|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
19-620 |
0e+00 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 798.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 19 MDARLDQETAQWLRWDQNPLTSESVKQLIAGGNKEELRKCFGARMEFGTAGLRAPMGAGISRMNDLTIIQTTQGFCRYLE 98
Cdd:PTZ00150 1 MMESLEAQVELWLKWDKDPETRKEIEELLASKDEEELKRRFLKRMEFGTAGLRGKMGAGFNCMNDLTVQQTAQGLCAYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 99 KQFS-DLKQRGVVISFDARAHpasggsSRRFARLAATAFITQGVPVYLFSDITPTPFVPYTVSHLKLCAGIMITASHNPK 177
Cdd:PTZ00150 81 ETFGqALKSRGVVIGYDGRYH------SRRFAEITASVFLSKGFKVYLFGQTVPTPFVPYAVRKLKCLAGVMVTASHNPK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 178 QDNGYKVYWDNGAQIISPHDRGISQAIEENLEPWPQAWEESlvdSSPLLHNPSASIGNDYFEDLK-KYCFHrtVNKESKV 256
Cdd:PTZ00150 155 EDNGYKVYWSNGAQIIPPHDKNISAKILSNLEPWSSSWEYL---TETLVEDPLAEVSDAYFATLKsEYNPA--CCDRSKV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 257 KFVHTSVHGVGHEFVQLAFKAFDLAPPEAVPQQKDPDPEFPTVKYPNPEEGKGVLTLSFALADKIKAKIVLANDPDADRL 336
Cdd:PTZ00150 230 KIVYTAMHGVGTRFVQKALHTVGLPNLLSVAQQAEPDPEFPTVTFPNPEEGKGALKLSMETAEAHGSTVVLANDPDADRL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 337 AVAEKQDSGeWRVFSGNELGALLGWWLFTSWKEKNQDQSNLkdtYMLSSTVSSKILRAIALKEGFHFEETLTGFKWMGNR 416
Cdd:PTZ00150 310 AVAEKLNNG-WKIFTGNELGALLAWWAMKRYRRQGIDKSKC---FFICTVVSSRMLKKMAEKEGFQYDETLTGFKWIGNK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 417 AQQLGD-QGKTVLFAFEEAIGYMCCPFVLDKDGVSAAVICAELASFLATKNLSLSQQLNAIYVEYGYHITTASYFICHDQ 495
Cdd:PTZ00150 386 AIELNAeNGLTTLFAYEEAIGFMLGTRVRDKDGVTAAAVVAEMALYLYERGKTLVEHLESLYKQYGYHFTNNSYYICYDP 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 496 GTIQNLFGNLRNyDGKnnYPKMCGKFEISAIRDLTTGYDDSQPDKKAVLPTSKSSQMITFTFANGGVATMRTSGTEPKIK 575
Cdd:PTZ00150 466 SRIVSIFNDIRN-NGS--YPTKLGGYPVTRIRDLTTGYDTATPDGKPLLPVSASTQMITFYFENGAIITIRGSGTEPKLK 542
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 71153048 576 YYAELCAppgnSDPEHLKKELDELVGAIEEHFFQPQKYNLQPKAE 620
Cdd:PTZ00150 543 WYAELSG----TKDEAVEKELAALVDEVVEQLMQPEKYGLVPRKE 583
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
62-600 |
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: 726.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 62 RMEFGTAGLRAPMGAGISRMNDLTIIQTTQGFCRYLEKQFSDLKQRGVVISFDARAHpasggsSRRFARLAATAFITQGV 141
Cdd:cd05799 1 RLEFGTAGLRGKMGAGTNRMNDYTVRQATQGLANYLKKKGPDAKNRGVVIGYDSRHN------SREFAELTAAVLAANGI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 142 PVYLFSDITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDRGISQAIEENLEPWPQAWEESLvd 221
Cdd:cd05799 75 KVYLFDDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAVLEPLDIKFEEAL-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 222 SSPLLHNPSASIGNDYFEDLKKYCFHRTVNKESKVKFVHTSVHGVGHEFVQLAFKAFDLAPPEAVPQQKDPDPEFPTVKY 301
Cdd:cd05799 153 DSGLIKYIGEEIDDAYLEAVKKLLVNPELNEGKDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVVEEQAEPDPDFPTVKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 302 PNPEEgKGVLTLSFALADKIKAKIVLANDPDADRLAVAEKQDSGEWRVFSGNELGALLGWWLFTSWKEKNQDqsnLKDTY 381
Cdd:cd05799 233 PNPEE-PGALDLAIELAKKVGADLILATDPDADRLGVAVKDKDGEWRLLTGNEIGALLADYLLEQRKEKGKL---PKNPV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 382 MLSSTVSSKILRAIALKEGFHFEETLTGFKWMGNRAQQLGDQGKTVLFAFEEAIGYMCCPFVLDKDGVSAAVICAELASF 461
Cdd:cd05799 309 IVKTIVSSELLRKIAKKYGVKVEETLTGFKWIGNKIEELESGGKKFLFGFEESIGYLVGPFVRDKDGISAAALLAEMAAY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 462 LATKNLSLSQQLNAIYVEYGYHITTASYFIC---HDQGTIQNLFGNLRNYDgknnypkmcgkfeisairdlttgyddsqp 538
Cdd:cd05799 389 LKAQGKTLLDRLDELYEKYGYYKEKTISITFegkEGPEKIKAIMDRLRNNP----------------------------- 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71153048 539 dkkavlptskssQMITFTFANGGVATMRTSGTEPKIKYYAELCAPpgnSDPEHLKKELDELV 600
Cdd:cd05799 440 ------------NVLTFYLEDGSRVTVRPSGTEPKIKFYIEVVGK---KTLEEAEKKLDALK 486
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
65-607 |
1.53e-89 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 285.17 E-value: 1.53e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 65 FGTAGLRAPMGAGisrMNDLTIIQTTQGFCRYLEKQfsdlKQRGVVISFDARAhpasggSSRRFARLAATAFITQGVPVY 144
