|
Name |
Accession |
Description |
Interval |
E-value |
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
4-438 |
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: 735.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 4 YFGTDGVRGVANKELTPELAFKIGRFGGYVLTKDTDRPKVIIGRDTRISGHMLEGALVAGLLSTGAEVMRLGVISTPGVA 83
Cdd:cd05802 1 LFGTDGIRGVANEPLTPELALKLGRAAGKVLGKGGGRPKVLIGKDTRISGYMLESALAAGLTSAGVDVLLLGVIPTPAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 84 YLTKALDAQAGVMISASHNPVQDNGIKFFGSDGFKLTDEQEAEIEALLDKEVDELPrpTGTNLGQVSDYFEGGQKYLQYI 163
Cdd:cd05802 81 YLTRKLRADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVEEEIEALIDKELELPP--TGEKIGRVYRIDDARGRYIEFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 164 KQTVE-EDFSGLHIALDCAHGATSSLAPYLFADLEADISTMGTSPNGMNINDGVGSTHPEVLAELVKEKGADIGLAFDGD 242
Cdd:cd05802 159 KSTFPkDLLSGLKIVLDCANGAAYKVAPEVFRELGAEVIVINNAPDGLNINVNCGSTHPESLQKAVLENGADLGIAFDGD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 243 GDRLIAVDEKGNIVDGDQIMFICAKYMKETGQLKHNTVVSTVMSNLGFYKALEANGITSDKTAVGDRYVMEEMKRGGYNL 322
Cdd:cd05802 239 ADRVIAVDEKGNIVDGDQILAICARDLKERGRLKGNTVVGTVMSNLGLEKALKELGIKLVRTKVGDRYVLEEMLKHGANL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 323 GGEQSGHIILLDYITTGDGMLSALQLVNIMKMTKKPLSELAGEMTKFPQLLVNVRVTDKKLALENEKIKEIIRVVEEEMN 402
Cdd:cd05802 319 GGEQSGHIIFLDHSTTGDGLLTALQLLAIMKRSGKSLSELASDMKLYPQVLVNVRVKDKKALLENPRVQAAIAEAEKELG 398
|
410 420 430
....*....|....*....|....*....|....*.
gi 446443619 403 GDGRILVRPSGTEPLIRVMAEAPTQEVCDAYVHRIV 438
Cdd:cd05802 399 GEGRVLVRPSGTEPLIRVMVEGEDEELVEKLAEELA 434
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
5-443 |
0e+00 |
|
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: 628.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 5 FGTDGVRGVANKE-LTPELAFKIGRFGGYVLTKDTD-RPKVIIGRDTRISGHMLEGALVAGLLSTGAEVMRLGVISTPGV 82
Cdd:TIGR01455 1 FGTDGVRGRAGQEpLTAELALLLGAAAGRVLRQGRDtAPRVVIGKDTRLSGYMLENALAAGLNSAGVDVLLLGPLPTPAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 83 AYLTKALDAQAGVMISASHNPVQDNGIKFFGSDGFKLTDEQEAEIEALLDKEvDELPRPTGTNLGQVSDYFEGGQKYLQY 162
Cdd:TIGR01455 81 AYLTRTLRADAGVMISASHNPYEDNGIKFFGPGGFKLDDATEAAIEALLDEA-DPLPRPESEGLGRVKRYPDAVGRYIEF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 163 IKQTV--EEDFSGLHIALDCAHGATSSLAPYLFADLEADISTMGTSPNGMNINDGVGSTHPEVLAELVKEKGADIGLAFD 240
Cdd:TIGR01455 160 LKSTLprGLTLSGLKVVLDCANGAAYKVAPHVFRELGAEVIAIGVEPDGLNINDGCGSTHLDALQKAVREHGADLGIAFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 241 GDGDRLIAVDEKGNIVDGDQIMFICAKYMKETGQLKHNTVVSTVMSNLGFYKALEANGITSDKTAVGDRYVMEEMKRGGY 320
Cdd:TIGR01455 240 GDADRVLAVDANGRIVDGDQILYIIARALKESGELAGNTVVATVMSNLGLERALEKLGLTLIRTAVGDRYVLEEMRESGY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 321 NLGGEQSGHIILLDYITTGDGMLSALQLVNIMKMTKKPLSELAGEMTKFPQLLVNVRVTDKKLAL-ENEKIKEIIRVVEE 399
Cdd:TIGR01455 320 NLGGEQSGHIILLDYSTTGDGIVSALQVLTIMKKSGSTLSELAAEFVPYPQTLVNVRVADRKLAAaEAPAVKAAIEDAEA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 446443619 400 EMNGDGRILVRPSGTEPLIRVMAEAPTQEVCDAYVHRIVEVVKA 443
Cdd:TIGR01455 400 ELGGTGRILLRPSGTEPLIRVMVEAADEELVQQLADTLADVVSA 443
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
2-445 |
0e+00 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 560.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 2 GKYFGTDGVRGVANKELTPELAFKIGRFGGYVLtKDTDRPKVIIGRDTRISGHMLEGALVAGLLSTGAEVMRLGVISTPG 81
Cdd:COG1109 4 KKLFGTDGIRGIVGEELTPEFVLKLGRAFGTYL-KEKGGPKVVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVPTPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 82 VAYLTKALDAQAGVMISASHNPVQDNGIKFFGSDGFKLTDEQEAEIEALLDKEvdELPRPTGTNLGQVSDYFEGGQKYLQ 161
Cdd:COG1109 83 LAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKE--DFRRAEAEEIGKVTRIEDVLEAYIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 162 YIKQTVEED--FSGLHIALDCAHGATSSLAPYLFADLEADISTMGTSPNGMNINDGVG--STHPEVLAELVKEKGADIGL 237
Cdd:COG1109 161 ALKSLVDEAlrLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFPNHNPNpePENLEDLIEAVKETGADLGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 238 AFDGDGDRLIAVDEKGNIVDGDQIMFICAKYMKETGqlKHNTVVSTVMSNLGFYKALEANGITSDKTAVGDRYVMEEMKR 317
