|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
24-620 |
0e+00 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 752.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 24 QLDTAIGQWLRWDKNPKTKEQIENLLRNGMNKELRDRLCCRMTFGTAGLRSAMGAGFCYINDLTVIQSTQGMYKYLERCF 103
Cdd:PTZ00150 4 SLEAQVELWLKWDKDPETRKEIEELLASKDEEELKRRFLKRMEFGTAGLRGKMGAGFNCMNDLTVQQTAQGLCAYVIETF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 104 S-DFKQRGFVVGYDTRGQvtsscsSQRLAKLTAAVLLAKDIPVYLFSRYVPTPFVPYAVQELKAVAGVMITASHNRKEDN 182
Cdd:PTZ00150 84 GqALKSRGVVIGYDGRYH------SRRFAEITASVFLSKGFKVYLFGQTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 183 GYKVYWETGAQITSPHDKEILKCIEECVEPWNDSWNDNlvdTSPLKKDPLQDICKKYMEDLKKI-CFYRDLNSKttLKFV 261
Cdd:PTZ00150 158 GYKVYWSNGAQIIPPHDKNISAKILSNLEPWSSSWEYL---TETLVEDPLAEVSDAYFATLKSEyNPACCDRSK--VKIV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 262 HTSFHGVGHDYVQLAFQVFGFKPPIPVPEQKDPDPDFSTVKCPNPEEGESVLELSLRLAEKENARIVLATDPDADRLAVA 341
Cdd:PTZ00150 233 YTAMHGVGTRFVQKALHTVGLPNLLSVAQQAEPDPEFPTVTFPNPEEGKGALKLSMETAEAHGSTVVLANDPDADRLAVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 342 ELQeNGRWKVFTGNELAALFGWWMfdcWKKN-KPNADVKNVYMLATTVSSKILKAIALKEGFHFEETLPGFKWIGSRIKD 420
Cdd:PTZ00150 313 EKL-NNGWKIFTGNELGALLAWWA---MKRYrRQGIDKSKCFFICTVVSSRMLKKMAEKEGFQYDETLTGFKWIGNKAIE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 421 LLG-NGKEVLFAFEESIGFLCGTSVLDKDGVSAAAVVAEMASFLDTRKVTLMEQLTKVYEIYGYHMSKTSYFLCYDPPTI 499
Cdd:PTZ00150 389 LNAeNGLTTLFAYEEAIGFMLGTRVRDKDGVTAAAVVAEMALYLYERGKTLVEHLESLYKQYGYHFTNNSYYICYDPSRI 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 500 KTIFERIRNFESpkeYPKFCGAFAILHVRDITTGYDSSQPNKKSVLPVSKNSQMITFTFQNGCVATLRTSGTEPKIKYYA 579
Cdd:PTZ00150 469 VSIFNDIRNNGS---YPTKLGGYPVTRIRDLTTGYDTATPDGKPLLPVSASTQMITFYFENGAIITIRGSGTEPKLKWYA 545
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 26333105 580 EMCASPGQSdttfLEEELKKLIDALIENFLEPSKNALVWRS 620
Cdd:PTZ00150 546 ELSGTKDEA----VEKELAALVDEVVEQLMQPEKYGLVPRK 582
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
64-606 |
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: 681.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 64 RMTFGTAGLRSAMGAGFCYINDLTVIQSTQGMYKYLERCFSDFKQRGFVVGYDTRGqvtsscSSQRLAKLTAAVLLAKDI 143
Cdd:cd05799 1 RLEFGTAGLRGKMGAGTNRMNDYTVRQATQGLANYLKKKGPDAKNRGVVIGYDSRH------NSREFAELTAAVLAANGI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 144 PVYLFSRYVPTPFVPYAVQELKAVAGVMITASHNRKEDNGYKVYWETGAQITSPHDKEILKCIEECVEPWNDSWNDNLvd 223
Cdd:cd05799 75 KVYLFDDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAVLEPLDIKFEEAL-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 224 TSPLKKDPLQDICKKYMEDLKKICFYRDLNSKTTLKFVHTSFHGVGHDYVQLAFQVFGFKPPIPVPEQKDPDPDFSTVKC 303
Cdd:cd05799 153 DSGLIKYIGEEIDDAYLEAVKKLLVNPELNEGKDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVVEEQAEPDPDFPTVKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 304 PNPEEgESVLELSLRLAEKENARIVLATDPDADRLAVAELQENGRWKVFTGNELAALFGWWMFDCWKKNkpNADVKNVYM 383
Cdd:cd05799 233 PNPEE-PGALDLAIELAKKVGADLILATDPDADRLGVAVKDKDGEWRLLTGNEIGALLADYLLEQRKEK--GKLPKNPVI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 384 LATTVSSKILKAIALKEGFHFEETLPGFKWIGSRIKDLLGNGKEVLFAFEESIGFLCGTSVLDKDGVSAAAVVAEMASFL 463
Cdd:cd05799 310 VKTIVSSELLRKIAKKYGVKVEETLTGFKWIGNKIEELESGGKKFLFGFEESIGYLVGPFVRDKDGISAAALLAEMAAYL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 464 DTRKVTLMEQLTKVYEIYGYHMSKTSYFLC---YDPPTIKTIFERIRNfespkeypkfcgafailhvrdittgydssqpn 540
Cdd:cd05799 390 KAQGKTLLDRLDELYEKYGYYKEKTISITFegkEGPEKIKAIMDRLRN-------------------------------- 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26333105 541 kksvlpvskNSQMITFTFQNGCVATLRTSGTEPKIKYYAEMCaspGQSDttflEEELKKLIDALIE 606
Cdd:cd05799 438 ---------NPNVLTFYLEDGSRVTVRPSGTEPKIKFYIEVV---GKKT----LEEAEKKLDALKK 487
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
64-605 |
2.04e-86 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 276.70 E-value: 2.04e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 64 RMTFGTAGLRSAMGAgfcYINDLTVIQSTQGMYKYLERCfsdfKQRGFVVGYDTRgqvtssCSSQRLAKLTAAVLLAKDI 143
Cdd:COG1109 4 KKLFGTDGIRGIVGE---ELTPEFVLKLGRAFGTYLKEK----GGPKVVVGRDTR------LSSPMLARALAAGLASAGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 144 PVYLFsRYVPTPFVPYAVQELKAVAGVMITASHNRKEDNGYKVYWETGAQITSPHDKEILKCIEecvepwndswNDNLVD 223
Cdd:COG1109 71 DVYDL-GLVPTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIE----------KEDFRR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 224 TSPLKKDPL---QDICKKYMEDLKKicFYRDLNSKTTLKFVHTSFHGVGHDYVQLAFQVFGFKpPIPVPEQkdPDPDFST 300
