|
Name |
Accession |
Description |
Interval |
E-value |
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
3-443 |
0e+00 |
|
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: 563.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 3 LFGTDGIRGVAGgEKMNPEVVAAFGRSIVSFCRKRNLPEKIIVGRDTRESGLMFEEALVAGISSAGGEAAVAGILPTPAL 82
Cdd:cd05802 1 LFGTDGIRGVAN-EPLTPELALKLGRAAGKVLGKGGGRPKVLIGKDTRISGYMLESALAAGLTSAGVDVLLLGVIPTPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 83 AFLIKEQRAGAGIVISASHNPFQDNGLKPFKNDGTKLSEEEEKELEGYILKKISSGTNDNISGKSSVVQEAKEKYIKFFL 162
Cdd:cd05802 80 AYLTRKLRADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVEEEIEALIDKELELPPTGEKIGRVYRIDDARGRYIEFLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 163 dktSYFFTLELSsrvKKRLVLDCANGATFEVAPAIFEKIAKETGLINANPDGTNINKNCGSQHPESLKREVLAKKADLGL 242
Cdd:cd05802 160 ---STFPKDLLS---GLKIVLDCANGAAYKVAPEVFRELGAEVIVINNAPDGLNINVNCGSTHPESLQKAVLENGADLGI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 243 AFDGDGDRVIAVDEKGNALTGDQMMYVIAKFLKEKGKLKNNLVVTTVMSNLGFVGALSKLGIGHIATGVGDRQVFFEMKN 322
Cdd:cd05802 234 AFDGDADRVIAVDEKGNIVDGDQILAICARDLKERGRLKGNTVVGTVMSNLGLEKALKELGIKLVRTKVGDRYVLEEMLK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 323 KGAILGGEESGHIIFFDFCPTGDGIIGGLMLLAAMSHFKKPLSELAEEVALFPKLLVNVEVKSKPDIGSISEIQDIIKKV 402
Cdd:cd05802 314 HGANLGGEQSGHIIFLDHSTTGDGLLTALQLLAIMKRSGKSLSELASDMKLYPQVLVNVRVKDKKALLENPRVQAAIAEA 393
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 818488919 403 EKKLGKEGRVLVRYSGTENLCRVMVEGRDEGEIRAFADAIA 443
Cdd:cd05802 394 EKELGGEGRVLVRPSGTEPLIRVMVEGEDEELVEKLAEELA 434
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
4-447 |
6.11e-162 |
|
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: 464.15 E-value: 6.11e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 4 FGTDGIRGVAGGEKMNPEVVAAFGRSIVSFCRKRNlPEK--IIVGRDTRESGLMFEEALVAGISSAGGEAAVAGILPTPA 81
Cdd:TIGR01455 1 FGTDGVRGRAGQEPLTAELALLLGAAAGRVLRQGR-DTAprVVIGKDTRLSGYMLENALAAGLNSAGVDVLLLGPLPTPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 82 LAFLIKEQRAGAGIVISASHNPFQDNGLKPFKNDGTKLSEEEEKELEGYILKKIS-SGTNDNISGKSSVVQEAKEKYIKF 160
Cdd:TIGR01455 80 VAYLTRTLRADAGVMISASHNPYEDNGIKFFGPGGFKLDDATEAAIEALLDEADPlPRPESEGLGRVKRYPDAVGRYIEF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 161 FLDKTSYFFTLElssrvKKRLVLDCANGATFEVAPAIFEKIAKETGLINANPDGTNINKNCGSQHPESLKREVLAKKADL 240
Cdd:TIGR01455 160 LKSTLPRGLTLS-----GLKVVLDCANGAAYKVAPHVFRELGAEVIAIGVEPDGLNINDGCGSTHLDALQKAVREHGADL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 241 GLAFDGDGDRVIAVDEKGNALTGDQMMYVIAKFLKEKGKLKNNLVVTTVMSNLGFVGALSKLGIGHIATGVGDRQVFFEM 320
Cdd:TIGR01455 235 GIAFDGDADRVLAVDANGRIVDGDQILYIIARALKESGELAGNTVVATVMSNLGLERALEKLGLTLIRTAVGDRYVLEEM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 321 KNKGAILGGEESGHIIFFDFCPTGDGIIGGLMLLAAMSHFKKPLSELAEEVALFPKLLVNVEVKS-KPDIGSISEIQDII 399
Cdd:TIGR01455 315 RESGYNLGGEQSGHIILLDYSTTGDGIVSALQVLTIMKKSGSTLSELAAEFVPYPQTLVNVRVADrKLAAAEAPAVKAAI 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 818488919 400 KKVEKKLGKEGRVLVRYSGTENLCRVMVEGRDEGEIRAFADAIAKKIK 447
Cdd:TIGR01455 395 EDAEAELGGTGRILLRPSGTEPLIRVMVEAADEELVQQLADTLADVVS 442
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
1-449 |
2.08e-156 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 449.97 E-value: 2.08e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 1 MKLFGTDGIRGVAGGEKMNPEVV-----AAfGRSIVSFCRKrnlpeKIIVGRDTRESGLMFEEALVAGISSAGGEAAVAG 75
Cdd:PRK10887 1 RKYFGTDGIRGKVGQAPITPDFVlklgwAA-GKVLARQGRP-----KVLIGKDTRISGYMLESALEAGLAAAGVDVLLTG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 76 ILPTPALAFLIKEQRAGAGIVISASHNPFQDNGLKPFKNDGTKLSEEEEKELEGYILKKISSGTNDNIsGKSSVVQEAKE 155
Cdd:PRK10887 75 PMPTPAVAYLTRTLRAEAGIVISASHNPYYDNGIKFFSADGTKLPDEVELAIEAELDKPLTCVESAEL-GKASRINDAAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 156 KYIKFFldKTSYFFTLELSsrvKKRLVLDCANGATFEVAPAIFEKIAKETGLINANPDGTNINKNCGSQHPESLKREVLA 235
Cdd:PRK10887 154 RYIEFC--KSTFPNELSLR---GLKIVVDCANGATYHIAPNVFRELGAEVIAIGCEPNGLNINDECGATDPEALQAAVLA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 236 KKADLGLAFDGDGDRVIAVDEKGNALTGDQMMYVIAKFLKEKGKLKNNlVVTTVMSNLGFVGALSKLGIGHIATGVGDRQ 315
Cdd:PRK10887 229 EKADLGIAFDGDGDRVIMVDHLGNLVDGDQLLYIIARDRLRRGQLRGG-VVGTLMSNMGLELALKQLGIPFVRAKVGDRY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 316 VFFEMKNKGAILGGEESGHIIFFDFCPTGDGIIGGLMLLAAMSHFKKPLSELAEEVALFPKLLVNVEVK-SKPDIGSISE 394
Cdd:PRK10887 308 VLEKLQEKGWRLGGENSGHILCLDKTTTGDGIVAALQVLAAMVRSGMSLADLCSGMKLFPQVLINVRFKpGADDPLESEA 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 818488919 395 IQDIIKKVEKKLGKEGRVLVRYSGTENLCRVMVEGRDEGEIRAFADAIAKKIKKH 449
Cdd:PRK10887 388 VKAALAEVEAELGGRGRVLLRKSGTEPLIRVMVEGEDEAQVTALAERIADAVKAA 442
