|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
15-612 |
0e+00 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 797.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 15 LDQETAQWLRWDKNSLTLEAVKRLIAEGNKEELRKCFGARMEFGTAGLRAAMGPGISRMNDLTIIQTTQGFCRYLEKQFS 94
Cdd:PTZ00150 5 LEAQVELWLKWDKDPETRKEIEELLASKDEEELKRRFLKRMEFGTAGLRGKMGAGFNCMNDLTVQQTAQGLCAYVIETFG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 95 -DLKQKGIVISFDARAHpssggsSRRFARLAATTFISQGIPVYLFSDITPTPFVPFTVSHLKLCAGIMITASHNPKQDNG 173
Cdd:PTZ00150 85 qALKSRGVVIGYDGRYH------SRRFAEITASVFLSKGFKVYLFGQTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 174 YKVYWDNGAQIISPHDKGISQAIEENLEPWPQAWDDSlidSSPLLHNPSASINNDYFEDLKKYCFHRSVNReTKVKFVHT 253
Cdd:PTZ00150 159 YKVYWSNGAQIIPPHDKNISAKILSNLEPWSSSWEYL---TETLVEDPLAEVSDAYFATLKSEYNPACCDR-SKVKIVYT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 254 SVHGVGHSFVQSAFKAFDLVPPEAVPEQKDPDPEFPTVKYPNPEEGKGVLTLSFALADKTKARIVLANDPDADRLAVAEK 333
Cdd:PTZ00150 235 AMHGVGTRFVQKALHTVGLPNLLSVAQQAEPDPEFPTVTFPNPEEGKGALKLSMETAEAHGSTVVLANDPDADRLAVAEK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 334 QDSGeWRVFSGNELGALLGWWLFTSWKEKNQDRSalkDTYMLSSTVSSKILRAIALKEGFHFEETLTGFKWMGNRAKQLI 413
Cdd:PTZ00150 315 LNNG-WKIFTGNELGALLAWWAMKRYRRQGIDKS---KCFFICTVVSSRMLKKMAEKEGFQYDETLTGFKWIGNKAIELN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 414 D-QGKTVLFAFEEAIGYMCCPFVLDKDGVSAAVISAELASFLATKNLSLSQQLKAIYVEYGYHITKASYFICHDQETIKK 492
Cdd:PTZ00150 391 AeNGLTTLFAYEEAIGFMLGTRVRDKDGVTAAAVVAEMALYLYERGKTLVEHLESLYKQYGYHFTNNSYYICYDPSRIVS 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 493 LFENLRNyDGKnnYPKACGKFEISAIRDLTTGYDDSQPDKKAVLPTSKSSQMITFTFANGGVATMRTSGTEPKIKYYAEL 572
Cdd:PTZ00150 471 IFNDIRN-NGS--YPTKLGGYPVTRIRDLTTGYDTATPDGKPLLPVSASTQMITFYFENGAIITIRGSGTEPKLKWYAEL 547
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 116242708 573 CAppgnSDPEQLKKELNELVSAIEEHFFQPQKYNLQPKAD 612
Cdd:PTZ00150 548 SG----TKDEAVEKELAALVDEVVEQLMQPEKYGLVPRKE 583
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
54-592 |
0e+00 |
|
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: 743.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 54 RMEFGTAGLRAAMGPGISRMNDLTIIQTTQGFCRYLEKQFSDLKQKGIVISFDARAHpssggsSRRFARLAATTFISQGI 133
Cdd:cd05799 1 RLEFGTAGLRGKMGAGTNRMNDYTVRQATQGLANYLKKKGPDAKNRGVVIGYDSRHN------SREFAELTAAVLAANGI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 134 PVYLFSDITPTPFVPFTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDKGISQAIEENLEPWPQAWDDSLid 213
Cdd:cd05799 75 KVYLFDDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAVLEPLDIKFEEAL-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 214 SSPLLHNPSASINNDYFEDLKKYCFHRSVNRETKVKFVHTSVHGVGHSFVQSAFKAFDLVPPEAVPEQKDPDPEFPTVKY 293
Cdd:cd05799 153 DSGLIKYIGEEIDDAYLEAVKKLLVNPELNEGKDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVVEEQAEPDPDFPTVKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 294 PNPEEgKGVLTLSFALADKTKARIVLANDPDADRLAVAEKQDSGEWRVFSGNELGALLGWWLFTSWKEKNQDrsaLKDTY 373
Cdd:cd05799 233 PNPEE-PGALDLAIELAKKVGADLILATDPDADRLGVAVKDKDGEWRLLTGNEIGALLADYLLEQRKEKGKL---PKNPV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 374 MLSSTVSSKILRAIALKEGFHFEETLTGFKWMGNRAKQLIDQGKTVLFAFEEAIGYMCCPFVLDKDGVSAAVISAELASF 453
Cdd:cd05799 309 IVKTIVSSELLRKIAKKYGVKVEETLTGFKWIGNKIEELESGGKKFLFGFEESIGYLVGPFVRDKDGISAAALLAEMAAY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 454 LATKNLSLSQQLKAIYVEYGYHITKASYFIC---HDQETIKKLFENLRNYDgknnypkacgkfeisairdlttgyddsqp 530
Cdd:cd05799 389 LKAQGKTLLDRLDELYEKYGYYKEKTISITFegkEGPEKIKAIMDRLRNNP----------------------------- 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116242708 531 dkkavlptskssQMITFTFANGGVATMRTSGTEPKIKYYAELCAPpgnSDPEQLKKELNELV 592
Cdd:cd05799 440 ------------NVLTFYLEDGSRVTVRPSGTEPKIKFYIEVVGK---KTLEEAEKKLDALK 486
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
57-599 |
1.49e-92 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 292.49 E-value: 1.49e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 57 FGTAGLRAAMGPGisrMNDLTIIQTTQGFCRYLEKQfsdlKQKGIVISFDARAhpssggSSRRFARLAATTFISQGIPVY 136