Cdd:COG1109 241 AFDGDADRLGVVDEKGRFLDGDQLLALLARYLLEKG--PGGTVVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKMRE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 318 GGYNLGGEQSGHIILLDYITTGDGMLSALQLVNIMKMTKKPLSELAGEMTKFPQLLVNVRVTDK-KLALENEKIKEI--- 393
Cdd:COG1109 319 TGAVLGGEESGGIIFPDFVPTDDGILAALLLLELLAKQGKSLSELLAELPRYPQPEINVRVPDEeKIGAVMEKLREAved 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 446443619 394 ------IRVVEEEMNGDGRILVRPSGTEPLIRVMAEAPTQEVCDAYVHRIVEVVKAEV 445
Cdd:COG1109 399 keeldtIDGVKVDLEDGGWVLVRPSGTEPLLRVYAEAKDEEEAEELLAELAELVEEAL 456
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
3-443 |
0e+00 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 555.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 3 KYFGTDGVRG-VANKELTPELAFKIGRFGGYVLTKdTDRPKVIIGRDTRISGHMLEGALVAGLLSTGAEVMRLGVISTPG 81
Cdd:PRK10887 2 KYFGTDGIRGkVGQAPITPDFVLKLGWAAGKVLAR-QGRPKVLIGKDTRISGYMLESALEAGLAAAGVDVLLTGPMPTPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 82 VAYLTKALDAQAGVMISASHNPVQDNGIKFFGSDGFKLTDEQEAEIEALLDKevdELPRPTGTNLGQVSDYFEGGQKYLQ 161
Cdd:PRK10887 81 VAYLTRTLRAEAGIVISASHNPYYDNGIKFFSADGTKLPDEVELAIEAELDK---PLTCVESAELGKASRINDAAGRYIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 162 YIKQTV--EEDFSGLHIALDCAHGATSSLAPYLFADLEADISTMGTSPNGMNINDGVGSTHPEVLAELVKEKGADIGLAF 239
Cdd:PRK10887 158 FCKSTFpnELSLRGLKIVVDCANGATYHIAPNVFRELGAEVIAIGCEPNGLNINDECGATDPEALQAAVLAEKADLGIAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 240 DGDGDRLIAVDEKGNIVDGDQIMFICAKYMKETGQLkHNTVVSTVMSNLGFYKALEANGITSDKTAVGDRYVMEEMKRGG 319
Cdd:PRK10887 238 DGDGDRVIMVDHLGNLVDGDQLLYIIARDRLRRGQL-RGGVVGTLMSNMGLELALKQLGIPFVRAKVGDRYVLEKLQEKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 320 YNLGGEQSGHIILLDYITTGDGMLSALQLVNIMKMTKKPLSELAGEMTKFPQLLVNVRVT-DKKLALENEKIKEIIRVVE 398
Cdd:PRK10887 317 WRLGGENSGHILCLDKTTTGDGIVAALQVLAAMVRSGMSLADLCSGMKLFPQVLINVRFKpGADDPLESEAVKAALAEVE 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 446443619 399 EEMNGDGRILVRPSGTEPLIRVMAEAPTQEVCDAYVHRIVEVVKA 443
Cdd:PRK10887 397 AELGGRGRVLLRKSGTEPLIRVMVEGEDEAQVTALAERIADAVKA 441
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
2-441 |
4.20e-131 |
|
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: 385.71 E-value: 4.20e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 2 GKYFGTDGVRGVANKELTPELAFKIGR-FGGYVltkdtDRPKVIIGRDTRISGHMLEGALVAGLLSTGAEVMRLGVISTP 80
Cdd:TIGR03990 1 MLLFGTSGIRGIVGEELTPELALKVGKaFGTYL-----RGGKVVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLGIAPTP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 81 GVAYLTKALDAQAGVMISASHNPVQDNGIKFFGSDGFKLTDEQEAEIEALLDKEvdELPRPTGTNLGQVSDYFEGGQKYL 160
Cdd:TIGR03990 76 TLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQEEEIEEIAESG--DFERADWDEIGTVTSDEDAIDDYI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 161 QYIKQTVEEDF---SGLHIALDCAHGATSSLAPYLFADLEADISTMGTSPngmninDGVGSTH-----PEVLAEL---VK 229
Cdd:TIGR03990 154 EAILDKVDVEAirkKGFKVVVDCGNGAGSLTTPYLLRELGCKVITLNCQP------DGTFPGRnpeptPENLKDLsalVK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 230 EKGADIGLAFDGDGDRLIAVDEKGNIVDGDQIMFICAKYMketgqLKHN--TVVSTVMSNLGFYKALEANGITSDKTAVG 307
Cdd:TIGR03990 228 ATGADLGIAHDGDADRLVFIDEKGRFIGGDYTLALFAKYL-----LEHGggKVVTNVSSSRAVEDVAERHGGEVIRTKVG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 308 DRYVMEEMKRGGYNLGGEQSGHIILLDYITTGDGMLSALQLVNIMKMTKKPLSELAGEMTKFPqllvNVRvtdKKLALEN 387
Cdd:TIGR03990 303 EVNVAEKMKEEGAVFGGEGNGGWIFPDHHYCRDGLMAAALFLELLAEEGKPLSELLAELPKYP----MSK---EKVELPD 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446443619 388 EKIKEIIRVVEEEMNG--------------DGRILVRPSGTEPLIRVMAEAPTQEVCDAYVHRIVEVV 441
Cdd:TIGR03990 376 EDKEEVMEAVEEEFADaeidtidgvridfeDGWVLVRPSGTEPIVRIYAEAKTEERAEELLEEGRSLV 443
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
4-441 |
1.64e-120 |
|
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: 358.42 E-value: 1.64e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 4 YFGTDGVRGVANKELTPELAFKIGR-FGGYVltkdtDRPKVIIGRDTRISGHMLEGALVAGLLSTGAEVMRLGVISTPGV 82
Cdd:cd03087 1 LFGTSGIRGVVGEELTPELALKVGKaLGTYL-----GGGTVVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDIGIVPTPAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 83 AYLTKALDAqAGVMISASHNPVQDNGIKFFGSDGFKLTDEQEAEIEALLDKEVdeLPRPTGTNLGQVSDYFEGGQKYLQY 162
