|
Name |
Accession |
Description |
Interval |
E-value |
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
3-467 |
0e+00 |
|
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: 661.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 3 IKFGTDGWRGIIADDFTFENVRYCAQAVAEHLRDRGLAPRGLVIGYDTRFASEHFAAAASEVLAANGIRVYLCPKPTPTP 82
Cdd:cd05800 1 IKFGTDGWRGIIAEDFTFENVRRVAQAIADYLKEEGGGGRGVVVGYDTRFLSEEFARAVAEVLAANGIDVYLSDRPVPTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 83 VISYGVVRQKAGGAIIITASHNPAQWNGFKIKSEDGASAPTEVEADVEARLPQIIgrgtterMPLKEALSQGLVEYLDLD 162
Cdd:cd05800 81 AVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARLASGE-------PPGLEARAEGLIETIDPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 163 PPYFQHIAKMVDLDSLRRSGLRVIVDSMYGAGDSYIKRLLDGGRIQIQEINVERNPIFPGIQPEPIARHLSKLCALVRDT 242
Cdd:cd05800 154 PDYLEALRSLVDLEAIREAGLKVVVDPMYGAGAGYLEELLRGAGVDVEEIRAERDPLFGGIPPEPIEKNLGELAEAVKEG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 243 GAHVGLATDGDADRVGIVDEGGNPLTPLQIFALLALYLLEVRGERGAIVRTVTTTSMLYRLGELYGVPVYETAVGFKHVA 322
Cdd:cd05800 234 GADLGLATDGDADRIGAVDEKGNFLDPNQILALLLDYLLENKGLRGPVVKTVSTTHLIDRIAEKHGLPVYETPVGFKYIA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 323 PKMMAENAIMGGEESSGFGFRGHVPERDGILAAMYFLDLMTRLGKSPSQLIEYLYSKVGPHHYERLDLQFPASQRETIVK 402
Cdd:cd05800 314 EKMLEEDVLIGGEESGGLGIRGHIPERDGILAGLLLLEAVAKTGKPLSELVAELEEEYGPSYYDRIDLRLTPAQKEAILE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490726200 403 RLASSPPDRIAGNAVTKVNTIDGHHFSLADGSWLLVRFSGTEPLLRMYAEASSIEKVKALIQDGR 467
Cdd:cd05800 394 KLKNEPPLSIAGGKVDEVNTIDGVKLVLEDGSWLLIRPSGTEPLLRIYAEAPSPEKVEALLDAGK 458
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
5-470 |
9.70e-155 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 447.34 E-value: 9.70e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 5 FGTDGWRGIIADDFTFENVRYCAQAVAEHLRDRGlaPRGLVIGYDTRFASEHFAAAASEVLAANGIRVYLCpKPTPTPVI 84
Cdd:COG1109 7 FGTDGIRGIVGEELTPEFVLKLGRAFGTYLKEKG--GPKVVVGRDTRLSSPMLARALAAGLASAGIDVYDL-GLVPTPAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 85 SYGVVRQKAGGAIIITASHNPAQWNGFKIKSEDGASAPTEVEADVEArlpqIIGRGTTERMPLKEalsQGLVEYL-DLDP 163
Cdd:COG1109 84 AFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEA----LIEKEDFRRAEAEE---IGKVTRIeDVLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 164 PYFQHIAKMVDlDSLRRSGLRVIVDSMYGAGDSYIKRLLDGGRIQIQEINVERNPIFPGIQPEPIARHLSKLCALVRDTG 243
Cdd:COG1109 157 AYIEALKSLVD-EALRLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFPNHNPNPEPENLEDLIEAVKETG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 244 AHVGLATDGDADRVGIVDEGGNPLTPLQIFALLALYLLEvRGERGAIVRTVTTTSMLYRLGELYGVPVYETAVGFKHVAP 323
Cdd:COG1109 236 ADLGIAFDGDADRLGVVDEKGRFLDGDQLLALLARYLLE-KGPGGTVVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 324 KMMAENAIMGGEESSGFGFRGHVPERDGILAAMYFLDLMTRLGKSPSQLIEylysKVGPHHYERLDLQFP-ASQRETIVK 402
Cdd:COG1109 315 KMRETGAVLGGEESGGIIFPDFVPTDDGILAALLLLELLAKQGKSLSELLA----ELPRYPQPEINVRVPdEEKIGAVME 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490726200 403 RLASSPPDRIagnavtKVNTIDGHHFSLADGSWLLVRFSGTEPLLRMYAEASSIEKVKALIQDGRSML 470
Cdd:COG1109 391 KLREAVEDKE------ELDTIDGVKVDLEDGGWVLVRPSGTEPLLRVYAEAKDEEEAEELLAELAELV 452
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
5-470 |
1.47e-95 |
|
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: 295.58 E-value: 1.47e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 5 FGTDGWRGIIADDFTFENVRYCAQAVAEHLRdrglaPRGLVIGYDTRFASEHFAAAASEVLAANGIRVYLCpKPTPTPVI 84
Cdd:TIGR03990 4 FGTSGIRGIVGEELTPELALKVGKAFGTYLR-----GGKVVVGRDTRTSGPMLENAVIAGLLSTGCDVVDL-GIAPTPTL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 85 SYGVVRQKAGGAIIITASHNPAQWNGFKIKSEDGasapTEVEADVEARLPQIIGRGTTERMPLKEalsQG-LVEYLDLDP 163
Cdd:TIGR03990 78 QYAVRELGADGGIMITASHNPPEYNGIKLLNSDG----TELSREQEEEIEEIAESGDFERADWDE---IGtVTSDEDAID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 164 PYFQHIAKMVDLDSLRRSGLRVIVDSMYGAGDSYIKRLLDGGRIQIQEINVERNPIFPGIQPEPIARHLSKLCALVRDTG 243
Cdd:TIGR03990 151 DYIEAILDKVDVEAIRKKGFKVVVDCGNGAGSLTTPYLLRELGCKVITLNCQPDGTFPGRNPEPTPENLKDLSALVKATG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 244 AHVGLATDGDADRVGIVDEGGNPLTPLQIFALLALYLLEVRGerGAIVRTVTTTSMLYRLGELYGVPVYETAVGFKHVAP 323
Cdd:TIGR03990 231 ADLGIAHDGDADRLVFIDEKGRFIGGDYTLALFAKYLLEHGG--GKVVTNVSSSRAVEDVAERHGGEVIRTKVGEVNVAE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 324 KMMAENAIMGGEESSGFGFRGHVPERDGILAAMYFLDLMTRLGKSPSQLIEYLyskvgPH-HYERLDLQFPASQRETIVK 402
Cdd:TIGR03990 309 KMKEEGAVFGGEGNGGWIFPDHHYCRDGLMAAALFLELLAEEGKPLSELLAEL-----PKyPMSKEKVELPDEDKEEVME 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490726200 403 RLASSPPDriagnavTKVNTIDGHHFSLADGsWLLVRFSGTEPLLRMYAEASSIEKVKALIQDGRSML 470
Cdd:TIGR03990 384 AVEEEFAD-------AEIDTIDGVRIDFEDG-WVLVRPSGTEPIVRIYAEAKTEERAEELLEEGRSLV 443
