGHGTILFSESFLSWLVSKQkdltakgQGGS 418
Cdd:cd03086 310 GVVQTAYANGASTKYLEDvLKVPVVCTPTGVKHLHHAAEEFDIGVYFEANGHGTVLFSESALAKIEENS-------SLSD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 419 EEHKAVSRLMAVSNLINQAVGDALSGVLLVEVILQHLGWSIEKWNELYKDLPSRQIKVEVPDRTAVVTTSEETEALRPMG 498
Cdd:cd03086 383 EQEKAAKTLLAFSRLINQTVGDAISDMLAVELILAALGWSPQDWDNLYTDLPNRQLKVKVPDRSVIKTTDAERRLVEPKG 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 19715620 499 IQDAINSEIKKYSRGRAFIRPSGTEDVVRVYAEASTQEDADSLANSVAQLV 549
Cdd:cd03086 463 LQDKIDAIVAKYNNGRAFVRPSGTEDVVRVYAEAATQEEADELANEVAELV 513
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
42-553 |
4.86e-34 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 134.17 E-value: 4.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 42 VYRVGILS------ALRSLKLGSatvGLMITASHNKVSDNGIKVSDPSGFMLSQEWEpfadqianasspeelvSLIRKFM 115
Cdd:COG1109 72 VYDLGLVPtpalafAVRHLGADG---GIMITASHNPPEYNGIKFFDADGGKLSPEEE----------------KEIEALI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 116 EKEEIAIGENNKgaevwlgrdtrpsgesllrageigvgsiLGSVAIDIGILttpqlhwmvraknkglkateNDYFENLST 195
Cdd:COG1109 133 EKEDFRRAEAEE----------------------------IGKVTRIEDVL--------------------EAYIEALKS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 196 SFRCLIDLipssgnDKLeisKLLVDGANGVGGQKIEKLRGSLsNLDVEIRNTGRDGgvLNEGVGADFVQK------EKVL 269
Cdd:COG1109 165 LVDEALRL------RGL---KVVVDCGNGAAGGVAPRLLREL-GAEVIVLNAEPDG--NFPNHNPNPEPEnledliEAVK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 270 PVGFgfkDVGMrcaSLDGDADRLVYFyipsdsSEKVELLDGDKILSLFALFIKEqlnaleddeerKQSRLGVVQTAYANG 349
Cdd:COG1109 233 ETGA---DLGI---AFDGDADRLGVV------DEKGRFLDGDQLLALLARYLLE-----------KGPGGTVVVTVMSSL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 350 ASTDYLKHLGLDVVFAKTGVKHLHEKAAEFDIGIYFEANGHgtILFSEsflswlvskqkdltakgqggseehkavsrlma 429
Cdd:COG1109 290 ALEDIAEKHGGEVVRTKVGFKYIKEKMRETGAVLGGEESGG--IIFPD-------------------------------- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 430 vsnliNQAVGDALSGVLLVEVILQHLGWSIEKWNELYKDLPSRQIKVEVPDRTAVVTTSEE-TEALRPMGIQDAINsEIK 508
Cdd:COG1109 336 -----FVPTDDGILAALLLLELLAKQGKSLSELLAELPRYPQPEINVRVPDEEKIGAVMEKlREAVEDKEELDTID-GVK 409
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 19715620 509 KY--SRGRAFIRPSGTEDVVRVYAEASTQEDADSLANSVAQLVKSFL 553
Cdd:COG1109 410 VDleDGGWVLVRPSGTEPLLRVYAEAKDEEEAEELLAELAELVEEAL 456
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
59-550 |
5.14e-24 |
|
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also designated in MrsA and YhbF E. coli, UreC in Helicobacter pylori, and femR315 or FemD in Staphlococcus aureus. It converts glucosamine-6-phosphate to glucosamine-1-phosphate as part of the pathway toward UDP-N-acetylglucosamine for peptidoglycan and lipopolysaccharides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]
Pssm-ID: 130522 Cd Length: 443 Bit Score: 104.76 E-value: 5.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 59 ATVGLMITASHNKVSDNGIKVSDPSGFMLSQEWEpfaDQIanasspeelvslirkfmekeEIAIGENNKGaevwlgrdTR 138
Cdd:TIGR01455 89 ADAGVMISASHNPYEDNGIKFFGPGGFKLDDATE---AAI--------------------EALLDEADPL--------PR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 139 PSGESLlrageigvgsilgsvaidigilttpqlhwmvrAKNKGLKATENDYFENLSTSFrclidliPSSGNdkLEISKLL 218
Cdd:TIGR01455 138 PESEGL--------------------------------GRVKRYPDAVGRYIEFLKSTL-------PRGLT--LSGLKVV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 219 VDGANGVGGQKIEKLRGSLsNLDVEIRNTGRDGGVLNEGVGADFVQ--KEKVLPVGfgfKDVGMrcaSLDGDADRLVYFy 296
Cdd:TIGR01455 177 LDCANGAAYKVAPHVFREL-GAEVIAIGVEPDGLNINDGCGSTHLDalQKAVREHG---ADLGI---AFDGDADRVLAV- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 297 ipsdsSEKVELLDGDKILSLFALFIKEQlNALEDDeerkqsrlGVVQTAYANGASTDYLKHLGLDVVFAKTGVKHLHEKA 376
Cdd:TIGR01455 249 -----DANGRIVDGDQILYIIARALKES-GELAGN--------TVVATVMSNLGLERALEKLGLTLIRTAVGDRYVLEEM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 377 AEFDIGIYFEANGHgtILFSesflswlvskqkdltakgqggseeHKAVSrlmavsnlinqavGDALSGVLLVEVILQHLG 456
Cdd:TIGR01455 315 RESGYNLGGEQSGH--IILL------------------------DYSTT-------------GDGIVSALQVLTIMKKSG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 457 WSIEkwnELYKDL---PSRQIKVEVPDRTAvvtTSEETEALRpMGIQDAinsEIKKYSRGRAFIRPSGTEDVVRVYAEAS 533
Cdd:TIGR01455 356 STLS---ELAAEFvpyPQTLVNVRVADRKL---AAAEAPAVK-AAIEDA---EAELGGTGRILLRPSGTEPLIRVMVEAA 425
|
490
....*....|....*..
