|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
1-558 |
0e+00 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 752.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 1 MEFGTAGLRAPMGAGISRMNDLTIIQTTQGFCRYLEKQFS-DLKQRGVVISFDARAHpasggsSRRFARLAATAFITQGV 79
Cdd:PTZ00150 45 MEFGTAGLRGKMGAGFNCMNDLTVQQTAQGLCAYVIETFGqALKSRGVVIGYDGRYH------SRRFAEITASVFLSKGF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 80 PVYLFSDITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDRGISQAIEENLEPWPQAWEESlvd 159
Cdd:PTZ00150 119 KVYLFGQTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVYWSNGAQIIPPHDKNISAKILSNLEPWSSSWEYL--- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 160 SSPLLHNPSASIGNDYFEDLK-KYCFHrtVNKESKVKFVHTSVHGVGHEFVQLAFKAFDLAPPEAVPQQKDPDPEFPTVK 238
Cdd:PTZ00150 196 TETLVEDPLAEVSDAYFATLKsEYNPA--CCDRSKVKIVYTAMHGVGTRFVQKALHTVGLPNLLSVAQQAEPDPEFPTVT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 239 YPNPEEGKGVLTLSFALADKIKAKIVLANDPDADRLAVAEKQDSGeWRVFSGNELGALLGWWLFTSWKEKNQDQSNLkdt 318
Cdd:PTZ00150 274 FPNPEEGKGALKLSMETAEAHGSTVVLANDPDADRLAVAEKLNNG-WKIFTGNELGALLAWWAMKRYRRQGIDKSKC--- 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 319 YMLSSTVSSKILRAIALKEGFHFEETLTGFKWMGNRAQQLGD-QGKTVLFAFEEAIGYMCCPFVLDKDGVSAAVICAELA 397
Cdd:PTZ00150 350 FFICTVVSSRMLKKMAEKEGFQYDETLTGFKWIGNKAIELNAeNGLTTLFAYEEAIGFMLGTRVRDKDGVTAAAVVAEMA 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 398 SFLATKNLSLSQQLNAIYVEYGYHITTASYFICHDQGTIQNLFGNLRNyDGKnnYPKMCGKFEISAIRDLTTGYDDSQPD 477
Cdd:PTZ00150 430 LYLYERGKTLVEHLESLYKQYGYHFTNNSYYICYDPSRIVSIFNDIRN-NGS--YPTKLGGYPVTRIRDLTTGYDTATPD 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 478 KKAVLPTSKSSQMITFTFANGGVATMRTSGTEPKIKYYAELCAppgnSDPEHLKKELDELVGAIEEHFFQPQKYNLQPKA 557
Cdd:PTZ00150 507 GKPLLPVSASTQMITFYFENGAIITIRGSGTEPKLKWYAELSG----TKDEAVEKELAALVDEVVEQLMQPEKYGLVPRK 582
|
.
gi 1255287537 558 E 558
Cdd:PTZ00150 583 E 583
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
1-538 |
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: 724.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 1 MEFGTAGLRAPMGAGISRMNDLTIIQTTQGFCRYLEKQFSDLKQRGVVISFDARAHpasggsSRRFARLAATAFITQGVP 80
Cdd:cd05799 2 LEFGTAGLRGKMGAGTNRMNDYTVRQATQGLANYLKKKGPDAKNRGVVIGYDSRHN------SREFAELTAAVLAANGIK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 81 VYLFSDITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDRGISQAIEENLEPWPQAWEESLvdS 160
Cdd:cd05799 76 VYLFDDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAVLEPLDIKFEEAL--D 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 161 SPLLHNPSASIGNDYFEDLKKYCFHRTVNKESKVKFVHTSVHGVGHEFVQLAFKAFDLAPPEAVPQQKDPDPEFPTVKYP 240
Cdd:cd05799 154 SGLIKYIGEEIDDAYLEAVKKLLVNPELNEGKDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVVEEQAEPDPDFPTVKFP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 241 NPEEgKGVLTLSFALADKIKAKIVLANDPDADRLAVAEKQDSGEWRVFSGNELGALLGWWLFTSWKEKNQDqsnLKDTYM 320
Cdd:cd05799 234 NPEE-PGALDLAIELAKKVGADLILATDPDADRLGVAVKDKDGEWRLLTGNEIGALLADYLLEQRKEKGKL---PKNPVI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 321 LSSTVSSKILRAIALKEGFHFEETLTGFKWMGNRAQQLGDQGKTVLFAFEEAIGYMCCPFVLDKDGVSAAVICAELASFL 400
Cdd:cd05799 310 VKTIVSSELLRKIAKKYGVKVEETLTGFKWIGNKIEELESGGKKFLFGFEESIGYLVGPFVRDKDGISAAALLAEMAAYL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 401 ATKNLSLSQQLNAIYVEYGYHITTASYFIC---HDQGTIQNLFGNLRNYDgknnypkmcgkfeisairdlttgyddsqpd 477
Cdd:cd05799 390 KAQGKTLLDRLDELYEKYGYYKEKTISITFegkEGPEKIKAIMDRLRNNP------------------------------ 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1255287537 478 kkavlptskssQMITFTFANGGVATMRTSGTEPKIKYYAELCAPpgnSDPEHLKKELDELV 538
Cdd:cd05799 440 -----------NVLTFYLEDGSRVTVRPSGTEPKIKFYIEVVGK---KTLEEAEKKLDALK 486
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
3-545 |
2.91e-90 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 285.17 E-value: 2.91e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 3 FGTAGLRAPMGAGisrMNDLTIIQTTQGFCRYLEKQfsdlKQRGVVISFDARAhpasggSSRRFARLAATAFITQGVPVY 82
Cdd:COG1109 7 FGTDGIRGIVGEE---LTPEFVLKLGRAFGTYLKEK----GGPKVVVGRDTRL------SSPMLARALAAGLASAGIDVY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 83 LFsDITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDRGISQAIEENLEPWPQAWEESLVdssp 162
Cdd:COG1109 74 DL-GLVPTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKEDFRRAEAEEIGKV---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 163 llhNPSASIGNDYFEDLKKYCFHRTvnKESKVKFVHTSVHGVGHEFVQLAFKAfdlAPPEAVPQQKDPDPEFPTVkYPNP 242
Cdd:COG1109 149 ---TRIEDVLEAYIEALKSLVDEAL--RLRGLKVVVDCGNGAAGGVAPRLLRE---LGAEVIVLNAEPDGNFPNH-NPNP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 243 EEgkGVLTLSFALADKIKAKIVLANDPDADRLAVAEKQdsGewRVFSGNELGALLGWWLftswKEKNqdqsnlKDTYMLS 322