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
2-465 |
3.28e-87 |
|
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: 275.15 E-value: 3.28e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 2 PIKFGTDGWRGIIA------DDFTfenVRYCAQAVAEHLRDRG--LAPRGLVIGYDTRFASEHFAAAASEVLAANGIRVY 73
Cdd:cd05799 1 RLEFGTAGLRGKMGagtnrmNDYT---VRQATQGLANYLKKKGpdAKNRGVVIGYDSRHNSREFAELTAAVLAANGIKVY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 74 LCPKPTPTPVISYGVVRQKAGGAIIITASHNPAQWNGFKIKSEDGASAPTEVEADVEARLPQIigrGTTERMPLKEALSQ 153
Cdd:cd05799 78 LFDDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAV---LEPLDIKFEEALDS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 154 GLVEYLD--LDPPYFQHIAKM-VDLDSLRRSGLRVIVDSMYGAGDSYIKRLLDggRIQIQEINVER-----NPIFPGIQ- 224
Cdd:cd05799 155 GLIKYIGeeIDDAYLEAVKKLlVNPELNEGKDLKIVYTPLHGVGGKFVPRALK--EAGFTNVIVVEeqaepDPDFPTVKf 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 225 --PE-PIArhLSKLCALVRDTGAHVGLATDGDADRVGIV----DEGGNPLTPLQIFALLALYLLEVR------GERGAIV 291
Cdd:cd05799 233 pnPEePGA--LDLAIELAKKVGADLILATDPDADRLGVAvkdkDGEWRLLTGNEIGALLADYLLEQRkekgklPKNPVIV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 292 RTVTTTSMLYRLGELYGVPVYETAVGFKHVAPKMM-----AENAIMGGEESSGFGFRGHVPERDGILAAMYFLDLMTRL- 365
Cdd:cd05799 311 KTIVSSELLRKIAKKYGVKVEETLTGFKWIGNKIEelesgGKKFLFGFEESIGYLVGPFVRDKDGISAAALLAEMAAYLk 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 366 --GKSPSQLIEYLYSKVGPHH----YERLDLQFPASQRETIVKRLassppdRIAGNAVTkvntidghhFSLADGSWLLVR 439
Cdd:cd05799 391 aqGKTLLDRLDELYEKYGYYKektiSITFEGKEGPEKIKAIMDRL------RNNPNVLT---------FYLEDGSRVTVR 455
|
490 500
....*....|....*....|....*....
gi 1490726200 440 FSGTEPLLRMYAEA---SSIEKVKALIQD 465
Cdd:cd05799 456 PSGTEPKIKFYIEVvgkKTLEEAEKKLDA 484
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
5-470 |
1.63e-84 |
|
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: 266.74 E-value: 1.63e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 5 FGTDGWRGIIADDFTFENVRYCAQAVAEHLRDRGLaprglVIGYDTRFASEHFAAAASEVLAANGIRVYLCpKPTPTPVI 84
Cdd:cd03087 2 FGTSGIRGVVGEELTPELALKVGKALGTYLGGGTV-----VVGRDTRTSGPMLKNAVIAGLLSAGCDVIDI-GIVPTPAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 85 SYGVVRQKAGGaIIITASHNPAQWNGFKIKSEDGasapTEVEADVEARLPQIIGRGTTERMPLKEalsQGLVEYLD-LDP 163
Cdd:cd03087 76 QYAVRKLGDAG-VMITASHNPPEYNGIKLVNPDG----TEFSREQEEEIEEIIFSERFRRVAWDE---VGSVRREDsAID 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 164 PYFQHIAKMVDLDSLRrsGLRVIVDSMYGAGD---SYIKRLLdGGRIQiqEINVERNPIFPGIQPEPIARHLSKLCALVR 240
Cdd:cd03087 148 EYIEAILDKVDIDGGK--GLKVVVDCGNGAGSlttPYLLREL-GCKVI--TLNANPDGFFPGRPPEPTPENLSELMELVR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 241 DTGAHVGLATDGDADRVGIVDEGGNPLTPLQIFALLALYLLEVRGerGAIVRTVTTTSMLYRLGELYGVPVYETAVGFKH 320
Cdd:cd03087 223 ATGADLGIAHDGDADRAVFVDEKGRFIDGDKLLALLAKYLLEEGG--GKVVTPVDASMLVEDVVEEAGGEVIRTPVGDVH 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 321 VAPKMMAENAIMGGEESSGFGFRGHVPERDGILAAMYFLDLMTRlGKSPSQLIeylySKVGPHHYERLDLQFPASQRETI 400
Cdd:cd03087 301 VAEEMIENGAVFGGEPNGGWIFPDHQLCRDGIMTAALLLELLAE-EKPLSELL----DELPKYPLLREKVECPDEKKEEV 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 401 VKRLASSPPDRIAgnavtKVNTIDGHHFSLADGsWLLVRFSGTEPLLRMYAEASSIEKVKALIQDGRSML 470
Cdd:cd03087 376 MEAVEEELSDADE-----DVDTIDGVRIEYEDG-WVLIRPSGTEPKIRITAEAKTEERAKELLEEGRSKV 439
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
95-467 |
1.52e-82 |
|
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: 258.83 E-value: 1.52e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 95 GAIIITASHNPAQWNGFKIKSEDGASAPTEVEADVEARLPQIIGRGTTERMPLKEalsqglVEYLDLDPPYFQHIAKMVD 174
Cdd:cd03084 31 GGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSAVAYELGGS------VKAVDILQRYFEALKKLFD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 175 LDSLRRSGLRVIVDSMYGAGDSYIKRLLDGGRIQIQEINVERNPIFPGIQPEPIA-RHLSKLCALVRDTGAHVGLATDGD 253
Cdd:cd03084 105 VAALSNKKFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCEPDGNFGNINPDPGSeTNLKQLLAVVKAEKADFGVAFDGD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 254 ADRVGIVDEGGNPLTPLQIFALLALYLLEVRGERGAIVRTVTTTSMLYRLGELYGVPVYETAVGFKHVAPKMMAENAIMG 333
Cdd:cd03084 185 ADRLIVVDENGGFLDGDELLALLAVELFLTFNPRGGVVKTVVSSGALDKVAKKLGIKVIRTKTGFKWVGEAMQEGDVVLG 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 334 GEESSGFGFRGHVPERDGILAAMYFLDLMTRLGKSPSQLIEYLYSkvgpHHYERLDLqfpasqretivkrlassppdria 413
Cdd:cd03084 265 GEESGGVIFPEFHPGRDGISAALLLLEILANLGKSLSELFSELPR----YYYIRLKV----------------------- 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1490726200 414 gnavtkvntidghhfsladGSWLLVRFSGTEPLLRMYAEASSIEKVKALIQDGR 467
Cdd:cd03084 318 -------------------RGWVLVRASGTEPAIRIYAEADTQEDVEQIKKEAR 352
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