Cdd:COG1109 7 FGTDGIRGIVGEE---LTPEFVLKLGRAFGTYLKEK----GGPKVVVGRDTRL------SSPMLARALAAGLASAGIDVY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 145 LFsDITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDRGISQAIEENLEPWPQAWEESLVdssp 224
Cdd:COG1109 74 DL-GLVPTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKEDFRRAEAEEIGKV---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 225 llhNPSASIGNDYFEDLKKYCFHRTvnKESKVKFVHTSVHGVGHEFVQLAFKAfdlAPPEAVPQQKDPDPEFPTVkYPNP 304
Cdd:COG1109 149 ---TRIEDVLEAYIEALKSLVDEAL--RLRGLKVVVDCGNGAAGGVAPRLLRE---LGAEVIVLNAEPDGNFPNH-NPNP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 305 EEgkGVLTLSFALADKIKAKIVLANDPDADRLAVAEKQdsGewRVFSGNELGALLGWWLftswKEKNqdqsnlKDTYMLS 384
Cdd:COG1109 220 EP--ENLEDLIEAVKETGADLGIAFDGDADRLGVVDEK--G--RFLDGDQLLALLARYL----LEKG------PGGTVVV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 385 STVSSKILRAIALKEGFHFEETLTGFKWMGNRAQQLGdqgktVLFAFEEAIGYMCCPFVLDKDGVSAAVICAELasfLAT 464
Cdd:COG1109 284 TVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKMRETG-----AVLGGEESGGIIFPDFVPTDDGILAALLLLEL---LAK 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 465 KNLSLSQQLNaiyvEYGYHITTASYFICHDQGTIQNLFGNLRNydgknnypkmcgkfEISAIRDLTTgyddsqpdkkavl 544
Cdd:COG1109 356 QGKSLSELLA----ELPRYPQPEINVRVPDEEKIGAVMEKLRE--------------AVEDKEELDT------------- 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71153048 545 ptsksSQMITFTFANGGVATMRTSGTEPKIKYYAElcAPpgnsDPEHLKKELDELVGAIEEHF 607
Cdd:COG1109 405 -----IDGVKVDLEDGGWVLVRPSGTEPLLRVYAE--AK----DEEEAEELLAELAELVEEAL 456
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
62-211 |
2.73e-40 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 143.52 E-value: 2.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 62 RMEFGTAGLRAPMGAGIsrMNDLTIIQTTQGFCRYLEKQfsdLKQRGVVISFDARAhpasggSSRRFARLAATAFITQGV 141
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGE--LTPEFALKLGQAIASYLRAQ---GGGGKVVVGRDTRY------SSRELARALAAGLASNGV 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 142 PVYLFsDITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDRGISQAIEENLEPW 211
Cdd:pfam02878 70 EVILL-GLLPTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKEDFYR 138
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
65-603 |
1.43e-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: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 65 FGTAGLRAPMGAGisrMNDLTIIQTTQGFCRYLEKqfsdlkqRGVVISFDARAhpasggSSRRFARLAATAFITQGVPVY 144
Cdd:TIGR03990 4 FGTSGIRGIVGEE---LTPELALKVGKAFGTYLRG-------GKVVVGRDTRT------SGPMLENAVIAGLLSTGCDVV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 145 LFsDITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVyWDNGAQIISPHD-RGISQAIEENLEPWPqAWEESLVDSS 223
Cdd:TIGR03990 68 DL-GIAPTPTLQYAVRELGADGGIMITASHNPPEYNGIKL-LNSDGTELSREQeEEIEEIAESGDFERA-DWDEIGTVTS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 224 PllhnpsASIGNDYFEDLKKyCFHRTVNKESKVKFVHTSVHGVGHEFVQLAFKAFDLappEAVPQQKDPDPEFPtvkYPN 303
Cdd:TIGR03990 145 D------EDAIDDYIEAILD-KVDVEAIRKKGFKVVVDCGNGAGSLTTPYLLRELGC---KVITLNCQPDGTFP---GRN 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 304 PEEGKGVLTLSFALADKIKAKIVLANDPDADRLA-VAEKqdsGewRVFSGNELGALLGWWLFtswkeknqdqSNLKDTym 382
Cdd:TIGR03990 212 PEPTPENLKDLSALVKATGADLGIAHDGDADRLVfIDEK---G--RFIGGDYTLALFAKYLL----------EHGGGK-- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 383 LSSTVS-SKILRAIALKEGFHFEETLTGFKWMGNRAQQLGdqgktVLFAFEEAIGYMCCPFVLDKDGVSAAvicAELASF 461
Cdd:TIGR03990 275 VVTNVSsSRAVEDVAERHGGEVIRTKVGEVNVAEKMKEEG-----AVFGGEGNGGWIFPDHHYCRDGLMAA---ALFLEL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 462 LATKNLSLSQQLNAIyveygyhittASYFIChdqgtiqnlfgnlrnydgKNNYPkmcgkfeisairdlttgYDDSQPDK- 540
Cdd:TIGR03990 347 LAEEGKPLSELLAEL----------PKYPMS------------------KEKVE-----------------LPDEDKEEv 381
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71153048 541 -KAVLPTSKSSQMIT-----FTFANGGVaTMRTSGTEPKIKYYAElcAPpgnsDPEHLKKELDELVGAI 603
Cdd:TIGR03990 382 mEAVEEEFADAEIDTidgvrIDFEDGWV-LVRPSGTEPIVRIYAE--AK----TEERAEELLEEGRSLV 443
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
19-620 |
0e+00 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 798.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 19 MDARLDQETAQWLRWDQNPLTSESVKQLIAGGNKEELRKCFGARMEFGTAGLRAPMGAGISRMNDLTIIQTTQGFCRYLE 98
