|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
24-621 |
0e+00 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 763.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 24 QLDTAIGQWLRWDKNPKTKEQIENLLRNGMNKELRDRLCCRMTFGTAGLRSAMGAGFCYINDLTVIQSTQGMYKYLERCF 103
Cdd:PTZ00150 4 SLEAQVELWLKWDKDPETRKEIEELLASKDEEELKRRFLKRMEFGTAGLRGKMGAGFNCMNDLTVQQTAQGLCAYVIETF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 104 S-DFKQRGFVVGYDTRGQvtsscsSQRLAKLTAAVLLAKDVPVYLFSRYVPTPFVPYAVQKLKAVAGVMITASHNRKEDN 182
Cdd:PTZ00150 84 GqALKSRGVVIGYDGRYH------SRRFAEITASVFLSKGFKVYLFGQTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 183 GYKVYWETGAQITSPHDKEILKCIEECVEPWNGSWNDNlvdTSPLKRDPLQDICRRYMEDLKKI-CFYRELNSKttLKFV 261
Cdd:PTZ00150 158 GYKVYWSNGAQIIPPHDKNISAKILSNLEPWSSSWEYL---TETLVEDPLAEVSDAYFATLKSEyNPACCDRSK--VKIV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 262 HTSFHGVGHDYVQLAFKVFGFKPPIPVPEQKDPDPDFSTVKCPNPEEGESVLELSLRLAEKENARVVLATDPDADRLAAA 341
Cdd:PTZ00150 233 YTAMHGVGTRFVQKALHTVGLPNLLSVAQQAEPDPEFPTVTFPNPEEGKGALKLSMETAEAHGSTVVLANDPDADRLAVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 342 ELQENGcWKVFTGNELAALFGWWMfdcWKKNKSRNADVKNVYMLATTVSSKILKAIALKEGFHFEETLPGFKWIGSRIID 421
Cdd:PTZ00150 313 EKLNNG-WKIFTGNELGALLAWWA---MKRYRRQGIDKSKCFFICTVVSSRMLKKMAEKEGFQYDETLTGFKWIGNKAIE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 422 LL-ENGKEVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMASYLETMNITLKQQLVKVYEKYGYHISKTSYFLCYEPPTI 500
Cdd:PTZ00150 389 LNaENGLTTLFAYEEAIGFMLGTRVRDKDGVTAAAVVAEMALYLYERGKTLVEHLESLYKQYGYHFTNNSYYICYDPSRI 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 501 KSIFERLRNFDSpkeYPKFCGTFAILHVRDVTTGYDSSQPNKKSVLPVSKNSQMITFTFQNGCVATLRTSGTEPKIKYYA 580
Cdd:PTZ00150 469 VSIFNDIRNNGS---YPTKLGGYPVTRIRDLTTGYDTATPDGKPLLPVSASTQMITFYFENGAIITIRGSGTEPKLKWYA 545
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 31377548 581 EMCASPDQSdtalLEEELKKLIDALIENFLQPSKNGLIWRS 621
Cdd:PTZ00150 546 ELSGTKDEA----VEKELAALVDEVVEQLMQPEKYGLVPRK 582
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
64-607 |
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: 680.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 64 RMTFGTAGLRSAMGAGFCYINDLTVIQSTQGMYKYLERCFSDFKQRGFVVGYDTRGqvtsscSSQRLAKLTAAVLLAKDV 143
Cdd:cd05799 1 RLEFGTAGLRGKMGAGTNRMNDYTVRQATQGLANYLKKKGPDAKNRGVVIGYDSRH------NSREFAELTAAVLAANGI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 144 PVYLFSRYVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKVYWETGAQITSPHDKEILKCIEECVEPWNGSWNDNLvd 223
Cdd:cd05799 75 KVYLFDDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAVLEPLDIKFEEAL-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 224 TSPLKRDPLQDICRRYMEDLKKICFYRELNSKTTLKFVHTSFHGVGHDYVQLAFKVFGFKPPIPVPEQKDPDPDFSTVKC 303
Cdd:cd05799 153 DSGLIKYIGEEIDDAYLEAVKKLLVNPELNEGKDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVVEEQAEPDPDFPTVKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 304 PNPEEgESVLELSLRLAEKENARVVLATDPDADRLAAAELQENGCWKVFTGNELAALFGWWMFDCWKKNKSrnaDVKNVY 383
Cdd:cd05799 233 PNPEE-PGALDLAIELAKKVGADLILATDPDADRLGVAVKDKDGEWRLLTGNEIGALLADYLLEQRKEKGK---LPKNPV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 384 MLATTVSSKILKAIALKEGFHFEETLPGFKWIGSRIIDLLENGKEVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMASY 463
Cdd:cd05799 309 IVKTIVSSELLRKIAKKYGVKVEETLTGFKWIGNKIEELESGGKKFLFGFEESIGYLVGPFVRDKDGISAAALLAEMAAY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 464 LETMNITLKQQLVKVYEKYGYHISKTSYFLCYE---PPTIKSIFERLRNfdspkeypkfcgtfailhvrdvttgydssqp 540
Cdd:cd05799 389 LKAQGKTLLDRLDELYEKYGYYKEKTISITFEGkegPEKIKAIMDRLRN------------------------------- 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31377548 541 nkksvlpvskNSQMITFTFQNGCVATLRTSGTEPKIKYYAEMCASPDqsdtallEEELKKLIDALIE 607
Cdd:cd05799 438 ----------NPNVLTFYLEDGSRVTVRPSGTEPKIKFYIEVVGKKT-------LEEAEKKLDALKK 487
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
64-606 |