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
1-450 |
2.95e-150 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 435.01 E-value: 2.95e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 1 MKLFGTDGIRGVAGgEKMNPEVVAAFGRSIVSFCRKRNLPeKIIVGRDTRESGLMFEEALVAGISSAGGEAAVAGILPTP 80
Cdd:COG1109 4 KKLFGTDGIRGIVG-EELTPEFVLKLGRAFGTYLKEKGGP-KVVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVPTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 81 ALAFLIKEQRAGAGIVISASHNPFQDNGLKPFKNDGTKLSEEEEKELEGYILKKISSGTNDNISGKSSVVQEAKEKYIKF 160
Cdd:COG1109 82 ALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKEDFRRAEAEEIGKVTRIEDVLEAYIEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 161 FLDKTSyfftlELSSRVKKRLVLDCANGATFEVAPAIFEKIAKETGLINANPDGTNINKNCG--SQHPESLKREVLAKKA 238
Cdd:COG1109 162 LKSLVD-----EALRLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFPNHNPNpePENLEDLIEAVKETGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 239 DLGLAFDGDGDRVIAVDEKGNALTGDQMMYVIAKFLKEKGklKNNLVVTTVMSNLGFVGALSKLGIGHIATGVGDRQVFF 318
Cdd:COG1109 237 DLGIAFDGDADRLGVVDEKGRFLDGDQLLALLARYLLEKG--PGGTVVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 319 EMKNKGAILGGEESGHIIFFDFCPTGDGIIGGLMLLAAMSHFKKPLSELAEEVALFPKLLVNVEVKSKPDIGSISEI--- 395
Cdd:COG1109 315 KMRETGAVLGGEESGGIIFPDFVPTDDGILAALLLLELLAKQGKSLSELLAELPRYPQPEINVRVPDEEKIGAVMEKlre 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818488919 396 -------QDIIKKVEKKLGKEGRVLVRYSGTENLCRVMVEGRDEGEIRAFADAIAKKIKKHL 450
Cdd:COG1109 395 avedkeeLDTIDGVKVDLEDGGWVLVRPSGTEPLLRVYAEAKDEEEAEELLAELAELVEEAL 456
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
1-446 |
8.93e-102 |
|
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: 310.60 E-value: 8.93e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 1 MKLFGTDGIRGVAGgEKMNPEVVAAFGRSIVSFCRKRnlpeKIIVGRDTRESGLMFEEALVAGISSAGGEAAVAGILPTP 80
Cdd:TIGR03990 1 MLLFGTSGIRGIVG-EELTPELALKVGKAFGTYLRGG----KVVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLGIAPTP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 81 ALAFLIKEQRAGAGIVISASHNPFQDNGLKPFKNDGTKLSEEEEKElegyILKKISSGTNDNIS----GKSSVVQEAKEK 156
Cdd:TIGR03990 76 TLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQEEE----IEEIAESGDFERADwdeiGTVTSDEDAIDD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 157 YIKFFLDKtsyfFTLELSSRVKKRLVLDCANGATFEVAPAIFEKIAKETGLINANPDGTNINKNcgsqhPE-------SL 229
Cdd:TIGR03990 152 YIEAILDK----VDVEAIRKKGFKVVVDCGNGAGSLTTPYLLRELGCKVITLNCQPDGTFPGRN-----PEptpenlkDL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 230 KREVLAKKADLGLAFDGDGDRVIAVDEKGNALTGDQMMYVIAKFLKEKGKLKnnlVVTTVMSNLGFVGALSKLGIGHIAT 309
Cdd:TIGR03990 223 SALVKATGADLGIAHDGDADRLVFIDEKGRFIGGDYTLALFAKYLLEHGGGK---VVTNVSSSRAVEDVAERHGGEVIRT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 310 GVGDRQVFFEMKNKGAILGGEESGHIIFFDFCPTGDGIIGGLMLLAAMSHFKKPLSELAEEVALFPKLLVNVEVKSKpdi 389
Cdd:TIGR03990 300 KVGEVNVAEKMKEEGAVFGGEGNGGWIFPDHHYCRDGLMAAALFLELLAEEGKPLSELLAELPKYPMSKEKVELPDE--- 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818488919 390 gsisEIQDIIKKVEKKL--------------GKEGRVLVRYSGTENLCRVMVEGRDEGEIRAFADAIAKKI 446
Cdd:TIGR03990 377 ----DKEEVMEAVEEEFadaeidtidgvridFEDGWVLVRPSGTEPIVRIYAEAKTEERAEELLEEGRSLV 443
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
3-446 |
8.24e-94 |
|
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: 290.24 E-value: 8.24e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 3 LFGTDGIRGVAGgEKMNPEVVAAFGRSIVSFCRKRnlpeKIIVGRDTRESGLMFEEALVAGISSAGGEAAVAGILPTPAL 82
Cdd:cd03087 1 LFGTSGIRGVVG-EELTPELALKVGKALGTYLGGG----TVVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDIGIVPTPAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 83 AFLIKEqRAGAGIVISASHNPFQDNGLKPFKNDGTKLSEEEEKELEGYILKKISSGTNDNISGKSSVVQEAKEKYIKFFL 162
Cdd:cd03087 76 QYAVRK-LGDAGVMITASHNPPEYNGIKLVNPDGTEFSREQEEEIEEIIFSERFRRVAWDEVGSVRREDSAIDEYIEAIL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 163 DKTSyfftLELSSRVKkrLVLDCANGATFEVAPAIFEKIAKETGLINANPDGTNInkncgSQHPE-------SLKREVLA 235
Cdd:cd03087 155 DKVD----IDGGKGLK--VVVDCGNGAGSLTTPYLLRELGCKVITLNANPDGFFP-----GRPPEptpenlsELMELVRA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 236 KKADLGLAFDGDGDRVIAVDEKGNALTGDQMMYVIAKFLKEKGKLKnnlVVTTVMSNLGFVGALSKLGIGHIATGVGDRQ 315
Cdd:cd03087 224 TGADLGIAHDGDADRAVFVDEKGRFIDGDKLLALLAKYLLEEGGGK---VVTPVDASMLVEDVVEEAGGEVIRTPVGDVH 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 316 VFFEMKNKGAILGGEESGHIIFFDFCPTGDGIIGGLMLLAAMSHfKKPLSELAEEVALFPKLLVNVEVKS--KPDI--GS 391
Cdd:cd03087 301 VAEEMIENGAVFGGEPNGGWIFPDHQLCRDGIMTAALLLELLAE-EKPLSELLDELPKYPLLREKVECPDekKEEVmeAV 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 392 ISEIQDIIKKVE-----KKLGKEGRVLVRYSGTENLCRVMVEGRDEGEIRAFADAIAKKI 446