9-463 |
3.27e-75 |
|
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: 242.98 E-value: 3.27e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 9 GWRGIIADDFTFENVRYCAQAVAEHLRDRGLAPRgLVIGYDTRFASEHFAAAASEVLAANGIRV-YLCPKPTPTpvISYG 87
Cdd:cd05803 6 GIRGIVGEGLTPEVITRYVAAFATWQPERTKGGK-IVVGRDGRPSGPMLEKIVIGALLACGCDViDLGIAPTPT--VQVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 88 VVRQKAGGAIIITASHNPAQWNGFKIKSEDGA-SAPTEVEadveaRLPQIIGRGTTERMPLKEALSqgLVEYLDLDPPYF 166
Cdd:cd05803 83 VRQSQASGGIIITASHNPPQWNGLKFIGPDGEfLTPDEGE-----EVLSCAEAGSAQKAGYDQLGE--VTFSEDAIAEHI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 167 QHIAKMVDLDS--LRRSGLRVIVDSMYGAGDSYIKRLLDGGRIQIQEINVERNPIFPgIQPEPIARHLSKLCALVRDTGA 244
Cdd:cd05803 156 DKVLALVDVDVikIRERNFKVAVDSVNGAGGLLIPRLLEKLGCEVIVLNCEPTGLFP-HTPEPLPENLTQLCAAVKESGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 245 HVGLATDGDADRVGIVDEGGNPLTPLQIFALLALYLLEVRGERGAIVRTVTTTSMLYRLGELYGVPVYETAVGFKHVAPK 324
Cdd:cd05803 235 DVGFAVDPDADRLALVDEDGRPIGEEYTLALAVDYVLKYGGRKGPVVVNLSTSRALEDIARKHGVPVFRSAVGEANVVEK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 325 MMAENAIMGGEESSGfgfrGHVPE----RDGILAAMYFLDLMTRLGKSPSQLIEYLyskvgPHHY---ERLDLqfPASQR 397
Cdd:cd05803 315 MKEVDAVIGGEGNGG----VILPDvhygRDSLVGIALVLQLLAASGKPLSEIVDEL-----PQYYiskTKVTI--AGEAL 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490726200 398 ETIVKRLASSPPDriagnavTKVNTIDGHHFSLADgSWLLVRFSGTEPLLRMYAEASSIEKVKALI 463
Cdd:cd05803 384 ERLLKKLEAYFKD-------AEASTLDGLRLDSED-SWVHVRPSNTEPIVRIIAEAPTQDEAEALA 441
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
11-470 |
7.15e-70 |
|
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: 228.94 E-value: 7.15e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 11 RGIIADDFTFENVRYCAQAVAEHLRDRGlaPRGLVIGYDTRFASEHFAAAASEVLAANGIRVY---LCPkptpTPVISYG 87
Cdd:cd03089 8 RGIAGEELTEEIAYAIGRAFGSWLLEKG--AKKVVVGRDGRLSSPELAAALIEGLLAAGCDVIdigLVP----TPVLYFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 88 VVRQKAGGAIIITASHNPAQWNGFKIKSEDGASAPTEVEAdvearLPQIIGRGttermPLKEALSQGLVEYLDLDPPYFQ 167
Cdd:cd03089 82 TFHLDADGGVMITASHNPPEYNGFKIVIGGGPLSGEDIQA-----LRERAEKG-----DFAAATGRGSVEKVDILPDYID 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 168 HIAKMVDLDSlrrSGLRVIVDSMYGAGDSYIKRLLDGGRIQIQEINVERNPIFPGIQPEP-IARHLSKLCALVRDTGAHV 246
Cdd:cd03089 152 RLLSDIKLGK---RPLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCEPDGTFPNHHPDPtDPENLEDLIAAVKENGADL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 247 GLATDGDADRVGIVDEGGNPLTPLQIFALLALYLLEvrGERGA-IVRTVTTTSMLYRL-GELYGVPVYeTAVGFKHVAPK 324
Cdd:cd03089 229 GIAFDGDGDRLGVVDEKGEIIWGDRLLALFARDILK--RNPGAtIVYDVKCSRNLYDFiEEAGGKPIM-WKTGHSFIKAK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 325 MMAENAIMGGEESSGFGFRghvpER-----DGILAAMYFLDLMTRLGKSPSQLIEYLyskvgPHHYERLDLQFPASQRE- 398
Cdd:cd03089 306 MKETGALLAGEMSGHIFFK----DRwygfdDGIYAALRLLELLSKSGKTLSELLADL-----PKYFSTPEIRIPVTEEDk 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490726200 399 -TIVKRLASSPPDRIAgnavtKVNTIDGHHFSLADGsWLLVRFSGTEPLLRMYAEASSIEKVKALIQDGRSML 470
Cdd:cd03089 377 fAVIERLKEHFEFPGA-----EIIDIDGVRVDFEDG-WGLVRASNTEPVLVLRFEADTEEGLEEIKAELRKLL 443
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
4-452 |
4.97e-62 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 210.76 E-value: 4.97e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 4 KFGTDGWRGIiADDFTF-EN-VRYCAQAVAEHLRDRGLA-PrgLVIGYDTRFASEHFAAAASEVLAANGIRVYLCPK--P 78
Cdd:PRK07564 39 KFGTSGHRGS-SLQPSFnENhILAIFQAICEYRGKQGITgP--LFVGGDTHALSEPAIQSALEVLAANGVGVVIVGRggY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 79 TPTPVIS-----YGVVRQKAGGAIIITASHNPAQWNGFKIKSEDGASAPTEVEADVEARLPQIIGRGTTE--RMPLKEAL 151
Cdd:PRK07564 116 TPTPAVShailkYNGRGGGLADGIVITPSHNPPEDGGIKYNPPNGGPADTDVTDAIEARANELLAYGLKGvkRIPLDRAL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 152 SQGLVEYLDLDPPYFQHIAKMVDLDSLRRSGLRVIVDSMYGAGDSYIKRLLDGGRIQIQEINVERNPIF---P-----GI 223
Cdd:PRK07564 196 ASMTVEVIDPVADYVEDLENVFDFDAIRKAGLRLGVDPLGGATGPYWKAIAERYGLDLTVVNAPVDPTFnfmPldddgKI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 224 QPEPIARH-LSKLCALvRDtGAHVGLATDGDADRVGIVDEGGnPLTPLQIFALLALYLLEVR---GERGAIVRTVTTTSM 299
Cdd:PRK07564 276 RMDCSSPYaMAGLLAL-KD-AFDLAFANDPDGDRHGIVTPGG-LMNPNHYLAVAIAYLFHHRpgwRAGAGVGKTLVSSAM 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 300 LYRLGELYGVPVYETAVGFKHVAPKMMAENAIMGGEESSGFGFRG-----HVPERDGILAAMYFLDLMTRLGKSPSQLIE 374
Cdd:PRK07564 353 IDRVAAKLGRKLYEVPVGFKWFVNGLDDGSLGFGGEESAGASFLRrdgsvWTTDKDGLIAVLLAAEILAVTGKSPSEIYR 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 375 YLYSKVGPHHYERLDLQFPASQRETIVKRLASSP-PDRIAGNAVTKVNT--------IDGHHFSLADGsWLLVRFSGTEP 445
Cdd:PRK07564 433 ELWARFGRPYYSRHDAPATPEQKAALRKLSPELVgATELAGDPIDASLTeapgngaaIGGLKVVTENG-WFAARPSGTET 511
|
....*..