7.48e-86 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 275.54 E-value: 7.48e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 64 RMTFGTAGLRSAMGAgfcYINDLTVIQSTQGMYKYLERCfsdfKQRGFVVGYDTRgqvtssCSSQRLAKLTAAVLLAKDV 143
Cdd:COG1109 4 KKLFGTDGIRGIVGE---ELTPEFVLKLGRAFGTYLKEK----GGPKVVVGRDTR------LSSPMLARALAAGLASAGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 144 PVYLFsRYVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKVYWETGAQITSPHDKEILKCIEEcVEPWNGSWNDNlvd 223
Cdd:COG1109 71 DVYDL-GLVPTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEK-EDFRRAEAEEI--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 224 tSPLKRdpLQDICRRYMEDLKKicFYRELNSKTTLKFVHTSFHGVGHDYVQLAFKVFGFKpPIPVPEQkdPDPDFSTVKc 303
Cdd:COG1109 146 -GKVTR--IEDVLEAYIEALKS--LVDEALRLRGLKVVVDCGNGAAGGVAPRLLRELGAE-VIVLNAE--PDGNFPNHN- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 304 PNPEEGesVLELSLRLAEKENARVVLATDPDADRLAAAElqENGcwKVFTGNELAALFGWWMfdcwkKNKSRNADVknvy 383
Cdd:COG1109 217 PNPEPE--NLEDLIEAVKETGADLGIAFDGDADRLGVVD--EKG--RFLDGDQLLALLARYL-----LEKGPGGTV---- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 384 mLATTVSSKILKAIALKEGFHFEETLPGFKWIGSRIidlLENGkeVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMASY 463
Cdd:COG1109 282 -VVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKM---RETG--AVLGGEESGGIIFPDFVPTDDGILAALLLLELLAK 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 464 LETmniTLKQqlvkVYEKYGYHISKTSYFLCYEPPTIKSIFERLRNfdspkeypkfcgtfAILHVRDVTTgydssqpnkk 543
Cdd:COG1109 356 QGK---SLSE----LLAELPRYPQPEINVRVPDEEKIGAVMEKLRE--------------AVEDKEELDT---------- 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31377548 544 svlpvsknSQMITFTFQNGCVATLRTSGTEPKIKYYAEmcaSPDQSDTALLEEELKKLIDALI 606
Cdd:COG1109 405 --------IDGVKVDLEDGGWVLVRPSGTEPLLRVYAE---AKDEEEAEELLAELAELVEEAL 456
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
64-208 |
1.31e-38 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 138.90 E-value: 1.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 64 RMTFGTAGLRSAMGAGFcyINDLTVIQSTQGMYKYLErcfSDFKQRGFVVGYDTRGqvtsscSSQRLAKLTAAVLLAKDV 143
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGE--LTPEFALKLGQAIASYLR---AQGGGGKVVVGRDTRY------SSRELARALAAGLASNGV 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31377548 144 PVYLFSrYVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKVYWETGAQITSPHDKEILKCIEE 208
Cdd:pfam02878 70 EVILLG-LLPTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEK 133
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
112-602 |
4.54e-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: 114.53 E-value: 4.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 112 VVGYDTRgqvtssCSSQRLAKLTAAVLLAKDVPVYLFSrYVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKVYWETG 191
Cdd:TIGR03990 39 VVGRDTR------TSGPMLENAVIAGLLSTGCDVVDLG-IAPTPTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 192 AQITSPHDKEILKCIEE---CVEPWNGswndnlvdTSPLKRDPlqDICRRYMED-LKKICfyRELNSKTTLKFVHTSFHG 267
Cdd:TIGR03990 112 TELSREQEEEIEEIAESgdfERADWDE--------IGTVTSDE--DAIDDYIEAiLDKVD--VEAIRKKGFKVVVDCGNG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 268 VGHDYVQLAFKVFGFKpPIPVPEQkdPDPDFSTvkcPNPEEGESVLELSLRLAEKENARVVLATDPDADRLAAaeLQENG 347
Cdd:TIGR03990 180 AGSLTTPYLLRELGCK-VITLNCQ--PDGTFPG---RNPEPTPENLKDLSALVKATGADLGIAHDGDADRLVF--IDEKG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 348 cwKVFTGNELAALFGWWMfdcWKKNKSRnadvknvymLATTVS-SKILKAIALKEGFHFEETLpgfkwIGSRII--DLLE 424
Cdd:TIGR03990 252 --RFIGGDYTLALFAKYL---LEHGGGK---------VVTNVSsSRAVEDVAERHGGEVIRTK-----VGEVNVaeKMKE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 425 NGkeVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMasyLETMNITLkQQLVKVYEKygYHISKTSyflcYEPPTIK--S 502
Cdd:TIGR03990 313 EG--AVFGGEGNGGWIFPDHHYCRDGLMAAALFLEL---LAEEGKPL-SELLAELPK--YPMSKEK----VELPDEDkeE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 503 IFERLRnfdspKEYPKFcgtfailhvrDVTT--GydssqpnkksvlpvsknsqmITFTFQNGCVaTLRTSGTEPKIKYYA 580
Cdd:TIGR03990 381 VMEAVE-----EEFADA----------EIDTidG--------------------VRIDFEDGWV-LVRPSGTEPIVRIYA 424
|
490 500
....*....|....*....|..
