|
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: 730.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 4 YFGTDGVRGVANEELTPELAFKIGRFGGYVLTKDTDRPKVIIGRDTRVSGHMLEGALVAGLLSTGAEVMRLGVISTPGVA 83
Cdd:cd05802 1 LFGTDGIRGVANEPLTPELALKLGRAAGKVLGKGGGRPKVLIGKDTRISGYMLESALAAGLTSAGVDVLLLGVIPTPAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 84 YLTKALGAQAGVMISASHNPVQDNGIKFFGSDGFKLTDEQEAEIEALLDKEVDELPrpTGTNLGQVSDYFEGGQKYLQYI 163
Cdd:cd05802 81 YLTRKLRADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVEEEIEALIDKELELPP--TGEKIGRVYRIDDARGRYIEFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 164 KQTVE-EDFSGLHIALDCAHGATSSLAPYLFADLEADISTMGTSPNGMNINAGVGSTHPEGLAELVKEKGADIGLAFDGD 242
Cdd:cd05802 159 KSTFPkDLLSGLKIVLDCANGAAYKVAPEVFRELGAEVIVINNAPDGLNINVNCGSTHPESLQKAVLENGADLGIAFDGD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 243 GDRLIAVDEKGNIVDGDQIMFICAKYMKETGQLKHNTVVSTVMSNLGFYKALEANNITSDKTAVGDRYVMEEMKRGGYNL 322
Cdd:cd05802 239 ADRVIAVDEKGNIVDGDQILAICARDLKERGRLKGNTVVGTVMSNLGLEKALKELGIKLVRTKVGDRYVLEEMLKHGANL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 323 GGEQSGHIILLDYITTGDGMLSALQLVNIMKMTKKPLSELAGEMTKFPQLLVNVRVTDKKLALENEKIKEIIRVVEEEMN 402
Cdd:cd05802 319 GGEQSGHIIFLDHSTTGDGLLTALQLLAIMKRSGKSLSELASDMKLYPQVLVNVRVKDKKALLENPRVQAAIAEAEKELG 398
|
410 420 430
....*....|....*....|....*....|....*.
gi 446443617 403 GDGRILVRPSGTEPLIRVMAEAPTQEVCNAYVHRIV 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: 623.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 5 FGTDGVRGVANEE-LTPELAFKIGRFGGYVLTKDTD-RPKVIIGRDTRVSGHMLEGALVAGLLSTGAEVMRLGVISTPGV 82
Cdd:TIGR01455 1 FGTDGVRGRAGQEpLTAELALLLGAAAGRVLRQGRDtAPRVVIGKDTRLSGYMLENALAAGLNSAGVDVLLLGPLPTPAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 83 AYLTKALGAQAGVMISASHNPVQDNGIKFFGSDGFKLTDEQEAEIEALLDKEvDELPRPTGTNLGQVSDYFEGGQKYLQY 162
Cdd:TIGR01455 81 AYLTRTLRADAGVMISASHNPYEDNGIKFFGPGGFKLDDATEAAIEALLDEA-DPLPRPESEGLGRVKRYPDAVGRYIEF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 163 IKQTV--EEDFSGLHIALDCAHGATSSLAPYLFADLEADISTMGTSPNGMNINAGVGSTHPEGLAELVKEKGADIGLAFD 240
Cdd:TIGR01455 160 LKSTLprGLTLSGLKVVLDCANGAAYKVAPHVFRELGAEVIAIGVEPDGLNINDGCGSTHLDALQKAVREHGADLGIAFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 241 GDGDRLIAVDEKGNIVDGDQIMFICAKYMKETGQLKHNTVVSTVMSNLGFYKALEANNITSDKTAVGDRYVMEEMKRGGY 320
Cdd:TIGR01455 240 GDADRVLAVDANGRIVDGDQILYIIARALKESGELAGNTVVATVMSNLGLERALEKLGLTLIRTAVGDRYVLEEMRESGY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 321 NLGGEQSGHIILLDYITTGDGMLSALQLVNIMKMTKKPLSELAGEMTKFPQLLVNVRVTDKKLAL-ENEKIKEIIRVVEE 399