Cdd:cd03087 380 EEELSDADEDVDtidgvRIEYEDGWVLIRPSGTEPKIRITAEAKTEERAKELLEEGRSKV 439
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
9-450 |
7.87e-79 |
|
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: 251.66 E-value: 7.87e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 9 IRGVAGGEkMNPEVVAAFGRSIVSFCRKRNLPeKIIVGRDTRESGLMFEEALVAGISSAGGEAAVAGILPTPALAFLIKE 88
Cdd:cd03089 7 IRGIAGEE-LTEEIAYAIGRAFGSWLLEKGAK-KVVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPVLYFATFH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 89 QRAGAGIVISASHNPFQDNGLKPFKNDGTKLSEEEEkelegYILKKISSGTNDNISGKSSVVQ-EAKEKYIKFFLDKTSy 167
Cdd:cd03089 85 LDADGGVMITASHNPPEYNGFKIVIGGGPLSGEDIQ-----ALRERAEKGDFAAATGRGSVEKvDILPDYIDRLLSDIK- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 168 fftleLSSRvKKRLVLDCANGATFEVAPAIFEKIAKETGLINANPDGTNINkncgsQHP--------ESLKREVLAKKAD 239
Cdd:cd03089 159 -----LGKR-PLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCEPDGTFPN-----HHPdptdpenlEDLIAAVKENGAD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 240 LGLAFDGDGDRVIAVDEKGNALTGDQMMYVIAK-FLKEKgklKNNLVVTTVMSNLGFVGALSKLGIGHIATGVGDRQVFF 318
Cdd:cd03089 228 LGIAFDGDGDRLGVVDEKGEIIWGDRLLALFARdILKRN---PGATIVYDVKCSRNLYDFIEEAGGKPIMWKTGHSFIKA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 319 EMKNKGAILGGEESGHIIF------FDfcptgDGIIGGLMLLAAMSHFKKPLSELaeeVALFPKLLVNVEVKSK-PDigs 391
Cdd:cd03089 305 KMKETGALLAGEMSGHIFFkdrwygFD-----DGIYAALRLLELLSKSGKTLSEL---LADLPKYFSTPEIRIPvTE--- 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818488919 392 iSEIQDIIKKVEKKL----------------GKEGRVLVRYSGTENLCRVMVEGRDEGEirafADAIAKKIKKHL 450
Cdd:cd03089 374 -EDKFAVIERLKEHFefpgaeiididgvrvdFEDGWGLVRASNTEPVLVLRFEADTEEG----LEEIKAELRKLL 443
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
3-446 |
1.48e-64 |
|
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: 211.83 E-value: 1.48e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 3 LFGTDGIRGVAGgEKMNPEVVAAFGRSIVSFcrkrnlpekiivgrdtresglmfeealvagissaggeaavagilptpal 82
Cdd:cd03084 1 IFGTSGVRGVVG-DDITPETAVALGQAIGST------------------------------------------------- 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 83 aflikeqragAGIVISASHNPFQDNGLKPFKNDGTKLSEEEEKELEGYILKKISSGTNDNISGKSSVVQEAKEKYIKFFL 162
Cdd:cd03084 31 ----------GGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSAVAYELGGSVKAVDILQRYFEALK 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 163 DKtsyfFTLELSSRVKKRLVLDCANGATFEVAPAIFEKIAKETGLINANPDG--TNINKNCGSqhPESLK--REVL-AKK 237
Cdd:cd03084 101 KL----FDVAALSNKKFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCEPDGnfGNINPDPGS--ETNLKqlLAVVkAEK 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 238 ADLGLAFDGDGDRVIAVDEKGNALTGDQMMYVIAKFLKEKGKlKNNLVVTTVMSNLGFVGALSKLGIGHIATGVGDRQVF 317
Cdd:cd03084 175 ADFGVAFDGDADRLIVVDENGGFLDGDELLALLAVELFLTFN-PRGGVVKTVVSSGALDKVAKKLGIKVIRTKTGFKWVG 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 318 FEMKNKGAILGGEESGHIIFFDFCPTGDGIIGGLMLLAAMSHFKKPLSELAEEVALFPKLLVNVevkskpdigsiseiqd 397
Cdd:cd03084 254 EAMQEGDVVLGGEESGGVIFPEFHPGRDGISAALLLLEILANLGKSLSELFSELPRYYYIRLKV---------------- 317
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 818488919 398 iikkvekklgkEGRVLVRYSGTENLCRVMVEGrDEGEIRAFADAIAKKI 446
Cdd:cd03084 318 -----------RGWVLVRASGTEPAIRIYAEA-DTQEDVEQIKKEAREL 354
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
4-446 |
4.51e-54 |
|
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: 186.99 E-value: 4.51e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 4 FGTDGIRGVAGgEKMNPEVVAAFGRSIVSFCRKRNLPEK-IIVGRDTRESGLMFEEALVAGISSAGGEAAVA-GILPTPA 81
Cdd:cd05800 3 FGTDGWRGIIA-EDFTFENVRRVAQAIADYLKEEGGGGRgVVVGYDTRFLSEEFARAVAEVLAANGIDVYLSdRPVPTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 82 LAFLIKEQRAGAGIVISASHNPFQDNGLKpFKNDGTKLSEEEEKELEGYILKKISSGTNDNISGKSSVVQEAKEKYIKFF 161
Cdd:cd05800 82 VSWAVKKLGAAGGVMITASHNPPEYNGVK-VKPAFGGSALPEITAAIEARLASGEPPGLEARAEGLIETIDPKPDYLEAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 162 LDktsyFFTLELSSRVKKRLVLDCANGATFEVAPAIFEKIAKETGLINA-----------NPDGTNINKncgsqhpesLK 230
Cdd:cd05800 161 RS----LVDLEAIREAGLKVVVDPMYGAGAGYLEELLRGAGVDVEEIRAerdplfggippEPIEKNLGE---------LA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 231 REVLAKKADLGLAFDGDGDRVIAVDEKGNALTGDQMMYVIAKFLKEKGKLKNNLVVTTVMSNLgfVGALS-KLGIGHIAT 309
Cdd:cd05800 228 EAVKEGGADLGLATDGDADRIGAVDEKGNFLDPNQILALLLDYLLENKGLRGPVVKTVSTTHL--IDRIAeKHGLPVYET 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 310 GVGDRQVFFEMKNKGAILGGEESGHIIFFDFCPTGDGIIGGLMLLAAMSHFKKPLSELAEEV-----ALFPK---LLVNV 381