gi 31377548 581 EmcaSPDQSDTALLEEELKKLI 602
Cdd:TIGR03990 425 E---AKTEERAEELLEEGRSLV 443
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
24-621 |
0e+00 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 763.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 24 QLDTAIGQWLRWDKNPKTKEQIENLLRNGMNKELRDRLCCRMTFGTAGLRSAMGAGFCYINDLTVIQSTQGMYKYLERCF 103
Cdd:PTZ00150 4 SLEAQVELWLKWDKDPETRKEIEELLASKDEEELKRRFLKRMEFGTAGLRGKMGAGFNCMNDLTVQQTAQGLCAYVIETF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 104 S-DFKQRGFVVGYDTRGQvtsscsSQRLAKLTAAVLLAKDVPVYLFSRYVPTPFVPYAVQKLKAVAGVMITASHNRKEDN 182
Cdd:PTZ00150 84 GqALKSRGVVIGYDGRYH------SRRFAEITASVFLSKGFKVYLFGQTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 183 GYKVYWETGAQITSPHDKEILKCIEECVEPWNGSWNDNlvdTSPLKRDPLQDICRRYMEDLKKI-CFYRELNSKttLKFV 261
Cdd:PTZ00150 158 GYKVYWSNGAQIIPPHDKNISAKILSNLEPWSSSWEYL---TETLVEDPLAEVSDAYFATLKSEyNPACCDRSK--VKIV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 262 HTSFHGVGHDYVQLAFKVFGFKPPIPVPEQKDPDPDFSTVKCPNPEEGESVLELSLRLAEKENARVVLATDPDADRLAAA 341
Cdd:PTZ00150 233 YTAMHGVGTRFVQKALHTVGLPNLLSVAQQAEPDPEFPTVTFPNPEEGKGALKLSMETAEAHGSTVVLANDPDADRLAVA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 342 ELQENGcWKVFTGNELAALFGWWMfdcWKKNKSRNADVKNVYMLATTVSSKILKAIALKEGFHFEETLPGFKWIGSRIID 421
Cdd:PTZ00150 313 EKLNNG-WKIFTGNELGALLAWWA---MKRYRRQGIDKSKCFFICTVVSSRMLKKMAEKEGFQYDETLTGFKWIGNKAIE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 422 LL-ENGKEVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMASYLETMNITLKQQLVKVYEKYGYHISKTSYFLCYEPPTI 500
Cdd:PTZ00150 389 LNaENGLTTLFAYEEAIGFMLGTRVRDKDGVTAAAVVAEMALYLYERGKTLVEHLESLYKQYGYHFTNNSYYICYDPSRI 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 501 KSIFERLRNFDSpkeYPKFCGTFAILHVRDVTTGYDSSQPNKKSVLPVSKNSQMITFTFQNGCVATLRTSGTEPKIKYYA 580
Cdd:PTZ00150 469 VSIFNDIRNNGS---YPTKLGGYPVTRIRDLTTGYDTATPDGKPLLPVSASTQMITFYFENGAIITIRGSGTEPKLKWYA 545
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 31377548 581 EMCASPDQSdtalLEEELKKLIDALIENFLQPSKNGLIWRS 621
Cdd:PTZ00150 546 ELSGTKDEA----VEKELAALVDEVVEQLMQPEKYGLVPRK 582
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
64-607 |
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: 680.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 64 RMTFGTAGLRSAMGAGFCYINDLTVIQSTQGMYKYLERCFSDFKQRGFVVGYDTRGqvtsscSSQRLAKLTAAVLLAKDV 143
Cdd:cd05799 1 RLEFGTAGLRGKMGAGTNRMNDYTVRQATQGLANYLKKKGPDAKNRGVVIGYDSRH------NSREFAELTAAVLAANGI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 144 PVYLFSRYVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKVYWETGAQITSPHDKEILKCIEECVEPWNGSWNDNLvd 223
Cdd:cd05799 75 KVYLFDDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAVLEPLDIKFEEAL-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 224 TSPLKRDPLQDICRRYMEDLKKICFYRELNSKTTLKFVHTSFHGVGHDYVQLAFKVFGFKPPIPVPEQKDPDPDFSTVKC 303
Cdd:cd05799 153 DSGLIKYIGEEIDDAYLEAVKKLLVNPELNEGKDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVVEEQAEPDPDFPTVKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 304 PNPEEgESVLELSLRLAEKENARVVLATDPDADRLAAAELQENGCWKVFTGNELAALFGWWMFDCWKKNKSrnaDVKNVY 383
Cdd:cd05799 233 PNPEE-PGALDLAIELAKKVGADLILATDPDADRLGVAVKDKDGEWRLLTGNEIGALLADYLLEQRKEKGK---LPKNPV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 384 MLATTVSSKILKAIALKEGFHFEETLPGFKWIGSRIIDLLENGKEVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMASY 463
Cdd:cd05799 309 IVKTIVSSELLRKIAKKYGVKVEETLTGFKWIGNKIEELESGGKKFLFGFEESIGYLVGPFVRDKDGISAAALLAEMAAY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 464 LETMNITLKQQLVKVYEKYGYHISKTSYFLCYE---PPTIKSIFERLRNfdspkeypkfcgtfailhvrdvttgydssqp 540