gi 1490726200 446 LLRMYAE 452
Cdd:PRK07564 512 TYKIYAE 518
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
5-465 |
7.16e-59 |
|
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: 199.63 E-value: 7.16e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 5 FGTDGWRGIIADDFTFENVRYCAQAVAEHLRDRGLAPRgLVIGYDTRFASEHFAAAASEVLAANGIRVYLCpKPTPTPVI 84
Cdd:cd05802 2 FGTDGIRGVANEPLTPELALKLGRAAGKVLGKGGGRPK-VLIGKDTRISGYMLESALAAGLTSAGVDVLLL-GVIPTPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 85 SYGVVRQKAGGAIIITASHNPAQWNGFKIKSEDGASAPTEVEADVEARL-------PQIIGRGTTERMPlkEALSQglve 157
Cdd:cd05802 80 AYLTRKLRADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVEEEIEALIdkelelpPTGEKIGRVYRID--DARGR---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 158 yldldppYFQHIAKMVDLDSLrrSGLRVIVDSMYGAGDSYIKRLLDGGRIQIQEINVE---RNpifpgiqpepI-----A 229
Cdd:cd05802 154 -------YIEFLKSTFPKDLL--SGLKIVLDCANGAAYKVAPEVFRELGAEVIVINNApdgLN----------InvncgS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 230 RHLSKLCALVRDTGAHVGLATDGDADRVGIVDEGGNPLTPLQIFALLALYLLEvRGE--RGAIVRTVTTTSMLYRLGELY 307
Cdd:cd05802 215 THPESLQKAVLENGADLGIAFDGDADRVIAVDEKGNIVDGDQILAICARDLKE-RGRlkGNTVVGTVMSNLGLEKALKEL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 308 GVPVYETAVGFKHVAPKMMAENAIMGGEESsgfgfrGHV------PERDGILAAMYFLDLMTRLGKSPSQLIEylyskvg 381
Cdd:cd05802 294 GIKLVRTKVGDRYVLEEMLKHGANLGGEQS------GHIifldhsTTGDGLLTALQLLAIMKRSGKSLSELAS------- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 382 phhyerlDLQ-FPASQRE-TIVKRLASSPPDRIAgNAVTKVNTIdghhfsLADGSWLLVRFSGTEPLLRMYAEASSIEKV 459
Cdd:cd05802 361 -------DMKlYPQVLVNvRVKDKKALLENPRVQ-AAIAEAEKE------LGGEGRVLVRPSGTEPLIRVMVEGEDEELV 426
|
....*.
gi 1490726200 460 KALIQD 465
Cdd:cd05802 427 EKLAEE 432
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
3-470 |
1.40e-58 |
|
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: 201.32 E-value: 1.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 3 IKFGTDGWRG-IIADDFTFENVRYCAQAVAEHLRDRGL-APrgLVIGYDTRFASEHFAAAASEVLAANGIRVYLCPK--P 78
Cdd:cd05801 21 VAFGTSGHRGsSLKGSFNEAHILAISQAICDYRKSQGItGP--LFLGKDTHALSEPAFISALEVLAANGVEVIIQQNdgY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 79 TPTPVISYGVV-------RQKAGGaIIITASHNPAQWNGFKIKSEDGASAPTEVEADVEARLPQIIGRG--TTERMPLKE 149
Cdd:cd05801 99 TPTPVISHAILtynrgrtEGLADG-IVITPSHNPPEDGGFKYNPPHGGPADTDITRWIEKRANALLANGlkGVKRIPLEA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 150 ALSQGLVEYLDLDPPYFQHIAKMVDLDSLRRSGLRVIVDSMYGAGDSYIKRLLDGGRIQIQEINVERNPIFPGIQPE--- 226
Cdd:cd05801 178 ALASGYTHRHDFVTPYVADLGNVIDMDAIRKSGLRLGVDPLGGASVPYWQPIAEKYGLNLTVVNPKVDPTFRFMTLDhdg 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 227 --------PIArhLSKLCALvRDTgAHVGLATDGDADRVGIVDEGGNPLTPLQIFALLALYLLEVR---GERGAIVRTVT 295
Cdd:cd05801 258 kirmdcssPYA--MAGLLKL-KDK-FDLAFANDPDADRHGIVTPSAGLMNPNHYLSVAIDYLFTHRplwNKSAGVGKTLV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 296 TTSMLYRLGELYGVPVYETAVGFKHVAPKMMAENAIMGGEESSGFGF---RGHV--PERDGILAAMYFLDLMTRLGKSPS 370
Cdd:cd05801 334 SSSMIDRVAAALGRKLYEVPVGFKWFVDGLLDGSLGFGGEESAGASFlrrDGTVwtTDKDGIIMCLLAAEILAVTGKDPG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 371 QLIEYLYSKVGPHHYERLDLqfPAS-QRETIVKRLAsspPDRI-----AGNAVTKVNT--------IDGHHFSLADGsWL 436
Cdd:cd05801 414 QLYQELTERFGEPYYARIDA--PATpEQKARLKKLS---PEQVtatelAGDPILAKLTrapgngasIGGLKVTTANG-WF 487
|
490 500 510
....*....|....*....|....*....|....*
gi 1490726200 437 LVRFSGTEPLLRMYAEA-SSIEKVKALIQDGRSML 470
Cdd:cd05801 488 AARPSGTEDVYKIYAESfLSEEHLKKIQKEAQEIV 522
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
5-462 |
2.24e-50 |
|
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: 177.56 E-value: 2.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 5 FGTDGWRGIiADDF--TFENVRYCAQAVAEHLRDRGLAPRGLVIGYDTRFASEHFAAAASEVLAANGIRVYLCpKPTPTP 82
Cdd:TIGR01455 1 FGTDGVRGR-AGQEplTAELALLLGAAAGRVLRQGRDTAPRVVIGKDTRLSGYMLENALAAGLNSAGVDVLLL-GPLPTP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 83 VISYGVVRQKAGGAIIITASHNPAQWNGFKIKSEDGASAPTEVEADVEARLPqiiGRGTTERmPLKEALSQgLVEYLDLD 162
Cdd:TIGR01455 79 AVAYLTRTLRADAGVMISASHNPYEDNGIKFFGPGGFKLDDATEAAIEALLD---EADPLPR-PESEGLGR-VKRYPDAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 163 PPYFQHIAKMVDlDSLRRSGLRVIVDSMYGAGDSYIKRLLDGGRIQIQEINVERNPIfpGIQPEPIARHLSKLCALVRDT 242
Cdd:TIGR01455 154 GRYIEFLKSTLP-RGLTLSGLKVVLDCANGAAYKVAPHVFRELGAEVIAIGVEPDGL--NINDGCGSTHLDALQKAVREH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 243 GAHVGLATDGDADRVGIVDEGGNPLTPLQIFALLALYLLEvRGE--RGAIVRTVTTTSMLYRLGELYGVPVYETAVGFKH 320
Cdd:TIGR01455 231 GADLGIAFDGDADRVLAVDANGRIVDGDQILYIIARALKE-SGElaGNTVVATVMSNLGLERALEKLGLTLIRTAVGDRY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 321 VAPKMMAENAIMGGEESSGFGFRGHVPERDGILAAMYFLDLMTRLGKSPSQlieyLYSKVGPhhyerldlqFPASQRETI 400