gi 19715620 534 TQEDADSLANSVAQLVK 550
Cdd:TIGR01455 426 DEELVQQLADTLADVVS 442
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
474-550 |
5.24e-08 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 49.96 E-value: 5.24e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19715620 474 IKVEVPDRTAVvttsEETEALRPMGIQdainSEIKKYSRGRAF-IRPSGTEDVVRVYAEASTQEDADSLANSVAQLVK 550
Cdd:pfam00408 2 INVRVAEKKKL----AALAAILKVFAD----AEKILGEDGRRLdVRPSGTEPVLRVMVEGDSDEELARLADEIADLLE 71
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
1-556 |
0e+00 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 967.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 1 MDEIQIASILKSSELFPIPQGVKLSYGTAGFRGDAKLLESTVYRVGILSALRSLKLGsATVGLMITASHNKVSDNGIKVS 80
Cdd:PLN02895 1 MDEIQRASLLAASSRFPPPQGVRFSYGTAGFRTDASLLESTVFRVGILAALRSLKTG-AATGLMITASHNPVSDNGVKIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 81 DPSGFMLSQEWEPFADQIANASSPEELVSLIRKFMEKEEIAIGENNKGAEVWLGRDTRPSGESLLRAGEIGVGSIlGSVA 160
Cdd:PLN02895 80 DPSGGMLPQAWEPFADALANAPDPDALVQLIREFVKKENIPAVGGNPPAEVLLGRDTRPSGPALLAAALKGVRAI-GARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 161 IDIGILTTPQLHWMVRAKNKGLKATENDYFENLSTSFRCLIDLIPSSGNDKLEISKLLVDGANGVGGQKIEKLRGSLSNL 240
Cdd:PLN02895 159 VDMGILTTPQLHWMVRAANKGMKATESDYFEQLSSSFRALLDLIPNGSGDDRADDKLVVDGANGVGAEKLETLKKALGGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 241 DVEIRNTGRDG-GVLNEGVGADFVQKEKVLPVGFGFKDVGMRCASLDGDADRLVYFYIPSDSSeKVELLDGDKILSLFAL 319
Cdd:PLN02895 239 DLEVRNSGKEGeGVLNEGVGADFVQKEKVPPTGFASKDVGLRCASLDGDADRLVYFYVSSAGS-KIDLLDGDKIASLFAL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 320 FIKEQLNALEDDEERK----QSRLGVVQTAYANGASTDYLKH-LGLDVVFAKTGVKHLHEKAAEFDIGIYFEANGHGTIL 394
Cdd:PLN02895 318 FIKEQLRILNGNGNEKpeelLVRLGVVQTAYANGASTAYLKQvLGLEVVCTPTGVKYLHEAAAEFDIGVYFEANGHGTVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 395 FSESFLSWLVSKQKDLTAKGQGgSEEHKAVSRLMAVSNLINQAVGDALSGVLLVEVILQHLGWSIEKWNELYKDLPSRQI 474
Cdd:PLN02895 398 FSERFLDWLEAAAAELSSKAKG-SEAHKAARRLLAVSRLINQAVGDALSGLLLVEAILQYRGWSLAEWNALYQDLPSRQL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 475 KVEVPDRTAVVTTSEETEALRPMGIQDAINSEIKKYSRGRAFIRPSGTEDVVRVYAEASTQEDADSLANSVAQLVKSFLG 554
Cdd:PLN02895 477 KVKVADRTAITTTDAETVVVRPAGLQDAIDAEVAKYPRGRAFVRPSGTEDVVRVYAEASTQEAADSLAREVARLVYDLLG 556
|
..