Cdd:COG1109 140 AEAEEIGKVtriEDVLEAYIEALKS--LVDEALRLRGLKVVVDCGNGAAGGVAPRLLRELGAE-VIVLNAE--PDGNFPN 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 301 VKcPNPEEGesVLELSLRLAEKENARIVLATDPDADRLAVAElqENGRwkVFTGNELAALFGWWMfdcwKKNKPNADVkn 380
Cdd:COG1109 215 HN-PNPEPE--NLEDLIEAVKETGADLGIAFDGDADRLGVVD--EKGR--FLDGDQLLALLARYL----LEKGPGGTV-- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 381 vymLATTVSSKILKAIALKEGFHFEETLPGFKWIGSRIKDLlgngkEVLFAFEESIGFLCGTSVLDKDGVSAAAVVAEMA 460
Cdd:COG1109 282 ---VVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKMRET-----GAVLGGEESGGIIFPDFVPTDDGILAALLLLELL 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 461 SFLDTRKVTLMEQLTKvyeiygYHMSKTSyFLCYDPPTIKTIFERIRNfespkeypkfcgafAILHVRDITTgydssqpn 540
Cdd:COG1109 354 AKQGKSLSELLAELPR------YPQPEIN-VRVPDEEKIGAVMEKLRE--------------AVEDKEELDT-------- 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26333105 541 kksvlpvsknSQMITFTFQNGCVATLRTSGTEPKIKYYAEmcaSPGQSDTTFLEEELKKLIDALI 605
Cdd:COG1109 405 ----------IDGVKVDLEDGGWVLVRPSGTEPLLRVYAE---AKDEEEAEELLAELAELVEEAL 456
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
64-208 |
4.06e-38 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 137.36 E-value: 4.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 64 RMTFGTAGLRSAMGAGFcyINDLTVIQSTQGMYKYLErcfSDFKQRGFVVGYDTRGqvtsscSSQRLAKLTAAVLLAKDI 143
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGE--LTPEFALKLGQAIASYLR---AQGGGGKVVVGRDTRY------SSRELARALAAGLASNGV 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26333105 144 PVYLFSrYVPTPFVPYAVQELKAVAGVMITASHNRKEDNGYKVYWETGAQITSPHDKEILKCIEE 208
Cdd:pfam02878 70 EVILLG-LLPTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEK 133
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
112-601 |
1.76e-27 |
|
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been characterized as the archaeal protein responsible for the second step of UDP-GlcNAc biosynthesis. This GlmM protein catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. The first-characterized bacterial GlmM protein is modeled by TIGR01455. These two families are members of the larger phosphoglucomutase/phosphomannomutase family (characterized by three domains: pfam02878, pfam02879 and pfam02880), but are not nearest neighbors to each other. This model also includes a number of sequences from non-archaea in the Bacteroides, Chlorobi, Chloroflexi, Planctomycetes and Spirochaetes lineages. Evidence supporting their inclusion in this equivalog as having the same activity comes from genomic context and phylogenetic profiling. A large number of these organisms are known to produce exo-polysaccharide and yet only appeared to contain the GlmS enzyme of the GlmSMU pathway for UDP-GlcNAc biosynthesis (GenProp0750). In some organisms including Leptospira, this archaeal GlmM is found adjacent to the GlmS as well as a putative GlmU non-orthologous homolog. Phylogenetic profiling of the GlmS-only pattern using PPP identifies members of this archaeal GlmM family as the highest-scoring result. [Central intermediary metabolism, Amino sugars]
Pssm-ID: 274906 Cd Length: 443 Bit Score: 115.69 E-value: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 112 VVGYDTRgqvtssCSSQRLAKLTAAVLLAKDIPVYLFSrYVPTPFVPYAVQELKAVAGVMITASHNRKEDNGYKVYWETG 191
Cdd:TIGR03990 39 VVGRDTR------TSGPMLENAVIAGLLSTGCDVVDLG-IAPTPTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 192 AQITSPHDKEILKCIEE---CVEPWNdswndnlvDTSPLKKDPlqDICKKYMED-LKKICfyRDLNSKTTLKFVHTSFHG 267
Cdd:TIGR03990 112 TELSREQEEEIEEIAESgdfERADWD--------EIGTVTSDE--DAIDDYIEAiLDKVD--VEAIRKKGFKVVVDCGNG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 268 VGHDYVQLAFQVFGFKpPIPVPEQkdPDPDFSTvkcPNPEEGESVLELSLRLAEKENARIVLATDPDADRLAVaeLQENG 347
Cdd:TIGR03990 180 AGSLTTPYLLRELGCK-VITLNCQ--PDGTFPG---RNPEPTPENLKDLSALVKATGADLGIAHDGDADRLVF--IDEKG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 348 RwkVFTGNELAALFGWWMfdcWKKNKPNadvknvymLATTVS-SKILKAIALKEGFHFEETLPGFKWIGSRIKDLlgngk 426
Cdd:TIGR03990 252 R--FIGGDYTLALFAKYL---LEHGGGK--------VVTNVSsSRAVEDVAERHGGEVIRTKVGEVNVAEKMKEE----- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 427 EVLFAFEESIGFLCGTSVLDKDGVSAAAVVAEMasfLDTRKVTLMEQLTkvyEIYGYHMSKTSYFLcyDPPTIKTIFERI 506
Cdd:TIGR03990 314 GAVFGGEGNGGWIFPDHHYCRDGLMAAALFLEL---LAEEGKPLSELLA---ELPKYPMSKEKVEL--PDEDKEEVMEAV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 507 RNFESPKEypkfcgafailhvrdITT--GydssqpnkksvlpvsknsqmITFTFQNGCVaTLRTSGTEPKIKYYAEmcaS 584
Cdd:TIGR03990 386 EEEFADAE---------------IDTidG--------------------VRIDFEDGWV-LVRPSGTEPIVRIYAE---A 426
|
490
....*....|....*..