Cdd:COG1109 7 FGTDGIRGIVGEE---LTPEFVLKLGRAFGTYLKEK----GGPKVVVGRDTRL------SSPMLARALAAGLASAGIDVY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 137 LFsDITPTPFVPFTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDKGISQAIEENLEPWPQAWDDSLIdssp 216
Cdd:COG1109 74 DL-GLVPTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKEDFRRAEAEEIGKV---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 217 llhNPSASINNDYFEDLKKYCFHRSvnRETKVKFVHTSVHGVGHSFVQSAFKA--FDLVPpeaVPEQkdPDPEFPTVkYP 294
Cdd:COG1109 149 ---TRIEDVLEAYIEALKSLVDEAL--RLRGLKVVVDCGNGAAGGVAPRLLRElgAEVIV---LNAE--PDGNFPNH-NP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 295 NPEEgkGVLTLSFALADKTKARIVLANDPDADRLAVAEKQdsGewRVFSGNELGALLGWWLftswKEKNqdrsalKDTYM 374
Cdd:COG1109 218 NPEP--ENLEDLIEAVKETGADLGIAFDGDADRLGVVDEK--G--RFLDGDQLLALLARYL----LEKG------PGGTV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 375 LSSTVSSKILRAIALKEGFHFEETLTGFKWMGNRAKQLidqgkTVLFAFEEAIGYMCCPFVLDKDGVSAAVISAELasfL 454
Cdd:COG1109 282 VVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKMRET-----GAVLGGEESGGIIFPDFVPTDDGILAALLLLEL---L 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 455 ATKNLSLSQQLKaiyvEYGYHITKASYFICHDQETIKKLFENLRNydgknnypkacgkfEISAIRDLTTgyddsqpdkka 534
Cdd:COG1109 354 AKQGKSLSELLA----ELPRYPQPEINVRVPDEEKIGAVMEKLRE--------------AVEDKEELDT----------- 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116242708 535 vlptsksSQMITFTFANGGVATMRTSGTEPKIKYYAElcAPpgnsDPEQLKKELNELVSAIEEHF 599
Cdd:COG1109 405 -------IDGVKVDLEDGGWVLVRPSGTEPLLRVYAE--AK----DEEEAEELLAELAELVEEAL 456
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
54-203 |
6.72e-41 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 145.06 E-value: 6.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 54 RMEFGTAGLRAAMGPGIsrMNDLTIIQTTQGFCRYLEKQfsdLKQKGIVISFDARAhpssggSSRRFARLAATTFISQGI 133
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGE--LTPEFALKLGQAIASYLRAQ---GGGGKVVVGRDTRY------SSRELARALAAGLASNGV 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 134 PVYLFsDITPTPFVPFTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDKGISQAIEENLEPW 203
Cdd:pfam02878 70 EVILL-GLLPTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKEDFYR 138
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
57-595 |
7.69e-27 |
|
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: 113.76 E-value: 7.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 57 FGTAGLRAAMGPGisrMNDLTIIQTTQGFCRYLEKqfsdlkqKGIVISFDARAhpssggSSRRFARLAATTFISQGIPVY 136
Cdd:TIGR03990 4 FGTSGIRGIVGEE---LTPELALKVGKAFGTYLRG-------GKVVVGRDTRT------SGPMLENAVIAGLLSTGCDVV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 137 LFsDITPTPFVPFTVSHLKLCAGIMITASHNPKQDNGYKVyWDNGAQIISPHD-KGISQAIEENLEPWPqAWDDSLIDSS 215
Cdd:TIGR03990 68 DL-GIAPTPTLQYAVRELGADGGIMITASHNPPEYNGIKL-LNSDGTELSREQeEEIEEIAESGDFERA-DWDEIGTVTS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 216 PllhnpsASINNDYFEDLKKycfhrSVNRET----KVKFVHTSVHGVGHSFVQSAFKAFDLvppEAVPEQKDPDPEFPtv 291
Cdd:TIGR03990 145 D------EDAIDDYIEAILD-----KVDVEAirkkGFKVVVDCGNGAGSLTTPYLLRELGC---KVITLNCQPDGTFP-- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 292 kYPNPEEGKGVLTLSFALADKTKARIVLANDPDADRLA-VAEKqdsGewRVFSGNELGALLGWWLFTSWKEKnqdrsalk 370
Cdd:TIGR03990 209 -GRNPEPTPENLKDLSALVKATGADLGIAHDGDADRLVfIDEK---G--RFIGGDYTLALFAKYLLEHGGGK-------- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 371 dtymLSSTVS-SKILRAIALKEGFHFEETLTGfkwMGNRAKQLIDQGktVLFAFEEAIGYMCCPFVLDKDGVSAAvisAE 449
Cdd:TIGR03990 275 ----VVTNVSsSRAVEDVAERHGGEVIRTKVG---EVNVAEKMKEEG--AVFGGEGNGGWIFPDHHYCRDGLMAA---AL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 450 LASFLATKNLSLSQQLKAIyveYGYHITKASyfICHDQETIKKLFENLrnydgKNNYPKAcgkfEISAIRDLTTGYDDSQ 529
Cdd:TIGR03990 343 FLELLAEEGKPLSELLAEL---PKYPMSKEK--VELPDEDKEEVMEAV-----EEEFADA----EIDTIDGVRIDFEDGW 408
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116242708 530 pdkkaVLptskssqmitftfanggvatMRTSGTEPKIKYYAElcAPpgnsDPEQLKKELNELVSAI 595
Cdd:TIGR03990 409 -----VL--------------------VRPSGTEPIVRIYAE--AK----TEERAEELLEEGRSLV 443