Cdd:TIGR01455 310 VLEEMRESGYNLGGEQSGHIILLDYSTTGDGIVSALQVLTIMKKSGSTLSE----LAAEFVP---------YPQTLVNVR 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490726200 401 VK----RLASSPPDRIAGNAVTKvntidghhfSLADGSWLLVRFSGTEPLLRMYAEASSIEKVKAL 462
Cdd:TIGR01455 377 VAdrklAAAEAPAVKAAIEDAEA---------ELGGTGRILLRPSGTEPLIRVMVEAADEELVQQL 433
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
3-458 |
2.37e-44 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 163.70 E-value: 2.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 3 IKFGTDGWRGIIADDFTFEN---VRYCAQAVAEHLRD---RGLAPRGLVIGYDTRFASEHFAAAASEVLAANGIRVYLCP 76
Cdd:PTZ00150 45 MEFGTAGLRGKMGAGFNCMNdltVQQTAQGLCAYVIEtfgQALKSRGVVIGYDGRYHSRRFAEITASVFLSKGFKVYLFG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 77 KPTPTPVISYGVVRQKAGGAIIITASHNPAQWNGFKIKSEDGAS--APTEVE--ADVEARLPqiigrgttermPLKEA-- 150
Cdd:PTZ00150 125 QTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVYWSNGAQiiPPHDKNisAKILSNLE-----------PWSSSwe 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 151 -LSQGLVE--YLDLDPPYFQHIAKMVDLDSLRRSGLRVIVDSMYGAGDSYIKRLLD----GGRIQIQEiNVERNPIFPGI 223
Cdd:PTZ00150 194 yLTETLVEdpLAEVSDAYFATLKSEYNPACCDRSKVKIVYTAMHGVGTRFVQKALHtvglPNLLSVAQ-QAEPDPEFPTV 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 224 Q---PEPIARHLSKLCALVRDTGAHVGLATDGDADRVGIVDEGGNP---LTPLQIFALLALYLLEVRGERG------AIV 291
Cdd:PTZ00150 273 TfpnPEEGKGALKLSMETAEAHGSTVVLANDPDADRLAVAEKLNNGwkiFTGNELGALLAWWAMKRYRRQGidkskcFFI 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 292 RTVTTTSMLYRLGELYGVPVYETAVGFKHV---APKMMAEN---AIMGGEESSGFGFRGHVPERDGILAAMYFLDLMTRL 365
Cdd:PTZ00150 353 CTVVSSRMLKKMAEKEGFQYDETLTGFKWIgnkAIELNAENgltTLFAYEEAIGFMLGTRVRDKDGVTAAAVVAEMALYL 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 366 ---GKSPSQLIEYLYSKVGPH-----HYERLDlqfpASQRETIVKRLASSP--PDRIAGNAVTKV---------NTIDGH 426
Cdd:PTZ00150 433 yerGKTLVEHLESLYKQYGYHftnnsYYICYD----PSRIVSIFNDIRNNGsyPTKLGGYPVTRIrdlttgydtATPDGK 508
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1490726200 427 H------------FSLADGSWLLVRFSGTEPLLRMYAEASSIEK 458
Cdd:PTZ00150 509 PllpvsastqmitFYFENGAIITIRGSGTEPKLKWYAELSGTKD 552
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
11-465 |
4.35e-44 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 160.53 E-value: 4.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 11 RGIIADDFTFENVRYCAQAVAEHLRDRGlAPRgLVIGYDTRFASEHFAAAASEVLAANG---IRVYLCPkptpTPVISYG 87
Cdd:PRK09542 7 RGVVGEQIDEDLVRDVGAAFARLMRAEG-ATT-VVIGHDMRDSSPELAAAFAEGVTAQGldvVRIGLAS----TDQLYFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 88 VVRQKAGGAIIiTASHNPAQWNGFKIkSEDGAsAP-------TEVEADVEARLPQIIG-RGT-TERmplkealsqglvey 158
Cdd:PRK09542 81 SGLLDCPGAMF-TASHNPAAYNGIKL-CRAGA-KPvgqdtglAAIRDDLIAGVPAYDGpPGTvTER-------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 159 lDLDPPYFQHIAKMVDLDSLRRsgLRVIVDSMYGAGDSYIKRLLDGGRIQIQEINVERNPIFPGIQPEPI-ARHLSKLCA 237
Cdd:PRK09542 144 -DVLADYAAFLRSLVDLSGIRP--LKVAVDAGNGMGGHTVPAVLGGLPITLLPLYFELDGTFPNHEANPLdPANLVDLQA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 238 LVRDTGAHVGLATDGDADRVGIVDEGGNPLTPLQIFALLALYLLEvRGERGAIVRTVTTTSMLYRL-GELYGVPVyETAV 316
Cdd:PRK09542 221 FVRETGADIGLAFDGDADRCFVVDERGQPVSPSAVTALVAARELA-REPGATIIHNLITSRAVPELvAERGGTPV-RTRV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 317 GFKHVAPKMMAENAIMGGEESSGFGFRGHVPERDGILAAMYfldLMTRLGKSPSQLIEYLyskvgpHHYERL----DLQF 392
Cdd:PRK09542 299 GHSFIKALMAETGAIFGGEHSAHYYFRDFWGADSGMLAALH---VLAALGEQDRPLSELM------ADYQRYaasgEINS 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490726200 393 PASQRETIVKRLASSPPDRIAGnavtkVNTIDGHHFSLADGSWLLVRFSGTEPLLRMYAEASSIEKVKALIQD 465
Cdd:PRK09542 370 TVADAPARMEAVLKAFADRIVS-----VDHLDGVTVDLGDGSWFNLRASNTEPLLRLNVEARTEEEVDALVDE 437
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
2-136 |
7.33e-37 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 132.35 E-value: 7.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 2 PIKFGTDGWRGII-ADDFTFENVRYCAQAVAEHLRDRGLAPRgLVIGYDTRFASEHFAAAASEVLAANGIRVYLcPKPTP 80
Cdd:pfam02878 1 RQLFGTSGIRGKVgVGELTPEFALKLGQAIASYLRAQGGGGK-VVVGRDTRYSSRELARALAAGLASNGVEVIL-LGLLP 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1490726200 81 TPVISYGVVRQKAGGAIIITASHNPAQWNGFKIKSEDGASAPTEVEADVEARLPQI 136
Cdd:pfam02878 79 TPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKE 134
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
271-379 |
1.01e-32 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 120.25 E-value: 1.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 271 QIFALLALYLLEVRGERG--AIVRTVTTTSMLYRLGELYGVPVYETAVGFKHVAPKMMAENAIMGGEESSGFGFRGHVPE 348
Cdd:pfam02880 4 QILALLAKYLLEQGKLPPgaGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLDHATT 83
|
90 100 110
....*....|....*....|....*....|.