Cdd:TIGR01455 320 NLGGEQSGHIILLDYSTTGDGIVSALQVLTIMKKSGSTLSELAAEFVPYPQTLVNVRVADRKLAAaEAPAVKAAIEDAEA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 446443617 400 EMNGDGRILVRPSGTEPLIRVMAEAPTQEVCNAYVHRIVEVVKA 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: 557.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 2 GKYFGTDGVRGVANEELTPELAFKIGRFGGYVLtKDTDRPKVIIGRDTRVSGHMLEGALVAGLLSTGAEVMRLGVISTPG 81
Cdd:COG1109 4 KKLFGTDGIRGIVGEELTPEFVLKLGRAFGTYL-KEKGGPKVVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVPTPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 82 VAYLTKALGAQAGVMISASHNPVQDNGIKFFGSDGFKLTDEQEAEIEALLDKEvdELPRPTGTNLGQVSDYFEGGQKYLQ 161
Cdd:COG1109 83 LAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKE--DFRRAEAEEIGKVTRIEDVLEAYIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 162 YIKQTVEED--FSGLHIALDCAHGATSSLAPYLFADLEADISTMGTSPNGMNINAGVG--STHPEGLAELVKEKGADIGL 237
Cdd:COG1109 161 ALKSLVDEAlrLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFPNHNPNpePENLEDLIEAVKETGADLGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 238 AFDGDGDRLIAVDEKGNIVDGDQIMFICAKYMKETGqlKHNTVVSTVMSNLGFYKALEANNITSDKTAVGDRYVMEEMKR 317
Cdd:COG1109 241 AFDGDADRLGVVDEKGRFLDGDQLLALLARYLLEKG--PGGTVVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKMRE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 318 GGYNLGGEQSGHIILLDYITTGDGMLSALQLVNIMKMTKKPLSELAGEMTKFPQLLVNVRVTDK-KLALENEKIKEI--- 393
Cdd:COG1109 319 TGAVLGGEESGGIIFPDFVPTDDGILAALLLLELLAKQGKSLSELLAELPRYPQPEINVRVPDEeKIGAVMEKLREAved 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 446443617 394 ------IRVVEEEMNGDGRILVRPSGTEPLIRVMAEAPTQEVCNAYVHRIVEVVKAEV 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: 551.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 3 KYFGTDGVRGVANEE-LTPELAFKIGRFGGYVLTKdTDRPKVIIGRDTRVSGHMLEGALVAGLLSTGAEVMRLGVISTPG 81
Cdd:PRK10887 2 KYFGTDGIRGKVGQApITPDFVLKLGWAAGKVLAR-QGRPKVLIGKDTRISGYMLESALEAGLAAAGVDVLLTGPMPTPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 82 VAYLTKALGAQAGVMISASHNPVQDNGIKFFGSDGFKLTDEQEAEIEALLDKevdELPRPTGTNLGQVSDYFEGGQKYLQ 161
Cdd:PRK10887 81 VAYLTRTLRAEAGIVISASHNPYYDNGIKFFSADGTKLPDEVELAIEAELDK---PLTCVESAELGKASRINDAAGRYIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 162 YIKQTV--EEDFSGLHIALDCAHGATSSLAPYLFADLEADISTMGTSPNGMNINAGVGSTHPEGLAELVKEKGADIGLAF 239
Cdd:PRK10887 158 FCKSTFpnELSLRGLKIVVDCANGATYHIAPNVFRELGAEVIAIGCEPNGLNINDECGATDPEALQAAVLAEKADLGIAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 240 DGDGDRLIAVDEKGNIVDGDQIMFICAKYMKETGQLkHNTVVSTVMSNLGFYKALEANNITSDKTAVGDRYVMEEMKRGG 319
Cdd:PRK10887 238 DGDGDRVIMVDHLGNLVDGDQLLYIIARDRLRRGQL-RGGVVGTLMSNMGLELALKQLGIPFVRAKVGDRYVLEKLQEKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 320 YNLGGEQSGHIILLDYITTGDGMLSALQLVNIMKMTKKPLSELAGEMTKFPQLLVNVRVT-DKKLALENEKIKEIIRVVE 398
Cdd:PRK10887 317 WRLGGENSGHILCLDKTTTGDGIVAALQVLAAMVRSGMSLADLCSGMKLFPQVLINVRFKpGADDPLESEAVKAALAEVE 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 446443617 399 EEMNGDGRILVRPSGTEPLIRVMAEAPTQEVCNAYVHRIVEVVKA 443