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
15-612 |
0e+00 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 797.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 15 LDQETAQWLRWDKNSLTLEAVKRLIAEGNKEELRKCFGARMEFGTAGLRAAMGPGISRMNDLTIIQTTQGFCRYLEKQFS 94
Cdd:PTZ00150 5 LEAQVELWLKWDKDPETRKEIEELLASKDEEELKRRFLKRMEFGTAGLRGKMGAGFNCMNDLTVQQTAQGLCAYVIETFG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 95 -DLKQKGIVISFDARAHpssggsSRRFARLAATTFISQGIPVYLFSDITPTPFVPFTVSHLKLCAGIMITASHNPKQDNG 173
Cdd:PTZ00150 85 qALKSRGVVIGYDGRYH------SRRFAEITASVFLSKGFKVYLFGQTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 174 YKVYWDNGAQIISPHDKGISQAIEENLEPWPQAWDDSlidSSPLLHNPSASINNDYFEDLKKYCFHRSVNReTKVKFVHT 253
Cdd:PTZ00150 159 YKVYWSNGAQIIPPHDKNISAKILSNLEPWSSSWEYL---TETLVEDPLAEVSDAYFATLKSEYNPACCDR-SKVKIVYT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 254 SVHGVGHSFVQSAFKAFDLVPPEAVPEQKDPDPEFPTVKYPNPEEGKGVLTLSFALADKTKARIVLANDPDADRLAVAEK 333
Cdd:PTZ00150 235 AMHGVGTRFVQKALHTVGLPNLLSVAQQAEPDPEFPTVTFPNPEEGKGALKLSMETAEAHGSTVVLANDPDADRLAVAEK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 334 QDSGeWRVFSGNELGALLGWWLFTSWKEKNQDRSalkDTYMLSSTVSSKILRAIALKEGFHFEETLTGFKWMGNRAKQLI 413
Cdd:PTZ00150 315 LNNG-WKIFTGNELGALLAWWAMKRYRRQGIDKS---KCFFICTVVSSRMLKKMAEKEGFQYDETLTGFKWIGNKAIELN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 414 D-QGKTVLFAFEEAIGYMCCPFVLDKDGVSAAVISAELASFLATKNLSLSQQLKAIYVEYGYHITKASYFICHDQETIKK 492
Cdd:PTZ00150 391 AeNGLTTLFAYEEAIGFMLGTRVRDKDGVTAAAVVAEMALYLYERGKTLVEHLESLYKQYGYHFTNNSYYICYDPSRIVS 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 493 LFENLRNyDGKnnYPKACGKFEISAIRDLTTGYDDSQPDKKAVLPTSKSSQMITFTFANGGVATMRTSGTEPKIKYYAEL 572
Cdd:PTZ00150 471 IFNDIRN-NGS--YPTKLGGYPVTRIRDLTTGYDTATPDGKPLLPVSASTQMITFYFENGAIITIRGSGTEPKLKWYAEL 547
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 116242708 573 CAppgnSDPEQLKKELNELVSAIEEHFFQPQKYNLQPKAD 612
Cdd:PTZ00150 548 SG----TKDEAVEKELAALVDEVVEQLMQPEKYGLVPRKE 583
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
54-592 |
0e+00 |
|
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: 743.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 54 RMEFGTAGLRAAMGPGISRMNDLTIIQTTQGFCRYLEKQFSDLKQKGIVISFDARAHpssggsSRRFARLAATTFISQGI 133
Cdd:cd05799 1 RLEFGTAGLRGKMGAGTNRMNDYTVRQATQGLANYLKKKGPDAKNRGVVIGYDSRHN------SREFAELTAAVLAANGI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 134 PVYLFSDITPTPFVPFTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDKGISQAIEENLEPWPQAWDDSLid 213
Cdd:cd05799 75 KVYLFDDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAVLEPLDIKFEEAL-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 214 SSPLLHNPSASINNDYFEDLKKYCFHRSVNRETKVKFVHTSVHGVGHSFVQSAFKAFDLVPPEAVPEQKDPDPEFPTVKY 293
Cdd:cd05799 153 DSGLIKYIGEEIDDAYLEAVKKLLVNPELNEGKDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVVEEQAEPDPDFPTVKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 294 PNPEEgKGVLTLSFALADKTKARIVLANDPDADRLAVAEKQDSGEWRVFSGNELGALLGWWLFTSWKEKNQDrsaLKDTY 373
Cdd:cd05799 233 PNPEE-PGALDLAIELAKKVGADLILATDPDADRLGVAVKDKDGEWRLLTGNEIGALLADYLLEQRKEKGKL---PKNPV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 374 MLSSTVSSKILRAIALKEGFHFEETLTGFKWMGNRAKQLIDQGKTVLFAFEEAIGYMCCPFVLDKDGVSAAVISAELASF 453
Cdd:cd05799 309 IVKTIVSSELLRKIAKKYGVKVEETLTGFKWIGNKIEELESGGKKFLFGFEESIGYLVGPFVRDKDGISAAALLAEMAAY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 454 LATKNLSLSQQLKAIYVEYGYHITKASYFIC---HDQETIKKLFENLRNYDgknnypkacgkfeisairdlttgyddsqp 530
Cdd:cd05799 389 LKAQGKTLLDRLDELYEKYGYYKEKTISITFegkEGPEKIKAIMDRLRNNP----------------------------- 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116242708 531 dkkavlptskssQMITFTFANGGVATMRTSGTEPKIKYYAELCAPpgnSDPEQLKKELNELV 592
Cdd:cd05799 440 ------------NVLTFYLEDGSRVTVRPSGTEPKIKFYIEVVGK---KTLEEAEKKLDALK 486
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
56-592 |
2.08e-110 |
|
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: 335.10 E-value: 2.08e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 56 EFGTAGLRAAMGPGIsrmNDLTIIQTTQGFCRYlekqfsdlkqkgivisfdarahpssggssrrfarlaattfisqgipv 135