Cdd:cd05800 306 PVGFKYIAEKMLEEDVLIGGEESGGLGIRGHIPERDGILAGLLLLEAVAKTGKPLSELVAELeeeygPSYYDridLRLTP 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818488919 382 EVK---------SKPDIGSISEIQDIIKK--VEKKLGKEGRVLVRYSGTENLCRVMVEGRDEGEIRAFADAIAKKI 446
Cdd:cd05800 386 AQKeaileklknEPPLSIAGGKVDEVNTIdgVKLVLEDGSWLLIRPSGTEPLLRIYAEAPSPEKVEALLDAGKKLA 461
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
8-445 |
7.00e-54 |
|
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: 186.36 E-value: 7.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 8 GIRGVAGgEKMNPEVVAAFGRSIVSFCRKRNLPEKIIVGRDTRESGLMFEEALVAGISSAGGEAAVAGILPTPALAFLIK 87
Cdd:cd05803 6 GIRGIVG-EGLTPEVITRYVAAFATWQPERTKGGKIVVGRDGRPSGPMLEKIVIGALLACGCDVIDLGIAPTPTVQVLVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 88 EQRAGAGIVISASHNPFQDNGLKPFKNDGTKLSEEEEKElegyILKKISSGTNDNISGKSSVVQEAKEKYIKFFLDKTSY 167
Cdd:cd05803 85 QSQASGGIIITASHNPPQWNGLKFIGPDGEFLTPDEGEE----VLSCAEAGSAQKAGYDQLGEVTFSEDAIAEHIDKVLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 168 FFTLELSSRVKK--RLVLDCANGATFEVAPAIFEKIAKETGLINANPDGTninkncgSQH-----PESLK---REVLAKK 237
Cdd:cd05803 161 LVDVDVIKIRERnfKVAVDSVNGAGGLLIPRLLEKLGCEVIVLNCEPTGL-------FPHtpeplPENLTqlcAAVKESG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 238 ADLGLAFDGDGDRVIAVDEKGNALTGDQMMYVIAKFLKEKGKLKNNLVVttvmsNLGFVGALSKLGIGH----IATGVGD 313
Cdd:cd05803 234 ADVGFAVDPDADRLALVDEDGRPIGEEYTLALAVDYVLKYGGRKGPVVV-----NLSTSRALEDIARKHgvpvFRSAVGE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 314 RQVFFEMKNKGAILGGEESGHIIFFDFCPTGDGIIGGLMLLAAMSHFKKPLSELAEEvalFPKLLVnveVKSKPDIgSIS 393
Cdd:cd05803 309 ANVVEKMKEVDAVIGGEGNGGVILPDVHYGRDSLVGIALVLQLLAASGKPLSEIVDE---LPQYYI---SKTKVTI-AGE 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818488919 394 EIQDIIKKVEKKLG--------------KEGRVLVRYSGTENLCRVMVEGRDEGEirafADAIAKK 445
Cdd:cd05803 382 ALERLLKKLEAYFKdaeastldglrldsEDSWVHVRPSNTEPIVRIIAEAPTQDE----AEALADR 443
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
1-116 |
7.71e-40 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 139.67 E-value: 7.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 1 MKLFGTDGIRGVAGGEKMNPEVVAAFGRSIVSFCRKRNLPEKIIVGRDTRESGLMFEEALVAGISSAGGEAAVAGILPTP 80
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGELTPEFALKLGQAIASYLRAQGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTP 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 818488919 81 ALAFLIKEQRAGAGIVISASHNPFQDNGLKPFKNDG 116
Cdd:pfam02878 81 AVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNG 116
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
4-448 |
2.79e-36 |
|
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: 139.18 E-value: 2.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 4 FGTDGIRGV--AGGEKMNPEVVAAFGRSIVSFCRKRNLPEK---IIVGRDTRESGLMFEEaLVAGI-SSAGGEAAV-AGI 76
Cdd:cd05799 4 FGTAGLRGKmgAGTNRMNDYTVRQATQGLANYLKKKGPDAKnrgVVIGYDSRHNSREFAE-LTAAVlAANGIKVYLfDDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 77 LPTPALAFLIKEQRAGAGIVISASHNPFQDNGLKPFKNDGtklseeeekeleGYIL----KKISSGTNDNISGKSSVVQE 152
Cdd:cd05799 83 RPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDG------------AQIIpphdAEIAEEIEAVLEPLDIKFEE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 153 AKEKY-IKFFLDKT--SYF-------FTLELSSRVKKRLVLDCANGATFEVAPAIFekiaKETGLIN-------ANPDGT 215
Cdd:cd05799 151 ALDSGlIKYIGEEIddAYLeavkkllVNPELNEGKDLKIVYTPLHGVGGKFVPRAL----KEAGFTNvivveeqAEPDPD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 216 niNKNCGSQHPE---SLKREV-LAKK--ADLGLAFDGDGDRViAVDEKGNA-----LTGDQMMYVIAKFL----KEKGKL 280
Cdd:cd05799 227 --FPTVKFPNPEepgALDLAIeLAKKvgADLILATDPDADRL-GVAVKDKDgewrlLTGNEIGALLADYLleqrKEKGKL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 281 KNNLVV--TTVMSNLGFVGAlSKLGIGHIATGVG-----DRQVFFEMKNKGAILGGEES-GHiIFFDFCPTGDGIIGGLM 352
Cdd:cd05799 304 PKNPVIvkTIVSSELLRKIA-KKYGVKVEETLTGfkwigNKIEELESGGKKFLFGFEESiGY-LVGPFVRDKDGISAAAL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 353 LLAAMSHFKKP-------LSELAEEVALFPKLLVNVEVKSKPDigsISEIQDIIKKVEK-------KLGKEGRVLVRYSG 418
Cdd:cd05799 382 LAEMAAYLKAQgktlldrLDELYEKYGYYKEKTISITFEGKEG---PEKIKAIMDRLRNnpnvltfYLEDGSRVTVRPSG 458
|
490 500 510
....*....|....*....|....*....|
gi 818488919 419 TENLCRVMVEGRDEGEIRAfADAIAKKIKK 448
Cdd:cd05799 459 TEPKIKFYIEVVGKKTLEE-AEKKLDALKK 487
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
262-371 |
6.38e-36 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 128.34 E-value: 6.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 262 TGDQMMYVIAKFLKEKGKLKNNL-VVTTVMSNLGFVGALSKLGIGHIATGVGDRQVFFEMKNKGAILGGEESGHIIFFDF 340
Cdd:pfam02880 1 DGDQILALLAKYLLEQGKLPPGAgVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLDH 80
|
90 100 110
....*....|....*....|....*....|.