gi 19715620 555 SS 556
Cdd:PLN02895 557 GV 558
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
25-549 |
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: 782.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 25 SYGTAGFRGDAKLLESTVYRVGILSALRSLKLGSATVGLMITASHNKVSDNGIKVSDPSGFMLSQEWEPFADQIANASSP 104
Cdd:cd03086 1 SYGTAGFRTKAELLDSVVFRVGILAALRSKKLGGKTIGVMITASHNPVEDNGVKIVDPDGEMLEESWEPYATQLANASDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 105 EELVSLIRKFMEKEEIAIgeNNKGAEVWLGRDTRPSGESLLRAGEIGVGSiLGSVAIDIGILTTPQLHWMVRAKNKGL-- 182
Cdd:cd03086 81 ELLVLVLMLISVKELNID--LSVPANVFVGRDTRPSGPALLQALLDGLKA-LGGNVIDYGLVTTPQLHYLVRAANTEGay 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 183 -KATENDYFENLSTSFRCLIDLIPSSGNdklEISKLLVDGANGVGGQKIEKLRGSLS-NLDVEIRNTGRDG-GVLNEGVG 259
Cdd:cd03086 158 gEPTEEGYYEKLSKAFNELYNLLQDGGD---EPEKLVVDCANGVGALKLKELLKRLKkGLSVKIINDGEEGpELLNDGCG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 260 ADFVQKEKVLPVGFGFKDVGMRCASLDGDADRLVYFYIpsDSSEKVELLDGDKILSLFALFIKEQLnalEDDEERKQSRL 339
Cdd:cd03086 235 ADYVKTKQKPPRGFELKPPGVRCCSFDGDADRLVYFYP--DSSNKFHLLDGDKIATLFAKFIKELL---KKAGEELKLTI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 340 GVVQTAYANGASTDYLKH-LGLDVVFAKTGVKHLHEKAAEFDIGIYFEANGHGTILFSESFLSWLVSKQkdltakgQGGS 418
Cdd:cd03086 310 GVVQTAYANGASTKYLEDvLKVPVVCTPTGVKHLHHAAEEFDIGVYFEANGHGTVLFSESALAKIEENS-------SLSD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 419 EEHKAVSRLMAVSNLINQAVGDALSGVLLVEVILQHLGWSIEKWNELYKDLPSRQIKVEVPDRTAVVTTSEETEALRPMG 498
Cdd:cd03086 383 EQEKAAKTLLAFSRLINQTVGDAISDMLAVELILAALGWSPQDWDNLYTDLPNRQLKVKVPDRSVIKTTDAERRLVEPKG 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 19715620 499 IQDAINSEIKKYSRGRAFIRPSGTEDVVRVYAEASTQEDADSLANSVAQLV 549
Cdd:cd03086 463 LQDKIDAIVAKYNNGRAFVRPSGTEDVVRVYAEAATQEEADELANEVAELV 513
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
6-555 |
0e+00 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 556.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 6 IASILKSSELFPIPQGVKLSYGTAGFRGDAKL--LESTVYRVGILSALRSL-------KLGSATVGLMITASHNKVSDNG 76
Cdd:PTZ00302 13 IELCGSKFPLRHSAIENPLTYGTAGFRTKAELppLEPVAYRVGILAALRSFlyggkraKRGNKSVGVMITASHNPIQDNG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 77 IKVSDPSGFMLSQEWEPFADQIANASSPEELVSLIRKFMEKEEIAIGENN--------KGAEVWLGRDTRPSGESLLRAG 148
Cdd:PTZ00302 93 VKIIDPDGGMLEESWEKICTDFANARTGEDLVSVLMDCLTEHGIKLSNLKldlnksncSKAKVHVGRDTRPSSPELVSAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 149 EIGVGSILGSVAIDIGILTTPQLHWMVRAKNKGLKA----TENDYFENLSTSF----RCLIDLIPSSGNDKLEiSKLLVD 220
Cdd:PTZ00302 173 LRGLKLLIGSNVRNFGIVTTPQLHFLVAFANGLGVDvvesSDELYYAYLLAAFkelyRTLQEGGPVDLTQNNS-KILVVD 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 221 GANGVGGQKIEKLRGSLSNL---DVEIRNTGRDGGVLNEGVGADFVQKEKVLPVGFGF--KDVGMRCASLDGDADRLVYF 295
Cdd:PTZ00302 252 CANGVGGYKIKRFFEALKQLgieIIPININCDEEELLNDKCGADYVQKTRKPPRAMKEwpGDEETRVASFDGDADRLVYF 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 296 YIPSDSSEKVELLDGDKILSLFALFIKEQLnaledDEERKQSRL--GVVQTAYANGASTDYLKHL--GLDVVFAKTGVKH 371
Cdd:PTZ00302 332 FPDKDGDDKWVLLDGDRIAILYAMLIKKLL-----GKIQLKKKLdiGVVQTAYANGASTNYLNELlgRLRVYCAPTGVKN 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 372 LHEKAAEFDIGIYFEANGHGTILFSESFLSWLVSKQKDLTAKgqggseeHKAVSRLMAVSNLINQAVGDALSGVLLVEVI 451
Cdd:PTZ00302 407 LHPKAHKYDIGIYFEANGHGTVLFNEKALAEWAKFLAKQNAL-------NSACRQLEKFLRLFNQTIGDAISDLLAVELA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 452 LQHLGWSIEKWNELYKDLPSRQIKVEVPDRTAVVTTSEETEALRPMGIQDAINSEIKKYSR-GRAFIRPSGTEDVVRVYA 530
Cdd:PTZ00302 480 LAFLGLSFQDWLNLYTDLPSRQDKVTVKDRTLITNTEDETRLLEPKGLQDKIDAIVSKYDNaARAFIRPSGTEPVVRVYA 559
|
570 580
....*....|....*....|....*
gi 19715620 531 EASTQEDADSLANSVAQLVKSFLGS 555