Cdd:cd05799 389 LKAQGKTLLDRLDELYEKYGYYKEKTISITFEGkegPEKIKAIMDRLRN------------------------------- 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31377548 541 nkksvlpvskNSQMITFTFQNGCVATLRTSGTEPKIKYYAEMCASPDqsdtallEEELKKLIDALIE 607
Cdd:cd05799 438 ----------NPNVLTFYLEDGSRVTVRPSGTEPKIKFYIEVVGKKT-------LEEAEKKLDALKK 487
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
64-606 |
7.48e-86 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 275.54 E-value: 7.48e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 64 RMTFGTAGLRSAMGAgfcYINDLTVIQSTQGMYKYLERCfsdfKQRGFVVGYDTRgqvtssCSSQRLAKLTAAVLLAKDV 143
Cdd:COG1109 4 KKLFGTDGIRGIVGE---ELTPEFVLKLGRAFGTYLKEK----GGPKVVVGRDTR------LSSPMLARALAAGLASAGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 144 PVYLFsRYVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKVYWETGAQITSPHDKEILKCIEEcVEPWNGSWNDNlvd 223
Cdd:COG1109 71 DVYDL-GLVPTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEK-EDFRRAEAEEI--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 224 tSPLKRdpLQDICRRYMEDLKKicFYRELNSKTTLKFVHTSFHGVGHDYVQLAFKVFGFKpPIPVPEQkdPDPDFSTVKc 303
Cdd:COG1109 146 -GKVTR--IEDVLEAYIEALKS--LVDEALRLRGLKVVVDCGNGAAGGVAPRLLRELGAE-VIVLNAE--PDGNFPNHN- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 304 PNPEEGesVLELSLRLAEKENARVVLATDPDADRLAAAElqENGcwKVFTGNELAALFGWWMfdcwkKNKSRNADVknvy 383
Cdd:COG1109 217 PNPEPE--NLEDLIEAVKETGADLGIAFDGDADRLGVVD--EKG--RFLDGDQLLALLARYL-----LEKGPGGTV---- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 384 mLATTVSSKILKAIALKEGFHFEETLPGFKWIGSRIidlLENGkeVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMASY 463
Cdd:COG1109 282 -VVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKM---RETG--AVLGGEESGGIIFPDFVPTDDGILAALLLLELLAK 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 464 LETmniTLKQqlvkVYEKYGYHISKTSYFLCYEPPTIKSIFERLRNfdspkeypkfcgtfAILHVRDVTTgydssqpnkk 543
Cdd:COG1109 356 QGK---SLSE----LLAELPRYPQPEINVRVPDEEKIGAVMEKLRE--------------AVEDKEELDT---------- 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31377548 544 svlpvsknSQMITFTFQNGCVATLRTSGTEPKIKYYAEmcaSPDQSDTALLEEELKKLIDALI 606
Cdd:COG1109 405 --------IDGVKVDLEDGGWVLVRPSGTEPLLRVYAE---AKDEEEAEELLAELAELVEEAL 456
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
167-602 |
5.41e-67 |
|
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: 222.62 E-value: 5.41e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 167 VAGVMITASHNRKEDNGYKVYWETGAQITSPHDKEILKCIEECVEPWNGSWNdnlvdtsPLKRDPLQDICRRYMEDLKKI 246
Cdd:cd03084 30 TGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSAVAYE-------LGGSVKAVDILQRYFEALKKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 247 CFYRELNsKTTLKFVHTSFHGVGHDYVQLAFKVFGFKppiPVPEQKDPDPDFsTVKCPNPEEGESVLELSLRLaEKENAR 326
Cdd:cd03084 103 FDVAALS-NKKFKVVVDSVNGVGGPIAPQLLEKLGAE---VIPLNCEPDGNF-GNINPDPGSETNLKQLLAVV-KAEKAD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 327 VVLATDPDADRLAAAElqENgcWKVFTGNELAALFGWWMFDCWKKNKsrnadvknvYMLATTVSSKILKAIALKEGFHFE 406
Cdd:cd03084 177 FGVAFDGDADRLIVVD--EN--GGFLDGDELLALLAVELFLTFNPRG---------GVVKTVVSSGALDKVAKKLGIKVI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 407 ETLPGFKWIGSRIIDllengKEVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMASYLetmNITLKQQLVKVYEKYGYHI 486
Cdd:cd03084 244 RTKTGFKWVGEAMQE-----GDVVLGGEESGGVIFPEFHPGRDGISAALLLLEILANL---GKSLSELFSELPRYYYIRL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 487 SKTSYFLcyepptiksiferlrnfdspkeypkfcgtfailhvrdvttgydssqpnkksvlpvsknsqmitftfqngcvat 566
Cdd:cd03084 316 KVRGWVL------------------------------------------------------------------------- 322
|
410 420 430
....*....|....*....|....*....|....*.