gi 818488919 341 CPTGDGIIGGLMLLAAMSHFKKPLSELAEEV 371
Cdd:pfam02880 81 ATTKDGILAALLVLEILARTGKSLSELLEEL 111
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
9-447 |
2.17e-28 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 116.62 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 9 IRGVAGgEKMNPEVVAAFGRSIVSFCRKRNLPeKIIVGRDTRESGLMFEEALVAGISSAGGEAAVAGILPTPALAFlike 88
Cdd:PRK09542 6 VRGVVG-EQIDEDLVRDVGAAFARLMRAEGAT-TVVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIGLASTDQLYF---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 89 qRAGA----GIVISASHNPFQDNGLK-------PFKNDGTKLSeeeekelegyILKKISSGTNDNISGKSSVV-QEAKEK 156
Cdd:PRK09542 80 -ASGLldcpGAMFTASHNPAAYNGIKlcragakPVGQDTGLAA----------IRDDLIAGVPAYDGPPGTVTeRDVLAD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 157 YIKFFLDktsyffTLELSSRVKKRLVLDCANGATFEVAPAIFEKIAKETGLINANPDGTNINKNCGSQHPES---LKREV 233
Cdd:PRK09542 149 YAAFLRS------LVDLSGIRPLKVAVDAGNGMGGHTVPAVLGGLPITLLPLYFELDGTFPNHEANPLDPANlvdLQAFV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 234 LAKKADLGLAFDGDGDRVIAVDEKGNALTGDQMMYVIA-KFLKEK--GKLKNNLVVTTVMSNLgfvgaLSKLGIGHIATG 310
Cdd:PRK09542 223 RETGADIGLAFDGDADRCFVVDERGQPVSPSAVTALVAaRELAREpgATIIHNLITSRAVPEL-----VAERGGTPVRTR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 311 VGDRQVFFEMKNKGAILGGEESGHIIFFDFCPTGDGIIGGLMLLAAMSHFKKPLSELAEE-------------VALFPKL 377
Cdd:PRK09542 298 VGHSFIKALMAETGAIFGGEHSAHYYFRDFWGADSGMLAALHVLAALGEQDRPLSELMADyqryaasgeinstVADAPAR 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 378 LVNVEVKSKPDIGSIseiqDIIKKVEKKLGKEGRVLVRYSGTENLCRVMVEGRDEGEIRAFADAIAKKIK 447
Cdd:PRK09542 378 MEAVLKAFADRIVSV----DHLDGVTVDLGDGSWFNLRASNTEPLLRLNVEARTEEEVDALVDEVLAIIR 443
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
33-450 |
3.62e-26 |
|
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: 110.76 E-value: 3.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 33 FCRKRNLPEKIIVGRDTRESGLMFEEALVAGISSAGGEAAVAGILPTPALAFLIKeqragagivisashnpFQDNGLKPF 112
Cdd:cd03086 95 LNIDLSVPANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYLVR----------------AANTEGAYG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 113 KNDGTklseeeekeleGYIlkkissgtndnisgkssvvqeakEKYIKFFLdktSYFFTLELSSRVKKRLVLDCANGatfe 192
Cdd:cd03086 159 EPTEE-----------GYY-----------------------EKLSKAFN---ELYNLLQDGGDEPEKLVVDCANG---- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 193 V-APAI--FEKIAKET---GLINANPDGTN-INKNCGSQH-------PESLKrevLAKKADLGLAFDGDGDRVIA--VDE 256
Cdd:cd03086 198 VgALKLkeLLKRLKKGlsvKIINDGEEGPElLNDGCGADYvktkqkpPRGFE---LKPPGVRCCSFDGDADRLVYfyPDS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 257 KGNA--LTGDQMMYVIAKFLKE---KGKLKNNL---VVTTVMSNLGFVGAL-SKLGIGHI--ATGVG---------DRQV 316
Cdd:cd03086 275 SNKFhlLDGDKIATLFAKFIKEllkKAGEELKLtigVVQTAYANGASTKYLeDVLKVPVVctPTGVKhlhhaaeefDIGV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 317 FFEMKNKGAIL---------------GGEESGHII----FFDFC--PTGDGIIGGLMLLAAMSHFKKPLSELAEEVALFP 375
Cdd:cd03086 355 YFEANGHGTVLfsesalakieensslSDEQEKAAKtllaFSRLInqTVGDAISDMLAVELILAALGWSPQDWDNLYTDLP 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 376 KLLVNVEVKSKPDIGSIS---------EIQDIIKKVEKKLgKEGRVLVRYSGTENLCRVMVEGRDEGEirafADAIAKKI 446
Cdd:cd03086 435 NRQLKVKVPDRSVIKTTDaerrlvepkGLQDKIDAIVAKY-NNGRAFVRPSGTEDVVRVYAEAATQEE----ADELANEV 509
|
....