Cdd:PRK10887 397 AELGGRGRVLLRKSGTEPLIRVMVEGEDEAQVTALAERIADAVKA 441
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
2-441 |
1.59e-130 |
|
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: 384.17 E-value: 1.59e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 2 GKYFGTDGVRGVANEELTPELAFKIGR-FGGYVltkdtDRPKVIIGRDTRVSGHMLEGALVAGLLSTGAEVMRLGVISTP 80
Cdd:TIGR03990 1 MLLFGTSGIRGIVGEELTPELALKVGKaFGTYL-----RGGKVVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLGIAPTP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 81 GVAYLTKALGAQAGVMISASHNPVQDNGIKFFGSDGFKLTDEQEAEIEALLDKEvdELPRPTGTNLGQVSDYFEGGQKYL 160
Cdd:TIGR03990 76 TLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQEEEIEEIAESG--DFERADWDEIGTVTSDEDAIDDYI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 161 QYIKQTVEEDF---SGLHIALDCAHGATSSLAPYLFADLEADISTMGTSPNGMNINagvgsTHPE-------GLAELVKE 230
Cdd:TIGR03990 154 EAILDKVDVEAirkKGFKVVVDCGNGAGSLTTPYLLRELGCKVITLNCQPDGTFPG-----RNPEptpenlkDLSALVKA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 231 KGADIGLAFDGDGDRLIAVDEKGNIVDGDQIMFICAKYMketgqLKHN--TVVSTVMSNLGFYKALEANNITSDKTAVGD 308
Cdd:TIGR03990 229 TGADLGIAHDGDADRLVFIDEKGRFIGGDYTLALFAKYL-----LEHGggKVVTNVSSSRAVEDVAERHGGEVIRTKVGE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 309 RYVMEEMKRGGYNLGGEQSGHIILLDYITTGDGMLSALQLVNIMKMTKKPLSELAGEMTKFPqllvNVRvtdKKLALENE 388
Cdd:TIGR03990 304 VNVAEKMKEEGAVFGGEGNGGWIFPDHHYCRDGLMAAALFLELLAEEGKPLSELLAELPKYP----MSK---EKVELPDE 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446443617 389 KIKEIIRVVEEEMNG--------------DGRILVRPSGTEPLIRVMAEAPTQEVCNAYVHRIVEVV 441
Cdd:TIGR03990 377 DKEEVMEAVEEEFADaeidtidgvridfeDGWVLVRPSGTEPIVRIYAEAKTEERAEELLEEGRSLV 443
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
4-441 |
1.99e-121 |
|
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: 360.73 E-value: 1.99e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 4 YFGTDGVRGVANEELTPELAFKIGR-FGGYVltkdtDRPKVIIGRDTRVSGHMLEGALVAGLLSTGAEVMRLGVISTPGV 82
Cdd:cd03087 1 LFGTSGIRGVVGEELTPELALKVGKaLGTYL-----GGGTVVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDIGIVPTPAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 83 AYLTKALGAqAGVMISASHNPVQDNGIKFFGSDGFKLTDEQEAEIEALLDKEVdeLPRPTGTNLGQVSDYFEGGQKYLQY 162
Cdd:cd03087 76 QYAVRKLGD-AGVMITASHNPPEYNGIKLVNPDGTEFSREQEEEIEEIIFSER--FRRVAWDEVGSVRREDSAIDEYIEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 163 IKQTVEEDFS-GLHIALDCAHGATSSLAPYLFADLEADISTMGTSPNGMNInagvgSTHPE-------GLAELVKEKGAD 234
Cdd:cd03087 153 ILDKVDIDGGkGLKVVVDCGNGAGSLTTPYLLRELGCKVITLNANPDGFFP-----GRPPEptpenlsELMELVRATGAD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 235 IGLAFDGDGDRLIAVDEKGNIVDGDQIMFICAKYMKETGQLKhntVVSTVMSNLGFYKALEANNITSDKTAVGDRYVMEE 314