gi 31377548 567 LRTSGTEPKIKYYAEMCAspdQSDTALLEEELKKLI 602
Cdd:cd03084 323 VRASGTEPAIRIYAEADT---QEDVEQIKKEARELV 355
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
65-602 |
3.16e-61 |
|
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: 210.49 E-value: 3.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 65 MTFGTAGLRSAMGAGFCYINDLTViqsTQGMYKYLERcfSDFKQRGFVVGYDTRGQvtsscsSQRLAKLTAAVLLAKDVP 144
Cdd:cd05800 1 IKFGTDGWRGIIAEDFTFENVRRV---AQAIADYLKE--EGGGGRGVVVGYDTRFL------SEEFARAVAEVLAANGID 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 145 VYLFSRYVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKVYWETGAqitsPHDKEILKCIEECVEPWNGSWNDNLVDT 224
Cdd:cd05800 70 VYLSDRPVPTPAVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGG----SALPEITAAIEARLASGEPPGLEARAEG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 225 SPLKRDPLQDicrrYMEDLKKIcFYRELNSKTTLKFVHTSFHGVGHDYVQLAFKVFGFKppipVPE-QKDPDPDFStVKC 303
Cdd:cd05800 146 LIETIDPKPD----YLEALRSL-VDLEAIREAGLKVVVDPMYGAGAGYLEELLRGAGVD----VEEiRAERDPLFG-GIP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 304 PNPEEgESVLELSLRLAEkENARVVLATDPDADRLAAAElqENGcwKVFTGNELAALFgwwMFDCWKKNKSRNADVKNVy 383
Cdd:cd05800 216 PEPIE-KNLGELAEAVKE-GGADLGLATDGDADRIGAVD--EKG--NFLDPNQILALL---LDYLLENKGLRGPVVKTV- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 384 mlATTVsskILKAIALKEGFHFEETLPGFKWIGSRIIDllengKEVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMASY 463
Cdd:cd05800 286 --STTH---LIDRIAEKHGLPVYETPVGFKYIAEKMLE-----EDVLIGGEESGGLGIRGHIPERDGILAGLLLLEAVAK 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 464 LETmniTLKQQLVKVYEKYGYHisktsYF----LCYEPPTIKSIFERLRNfdspkEYPKFCGTFAILHVRDVtTGYdssq 539
Cdd:cd05800 356 TGK---PLSELVAELEEEYGPS-----YYdridLRLTPAQKEAILEKLKN-----EPPLSIAGGKVDEVNTI-DGV---- 417
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31377548 540 pnKksvlpvsknsqmitFTFQNGCVATLRTSGTEPKIKYYAEMcasPDQSDTALLEEELKKLI 602
Cdd:cd05800 418 --K--------------LVLEDGSWLLIRPSGTEPLLRIYAEA---PSPEKVEALLDAGKKLA 461
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
64-208 |
1.31e-38 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 138.90 E-value: 1.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 64 RMTFGTAGLRSAMGAGFcyINDLTVIQSTQGMYKYLErcfSDFKQRGFVVGYDTRGqvtsscSSQRLAKLTAAVLLAKDV 143
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGE--LTPEFALKLGQAIASYLR---AQGGGGKVVVGRDTRY------SSRELARALAAGLASNGV 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31377548 144 PVYLFSrYVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKVYWETGAQITSPHDKEILKCIEE 208
Cdd:pfam02878 70 EVILLG-LLPTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEK 133
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
112-602 |
4.54e-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: 114.53 E-value: 4.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 112 VVGYDTRgqvtssCSSQRLAKLTAAVLLAKDVPVYLFSrYVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKVYWETG 191
Cdd:TIGR03990 39 VVGRDTR------TSGPMLENAVIAGLLSTGCDVVDLG-IAPTPTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 192 AQITSPHDKEILKCIEE---CVEPWNGswndnlvdTSPLKRDPlqDICRRYMED-LKKICfyRELNSKTTLKFVHTSFHG 267
Cdd:TIGR03990 112 TELSREQEEEIEEIAESgdfERADWDE--------IGTVTSDE--DAIDDYIEAiLDKVD--VEAIRKKGFKVVVDCGNG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 268 VGHDYVQLAFKVFGFKpPIPVPEQkdPDPDFSTvkcPNPEEGESVLELSLRLAEKENARVVLATDPDADRLAAaeLQENG 347
Cdd:TIGR03990 180 AGSLTTPYLLRELGCK-VITLNCQ--PDGTFPG---RNPEPTPENLKDLSALVKATGADLGIAHDGDADRLVF--IDEKG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 348 cwKVFTGNELAALFGWWMfdcWKKNKSRnadvknvymLATTVS-SKILKAIALKEGFHFEETLpgfkwIGSRII--DLLE 424
Cdd:TIGR03990 252 --RFIGGDYTLALFAKYL---LEHGGGK---------VVTNVSsSRAVEDVAERHGGEVIRTK-----VGEVNVaeKMKE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 425 NGkeVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMasyLETMNITLkQQLVKVYEKygYHISKTSyflcYEPPTIK--S 502
Cdd:TIGR03990 313 EG--AVFGGEGNGGWIFPDHHYCRDGLMAAALFLEL---LAEEGKPL-SELLAELPK--YPMSKEK----VELPDEDkeE 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 503 IFERLRnfdspKEYPKFcgtfailhvrDVTT--GydssqpnkksvlpvsknsqmITFTFQNGCVaTLRTSGTEPKIKYYA 580
Cdd:TIGR03990 381 VMEAVE-----EEFADA----------EIDTidG--------------------VRIDFEDGWV-LVRPSGTEPIVRIYA 424
|
490 500
....*....|....*....|..