gi 818488919 447 KKHL 450
Cdd:cd03086 510 AELV 513
|
|
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
3-431 |
1.85e-25 |
|
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: 108.10 E-value: 1.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 3 LFGTDGIRGVAGGEkMNPEVV----AAFGRSIvsfcrKRNlpEKIIVGRDTRESGLMFEEALVAGISSAGGEAAVAGILP 78
Cdd:cd05805 1 LFGGRGVSGLINVD-ITPEFAtrlgAAYGSTL-----PPG--STVTVSRDASRASRMLKRALISGLLSTGVNVRDLGALP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 79 TPALAFLIKEQRAGAGIVISASHNPFQDNGLKPFKNDGTKlseeeekelegyilkkISSGTNDNIS-------------- 144
Cdd:cd05805 73 LPVARYAIRFLGASGGIHVRTSPDDPDKVEIEFFDSRGLN----------------ISRAMERKIEnaffredfrrahvd 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 145 --GKSSVVQEAKEKYIKFFLDKTSyfftLELSSRVKKRLVLDCANGATFEVAPAIFEKIAKETGLINANPDGTN-INKNC 221
Cdd:cd05805 137 eiGDITEPPDFVEYYIRGLLRALD----TSGLKKSGLKVVIDYAYGVAGIVLPGLLSRLGCDVVILNARLDEDApRTDTE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 222 GSQHPESLKREVLAKKADLGLAFDGDGDRVIAVDEKGNALTGDQMMYVIAKFLKEKGKlKNNLVVTTVMSNLgfVGALSK 301
Cdd:cd05805 213 RQRSLDRLGRIVKALGADFGVIIDPNGERLILVDEAGRVISDDLLTALVSLLVLKSEP-GGTVVVPVTAPSV--IEQLAE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 302 LGIGHIATGVGDRQVFFEMKNKGAILGGEESGHIIFFDFCPTGDGIIGGLMLLAAMSHFKKPLSELAEEVALFpkLLVNV 381
Cdd:cd05805 290 RYGGRVIRTKTSPQALMEAALENVVLAGDGDGGFIFPEFHPGFDAIAALVKILEMLARTNISLSQIVDELPRF--YVLHK 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818488919 382 EVK-SKPDIGS-----ISEIQDiiKKVE-----KKLGKEGRVLVRYSGTENLCRVMVEGRD 431
Cdd:cd05805 368 EVPcPWEAKGRvmrrlIEEAPD--KSIElidgvKIYEDDGWVLVLPDADEPLCHIYAEGSD 426
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
9-435 |
2.99e-24 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 104.64 E-value: 2.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 9 IRGVAGgEKMNPEVVAAFGRSIVSFCRkrnlPEKIIVGRDTRESGLMFEEALVAGISSAGGEAAVAGILPTPALAFLIKE 88
Cdd:PRK15414 12 IRGKLG-EELNEDIAWRIGRAYGEFLK----PKTIVLGGDVRLTSETLKLALAKGLQDAGVDVLDIGMSGTEEIYFATFH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 89 QRAGAGIVISASHNPFQDNGLKPFKNDGtklseeeekelegyilKKIS--SGTND----NISGKSSVVQEAKEKYIKFFL 162
Cdd:PRK15414 87 LGVDGGIEVTASHNPMDYNGMKLVREGA----------------RPISgdTGLRDvqrlAEANDFPPVDETKRGRYQQIN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 163 DKTSY----FFTLELSSRVKKRLVLDCANGATFEVAPAIfEKIAKETGL------INANPDGTNINKNCGSQHPE---SL 229
Cdd:PRK15414 151 LRDAYvdhlFGYINVKNLTPLKLVINSGNGAAGPVVDAI-EARFKALGApvelikVHNTPDGNFPNGIPNPLLPEcrdDT 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 230 KREVLAKKADLGLAFDGDGDRVIAVDEKGNALTGDQMMYVIAKFLKEKG---------KLKNNLVvtTVMSNLGFVGALS 300
Cdd:PRK15414 230 RNAVIKHGADMGIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNpgakiihdpRLSWNTV--DVVTAAGGTPVMS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 301 KLGIGHIATgvgdrqvffEMKNKGAILGGEESGHIIFFDFCPTGDGIIGGLMLLAAMSHFKKPLSEL-AEEVALFPkllV 379
Cdd:PRK15414 308 KTGHAFIKE---------RMRKEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELVCLKGKTLGELvRDRMAAFP---A 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818488919 380 NVEVKSKpdigsISEIQDIIKKVEKKLGKEG----------------RVLVRYSGTENLCRVMVEGRDEGEI 435
Cdd:PRK15414 376 SGEINSK-----LAQPVEAINRVEQHFSREAlavdrtdgismtfadwRFNLRSSNTEPVVRLNVESRGDVPL 442
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
5-276 |
6.49e-22 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 98.59 E-value: 6.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 5 GTDgIRGVA-GGEK-----MNPEVVAAFGRSIVSFCR--KRNLPE---KIIVGRDTRESGLMFEEALVAGISSAGGEAAV 73
Cdd:PLN02371 70 GSD-IRGVAvEGVEgepvtLTPPAVEAIGAAFAEWLLekKKADGSgelRVSVGRDPRISGPRLADAVFAGLASAGLDVVD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 74 AGILPTPALAF--LIKEQRAGAGIVISASHNPFQDNGLKPFKNDGTKLSEEEEKelegyILKKISSGTNDNISGKSSVVQ 151
Cdd:PLN02371 149 MGLATTPAMFMstLTEREDYDAPIMITASHLPYNRNGLKFFTKDGGLGKPDIKD-----ILERAARIYKEWSDEGLLKSS 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 152 EAKEKYIKF--FLDktsyFFTLELSSRVKKR---------------LVLDCANGATFEVAPAIFEKI-AKETGLINANPD 213
Cdd:PLN02371 224 SGASSVVCRvdFMS----TYAKHLRDAIKEGvghptnyetplegfkIVVDAGNGAGGFFAEKVLEPLgADTSGSLFLEPD 299
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818488919 214 GTNINKNCGSQHPESLK---REVLAKKADLGLAFDGDGDRVIAVDEKGNALTGDQ---MMYVIakFLKE 276
Cdd:PLN02371 300 GMFPNHIPNPEDKAAMSattQAVLANKADLGIIFDTDVDRSAVVDSSGREINRNRliaLMSAI--VLEE 366