Cdd:cd03087 76 QYAVRKLGD-AGVMITASHNPPEYNGIKLVNPDGTEFSREQEEEIEEIIFSER--FRRVAWDEVGSVRREDSAIDEYIEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 163 IKQTVEEDFS-GLHIALDCAHGATSSLAPYLFADLEADISTMGTSPNGMNIndgvgSTHPE-------VLAELVKEKGAD 234
Cdd:cd03087 153 ILDKVDIDGGkGLKVVVDCGNGAGSLTTPYLLRELGCKVITLNANPDGFFP-----GRPPEptpenlsELMELVRATGAD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 235 IGLAFDGDGDRLIAVDEKGNIVDGDQIMFICAKYMKETGQLKhntVVSTVMSNLGFYKALEANGITSDKTAVGDRYVMEE 314
Cdd:cd03087 228 LGIAHDGDADRAVFVDEKGRFIDGDKLLALLAKYLLEEGGGK---VVTPVDASMLVEDVVEEAGGEVIRTPVGDVHVAEE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 315 MKRGGYNLGGEQSGHIILLDYITTGDGMLSALQLVNIMKmTKKPLSELAGEMTKFPQLLVNVRVTDKKLALENEKIKEII 394
Cdd:cd03087 305 MIENGAVFGGEPNGGWIFPDHQLCRDGIMTAALLLELLA-EEKPLSELLDELPKYPLLREKVECPDEKKEEVMEAVEEEL 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 446443619 395 RVVEEEMN---------GDGRILVRPSGTEPLIRVMAEAPTQEVCDAYVHRIVEVV 441
Cdd:cd03087 384 SDADEDVDtidgvrieyEDGWVLIRPSGTEPKIRITAEAKTEERAKELLEEGRSKV 439
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
10-441 |
1.23e-93 |
|
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: 289.80 E-value: 1.23e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 10 VRGVANKELTPELAFKIGR-FGGYVltKDTDRPKVIIGRDTRISGHMLEGALVAGLLSTGAEVMRLGVISTPGVAYLTKA 88
Cdd:cd03089 7 IRGIAGEELTEEIAYAIGRaFGSWL--LEKGAKKVVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPVLYFATFH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 89 LDAQAGVMISASHNPVQDNGIKFFGSDGfKLTDEQEAEIEALLDKEVDELPRPTGTnlGQVSDYFEggqKYLQYIKQTVE 168
Cdd:cd03089 85 LDADGGVMITASHNPPEYNGFKIVIGGG-PLSGEDIQALRERAEKGDFAAATGRGS--VEKVDILP---DYIDRLLSDIK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 169 EDFSGLHIALDCAHGATSSLAPYLFADLEADISTM-----GTSPNGmnINDgvgSTHPEVLAEL---VKEKGADIGLAFD 240
Cdd:cd03089 159 LGKRPLKVVVDAGNGAAGPIAPQLLEALGCEVIPLfcepdGTFPNH--HPD---PTDPENLEDLiaaVKENGADLGIAFD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 241 GDGDRLIAVDEKGNIVDGDQIMFICAKYMketgqLKHN---TVVSTVMSNLGFYKALEANGITSDKTAVGDRYVMEEMKR 317
Cdd:cd03089 234 GDGDRLGVVDEKGEIIWGDRLLALFARDI-----LKRNpgaTIVYDVKCSRNLYDFIEEAGGKPIMWKTGHSFIKAKMKE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 318 GGYNLGGEQSGHIIL------LDyittgDGMLSALQLVNIMKMTKKPLSELAGEMTKFPQLL-VNVRVTDKKLALENEKI 390
Cdd:cd03089 309 TGALLAGEMSGHIFFkdrwygFD-----DGIYAALRLLELLSKSGKTLSELLADLPKYFSTPeIRIPVTEEDKFAVIERL 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 391 KEIIRVVEEEMN---------GDGRILVRPSGTEPLIRVMAEAPTQEVCDAYVHRIVEVV 441
Cdd:cd03089 384 KEHFEFPGAEIIdidgvrvdfEDGWGLVRASNTEPVLVLRFEADTEEGLEEIKAELRKLL 443
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
4-428 |
8.64e-77 |
|
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: 243.42 E-value: 8.64e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 4 YFGTDGVRGVANKELTPELAFKIGRfggyvltkdtdrpkvIIGRdtrisghmlegalvagllstgaevmrlgvistpgva 83
Cdd:cd03084 1 IFGTSGVRGVVGDDITPETAVALGQ---------------AIGS------------------------------------ 29
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 84 yltkaldaQAGVMISASHNPVQDNGIKFFGSDGFKLTDEQEAEIEALLDKEvdELPRPTGTNLGQVS-------DYFEGG 156
Cdd:cd03084 30 --------TGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKE--DEPSAVAYELGGSVkavdilqRYFEAL 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 157 QKYLQyiKQTVEEdfSGLHIALDCAHGATSSLAPYLFADLEADISTMGTSPNGmniNDGVGSTHPEV------LAELVKE 230
Cdd:cd03084 100 KKLFD--VAALSN--KKFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCEPDG---NFGNINPDPGSetnlkqLLAVVKA 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 231 KGADIGLAFDGDGDRLIAVDEKGNIVDGDQIMFICAKYMKETGQLKhNTVVSTVMSNLGFYKALEANGITSDKTAVGDRY 310
Cdd:cd03084 173 EKADFGVAFDGDADRLIVVDENGGFLDGDELLALLAVELFLTFNPR-GGVVKTVVSSGALDKVAKKLGIKVIRTKTGFKW 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 311 VMEEMKRGGYNLGGEQSGHIILLDYITTGDGMLSALQLVNIMKMTKKPLSELAGEMTKFPQLLVNVRvtdkklaleneki 390
Cdd:cd03084 252 VGEAMQEGDVVLGGEESGGVIFPEFHPGRDGISAALLLLEILANLGKSLSELFSELPRYYYIRLKVR------------- 318
|
410 420 430
....*....|....*....|....*....|....*...