gi 31377548 581 EmcaSPDQSDTALLEEELKKLI 602
Cdd:TIGR03990 425 E---AKTEERAEELLEEGRSLV 443
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
104-602 |
2.22e-26 |
|
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: 112.28 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 104 SDFKQRGFVVGYDTRgqvtssCSSQRLAKLTAAVLLAKDVPVYLFSrYVPTPFVPYAVQKLkAVAGVMITASHNRKEDNG 183
Cdd:cd03087 29 TYLGGGTVVVGRDTR------TSGPMLKNAVIAGLLSAGCDVIDIG-IVPTPALQYAVRKL-GDAGVMITASHNPPEYNG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 184 YKVYWETGAQITSPHDKEILKCIEEcvEPWN-GSWNdnlvDTSPLKRDPlqDICRRYMED-LKKIcfyrELNSKTTLKFV 261
Cdd:cd03087 101 IKLVNPDGTEFSREQEEEIEEIIFS--ERFRrVAWD----EVGSVRRED--SAIDEYIEAiLDKV----DIDGGKGLKVV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 262 HTSFHGVGHDYVQLAFKVFGFKpPIPVPEQkdPDPDFSTvkcPNPEEGESVLELSLRLAEKENARVVLATDPDADRLAAa 341
Cdd:cd03087 169 VDCGNGAGSLTTPYLLRELGCK-VITLNAN--PDGFFPG---RPPEPTPENLSELMELVRATGADLGIAHDGDADRAVF- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 342 eLQENGcwKVFTGNELAALFGWWMfdCWKKNKSrnadvknvymLATTVS-SKILKAIALKEGFHFEETLpgfkwIGSRII 420
Cdd:cd03087 242 -VDEKG--RFIDGDKLLALLAKYL--LEEGGGK----------VVTPVDaSMLVEDVVEEAGGEVIRTP-----VGDVHV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 421 DLLENGKEVLFAFEESIGFLCGTSVLDKDGVSAAVVVAEMASYLETMNitlkqQLVKVYEKygYHISKTSYflcyeppti 500
Cdd:cd03087 302 AEEMIENGAVFGGEPNGGWIFPDHQLCRDGIMTAALLLELLAEEKPLS-----ELLDELPK--YPLLREKV--------- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 501 ksiferlrnfDSPKEYPKfcgtfAIL-HVRDVTTGYDssqpnkKSVLPVSKnsqmITFTFQNGCVaTLRTSGTEPKIKYY 579
Cdd:cd03087 366 ----------ECPDEKKE-----EVMeAVEEELSDAD------EDVDTIDG----VRIEYEDGWV-LIRPSGTEPKIRIT 419
|
490 500
....*....|....*....|...
gi 31377548 580 AEmcaSPDQSDTALLEEELKKLI 602
Cdd:cd03087 420 AE---AKTEERAKELLEEGRSKV 439
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
239-347 |
4.56e-23 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 93.89 E-value: 4.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 239 YMEDLKKICFyRELNSKTTLKFVHTSFHGVGHDYVQLAFKVFGFkppIPVPEQKDPDPDFSTvKCPNPEEGEsVLELSLR 318
Cdd:pfam02879 2 YIDHLLELVD-SEALKKRGLKVVYDPLHGVGGGYLPELLKRLGC---DVVEENCEPDPDFPT-RAPNPEEPE-ALALLIE 75
|
90 100
....*....|....*....|....*....