Cdd:PTZ00150 1 MMESLEAQVELWLKWDKDPETRKEIEELLASKDEEELKRRFLKRMEFGTAGLRGKMGAGFNCMNDLTVQQTAQGLCAYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 99 KQFS-DLKQRGVVISFDARAHpasggsSRRFARLAATAFITQGVPVYLFSDITPTPFVPYTVSHLKLCAGIMITASHNPK 177
Cdd:PTZ00150 81 ETFGqALKSRGVVIGYDGRYH------SRRFAEITASVFLSKGFKVYLFGQTVPTPFVPYAVRKLKCLAGVMVTASHNPK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 178 QDNGYKVYWDNGAQIISPHDRGISQAIEENLEPWPQAWEESlvdSSPLLHNPSASIGNDYFEDLK-KYCFHrtVNKESKV 256
Cdd:PTZ00150 155 EDNGYKVYWSNGAQIIPPHDKNISAKILSNLEPWSSSWEYL---TETLVEDPLAEVSDAYFATLKsEYNPA--CCDRSKV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 257 KFVHTSVHGVGHEFVQLAFKAFDLAPPEAVPQQKDPDPEFPTVKYPNPEEGKGVLTLSFALADKIKAKIVLANDPDADRL 336
Cdd:PTZ00150 230 KIVYTAMHGVGTRFVQKALHTVGLPNLLSVAQQAEPDPEFPTVTFPNPEEGKGALKLSMETAEAHGSTVVLANDPDADRL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 337 AVAEKQDSGeWRVFSGNELGALLGWWLFTSWKEKNQDQSNLkdtYMLSSTVSSKILRAIALKEGFHFEETLTGFKWMGNR 416
Cdd:PTZ00150 310 AVAEKLNNG-WKIFTGNELGALLAWWAMKRYRRQGIDKSKC---FFICTVVSSRMLKKMAEKEGFQYDETLTGFKWIGNK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 417 AQQLGD-QGKTVLFAFEEAIGYMCCPFVLDKDGVSAAVICAELASFLATKNLSLSQQLNAIYVEYGYHITTASYFICHDQ 495
Cdd:PTZ00150 386 AIELNAeNGLTTLFAYEEAIGFMLGTRVRDKDGVTAAAVVAEMALYLYERGKTLVEHLESLYKQYGYHFTNNSYYICYDP 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 496 GTIQNLFGNLRNyDGKnnYPKMCGKFEISAIRDLTTGYDDSQPDKKAVLPTSKSSQMITFTFANGGVATMRTSGTEPKIK 575
Cdd:PTZ00150 466 SRIVSIFNDIRN-NGS--YPTKLGGYPVTRIRDLTTGYDTATPDGKPLLPVSASTQMITFYFENGAIITIRGSGTEPKLK 542
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 71153048 576 YYAELCAppgnSDPEHLKKELDELVGAIEEHFFQPQKYNLQPKAE 620
Cdd:PTZ00150 543 WYAELSG----TKDEAVEKELAALVDEVVEQLMQPEKYGLVPRKE 583
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
62-600 |
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: 726.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 62 RMEFGTAGLRAPMGAGISRMNDLTIIQTTQGFCRYLEKQFSDLKQRGVVISFDARAHpasggsSRRFARLAATAFITQGV 141
Cdd:cd05799 1 RLEFGTAGLRGKMGAGTNRMNDYTVRQATQGLANYLKKKGPDAKNRGVVIGYDSRHN------SREFAELTAAVLAANGI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 142 PVYLFSDITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDRGISQAIEENLEPWPQAWEESLvd 221
Cdd:cd05799 75 KVYLFDDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAVLEPLDIKFEEAL-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 222 SSPLLHNPSASIGNDYFEDLKKYCFHRTVNKESKVKFVHTSVHGVGHEFVQLAFKAFDLAPPEAVPQQKDPDPEFPTVKY 301
Cdd:cd05799 153 DSGLIKYIGEEIDDAYLEAVKKLLVNPELNEGKDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVVEEQAEPDPDFPTVKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 302 PNPEEgKGVLTLSFALADKIKAKIVLANDPDADRLAVAEKQDSGEWRVFSGNELGALLGWWLFTSWKEKNQDqsnLKDTY 381
Cdd:cd05799 233 PNPEE-PGALDLAIELAKKVGADLILATDPDADRLGVAVKDKDGEWRLLTGNEIGALLADYLLEQRKEKGKL---PKNPV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 382 MLSSTVSSKILRAIALKEGFHFEETLTGFKWMGNRAQQLGDQGKTVLFAFEEAIGYMCCPFVLDKDGVSAAVICAELASF 461
Cdd:cd05799 309 IVKTIVSSELLRKIAKKYGVKVEETLTGFKWIGNKIEELESGGKKFLFGFEESIGYLVGPFVRDKDGISAAALLAEMAAY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 462 LATKNLSLSQQLNAIYVEYGYHITTASYFIC---HDQGTIQNLFGNLRNYDgknnypkmcgkfeisairdlttgyddsqp 538
Cdd:cd05799 389 LKAQGKTLLDRLDELYEKYGYYKEKTISITFegkEGPEKIKAIMDRLRNNP----------------------------- 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71153048 539 dkkavlptskssQMITFTFANGGVATMRTSGTEPKIKYYAELCAPpgnSDPEHLKKELDELV 600
Cdd:cd05799 440 ------------NVLTFYLEDGSRVTVRPSGTEPKIKFYIEVVGK---KTLEEAEKKLDALK 486
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
166-600 |
1.00e-103 |
|
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: 1.00e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 166 AGIMITASHNPKQDNGYKVYWDNGAQIISPHDRGISQAIEENLEPWPQAWEESlvdssplLHNPSASIGNDYFEDLKKYC 245
Cdd:cd03084 31 GGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSAVAYELG-------GSVKAVDILQRYFEALKKLF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 246 FHRTVNkESKVKFVHTSVHGVGHEFVQLAFKAFDlapPEAVPQQKDPDPEFPtVKYPNPEEGKGVLTLSFALaDKIKAKI 325
Cdd:cd03084 104 DVAALS-NKKFKVVVDSVNGVGGPIAPQLLEKLG---AEVIPLNCEPDGNFG-NINPDPGSETNLKQLLAVV-KAEKADF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 326 VLANDPDADRLAVAEKQdsgeWRVFSGNELGALLGWWLFTSWKeknqdqsnlKDTYMLSSTVSSKILRAIALKEGFHFEE 405