gi 446443619 391 keiirvveeemngdGRILVRPSGTEPLIRVMAEAPTQE 428
Cdd:cd03084 319 --------------GWVLVRASGTEPAIRIYAEADTQE 342
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
5-428 |
8.96e-74 |
|
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: 238.99 E-value: 8.96e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 5 FGTDGVRGVANKELTPE----LAFKIGRfggYVLTKDTDRPKVIIGRDTR-ISGHMleGALVAGLL-STGAEVmRL--GV 76
Cdd:cd05800 3 FGTDGWRGIIAEDFTFEnvrrVAQAIAD---YLKEEGGGGRGVVVGYDTRfLSEEF--ARAVAEVLaANGIDV-YLsdRP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 77 ISTPGVAYLTKALDAQAGVMISASHNPVQDNGIKFFGSDGFKLTDEQEAEIEALLDKEVDELPRPTGTNLGQVSDYFEGg 156
Cdd:cd05800 77 VPTPAVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARLASGEPPGLEARAEGLIETIDPKPD- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 157 qkYLQYIKQTVEEDF---SGLHIALDCAHGATSSLAPYLFADLEADISTmgtspngmnINDGV----GSTHPE------- 222
Cdd:cd05800 156 --YLEALRSLVDLEAireAGLKVVVDPMYGAGAGYLEELLRGAGVDVEE---------IRAERdplfGGIPPEpieknlg 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 223 VLAELVKEKGADIGLAFDGDGDRLIAVDEKGNIVDGDQIMFICAKYMKETGQLKhNTVVSTV-MSNLgFYKALEANGITS 301
Cdd:cd05800 225 ELAEAVKEGGADLGLATDGDADRIGAVDEKGNFLDPNQILALLLDYLLENKGLR-GPVVKTVsTTHL-IDRIAEKHGLPV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 302 DKTAVGDRYVMEEMKRGGYNLGGEQSGHIILLDYITTGDGMLSALQLVNIMKMTKKPLSELAGEMTK----FPQLLVNVR 377
Cdd:cd05800 303 YETPVGFKYIAEKMLEEDVLIGGEESGGLGIRGHIPERDGILAGLLLLEAVAKTGKPLSELVAELEEeygpSYYDRIDLR 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446443619 378 VTDKKLA-----LENEKIKEII--RVVEE-EMNG-------DGRILVRPSGTEPLIRVMAEAPTQE 428
Cdd:cd05800 383 LTPAQKEailekLKNEPPLSIAggKVDEVnTIDGvklvledGSWLLIRPSGTEPLLRIYAEAPSPE 448
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
9-432 |
2.81e-72 |
|
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: 234.51 E-value: 2.81e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 9 GVRGVANKELTPELAFK-IGRFGGYVLTKdTDRPKVIIGRDTRISGHMLEGALVAGLLSTGAEVMRLGVISTPGVAYLTK 87
Cdd:cd05803 6 GIRGIVGEGLTPEVITRyVAAFATWQPER-TKGGKIVVGRDGRPSGPMLEKIVIGALLACGCDVIDLGIAPTPTVQVLVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 88 ALDAQAGVMISASHNPVQDNGIKFFGSDGFKLTDEQEAEIEALLDKevDELPRPTGTNLGQVSDYFEGGQKYLQYIKQTV 167
Cdd:cd05803 85 QSQASGGIIITASHNPPQWNGLKFIGPDGEFLTPDEGEEVLSCAEA--GSAQKAGYDQLGEVTFSEDAIAEHIDKVLALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 168 EEDFSGLH-----IALDCAHGATSSLAPYLFADLEADISTMGTSPngmninDGVGSTHPEVLAE-------LVKEKGADI 235
Cdd:cd05803 163 DVDVIKIRernfkVAVDSVNGAGGLLIPRLLEKLGCEVIVLNCEP------TGLFPHTPEPLPEnltqlcaAVKESGADV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 236 GLAFDGDGDRLIAVDEKGNIVDGDQIMFICAKYMKETGQLKHNTVVSTVMSNLGFYKAlEANGITSDKTAVGDRYVMEEM 315
Cdd:cd05803 237 GFAVDPDADRLALVDEDGRPIGEEYTLALAVDYVLKYGGRKGPVVVNLSTSRALEDIA-RKHGVPVFRSAVGEANVVEKM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 316 KRGGYNLGGEQSGHIILLDYITTGDGMLSALQLVNIMKMTKKPLSELAGEMTKFPQLLVNVRVTDKKLA-LENEKIKEII 394
Cdd:cd05803 316 KEVDAVIGGEGNGGVILPDVHYGRDSLVGIALVLQLLAASGKPLSEIVDELPQYYISKTKVTIAGEALErLLKKLEAYFK 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 446443619 395 RVVEEEMNG------DGRILVRPSGTEPLIRVMAEAPTQEVCDA 432
Cdd:cd05803 396 DAEASTLDGlrldseDSWVHVRPSNTEPIVRIIAEAPTQDEAEA 439
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
10-443 |
2.17e-52 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 182.10 E-value: 2.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 10 VRGVANKELTPELAFKIGrfGGYV-LTKDTDRPKVIIGRDTRISGHMLEGALVAGLLSTGAEVMRLGVISTPGVAYLTKA 88
Cdd:PRK09542 6 VRGVVGEQIDEDLVRDVG--AAFArLMRAEGATTVVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIGLASTDQLYFASGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 89 LDAqAGVMISASHNPVQDNGIKF-------FGSD-GFkltdeqeAEIEALLDKEVDELPRPTGTNLGQvsDYFEGgqkYL 160
Cdd:PRK09542 84 LDC-PGAMFTASHNPAAYNGIKLcragakpVGQDtGL-------AAIRDDLIAGVPAYDGPPGTVTER--DVLAD---YA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 161 QYIKQTVeeDFSG---LHIALDCAHGATSSLAPYLFADLEADISTM-----GTSPNG-------MNINDgvgsthpevLA 225
Cdd:PRK09542 151 AFLRSLV--DLSGirpLKVAVDAGNGMGGHTVPAVLGGLPITLLPLyfeldGTFPNHeanpldpANLVD---------LQ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 226 ELVKEKGADIGLAFDGDGDRLIAVDEKGNIVDGDQIMFICAKymKETGQLKHNTVVSTVMSNLGFYKALEANGITSDKTA 305
Cdd:PRK09542 220 AFVRETGADIGLAFDGDADRCFVVDERGQPVSPSAVTALVAA--RELAREPGATIIHNLITSRAVPELVAERGGTPVRTR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 306 VGDRYVMEEMKRGGYNLGGEQSGHIILLDYITTGDGMLSALQLVNIMKMTKKPLSELAGEMTKFPQL-LVNVRVTDKKLA 384
Cdd:PRK09542 298 VGHSFIKALMAETGAIFGGEHSAHYYFRDFWGADSGMLAALHVLAALGEQDRPLSELMADYQRYAASgEINSTVADAPAR 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446443619 385 LenEKIKEII--RVVE-EEMNG------DGRIL-VRPSGTEPLIRVMAEAPTQEVCDAYVHRIVEVVKA 443
Cdd:PRK09542 378 M--EAVLKAFadRIVSvDHLDGvtvdlgDGSWFnLRASNTEPLLRLNVEARTEEEVDALVDEVLAIIRA 444
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
2-134 |
4.69e-52 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 171.64 E-value: 4.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 2 GKYFGTDGVRGVAN-KELTPELAFKIGRFGGYVLTKDTDRPKVIIGRDTRISGHMLEGALVAGLLSTGAEVMRLGVISTP 80
Cdd:pfam02878 1 RQLFGTSGIRGKVGvGELTPEFALKLGQAIASYLRAQGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 446443619 81 GVAYLTKALDAQAGVMISASHNPVQDNGIKFFGSDGFKLTDEQEAEIEALLDKE 134
Cdd:pfam02878 81 AVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKE 134
|
|