Cdd:cd03087 228 LGIAHDGDADRAVFVDEKGRFIDGDKLLALLAKYLLEEGGGK---VVTPVDASMLVEDVVEEAGGEVIRTPVGDVHVAEE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 315 MKRGGYNLGGEQSGHIILLDYITTGDGMLSALQLVNIMKmTKKPLSELAGEMTKFPQLLVNVRVTDKKLALENEKIKEII 394
Cdd:cd03087 305 MIENGAVFGGEPNGGWIFPDHQLCRDGIMTAALLLELLA-EEKPLSELLDELPKYPLLREKVECPDEKKEEVMEAVEEEL 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 446443617 395 RVVEEEMN---------GDGRILVRPSGTEPLIRVMAEAPTQEVCNAYVHRIVEVV 441
Cdd:cd03087 384 SDADEDVDtidgvrieyEDGWVLIRPSGTEPKIRITAEAKTEERAKELLEEGRSKV 439
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
10-441 |
5.25e-92 |
|
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: 285.56 E-value: 5.25e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 10 VRGVANEELTPELAFKIGR-FGGYVltKDTDRPKVIIGRDTRVSGHMLEGALVAGLLSTGAEVMRLGVISTPGVAYLTKA 88
Cdd:cd03089 7 IRGIAGEELTEEIAYAIGRaFGSWL--LEKGAKKVVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPVLYFATFH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 89 LGAQAGVMISASHNPVQDNGIKFFGSDGfKLTDEQEAEIEALLDKEVDELPRPTGTnlGQVSDYFEggqKYLQYIKQTVE 168
Cdd:cd03089 85 LDADGGVMITASHNPPEYNGFKIVIGGG-PLSGEDIQALRERAEKGDFAAATGRGS--VEKVDILP---DYIDRLLSDIK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 169 EDFSGLHIALDCAHGATSSLAPYLFADLEADISTM-----GTSPNGmninagvgstHP--------EGLAELVKEKGADI 235
Cdd:cd03089 159 LGKRPLKVVVDAGNGAAGPIAPQLLEALGCEVIPLfcepdGTFPNH----------HPdptdpenlEDLIAAVKENGADL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 236 GLAFDGDGDRLIAVDEKGNIVDGDQIMFICAKYMketgqLKHN---TVVSTVMSNLGFYKALEANNITSDKTAVGDRYVM 312
Cdd:cd03089 229 GIAFDGDGDRLGVVDEKGEIIWGDRLLALFARDI-----LKRNpgaTIVYDVKCSRNLYDFIEEAGGKPIMWKTGHSFIK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 313 EEMKRGGYNLGGEQSGHIIL------LDyittgDGMLSALQLVNIMKMTKKPLSELAGEMTKFPQLL-VNVRVTDKKLAL 385
Cdd:cd03089 304 AKMKETGALLAGEMSGHIFFkdrwygFD-----DGIYAALRLLELLSKSGKTLSELLADLPKYFSTPeIRIPVTEEDKFA 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446443617 386 ENEKIKEIIRVVEEEMN---------GDGRILVRPSGTEPLIRVMAEAPTQEVCNAYVHRIVEVV 441
Cdd:cd03089 379 VIERLKEHFEFPGAEIIdidgvrvdfEDGWGLVRASNTEPVLVLRFEADTEEGLEEIKAELRKLL 443
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
4-428 |
7.70e-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: 7.70e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 4 YFGTDGVRGVANEELTPELAFKIGRfggyvltkdtdrpkviigrdtrvsghmlegalvagllstgaevmrlgvistpgva 83
Cdd:cd03084 1 IFGTSGVRGVVGDDITPETAVALGQ------------------------------------------------------- 25
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 84 yltkALGAQAGVMISASHNPVQDNGIKFFGSDGFKLTDEQEAEIEALLDKEvdELPRPTGTNLGQVS-------DYFEGG 156