Cdd:PTZ00302 560 EAPTLEQADELANEVKGLVLRYCSG 584
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
26-549 |
5.71e-41 |
|
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: 151.35 E-value: 5.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 26 YGTAGFRG--DAKLLESTVYRVGIlSALRslklgsaTVGLMITASHNKVSDNGIKVSDPSGFMLSQEWEPFADQIANASs 103
Cdd:cd03084 2 FGTSGVRGvvGDDITPETAVALGQ-AIGS-------TGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKE- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 104 peelvslirkfmekeeiaigennkgaevwlgrdtrpsgeslLRAGEIGVGSILGSVAIDIgilttpqlhwmvraknkglk 183
Cdd:cd03084 73 -----------------------------------------DEPSAVAYELGGSVKAVDI-------------------- 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 184 atENDYFEnlstSFRCLIDLIPSSGNDKleisKLLVDGANGVGGQKIEKLrgsLSNLDVEIRNTGRD------GGVLNEG 257
Cdd:cd03084 92 --LQRYFE----ALKKLFDVAALSNKKF----KVVVDSVNGVGGPIAPQL---LEKLGAEVIPLNCEpdgnfgNINPDPG 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 258 VGADFVQ-KEKVLPVGFGFKdvgmrcASLDGDADRLVYFYipsdssEKVELLDGDKILSLFALFIKEQLNaleddeerkq 336
Cdd:cd03084 159 SETNLKQlLAVVKAEKADFG------VAFDGDADRLIVVD------ENGGFLDGDELLALLAVELFLTFN---------- 216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 337 SRLGVVQTAYANGASTDYLKHLGLDVVFAKTGVKHLHEKAAEFDIGIYFEANGHGTILFsesflswlvskqkdltakgqg 416
Cdd:cd03084 217 PRGGVVKTVVSSGALDKVAKKLGIKVIRTKTGFKWVGEAMQEGDVVLGGEESGGVIFPE--------------------- 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 417 gseehkavsrlmavsnliNQAVGDALSGVLLVEVILQHLGWSIEKWNELYKDLPSRQIKVevpdrtavvttseetealrp 496
Cdd:cd03084 276 ------------------FHPGRDGISAALLLLEILANLGKSLSELFSELPRYYYIRLKV-------------------- 317
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 19715620 497 mgiqdainseikkysRGRAFIRPSGTEDVVRVYAEASTQEDADSLANSVAQLV 549
Cdd:cd03084 318 ---------------RGWVLVRASGTEPAIRIYAEADTQEDVEQIKKEARELV 355
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
42-553 |
4.86e-34 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 134.17 E-value: 4.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 42 VYRVGILS------ALRSLKLGSatvGLMITASHNKVSDNGIKVSDPSGFMLSQEWEpfadqianasspeelvSLIRKFM 115
Cdd:COG1109 72 VYDLGLVPtpalafAVRHLGADG---GIMITASHNPPEYNGIKFFDADGGKLSPEEE----------------KEIEALI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 116 EKEEIAIGENNKgaevwlgrdtrpsgesllrageigvgsiLGSVAIDIGILttpqlhwmvraknkglkateNDYFENLST 195
Cdd:COG1109 133 EKEDFRRAEAEE----------------------------IGKVTRIEDVL--------------------EAYIEALKS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 196 SFRCLIDLipssgnDKLeisKLLVDGANGVGGQKIEKLRGSLsNLDVEIRNTGRDGgvLNEGVGADFVQK------EKVL 269
Cdd:COG1109 165 LVDEALRL------RGL---KVVVDCGNGAAGGVAPRLLREL-GAEVIVLNAEPDG--NFPNHNPNPEPEnledliEAVK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 270 PVGFgfkDVGMrcaSLDGDADRLVYFyipsdsSEKVELLDGDKILSLFALFIKEqlnaleddeerKQSRLGVVQTAYANG 349
Cdd:COG1109 233 ETGA---DLGI---AFDGDADRLGVV------DEKGRFLDGDQLLALLARYLLE-----------KGPGGTVVVTVMSSL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 350 ASTDYLKHLGLDVVFAKTGVKHLHEKAAEFDIGIYFEANGHgtILFSEsflswlvskqkdltakgqggseehkavsrlma 429
Cdd:COG1109 290 ALEDIAEKHGGEVVRTKVGFKYIKEKMRETGAVLGGEESGG--IIFPD-------------------------------- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 430 vsnliNQAVGDALSGVLLVEVILQHLGWSIEKWNELYKDLPSRQIKVEVPDRTAVVTTSEE-TEALRPMGIQDAINsEIK 508
Cdd:COG1109 336 -----FVPTDDGILAALLLLELLAKQGKSLSELLAELPRYPQPEINVRVPDEEKIGAVMEKlREAVEDKEELDTID-GVK 409
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 19715620 509 KY--SRGRAFIRPSGTEDVVRVYAEASTQEDADSLANSVAQLVKSFL 553
Cdd:COG1109 410 VDleDGGWVLVRPSGTEPLLRVYAEAKDEEEAEELLAELAELVEEAL 456
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
42-546 |
2.46e-32 |
|