Cdd:COG1109 220 EP--ENLEDLIEAVKETGADLGIAFDGDADRLGVVDEK--G--RFLDGDQLLALLARYL----LEKG------PGGTVVV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 323 STVSSKILRAIALKEGFHFEETLTGFKWMGNRAQQLGdqgktVLFAFEEAIGYMCCPFVLDKDGVSAAVICAELasfLAT 402
Cdd:COG1109 284 TVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKMRETG-----AVLGGEESGGIIFPDFVPTDDGILAALLLLEL---LAK 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 403 KNLSLSQQLNaiyvEYGYHITTASYFICHDQGTIQNLFGNLRNydgknnypkmcgkfEISAIRDLTTgyddsqpdkkavl 482
Cdd:COG1109 356 QGKSLSELLA----ELPRYPQPEINVRVPDEEKIGAVMEKLRE--------------AVEDKEELDT------------- 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1255287537 483 ptsksSQMITFTFANGGVATMRTSGTEPKIKYYAElcAPpgnsDPEHLKKELDELVGAIEEHF 545
Cdd:COG1109 405 -----IDGVKVDLEDGGWVLVRPSGTEPLLRVYAE--AK----DEEEAEELLAELAELVEEAL 456
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
1-149 |
6.09e-40 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 141.59 E-value: 6.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 1 MEFGTAGLRAPMGAGIsrMNDLTIIQTTQGFCRYLEKQfsdLKQRGVVISFDARAhpasggSSRRFARLAATAFITQGVP 80
Cdd:pfam02878 2 QLFGTSGIRGKVGVGE--LTPEFALKLGQAIASYLRAQ---GGGGKVVVGRDTRY------SSRELARALAAGLASNGVE 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1255287537 81 VYLFsDITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDRGISQAIEENLEPW 149
Cdd:pfam02878 71 VILL-GLLPTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKEDFYR 138
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
3-541 |
1.11e-21 |
|
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been characterized as the archaeal protein responsible for the second step of UDP-GlcNAc biosynthesis. This GlmM protein catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. The first-characterized bacterial GlmM protein is modeled by TIGR01455. These two families are members of the larger phosphoglucomutase/phosphomannomutase family (characterized by three domains: pfam02878, pfam02879 and pfam02880), but are not nearest neighbors to each other. This model also includes a number of sequences from non-archaea in the Bacteroides, Chlorobi, Chloroflexi, Planctomycetes and Spirochaetes lineages. Evidence supporting their inclusion in this equivalog as having the same activity comes from genomic context and phylogenetic profiling. A large number of these organisms are known to produce exo-polysaccharide and yet only appeared to contain the GlmS enzyme of the GlmSMU pathway for UDP-GlcNAc biosynthesis (GenProp0750). In some organisms including Leptospira, this archaeal GlmM is found adjacent to the GlmS as well as a putative GlmU non-orthologous homolog. Phylogenetic profiling of the GlmS-only pattern using PPP identifies members of this archaeal GlmM family as the highest-scoring result. [Central intermediary metabolism, Amino sugars]
Pssm-ID: 274906 Cd Length: 443 Bit Score: 97.97 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 3 FGTAGLRAPMGAGisrMNDLTIIQTTQGFCRYLEKqfsdlkqRGVVISFDARAhpasggSSRRFARLAATAFITQGVPVY 82
Cdd:TIGR03990 4 FGTSGIRGIVGEE---LTPELALKVGKAFGTYLRG-------GKVVVGRDTRT------SGPMLENAVIAGLLSTGCDVV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 83 LFsDITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVyWDNGAQIISPHD-RGISQAIEENLEPWPqAWEESLVDSS 161
Cdd:TIGR03990 68 DL-GIAPTPTLQYAVRELGADGGIMITASHNPPEYNGIKL-LNSDGTELSREQeEEIEEIAESGDFERA-DWDEIGTVTS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 162 PllhnpsASIGNDYFEDLKKyCFHRTVNKESKVKFVHTSVHGVGHEFVQLAFKAFDLappEAVPQQKDPDPEFPtvkYPN 241
Cdd:TIGR03990 145 D------EDAIDDYIEAILD-KVDVEAIRKKGFKVVVDCGNGAGSLTTPYLLRELGC---KVITLNCQPDGTFP---GRN 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 242 PEEGKGVLTLSFALADKIKAKIVLANDPDADRLA-VAEKqdsGewRVFSGNELGALLGWWLFtswkeknqdqSNLKDTym 320
Cdd:TIGR03990 212 PEPTPENLKDLSALVKATGADLGIAHDGDADRLVfIDEK---G--RFIGGDYTLALFAKYLL----------EHGGGK-- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 321 LSSTVS-SKILRAIALKEGFHFEETLTGFKWMGNRAQQLGdqgktVLFAFEEAIGYMCCPFVLDKDGVSAAvicAELASF 399
Cdd:TIGR03990 275 VVTNVSsSRAVEDVAERHGGEVIRTKVGEVNVAEKMKEEG-----AVFGGEGNGGWIFPDHHYCRDGLMAA---ALFLEL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 400 LATKNLSLSQQLNAIyveygyhittASYFIChdqgtiqnlfgnlrnydgKNNYPkmcgkfeisairdlttgYDDSQPDK- 478
Cdd:TIGR03990 347 LAEEGKPLSELLAEL----------PKYPMS------------------KEKVE-----------------LPDEDKEEv 381
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1255287537 479 -KAVLPTSKSSQMIT-----FTFANGGVaTMRTSGTEPKIKYYAElcAPpgnsDPEHLKKELDELVGAI 541
Cdd:TIGR03990 382 mEAVEEEFADAEIDTidgvrIDFEDGWV-LVRPSGTEPIVRIYAE--AK----TEERAEELLEEGRSLV 443
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
1-558 |