Cdd:cd03084 26 ----AIGSTGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKE--DEPSAVAYELGGSVkavdilqRYFEAL 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 157 QKYLQyiKQTVEEdfSGLHIALDCAHGATSSLAPYLFADLEADISTMGTSPNGMNINAgvgstHPE--------GLAELV 228
Cdd:cd03084 100 KKLFD--VAALSN--KKFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCEPDGNFGNI-----NPDpgsetnlkQLLAVV 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 229 KEKGADIGLAFDGDGDRLIAVDEKGNIVDGDQIMFICAKYMKETGQlKHNTVVSTVMSNLGFYKALEANNITSDKTAVGD 308
Cdd:cd03084 171 KAEKADFGVAFDGDADRLIVVDENGGFLDGDELLALLAVELFLTFN-PRGGVVKTVVSSGALDKVAKKLGIKVIRTKTGF 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 309 RYVMEEMKRGGYNLGGEQSGHIILLDYITTGDGMLSALQLVNIMKMTKKPLSELAGEMTKFPQLLVNVRvtdkklalene 388
Cdd:cd03084 250 KWVGEAMQEGDVVLGGEESGGVIFPEFHPGRDGISAALLLLEILANLGKSLSELFSELPRYYYIRLKVR----------- 318
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 446443617 389 kikeiirvveeemngdGRILVRPSGTEPLIRVMAEAPTQE 428
Cdd:cd03084 319 ----------------GWVLVRASGTEPAIRIYAEADTQE 342
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
5-428 |
1.23e-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: 240.92 E-value: 1.23e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 5 FGTDGVRGVANEELTPE----LAFKIGRfggYVLTKDTDRPKVIIGRDTR-VSGHMleGALVAGLL-STGAEVmRL--GV 76
Cdd:cd05800 3 FGTDGWRGIIAEDFTFEnvrrVAQAIAD---YLKEEGGGGRGVVVGYDTRfLSEEF--ARAVAEVLaANGIDV-YLsdRP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 77 ISTPGVAYLTKALGAQAGVMISASHNPVQDNGIKFFGSDGFKLTDEQEAEIEALLDKEVDELPRPTGTNLGQVSDYFEGg 156
Cdd:cd05800 77 VPTPAVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARLASGEPPGLEARAEGLIETIDPKPD- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 157 qkYLQYIKQTVEEDF---SGLHIALDCAHGATSSLAPYLFADLEADISTMGTSPngmniNAGVGSTHPE-------GLAE 226
Cdd:cd05800 156 --YLEALRSLVDLEAireAGLKVVVDPMYGAGAGYLEELLRGAGVDVEEIRAER-----DPLFGGIPPEpieknlgELAE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 227 LVKEKGADIGLAFDGDGDRLIAVDEKGNIVDGDQIMFICAKYMKETGQLKhNTVVSTV-MSNLgFYKALEANNITSDKTA 305
Cdd:cd05800 229 AVKEGGADLGLATDGDADRIGAVDEKGNFLDPNQILALLLDYLLENKGLR-GPVVKTVsTTHL-IDRIAEKHGLPVYETP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 306 VGDRYVMEEMKRGGYNLGGEQSGHIILLDYITTGDGMLSALQLVNIMKMTKKPLSELAGEMTK----FPQLLVNVRVTDK 381
Cdd:cd05800 307 VGFKYIAEKMLEEDVLIGGEESGGLGIRGHIPERDGILAGLLLLEAVAKTGKPLSELVAELEEeygpSYYDRIDLRLTPA 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446443617 382 KLA-----LENEKIKEII--RVVEE-EMNG-------DGRILVRPSGTEPLIRVMAEAPTQE 428
Cdd:cd05800 387 QKEailekLKNEPPLSIAggKVDEVnTIDGvklvledGSWLLIRPSGTEPLLRIYAEAPSPE 448
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
9-428 |
5.30e-74 |
|
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: 238.75 E-value: 5.30e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 9 GVRGVANEELTPELAFK-IGRFGGYVLTKdTDRPKVIIGRDTRVSGHMLEGALVAGLLSTGAEVMRLGVISTPGVAYLTK 87