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
5-441 |
6.26e-50 |
|
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: 175.51 E-value: 6.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 5 FGTDGVRGVANKELTPELAFKIGRFGGYVLTKDTdrpKVIIGRDTRISGHMLEGALVAGLLSTGAEVMRLGVISTPGVAY 84
Cdd:cd05805 2 FGGRGVSGLINVDITPEFATRLGAAYGSTLPPGS---TVTVSRDASRASRMLKRALISGLLSTGVNVRDLGALPLPVARY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 85 LTKALDAQAGVMISAShnpVQDNG---IKFFGSDGFKLTDEQEAEIEALLDKE------VDELPRPtgTNLGQVSDYfeg 155
Cdd:cd05805 79 AIRFLGASGGIHVRTS---PDDPDkveIEFFDSRGLNISRAMERKIENAFFREdfrrahVDEIGDI--TEPPDFVEY--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 156 gqkYLQYIKQTVEED---FSGLHIALDCAHGATSSLAPYLFADLEADISTmgtspNGMNINDGVGSTHPEV------LAE 226
Cdd:cd05805 151 ---YIRGLLRALDTSglkKSGLKVVIDYAYGVAGIVLPGLLSRLGCDVVI-----LNARLDEDAPRTDTERqrsldrLGR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 227 LVKEKGADIGLAFDGDGDRLIAVDEKGNIVDGDQIMFICAKYMKETGQLKhnTVV-----STVMSNLgfykaLEANGITS 301
Cdd:cd05805 223 IVKALGADFGVIIDPNGERLILVDEAGRVISDDLLTALVSLLVLKSEPGG--TVVvpvtaPSVIEQL-----AERYGGRV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 302 DKTAVGDRYVMEEMKRGGYNLGGEQSGHIILLDYITTgDGMLSALQLVNIMKMTKKPLSELAGEMTKFPQLLVNVRV--T 379
Cdd:cd05805 296 IRTKTSPQALMEAALENVVLAGDGDGGFIFPEFHPGF-DAIAALVKILEMLARTNISLSQIVDELPRFYVLHKEVPCpwE 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446443619 380 DK-----KLALENEKiKEI-----IRVVEEemngDGRILVRPSGTEPLIRVMAEAPTQEVCDAYVHRIVEVV 441
Cdd:cd05805 375 AKgrvmrRLIEEAPD-KSIelidgVKIYED----DGWVLVLPDADEPLCHIYAEGSDQERAEELTEFYVEKV 441
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
257-368 |
4.99e-47 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 157.61 E-value: 4.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 257 DGDQIMFICAKYMKETGQLKHNT-VVSTVMSNLGFYKALEANGITSDKTAVGDRYVMEEMKRGGYNLGGEQSGHIILLDY 335
Cdd:pfam02880 1 DGDQILALLAKYLLEQGKLPPGAgVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLDH 80
|
90 100 110
....*....|....*....|....*....|...
gi 446443619 336 ITTGDGMLSALQLVNIMKMTKKPLSELAGEMTK 368
Cdd:pfam02880 81 ATTKDGILAALLVLEILARTGKSLSELLEELPE 113
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
5-424 |
7.72e-35 |
|
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: 135.33 E-value: 7.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 5 FGTDGVRGV----ANK--ELTpelafkIGR----FGGYVLTKDTDR--PKVIIGRDTRisgHM-----LEGALVagLLST 67
Cdd:cd05799 4 FGTAGLRGKmgagTNRmnDYT------VRQatqgLANYLKKKGPDAknRGVVIGYDSR---HNsrefaELTAAV--LAAN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 68 GAEVMRL-GVISTPGVAYLTKALDAQAGVMISASHNPVQDNGIKFFGSDGFKLTDEQEAEIEALLDK--------EVDEL 138
Cdd:cd05799 73 GIKVYLFdDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAvlepldikFEEAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 139 PRPTGTNLGQ--VSDYFEGGQKYLQYIKQTVEEDFSGLHIALdcaHGATSSLAPYLFADL------------EADistmG 204
Cdd:cd05799 153 DSGLIKYIGEeiDDAYLEAVKKLLVNPELNEGKDLKIVYTPL---HGVGGKFVPRALKEAgftnvivveeqaEPD----P 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 205 TSPNgmnindgVGSTHPE-----VLA-ELVKEKGADIGLAFDGDGDRL-IAV---DEKGNIVDGDQIMFICAKY----MK 270
Cdd:cd05799 226 DFPT-------VKFPNPEepgalDLAiELAKKVGADLILATDPDADRLgVAVkdkDGEWRLLTGNEIGALLADYlleqRK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 271 ETGQLKHNTVV--STVMSNLGfyKAL-EANGITSDKTAVGDRY---VMEEMKRGGYNL--GGEQS-GHIIlLDYITTGDG 341
Cdd:cd05799 299 EKGKLPKNPVIvkTIVSSELL--RKIaKKYGVKVEETLTGFKWignKIEELESGGKKFlfGFEESiGYLV-GPFVRDKDG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 342 MLSALQLVNIMKMTKKP-------LSELAGE----MTKfpqlLVNVRVTDKKlalENEKIKEIIR-------VVEEEMNG 403
Cdd:cd05799 376 ISAAALLAEMAAYLKAQgktlldrLDELYEKygyyKEK----TISITFEGKE---GPEKIKAIMDrlrnnpnVLTFYLED 448
|
490 500
....*....|....*....|.
gi 446443619 404 DGRILVRPSGTEPLIRVMAEA 424
Cdd:cd05799 449 GSRVTVRPSGTEPKIKFYIEV 469
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
5-438 |
2.32e-34 |
|
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: 133.48 E-value: 2.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 5 FGTDGVRGVANkELTPELAFKIGR-FGGYVLTKdTDRPKVIIGRDTRISGHMLEGALVAGLLSTGAEVMRLGVISTPGVA 83
Cdd:cd03088 2 FGTSGLRGLVT-DLTDEVCYAYTRaFLQHLESK-FPGDTVAVGRDLRPSSPRIAAACAAALRDAGFRVVDCGAVPTPALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 84 YltKALDAQAG-VMISASHNPVQDNGIKFFGSDGfKLTDEQEAEIEALLDKEVDELPRPTGTNLGQVSDyfeGGQKYLQ- 161
Cdd:cd03088 80 L--YAMKRGAPaIMVTGSHIPADRNGLKFYRPDG-EITKADEAAILAALVELPEALFDPAGALLPPDTD---AADAYIAr 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 162 YIKQTVEEDFSGLHIALDcAHgatSSLA----PYLFADLEADISTMGTSPNGMNIN-DGVGSTHPEVLAELVKEKGADIG 236
Cdd:cd03088 154 YTDFFGAGALKGLRIGVY-QH---SSVGrdllVRILEALGAEVVPLGRSDTFIPVDtEAVRPEDRALAAAWAAEHGLDAI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 237 LAFDGDGDR-LIAvDEKGNIVDGDQIMFICAKYmketgqLKHNTVVSTVMSNlgfyKALEANGITS--DKTAVGDRYVME 313
Cdd:cd03088 230 VSTDGDGDRpLVA-DETGEWLRGDILGLLTARF------LGADTVVTPVSSN----SAIELSGFFKrvVRTRIGSPYVIA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 314 EMKR---------------GGYNLGGEQSGHIILLDYITTGDGMLSALQLVNIMKMTKKPLSELAGEMTK---------- 368
Cdd:cd03088 299 AMAEaaaagagrvvgyeanGGFLLGSDIERNGRTLKALPTRDAVLPILAVLAAAKEAGIPLSELVASLPArftasdrlqn 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 369 FPQ-----LLVNVRVTDKKLA-LENEKIKEIIRVveEEMNG------DGRIL-VRPSGTEPLIRVMAEAPTQEVCDAYVH 435
Cdd:cd03088 379 FPTeksqaLIARLSADPEARAaFFFALGGEVASI--DTTDGlrmtfaNGDIVhLRPSGNAPELRCYVEADSEERARELLA 456
|
...