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: 129.14 E-value: 2.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 42 VYRVGIL-----SAL-RSLKlgsATVGLMITASHNKVSDNGIKVSDPSGFMLSQEWEpfadqianasspeelvslirkfm 115
Cdd:cd05802 68 VLLLGVIptpavAYLtRKLR---ADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVE----------------------- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 116 ekEEIaigennkgaevwlgrdtrpsgESLLRAGEIGVgsilgSVAIDIGilttpqlhwmvRAKNkgLKATENDYFENLST 195
Cdd:cd05802 122 --EEI---------------------EALIDKELELP-----PTGEKIG-----------RVYR--IDDARGRYIEFLKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 196 SFrclidliPSSGNDKLeisKLLVDGANG----VGGQKIEKLRgslsnLDVEIRNTGRDGGVLNEGVGADFVQ--KEKVL 269
Cdd:cd05802 161 TF-------PKDLLSGL---KIVLDCANGaaykVAPEVFRELG-----AEVIVINNAPDGLNINVNCGSTHPEslQKAVL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 270 PVGFgfkDVGMrcaSLDGDADRLvyfyIPSDssEKVELLDGDKILSLFALFIKEQlNALEDDeerkqsrlGVVQTAYANG 349
Cdd:cd05802 226 ENGA---DLGI---AFDGDADRV----IAVD--EKGNIVDGDQILAICARDLKER-GRLKGN--------TVVGTVMSNL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 350 ASTDYLKHLGLDVVFAKTGVKHLHEKAAEFDIGIYFEANGHgtILFSEsflswlvskqKDLTakgqggseehkavsrlma 429
Cdd:cd05802 285 GLEKALKELGIKLVRTKVGDRYVLEEMLKHGANLGGEQSGH--IIFLD----------HSTT------------------ 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 430 vsnlinqavGDA-LSGVLLVEVILQHlGWSIEKWNELYKDLPSRQIKVEVPDRTAVVTTSEetealrpmgIQDAINSEIK 508
Cdd:cd05802 335 ---------GDGlLTALQLLAIMKRS-GKSLSELASDMKLYPQVLVNVRVKDKKALLENPR---------VQAAIAEAEK 395
|
490 500 510
....*....|....*....|....*....|....*....
gi 19715620 509 KYS-RGRAFIRPSGTEDVVRVYAEASTQEDADSLANSVA 546
Cdd:cd05802 396 ELGgEGRVLVRPSGTEPLIRVMVEGEDEELVEKLAEELA 434
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
59-550 |
5.14e-24 |
|
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also designated in MrsA and YhbF E. coli, UreC in Helicobacter pylori, and femR315 or FemD in Staphlococcus aureus. It converts glucosamine-6-phosphate to glucosamine-1-phosphate as part of the pathway toward UDP-N-acetylglucosamine for peptidoglycan and lipopolysaccharides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]
Pssm-ID: 130522 Cd Length: 443 Bit Score: 104.76 E-value: 5.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 59 ATVGLMITASHNKVSDNGIKVSDPSGFMLSQEWEpfaDQIanasspeelvslirkfmekeEIAIGENNKGaevwlgrdTR 138
Cdd:TIGR01455 89 ADAGVMISASHNPYEDNGIKFFGPGGFKLDDATE---AAI--------------------EALLDEADPL--------PR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 139 PSGESLlrageigvgsilgsvaidigilttpqlhwmvrAKNKGLKATENDYFENLSTSFrclidliPSSGNdkLEISKLL 218
Cdd:TIGR01455 138 PESEGL--------------------------------GRVKRYPDAVGRYIEFLKSTL-------PRGLT--LSGLKVV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 219 VDGANGVGGQKIEKLRGSLsNLDVEIRNTGRDGGVLNEGVGADFVQ--KEKVLPVGfgfKDVGMrcaSLDGDADRLVYFy 296
Cdd:TIGR01455 177 LDCANGAAYKVAPHVFREL-GAEVIAIGVEPDGLNINDGCGSTHLDalQKAVREHG---ADLGI---AFDGDADRVLAV- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 297 ipsdsSEKVELLDGDKILSLFALFIKEQlNALEDDeerkqsrlGVVQTAYANGASTDYLKHLGLDVVFAKTGVKHLHEKA 376
Cdd:TIGR01455 249 -----DANGRIVDGDQILYIIARALKES-GELAGN--------TVVATVMSNLGLERALEKLGLTLIRTAVGDRYVLEEM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 377 AEFDIGIYFEANGHgtILFSesflswlvskqkdltakgqggseeHKAVSrlmavsnlinqavGDALSGVLLVEVILQHLG 456
Cdd:TIGR01455 315 RESGYNLGGEQSGH--IILL------------------------DYSTT-------------GDGIVSALQVLTIMKKSG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 457 WSIEkwnELYKDL---PSRQIKVEVPDRTAvvtTSEETEALRpMGIQDAinsEIKKYSRGRAFIRPSGTEDVVRVYAEAS 533
Cdd:TIGR01455 356 STLS---ELAAEFvpyPQTLVNVRVADRKL---AAAEAPAVK-AAIEDA---EAELGGTGRILLRPSGTEPLIRVMVEAA 425
|
490
....*....|....*..