Cdd:cd03084 1 IFGTSGVRGVVGDDI---TPETAVALGQAIGST----------------------------------------------- 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 136 ylfsditptpfvpftvshlklcAGIMITASHNPKQDNGYKVYWDNGAQIISPHDKGISQAIEENLEPWPQAWDdslidss 215
Cdd:cd03084 31 ----------------------GGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSAVAYE------- 81
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 216 PLLHNPSASINNDYFEDLKKYCFHRSVNrETKVKFVHTSVHGVGHSFVQSAFKAFDlvpPEAVPEQKDPDPEFPtVKYPN 295
Cdd:cd03084 82 LGGSVKAVDILQRYFEALKKLFDVAALS-NKKFKVVVDSVNGVGGPIAPQLLEKLG---AEVIPLNCEPDGNFG-NINPD 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 296 PEEGKGVLTLSFALaDKTKARIVLANDPDADRLAVAEKQdsgeWRVFSGNELGALLGWWLFTSWKeknqdrsalKDTYML 375
Cdd:cd03084 157 PGSETNLKQLLAVV-KAEKADFGVAFDGDADRLIVVDEN----GGFLDGDELLALLAVELFLTFN---------PRGGVV 222
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 376 SSTVSSKILRAIALKEGFHFEETLTGFKWMGNRAKQlidqgKTVLFAFEEAIGYMCCPFVLDKDGVSAAVISAELASFLa 455
Cdd:cd03084 223 KTVVSSGALDKVAKKLGIKVIRTKTGFKWVGEAMQE-----GDVVLGGEESGGVIFPEFHPGRDGISAALLLLEILANL- 296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 456 tkNLSLSQQLKAIYVEYGYHITKAsyfichdqetikklfenlrnydgknnypkacgkfeisairdlttgyddsqpdkkav 535
Cdd:cd03084 297 --GKSLSELFSELPRYYYIRLKVR-------------------------------------------------------- 318
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 116242708 536 lptskssqmitftfangGVATMRTSGTEPKIKYYAELCAPpgnSDPEQLKKELNELV 592
Cdd:cd03084 319 -----------------GWVLVRASGTEPAIRIYAEADTQ---EDVEQIKKEARELV 355
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
57-599 |
1.49e-92 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 292.49 E-value: 1.49e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 57 FGTAGLRAAMGPGisrMNDLTIIQTTQGFCRYLEKQfsdlKQKGIVISFDARAhpssggSSRRFARLAATTFISQGIPVY 136
Cdd:COG1109 7 FGTDGIRGIVGEE---LTPEFVLKLGRAFGTYLKEK----GGPKVVVGRDTRL------SSPMLARALAAGLASAGIDVY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 137 LFsDITPTPFVPFTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDKGISQAIEENLEPWPQAWDDSLIdssp 216
Cdd:COG1109 74 DL-GLVPTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKEDFRRAEAEEIGKV---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 217 llhNPSASINNDYFEDLKKYCFHRSvnRETKVKFVHTSVHGVGHSFVQSAFKA--FDLVPpeaVPEQkdPDPEFPTVkYP 294
Cdd:COG1109 149 ---TRIEDVLEAYIEALKSLVDEAL--RLRGLKVVVDCGNGAAGGVAPRLLRElgAEVIV---LNAE--PDGNFPNH-NP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 295 NPEEgkGVLTLSFALADKTKARIVLANDPDADRLAVAEKQdsGewRVFSGNELGALLGWWLftswKEKNqdrsalKDTYM 374
Cdd:COG1109 218 NPEP--ENLEDLIEAVKETGADLGIAFDGDADRLGVVDEK--G--RFLDGDQLLALLARYL----LEKG------PGGTV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 375 LSSTVSSKILRAIALKEGFHFEETLTGFKWMGNRAKQLidqgkTVLFAFEEAIGYMCCPFVLDKDGVSAAVISAELasfL 454
Cdd:COG1109 282 VVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKMRET-----GAVLGGEESGGIIFPDFVPTDDGILAALLLLEL---L 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 455 ATKNLSLSQQLKaiyvEYGYHITKASYFICHDQETIKKLFENLRNydgknnypkacgkfEISAIRDLTTgyddsqpdkka 534
Cdd:COG1109 354 AKQGKSLSELLA----ELPRYPQPEINVRVPDEEKIGAVMEKLRE--------------AVEDKEELDT----------- 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116242708 535 vlptsksSQMITFTFANGGVATMRTSGTEPKIKYYAElcAPpgnsDPEQLKKELNELVSAIEEHF 599
Cdd:COG1109 405 -------IDGVKVDLEDGGWVLVRPSGTEPLLRVYAE--AK----DEEEAEELLAELAELVEEAL 456
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
55-592 |
1.43e-57 |
|
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: 200.47 E-value: 1.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 55 MEFGTAGLRAAMGPGISRMNdLTIIqtTQGFCRYLEKQFsdLKQKGIVISFDARAHpssggsSRRFARLAATTFISQGIP 134
Cdd:cd05800 1 IKFGTDGWRGIIAEDFTFEN-VRRV--AQAIADYLKEEG--GGGRGVVVGYDTRFL------SEEFARAVAEVLAANGID 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 135 VYLFSDITPTPFVPFTVSHLKLCAGIMITASHNPKQDNGYKvywdngaqiISPHDKG-----ISQAIEENLEPWPQAWDD 209
Cdd:cd05800 70 VYLSDRPVPTPAVSWAVKKLGAAGGVMITASHNPPEYNGVK---------VKPAFGGsalpeITAAIEARLASGEPPGLE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 210 SLIDSSPLLHNPSasinNDYFEDLKKYcFHRSVNRETKVKFVHTSVHGVGHSFVQSAFKAFDLvppEAVPEQKDPDPEFP 289