Cdd:cd03084 178 GVAFDGDADRLIVVDEN----GGFLDGDELLALLAVELFLTFN---------PRGGVVKTVVSSGALDKVAKKLGIKVIR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 406 TLTGFKWMGNRAQQlgdqgKTVLFAFEEAIGYMCCPFVLDKDGVSAAVICAELASFLatkNLSLSQQLNAIYVEYGYHIT 485
Cdd:cd03084 245 TKTGFKWVGEAMQE-----GDVVLGGEESGGVIFPEFHPGRDGISAALLLLEILANL---GKSLSELFSELPRYYYIRLK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 486 TAsyfichdqgtiqnlfgnlrnydgknnypkmcgkfeisairdlttgyddsqpdkkavlptskssqmitftfangGVATM 565
Cdd:cd03084 317 VR-------------------------------------------------------------------------GWVLV 323
|
410 420 430
....*....|....*....|....*....|....*
gi 71153048 566 RTSGTEPKIKYYAELCAPpgnSDPEHLKKELDELV 600
Cdd:cd03084 324 RASGTEPAIRIYAEADTQ---EDVEQIKKEARELV 355
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
65-607 |
1.53e-89 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 285.17 E-value: 1.53e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 65 FGTAGLRAPMGAGisrMNDLTIIQTTQGFCRYLEKQfsdlKQRGVVISFDARAhpasggSSRRFARLAATAFITQGVPVY 144
Cdd:COG1109 7 FGTDGIRGIVGEE---LTPEFVLKLGRAFGTYLKEK----GGPKVVVGRDTRL------SSPMLARALAAGLASAGIDVY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 145 LFsDITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDRGISQAIEENLEPWPQAWEESLVdssp 224
Cdd:COG1109 74 DL-GLVPTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKEDFRRAEAEEIGKV---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 225 llhNPSASIGNDYFEDLKKYCFHRTvnKESKVKFVHTSVHGVGHEFVQLAFKAfdlAPPEAVPQQKDPDPEFPTVkYPNP 304
Cdd:COG1109 149 ---TRIEDVLEAYIEALKSLVDEAL--RLRGLKVVVDCGNGAAGGVAPRLLRE---LGAEVIVLNAEPDGNFPNH-NPNP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 305 EEgkGVLTLSFALADKIKAKIVLANDPDADRLAVAEKQdsGewRVFSGNELGALLGWWLftswKEKNqdqsnlKDTYMLS 384
Cdd:COG1109 220 EP--ENLEDLIEAVKETGADLGIAFDGDADRLGVVDEK--G--RFLDGDQLLALLARYL----LEKG------PGGTVVV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 385 STVSSKILRAIALKEGFHFEETLTGFKWMGNRAQQLGdqgktVLFAFEEAIGYMCCPFVLDKDGVSAAVICAELasfLAT 464
Cdd:COG1109 284 TVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKMRETG-----AVLGGEESGGIIFPDFVPTDDGILAALLLLEL---LAK 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 465 KNLSLSQQLNaiyvEYGYHITTASYFICHDQGTIQNLFGNLRNydgknnypkmcgkfEISAIRDLTTgyddsqpdkkavl 544
Cdd:COG1109 356 QGKSLSELLA----ELPRYPQPEINVRVPDEEKIGAVMEKLRE--------------AVEDKEELDT------------- 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71153048 545 ptsksSQMITFTFANGGVATMRTSGTEPKIKYYAElcAPpgnsDPEHLKKELDELVGAIEEHF 607
Cdd:COG1109 405 -----IDGVKVDLEDGGWVLVRPSGTEPLLRVYAE--AK----DEEEAEELLAELAELVEEAL 456
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
63-600 |
3.27e-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: 3.27e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 63 MEFGTAGLRAPMGAGISRMNdLTIIqtTQGFCRYLEKQFsdLKQRGVVISFDARAHpasggsSRRFARLAATAFITQGVP 142
Cdd:cd05800 1 IKFGTDGWRGIIAEDFTFEN-VRRV--AQAIADYLKEEG--GGGRGVVVGYDTRFL------SEEFARAVAEVLAANGID 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 143 VYLFSDITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAqiisPHDRGISQAIEENLEPWPQAWEESLVDS 222
Cdd:cd05800 70 VYLSDRPVPTPAVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGG----SALPEITAAIEARLASGEPPGLEARAEG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 223 SPLLHNPSasigNDYFEDLKKYcfhrtVN----KESKVKFVHTSVHGVGHEFVQLAFKAFDLappEAVPQQKDPDPEFPT 298
Cdd:cd05800 146 LIETIDPK----PDYLEALRSL-----VDleaiREAGLKVVVDPMYGAGAGYLEELLRGAGV---DVEEIRAERDPLFGG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 299 VKyPNPEEGkgvlTLSfALADKIK---AKIVLANDPDADRLAVAEKQDsgewRVFSGNELGALLGWWLftsWKEKNQDQS 375
Cdd:cd05800 214 IP-PEPIEK----NLG-ELAEAVKeggADLGLATDGDADRIGAVDEKG----NFLDPNQILALLLDYL---LENKGLRGP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 376 NLKdtymlssTVS-SKILRAIALKEGFHFEETLTGFKWMGNRAQQlgdqgKTVLFAFEEAIGYMCCPFVLDKDGVSAAVI 454
Cdd:cd05800 281 VVK-------TVStTHLIDRIAEKHGLPVYETPVGFKYIAEKMLE-----EDVLIGGEESGGLGIRGHIPERDGILAGLL 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 455 CAELasfLATKNLSLSQQLNAIYVEYGYHittasyfichdqgtiqnlfgnlrnYDGKNNYpkmcgKFEISAIRDLTTGYD 534