gi 19715620 534 TQEDADSLANSVAQLVK 550
Cdd:TIGR01455 426 DEELVQQLADTLADVVS 442
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
42-549 |
5.73e-18 |
|
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: 86.41 E-value: 5.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 42 VYRVGILS--AL-RSLKLGSATVGLMITASHNKVSDNGIKVSDPSGFMLSQEWEpfadqianasspEELvslirkfmekE 118
Cdd:TIGR03990 66 VVDLGIAPtpTLqYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQE------------EEI----------E 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 119 EIAIGENNKGAEvW--LGRDTRPSgesllRAGEIGVGSILGSVAIDigilttpqlhwmvRAKNKGLKAtendyfenlsts 196
Cdd:TIGR03990 124 EIAESGDFERAD-WdeIGTVTSDE-----DAIDDYIEAILDKVDVE-------------AIRKKGFKV------------ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 197 frclidlipssgndkleisklLVDGANGVGGQKIEKLrgsLSNLDVEIR--NTGRDG--------------GVLNEGV-- 258
Cdd:TIGR03990 173 ---------------------VVDCGNGAGSLTTPYL---LRELGCKVItlNCQPDGtfpgrnpeptpenlKDLSALVka 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 259 -GADFvqkekvlpvGFGFkdvgmrcaslDGDADRLVYFyipsdsSEKVELLDGDKILSLFALFIkeqlnaledDEERKQS 337
Cdd:TIGR03990 229 tGADL---------GIAH----------DGDADRLVFI------DEKGRFIGGDYTLALFAKYL---------LEHGGGK 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 338 rlgVVQTAYANGASTDYLKHLGLDVVFAKTGVKHLHEKAAEFDIGIYFEANGHgtILFSEsflswlvskqkdltakgqgg 417
Cdd:TIGR03990 275 ---VVTNVSSSRAVEDVAERHGGEVIRTKVGEVNVAEKMKEEGAVFGGEGNGG--WIFPD-------------------- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 418 seehkavsrlmavsnliNQAVGDALSGVLLvevILQHLGWSIEKWNELYKDLPSRQI---KVEVPD--RTAVVTTSEETE 492
Cdd:TIGR03990 330 -----------------HHYCRDGLMAAAL---FLELLAEEGKPLSELLAELPKYPMskeKVELPDedKEEVMEAVEEEF 389
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 19715620 493 ALRPMGIQDAINSEikkYSRGRAFIRPSGTEDVVRVYAEASTQEDADSLANSVAQLV 549
Cdd:TIGR03990 390 ADAEIDTIDGVRID---FEDGWVLVRPSGTEPIVRIYAEAKTEERAEELLEEGRSLV 443
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
121-549 |
8.67e-17 |
|
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: 82.62 E-value: 8.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 121 AIGENNKGAEVWLGRDTRPSGESLLRAGEIGVGSIlGSVAIDIGILTTPQLHWMVRAKNK---------------GLK-- 183
Cdd:cd03087 26 ALGTYLGGGTVVVGRDTRTSGPMLKNAVIAGLLSA-GCDVIDIGIVPTPALQYAVRKLGDagvmitashnppeynGIKlv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 184 -------------ATENDYFENlstSFRC----------------------LIDLIPSSGNDKLeisKLLVDGANGVGGQ 228
Cdd:cd03087 105 npdgtefsreqeeEIEEIIFSE---RFRRvawdevgsvrredsaideyieaILDKVDIDGGKGL---KVVVDCGNGAGSL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 229 KIEKLRGSLsNLDVEIRNTGRDG--------------GVLNEGV---GADFvqkekvlpvGFGFkdvgmrcaslDGDADR 291
Cdd:cd03087 179 TTPYLLREL-GCKVITLNANPDGffpgrppeptpenlSELMELVratGADL---------GIAH----------DGDADR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 292 LVYFyipsdsSEKVELLDGDKILSLFALFIkeqlnaledDEERKQSrlgVVQTAYANGASTDYLKHLGLDVVFAKTGVKH 371
Cdd:cd03087 239 AVFV------DEKGRFIDGDKLLALLAKYL---------LEEGGGK---VVTPVDASMLVEDVVEEAGGEVIRTPVGDVH 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 372 LHEKAAEFDIGIYFEANGhgTILFSEsflswlvskqkdltakgqggseehkavsrlmavsnlINQAVGDALSGVLLVEVI 451
Cdd:cd03087 301 VAEEMIENGAVFGGEPNG--GWIFPD------------------------------------HQLCRDGIMTAALLLELL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 452 lqhlgwsIEKWN--ELYKDLPSRQIKvevpdRTAVVTTSEETEALRpmgiqDAINSEIKKYSR--------------GRA 515
Cdd:cd03087 343 -------AEEKPlsELLDELPKYPLL-----REKVECPDEKKEEVM-----EAVEEELSDADEdvdtidgvrieyedGWV 405
|
490 500 510
....*....|....*....|....*....|....