0e+00 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 752.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 1 MEFGTAGLRAPMGAGISRMNDLTIIQTTQGFCRYLEKQFS-DLKQRGVVISFDARAHpasggsSRRFARLAATAFITQGV 79
Cdd:PTZ00150 45 MEFGTAGLRGKMGAGFNCMNDLTVQQTAQGLCAYVIETFGqALKSRGVVIGYDGRYH------SRRFAEITASVFLSKGF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 80 PVYLFSDITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDRGISQAIEENLEPWPQAWEESlvd 159
Cdd:PTZ00150 119 KVYLFGQTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVYWSNGAQIIPPHDKNISAKILSNLEPWSSSWEYL--- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 160 SSPLLHNPSASIGNDYFEDLK-KYCFHrtVNKESKVKFVHTSVHGVGHEFVQLAFKAFDLAPPEAVPQQKDPDPEFPTVK 238
Cdd:PTZ00150 196 TETLVEDPLAEVSDAYFATLKsEYNPA--CCDRSKVKIVYTAMHGVGTRFVQKALHTVGLPNLLSVAQQAEPDPEFPTVT 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 239 YPNPEEGKGVLTLSFALADKIKAKIVLANDPDADRLAVAEKQDSGeWRVFSGNELGALLGWWLFTSWKEKNQDQSNLkdt 318
Cdd:PTZ00150 274 FPNPEEGKGALKLSMETAEAHGSTVVLANDPDADRLAVAEKLNNG-WKIFTGNELGALLAWWAMKRYRRQGIDKSKC--- 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 319 YMLSSTVSSKILRAIALKEGFHFEETLTGFKWMGNRAQQLGD-QGKTVLFAFEEAIGYMCCPFVLDKDGVSAAVICAELA 397
Cdd:PTZ00150 350 FFICTVVSSRMLKKMAEKEGFQYDETLTGFKWIGNKAIELNAeNGLTTLFAYEEAIGFMLGTRVRDKDGVTAAAVVAEMA 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 398 SFLATKNLSLSQQLNAIYVEYGYHITTASYFICHDQGTIQNLFGNLRNyDGKnnYPKMCGKFEISAIRDLTTGYDDSQPD 477
Cdd:PTZ00150 430 LYLYERGKTLVEHLESLYKQYGYHFTNNSYYICYDPSRIVSIFNDIRN-NGS--YPTKLGGYPVTRIRDLTTGYDTATPD 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 478 KKAVLPTSKSSQMITFTFANGGVATMRTSGTEPKIKYYAELCAppgnSDPEHLKKELDELVGAIEEHFFQPQKYNLQPKA 557
Cdd:PTZ00150 507 GKPLLPVSASTQMITFYFENGAIITIRGSGTEPKLKWYAELSG----TKDEAVEKELAALVDEVVEQLMQPEKYGLVPRK 582
|
.
gi 1255287537 558 E 558
Cdd:PTZ00150 583 E 583
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
1-538 |
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: 724.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 1 MEFGTAGLRAPMGAGISRMNDLTIIQTTQGFCRYLEKQFSDLKQRGVVISFDARAHpasggsSRRFARLAATAFITQGVP 80
Cdd:cd05799 2 LEFGTAGLRGKMGAGTNRMNDYTVRQATQGLANYLKKKGPDAKNRGVVIGYDSRHN------SREFAELTAAVLAANGIK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 81 VYLFSDITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDRGISQAIEENLEPWPQAWEESLvdS 160
Cdd:cd05799 76 VYLFDDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAVLEPLDIKFEEAL--D 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 161 SPLLHNPSASIGNDYFEDLKKYCFHRTVNKESKVKFVHTSVHGVGHEFVQLAFKAFDLAPPEAVPQQKDPDPEFPTVKYP 240
Cdd:cd05799 154 SGLIKYIGEEIDDAYLEAVKKLLVNPELNEGKDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVVEEQAEPDPDFPTVKFP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 241 NPEEgKGVLTLSFALADKIKAKIVLANDPDADRLAVAEKQDSGEWRVFSGNELGALLGWWLFTSWKEKNQDqsnLKDTYM 320
Cdd:cd05799 234 NPEE-PGALDLAIELAKKVGADLILATDPDADRLGVAVKDKDGEWRLLTGNEIGALLADYLLEQRKEKGKL---PKNPVI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 321 LSSTVSSKILRAIALKEGFHFEETLTGFKWMGNRAQQLGDQGKTVLFAFEEAIGYMCCPFVLDKDGVSAAVICAELASFL 400
Cdd:cd05799 310 VKTIVSSELLRKIAKKYGVKVEETLTGFKWIGNKIEELESGGKKFLFGFEESIGYLVGPFVRDKDGISAAALLAEMAAYL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 401 ATKNLSLSQQLNAIYVEYGYHITTASYFIC---HDQGTIQNLFGNLRNYDgknnypkmcgkfeisairdlttgyddsqpd 477
Cdd:cd05799 390 KAQGKTLLDRLDELYEKYGYYKEKTISITFegkEGPEKIKAIMDRLRNNP------------------------------ 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1255287537 478 kkavlptskssQMITFTFANGGVATMRTSGTEPKIKYYAELCAPpgnSDPEHLKKELDELV 538
Cdd:cd05799 440 -----------NVLTFYLEDGSRVTVRPSGTEPKIKFYIEVVGK---KTLEEAEKKLDALK 486
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
104-538 |
1.70e-104 |
|
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: 318.15 E-value: 1.70e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 104 AGIMITASHNPKQDNGYKVYWDNGAQIISPHDRGISQAIEENLEPWPQAWEESlvdssplLHNPSASIGNDYFEDLKKYC 183
Cdd:cd03084 31 GGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSAVAYELG-------GSVKAVDILQRYFEALKKLF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 184 FHRTVNkESKVKFVHTSVHGVGHEFVQLAFKAFDlapPEAVPQQKDPDPEFPtVKYPNPEEGKGVLTLSFALaDKIKAKI 263
Cdd:cd03084 104 DVAALS-NKKFKVVVDSVNGVGGPIAPQLLEKLG---AEVIPLNCEPDGNFG-NINPDPGSETNLKQLLAVV-KAEKADF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 264 VLANDPDADRLAVAEKQdsgeWRVFSGNELGALLGWWLFTSWKeknqdqsnlKDTYMLSSTVSSKILRAIALKEGFHFEE 343
Cdd:cd03084 178 GVAFDGDADRLIVVDEN----GGFLDGDELLALLAVELFLTFN---------PRGGVVKTVVSSGALDKVAKKLGIKVIR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 344 TLTGFKWMGNRAQQlgdqgKTVLFAFEEAIGYMCCPFVLDKDGVSAAVICAELASFLatkNLSLSQQLNAIYVEYGYHIT 423