Cdd:cd05800 349 LLEA---VAKTGKPLSELVAELEEEYGPS------------------------YYDRIDL-----RLTPAQKEAILEKLK 396
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71153048 535 DSQPDKKAVLPTSKSSQM--ITFTFANGGVATMRTSGTEPKIKYYAElcappgNSDPEHLKKELDELV 600
Cdd:cd05800 397 NEPPLSIAGGKVDEVNTIdgVKLVLEDGSWLLIRPSGTEPLLRIYAE------APSPEKVEALLDAGK 458
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
62-211 |
2.73e-40 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 143.52 E-value: 2.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 62 RMEFGTAGLRAPMGAGIsrMNDLTIIQTTQGFCRYLEKQfsdLKQRGVVISFDARAhpasggSSRRFARLAATAFITQGV 141
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGE--LTPEFALKLGQAIASYLRAQ---GGGGKVVVGRDTRY------SSRELARALAAGLASNGV 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 142 PVYLFsDITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIISPHDRGISQAIEENLEPW 211
Cdd:pfam02878 70 EVILL-GLLPTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKEDFYR 138
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
236-341 |
2.22e-22 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 91.97 E-value: 2.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 236 DYFEDLKKYCFhRTVNKESKVKFVHTSVHGVGHEFVQLAFKAFDLAPpeaVPQQKDPDPEFPTvKYPNPEEgKGVLTLSF 315
Cdd:pfam02879 1 AYIDHLLELVD-SEALKKRGLKVVYDPLHGVGGGYLPELLKRLGCDV---VEENCEPDPDFPT-RAPNPEE-PEALALLI 74
|
90 100
....*....|....*....|....*.
gi 71153048 316 ALADKIKAKIVLANDPDADRLAVAEK 341
Cdd:pfam02879 75 ELVKSVGADLGIATDGDADRLGVVDE 100
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
65-603 |
1.43e-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: 1.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 65 FGTAGLRAPMGAGisrMNDLTIIQTTQGFCRYLEKqfsdlkqRGVVISFDARAhpasggSSRRFARLAATAFITQGVPVY 144
Cdd:TIGR03990 4 FGTSGIRGIVGEE---LTPELALKVGKAFGTYLRG-------GKVVVGRDTRT------SGPMLENAVIAGLLSTGCDVV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 145 LFsDITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVyWDNGAQIISPHD-RGISQAIEENLEPWPqAWEESLVDSS 223
Cdd:TIGR03990 68 DL-GIAPTPTLQYAVRELGADGGIMITASHNPPEYNGIKL-LNSDGTELSREQeEEIEEIAESGDFERA-DWDEIGTVTS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 224 PllhnpsASIGNDYFEDLKKyCFHRTVNKESKVKFVHTSVHGVGHEFVQLAFKAFDLappEAVPQQKDPDPEFPtvkYPN 303
Cdd:TIGR03990 145 D------EDAIDDYIEAILD-KVDVEAIRKKGFKVVVDCGNGAGSLTTPYLLRELGC---KVITLNCQPDGTFP---GRN 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 304 PEEGKGVLTLSFALADKIKAKIVLANDPDADRLA-VAEKqdsGewRVFSGNELGALLGWWLFtswkeknqdqSNLKDTym 382
Cdd:TIGR03990 212 PEPTPENLKDLSALVKATGADLGIAHDGDADRLVfIDEK---G--RFIGGDYTLALFAKYLL----------EHGGGK-- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 383 LSSTVS-SKILRAIALKEGFHFEETLTGFKWMGNRAQQLGdqgktVLFAFEEAIGYMCCPFVLDKDGVSAAvicAELASF 461
Cdd:TIGR03990 275 VVTNVSsSRAVEDVAERHGGEVIRTKVGEVNVAEKMKEEG-----AVFGGEGNGGWIFPDHHYCRDGLMAA---ALFLEL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 462 LATKNLSLSQQLNAIyveygyhittASYFIChdqgtiqnlfgnlrnydgKNNYPkmcgkfeisairdlttgYDDSQPDK- 540
Cdd:TIGR03990 347 LAEEGKPLSELLAEL----------PKYPMS------------------KEKVE-----------------LPDEDKEEv 381
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71153048 541 -KAVLPTSKSSQMIT-----FTFANGGVaTMRTSGTEPKIKYYAElcAPpgnsDPEHLKKELDELVGAI 603
Cdd:TIGR03990 382 mEAVEEEFADAEIDTidgvrIDFEDGWV-LVRPSGTEPIVRIYAE--AK----TEERAEELLEEGRSLV 443
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
95-359 |
3.81e-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: 3.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 95 RYLEKQFSDLKQRGVVISFDARAhpasggSSRRFARLAATAFITQGVPVYlfsDI--TPTPFVPYTVSHLKLCAGIMITA 172
Cdd:cd03089 25 RAFGSWLLEKGAKKVVVGRDGRL------SSPELAAALIEGLLAAGCDVI---DIglVPTPVLYFATFHLDADGGVMITA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 173 SHNPKQDNGYKVYWDNGAqiISPHD-RGISQAIEENLEPWPQAwEESLVdsspllhnpSASIGNDYFEDLKKYCFHRtvn 251
Cdd:cd03089 96 SHNPPEYNGFKIVIGGGP--LSGEDiQALRERAEKGDFAAATG-RGSVE---------KVDILPDYIDRLLSDIKLG--- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 252 kESKVKFVHTSVHGVGHEFVQLAFKAFDLappEAVPQQKDPDPEFPTvKYPNPEEGKgvltlsfALADKIKAkiVLAN-- 329
Cdd:cd03089 161 -KRPLKVVVDAGNGAAGPIAPQLLEALGC---EVIPLFCEPDGTFPN-HHPDPTDPE-------NLEDLIAA--VKENga 226
|
250 260 270
....*....|....*....|....*....|....*.