Cdd:cd05803 6 GIRGIVGEGLTPEVITRyVAAFATWQPER-TKGGKIVVGRDGRPSGPMLEKIVIGALLACGCDVIDLGIAPTPTVQVLVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 88 ALGAQAGVMISASHNPVQDNGIKFFGSDGFKLTDEQEAEIEALLDKevDELPRPTGTNLGQVSDYFEGGQKYLQYIKQTV 167
Cdd:cd05803 85 QSQASGGIIITASHNPPQWNGLKFIGPDGEFLTPDEGEEVLSCAEA--GSAQKAGYDQLGEVTFSEDAIAEHIDKVLALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 168 EEDFSGLH-----IALDCAHGATSSLAPYLFADLEADISTMGTSPNGmninagvGSTH-PE-------GLAELVKEKGAD 234
Cdd:cd05803 163 DVDVIKIRernfkVAVDSVNGAGGLLIPRLLEKLGCEVIVLNCEPTG-------LFPHtPEplpenltQLCAAVKESGAD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 235 IGLAFDGDGDRLIAVDEKGNIVDGDQIMFICAKYMKETGQLKHNTVVSTVMSNLGFYKAlEANNITSDKTAVGDRYVMEE 314
Cdd:cd05803 236 VGFAVDPDADRLALVDEDGRPIGEEYTLALAVDYVLKYGGRKGPVVVNLSTSRALEDIA-RKHGVPVFRSAVGEANVVEK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 315 MKRGGYNLGGEQSGHIILLDYITTGDGMLSALQLVNIMKMTKKPLSELAGEMTKFPQLLVNVRVTDKKLA-LENEKIKEI 393
Cdd:cd05803 315 MKEVDAVIGGEGNGGVILPDVHYGRDSLVGIALVLQLLAASGKPLSEIVDELPQYYISKTKVTIAGEALErLLKKLEAYF 394
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 446443617 394 IRVVEEEMNG------DGRILVRPSGTEPLIRVMAEAPTQE 428
Cdd:cd05803 395 KDAEASTLDGlrldseDSWVHVRPSNTEPIVRIIAEAPTQD 435
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
2-134 |
4.63e-52 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 171.64 E-value: 4.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 2 GKYFGTDGVRGVAN-EELTPELAFKIGRFGGYVLTKDTDRPKVIIGRDTRVSGHMLEGALVAGLLSTGAEVMRLGVISTP 80
Cdd:pfam02878 1 RQLFGTSGIRGKVGvGELTPEFALKLGQAIASYLRAQGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 446443617 81 GVAYLTKALGAQAGVMISASHNPVQDNGIKFFGSDGFKLTDEQEAEIEALLDKE 134
Cdd:pfam02878 81 AVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKE 134
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
10-443 |
3.53e-51 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 179.02 E-value: 3.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 10 VRGVANEELTPELAFKIGrfGGYV-LTKDTDRPKVIIGRDTRVSGHMLEGALVAGLLSTGAEVMRLGVISTPGVAYLTKA 88
Cdd:PRK09542 6 VRGVVGEQIDEDLVRDVG--AAFArLMRAEGATTVVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIGLASTDQLYFASGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 89 LGAqAGVMISASHNPVQDNGIKF-------FGSD-GFkltdeqeAEIEALLDKEVDELPRPTGTNLGQvsDYFEGgqkYL 160
Cdd:PRK09542 84 LDC-PGAMFTASHNPAAYNGIKLcragakpVGQDtGL-------AAIRDDLIAGVPAYDGPPGTVTER--DVLAD---YA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 161 QYIKQTVeeDFSG---LHIALDCAHGATSSLAPYLFADLEADISTM-----GTSPNgmninagvgstH------PEGLAE 226