gi 26333105 585 PGQSDTTFLEEELKKLI 601
Cdd:TIGR03990 427 KTEERAEELLEEGRSLV 443
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
24-620 |
0e+00 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 752.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 24 QLDTAIGQWLRWDKNPKTKEQIENLLRNGMNKELRDRLCCRMTFGTAGLRSAMGAGFCYINDLTVIQSTQGMYKYLERCF 103
Cdd:PTZ00150 4 SLEAQVELWLKWDKDPETRKEIEELLASKDEEELKRRFLKRMEFGTAGLRGKMGAGFNCMNDLTVQQTAQGLCAYVIETF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 104 S-DFKQRGFVVGYDTRGQvtsscsSQRLAKLTAAVLLAKDIPVYLFSRYVPTPFVPYAVQELKAVAGVMITASHNRKEDN 182
Cdd:PTZ00150 84 GqALKSRGVVIGYDGRYH------SRRFAEITASVFLSKGFKVYLFGQTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 183 GYKVYWETGAQITSPHDKEILKCIEECVEPWNDSWNDNlvdTSPLKKDPLQDICKKYMEDLKKI-CFYRDLNSKttLKFV 261
Cdd:PTZ00150 158 GYKVYWSNGAQIIPPHDKNISAKILSNLEPWSSSWEYL---TETLVEDPLAEVSDAYFATLKSEyNPACCDRSK--VKIV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 262 HTSFHGVGHDYVQLAFQVFGFKPPIPVPEQKDPDPDFSTVKCPNPEEGESVLELSLRLAEKENARIVLATDPDADRLAVA 341
Cdd:PTZ00150 233 YTAMHGVGTRFVQKALHTVGLPNLLSVAQQAEPDPEFPTVTFPNPEEGKGALKLSMETAEAHGSTVVLANDPDADRLAVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 342 ELQeNGRWKVFTGNELAALFGWWMfdcWKKN-KPNADVKNVYMLATTVSSKILKAIALKEGFHFEETLPGFKWIGSRIKD 420
Cdd:PTZ00150 313 EKL-NNGWKIFTGNELGALLAWWA---MKRYrRQGIDKSKCFFICTVVSSRMLKKMAEKEGFQYDETLTGFKWIGNKAIE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 421 LLG-NGKEVLFAFEESIGFLCGTSVLDKDGVSAAAVVAEMASFLDTRKVTLMEQLTKVYEIYGYHMSKTSYFLCYDPPTI 499
Cdd:PTZ00150 389 LNAeNGLTTLFAYEEAIGFMLGTRVRDKDGVTAAAVVAEMALYLYERGKTLVEHLESLYKQYGYHFTNNSYYICYDPSRI 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 500 KTIFERIRNFESpkeYPKFCGAFAILHVRDITTGYDSSQPNKKSVLPVSKNSQMITFTFQNGCVATLRTSGTEPKIKYYA 579
Cdd:PTZ00150 469 VSIFNDIRNNGS---YPTKLGGYPVTRIRDLTTGYDTATPDGKPLLPVSASTQMITFYFENGAIITIRGSGTEPKLKWYA 545
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 26333105 580 EMCASPGQSdttfLEEELKKLIDALIENFLEPSKNALVWRS 620
Cdd:PTZ00150 546 ELSGTKDEA----VEKELAALVDEVVEQLMQPEKYGLVPRK 582
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
64-606 |
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: 681.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 64 RMTFGTAGLRSAMGAGFCYINDLTVIQSTQGMYKYLERCFSDFKQRGFVVGYDTRGqvtsscSSQRLAKLTAAVLLAKDI 143
Cdd:cd05799 1 RLEFGTAGLRGKMGAGTNRMNDYTVRQATQGLANYLKKKGPDAKNRGVVIGYDSRH------NSREFAELTAAVLAANGI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 144 PVYLFSRYVPTPFVPYAVQELKAVAGVMITASHNRKEDNGYKVYWETGAQITSPHDKEILKCIEECVEPWNDSWNDNLvd 223
Cdd:cd05799 75 KVYLFDDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAVLEPLDIKFEEAL-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 224 TSPLKKDPLQDICKKYMEDLKKICFYRDLNSKTTLKFVHTSFHGVGHDYVQLAFQVFGFKPPIPVPEQKDPDPDFSTVKC 303
Cdd:cd05799 153 DSGLIKYIGEEIDDAYLEAVKKLLVNPELNEGKDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVVEEQAEPDPDFPTVKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 304 PNPEEgESVLELSLRLAEKENARIVLATDPDADRLAVAELQENGRWKVFTGNELAALFGWWMFDCWKKNkpNADVKNVYM 383
Cdd:cd05799 233 PNPEE-PGALDLAIELAKKVGADLILATDPDADRLGVAVKDKDGEWRLLTGNEIGALLADYLLEQRKEK--GKLPKNPVI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 384 LATTVSSKILKAIALKEGFHFEETLPGFKWIGSRIKDLLGNGKEVLFAFEESIGFLCGTSVLDKDGVSAAAVVAEMASFL 463
Cdd:cd05799 310 VKTIVSSELLRKIAKKYGVKVEETLTGFKWIGNKIEELESGGKKFLFGFEESIGYLVGPFVRDKDGISAAALLAEMAAYL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 464 DTRKVTLMEQLTKVYEIYGYHMSKTSYFLC---YDPPTIKTIFERIRNfespkeypkfcgafailhvrdittgydssqpn 540