gi 1490726200 349 RDGILAAMYFLDLMTRLGKSPSQLIEYLYSK 379
Cdd:pfam02880 84 KDGILAALLVLEILARTGKSLSELLEELPEK 114
|
|
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
79-465 |
1.23e-29 |
|
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose pyrophosphorylase, is a bifunctional enzyme with both phosphomannose isomerase (PMI) activity and GDP-mannose phosphorylase (GMP) activity. The protein contains an N-terminal NTP transferase domain, an L-beta-H domain, and a C-terminal PGM-like domain that belongs to the alpha-D-phosphohexomutase superfamily. This subfamily is limited to bacteria and archaea. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this group appear to lack conserved residues necessary for metal binding and catalytic activity. Other 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: 100097 Cd Length: 441 Bit Score: 120.43 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 79 TPTPVISYGVVRQKAGGAIIITASHNPAQWNGFKIKSEDGASAPTEVEADVE----------ARLPQIigrGTTERMPlk 148
Cdd:cd05805 71 LPLPVARYAIRFLGASGGIHVRTSPDDPDKVEIEFFDSRGLNISRAMERKIEnaffredfrrAHVDEI---GDITEPP-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 149 ealsqGLVEYldldppYFQHIAKMVDLDSLRRSGLRVIVDSMYGAGDSYIKRLLDGGRIQIQEINVERNPIFPgIQPEPI 228
Cdd:cd05805 146 -----DFVEY------YIRGLLRALDTSGLKKSGLKVVIDYAYGVAGIVLPGLLSRLGCDVVILNARLDEDAP-RTDTER 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 229 ARHLSKLCALVRDTGAHVGLATDGDADRVGIVDEGGNPLTPLQIFALLALYLLEVRGeRGAIVRTVTTTSMLYRLGELYG 308
Cdd:cd05805 214 QRSLDRLGRIVKALGADFGVIIDPNGERLILVDEAGRVISDDLLTALVSLLVLKSEP-GGTVVVPVTAPSVIEQLAERYG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 309 VPV--YETAVGFKHVApkmMAENAIMGGEESSGFGFRGHVPERDGILAAMYFLDLMTRLGKSPSQLIEYLyskvgPH-HY 385
Cdd:cd05805 293 GRVirTKTSPQALMEA---ALENVVLAGDGDGGFIFPEFHPGFDAIAALVKILEMLARTNISLSQIVDEL-----PRfYV 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 386 ERLDLQFPASQRETIVKRLASSPPDRiagnavtKVNTIDG---HHfslaDGSWLLVRFSGTEPLLRMYAEASSIEKVKAL 462
Cdd:cd05805 365 LHKEVPCPWEAKGRVMRRLIEEAPDK-------SIELIDGvkiYE----DDGWVLVLPDADEPLCHIYAEGSDQERAEEL 433
|
...
gi 1490726200 463 IQD 465
Cdd:cd05805 434 TEF 436
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
28-470 |
4.31e-28 |
|
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate (G-1-P) and glucose-6-phosphate (G-6-P) via a glucose 1,6-diphosphate intermediate, an important metabolic step in prokaryotes and eukaryotes. In one direction, G-1-P produced from sucrose catabolism is converted to G-6-P, the first intermediate in glycolysis. In the other direction, conversion of G-6-P to G-1-P generates a substrate for synthesis of UDP-glucose which is required for synthesis of a variety of cellular constituents including cell wall polymers and glycoproteins. The PGM1 family also includes a non-enzymatic PGM-related protein (PGM-RP) thought to play a structural role in eukaryotes, as well as pp63/parafusin, a phosphoglycoprotein that plays an important role in calcium-regulated exocytosis in ciliated protozoans. PGM1 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 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: 100087 [Multi-domain] Cd Length: 548 Bit Score: 116.94 E-value: 4.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 28 QAVAEHLRDRGLAPRGLVIGYDTRFASEHFAAAASEVLAANGIRVYLCPKPT--PTPVISYGVVRQKAGGAIIITASHNP 105
Cdd:cd03085 36 QSIFNALPPEKLKGATLVVGGDGRYYNKEAIQIIIKIAAANGVGKVVVGQNGllSTPAVSAVIRKRKATGGIILTASHNP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 106 AQWNG-FKIK--SEDGASAP-----------TEVEADVEARLPQI----IGRGTTERMPLkealsqgLVEYLDLDPPYFQ 167
Cdd:cd03085 116 GGPEGdFGIKynTSNGGPAPesvtdkiyeitKKITEYKIADDPDVdlskIGVTKFGGKPF-------TVEVIDSVEDYVE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 168 HIAKMVDLDSLR----RSGLRVIVDSMYGAGDSYIKRLLdGGRIQIQE---INVERNPIFPGIQPEPIARHLSKLCALVR 240
Cdd:cd03085 189 LMKEIFDFDAIKkllsRKGFKVRFDAMHGVTGPYAKKIF-VEELGAPEssvVNCTPLPDFGGGHPDPNLTYAKDLVELMK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 241 DTGAHVGLATDGDADRVGIVDEGGNpLTPLQIFALLALYLLEV-----RGERGaIVRTVTTTSMLYRLGELYGVPVYETA 315
Cdd:cd03085 268 SGEPDFGAASDGDGDRNMILGKGFF-VTPSDSVAVIAANAKLIpyfykGGLKG-VARSMPTSGALDRVAKKLGIPLFETP 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 316 VGFKHVAPKMMAENAIMGGEESSGFGfRGHVPERDGILAAMYFLDLMTRLGKSPSQLIEYLYSKVGPHHYERLDLQFPAS 395
Cdd:cd03085 346 TGWKFFGNLMDAGKLSLCGEESFGTG-SDHIREKDGLWAVLAWLSILAHRNVSVEDIVKEHWQKYGRNFYTRYDYEEVDS 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 396 QR-----ETIVKRLASSPPDRIAGNAVTKVNTID----------------GHHFSLADGSWLLVRFSGTE---PLLRMYA 451
Cdd:cd03085 425 EAankmmDHLRALVSDLPGVGKSGDKGYKVAKADdfsytdpvdgsvskkqGLRIIFEDGSRIIFRLSGTGssgATIRLYI 504
|
490 500
....*....|....*....|
gi 1490726200 452 EasSIEKVKALI-QDGRSML 470
Cdd:cd03085 505 E--SYEKDPSKYgLDAQVAL 522
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
164-264 |
3.20e-27 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 104.68 E-value: 3.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 164 PYFQHIAKMVDLDSLRRSGLRVIVDSMYGAGDSYIKRLLDGGRIQIQEINVERNPIFPGIQPEPIAR-HLSKLCALVRDT 242
Cdd:pfam02879 1 AYIDHLLELVDSEALKKRGLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDPDFPTRAPNPEEPeALALLIELVKSV 80
|
90 100
....*....|....*....|..