gi 19715620 516 FIRPSGTEDVVRVYAEASTQEDADSLANSVAQLV 549
Cdd:cd03087 406 LIRPSGTEPKIRITAEAKTEERAKELLEEGRSKV 439
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
62-549 |
2.33e-11 |
|
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: 66.04 E-value: 2.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 62 GLMITASHNKVSDNGIKVSDPSGfmlsqewepfadqianASSPEELVSLIRKFMEKEEiaigennkgaevwlgrdtrPSG 141
Cdd:cd05800 94 GVMITASHNPPEYNGVKVKPAFG----------------GSALPEITAAIEARLASGE-------------------PPG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 142 ESLLRAGEIgvgsilgsVAIDIgilttpqlhwmvraknkglkatENDYFENLSTsfrcLIDL--IPSSGNdkleisKLLV 219
Cdd:cd05800 139 LEARAEGLI--------ETIDP----------------------KPDYLEALRS----LVDLeaIREAGL------KVVV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 220 DGANGVGGQKIEK-LRGSlsNLDVEIRNTGRD---GGVLNEGVG------ADFVQKEKvlpvgfgfKDVGMrcaSLDGDA 289
Cdd:cd05800 179 DPMYGAGAGYLEElLRGA--GVDVEEIRAERDplfGGIPPEPIEknlgelAEAVKEGG--------ADLGL---ATDGDA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 290 DRL--VyfyipsdsSEKVELLDGDKILSLFALFIKEqlnaleddeeRKQSRLGVVQTAyangaSTDYL-----KHLGLDV 362
Cdd:cd05800 246 DRIgaV--------DEKGNFLDPNQILALLLDYLLE----------NKGLRGPVVKTV-----STTHLidriaEKHGLPV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 363 VFAKTGVKHLHEKAAEFDIGIyfeanghgtilfsesflswlvskqkdltakgqgGSEEHKAVSRLMAVSNlinqavGDA- 441
Cdd:cd05800 303 YETPVGFKYIAEKMLEEDVLI---------------------------------GGEESGGLGIRGHIPE------RDGi 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 442 LSGVLLVEVILQH---LGwsiekwnELYKDLPSRqIKVEVPDRTAVVTTSEETEALRPMGIQDA----INSEIKKYSR-- 512
Cdd:cd05800 344 LAGLLLLEAVAKTgkpLS-------ELVAELEEE-YGPSYYDRIDLRLTPAQKEAILEKLKNEPplsiAGGKVDEVNTid 415
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 19715620 513 GRAF---------IRPSGTEDVVRVYAEASTQEDADSLANSVAQLV 549
Cdd:cd05800 416 GVKLvledgswllIRPSGTEPLLRIYAEAPSPEKVEALLDAGKKLA 461
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
250-551 |
7.56e-11 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 64.39 E-value: 7.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 250 DGGVLNEGVGADFVQ--KEKVLPVGfgfKDVGMrcaSLDGDADRLVYFyipsdsSEKVELLDGDKILSLFAlfikeqlna 327
Cdd:PRK10887 206 NGLNINDECGATDPEalQAAVLAEK---ADLGI---AFDGDGDRVIMV------DHLGNLVDGDQLLYIIA--------- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 328 lEDDEERKQSRLGVVQTAYANGASTDYLKHLGLDVVFAKTGVKHLHEKAAEFDIGIYFEANGHgtilfsesflswLVSKQ 407
Cdd:PRK10887 265 -RDRLRRGQLRGGVVGTLMSNMGLELALKQLGIPFVRAKVGDRYVLEKLQEKGWRLGGENSGH------------ILCLD 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 408 KDLTakgqggseehkavsrlmavsnlinqavGDALSGVLLVEVILQHLGWSIEKWNELYKDLPsrQIKVEVP-------- 479
Cdd:PRK10887 332 KTTT---------------------------GDGIVAALQVLAAMVRSGMSLADLCSGMKLFP--QVLINVRfkpgaddp 382
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19715620 480 -DRTAVVTTSEETEALrpMGiqdainseikkySRGRAFIRPSGTEDVVRVYAEASTQEDADSLANSVAQLVKS 551
Cdd:PRK10887 383 lESEAVKAALAEVEAE--LG------------GRGRVLLRKSGTEPLIRVMVEGEDEAQVTALAERIADAVKA 441
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
474-550 |
5.24e-08 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 49.96 E-value: 5.24e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19715620 474 IKVEVPDRTAVvttsEETEALRPMGIQdainSEIKKYSRGRAF-IRPSGTEDVVRVYAEASTQEDADSLANSVAQLVK 550
Cdd:pfam00408 2 INVRVAEKKKL----AALAAILKVFAD----AEKILGEDGRRLdVRPSGTEPVLRVMVEGDSDEELARLADEIADLLE 71