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
42-451 |
1.85e-20 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 93.95 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 42 KIIVGRDTRESGLMFEEALVAGISSAGGEAAVA-GILPTPALAFLIkeqragagivisASHNpfqdnglkpfkndgtkls 120
Cdd:PTZ00302 154 KVHVGRDTRPSSPELVSALLRGLKLLIGSNVRNfGIVTTPQLHFLV------------AFAN------------------ 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 121 eeeekelegyilkkiSSGTNDNISGKSSVVQEAKEKYIKF--FLDKTsyfFTLELSSRVKKRLVLDCANGATFEVAPA-- 196
Cdd:PTZ00302 204 ---------------GLGVDVVESSDELYYAYLLAAFKELyrTLQEG---GPVDLTQNNSKILVVDCANGVGGYKIKRff 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 197 -IFEKIAKETGLINANPDGTNI-NKNCGSQH-------PESLKrEVLAKKADLGLAFDGDGDRVIA--VDEKGNA----L 261
Cdd:PTZ00302 266 eALKQLGIEIIPININCDEEELlNDKCGADYvqktrkpPRAMK-EWPGDEETRVASFDGDADRLVYffPDKDGDDkwvlL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 262 TGDQMMYVIAKFLKE---KGKLKNNL---VVTTVMSNLGFVGALSKLgIGHI-----ATGVG---------DRQVFFEMK 321
Cdd:PTZ00302 345 DGDRIAILYAMLIKKllgKIQLKKKLdigVVQTAYANGASTNYLNEL-LGRLrvycaPTGVKnlhpkahkyDIGIYFEAN 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 322 NKGAIL-------GGEESGHII---------FFDFC-----PTGDGIIGGLMLLAAMSHFKKPLSELAEEVALFPKLLVN 380
Cdd:PTZ00302 424 GHGTVLfnekalaEWAKFLAKQnalnsacrqLEKFLrlfnqTIGDAISDLLAVELALAFLGLSFQDWLNLYTDLPSRQDK 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 381 VEVKsKPDIGSISE----------IQDIIKKVEKKLGKEGRVLVRYSGTENLCRVMVEGRDEGEIRAFADAIAKKIKKHL 450
Cdd:PTZ00302 504 VTVK-DRTLITNTEdetrllepkgLQDKIDAIVSKYDNAARAFIRPSGTEPVVRVYAEAPTLEQADELANEVKGLVLRYC 582
|
.
gi 818488919 451 G 451
Cdd:PTZ00302 583 S 583
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
4-376 |
6.57e-20 |
|
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: 91.88 E-value: 6.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 4 FGTDGIRGVAGGekMNPEVVAAFGRSIVSFCRKRNLPEKIIVGRDTRESGLMFEEALVAGISSAGGEAAVAGILPTPALA 83
Cdd:cd03088 2 FGTSGLRGLVTD--LTDEVCYAYTRAFLQHLESKFPGDTVAVGRDLRPSSPRIAAACAAALRDAGFRVVDCGAVPTPALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 84 fLIKEQRAGAGIVISASHNPFQDNGLKPFKNDGTklseeeekelegyILK-----------KISSGTNDNISGKSSVVQE 152
Cdd:cd03088 80 -LYAMKRGAPAIMVTGSHIPADRNGLKFYRPDGE-------------ITKadeaailaalvELPEALFDPAGALLPPDTD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 153 AKEKYIKFFLDktsyFFTLE-LSSrvkKRLVLDCANGATFEVAPAIFEKI-AKETGLINAN---PDGTninkncgsqhpE 227
Cdd:cd03088 146 AADAYIARYTD----FFGAGaLKG---LRIGVYQHSSVGRDLLVRILEALgAEVVPLGRSDtfiPVDT-----------E 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 228 SLKREVLAKKADLGLAF--------DGDGDRVIAVDEKGNALTGDQMMYVIAKFLKEKgklknnLVVTTVMSN-----LG 294
Cdd:cd03088 208 AVRPEDRALAAAWAAEHgldaivstDGDGDRPLVADETGEWLRGDILGLLTARFLGAD------TVVTPVSSNsaielSG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 295 FVGALSKLGIG---------HIATGVGDRQVFFEmKNKGAILGgeesghiifFDFC---------PTGDGIIGGLMLLAA 356
Cdd:cd03088 282 FFKRVVRTRIGspyviaamaEAAAAGAGRVVGYE-ANGGFLLG---------SDIErngrtlkalPTRDAVLPILAVLAA 351
|
410 420
....*....|....*....|
gi 818488919 357 MSHFKKPLSELaeeVALFPK 376
Cdd:cd03088 352 AKEAGIPLSEL---VASLPA 368
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
378-447 |
3.64e-16 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 72.69 E-value: 3.64e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818488919 378 LVNVEVKSKPDIGSISEIQDIIKKVEKKLGKEGRVL-VRYSGTENLCRVMVEGRDEGEIRAFADAIAKKIK 447
Cdd:pfam00408 1 LINVRVAEKKKLAALAAILKVFADAEKILGEDGRRLdVRPSGTEPVLRVMVEGDSDEELARLADEIADLLE 71
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
157-258 |
2.21e-15 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 71.55 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 157 YIKFFLDKtsyfFTLELSSRVKKRLVLDCANGATFEVAPAIFEKIAKETGLINANPDGTNINKNC---GSQHPESLKREV 233
Cdd:pfam02879 2 YIDHLLEL----VDSEALKKRGLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDPDFPTRAPnpeEPEALALLIELV 77
|
90 100
....*....|....*....|....*
gi 818488919 234 LAKKADLGLAFDGDGDRVIAVDEKG 258
Cdd:pfam02879 78 KSVGADLGIATDGDADRLGVVDERG 102
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
38-451 |
6.69e-11 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 64.27 E-value: 6.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 38 NLPEKIIVGRDTRESGLMFEEALVAGISSAGGEAAVAGILPTPALAFLIKeqragagivisASHNPFQDNGLKPFKNdgt 117