Cdd:cd05799 390 KAQGKTLLDRLDELYEKYGYYKEKTISITFegkEGPEKIKAIMDRLRN-------------------------------- 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26333105 541 kksvlpvskNSQMITFTFQNGCVATLRTSGTEPKIKYYAEMCaspGQSDttflEEELKKLIDALIE 606
Cdd:cd05799 438 ---------NPNVLTFYLEDGSRVTVRPSGTEPKIKFYIEVV---GKKT----LEEAEKKLDALKK 487
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
64-605 |
2.04e-86 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 276.70 E-value: 2.04e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 64 RMTFGTAGLRSAMGAgfcYINDLTVIQSTQGMYKYLERCfsdfKQRGFVVGYDTRgqvtssCSSQRLAKLTAAVLLAKDI 143
Cdd:COG1109 4 KKLFGTDGIRGIVGE---ELTPEFVLKLGRAFGTYLKEK----GGPKVVVGRDTR------LSSPMLARALAAGLASAGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 144 PVYLFsRYVPTPFVPYAVQELKAVAGVMITASHNRKEDNGYKVYWETGAQITSPHDKEILKCIEecvepwndswNDNLVD 223
Cdd:COG1109 71 DVYDL-GLVPTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIE----------KEDFRR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 224 TSPLKKDPL---QDICKKYMEDLKKicFYRDLNSKTTLKFVHTSFHGVGHDYVQLAFQVFGFKpPIPVPEQkdPDPDFST 300
Cdd:COG1109 140 AEAEEIGKVtriEDVLEAYIEALKS--LVDEALRLRGLKVVVDCGNGAAGGVAPRLLRELGAE-VIVLNAE--PDGNFPN 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 301 VKcPNPEEGesVLELSLRLAEKENARIVLATDPDADRLAVAElqENGRwkVFTGNELAALFGWWMfdcwKKNKPNADVkn 380
Cdd:COG1109 215 HN-PNPEPE--NLEDLIEAVKETGADLGIAFDGDADRLGVVD--EKGR--FLDGDQLLALLARYL----LEKGPGGTV-- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 381 vymLATTVSSKILKAIALKEGFHFEETLPGFKWIGSRIKDLlgngkEVLFAFEESIGFLCGTSVLDKDGVSAAAVVAEMA 460
Cdd:COG1109 282 ---VVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKMRET-----GAVLGGEESGGIIFPDFVPTDDGILAALLLLELL 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 461 SFLDTRKVTLMEQLTKvyeiygYHMSKTSyFLCYDPPTIKTIFERIRNfespkeypkfcgafAILHVRDITTgydssqpn 540
Cdd:COG1109 354 AKQGKSLSELLAELPR------YPQPEIN-VRVPDEEKIGAVMEKLRE--------------AVEDKEELDT-------- 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26333105 541 kksvlpvsknSQMITFTFQNGCVATLRTSGTEPKIKYYAEmcaSPGQSDTTFLEEELKKLIDALI 605
Cdd:COG1109 405 ----------IDGVKVDLEDGGWVLVRPSGTEPLLRVYAE---AKDEEEAEELLAELAELVEEAL 456
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
167-600 |
5.86e-70 |
|
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: 230.32 E-value: 5.86e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 167 VAGVMITASHNRKEDNGYKVYWETGAQITSPHDKEILKCIEECVEPWNDSWNdnlvdtsPLKKDPLQDICKKYMEDLKKI 246
Cdd:cd03084 30 TGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSAVAYE-------LGGSVKAVDILQRYFEALKKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 247 CFYRDLNsKTTLKFVHTSFHGVGHDYVQLAFQVFGFKppiPVPEQKDPDPDFsTVKCPNPEEGESVLELSLRLaEKENAR 326
Cdd:cd03084 103 FDVAALS-NKKFKVVVDSVNGVGGPIAPQLLEKLGAE---VIPLNCEPDGNF-GNINPDPGSETNLKQLLAVV-KAEKAD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 327 IVLATDPDADRLAVAElqENGRWkvFTGNELAALFGWWMFDCWKKNKpnadvknvYMLATTVSSKILKAIALKEGFHFEE 406
Cdd:cd03084 177 FGVAFDGDADRLIVVD--ENGGF--LDGDELLALLAVELFLTFNPRG--------GVVKTVVSSGALDKVAKKLGIKVIR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 407 TLPGFKWIGSRIKDllgngKEVLFAFEESIGFLCGTSVLDKDGVSAAAVVAEMASFLdtrKVTLMEQLTKVYEIYGYHMS 486
Cdd:cd03084 245 TKTGFKWVGEAMQE-----GDVVLGGEESGGVIFPEFHPGRDGISAALLLLEILANL---GKSLSELFSELPRYYYIRLK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 487 KTSYFLcydpptiktiferirnfespkeypkfcgafailhvrdittgydssqpnkksvlpvsknsqmitftfqngcvatL 566
Cdd:cd03084 317 VRGWVL-------------------------------------------------------------------------V 323
|
410 420 430
....*....|....*....|....*....|....