gi 31377548 319 LAEKENARVVLATDPDADRLAAAElqENG 347
Cdd:pfam02879 76 LVKSVGADLGIATDGDADRLGVVD--ERG 102
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
112-361 |
3.85e-18 |
|
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: 87.18 E-value: 3.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 112 VVGYDTRgqvtssCSSQRLAKLTAAVLLAKDVPVYLFSRyVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKvyWETG 191
Cdd:cd03089 40 VVGRDGR------LSSPELAAALIEGLLAAGCDVIDIGL-VPTPVLYFATFHLDADGGVMITASHNPPEYNGFK--IVIG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 192 AQITSPHD-KEILKCIEecvepwNGSWNDNLVDTSPLKRDPLQDICRRYMEDLKKicfyrelnSKTTLKFVHTSFHGVGH 270
Cdd:cd03089 111 GGPLSGEDiQALRERAE------KGDFAAATGRGSVEKVDILPDYIDRLLSDIKL--------GKRPLKVVVDAGNGAAG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 271 DYVQLAFKVFGFKppiPVPEQKDPDPDFSTvKCPNPEEGESVLELSLRLAEkENARVVLATDPDADRLAAaeLQENGcwK 350
Cdd:cd03089 177 PIAPQLLEALGCE---VIPLFCEPDGTFPN-HHPDPTDPENLEDLIAAVKE-NGADLGIAFDGDGDRLGV--VDEKG--E 247
|
250
....*....|.
gi 31377548 351 VFTGNELAALF 361
Cdd:cd03089 248 IIWGDRLLALF 258
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
353-482 |
2.26e-15 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 72.48 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 353 TGNELAALFGWWMFDcwKKNKSRNADVknvymLATTVSSKILKAIALKEGFHFEETLPGFKWIGSRiidLLENGkeVLFA 432
Cdd:pfam02880 1 DGDQILALLAKYLLE--QGKLPPGAGV-----VKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEK---MREEG--ALFG 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 31377548 433 FEESIGFLCGTSVLDKDGVSAAVVVAEMASYletMNITLKQQLVKVYEKY 482
Cdd:pfam02880 69 GEESGHIIFLDHATTKDGILAALLVLEILAR---TGKSLSELLEELPEKY 115
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
102-339 |
3.03e-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: 75.42 E-value: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 102 CFSDFKQRGFVVGYDTRGqvtsscSSQRLAKLTAAVLLA--KDVpVYLfsRYVPTPFVPYAVQKLKAVAGVMITASHNRK 179
Cdd:cd05803 31 QPERTKGGKIVVGRDGRP------SGPMLEKIVIGALLAcgCDV-IDL--GIAPTPTVQVLVRQSQASGGIIITASHNPP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 180 EDNGYKVYWETGAQITSPHDKEILKCIEECVEPWNGswNDNL--VDTSPlkrDPLQDicrrYMED-LKKICFYRELNSKT 256
Cdd:cd05803 102 QWNGLKFIGPDGEFLTPDEGEEVLSCAEAGSAQKAG--YDQLgeVTFSE---DAIAE----HIDKvLALVDVDVIKIRER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 257 TLKFVHTSFHGVGHDYV-----QL--AFKVFGFKPPIPVPEQKDPDPdfstvkcpnpeegESVLELSlRLAEKENARVVL 329
Cdd:cd05803 173 NFKVAVDSVNGAGGLLIprlleKLgcEVIVLNCEPTGLFPHTPEPLP-------------ENLTQLC-AAVKESGADVGF 238
|
250
....*....|
gi 31377548 330 ATDPDADRLA 339
Cdd:cd05803 239 AVDPDADRLA 248
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
64-607 |
1.83e-11 |
|
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100094 [Multi-domain] Cd Length: 522 Bit Score: 66.89 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 64 RMTFGTAGLR-SAMGAGFcyiNDLTVIQSTQGMYKYleRcfsdfKQRGF----VVGYDTRGQvtsscssQRLAKLTA-AV 137
Cdd:cd05801 20 RVAFGTSGHRgSSLKGSF---NEAHILAISQAICDY--R-----KSQGItgplFLGKDTHAL-------SEPAFISAlEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 138 LLAKDVPVYLFSR--YVPTPFVPYAV-----QKLKAVA-GVMITASHNRKEDNGYKVYWETGAqitsPHDKEILKCIEEC 209
Cdd:cd05801 83 LAANGVEVIIQQNdgYTPTPVISHAIltynrGRTEGLAdGIVITPSHNPPEDGGFKYNPPHGG----PADTDITRWIEKR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 210 VepwNGSWNDNLVDtspLKRDPL-----------QDICRRYMEDLKKIcfyreLN----SKTTLKFVHTSFHGVGHDYVQ 274
Cdd:cd05801 159 A---NALLANGLKG---VKRIPLeaalasgythrHDFVTPYVADLGNV-----IDmdaiRKSGLRLGVDPLGGASVPYWQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 275 LAFKVFGFKPPIPVPEQkDPDPDFSTV--------KCPNPEEGESVLELslrlaeKENARVVLATDPDADRLAAAElqen 346
Cdd:cd05801 228 PIAEKYGLNLTVVNPKV-DPTFRFMTLdhdgkirmDCSSPYAMAGLLKL------KDKFDLAFANDPDADRHGIVT---- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 347 GCWKVFTGNELAALFGWWMFdcwkknKSRNADVKNVYMLATTVSSKILKAIALKEGFHFEETLPGFKWigsrIIDLLENG 426
Cdd:cd05801 297 PSAGLMNPNHYLSVAIDYLF------THRPLWNKSAGVGKTLVSSSMIDRVAAALGRKLYEVPVGFKW----FVDGLLDG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 427 KeVLFAFEESIG--FLC--GTS-VLDKDGVSAAVVVAEMasyLETMNITLKQQLVKVYEKYGYHIsktsYFLCYEP--PT 499
Cdd:cd05801 367 S-LGFGGEESAGasFLRrdGTVwTTDKDGIIMCLLAAEI---LAVTGKDPGQLYQELTERFGEPY----YARIDAPatPE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 500 IKSIFERLrnfdSPKE-YPKFCGTFAILHVRDVTTGYDSSQPNKKsvlpvsknsqmitFTFQNGCVAtLRTSGTEPKIKY 578
Cdd:cd05801 439 QKARLKKL----SPEQvTATELAGDPILAKLTRAPGNGASIGGLK-------------VTTANGWFA-ARPSGTEDVYKI 500
|
570 580
....*....|....*....|....*....