gi 71153048 330 ------DPDADRLAVAEKqdSGewRVFSGNELGALL 359
Cdd:cd03089 227 dlgiafDGDGDRLGVVDE--KG--EIIWGDRLLALF 258
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
65-603 |
1.05e-17 |
|
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100089 Cd Length: 439 Bit Score: 86.09 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 65 FGTAGLRAPMGagisrmNDLT---IIQTTQGFCRYLEKqfsdlkqRGVVISFDARAhpasggSSRRFARLAATAFITQGV 141
Cdd:cd03087 2 FGTSGIRGVVG------EELTpelALKVGKALGTYLGG-------GTVVVGRDTRT------SGPMLKNAVIAGLLSAGC 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 142 PVYLFsDITPTPFVPYTVSHLKLcAGIMITASHNPKQDNGYKVYWDNGAQIISPHDRGISQAIEENLEPwPQAWEEslVD 221
Cdd:cd03087 63 DVIDI-GIVPTPALQYAVRKLGD-AGVMITASHNPPEYNGIKLVNPDGTEFSREQEEEIEEIIFSERFR-RVAWDE--VG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 222 SSpllhNPSASIGNDYFEDLKKYCfhrTVNKESKVKFVHTSVHGVGHefvqlafkafdLAPPEA--------VPQQKDPD 293
Cdd:cd03087 138 SV----RREDSAIDEYIEAILDKV---DIDGGKGLKVVVDCGNGAGS-----------LTTPYLlrelgckvITLNANPD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 294 PEFPTvkyPNPEEGKGVLTLSFALADKIKAKIVLANDPDADRL-AVAEKqdsGewRVFSGNELGALLGWWLFTSWKEKnq 372
Cdd:cd03087 200 GFFPG---RPPEPTPENLSELMELVRATGADLGIAHDGDADRAvFVDEK---G--RFIDGDKLLALLAKYLLEEGGGK-- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 373 dqsnlkdtymLSSTVS-SKILRAIALKEGFHFEETltgfkwmgnraqQLGD-------QGKTVLFAFEEAIGYMCCPFVL 444
Cdd:cd03087 270 ----------VVTPVDaSMLVEDVVEEAGGEVIRT------------PVGDvhvaeemIENGAVFGGEPNGGWIFPDHQL 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 445 DKDGV-SAAVICAELAsflatKNLSLSQQLNAIYVeygYHITTASYFICHDQgtiqnlfgnlrnydgknnypkmcgKFEI 523
Cdd:cd03087 328 CRDGImTAALLLELLA-----EEKPLSELLDELPK---YPLLREKVECPDEK------------------------KEEV 375
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 524 -SAIRDLTTGYDDSqpdkkaVLPTSKssqmITFTFANGGVaTMRTSGTEPKIKYYAElcappgNSDPEHLKKELDELVGA 602
Cdd:cd03087 376 mEAVEEELSDADED------VDTIDG----VRIEYEDGWV-LIRPSGTEPKIRITAE------AKTEERAKELLEEGRSK 438
|
.
gi 71153048 603 I 603
Cdd:cd03087 439 V 439
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
352-480 |
1.83e-15 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 72.87 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 352 GNELGALLGWWLFTSWKEKnqdqsnlKDTYMLSSTVSSKILRAIALKEGFHFEETLTGFKWMGNRAQQLGdqgktVLFAF 431
Cdd:pfam02880 2 GDQILALLAKYLLEQGKLP-------PGAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEG-----ALFGG 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 71153048 432 EEAIGYMCCPFVLDKDGVSAAVICAELasfLATKNLSLSQQLNAIYVEY 480
Cdd:pfam02880 70 EESGHIIFLDHATTKDGILAALLVLEI---LARTGKSLSELLEELPEKY 115
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
69-338 |
3.46e-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: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 69 GLRAPMGAGISRMNdltIIQTTQGFCRYlekQFSDLKQRGVVISFDARAhpasggSSRRFARLAATAFITQGVPVyLFSD 148
Cdd:cd05803 6 GIRGIVGEGLTPEV---ITRYVAAFATW---QPERTKGGKIVVGRDGRP------SGPMLEKIVIGALLACGCDV-IDLG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 149 ITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYW--------DNGAQIISPHDRGisqaiEENLEPWPQAWE-ESL 219
Cdd:cd05803 73 IAPTPTVQVLVRQSQASGGIIITASHNPPQWNGLKFIGpdgefltpDEGEEVLSCAEAG-----SAQKAGYDQLGEvTFS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 220 VDSSPllhnpsASIGNdyfeDLKKYCFHRTVNKESKVKFVHTSVHGVGHEFVQLAFKAFDLappEAVPQQKDPDPEFPTV 299
Cdd:cd05803 148 EDAIA------EHIDK----VLALVDVDVIKIRERNFKVAVDSVNGAGGLLIPRLLEKLGC---EVIVLNCEPTGLFPHT 214
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 71153048 300 KYPNPEEgkgvLT-LSFALADKiKAKIVLANDPDADRLAV 338
Cdd:cd05803 215 PEPLPEN----LTqLCAAVKES-GADVGFAVDPDADRLAL 249
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
140-242 |
1.69e-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: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 140 GVPVYLFsDITPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQiisphdrgISQAIEENLepwpqaweESL 219
Cdd:cd05802 65 GVDVLLL-GVIPTPAVAYLTRKLRADAGVVISASHNPFEDNGIKFFSSDGYK--------LPDEVEEEI--------EAL 127
|
90 100 110
....*....|....*....|....*....|..