gi 26333105 567 RTSGTEPKIKYYAEmcaspgqSDTTFLEEELKKL 600
Cdd:cd03084 324 RASGTEPAIRIYAE-------ADTQEDVEQIKKE 350
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
65-601 |
9.78e-63 |
|
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: 214.34 E-value: 9.78e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 65 MTFGTAGLRSAMGAGFCYINDLTViqsTQGMYKYLERcfSDFKQRGFVVGYDTRGQvtsscsSQRLAKLTAAVLLAKDIP 144
Cdd:cd05800 1 IKFGTDGWRGIIAEDFTFENVRRV---AQAIADYLKE--EGGGGRGVVVGYDTRFL------SEEFARAVAEVLAANGID 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 145 VYLFSRYVPTPFVPYAVQELKAVAGVMITASHNRKEDNGYKVYWETGAqitsPHDKEILKCIEECVEPWNDSWNDNLVDT 224
Cdd:cd05800 70 VYLSDRPVPTPAVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGG----SALPEITAAIEARLASGEPPGLEARAEG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 225 SPLKKDPLQDickkYMEDLKKIcFYRDLNSKTTLKFVHTSFHGVGHDYVQLAFQVFGFKppipVPE-QKDPDPDFStVKC 303
Cdd:cd05800 146 LIETIDPKPD----YLEALRSL-VDLEAIREAGLKVVVDPMYGAGAGYLEELLRGAGVD----VEEiRAERDPLFG-GIP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 304 PNPEEgESVLELSLRLAEkENARIVLATDPDADRLAVAElqENGRwkVFTGNELAALFGWWMFDcwKKNKPNADVKNVym 383
Cdd:cd05800 216 PEPIE-KNLGELAEAVKE-GGADLGLATDGDADRIGAVD--EKGN--FLDPNQILALLLDYLLE--NKGLRGPVVKTV-- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 384 lATTVsskILKAIALKEGFHFEETLPGFKWIGSRIKDllgngKEVLFAFEESIGFLCGTSVLDKDGVSAAAVVAEMASfl 463
Cdd:cd05800 286 -STTH---LIDRIAEKHGLPVYETPVGFKYIAEKMLE-----EDVLIGGEESGGLGIRGHIPERDGILAGLLLLEAVA-- 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 464 dTRKVTLMEQLTKVYEIYGY-HMSKTSYFLcyDPPTIKTIFERIRNFEspkeyPKFCGAFAILHVRDItTGYdssqpnKk 542
Cdd:cd05800 355 -KTGKPLSELVAELEEEYGPsYYDRIDLRL--TPAQKEAILEKLKNEP-----PLSIAGGKVDEVNTI-DGV------K- 418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 26333105 543 svlpvsknsqmitFTFQNGCVATLRTSGTEPKIKYYAEMcASPGQSDTtfLEEELKKLI 601
Cdd:cd05800 419 -------------LVLEDGSWLLIRPSGTEPLLRIYAEA-PSPEKVEA--LLDAGKKLA 461
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
64-208 |
4.06e-38 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 137.36 E-value: 4.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 64 RMTFGTAGLRSAMGAGFcyINDLTVIQSTQGMYKYLErcfSDFKQRGFVVGYDTRGqvtsscSSQRLAKLTAAVLLAKDI 143
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGE--LTPEFALKLGQAIASYLR---AQGGGGKVVVGRDTRY------SSRELARALAAGLASNGV 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26333105 144 PVYLFSrYVPTPFVPYAVQELKAVAGVMITASHNRKEDNGYKVYWETGAQITSPHDKEILKCIEE 208
Cdd:pfam02878 70 EVILLG-LLPTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEK 133
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
112-601 |
1.76e-27 |
|
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been characterized as the archaeal protein responsible for the second step of UDP-GlcNAc biosynthesis. This GlmM protein catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. The first-characterized bacterial GlmM protein is modeled by TIGR01455. These two families are members of the larger phosphoglucomutase/phosphomannomutase family (characterized by three domains: pfam02878, pfam02879 and pfam02880), but are not nearest neighbors to each other. This model also includes a number of sequences from non-archaea in the Bacteroides, Chlorobi, Chloroflexi, Planctomycetes and Spirochaetes lineages. Evidence supporting their inclusion in this equivalog as having the same activity comes from genomic context and phylogenetic profiling. A large number of these organisms are known to produce exo-polysaccharide and yet only appeared to contain the GlmS enzyme of the GlmSMU pathway for UDP-GlcNAc biosynthesis (GenProp0750). In some organisms including Leptospira, this archaeal GlmM is found adjacent to the GlmS as well as a putative GlmU non-orthologous homolog. Phylogenetic profiling of the GlmS-only pattern using PPP identifies members of this archaeal GlmM family as the highest-scoring result. [Central intermediary metabolism, Amino sugars]