gi 446443619 436 RIV 438
Cdd:cd03088 457 RGL 459
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
6-444 |
1.22e-31 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 127.48 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 6 GTDgVRGVA--NKE-----LTPELAFKIGR-FGGYVLTK----DTDRPKVIIGRDTRISGHMLEGALVAGLLSTGAEVMR 73
Cdd:PLN02371 70 GSD-IRGVAveGVEgepvtLTPPAVEAIGAaFAEWLLEKkkadGSGELRVSVGRDPRISGPRLADAVFAGLASAGLDVVD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 74 LGVISTPGVAY--LTKALDAQAGVMISASHNPVQDNGIKFFGSDGfKLTdeqEAEIEALLDKEVDELPRPTGTNLGQVS- 150
Cdd:PLN02371 149 MGLATTPAMFMstLTEREDYDAPIMITASHLPYNRNGLKFFTKDG-GLG---KPDIKDILERAARIYKEWSDEGLLKSSs 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 151 ---------DYFEGGQKYL-QYIKQTV------EEDFSGLHIALDCAHGATSSLAPYLFADLEADIS-TMGTSPNGMNIN 213
Cdd:PLN02371 225 gassvvcrvDFMSTYAKHLrDAIKEGVghptnyETPLEGFKIVVDAGNGAGGFFAEKVLEPLGADTSgSLFLEPDGMFPN 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 214 DGVGSTHPEVLAEL---VKEKGADIGLAFDGDGDRLIAVDEKGNIVDGDQ-IMFICAKYMKEtgqlkH--NTVVSTVMSN 287
Cdd:PLN02371 305 HIPNPEDKAAMSATtqaVLANKADLGIIFDTDVDRSAVVDSSGREINRNRlIALMSAIVLEE-----HpgTTIVTDSVTS 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 288 LGFYKALEANGITSDKTAVGDRYVMEEMKR---GGY--NLGGEQSGHIIL-----LDyittgDGMLSALQLVNIMKMTK- 356
Cdd:PLN02371 380 DGLTTFIEKKGGKHHRFKRGYKNVIDKGVRlnsDGEetHLMIETSGHGALkenhfLD-----DGAYLAVKIIIELVRMRa 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 357 -----------KPLSELA----------GEMTKFPQLLVNVRVTDKKLALENEKIK------EIIRVVEEEMNGDGRILV 409
Cdd:PLN02371 455 agaggglgdliEDLEEPLeavelrlkilDEGKDFKAYGEEVLEHLRNSIESDGKLEgapvnyEGVRVSDEGEGFGGWFLL 534
|
490 500 510
....*....|....*....|....*....|....*
gi 446443619 410 RPSGTEPLIRVMAEAPTQEVCDAYVHRIVEVVKAE 444
Cdd:PLN02371 535 RQSLHDPVIPLNIESSSPGGAQKMALVVLTWLKEF 569
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
10-424 |
2.76e-30 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 121.98 E-value: 2.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 10 VRGVANKELTPELAFKIGR-FGGYVltkdtdRPKVII-GRDTRISGHMLEGALVAGLLSTGAEVMRLGVISTPGVAYLTK 87
Cdd:PRK15414 12 IRGKLGEELNEDIAWRIGRaYGEFL------KPKTIVlGGDVRLTSETLKLALAKGLQDAGVDVLDIGMSGTEEIYFATF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 88 ALDAQAGVMISASHNPVQDNGIKFF--------GSDGfkLTDEQEAEiEALLDKEVDELPRPTGTNLGQVSDYFEggqKY 159
Cdd:PRK15414 86 HLGVDGGIEVTASHNPMDYNGMKLVregarpisGDTG--LRDVQRLA-EANDFPPVDETKRGRYQQINLRDAYVD---HL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 160 LQYIKQtveEDFSGLHIALDCAHGATSSLAPYLFADLEA-----DISTMGTSPNGmNINDGV-GSTHPEVLAEL---VKE 230
Cdd:PRK15414 160 FGYINV---KNLTPLKLVINSGNGAAGPVVDAIEARFKAlgapvELIKVHNTPDG-NFPNGIpNPLLPECRDDTrnaVIK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 231 KGADIGLAFDGDGDRLIAVDEKGNIVDGDQIMFICAKYMKETG---------QLKHNTVvstvmsnlgfyKALEANGITS 301
Cdd:PRK15414 236 HGADMGIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNpgakiihdpRLSWNTV-----------DVVTAAGGTP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 302 DKTAVGDRYVMEEMKRGGYNLGGEQSGHIILLDYITTGDGMLSALQLVNIMKMTKKPLSELAGE-MTKFPQL-LVNVRVT 379
Cdd:PRK15414 305 VMSKTGHAFIKERMRKEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELVCLKGKTLGELVRDrMAAFPASgEINSKLA 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 446443619 380 DKKLALEN------EKIKEIIRVVEEEMN-GDGRILVRPSGTEPLIRVMAEA 424
Cdd:PRK15414 385 QPVEAINRveqhfsREALAVDRTDGISMTfADWRFNLRSSNTEPVVRLNVES 436
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
13-441 |
2.29e-28 |
|
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: 117.31 E-value: 2.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 13 VANKELTPELAFKIGRFGGYVLTKDTD-RPKVIIGRDTRISGHMLEGALVAGLLSTGAEVMRLGVISTPGVAYLTKAlda 91
Cdd:cd03086 74 LANASDDELLVLVLMLISVKELNIDLSvPANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYLVRA--- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 92 qagvmisasHNpvqdngikffgsdgfkltdeqeaeiealldkevdelprpTGTNLGQVSD--YFEGGQK-YLQYIKQTVE 168
Cdd:cd03086 151 ---------AN---------------------------------------TEGAYGEPTEegYYEKLSKaFNELYNLLQD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 169 EDFSGLHIALDCAHG----ATSSLAPYLFADLEADISTMGTSPNGMnINDGVGsthpevlAELVK-EKGADIGL------ 237
Cdd:cd03086 183 GGDEPEKLVVDCANGvgalKLKELLKRLKKGLSVKIINDGEEGPEL-LNDGCG-------ADYVKtKQKPPRGFelkppg 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 238 ----AFDGDGDRLIA--VDEKGN--IVDGDQIMFICAKYMKE-----------------------------TGQLKHNTV 280
Cdd:cd03086 255 vrccSFDGDADRLVYfyPDSSNKfhLLDGDKIATLFAKFIKEllkkageelkltigvvqtayangastkylEDVLKVPVV 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 281 -VSTVMSNL---------GFYkaLEANG----ITSDKTAVGDRYVMEemkrggynLGGEQSGHIILLDYI------TTGD 340
Cdd:cd03086 335 cTPTGVKHLhhaaeefdiGVY--FEANGhgtvLFSESALAKIEENSS--------LSDEQEKAAKTLLAFsrlinqTVGD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 341 ---GMLSALQLVNIMKMTkkpLSELAGEMTKFPQLLVNVRVTDKKL---------ALE----NEKIKEIIRVVEeemngD 404
Cdd:cd03086 405 aisDMLAVELILAALGWS---PQDWDNLYTDLPNRQLKVKVPDRSVikttdaerrLVEpkglQDKIDAIVAKYN-----N 476
|
490 500 510
....*....|....*....|....*....|....*..