gi 71153048 220 VDSSPLLHNPSASIG---------NDYFEDLK 242
Cdd:cd05802 128 IDKELELPPTGEKIGrvyriddarGRYIEFLK 159
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
65-598 |
7.88e-11 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 64.77 E-value: 7.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 65 FGTAGLRapmgaGISR---MNDLTIIQTTQGFCRYLEKQFSDLKqrgVVISFDARAHpasggsSRRfarlaatAFIT--- 138
Cdd:PRK07564 40 FGTSGHR-----GSSLqpsFNENHILAIFQAICEYRGKQGITGP---LFVGGDTHAL------SEP-------AIQSale 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 139 ----QGVPVYLFSD--ITPTPfvpyTVSHLKLCA---------GIMITASHNPKQDNGYKVYWDNGAqiisPHDRGISQA 203
Cdd:PRK07564 99 vlaaNGVGVVIVGRggYTPTP----AVSHAILKYngrgggladGIVITPSHNPPEDGGIKYNPPNGG----PADTDVTDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 204 IEE--------NLE-----PWPQAWEESLVDSspllHNPSAsignDYFEDLKKyCFHRTVNKESKVKFVHTSVHGVGHEF 270
Cdd:PRK07564 171 IEAranellayGLKgvkriPLDRALASMTVEV----IDPVA----DYVEDLEN-VFDFDAIRKAGLRLGVDPLGGATGPY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 271 VQLAFKAFDL------APPEAV----PQQKD----PDPefptvkypnpeegkgvlTLSFALADKIKAK----IVLANDPD 332
Cdd:PRK07564 242 WKAIAERYGLdltvvnAPVDPTfnfmPLDDDgkirMDC-----------------SSPYAMAGLLALKdafdLAFANDPD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 333 ADR---------------LAVAekqdsgewrvfsgnelgallGWWLFT---SWKeknqdqsnlKDTYMLSSTVSSKILRA 394
Cdd:PRK07564 305 GDRhgivtpgglmnpnhyLAVA--------------------IAYLFHhrpGWR---------AGAGVGKTLVSSAMIDR 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 395 IALKEGFHFEETLTGFKWMGNraqqLGDQGKtVLFAFEEAIG-----YMCCPFVLDKDGVSAAVICAELasfLATKNLSL 469
Cdd:PRK07564 356 VAAKLGRKLYEVPVGFKWFVN----GLDDGS-LGFGGEESAGasflrRDGSVWTTDKDGLIAVLLAAEI---LAVTGKSP 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 470 SQQLNAIYVEYGyhittASYFICHDqgtiqnlfgnlrnydgknnYPkmCGKFEISAIRDLTTgyddSQPDKK-------- 541
Cdd:PRK07564 428 SEIYRELWARFG-----RPYYSRHD-------------------AP--ATPEQKAALRKLSP----ELVGATelagdpid 477
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71153048 542 AVLPTSKSSQM----ITFTFANGGVAtMRTSGTEPKIKYYAElcappgnS--DPEHLKKELDE 598
Cdd:PRK07564 478 ASLTEAPGNGAaiggLKVVTENGWFA-ARPSGTETTYKIYAE-------SfeGDEHLHQIQKE 532
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
62-598 |
1.59e-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: 63.81 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 62 RMEFGTAGLRAPMGAGisRMNDLTIIQTTQGFCRYLEKQFSDlkqrGVV-ISFDARAhpasggssrrfarLAATAFIT-- 138
Cdd:cd05801 20 RVAFGTSGHRGSSLKG--SFNEAHILAISQAICDYRKSQGIT----GPLfLGKDTHA-------------LSEPAFISal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 139 -----QGVPVYLFSD--ITPTPFVPYTV------SHLKLCAGIMITASHNPKQDNGYKVYWDNGAqiisPHDRGISQAIE 205
Cdd:cd05801 81 evlaaNGVEVIIQQNdgYTPTPVISHAIltynrgRTEGLADGIVITPSHNPPEDGGFKYNPPHGG----PADTDITRWIE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 206 E--------NLE-----PWPQAWeeslvdSSPLLHNpsASIGNDYFEDLKKyCFHRTVNKESKVKFvhtSVHGVG----H 268
Cdd:cd05801 157 KranallanGLKgvkriPLEAAL------ASGYTHR--HDFVTPYVADLGN-VIDMDAIRKSGLRL---GVDPLGgasvP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 269 EFVQLAFK-AFDLappEAVPQQKDPDPEFPTVKYpnpeEGKGVLTLS--FALADKIKAK----IVLANDPDADRLAVAEK 341
Cdd:cd05801 225 YWQPIAEKyGLNL---TVVNPKVDPTFRFMTLDH----DGKIRMDCSspYAMAGLLKLKdkfdLAFANDPDADRHGIVTP 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 342 QdsgeWRVFSGNELGALLGWWLFTSWKEKNQDQSNLKdTYmlsstVSSKILRAIALKEGFHFEETLTGFKWMgnrAQQLG 421
Cdd:cd05801 298 S----AGLMNPNHYLSVAIDYLFTHRPLWNKSAGVGK-TL-----VSSSMIDRVAAALGRKLYEVPVGFKWF---VDGLL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 422 DQgkTVLFAFEEAIG-----YMCCPFVLDKDGVSAAVICAELASfLATKNLS-LSQQLNAIYVEYGYHITTASyfICHDQ 495
Cdd:cd05801 365 DG--SLGFGGEESAGasflrRDGTVWTTDKDGIIMCLLAAEILA-VTGKDPGqLYQELTERFGEPYYARIDAP--ATPEQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 496 GTIqnlFGNLRNYDGKnnyPKMCGKFEISAIrdLTTGyddsqPDKKAVLPTSKssqmitFTFANGGVATmRTSGTEPKIK 575
Cdd:cd05801 440 KAR---LKKLSPEQVT---ATELAGDPILAK--LTRA-----PGNGASIGGLK------VTTANGWFAA-RPSGTEDVYK 499