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
41-101 |
1.88e-07 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 50.30 E-value: 1.88e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19715620 41 TVYRVGILS------ALRSLKlgsATVGLMITASHNKVSDNGIKVSDPSGFMLSqewEPFADQIANA 101
Cdd:pfam02878 70 EVILLGLLPtpavsfATRKLK---ADGGIMITASHNPPEYNGIKVFDSNGGPIP---PEVEKKIEAI 130
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
103-546 |
2.53e-07 |
|
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: 53.08 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 103 SPEELVSLIRKFMEkeeiAIGENNKGAEVWLGRDTRPSGeSLLRAGEIGVGSILGSVAIDIGILTTPQLHWMVR------ 176
Cdd:cd05803 16 TPEVITRYVAAFAT----WQPERTKGGKIVVGRDGRPSG-PMLEKIVIGALLACGCDVIDLGIAPTPTVQVLVRqsqasg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 177 ----------AKNKGLK--------------------ATENDYF----------ENLSTSFRCLIDLI---PSSGNDKLE 213
Cdd:cd05803 91 giiitashnpPQWNGLKfigpdgefltpdegeevlscAEAGSAQkagydqlgevTFSEDAIAEHIDKVlalVDVDVIKIR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 214 IS--KLLVDGANGVGGQKIEKLRGSLsNLDVEIRNTGRDGGVLN--EGVGADFVQ-----KEKVLPVGFGfkdvgmrcas 284
Cdd:cd05803 171 ERnfKVAVDSVNGAGGLLIPRLLEKL-GCEVIVLNCEPTGLFPHtpEPLPENLTQlcaavKESGADVGFA---------- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 285 LDGDADRLVyfyipsdssekveLLDGDKI-------LSLFALFikeqlnALEDdeerkQSRLGVVQTayaNGASTdylkh 357
Cdd:cd05803 240 VDPDADRLA-------------LVDEDGRpigeeytLALAVDY------VLKY-----GGRKGPVVV---NLSTS----- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 358 LGLDVVFAKTGVKHLHEKaaefdIGiyfEANghgtilfsesflswLVSKQKDLTA----KGQGGseehkavsrlmavsnL 433
Cdd:cd05803 288 RALEDIARKHGVPVFRSA-----VG---EAN--------------VVEKMKEVDAviggEGNGG---------------V 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 434 INQAVG---DALSGVLLVeviLQHLGWSIEKWNELYKDLPSRQI---KVEVP--DRTAVVTTSEE----TEALRPMGIQd 501
Cdd:cd05803 331 ILPDVHygrDSLVGIALV---LQLLAASGKPLSEIVDELPQYYIsktKVTIAgeALERLLKKLEAyfkdAEASTLDGLR- 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 19715620 502 aINSEikkysRGRAFIRPSGTEDVVRVYAEASTQEDADSLANSVA 546
Cdd:cd05803 407 -LDSE-----DSWVHVRPSNTEPIVRIIAEAPTQDEAEALADRFI 445
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
121-179 |
5.61e-06 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 46.06 E-value: 5.61e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19715620 121 AIGENNKGAEVWLGRDTRPSGESLLRAgeigVGSILGSV---AIDIGILTTPQLHWMVRAKN 179
Cdd:pfam02878 33 YLRAQGGGGKVVVGRDTRYSSRELARA----LAAGLASNgveVILLGLLPTPAVSFATRKLK 90
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
309-394 |
1.58e-05 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 44.36 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19715620 309 DGDKILSLFALFIKEQlnaleddeERKQSRLGVVQTAYANGASTDYLKHLGLDVVFAKTGVKHLHEKAAEFDIGIYFEAN 388
Cdd:pfam02880 1 DGDQILALLAKYLLEQ--------GKLPPGAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEES 72
|
....*.
gi 19715620 389 GHGTIL 394
Cdd:pfam02880 73 GHIIFL 78
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
47-101 |
4.27e-04 |
|
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: 42.88 E-value: 4.27e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 19715620 47 ILS-ALRSLKlgsATVGLMITASHNKVSDNGIKVSDPSGF-MLSqewePFADQIANA 101
Cdd:cd05799 87 LLSfAVRHLG---ADAGIMITASHNPKEYNGYKVYWEDGAqIIP----PHDAEIAEE 136
|
|
| |