Cdd:cd05800 141 ARAEGLIETIDPK----PDYLEALRSL-VDLEAIREAGLKVVVDPMYGAGAGYLEELLRGAGV---DVEEIRAERDPLFG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 290 TVKyPNPEEgkGVLTLSFALADKTKARIVLANDPDADRLAVAEKQDsgewRVFSGNELGALLGWWLftsWKEKNQDRSAL 369
Cdd:cd05800 213 GIP-PEPIE--KNLGELAEAVKEGGADLGLATDGDADRIGAVDEKG----NFLDPNQILALLLDYL---LENKGLRGPVV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 370 KdtymlssTVS-SKILRAIALKEGFHFEETLTGFKWMGnrakQLIDQGKtVLFAFEEAIGYMCCPFVLDKDGVSAAVISA 448
Cdd:cd05800 283 K-------TVStTHLIDRIAEKHGLPVYETPVGFKYIA----EKMLEED-VLIGGEESGGLGIRGHIPERDGILAGLLLL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 449 ELasfLATKNLSLSQQLKAIYVEYGYHITKASYFICHDQ--ETIKKLFenlrnydgKNNYPKACGKFEISAIRDLtTGYd 526
Cdd:cd05800 351 EA---VAKTGKPLSELVAELEEEYGPSYYDRIDLRLTPAqkEAILEKL--------KNEPPLSIAGGKVDEVNTI-DGV- 417
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116242708 527 dsqpdKkavlptskssqmitFTFANGGVATMRTSGTEPKIKYYAElcappgNSDPEQLKKELNELV 592
Cdd:cd05800 418 -----K--------------LVLEDGSWLLIRPSGTEPLLRIYAE------APSPEKVEALLDAGK 458
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
54-203 |
6.72e-41 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 145.06 E-value: 6.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 54 RMEFGTAGLRAAMGPGIsrMNDLTIIQTTQGFCRYLEKQfsdLKQKGIVISFDARAhpssggSSRRFARLAATTFISQGI 133
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGE--LTPEFALKLGQAIASYLRAQ---GGGGKVVVGRDTRY------SSRELARALAAGLASNGV 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 134 PVYLFsDITPTPFVPFTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDKGISQAIEENLEPW 203
Cdd:pfam02878 70 EVILL-GLLPTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKEDFYR 138
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
57-595 |
7.69e-27 |
|
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: 113.76 E-value: 7.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 57 FGTAGLRAAMGPGisrMNDLTIIQTTQGFCRYLEKqfsdlkqKGIVISFDARAhpssggSSRRFARLAATTFISQGIPVY 136
Cdd:TIGR03990 4 FGTSGIRGIVGEE---LTPELALKVGKAFGTYLRG-------GKVVVGRDTRT------SGPMLENAVIAGLLSTGCDVV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 137 LFsDITPTPFVPFTVSHLKLCAGIMITASHNPKQDNGYKVyWDNGAQIISPHD-KGISQAIEENLEPWPqAWDDSLIDSS 215
Cdd:TIGR03990 68 DL-GIAPTPTLQYAVRELGADGGIMITASHNPPEYNGIKL-LNSDGTELSREQeEEIEEIAESGDFERA-DWDEIGTVTS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 216 PllhnpsASINNDYFEDLKKycfhrSVNRET----KVKFVHTSVHGVGHSFVQSAFKAFDLvppEAVPEQKDPDPEFPtv 291
Cdd:TIGR03990 145 D------EDAIDDYIEAILD-----KVDVEAirkkGFKVVVDCGNGAGSLTTPYLLRELGC---KVITLNCQPDGTFP-- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 292 kYPNPEEGKGVLTLSFALADKTKARIVLANDPDADRLA-VAEKqdsGewRVFSGNELGALLGWWLFTSWKEKnqdrsalk 370
Cdd:TIGR03990 209 -GRNPEPTPENLKDLSALVKATGADLGIAHDGDADRLVfIDEK---G--RFIGGDYTLALFAKYLLEHGGGK-------- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 371 dtymLSSTVS-SKILRAIALKEGFHFEETLTGfkwMGNRAKQLIDQGktVLFAFEEAIGYMCCPFVLDKDGVSAAvisAE 449
Cdd:TIGR03990 275 ----VVTNVSsSRAVEDVAERHGGEVIRTKVG---EVNVAEKMKEEG--AVFGGEGNGGWIFPDHHYCRDGLMAA---AL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 450 LASFLATKNLSLSQQLKAIyveYGYHITKASyfICHDQETIKKLFENLrnydgKNNYPKAcgkfEISAIRDLTTGYDDSQ 529
Cdd:TIGR03990 343 FLELLAEEGKPLSELLAEL---PKYPMSKEK--VELPDEDKEEVMEAV-----EEEFADA----EIDTIDGVRIDFEDGW 408
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116242708 530 pdkkaVLptskssqmitftfanggvatMRTSGTEPKIKYYAElcAPpgnsDPEQLKKELNELVSAI 595
Cdd:TIGR03990 409 -----VL--------------------VRPSGTEPIVRIYAE--AK----TEERAEELLEEGRSLV 443
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
228-333 |
8.58e-23 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 93.12 E-value: 8.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 228 DYFEDLKKYCFhRSVNRETKVKFVHTSVHGVGHSFVQSAFKAFDLvppEAVPEQKDPDPEFPTvKYPNPEEgKGVLTLSF 307
Cdd:pfam02879 1 AYIDHLLELVD-SEALKKRGLKVVYDPLHGVGGGYLPELLKRLGC---DVVEENCEPDPDFPT-RAPNPEE-PEALALLI 74
|
90 100
....*....|....*....|....*.