|
570 580
....*....|....*....|....*
gi 71153048 576 YYAElcappgnS--DPEHLKKELDE 598
Cdd:cd05801 500 IYAE-------SflSEEHLKKIQKE 517
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
65-377 |
2.01e-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: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 65 FGTAGLRAPmgAGISRMNDLTIIQTTQGFCRYLEKQFSdlKQRGVVISFDARAhpasggSSRRFARLAATAFITQGVPVY 144
Cdd:TIGR01455 1 FGTDGVRGR--AGQEPLTAELALLLGAAAGRVLRQGRD--TAPRVVIGKDTRL------SGYMLENALAAGLNSAGVDVL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 145 LFSDItPTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIisphDRGISQAIEENLEpwpQAWEESLVDSSP 224
Cdd:TIGR01455 71 LLGPL-PTPAVAYLTRTLRADAGVMISASHNPYEDNGIKFFGPGGFKL----DDATEAAIEALLD---EADPLPRPESEG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 225 LLHNPSASIGNDYFEDLKKYCFHRTVNKeSKVKFVHTSVHGVGhefVQLAFKAFDLAPPEAVPQQKDPDPEfptvkypNP 304
Cdd:TIGR01455 143 LGRVKRYPDAVGRYIEFLKSTLPRGLTL-SGLKVVLDCANGAA---YKVAPHVFRELGAEVIAIGVEPDGL-------NI 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71153048 305 EEGKGVLTLSfALADKIK---AKIVLANDPDADR-LAVAEKQDsgewrVFSGNELGALLGwwlfTSWKEKNQDQSNL 377
Cdd:TIGR01455 212 NDGCGSTHLD-ALQKAVRehgADLGIAFDGDADRvLAVDANGR-----IVDGDQILYIIA----RALKESGELAGNT 278
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
151-218 |
1.23e-06 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 51.29 E-value: 1.23e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71153048 151 PTPFVPYTVSHLKLCAGIMITASHNPKQDNGYKVYWDNGAQIisPHDrgISQAIEENLEPwPQAWEES 218
Cdd:PRK10887 77 PTPAVAYLTRTLRAEAGIVISASHNPYYDNGIKFFSADGTKL--PDE--VELAIEAELDK-PLTCVES 139
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
65-219 |
3.44e-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: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 65 FGTAGLRapmgaG-ISRMNDLTIIQTTQGFCRYLEKQFsdlKQRGVVISFDARAhpasggSSRRFARLAATAFITQGV-P 142
Cdd:cd03088 2 FGTSGLR-----GlVTDLTDEVCYAYTRAFLQHLESKF---PGDTVAVGRDLRP------SSPRIAAACAAALRDAGFrV 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71153048 143 VYLfsDITPTPFVPYTVSHLKlCAGIMITASHNPKQDNGYKVYWDNGaQIISPHDRGISQAIEENLEPWPQAWEESL 219
Cdd:cd03088 68 VDC--GAVPTPALALYAMKRG-APAIMVTGSHIPADRNGLKFYRPDG-EITKADEAAILAALVELPEALFDPAGALL 140
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
167-209 |
2.74e-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: 2.74e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 71153048 167 GIMITASHNPKQDNGYKvywdngaqIISPHDRGISQAIEENLE 209
Cdd:cd03086 38 GVMITASHNPVEDNGVK--------IVDPDGEMLEESWEPYAT 72
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
156-209 |
5.91e-05 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 46.19 E-value: 5.91e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 71153048 156 PYTVSHLKLCAGIMITASHNPKQDNGYKvywdngaqIISPHDRGISQAIEENLE 209
Cdd:PTZ00302 67 GKRAKRGNKSVGVMITASHNPIQDNGVK--------IIDPDGGMLEESWEKICT 112
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
88-183 |
7.79e-04 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 42.28 E-value: 7.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71153048 88 QTTQGFCRYLEKQFSDL----KQRGVVISFDARahPASGGSSRRFARlAATAfitQGVPVYLFSdITPTPFVPYTVSHLK 163
Cdd:PRK09542 13 QIDEDLVRDVGAAFARLmraeGATTVVIGHDMR--DSSPELAAAFAE-GVTA---QGLDVVRIG-LASTDQLYFASGLLD 85
|
90 100
....*....|....*....|
gi 71153048 164 lCAGIMITASHNPKQDNGYK 183
Cdd:PRK09542 86 -CPGAMFTASHNPAAYNGIK 104
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
550-604 |
1.07e-03 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 38.02 E-value: 1.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 71153048 550 SQMITFTFANGGVATMRTSGTEPKIKYYAElcAPpgnsDPEHLKKELDELVGAIE 604
Cdd:pfam00408 23 ADAEKILGEDGRRLDVRPSGTEPVLRVMVE--GD----SDEELARLADEIADLLE 71
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
167-184 |
2.76e-03 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 40.78 E-value: 2.76e-03
|
| |