Cdd:PRK09542 151 AFLRSLV--DLSGirpLKVAVDAGNGMGGHTVPAVLGGLPITLLPLyfeldGTFPN-----------HeanpldPANLVD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 227 L---VKEKGADIGLAFDGDGDRLIAVDEKGNIVDGDQIMFICAKymKETGQLKHNTVVSTVMSNLGFYKALEANNITSDK 303
Cdd:PRK09542 218 LqafVRETGADIGLAFDGDADRCFVVDERGQPVSPSAVTALVAA--RELAREPGATIIHNLITSRAVPELVAERGGTPVR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 304 TAVGDRYVMEEMKRGGYNLGGEQSGHIILLDYITTGDGMLSALQLVNIMKMTKKPLSELAGEMTKFPQL-LVNVRVTDKK 382
Cdd:PRK09542 296 TRVGHSFIKALMAETGAIFGGEHSAHYYFRDFWGADSGMLAALHVLAALGEQDRPLSELMADYQRYAASgEINSTVADAP 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446443617 383 LALenEKIKEII--RVVE-EEMNG------DGRIL-VRPSGTEPLIRVMAEAPTQEVCNAYVHRIVEVVKA 443
Cdd:PRK09542 376 ARM--EAVLKAFadRIVSvDHLDGvtvdlgDGSWFnLRASNTEPLLRLNVEARTEEEVDALVDEVLAIIRA 444
|
|
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
5-441 |
1.16e-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: 177.44 E-value: 1.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 5 FGTDGVRGVANEELTPELAFKIGRFGGYVLTKDTdrpKVIIGRDTRVSGHMLEGALVAGLLSTGAEVMRLGVISTPGVAY 84
Cdd:cd05805 2 FGGRGVSGLINVDITPEFATRLGAAYGSTLPPGS---TVTVSRDASRASRMLKRALISGLLSTGVNVRDLGALPLPVARY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 85 LTKALGAQAGVMISAShnpVQDNG---IKFFGSDGFKLTDEQEAEIEALLDKE------VDELPRPtgTNLGQVSDYfeg 155
Cdd:cd05805 79 AIRFLGASGGIHVRTS---PDDPDkveIEFFDSRGLNISRAMERKIENAFFREdfrrahVDEIGDI--TEPPDFVEY--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 156 gqkYLQYIKQTVEED---FSGLHIALDCAHGATSSLAPYLFADLEADISTmgtspNGMNINAGVGSTHP------EGLAE 226
Cdd:cd05805 151 ---YIRGLLRALDTSglkKSGLKVVIDYAYGVAGIVLPGLLSRLGCDVVI-----LNARLDEDAPRTDTerqrslDRLGR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 227 LVKEKGADIGLAFDGDGDRLIAVDEKGNIVDGDQIMFICAKYMKETGQLKhnTVV-----STVMSNLgfykaLEANNITS 301
Cdd:cd05805 223 IVKALGADFGVIIDPNGERLILVDEAGRVISDDLLTALVSLLVLKSEPGG--TVVvpvtaPSVIEQL-----AERYGGRV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 302 DKTAVGDRYVMEEMKRGGYNLGGEQSGHIILLDYITTgDGMLSALQLVNIMKMTKKPLSELAGEMTKFPQLLVNVRV--T 379
Cdd:cd05805 296 IRTKTSPQALMEAALENVVLAGDGDGGFIFPEFHPGF-DAIAALVKILEMLARTNISLSQIVDELPRFYVLHKEVPCpwE 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446443617 380 DK-----KLALENEKiKEI-----IRVVEEemngDGRILVRPSGTEPLIRVMAEAPTQEVCNAYVHRIVEVV 441
Cdd:cd05805 375 AKgrvmrRLIEEAPD-KSIelidgVKIYED----DGWVLVLPDADEPLCHIYAEGSDQERAEELTEFYVEKV 441
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
257-368 |
1.84e-46 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 156.07 E-value: 1.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 257 DGDQIMFICAKYMKETGQLKHNT-VVSTVMSNLGFYKALEANNITSDKTAVGDRYVMEEMKRGGYNLGGEQSGHIILLDY 335
Cdd:pfam02880 1 DGDQILALLAKYLLEQGKLPPGAgVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLDH 80
|
90 100 110
....*....|....*....|....*....|...