gi 116242708 308 ALADKTKARIVLANDPDADRLAVAEK 333
Cdd:pfam02879 75 ELVKSVGADLGIATDGDADRLGVVDE 100
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
94-595 |
4.36e-21 |
|
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100089 Cd Length: 439 Bit Score: 96.10 E-value: 4.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 94 SDLKQKGIVISFDARAhpssggSSRRFARLAATTFISQGIPVYLFsDITPTPFVPFTVSHLKLcAGIMITASHNPKQDNG 173
Cdd:cd03087 29 TYLGGGTVVVGRDTRT------SGPMLKNAVIAGLLSAGCDVIDI-GIVPTPALQYAVRKLGD-AGVMITASHNPPEYNG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 174 YKVYWDNGAQIISPHDKGISQAIEENLEPwPQAWDDSLIDSSPllhnpsASINNDYFEDLKKYCfhrSVNRETKVKFVHT 253
Cdd:cd03087 101 IKLVNPDGTEFSREQEEEIEEIIFSERFR-RVAWDEVGSVRRE------DSAIDEYIEAILDKV---DIDGGKGLKVVVD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 254 SVHGVGHsfvqsafkafdLVPPEAVPE--------QKDPDPEFPTvkyPNPEEGKGVLTLSFALADKTKARIVLANDPDA 325
Cdd:cd03087 171 CGNGAGS-----------LTTPYLLRElgckvitlNANPDGFFPG---RPPEPTPENLSELMELVRATGADLGIAHDGDA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 326 DRL-AVAEKqdsGewRVFSGNELGALLGWWLFTSWKEKnqdrsalkdtymLSSTVS-SKILRAIALKEGFHFEETLTGfk 403
Cdd:cd03087 237 DRAvFVDEK---G--RFIDGDKLLALLAKYLLEEGGGK------------VVTPVDaSMLVEDVVEEAGGEVIRTPVG-- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 404 wMGNRAKQLIDQGktVLFAFEEAIGYMCCPFVLDKDGVSAAVISAELASflatKNLSLSQQLKAIYVeygYHITKASYFI 483
Cdd:cd03087 298 -DVHVAEEMIENG--AVFGGEPNGGWIFPDHQLCRDGIMTAALLLELLA----EEKPLSELLDELPK---YPLLREKVEC 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 484 CHDQ--ETIKKLFENLRNYDGKNNypkacgkfEISAIRdltTGYDDSQpdkkaVLptskssqmitftfanggvatMRTSG 561
Cdd:cd03087 368 PDEKkeEVMEAVEEELSDADEDVD--------TIDGVR---IEYEDGW-----VL--------------------IRPSG 411
|
490 500 510
....*....|....*....|....*....|....
gi 116242708 562 TEPKIKYYAElcappgNSDPEQLKKELNELVSAI 595
Cdd:cd03087 412 TEPKIRITAE------AKTEERAKELLEEGRSKV 439
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
87-351 |
4.87e-21 |
|
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: 96.04 E-value: 4.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 87 RYLEKQFSDLKQKGIVISFDARAhpssggSSRRFARLAATTFISQGIPVYlfsDI--TPTPFVPFTVSHLKLCAGIMITA 164
Cdd:cd03089 25 RAFGSWLLEKGAKKVVVGRDGRL------SSPELAAALIEGLLAAGCDVI---DIglVPTPVLYFATFHLDADGGVMITA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 165 SHNPKQDNGYKVYWDNGAqiISPHD-KGISQAIEENLEPWPQAwDDSLIdsspllhnpSASINNDYFEDLKKYCFHrsvn 243
Cdd:cd03089 96 SHNPPEYNGFKIVIGGGP--LSGEDiQALRERAEKGDFAAATG-RGSVE---------KVDILPDYIDRLLSDIKL---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 244 RETKVKFVHTSVHGVGHSFVQSAFKAFDLvppEAVPEQKDPDPEFPTvKYPNPEEGKgvltlsfALAD------KTKARI 317
Cdd:cd03089 160 GKRPLKVVVDAGNGAAGPIAPQLLEALGC---EVIPLFCEPDGTFPN-HHPDPTDPE-------NLEDliaavkENGADL 228
|
250 260 270
....*....|....*....|....*....|....
gi 116242708 318 VLANDPDADRLAVAEKqdSGewRVFSGNELGALL 351
Cdd:cd03089 229 GIAFDGDGDRLGVVDE--KG--EIIWGDRLLALF 258
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
344-472 |
7.18e-15 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 70.94 E-value: 7.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 344 GNELGALLGWWLFTSWKEKnqdrsalKDTYMLSSTVSSKILRAIALKEGFHFEETLTGFKWMGNRAKQlidqgKTVLFAF 423
Cdd:pfam02880 2 GDQILALLAKYLLEQGKLP-------PGAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMRE-----EGALFGG 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 116242708 424 EEAIGYMCCPFVLDKDGVSAAVISAELasfLATKNLSLSQQLKAIYVEY 472
Cdd:pfam02880 70 EESGHIIFLDHATTKDGILAALLVLEI---LARTGKSLSELLEELPEKY 115
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
61-330 |
8.88e-15 |
|
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: 76.96 E-value: 8.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 61 GLRAAMGPGISRMNdltIIQTTQGFCRYlekQFSDLKQKGIVISFDARAhpssggSSRRFARLAATTFISQGIPVyLFSD 140
Cdd:cd05803 6 GIRGIVGEGLTPEV---ITRYVAAFATW---QPERTKGGKIVVGRDGRP------SGPMLEKIVIGALLACGCDV-IDLG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 141 ITPTPFVPFTVSHLKLCAGIMITASHNPKQDNGYKVYW--------DNGAQIISPHDKGISQaieenlepwPQAWDDSL- 211
Cdd:cd05803 73 IAPTPTVQVLVRQSQASGGIIITASHNPPQWNGLKFIGpdgefltpDEGEEVLSCAEAGSAQ---------KAGYDQLGe 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 212 IDSSPllhnpsasinnDYFED-----LKKYCFHRSVNRETKVKFVHTSVHGVGHSFVQSAFKAFDLVPPEAVPEqkdPDP 286