Cdd:cd03084 245 TKTGFKWVGEAMQE-----GDVVLGGEESGGVIFPEFHPGRDGISAALLLLEILANL---GKSLSELFSELPRYYYIRLK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 424 TAsyfichdqgtiqnlfgnlrnydgknnypkmcgkfeisairdlttgyddsqpdkkavlptskssqmitftfangGVATM 503
Cdd:cd03084 317 VR-------------------------------------------------------------------------GWVLV 323
|
410 420 430
....*....|....*....|....*....|....*
gi 1255287537 504 RTSGTEPKIKYYAELCAPpgnSDPEHLKKELDELV 538
Cdd:cd03084 324 RASGTEPAIRIYAEADTQ---EDVEQIKKEARELV 355
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
3-545 |
2.91e-90 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 285.17 E-value: 2.91e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 3 FGTAGLRAPMGAGisrMNDLTIIQTTQGFCRYLEKQfsdlKQRGVVISFDARAhpasggSSRRFARLAATAFITQGVPVY 82
Cdd:COG1109 7 FGTDGIRGIVGEE---LTPEFVLKLGRAFGTYLKEK----GGPKVVVGRDTRL------SSPMLARALAAGLASAGIDVY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 83 LFsDITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDRGISQAIEENLEPWPQAWEESLVdssp 162
Cdd:COG1109 74 DL-GLVPTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKEDFRRAEAEEIGKV---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 163 llhNPSASIGNDYFEDLKKYCFHRTvnKESKVKFVHTSVHGVGHEFVQLAFKAfdlAPPEAVPQQKDPDPEFPTVkYPNP 242
Cdd:COG1109 149 ---TRIEDVLEAYIEALKSLVDEAL--RLRGLKVVVDCGNGAAGGVAPRLLRE---LGAEVIVLNAEPDGNFPNH-NPNP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 243 EEgkGVLTLSFALADKIKAKIVLANDPDADRLAVAEKQdsGewRVFSGNELGALLGWWLftswKEKNqdqsnlKDTYMLS 322
Cdd:COG1109 220 EP--ENLEDLIEAVKETGADLGIAFDGDADRLGVVDEK--G--RFLDGDQLLALLARYL----LEKG------PGGTVVV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 323 STVSSKILRAIALKEGFHFEETLTGFKWMGNRAQQLGdqgktVLFAFEEAIGYMCCPFVLDKDGVSAAVICAELasfLAT 402
Cdd:COG1109 284 TVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKMRETG-----AVLGGEESGGIIFPDFVPTDDGILAALLLLEL---LAK 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 403 KNLSLSQQLNaiyvEYGYHITTASYFICHDQGTIQNLFGNLRNydgknnypkmcgkfEISAIRDLTTgyddsqpdkkavl 482
Cdd:COG1109 356 QGKSLSELLA----ELPRYPQPEINVRVPDEEKIGAVMEKLRE--------------AVEDKEELDT------------- 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1255287537 483 ptsksSQMITFTFANGGVATMRTSGTEPKIKYYAElcAPpgnsDPEHLKKELDELVGAIEEHF 545
Cdd:COG1109 405 -----IDGVKVDLEDGGWVLVRPSGTEPLLRVYAE--AK----DEEEAEELLAELAELVEEAL 456
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
1-538 |
1.07e-53 |
|
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: 188.92 E-value: 1.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 1 MEFGTAGLRAPMGAGISRMNdLTIIqtTQGFCRYLEKQFsdLKQRGVVISFDARAHpasggsSRRFARLAATAFITQGVP 80
Cdd:cd05800 1 IKFGTDGWRGIIAEDFTFEN-VRRV--AQAIADYLKEEG--GGGRGVVVGYDTRFL------SEEFARAVAEVLAANGID 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 81 VYLFSDITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAqiisPHDRGISQAIEENLEPWPQAWEESLVDS 160
Cdd:cd05800 70 VYLSDRPVPTPAVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGG----SALPEITAAIEARLASGEPPGLEARAEG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 161 SPLLHNPSasigNDYFEDLKKYcfhrtVN----KESKVKFVHTSVHGVGHEFVQLAFKAFDLappEAVPQQKDPDPEFPT 236
Cdd:cd05800 146 LIETIDPK----PDYLEALRSL-----VDleaiREAGLKVVVDPMYGAGAGYLEELLRGAGV---DVEEIRAERDPLFGG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 237 VKyPNPEEGkgvlTLSfALADKIK---AKIVLANDPDADRLAVAEKQDsgewRVFSGNELGALLGWWLftsWKEKNQDQS 313
Cdd:cd05800 214 IP-PEPIEK----NLG-ELAEAVKeggADLGLATDGDADRIGAVDEKG----NFLDPNQILALLLDYL---LENKGLRGP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 314 NLKdtymlssTVS-SKILRAIALKEGFHFEETLTGFKWMGNRAQQlgdqgKTVLFAFEEAIGYMCCPFVLDKDGVSAAVI 392
Cdd:cd05800 281 VVK-------TVStTHLIDRIAEKHGLPVYETPVGFKYIAEKMLE-----EDVLIGGEESGGLGIRGHIPERDGILAGLL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 393 CAELasfLATKNLSLSQQLNAIYVEYGYHittasyfichdqgtiqnlfgnlrnYDGKNNYpkmcgKFEISAIRDLTTGYD 472
Cdd:cd05800 349 LLEA---VAKTGKPLSELVAELEEEYGPS------------------------YYDRIDL-----RLTPAQKEAILEKLK 396
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1255287537 473 DSQPDKKAVLPTSKSSQM--ITFTFANGGVATMRTSGTEPKIKYYAElcappgNSDPEHLKKELDELV 538
Cdd:cd05800 397 NEPPLSIAGGKVDEVNTIdgVKLVLEDGSWLLIRPSGTEPLLRIYAE------APSPEKVEALLDAGK 458
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
1-149 |
6.09e-40 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 141.59 E-value: 6.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 1 MEFGTAGLRAPMGAGIsrMNDLTIIQTTQGFCRYLEKQfsdLKQRGVVISFDARAhpasggSSRRFARLAATAFITQGVP 80
Cdd:pfam02878 2 QLFGTSGIRGKVGVGE--LTPEFALKLGQAIASYLRAQ---GGGGKVVVGRDTRY------SSRELARALAAGLASNGVE 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1255287537 81 VYLFsDITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDRGISQAIEENLEPW 149
Cdd:pfam02878 71 VILL-GLLPTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKEDFYR 138
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
174-279 |
2.48e-22 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 91.58 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 174 DYFEDLKKYCFhRTVNKESKVKFVHTSVHGVGHEFVQLAFKAFDLAPpeaVPQQKDPDPEFPTvKYPNPEEgKGVLTLSF 253
Cdd:pfam02879 1 AYIDHLLELVD-SEALKKRGLKVVYDPLHGVGGGYLPELLKRLGCDV---VEENCEPDPDFPT-RAPNPEE-PEALALLI 74
|
90 100
....*....|....*....|....*.
gi 1255287537 254 ALADKIKAKIVLANDPDADRLAVAEK 279
Cdd:pfam02879 75 ELVKSVGADLGIATDGDADRLGVVDE 100
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
3-541 |
1.11e-21 |
|
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been characterized as the archaeal protein responsible for the second step of UDP-GlcNAc biosynthesis. This GlmM protein catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. The first-characterized bacterial GlmM protein is modeled by TIGR01455. These two families are members of the larger phosphoglucomutase/phosphomannomutase family (characterized by three domains: pfam02878, pfam02879 and pfam02880), but are not nearest neighbors to each other. This model also includes a number of sequences from non-archaea in the Bacteroides, Chlorobi, Chloroflexi, Planctomycetes and Spirochaetes lineages. Evidence supporting their inclusion in this equivalog as having the same activity comes from genomic context and phylogenetic profiling. A large number of these organisms are known to produce exo-polysaccharide and yet only appeared to contain the GlmS enzyme of the GlmSMU pathway for UDP-GlcNAc biosynthesis (GenProp0750). In some organisms including Leptospira, this archaeal GlmM is found adjacent to the GlmS as well as a putative GlmU non-orthologous homolog. Phylogenetic profiling of the GlmS-only pattern using PPP identifies members of this archaeal GlmM family as the highest-scoring result. [Central intermediary metabolism, Amino sugars]
Pssm-ID: 274906 Cd Length: 443 Bit Score: 97.97 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 3 FGTAGLRAPMGAGisrMNDLTIIQTTQGFCRYLEKqfsdlkqRGVVISFDARAhpasggSSRRFARLAATAFITQGVPVY 82
Cdd:TIGR03990 4 FGTSGIRGIVGEE---LTPELALKVGKAFGTYLRG-------GKVVVGRDTRT------SGPMLENAVIAGLLSTGCDVV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 83 LFsDITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVyWDNGAQIISPHD-RGISQAIEENLEPWPqAWEESLVDSS 161
Cdd:TIGR03990 68 DL-GIAPTPTLQYAVRELGADGGIMITASHNPPEYNGIKL-LNSDGTELSREQeEEIEEIAESGDFERA-DWDEIGTVTS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 162 PllhnpsASIGNDYFEDLKKyCFHRTVNKESKVKFVHTSVHGVGHEFVQLAFKAFDLappEAVPQQKDPDPEFPtvkYPN 241
Cdd:TIGR03990 145 D------EDAIDDYIEAILD-KVDVEAIRKKGFKVVVDCGNGAGSLTTPYLLRELGC---KVITLNCQPDGTFP---GRN 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 242 PEEGKGVLTLSFALADKIKAKIVLANDPDADRLA-VAEKqdsGewRVFSGNELGALLGWWLFtswkeknqdqSNLKDTym 320
Cdd:TIGR03990 212 PEPTPENLKDLSALVKATGADLGIAHDGDADRLVfIDEK---G--RFIGGDYTLALFAKYLL----------EHGGGK-- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 321 LSSTVS-SKILRAIALKEGFHFEETLTGFKWMGNRAQQLGdqgktVLFAFEEAIGYMCCPFVLDKDGVSAAvicAELASF 399
Cdd:TIGR03990 275 VVTNVSsSRAVEDVAERHGGEVIRTKVGEVNVAEKMKEEG-----AVFGGEGNGGWIFPDHHYCRDGLMAA---ALFLEL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 400 LATKNLSLSQQLNAIyveygyhittASYFIChdqgtiqnlfgnlrnydgKNNYPkmcgkfeisairdlttgYDDSQPDK- 478
Cdd:TIGR03990 347 LAEEGKPLSELLAEL----------PKYPMS------------------KEKVE-----------------LPDEDKEEv 381
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1255287537 479 -KAVLPTSKSSQMIT-----FTFANGGVaTMRTSGTEPKIKYYAElcAPpgnsDPEHLKKELDELVGAI 541
Cdd:TIGR03990 382 mEAVEEEFADAEIDTidgvrIDFEDGWV-LVRPSGTEPIVRIYAE--AK----TEERAEELLEEGRSLV 443
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
33-297 |
2.97e-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: 96.43 E-value: 2.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 33 RYLEKQFSDLKQRGVVISFDARAhpasggSSRRFARLAATAFITQGVPVYlfsDI--TPTPFVPYTVSHLKLCAGIMITA 110
Cdd:cd03089 25 RAFGSWLLEKGAKKVVVGRDGRL------SSPELAAALIEGLLAAGCDVI---DIglVPTPVLYFATFHLDADGGVMITA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 111 SHNPKQDNGYKVYWDNGAqiISPHD-RGISQAIEENLEPWPQAwEESLVdsspllhnpSASIGNDYFEDLKKYCFHRtvn 189
Cdd:cd03089 96 SHNPPEYNGFKIVIGGGP--LSGEDiQALRERAEKGDFAAATG-RGSVE---------KVDILPDYIDRLLSDIKLG--- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 190 kESKVKFVHTSVHGVGHEFVQLAFKAFDLappEAVPQQKDPDPEFPTvKYPNPEEGKgvltlsfALADKIKAkiVLAN-- 267
Cdd:cd03089 161 -KRPLKVVVDAGNGAAGPIAPQLLEALGC---EVIPLFCEPDGTFPN-HHPDPTDPE-------NLEDLIAA--VKENga 226
|
250 260 270
....*....|....*....|....*....|....*.