gi 446443619 405 GRILVRPSGTEPLIRVMAEAPTQEVCDAYVHRIVEVV 441
Cdd:cd03086 477 GRAFVRPSGTEDVVRVYAEAATQEEADELANEVAELV 513
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
42-446 |
3.81e-20 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 93.18 E-value: 3.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 42 KVIIGRDTRISGHMLEGALVAGL-LSTGAEVMRLGVISTPGVAYLTkaldaqagvmisASHNPvqdngikfFGSDGFKLT 120
Cdd:PTZ00302 154 KVHVGRDTRPSSPELVSALLRGLkLLIGSNVRNFGIVTTPQLHFLV------------AFANG--------LGVDVVESS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 121 DEQEAEiealldkevdelprptgtnlgQVSDYFEGGQKYLQYIKQTVEEDFSGLHIALDCAHGatssLAPYLFADLEADI 200
Cdd:PTZ00302 214 DELYYA---------------------YLLAAFKELYRTLQEGGPVDLTQNNSKILVVDCANG----VGGYKIKRFFEAL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 201 STMGTSPNGMNINDgvgsTHPEVL-----AELV-KEKGADIGL------------AFDGDGDRLIA--VDEKGN----IV 256
Cdd:PTZ00302 269 KQLGIEIIPININC----DEEELLndkcgADYVqKTRKPPRAMkewpgdeetrvaSFDGDADRLVYffPDKDGDdkwvLL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 257 DGDQIMFICAKYMKE---TGQLKHN---TVVSTVMSNLGFYKAL--------------------------------EANG 298
Cdd:PTZ00302 345 DGDRIAILYAMLIKKllgKIQLKKKldiGVVQTAYANGASTNYLnellgrlrvycaptgvknlhpkahkydigiyfEANG 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 299 ----ITSDKtavgdryVMEEMKRGGYNLGGEQSGHIILLDYI-----TTGDGM--LSALQLV-NIMKMTkkpLSELAGEM 366
Cdd:PTZ00302 425 hgtvLFNEK-------ALAEWAKFLAKQNALNSACRQLEKFLrlfnqTIGDAIsdLLAVELAlAFLGLS---FQDWLNLY 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 367 TKFPQLLVNVRVTDKKL---------ALE----NEKIKEIIRVVEEEmngdGRILVRPSGTEPLIRVMAEAPTQEVCDAY 433
Cdd:PTZ00302 495 TDLPSRQDKVTVKDRTLitntedetrLLEpkglQDKIDAIVSKYDNA----ARAFIRPSGTEPVVRVYAEAPTLEQADEL 570
|
490
....*....|...
gi 446443619 434 VHRIVEVVKAEVG 446
Cdd:PTZ00302 571 ANEVKGLVLRYCS 583
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
373-442 |
7.24e-19 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 80.39 E-value: 7.24e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446443619 373 LVNVRVTDKKLALENEKIKEIIRVVEEEMNGDGRIL-VRPSGTEPLIRVMAEAPTQEVCDAYVHRIVEVVK 442
Cdd:pfam00408 1 LINVRVAEKKKLAALAAILKVFADAEKILGEDGRRLdVRPSGTEPVLRVMVEGDSDEELARLADEIADLLE 71
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
36-446 |
3.39e-15 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 77.76 E-value: 3.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 36 KDTDRPKVIIGRDTRISGHMLEGALVAGLLSTGAEVMRLGVISTPGVAYltkaldaqagvMISASHNPVQDNgikffgsd 115
Cdd:PLN02895 123 GGNPPAEVLLGRDTRPSGPALLAAALKGVRAIGARAVDMGILTTPQLHW-----------MVRAANKGMKAT-------- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 116 gfkltdeqeaeiealldkevdelprptgtnlgqVSDYFEGGQKY----LQYIKQTVEEDFSGLHIALDCAHGA----TSS 187
Cdd:PLN02895 184 ---------------------------------ESDYFEQLSSSfralLDLIPNGSGDDRADDKLVVDGANGVgaekLET 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 188 LAPyLFADLEADISTMGTSPNGMnINDGVGsthpevlAELV-KEK-------GADIGL---AFDGDGDRLIAVDEKGN-- 254
Cdd:PLN02895 231 LKK-ALGGLDLEVRNSGKEGEGV-LNEGVG-------ADFVqKEKvpptgfaSKDVGLrcaSLDGDADRLVYFYVSSAgs 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 255 ---IVDGDQIMFICAKYMKEtgQLK-----HNTVVSTVMSNLGFYKALEANGITSDK-----------TAVGDRYVMEEM 315
Cdd:PLN02895 302 kidLLDGDKIASLFALFIKE--QLRilngnGNEKPEELLVRLGVVQTAYANGASTAYlkqvlglevvcTPTGVKYLHEAA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 316 KrgGYNLG--GEQSGH-IIL-----LDYITTGDGMLSAL-----------------QLVN---------------IMKMT 355
Cdd:PLN02895 380 A--EFDIGvyFEANGHgTVLfserfLDWLEAAAAELSSKakgseahkaarrllavsRLINqavgdalsglllveaILQYR 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 356 KKPLSELAGEMTKFPQLLVNVRVTDK---------KLALENEKIKEIIRVVEEEMNGdGRILVRPSGTEPLIRVMAEAPT 426
Cdd:PLN02895 458 GWSLAEWNALYQDLPSRQLKVKVADRtaitttdaeTVVVRPAGLQDAIDAEVAKYPR-GRAFVRPSGTEDVVRVYAEAST 536
|
490 500
....*....|....*....|
gi 446443619 427 QEVCDAYVHRIVEVVKAEVG 446
Cdd:PLN02895 537 QEAADSLAREVARLVYDLLG 556
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
68-423 |
1.03e-14 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 75.94 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 68 GAEVM---RLGVISTPGV-----AYLTKALDAQAGVMISASHNPVQDNGIKFFGSDG----FKLTDEQEAEIEALLDKEV 135
Cdd:PRK07564 104 GVGVVivgRGGYTPTPAVshailKYNGRGGGLADGIVITPSHNPPEDGGIKYNPPNGgpadTDVTDAIEARANELLAYGL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 136 DELPRPTGTNLGQ---------VSDYFEGGQKYLqyikqtveeDF-----SGLHIALDCAHGATSSLAPYLFADLEADIS 201