Pssm-ID: 274906 Cd Length: 443 Bit Score: 115.69 E-value: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 112 VVGYDTRgqvtssCSSQRLAKLTAAVLLAKDIPVYLFSrYVPTPFVPYAVQELKAVAGVMITASHNRKEDNGYKVYWETG 191
Cdd:TIGR03990 39 VVGRDTR------TSGPMLENAVIAGLLSTGCDVVDLG-IAPTPTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 192 AQITSPHDKEILKCIEE---CVEPWNdswndnlvDTSPLKKDPlqDICKKYMED-LKKICfyRDLNSKTTLKFVHTSFHG 267
Cdd:TIGR03990 112 TELSREQEEEIEEIAESgdfERADWD--------EIGTVTSDE--DAIDDYIEAiLDKVD--VEAIRKKGFKVVVDCGNG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 268 VGHDYVQLAFQVFGFKpPIPVPEQkdPDPDFSTvkcPNPEEGESVLELSLRLAEKENARIVLATDPDADRLAVaeLQENG 347
Cdd:TIGR03990 180 AGSLTTPYLLRELGCK-VITLNCQ--PDGTFPG---RNPEPTPENLKDLSALVKATGADLGIAHDGDADRLVF--IDEKG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 348 RwkVFTGNELAALFGWWMfdcWKKNKPNadvknvymLATTVS-SKILKAIALKEGFHFEETLPGFKWIGSRIKDLlgngk 426
Cdd:TIGR03990 252 R--FIGGDYTLALFAKYL---LEHGGGK--------VVTNVSsSRAVEDVAERHGGEVIRTKVGEVNVAEKMKEE----- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 427 EVLFAFEESIGFLCGTSVLDKDGVSAAAVVAEMasfLDTRKVTLMEQLTkvyEIYGYHMSKTSYFLcyDPPTIKTIFERI 506
Cdd:TIGR03990 314 GAVFGGEGNGGWIFPDHHYCRDGLMAAALFLEL---LAEEGKPLSELLA---ELPKYPMSKEKVEL--PDEDKEEVMEAV 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 507 RNFESPKEypkfcgafailhvrdITT--GydssqpnkksvlpvsknsqmITFTFQNGCVaTLRTSGTEPKIKYYAEmcaS 584
Cdd:TIGR03990 386 EEEFADAE---------------IDTidG--------------------VRIDFEDGWV-LVRPSGTEPIVRIYAE---A 426
|
490
....*....|....*..
gi 26333105 585 PGQSDTTFLEEELKKLI 601
Cdd:TIGR03990 427 KTEERAEELLEEGRSLV 443
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
104-580 |
6.78e-27 |
|
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: 113.82 E-value: 6.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 104 SDFKQRGFVVGYDTRgqvtssCSSQRLAKLTAAVLLAKDIPVYLFSrYVPTPFVPYAVQELkAVAGVMITASHNRKEDNG 183
Cdd:cd03087 29 TYLGGGTVVVGRDTR------TSGPMLKNAVIAGLLSAGCDVIDIG-IVPTPALQYAVRKL-GDAGVMITASHNPPEYNG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 184 YKVYWETGAQITSPHDKEILKCIEEcvEPWND-SWND--NLVDTSPLKKDplqdickkYMED-LKKIcfyrDLNSKTTLK 259
Cdd:cd03087 101 IKLVNPDGTEFSREQEEEIEEIIFS--ERFRRvAWDEvgSVRREDSAIDE--------YIEAiLDKV----DIDGGKGLK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 260 FVHTSFHGVGHDYVQLAFQVFGFKpPIPVPEQkdPDPDFSTvkcPNPEEGESVLELSLRLAEKENARIVLATDPDADRLA 339
Cdd:cd03087 167 VVVDCGNGAGSLTTPYLLRELGCK-VITLNAN--PDGFFPG---RPPEPTPENLSELMELVRATGADLGIAHDGDADRAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 340 VaeLQENGRwkVFTGNELAALFGWWMfdCWKKNKPnadvknvymLATTVS-SKILKAIALKEGFHFEETLPGFKWIGSRI 418
Cdd:cd03087 241 F--VDEKGR--FIDGDKLLALLAKYL--LEEGGGK---------VVTPVDaSMLVEDVVEEAGGEVIRTPVGDVHVAEEM 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 419 kdllgNGKEVLFAFEESIGFLCGTSVLDKDGVSAAAVVAEMASfldtRKVTLMEQLTkvyEIYGYHMSKTSYFlcYDPPT 498
Cdd:cd03087 306 -----IENGAVFGGEPNGGWIFPDHQLCRDGIMTAALLLELLA----EEKPLSELLD---ELPKYPLLREKVE--CPDEK 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 499 IKTIFERIRNFESPKEYpkfcgafailhvrDITT--GydssqpnkksvlpvsknsqmITFTFQNGCVaTLRTSGTEPKIK 576
Cdd:cd03087 372 KEEVMEAVEEELSDADE-------------DVDTidG--------------------VRIEYEDGWV-LIRPSGTEPKIR 417
|
....
gi 26333105 577 YYAE 580
Cdd:cd03087 418 ITAE 421
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
239-347 |
1.91e-23 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 95.05 E-value: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 239 YMEDLKKICFyRDLNSKTTLKFVHTSFHGVGHDYVQLAFQVFGFkppIPVPEQKDPDPDFSTvKCPNPEEGEsVLELSLR 318
Cdd:pfam02879 2 YIDHLLELVD-SEALKKRGLKVVYDPLHGVGGGYLPELLKRLGC---DVVEENCEPDPDFPT-RAPNPEEPE-ALALLIE 75
|
90 100
....*....|....*....|....*....