gi 1490726200 243 GAHVGLATDGDADRVGIVDEGG 264
Cdd:pfam02879 81 GADLGIATDGDADRLGVVDERG 102
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
5-464 |
2.20e-26 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 111.00 E-value: 2.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 5 FGTDGWRG-----IIADDFtfenVRYCAQAVAEHLRDRGlAPRgLVIGYDTR-------------FASEhfaaaasevla 66
Cdd:PRK10887 4 FGTDGIRGkvgqaPITPDF----VLKLGWAAGKVLARQG-RPK-VLIGKDTRisgymlesaleagLAAA----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 67 anGIRVYLCpKPTPTPVISYGVVRQKAGGAIIITASHNPAQWNGFKIKSEDGASAPTEVEADVEARLPQiigrgttermP 146
Cdd:PRK10887 67 --GVDVLLT-GPMPTPAVAYLTRTLRAEAGIVISASHNPYYDNGIKFFSADGTKLPDEVELAIEAELDK----------P 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 147 LKEALSQGL--VEYLDlDPPY---------FQHiakmvdldSLRRSGLRVIVDSMYGAGdsYikrlldggriQI-----Q 210
Cdd:PRK10887 134 LTCVESAELgkASRIN-DAAGryiefckstFPN--------ELSLRGLKIVVDCANGAT--Y----------HIapnvfR 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 211 EINVERNPIfpGIQPEPI-------ARHLSKLCALVRDTGAHVGLATDGDADRVGIVDEGGNPLTPLQIFALLALYLLEV 283
Cdd:PRK10887 193 ELGAEVIAI--GCEPNGLnindecgATDPEALQAAVLAEKADLGIAFDGDGDRVIMVDHLGNLVDGDQLLYIIARDRLRR 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 284 RGERGAIVRTVTTT-SMLYRLGELyGVPVYETAVGFKHVAPKMMAENAIMGGEESsgfgfrGHVPER------DGILAAM 356
Cdd:PRK10887 271 GQLRGGVVGTLMSNmGLELALKQL-GIPFVRAKVGDRYVLEKLQEKGWRLGGENS------GHILCLdktttgDGIVAAL 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 357 YFLDLMTRLGKSPSQLIeylyskvgphhyERLDLqFPasQReTIVKRLASSPPDRIAGNAVTKVntIDGHHFSLADGSWL 436
Cdd:PRK10887 344 QVLAAMVRSGMSLADLC------------SGMKL-FP--QV-LINVRFKPGADDPLESEAVKAA--LAEVEAELGGRGRV 405
|
490 500
....*....|....*....|....*...
gi 1490726200 437 LVRFSGTEPLLRMYAEASSIEKVKALIQ 464
Cdd:PRK10887 406 LLRKSGTEPLIRVMVEGEDEAQVTALAE 433
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
4-466 |
1.59e-21 |
|
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: 96.89 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 4 KFGTDGWRGIiADDFTFENVRYCAQAVAEHLRDRGLApRGLVIGYDTRFASEHFAAAASEVLAANGIRVYLCpKPTPTPV 83
Cdd:cd03088 1 KFGTSGLRGL-VTDLTDEVCYAYTRAFLQHLESKFPG-DTVAVGRDLRPSSPRIAAACAAALRDAGFRVVDC-GAVPTPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 84 ISYgVVRQKAGGAIIITASHNPAQWNGFKIKSEDGasaptEV----EADVEARLPQIIGRGTTERMPLKEALSQGLVEYl 159
Cdd:cd03088 78 LAL-YAMKRGAPAIMVTGSHIPADRNGLKFYRPDG-----EItkadEAAILAALVELPEALFDPAGALLPPDTDAADAY- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 160 dldppyfqhIAKMVDL---DSLrrSGLRVIVDSMYGAGDSYIKRLLD--GGRIqiqeINVERNPIF-P----GIQPEPIA 229
Cdd:cd03088 151 ---------IARYTDFfgaGAL--KGLRIGVYQHSSVGRDLLVRILEalGAEV----VPLGRSDTFiPvdteAVRPEDRA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 230 RhlskLCALVRDTGAHVGLATDGDADRVGIVDEGGNPLtPLQIFALL-ALYLlevrgERGAIVRTVTTTSMLYRLGelYG 308
Cdd:cd03088 216 L----AAAWAAEHGLDAIVSTDGDGDRPLVADETGEWL-RGDILGLLtARFL-----GADTVVTPVSSNSAIELSG--FF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 309 VPVYETAVGFKHVAPKMMAE-----NAIMGGEESSGF--GFRGHV--------PERDGILAAMYFLDLMTRLGKSPSQLI 373
Cdd:cd03088 284 KRVVRTRIGSPYVIAAMAEAaaagaGRVVGYEANGGFllGSDIERngrtlkalPTRDAVLPILAVLAAAKEAGIPLSELV 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 374 EYLyskvgPHHY---ERLDlQFPASQRETIVKRLASSPPDR-----IAGNAVTKVNTIDGHHFSLADGSWLLVRFSGTEP 445
Cdd:cd03088 364 ASL-----PARFtasDRLQ-NFPTEKSQALIARLSADPEARaafffALGGEVASIDTTDGLRMTFANGDIVHLRPSGNAP 437
|
490 500
....*....|....*....|.
gi 1490726200 446 LLRMYAEASSIEKVKALIQDG 466
Cdd:cd03088 438 ELRCYVEADSEERARELLARG 458
|
|
| PLN02307 |
PLN02307 |
phosphoglucomutase |
2-452 |
5.08e-21 |
|
phosphoglucomutase
Pssm-ID: 177942 [Multi-domain] Cd Length: 579 Bit Score: 95.88 E-value: 5.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 2 PI---KFGTDGWRGIIADdFTFENvrYCA---QAVAEHLRDRGLAPRGLVIGYDTRFASEHFAAAASEVLAANGIRVYLC 75
Cdd:PLN02307 19 PIegqKPGTSGLRKKVKV-FMQEN--YLAnfvQALFNALPAEKVKGATLVLGGDGRYFNKEAIQIIIKIAAANGVRRVWV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 76 PKPT--PTPVISyGVVR----QKAGGAIIITASHNPA----QWnGFKIKSEDGASAPteveadvEARLPQIIGRGTT--- 142
Cdd:PLN02307 96 GQNGllSTPAVS-AVIRerdgSKANGGFILTASHNPGgpeeDF-GIKYNYESGQPAP-------ESITDKIYGNTLTike 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 143 ----ERMPLKEALSQGLVEYLDLDP-------PYFQHIAKM---VDLDSLR----RSGLRVIVDSMYGAGDSYIKRLLdg 204
Cdd:PLN02307 167 ykmaEDIPDVDLSAVGVTKFGGPEDfdvevidPVEDYVKLMksiFDFELIKkllsRPDFTFCFDAMHGVTGAYAKRIF-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 205 griqIQE--------INVERNPIFPGIQPEP---IARHLSKLCALVRD----TGAHVGLATDGDADRVGIVdegGNP--L 267
Cdd:PLN02307 245 ----VEElgapesslLNCVPKEDFGGGHPDPnltYAKELVKRMGLGKTsygdEPPEFGAASDGDGDRNMIL---GKRffV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 268 TPLQIFALLALYLLEV----RGERGAIVRTVTTTSMLYRLGELYGVPVYETAVGFKHVAPKMMAENAIMGGEESSGFGfR 343
Cdd:PLN02307 318 TPSDSVAIIAANAQEAipyfSGGLKGVARSMPTSAALDVVAKKLNLPFFEVPTGWKFFGNLMDAGKLSICGEESFGTG-S 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 344 GHVPERDGILAAMYFLDLMTRLGK---------SPSQLIEYLYSKVGPHHYERLDLQFPASQR-----ETIVKRLASSPP 409