Cdd:cd05803 144 VTFSE-----------DAIAEhidkvLALVDVDVIKIRERNFKVAVDSVNGAGGLLIPRLLEKLGCEVIVLNCE---PTG 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 116242708 287 EFPTVKYPNPEEgkgvLTLSFALADKTKARIVLANDPDADRLAV 330
Cdd:cd05803 210 LFPHTPEPLPEN----LTQLCAAVKESGADVGFAVDPDADRLAL 249
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
57-571 |
7.33e-13 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 71.32 E-value: 7.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 57 FGTAGLR-AAMGPGisrMNDLTIIQTTQGFCRYLekqfsdlKQKGI----VISFDARAHpssggsSRRFARLAATTFISQ 131
Cdd:PRK07564 40 FGTSGHRgSSLQPS---FNENHILAIFQAICEYR-------GKQGItgplFVGGDTHAL------SEPAIQSALEVLAAN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 132 GIPVYLFSD--ITPTPfvpfTVSHLKLCA---------GIMITASHNPKQDNGYKVYWDNGAqiisPHDKGISQAIEE-- 198
Cdd:PRK07564 104 GVGVVIVGRggYTPTP----AVSHAILKYngrgggladGIVITPSHNPPEDGGIKYNPPNGG----PADTDVTDAIEAra 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 199 ------NLE-----PWPQAWDDSLIDSspllHNPSAsinnDYFEDLKKyCFHRSVNRETKVKFVHTSVHGVGHSFVQSAF 267
Cdd:PRK07564 176 nellayGLKgvkriPLDRALASMTVEV----IDPVA----DYVEDLEN-VFDFDAIRKAGLRLGVDPLGGATGPYWKAIA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 268 KAFDLvPPEAVPEQKDPDPEFPTVKY-----PNPeegkgvlTLSFALAD----KTKARIVLANDPDADR----------- 327
Cdd:PRK07564 247 ERYGL-DLTVVNAPVDPTFNFMPLDDdgkirMDC-------SSPYAMAGllalKDAFDLAFANDPDGDRhgivtpgglmn 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 328 ----LAVAekqdsgewrvfsgnelgallGWWLFT---SWKeknqDRSALKDTYmlsstVSSKILRAIALKEGFHFEETLT 400
Cdd:PRK07564 319 pnhyLAVA--------------------IAYLFHhrpGWR----AGAGVGKTL-----VSSAMIDRVAAKLGRKLYEVPV 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 401 GFKWMGNrakqLIDQGKtVLFAFEEAIG-----YMCCPFVLDKDGVSAAVISAELasfLATKNLSLSQQLKAIYVEYGyh 475
Cdd:PRK07564 370 GFKWFVN----GLDDGS-LGFGGEESAGasflrRDGSVWTTDKDGLIAVLLAAEI---LAVTGKSPSEIYRELWARFG-- 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 476 itkASYFICHDQETI---KKLFENLRnydgknnyPKACGKFEISAirDLTTGYDDSQPDKKAVLPTSKssqmitFTFANG 552
Cdd:PRK07564 440 ---RPYYSRHDAPATpeqKAALRKLS--------PELVGATELAG--DPIDASLTEAPGNGAAIGGLK------VVTENG 500
|
570
....*....|....*....
gi 116242708 553 GVAtMRTSGTEPKIKYYAE 571
Cdd:PRK07564 501 WFA-ARPSGTETTYKIYAE 518
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
54-571 |
3.64e-11 |
|
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: 65.73 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 54 RMEFGTAGLRAAMGPGisRMNDLTIIQTTQGFCRYLekqfsdlKQKGI----VISFDAraHPSSGGssrrfARLAA-TTF 128
Cdd:cd05801 20 RVAFGTSGHRGSSLKG--SFNEAHILAISQAICDYR-------KSQGItgplFLGKDT--HALSEP-----AFISAlEVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 129 ISQGIPVYLFSD--ITPTPFVPFTV------SHLKLCAGIMITASHNPKQDNGYKVYWDNGAqiisPHDKGISQAIEE-- 198
Cdd:cd05801 84 AANGVEVIIQQNdgYTPTPVISHAIltynrgRTEGLADGIVITPSHNPPEDGGFKYNPPHGG----PADTDITRWIEKra 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 199 ------NLE-----PWPQAWDDSLIDSSPLLHNpsasinndYFEDLKKyCFHRSVNRETKVKFvhtSVHGVGHSFVQ--- 264
Cdd:cd05801 160 nallanGLKgvkriPLEAALASGYTHRHDFVTP--------YVADLGN-VIDMDAIRKSGLRL---GVDPLGGASVPywq 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 265 --SAFKAFDLvppEAVPEQKDPDPEFPTVKYpnpeEGKGVLTLS--FALAD----KTKARIVLANDPDADRLAVAEKQds 336
Cdd:cd05801 228 piAEKYGLNL---TVVNPKVDPTFRFMTLDH----DGKIRMDCSspYAMAGllklKDKFDLAFANDPDADRHGIVTPS-- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 337 geWRVFSGNELGALLGWWLFTS---WKEknqdRSALKDTYmlsstVSSKILRAIALKEGFHFEETLTGFKWMgnrAKQLI 413
Cdd:cd05801 299 --AGLMNPNHYLSVAIDYLFTHrplWNK----SAGVGKTL-----VSSSMIDRVAAALGRKLYEVPVGFKWF---VDGLL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 414 DQgkTVLFAFEEAIG-----YMCCPFVLDKDGVSAAVISAELasfLATKNLSLSQQLKAIYVEYGYHITK-ASYFICHDQ 487
Cdd:cd05801 365 DG--SLGFGGEESAGasflrRDGTVWTTDKDGIIMCLLAAEI---LAVTGKDPGQLYQELTERFGEPYYArIDAPATPEQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 488 etiKKLFENLRNYDGKnnyPKACGKFEISAIrdLTTGyddsqPDKKAVLPTSKssqmitFTFANGGVATmRTSGTEPKIK 567
Cdd:cd05801 440 ---KARLKKLSPEQVT---ATELAGDPILAK--LTRA-----PGNGASIGGLK------VTTANGWFAA-RPSGTEDVYK 499
|
....