Cdd:PRK07564 184 KGVKRIPLDRALAsmtvevidpVADYVEDLENVF---------DFdairkAGLRLGVDPLGGATGPYWKAIAERYGLDLT 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 202 TMGTSP----NGMNI-NDGVG-----STHpeVLAELVKEKGA-DIGLAFDGDGDRliavdekgN-IVDGDQIM------F 263
Cdd:PRK07564 255 VVNAPVdptfNFMPLdDDGKIrmdcsSPY--AMAGLLALKDAfDLAFANDPDGDR--------HgIVTPGGLMnpnhylA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 264 ICAKYmketgqLKHN------------TVVSTVMSNlgfyKALEANGITSDKTAVGDRYVMEEMKRGGYNLGGEQS-GHI 330
Cdd:PRK07564 325 VAIAY------LFHHrpgwragagvgkTLVSSAMID----RVAAKLGRKLYEVPVGFKWFVNGLDDGSLGFGGEESaGAS 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 331 ILL----DYITTGDGMLSALQLVNIMKMTKKPLSELAGEMT---------------------KFPQLLVNVrVTDKKLAl 385
Cdd:PRK07564 395 FLRrdgsVWTTDKDGLIAVLLAAEILAVTGKSPSEIYRELWarfgrpyysrhdapatpeqkaALRKLSPEL-VGATELA- 472
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 446443619 386 eNEKIKEI-------------IRVVEEemngDGRILVRPSGTEPLIRVMAE 423
Cdd:PRK07564 473 -GDPIDASlteapgngaaiggLKVVTE----NGWFAARPSGTETTYKIYAE 518
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
159-253 |
3.88e-14 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 68.09 E-value: 3.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 159 YLQYIKQTVEEDF---SGLHIALDCAHGATSSLAPYLFADLEADISTMGTSPNGMNINDGVGSTHPEVLA---ELVKEKG 232
Cdd:pfam02879 2 YIDHLLELVDSEAlkkRGLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDPDFPTRAPNPEEPEALAlliELVKSVG 81
|
90 100
....*....|....*....|.
gi 446443619 233 ADIGLAFDGDGDRLIAVDEKG 253
Cdd:pfam02879 82 ADLGIATDGDADRLGVVDERG 102
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
43-307 |
1.40e-13 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 72.79 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 43 VIIGRDTRIsgHMLEGALVAG--LLSTGAEVMRLG-VISTPGVAYLTKALDAQAGVMISASHNPVQDNGIKFFGSDGFKL 119
Cdd:PTZ00150 92 VVIGYDGRY--HSRRFAEITAsvFLSKGFKVYLFGqTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVYWSNGAQI 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 120 TDEQEAEIEALLDKEVDELPRP-TGTNLGQVSD-YFEGGQKYLQYIKQTV---EEDFSGLHIALDCAHG----------A 184
Cdd:PTZ00150 170 IPPHDKNISAKILSNLEPWSSSwEYLTETLVEDpLAEVSDAYFATLKSEYnpaCCDRSKVKIVYTAMHGvgtrfvqkalH 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 185 TSSLAPYLFADLEA----DISTMgTSPNgmnindgvgsthPE----VLA---ELVKEKGADIGLAFDGDGDRLiAVDEKG 253
Cdd:PTZ00150 250 TVGLPNLLSVAQQAepdpEFPTV-TFPN------------PEegkgALKlsmETAEAHGSTVVLANDPDADRL-AVAEKL 315
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446443619 254 N----IVDGDQIMFICA-----KYMKETGQLKHNTVVSTVMSNLGFYKALEANGITSDKTAVG 307
Cdd:PTZ00150 316 NngwkIFTGNELGALLAwwamkRYRRQGIDKSKCFFICTVVSSRMLKKMAEKEGFQYDETLTG 378
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
75-245 |
7.49e-08 |
|
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: 54.54 E-value: 7.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 75 GVISTPGVAYLTKALDAQAGVMISASHNP---VQDNGIKFFGSDGF----KLTD---EQEAEIEALL---DKEVDelprp 141
Cdd:cd03085 87 GLLSTPAVSAVIRKRKATGGIILTASHNPggpEGDFGIKYNTSNGGpapeSVTDkiyEITKKITEYKiadDPDVD----- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 142 tgtnLGQVSDY-FEGG----------QKYLQYIKQTVeeDF---------SGLHIALDCAHGATSSLAPYLFAD-LEADI 200
Cdd:cd03085 162 ----LSKIGVTkFGGKpftvevidsvEDYVELMKEIF--DFdaikkllsrKGFKVRFDAMHGVTGPYAKKIFVEeLGAPE 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446443619 201 STMgtsPNGMNINDgVGSTHP-------EVLAELVKEKGADIGLAFDGDGDR 245
Cdd:cd03085 236 SSV---VNCTPLPD-FGGGHPdpnltyaKDLVELMKSGEPDFGAASDGDGDR 283
|
|
| PLN02307 |
PLN02307 |
phosphoglucomutase |
75-245 |
2.87e-05 |
|
phosphoglucomutase
Pssm-ID: 177942 [Multi-domain] Cd Length: 579 Bit Score: 46.57 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 75 GVISTPGVAYLTKALD---AQAGVMISASHN---PVQDNGIKFFGSDGF----KLTD---EQEAEIEALldKEVDELPR- 140
Cdd:PLN02307 99 GLLSTPAVSAVIRERDgskANGGFILTASHNpggPEEDFGIKYNYESGQpapeSITDkiyGNTLTIKEY--KMAEDIPDv 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443619 141 ----PTGTNLGQVSDY----FEGGQKYLQYIKQTVeeDFSGLHIAL---------DCAHGATSSLAPYLFAD-LEADIST 202
Cdd:PLN02307 177 dlsaVGVTKFGGPEDFdvevIDPVEDYVKLMKSIF--DFELIKKLLsrpdftfcfDAMHGVTGAYAKRIFVEeLGAPESS 254
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446443619 203 MgtsPNGMNINDgVGSTHPE----VLAELVK----------EKGADIGLAFDGDGDR 245
Cdd:PLN02307 255 L---LNCVPKED-FGGGHPDpnltYAKELVKrmglgktsygDEPPEFGAASDGDGDR 307
|
|
| |