gi 1255287537 268 ------DPDADRLAVAEKqdSGewRVFSGNELGALL 297
Cdd:cd03089 227 dlgiafDGDGDRLGVVDE--KG--EIIWGDRLLALF 258
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
3-541 |
8.50e-18 |
|
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: 86.09 E-value: 8.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 3 FGTAGLRAPMGagisrmNDLT---IIQTTQGFCRYLEKqfsdlkqRGVVISFDARAhpasggSSRRFARLAATAFITQGV 79
Cdd:cd03087 2 FGTSGIRGVVG------EELTpelALKVGKALGTYLGG-------GTVVVGRDTRT------SGPMLKNAVIAGLLSAGC 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 80 PVYLFsDITPTPFVPYTVSHLKLcAGIMITASHNPKQDNGYKVYWDNGAQIISPHDRGISQAIEENLEPwPQAWEEslVD 159
Cdd:cd03087 63 DVIDI-GIVPTPALQYAVRKLGD-AGVMITASHNPPEYNGIKLVNPDGTEFSREQEEEIEEIIFSERFR-RVAWDE--VG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 160 SSpllhNPSASIGNDYFEDLKKYCfhrTVNKESKVKFVHTSVHGVGHefvqlafkafdLAPPEA--------VPQQKDPD 231
Cdd:cd03087 138 SV----RREDSAIDEYIEAILDKV---DIDGGKGLKVVVDCGNGAGS-----------LTTPYLlrelgckvITLNANPD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 232 PEFPTvkyPNPEEGKGVLTLSFALADKIKAKIVLANDPDADRL-AVAEKqdsGewRVFSGNELGALLGWWLFTSWKEKnq 310
Cdd:cd03087 200 GFFPG---RPPEPTPENLSELMELVRATGADLGIAHDGDADRAvFVDEK---G--RFIDGDKLLALLAKYLLEEGGGK-- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 311 dqsnlkdtymLSSTVS-SKILRAIALKEGFHFEETltgfkwmgnraqQLGD-------QGKTVLFAFEEAIGYMCCPFVL 382
Cdd:cd03087 270 ----------VVTPVDaSMLVEDVVEEAGGEVIRT------------PVGDvhvaeemIENGAVFGGEPNGGWIFPDHQL 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 383 DKDGV-SAAVICAELAsflatKNLSLSQQLNAIYVeygYHITTASYFICHDQgtiqnlfgnlrnydgknnypkmcgKFEI 461
Cdd:cd03087 328 CRDGImTAALLLELLA-----EEKPLSELLDELPK---YPLLREKVECPDEK------------------------KEEV 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 462 -SAIRDLTTGYDDSqpdkkaVLPTSKssqmITFTFANGGVaTMRTSGTEPKIKYYAElcappgNSDPEHLKKELDELVGA 540
Cdd:cd03087 376 mEAVEEELSDADED------VDTIDG----VRIEYEDGWV-LIRPSGTEPKIRITAE------AKTEERAKELLEEGRSK 438
|
.
gi 1255287537 541 I 541
Cdd:cd03087 439 V 439
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
290-418 |
1.63e-15 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 72.87 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 290 GNELGALLGWWLFTSWKEKnqdqsnlKDTYMLSSTVSSKILRAIALKEGFHFEETLTGFKWMGNRAQQLGdqgktVLFAF 369
Cdd:pfam02880 2 GDQILALLAKYLLEQGKLP-------PGAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEG-----ALFGG 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1255287537 370 EEAIGYMCCPFVLDKDGVSAAVICAELasfLATKNLSLSQQLNAIYVEY 418
Cdd:pfam02880 70 EESGHIIFLDHATTKDGILAALLVLEI---LARTGKSLSELLEELPEKY 115
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
7-276 |
2.88e-12 |
|
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate guanyltransferase domain in a protein of unknown function that is found in both prokaryotes and eukaryotes. This domain belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100096 Cd Length: 445 Bit Score: 68.87 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 7 GLRAPMGAGISRMNdltIIQTTQGFCRYlekQFSDLKQRGVVISFDARAhpasggSSRRFARLAATAFITQGVPVyLFSD 86
Cdd:cd05803 6 GIRGIVGEGLTPEV---ITRYVAAFATW---QPERTKGGKIVVGRDGRP------SGPMLEKIVIGALLACGCDV-IDLG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 87 ITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYW--------DNGAQIISPHDRGisqaiEENLEPWPQAWE-ESL 157
Cdd:cd05803 73 IAPTPTVQVLVRQSQASGGIIITASHNPPQWNGLKFIGpdgefltpDEGEEVLSCAEAG-----SAQKAGYDQLGEvTFS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 158 VDSSPllhnpsASIGNdyfeDLKKYCFHRTVNKESKVKFVHTSVHGVGHEFVQLAFKAFDLappEAVPQQKDPDPEFPTV 237
Cdd:cd05803 148 EDAIA------EHIDK----VLALVDVDVIKIRERNFKVAVDSVNGAGGLLIPRLLEKLGC---EVIVLNCEPTGLFPHT 214
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1255287537 238 KYPNPEEgkgvLT-LSFALADKiKAKIVLANDPDADRLAV 276
Cdd:cd05803 215 PEPLPEN----LTqLCAAVKES-GADVGFAVDPDADRLAL 249
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
78-180 |
1.41e-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: 66.74 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 78 GVPVYLFsDITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQiisphdrgISQAIEENLepwpqaweESL 157
Cdd:cd05802 65 GVDVLLL-GVIPTPAVAYLTRKLRADAGVVISASHNPFEDNGIKFFSSDGYK--------LPDEVEEEI--------EAL 127
|
90 100 110
....*....|....*....|....*....|..