gi 26333105 319 LAEKENARIVLATDPDADRLAVAElqENG 347
Cdd:pfam02879 76 LVKSVGADLGIATDGDADRLGVVD--ERG 102
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
112-401 |
4.84e-19 |
|
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: 90.27 E-value: 4.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 112 VVGYDTRgqvtssCSSQRLAKLTAAVLLAKDIPVYLFSRyVPTPFVPYAVQELKAVAGVMITASHNRKEDNGYKvyWETG 191
Cdd:cd03089 40 VVGRDGR------LSSPELAAALIEGLLAAGCDVIDIGL-VPTPVLYFATFHLDADGGVMITASHNPPEYNGFK--IVIG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 192 AQITSPHD-KEILKCIEEcvepwNDSWNDNlVDTSPLKKDPLQDickkYMEDLKKICfyrDLNSKtTLKFVHTSFHGVGH 270
Cdd:cd03089 111 GGPLSGEDiQALRERAEK-----GDFAAAT-GRGSVEKVDILPD----YIDRLLSDI---KLGKR-PLKVVVDAGNGAAG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 271 DYVQLAFQVFGFKppiPVPEQKDPDPDFSTvKCPNPEEGESVLELSLRLAEkENARIVLATDPDADRLAVaeLQENGRwk 350
Cdd:cd03089 177 PIAPQLLEALGCE---VIPLFCEPDGTFPN-HHPDPTDPENLEDLIAAVKE-NGADLGIAFDGDGDRLGV--VDEKGE-- 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 26333105 351 VFTGNELAALFgwwmfdcWK---KNKPNA----DVKNVYMLATTVSSKILKAIALKEG 401
Cdd:cd03089 248 IIWGDRLLALF-------ARdilKRNPGAtivyDVKCSRNLYDFIEEAGGKPIMWKTG 298
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
353-481 |
2.02e-16 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 75.56 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 353 TGNELAALFGWWMFDCWKKNKPNADVKNVymlattVSSKILKAIALKEGFHFEETLPGFKWIGSRIKDllgngKEVLFAF 432
Cdd:pfam02880 1 DGDQILALLAKYLLEQGKLPPGAGVVKTV------MSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMRE-----EGALFGG 69
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 26333105 433 EESIGFLCGTSVLDKDGVSAAAVVAEMASfldTRKVTLMEQLTKVYEIY 481
Cdd:pfam02880 70 EESGHIIFLDHATTKDGILAALLVLEILA---RTGKSLSELLEELPEKY 115
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
64-606 |
1.98e-14 |
|
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: 76.13 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 64 RMTFGTAGLR-SAMGAGFcyiNDLTVIQSTQGMYKYleRcfsdfKQRGF----VVGYDTRGQvtsscssQRLAKLTA-AV 137
Cdd:cd05801 20 RVAFGTSGHRgSSLKGSF---NEAHILAISQAICDY--R-----KSQGItgplFLGKDTHAL-------SEPAFISAlEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 138 LLAKDIPVYLFSR--YVPTPFVPYAV-----QELKAVA-GVMITASHNRKEDNGYKVYWETGAqitsPHDKEILKCIEEC 209
Cdd:cd05801 83 LAANGVEVIIQQNdgYTPTPVISHAIltynrGRTEGLAdGIVITPSHNPPEDGGFKYNPPHGG----PADTDITRWIEKR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 210 VepwNDSWNDNLVDtspLKKDPL-----------QDICKKYMEDLKKICfyrDLNS--KTTLKFVHTSFHGVGHDYVQLA 276
Cdd:cd05801 159 A---NALLANGLKG---VKRIPLeaalasgythrHDFVTPYVADLGNVI---DMDAirKSGLRLGVDPLGGASVPYWQPI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 277 FQVFGFKPPIPVPEQkDPDPDFSTV--------KCPNPEEGESVLELslrlaeKENARIVLATDPDADRLAVAElqenGR 348
Cdd:cd05801 230 AEKYGLNLTVVNPKV-DPTFRFMTLdhdgkirmDCSSPYAMAGLLKL------KDKFDLAFANDPDADRHGIVT----PS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 349 WKVFTGNELAALFGWWMFdcwkKNKPNADvKNVYMLATTVSSKILKAIALKEGFHFEETLPGFKWigsrIKDLLGNGKeV 428
Cdd:cd05801 299 AGLMNPNHYLSVAIDYLF----THRPLWN-KSAGVGKTLVSSSMIDRVAAALGRKLYEVPVGFKW----FVDGLLDGS-L 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 429 LFAFEESIG--FLC--GTS-VLDKDGVSAAAVVAEMASFLDTRKVTLMEQLTkvyEIYGyhmskTSYFLCYDPPTI---K 500
Cdd:cd05801 369 GFGGEESAGasFLRrdGTVwTTDKDGIIMCLLAAEILAVTGKDPGQLYQELT---ERFG-----EPYYARIDAPATpeqK 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 501 TIFERIrnfeSPKE-YPKFCGAFAILHVRDITTGYDSSQPNKKsvlpvsknsqmitFTFQNGCVAtLRTSGTEPKIKYYA 579
Cdd:cd05801 441 ARLKKL----SPEQvTATELAGDPILAKLTRAPGNGASIGGLK-------------VTTANGWFA-ARPSGTEDVYKIYA 502
|
570 580
....*....|....*....|....*...