Cdd:PLN02895 125 NPPAEVLLGRDTRPSGPALLAAALKGVRAIGARAVDMGILTTPQLHWMVR-----------AANKGMKATESDYFEQ--- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 118 klseeeekELEGYilKKISSGTNDNISGKssvvqeakekyikffldktsyfftlelssRVKKRLVLDCANGatfeVAPAI 197
Cdd:PLN02895 191 --------LSSSF--RALLDLIPNGSGDD-----------------------------RADDKLVVDGANG----VGAEK 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 198 FEKIAKETG-----LINANPDGTNI-NKNCGS---QHPESLKREVLAKKADLGLA-FDGDGDRVIAVDEKGNA-----LT 262
Cdd:PLN02895 228 LETLKKALGgldleVRNSGKEGEGVlNEGVGAdfvQKEKVPPTGFASKDVGLRCAsLDGDADRLVYFYVSSAGskidlLD 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 263 GDQMMYVIAKFLKE-------KGKLKNNL------VVTTVMSN----------LGFVGALSKLGIGHI--ATGVGDRQVF 317
Cdd:PLN02895 308 GDKIASLFALFIKEqlrilngNGNEKPEEllvrlgVVQTAYANgastaylkqvLGLEVVCTPTGVKYLheAAAEFDIGVY 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 318 FEMKNKGAILGGEEsghiiFFDFCPT--------------------------------GDGIIGGLMLLAAMSHFKKPLS 365
Cdd:PLN02895 388 FEANGHGTVLFSER-----FLDWLEAaaaelsskakgseahkaarrllavsrlinqavGDALSGLLLVEAILQYRGWSLA 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 366 ELAEEVALFPKLLVNVEVKskpDIGSIS------------EIQDIIKKVEKKLGKeGRVLVRYSGTENLCRVMVEGRDEG 433
Cdd:PLN02895 463 EWNALYQDLPSRQLKVKVA---DRTAITttdaetvvvrpaGLQDAIDAEVAKYPR-GRAFVRPSGTEDVVRVYAEASTQE 538
|
490
....*....|....*...
gi 818488919 434 EIRAFADAIAKKIKKHLG 451
Cdd:PLN02895 539 AADSLAREVARLVYDLLG 556
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
4-250 |
1.42e-09 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 60.15 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 4 FGTDGIRGVAGGEKMNPEVVAAFGRSIVSFCRKRNLPEKIIVGRDTRE-SglmfEEALVAGIssaggEAAVA-------- 74
Cdd:PRK07564 40 FGTSGHRGSSLQPSFNENHILAIFQAICEYRGKQGITGPLFVGGDTHAlS----EPAIQSAL-----EVLAAngvgvviv 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 75 ---GILPTPALAFLI---KEQRAGA--GIVISASHNPFQDNGLK-------PFKNDGTKLSEEEEKELEGYIL---KKIS 136
Cdd:PRK07564 111 grgGYTPTPAVSHAIlkyNGRGGGLadGIVITPSHNPPEDGGIKynppnggPADTDVTDAIEARANELLAYGLkgvKRIP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 137 SGTndniSGKSSVVQEakEKYIKFFLDKTSYFFTLELSSRVKKRLVLDCANGATFEVAPAIFEKIAKETGLINANPDGT- 215
Cdd:PRK07564 191 LDR----ALASMTVEV--IDPVADYVEDLENVFDFDAIRKAGLRLGVDPLGGATGPYWKAIAERYGLDLTVVNAPVDPTf 264
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 818488919 216 ---------NINKNCGSQHpeSLKREVLAKKA-DLGLAFDGDGDR 250
Cdd:PRK07564 265 nfmpldddgKIRMDCSSPY--AMAGLLALKDAfDLAFANDPDGDR 307
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
75-250 |
2.84e-09 |
|
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: 59.16 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 75 GILPTPALAFLIKEQRAGAGIVISASHNP---FQDNGLK-------PFKNDGTKLSEEEEKELEGYilkKISSGTNDNIS 144
Cdd:cd03085 87 GLLSTPAVSAVIRKRKATGGIILTASHNPggpEGDFGIKyntsnggPAPESVTDKIYEITKKITEY---KIADDPDVDLS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 145 --GKSSV--------VQEAKEKYIKffLDKTSYFFTL--ELSSRVKKRLVLDCANGATFEVAPAIFEKI--AKETGLINA 210
Cdd:cd03085 164 kiGVTKFggkpftveVIDSVEDYVE--LMKEIFDFDAikKLLSRKGFKVRFDAMHGVTGPYAKKIFVEElgAPESSVVNC 241
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 818488919 211 NPdgtniNKNCGSQHP-------ESLKREVLAKKADLGLAFDGDGDR 250
Cdd:cd03085 242 TP-----LPDFGGGHPdpnltyaKDLVELMKSGEPDFGAASDGDGDR 283
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
4-110 |
2.33e-08 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 56.23 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 4 FGTDGIRGV--AGGEKMNPEVVAAFGRSIVSFCRKRNLPEK----IIVGRDTRESGLMFEEALVAGISSAGGEAAVAG-I 76
Cdd:PTZ00150 47 FGTAGLRGKmgAGFNCMNDLTVQQTAQGLCAYVIETFGQALksrgVVIGYDGRYHSRRFAEITASVFLSKGFKVYLFGqT 126
|
90 100 110
....*....|....*....|....*....|....
gi 818488919 77 LPTPALAFLIKEQRAGAGIVISASHNPFQDNGLK 110
Cdd:PTZ00150 127 VPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYK 160
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
4-110 |
6.02e-06 |
|
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: 48.40 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818488919 4 FGTDGIRGVAGGEKMNPEVVAAFGRSIVSFCRKRNLPEKIIVGRDT-------RESGLmfeEALVAGissaGGEAAVA-- 74
Cdd:cd05801 23 FGTSGHRGSSLKGSFNEAHILAISQAICDYRKSQGITGPLFLGKDThalsepaFISAL---EVLAAN----GVEVIIQqn 95
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 818488919 75 -GILPTPALAFLIKEQRAGA------GIVISASHNPFQDNGLK 110
Cdd:cd05801 96 dGYTPTPVISHAILTYNRGRtegladGIVITPSHNPPEDGGFK 138
|
|
| |