gi 1255287537 158 VDSSPLLHNPSASIG---------NDYFEDLK 180
Cdd:cd05802 128 IDKELELPPTGEKIGrvyriddarGRYIEFLK 159
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
3-536 |
6.55e-11 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 64.77 E-value: 6.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 3 FGTAGLRapmgaGISR---MNDLTIIQTTQGFCRYLEKQFSDLKqrgVVISFDARAHpasggsSRRfarlaatAFIT--- 76
Cdd:PRK07564 40 FGTSGHR-----GSSLqpsFNENHILAIFQAICEYRGKQGITGP---LFVGGDTHAL------SEP-------AIQSale 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 77 ----QGVPVYLFSD--ITPTPfvpyTVSHLKLCA---------GIMITASHNPKQDNGYKVYWDNGAqiisPHDRGISQA 141
Cdd:PRK07564 99 vlaaNGVGVVIVGRggYTPTP----AVSHAILKYngrgggladGIVITPSHNPPEDGGIKYNPPNGG----PADTDVTDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 142 IEE--------NLE-----PWPQAWEESLVDSspllHNPSAsignDYFEDLKKyCFHRTVNKESKVKFVHTSVHGVGHEF 208
Cdd:PRK07564 171 IEAranellayGLKgvkriPLDRALASMTVEV----IDPVA----DYVEDLEN-VFDFDAIRKAGLRLGVDPLGGATGPY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 209 VQLAFKAFDL------APPEAV----PQQKD----PDPefptvkypnpeegkgvlTLSFALADKIKAK----IVLANDPD 270
Cdd:PRK07564 242 WKAIAERYGLdltvvnAPVDPTfnfmPLDDDgkirMDC-----------------SSPYAMAGLLALKdafdLAFANDPD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 271 ADR---------------LAVAekqdsgewrvfsgnelgallGWWLFT---SWKeknqdqsnlKDTYMLSSTVSSKILRA 332
Cdd:PRK07564 305 GDRhgivtpgglmnpnhyLAVA--------------------IAYLFHhrpGWR---------AGAGVGKTLVSSAMIDR 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 333 IALKEGFHFEETLTGFKWMGNraqqLGDQGKtVLFAFEEAIG-----YMCCPFVLDKDGVSAAVICAELasfLATKNLSL 407
Cdd:PRK07564 356 VAAKLGRKLYEVPVGFKWFVN----GLDDGS-LGFGGEESAGasflrRDGSVWTTDKDGLIAVLLAAEI---LAVTGKSP 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 408 SQQLNAIYVEYGyhittASYFICHDqgtiqnlfgnlrnydgknnYPkmCGKFEISAIRDLTTgyddSQPDKK-------- 479
Cdd:PRK07564 428 SEIYRELWARFG-----RPYYSRHD-------------------AP--ATPEQKAALRKLSP----ELVGATelagdpid 477
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1255287537 480 AVLPTSKSSQM----ITFTFANGGVAtMRTSGTEPKIKYYAElcappgnS--DPEHLKKELDE 536
Cdd:PRK07564 478 ASLTEAPGNGAaiggLKVVTENGWFA-ARPSGTETTYKIYAE-------SfeGDEHLHQIQKE 532
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
3-536 |
2.43e-10 |
|
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: 63.03 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 3 FGTAGLRAPMGAGisRMNDLTIIQTTQGFCRYLEKQFSDlkqrGVV-ISFDARAhpasggssrrfarLAATAFIT----- 76
Cdd:cd05801 23 FGTSGHRGSSLKG--SFNEAHILAISQAICDYRKSQGIT----GPLfLGKDTHA-------------LSEPAFISalevl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 77 --QGVPVYLFSD--ITPTPFVPYTV------SHLKLCAGIMITASHNPKQDNGYKVYWDNGAqiisPHDRGISQAIEE-- 144
Cdd:cd05801 84 aaNGVEVIIQQNdgYTPTPVISHAIltynrgRTEGLADGIVITPSHNPPEDGGFKYNPPHGG----PADTDITRWIEKra 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 145 ------NLE-----PWPQAWeeslvdSSPLLHNpsASIGNDYFEDLKKyCFHRTVNKESKVKFvhtSVHGVG----HEFV 209
Cdd:cd05801 160 nallanGLKgvkriPLEAAL------ASGYTHR--HDFVTPYVADLGN-VIDMDAIRKSGLRL---GVDPLGgasvPYWQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 210 QLAFK-AFDLappEAVPQQKDPDPEFPTVKYpnpeEGKGVLTLS--FALADKIKAK----IVLANDPDADRLAVAEKQds 282
Cdd:cd05801 228 PIAEKyGLNL---TVVNPKVDPTFRFMTLDH----DGKIRMDCSspYAMAGLLKLKdkfdLAFANDPDADRHGIVTPS-- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 283 geWRVFSGNELGALLGWWLFTSWKEKNQDQSNLKdTYmlsstVSSKILRAIALKEGFHFEETLTGFKWMgnrAQQLGDQg 362
Cdd:cd05801 299 --AGLMNPNHYLSVAIDYLFTHRPLWNKSAGVGK-TL-----VSSSMIDRVAAALGRKLYEVPVGFKWF---VDGLLDG- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 363 kTVLFAFEEAIG-----YMCCPFVLDKDGVSAAVICAELASfLATKNLS-LSQQLNAIYVEYGYHITTASyfICHDQGTI 436
Cdd:cd05801 367 -SLGFGGEESAGasflrRDGTVWTTDKDGIIMCLLAAEILA-VTGKDPGqLYQELTERFGEPYYARIDAP--ATPEQKAR 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 437 qnlFGNLRNYDGKnnyPKMCGKFEISAIrdLTTGyddsqPDKKAVLPTSKssqmitFTFANGGVATmRTSGTEPKIKYYA 516
Cdd:cd05801 443 ---LKKLSPEQVT---ATELAGDPILAK--LTRA-----PGNGASIGGLK------VTTANGWFAA-RPSGTEDVYKIYA 502
|
570 580
....*....|....*....|..