Cdd:PLN02307 397 DHIREKDGIWAVLAWLSILAHKNKdvlpggklvTVEDIVREHWATYGRNFYSRYDYENVDSEAankmmDHLRDLVNKSKK 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 410 DRIAGNAVTK-------VNTIDGH-------HFSLADGSWLLVRFSGTE---PLLRMYAE 452
Cdd:PLN02307 477 GIKYGVYTLAfaddfeyTDPVDGSvsskqgiRFLFTDGSRIIFRLSGTGsagATIRLYIE 536
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
39-470 |
9.89e-21 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 94.24 E-value: 9.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 39 LAPRGLVIGYDTRFASEHFAAAASEVLAANGIRVyLCPKPTPTPVISYGVVRQKAGGAIIITASHNPAQWNGFKIKSEdG 118
Cdd:PRK15414 36 LKPKTIVLGGDVRLTSETLKLALAKGLQDAGVDV-LDIGMSGTEEIYFATFHLGVDGGIEVTASHNPMDYNGMKLVRE-G 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 119 ASApteVEADVEARLPQIIGRGTTerMPLKEALSQGLVEYLDLDPPYFQHIAKMVDLDSLrrSGLRVIVDSMYGAGDSYI 198
Cdd:PRK15414 114 ARP---ISGDTGLRDVQRLAEAND--FPPVDETKRGRYQQINLRDAYVDHLFGYINVKNL--TPLKLVINSGNGAAGPVV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 199 KRL---LDGGRIQIQEINVERNP--IFPGIQPEPIarhLSKLCALVRDT----GAHVGLATDGDADRVGIVDEGGNPLTP 269
Cdd:PRK15414 187 DAIearFKALGAPVELIKVHNTPdgNFPNGIPNPL---LPECRDDTRNAvikhGADMGIAFDGDFDRCFLFDEKGQFIEG 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 270 LQIFALLALYLLEvRGERGAIVR----TVTTTSMLYRLGelyGVPVYeTAVGFKHVAPKMMAENAIMGGEESSGFGFRGH 345
Cdd:PRK15414 264 YYIVGLLAEAFLE-KNPGAKIIHdprlSWNTVDVVTAAG---GTPVM-SKTGHAFIKERMRKEDAIYGGEMSAHHYFRDF 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 346 VPERDGILAAMYFLDLMTRLGKSPSQLIEylyskvgphhyERLdLQFPASQRetIVKRLAsSPPDRIA------GNAVTK 419
Cdd:PRK15414 339 AYCDSGMIPWLLVAELVCLKGKTLGELVR-----------DRM-AAFPASGE--INSKLA-QPVEAINrveqhfSREALA 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1490726200 420 VNTIDGHHFSLADGSWLLvRFSGTEPLLRMYAEA-SSIEKVKALIQDGRSML 470
Cdd:PRK15414 404 VDRTDGISMTFADWRFNL-RSSNTEPVVRLNVESrGDVPLMEARTRTLLTLL 454
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
96-321 |
2.32e-10 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 62.77 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 96 AIIITASHNPAQWNGFKIKSEDGASAPTEVEaDVEARLPQIIGRGTTERMPLKEALSQGLVEYLDLDPPYFQHIAKMVdl 175
Cdd:PLN02371 171 PIMITASHLPYNRNGLKFFTKDGGLGKPDIK-DILERAARIYKEWSDEGLLKSSSGASSVVCRVDFMSTYAKHLRDAI-- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 176 dsLRR-----------SGLRVIVDSMYGAGDSYIKRLLDG-GRIQIQEINVERNPIFPGIQPEP---IArhLSKLCALVR 240
Cdd:PLN02371 248 --KEGvghptnyetplEGFKIVVDAGNGAGGFFAEKVLEPlGADTSGSLFLEPDGMFPNHIPNPedkAA--MSATTQAVL 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 241 DTGAHVGLATDGDADRVGIVDEGGNPLTPLQIFALLALYLLEVRGerGAIVRTVTTTSMlyrlgelyGVPVYETAVGFKH 320
Cdd:PLN02371 324 ANKADLGIIFDTDVDRSAVVDSSGREINRNRLIALMSAIVLEEHP--GTTIVTDSVTSD--------GLTTFIEKKGGKH 393
|
.
gi 1490726200 321 V 321
Cdd:PLN02371 394 H 394
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
409-465 |
1.27e-07 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 48.80 E-value: 1.27e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1490726200 409 PDRIAGNAVTKVNTIDGHHFSLADGSWLLVRFSGTEPLLRMYAEASSIEKVKALIQD 465
Cdd:pfam00408 9 KKKLAALAAILKVFADAEKILGEDGRRLDVRPSGTEPVLRVMVEGDSDEELARLADE 65
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
97-462 |
1.68e-07 |
|
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: 53.37 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 97 IIITASHNPAQWNGFKIKSEDG--------------ASAPTEVEADVEARLPQ--------------IIGRGTTERMP-L 147
Cdd:cd03086 39 VMITASHNPVEDNGVKIVDPDGemleeswepyatqlANASDDELLVLVLMLISvkelnidlsvpanvFVGRDTRPSGPaL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 148 KEALSQGL----VEYLDL-------------------------DPPYFQHIAK-----MVDLDSLRRSGLRVIVDSMYGA 193
Cdd:cd03086 119 LQALLDGLkalgGNVIDYglvttpqlhylvraantegaygeptEEGYYEKLSKafnelYNLLQDGGDEPEKLVVDCANGV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 194 GDSYIKRLLD--GGRIQIQEIN-----------------VERNPIFP-GIQPEPiarHLSKLCALvrdtgahvglatDGD 253
Cdd:cd03086 199 GALKLKELLKrlKKGLSVKIINdgeegpellndgcgadyVKTKQKPPrGFELKP---PGVRCCSF------------DGD 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 254 ADRV-----------GIVDegGNpltplQIFALLALY---LLEVRGERG----AIVRT--VTTTSMLYrLGELYGVPVYE 313
Cdd:cd03086 264 ADRLvyfypdssnkfHLLD--GD-----KIATLFAKFikeLLKKAGEELkltiGVVQTayANGASTKY-LEDVLKVPVVC 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 314 TAVGFKHVAPKmmAENAIMGGE-ESSGFG---FRGHV------------PERDGILAAMYFLDLMT-------------- 363
Cdd:cd03086 336 TPTGVKHLHHA--AEEFDIGVYfEANGHGtvlFSESAlakieensslsdEQEKAAKTLLAFSRLINqtvgdaisdmlave 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490726200 364 ----RLGKSPSQLIEyLYSkvgphhyerlDLqfPASQRETIVK-----------RLASSPP---DRIaGNAVTKVNtiDG 425
Cdd:cd03086 414 lilaALGWSPQDWDN-LYT----------DL--PNRQLKVKVPdrsvikttdaeRRLVEPKglqDKI-DAIVAKYN--NG 477
|
490 500 510
....*....|....*....|....*....|....*..
gi 1490726200 426 HHFsladgswllVRFSGTEPLLRMYAEASSIEKVKAL 462
Cdd:cd03086 478 RAF---------VRPSGTEDVVRVYAEAATQEEADEL 505
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
83-118 |
3.40e-04 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 43.10 E-value: 3.40e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1490726200 83 VISYGVVRQKAGG---AIIITASHNPAQWNGFKIKSEDG 118
Cdd:PTZ00302 62 SFLYGGKRAKRGNksvGVMITASHNPIQDNGVKIIDPDG 100
|
|
| |