gi 116242708 568 YYAE 571
Cdd:cd05801 500 IYAE 503
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
128-201 |
5.80e-11 |
|
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: 64.81 E-value: 5.80e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116242708 128 FISQGIPVYLFsDITPTPFVPFTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQiisphdkgISQAIEENLE 201
Cdd:cd05802 61 LTSAGVDVLLL-GVIPTPAVAYLTRKLRADAGVVISASHNPFEDNGIKFFSSDGYK--------LPDEVEEEIE 125
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
57-197 |
1.59e-08 |
|
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: 57.38 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 57 FGTAGLRAAMGPGIsrmndLTIIQTTQG--FCRYLEKQFSDLKQKgIVISFDARAhpssggSSRRFARLAATTFISQGIP 134
Cdd:TIGR01455 1 FGTDGVRGRAGQEP-----LTAELALLLgaAAGRVLRQGRDTAPR-VVIGKDTRL------SGYMLENALAAGLNSAGVD 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116242708 135 VYLFSDItPTPFVPFTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIisphDKGISQAIE 197
Cdd:TIGR01455 69 VLLLGPL-PTPAVAYLTRTLRADAGVMISASHNPYEDNGIKFFGPGGFKL----DDATEAAIE 126
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
143-201 |
5.57e-06 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 48.98 E-value: 5.57e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 116242708 143 PTPFVPFTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIisphDKGISQAIEENLE 201
Cdd:PRK10887 77 PTPAVAYLTRTLRAEAGIVISASHNPYYDNGIKFFSADGTKL----PDEVELAIEAELD 131
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
96-296 |
1.19e-05 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 48.02 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 96 LKQKGIVISFDARAhpssggSSRRFARLAATTFISQGIPVyLFSDITPTPFVPFTVSHLKLCAGIMITASHNPKQDNGYK 175
Cdd:PRK15414 36 LKPKTIVLGGDVRL------TSETLKLALAKGLQDAGVDV-LDIGMSGTEEIYFATFHLGVDGGIEVTASHNPMDYNGMK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 176 VYWDnGAQIISpHDKGIsqaieENLEPWPQAWDDSLIDSSPLLHNPSASINNDYFEDLKKYCfhrSVNRETKVKFVHTSV 255
Cdd:PRK15414 109 LVRE-GARPIS-GDTGL-----RDVQRLAEANDFPPVDETKRGRYQQINLRDAYVDHLFGYI---NVKNLTPLKLVINSG 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 116242708 256 HGVGHSFV---QSAFKAFDlVPPEAVPEQKDPDPEFPTvKYPNP 296
Cdd:PRK15414 179 NGAAGPVVdaiEARFKALG-APVELIKVHNTPDGNFPN-GIPNP 220
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
57-206 |
2.89e-05 |
|
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose 6-phosphate to mannose-1-phosphate in the second of three steps in the GDP-mannose pathway, in which GDP-D-mannose is synthesized from fructose-6-phosphate. In Mycobacterium tuberculosis, the causative agent of tuberculosis, PMM is involved in the biosynthesis of mannosylated lipoglycans that participate in the association of mycobacteria with host macrophage phagocytic receptors. ManB belongs to the the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100090 Cd Length: 459 Bit Score: 46.81 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 57 FGTAGLRAAmgpgISRMNDLTIIQTTQGFCRYLEKQFsdlKQKGIVISFDARAhpssggSSRRFARLAATTFISQGI-PV 135
Cdd:cd03088 2 FGTSGLRGL----VTDLTDEVCYAYTRAFLQHLESKF---PGDTVAVGRDLRP------SSPRIAAACAAALRDAGFrVV 68
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116242708 136 YLfsDITPTPFVPFTVSHLKlCAGIMITASHNPKQDNGYKVYWDNGaQIISPHDKGISQAIEENLEPWPQA 206
Cdd:cd03088 69 DC--GAVPTPALALYAMKRG-APAIMVTGSHIPADRNGLKFYRPDG-EITKADEAAILAALVELPEALFDP 135
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
159-176 |
9.18e-05 |
|
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: 45.28 E-value: 9.18e-05
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
101-327 |
1.36e-04 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 44.59 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 101 IVISFDARahPSSGGSSRRFARLAAttfiSQGIPVYLFSdITPTPFVPFTVSHLKlCAGIMITASHNPKQDNGYKVyWDN 180
Cdd:PRK09542 38 VVIGHDMR--DSSPELAAAFAEGVT----AQGLDVVRIG-LASTDQLYFASGLLD-CPGAMFTASHNPAAYNGIKL-CRA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116242708 181 GAQIISpHDKGISQAIEEnlepwpqawddsLIDSSPLLHNPSASINN-DYFEDLKKYCfhRSVNRETKVKFVHTSV---H 256
Cdd:PRK09542 109 GAKPVG-QDTGLAAIRDD------------LIAGVPAYDGPPGTVTErDVLADYAAFL--RSLVDLSGIRPLKVAVdagN 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116242708 257 GVGHSFVQSAFKAFDLvppEAVPEQKDPDPEFPTVKyPNPEEGKGVLTLSFALADkTKARIVLANDPDADR 327
Cdd:PRK09542 174 GMGGHTVPAVLGGLPI---TLLPLYFELDGTFPNHE-ANPLDPANLVDLQAFVRE-TGADIGLAFDGDADR 239
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
158-184 |
1.56e-04 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 44.64 E-value: 1.56e-04
10 20
....*....|....*....|....*..
gi 116242708 158 AGIMITASHNPKQDNGYKVYWDNGAQI 184
Cdd:PTZ00302 77 VGVMITASHNPIQDNGVKIIDPDGGML 103
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
159-176 |
2.71e-03 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 40.78 E-value: 2.71e-03
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
542-596 |
6.73e-03 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 35.71 E-value: 6.73e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 116242708 542 SQMITFTFANGGVATMRTSGTEPKIKYYAElcAPpgnsDPEQLKKELNELVSAIE 596
Cdd:pfam00408 23 ADAEKILGEDGRRLDVRPSGTEPVLRVMVE--GD----SDEELARLADEIADLLE 71
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