gi 1255287537 517 ElcappgnS--DPEHLKKELDE 536
Cdd:cd05801 503 E-------SflSEEHLKKIQKE 517
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
3-315 |
1.69e-09 |
|
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: 60.07 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 3 FGTAGLRAPmgAGISRMNDLTIIQTTQGFCRYLEKQFSdlKQRGVVISFDARAhpasggSSRRFARLAATAFITQGVPVY 82
Cdd:TIGR01455 1 FGTDGVRGR--AGQEPLTAELALLLGAAAGRVLRQGRD--TAPRVVIGKDTRL------SGYMLENALAAGLNSAGVDVL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 83 LFSDItPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIisphDRGISQAIEENLEpwpQAWEESLVDSSP 162
Cdd:TIGR01455 71 LLGPL-PTPAVAYLTRTLRADAGVMISASHNPYEDNGIKFFGPGGFKL----DDATEAAIEALLD---EADPLPRPESEG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 163 LLHNPSASIGNDYFEDLKKYCFHRTVNKeSKVKFVHTSVHGVGhefVQLAFKAFDLAPPEAVPQQKDPDPEfptvkypNP 242
Cdd:TIGR01455 143 LGRVKRYPDAVGRYIEFLKSTLPRGLTL-SGLKVVLDCANGAA---YKVAPHVFRELGAEVIAIGVEPDGL-------NI 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1255287537 243 EEGKGVLTLSfALADKIK---AKIVLANDPDADR-LAVAEKQDsgewrVFSGNELGALLGwwlfTSWKEKNQDQSNL 315
Cdd:TIGR01455 212 NDGCGSTHLD-ALQKAVRehgADLGIAFDGDADRvLAVDANGR-----IVDGDQILYIIA----RALKESGELAGNT 278
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
89-156 |
1.05e-06 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 51.29 E-value: 1.05e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1255287537 89 PTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIisPHDrgISQAIEENLEPwPQAWEES 156
Cdd:PRK10887 77 PTPAVAYLTRTLRAEAGIVISASHNPYYDNGIKFFSADGTKL--PDE--VELAIEAELDK-PLTCVES 139
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
3-157 |
2.95e-06 |
|
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: 49.89 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 3 FGTAGLRapmgaG-ISRMNDLTIIQTTQGFCRYLEKQFsdlKQRGVVISFDARAhpasggSSRRFARLAATAFITQGV-P 80
Cdd:cd03088 2 FGTSGLR-----GlVTDLTDEVCYAYTRAFLQHLESKF---PGDTVAVGRDLRP------SSPRIAAACAAALRDAGFrV 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1255287537 81 VYLfsDITPTPFVPYTVSHLKlCAGIMITASHNPKQDNGYKVYWDNGaQIISPHDRGISQAIEENLEPWPQAWEESL 157
Cdd:cd03088 68 VDC--GAVPTPALALYAMKRG-APAIMVTGSHIPADRNGLKFYRPDG-EITKADEAAILAALVELPEALFDPAGALL 140
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
105-147 |
2.36e-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: 47.20 E-value: 2.36e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1255287537 105 GIMITASHNPKQDNGYKvywdngaqIISPHDRGISQAIEENLE 147
Cdd:cd03086 38 GVMITASHNPVEDNGVK--------IVDPDGEMLEESWEPYAT 72
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
94-147 |
5.09e-05 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 46.19 E-value: 5.09e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1255287537 94 PYTVSHLKLCAGIMITASHNPKQDNGYKvywdngaqIISPHDRGISQAIEENLE 147
Cdd:PTZ00302 67 GKRAKRGNKSVGVMITASHNPIQDNGVK--------IIDPDGGMLEESWEKICT 112
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
26-121 |
6.76e-04 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 42.28 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1255287537 26 QTTQGFCRYLEKQFSDL----KQRGVVISFDARahPASGGSSRRFARlAATAfitQGVPVYLFSdITPTPFVPYTVSHLK 101
Cdd:PRK09542 13 QIDEDLVRDVGAAFARLmraeGATTVVIGHDMR--DSSPELAAAFAE-GVTA---QGLDVVRIG-LASTDQLYFASGLLD 85
|
90 100
....*....|....*....|
gi 1255287537 102 lCAGIMITASHNPKQDNGYK 121
Cdd:PRK09542 86 -CPGAMFTASHNPAAYNGIK 104
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
488-542 |
9.63e-04 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 38.02 E-value: 9.63e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1255287537 488 SQMITFTFANGGVATMRTSGTEPKIKYYAElcAPpgnsDPEHLKKELDELVGAIE 542
Cdd:pfam00408 23 ADAEKILGEDGRRLDVRPSGTEPVLRVMVE--GD----SDEELARLADEIADLLE 71
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
105-122 |
2.40e-03 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 40.78 E-value: 2.40e-03
|
| |