gi 31377548 579 YAEMCASpdqsdtallEEELKKLIDALIE 607
Cdd:cd05801 501 YAESFLS---------EEHLKKIQKEAQE 520
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
111-211 |
7.69e-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: 64.43 E-value: 7.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 111 FVVGYDTRgqvtssCSSQRLAKLTAAVLLAKDVPVYLFSrYVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKVYWET 190
Cdd:cd05802 40 VLIGKDTR------ISGYMLESALAAGLTSAGVDVLLLG-VIPTPAVAYLTRKLRADAGVVISASHNPFEDNGIKFFSSD 112
|
90 100
....*....|....*....|.
gi 31377548 191 GAQItsPHDKEILkcIEECVE 211
Cdd:cd05802 113 GYKL--PDEVEEE--IEALID 129
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
112-187 |
6.80e-10 |
|
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: 61.61 E-value: 6.80e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31377548 112 VVGYDTRgqvtssCSSQRLAKLTAAVLLAKDVPVYLFSrYVPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYKVY 187
Cdd:TIGR01455 42 VIGKDTR------LSGYMLENALAAGLNSAGVDVLLLG-PLPTPAVAYLTRTLRADAGVMISASHNPYEDNGIKFF 110
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
67-204 |
1.45e-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: 51.05 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31377548 67 FGTAGLR---SAMGAGFCYINdltviqsTQGMYKYLErcfSDFKQRGFVVGYDTRGqvtsscSSQRLAKLTAAVLLAKDV 143
Cdd:cd03088 2 FGTSGLRglvTDLTDEVCYAY-------TRAFLQHLE---SKFPGDTVAVGRDLRP------SSPRIAAACAAALRDAGF 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31377548 144 -PVYLFSryVPTPFVPYAVQKLKAvAGVMITASHNRKEDNGYKVYWETGaqitsphdkEILK 204
Cdd:cd03088 66 rVVDCGA--VPTPALALYAMKRGA-PAIMVTGSHIPADRNGLKFYRPDG---------EITK 115
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
152-185 |
2.95e-05 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 46.67 E-value: 2.95e-05
10 20 30
....*....|....*....|....*....|....
gi 31377548 152 VPTPFVPYAVQKLKAVAGVMITASHNRKEDNGYK 185
Cdd:PRK10887 76 MPTPAVAYLTRTLRAEAGIVISASHNPYYDNGIK 109
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
165-186 |
5.42e-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: 5.42e-04
10 20
....*....|....*....|..
gi 31377548 165 KAVAGVMITASHNRKEDNGYKV 186
Cdd:cd03086 34 GKTIGVMITASHNPVEDNGVKI 55
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
163-186 |
9.05e-04 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 42.32 E-value: 9.05e-04
10 20
....*....|....*....|....
gi 31377548 163 KLKAVAGVMITASHNRKEDNGYKV 186
Cdd:PLN02895 55 KTGAATGLMITASHNPVSDNGVKI 78
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
552-602 |
1.04e-03 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 38.02 E-value: 1.04e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 31377548 552 SQMITFTFQNGCVATLRTSGTEPKIKYYAEmcaSPDQSDTALLEEELKKLI 602
Cdd:pfam00408 23 ADAEKILGEDGRRLDVRPSGTEPVLRVMVE---GDSDEELARLADEIADLL 70
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
555-608 |
1.05e-03 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 41.95 E-value: 1.05e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 31377548 555 ITFTFQNGCVATLRTSGTEPKIKYYAEmcaSPDQSDTALLEEELKKLIDALIEN 608
Cdd:PTZ00302 534 IVSKYDNAARAFIRPSGTEPVVRVYAE---APTLEQADELANEVKGLVLRYCSG 584
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
167-194 |
9.84e-03 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 38.87 E-value: 9.84e-03
10 20
....*....|....*....|....*...
gi 31377548 167 VAGVMITASHNRKEDNGYKVYWETGAQI 194
Cdd:PTZ00302 76 SVGVMITASHNPIQDNGVKIIDPDGGML 103
|
|
| |