gi 26333105 580 EmcaspgqsdtTFL-EEELKKLIDALIE 606
Cdd:cd05801 503 E----------SFLsEEHLKKIQKEAQE 520
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
102-348 |
4.80e-14 |
|
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: 74.65 E-value: 4.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 102 CFSDFKQRGFVVGYDTRGqvtsscSSQRLAKLTAAVLLA-----KDIPVylfsryVPTPFVPYAVQELKAVAGVMITASH 176
Cdd:cd05803 31 QPERTKGGKIVVGRDGRP------SGPMLEKIVIGALLAcgcdvIDLGI------APTPTVQVLVRQSQASGGIIITASH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 177 NRKEDNGYKVYWETGAQITSPHDKEILKCIEECVEPWnDSWNDNL-VDTSPlkkDPLQDICKKYmedLKKICFYRDLNSK 255
Cdd:cd05803 99 NPPQWNGLKFIGPDGEFLTPDEGEEVLSCAEAGSAQK-AGYDQLGeVTFSE---DAIAEHIDKV---LALVDVDVIKIRE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 256 TTLKFVHTSFHGVGHDYV-----QLAFQVF--GFKPPIPVPEQKDPDPdfstvkcpnpeegESVLELSlRLAEKENARIV 328
Cdd:cd05803 172 RNFKVAVDSVNGAGGLLIprlleKLGCEVIvlNCEPTGLFPHTPEPLP-------------ENLTQLC-AAVKESGADVG 237
|
250 260
....*....|....*....|
gi 26333105 329 LATDPDADRLAVaeLQENGR 348
Cdd:cd05803 238 FAVDPDADRLAL--VDEDGR 255
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
111-211 |
2.90e-10 |
|
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: 62.50 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 111 FVVGYDTRgqvtssCSSQRLAKLTAAVLLAKDIPVYLFSrYVPTPFVPYAVQELKAVAGVMITASHNRKEDNGYKVYWET 190
Cdd:cd05802 40 VLIGKDTR------ISGYMLESALAAGLTSAGVDVLLLG-VIPTPAVAYLTRKLRADAGVVISASHNPFEDNGIKFFSSD 112
|
90 100
....*....|....*....|.
gi 26333105 191 GAQItsPHDKEILkcIEECVE 211
Cdd:cd05802 113 GYKL--PDEVEEE--IEALID 129
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
112-187 |
1.99e-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: 1.99e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26333105 112 VVGYDTRgqvtssCSSQRLAKLTAAVLLAKDIPVYLFSrYVPTPFVPYAVQELKAVAGVMITASHNRKEDNGYKVY 187
Cdd:TIGR01455 42 VIGKDTR------LSGYMLENALAAGLNSAGVDVLLLG-PLPTPAVAYLTRTLRADAGVMISASHNPYEDNGIKFF 110
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
67-204 |
1.91e-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: 50.66 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 67 FGTAGLR---SAMGAGFCYINdltviqsTQGMYKYLErcfSDFKQRGFVVGYDTRGqvtsscSSQRLAKLTAAVLLAKDI 143
Cdd:cd03088 2 FGTSGLRglvTDLTDEVCYAY-------TRAFLQHLE---SKFPGDTVAVGRDLRP------SSPRIAAACAAALRDAGF 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26333105 144 -PVYLFSryVPTPFVPYAVQELKAvAGVMITASHNRKEDNGYKVYWETGaqitsphdkEILK 204
Cdd:cd03088 66 rVVDCGA--VPTPALALYAMKRGA-PAIMVTGSHIPADRNGLKFYRPDG---------EITK 115
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
152-185 |
3.04e-05 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 46.67 E-value: 3.04e-05
10 20 30
....*....|....*....|....*....|....
gi 26333105 152 VPTPFVPYAVQELKAVAGVMITASHNRKEDNGYK 185
Cdd:PRK10887 76 MPTPAVAYLTRTLRAEAGIVISASHNPYYDNGIK 109
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
165-186 |
5.41e-04 |
|
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: 42.97 E-value: 5.41e-04
10 20
....*....|....*....|..
gi 26333105 165 KAVAGVMITASHNRKEDNGYKV 186
Cdd:cd03086 34 GKTIGVMITASHNPVEDNGVKI 55
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
167-251 |
1.28e-03 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 41.95 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333105 167 VAGVMITASHNRKEDNGYKVY----------WETGAQ--ITSPHDKEILKCIEECVEpwndswnDNLVDTSPLKKDPLQD 234
Cdd:PTZ00302 76 SVGVMITASHNPIQDNGVKIIdpdggmleesWEKICTdfANARTGEDLVSVLMDCLT-------EHGIKLSNLKLDLNKS 148
|
90
....*....|....*..
gi 26333105 235 ICKKYmedlkKICFYRD 251
Cdd:PTZ00302 149 NCSKA-----KVHVGRD 160
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
164-186 |
2.65e-03 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 40.78 E-value: 2.65e-03
10 20
....*....|....*....|...
gi 26333105 164 LKAVAGVMITASHNRKEDNGYKV 186
Cdd:PLN02895 56 TGAATGLMITASHNPVSDNGVKI 78
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
554-607 |
7.79e-03 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 39.25 E-value: 7.79e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 26333105 554 ITFTFQNGCVATLRTSGTEPKIKYYAEmcaSPGQSDTTFLEEELKKLIDALIEN 607
Cdd:PTZ00302 534 IVSKYDNAARAFIRPSGTEPVVRVYAE---APTLEQADELANEVKGLVLRYCSG 584
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
551-606 |
9.84e-03 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 35.32 E-value: 9.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 26333105 551 SQMITFTFQNGCVATLRTSGTEPKIKYYAEmcaspGQSDttfleEELKKLIDALIE 606
Cdd:pfam00408 23 ADAEKILGEDGRRLDVRPSGTEPVLRVMVE-----GDSD-----EELARLADEIAD 68
|
|
| |