gi 446443617 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 |
1.76e-34 |
|
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: 134.17 E-value: 1.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 5 FGTDGVRGV----ANE--ELTpelafkIGR----FGGYVLTKDTDR--PKVIIGRDTRvsgHM-----LEGALVagLLST 67
Cdd:cd05799 4 FGTAGLRGKmgagTNRmnDYT------VRQatqgLANYLKKKGPDAknRGVVIGYDSR---HNsrefaELTAAV--LAAN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 68 GAEVMRL-GVISTPGVAYLTKALGAQAGVMISASHNPVQDNGIKFFGSDGFKLTDEQEAEIEALLDK--------EVDEL 138
Cdd:cd05799 73 GIKVYLFdDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAvlepldikFEEAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 139 PRPTGTNLGQ--VSDYFEGGQKYLQYIKQTVEEDFSGLHIALdcaHGATSSLAPYLFADL------------EADistmG 204
Cdd:cd05799 153 DSGLIKYIGEeiDDAYLEAVKKLLVNPELNEGKDLKIVYTPL---HGVGGKFVPRALKEAgftnvivveeqaEPD----P 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 205 TSPNgmninagVGSTHPEG-----LA-ELVKEKGADIGLAFDGDGDRL-IAV---DEKGNIVDGDQIMFICAKY----MK 270
Cdd:cd05799 226 DFPT-------VKFPNPEEpgaldLAiELAKKVGADLILATDPDADRLgVAVkdkDGEWRLLTGNEIGALLADYlleqRK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 271 ETGQLKHNTVV--STVMSNLGfyKAL-EANNITSDKTAVGDRY---VMEEMKRGGYNL--GGEQS-GHIIlLDYITTGDG 341
Cdd:cd05799 299 EKGKLPKNPVIvkTIVSSELL--RKIaKKYGVKVEETLTGFKWignKIEELESGGKKFlfGFEESiGYLV-GPFVRDKDG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 342 MLSALQLVNIMKMTKKP-------LSELAGE----MTKfpqlLVNVRVTDKKlalENEKIKEIIR-------VVEEEMNG 403
Cdd:cd05799 376 ISAAALLAEMAAYLKAQgktlldrLDELYEKygyyKEK----TISITFEGKE---GPEKIKAIMDrlrnnpnVLTFYLED 448
|
490 500
....*....|....*....|.
gi 446443617 404 DGRILVRPSGTEPLIRVMAEA 424
Cdd:cd05799 449 GSRVTVRPSGTEPKIKFYIEV 469
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
5-438 |
2.17e-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: 2.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 5 FGTDGVRGVAnEELTPELAFKIGR-FGGYVLTKdTDRPKVIIGRDTRVSGHMLEGALVAGLLSTGAEVMRLGVISTPGVA 83
Cdd:cd03088 2 FGTSGLRGLV-TDLTDEVCYAYTRaFLQHLESK-FPGDTVAVGRDLRPSSPRIAAACAAALRDAGFRVVDCGAVPTPALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 84 YltKALGAQAG-VMISASHNPVQDNGIKFFGSDGfKLTDEQEAEIEALLDKEVDELPRPTGTNLGQVSDyfeGGQKYLQ- 161
Cdd:cd03088 80 L--YAMKRGAPaIMVTGSHIPADRNGLKFYRPDG-EITKADEAAILAALVELPEALFDPAGALLPPDTD---AADAYIAr 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 162 YIKQTVEEDFSGLHIALDcAHgatSSLA----PYLFADLEADISTMGTSPNGMNINA-GVGSTHPEGLAELVKEKGADIG 236
Cdd:cd03088 154 YTDFFGAGALKGLRIGVY-QH---SSVGrdllVRILEALGAEVVPLGRSDTFIPVDTeAVRPEDRALAAAWAAEHGLDAI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 237 LAFDGDGDR-LIAvDEKGNIVDGDQIMFICAKYmketgqLKHNTVVSTVMSNlgfyKALEANNITS--DKTAVGDRYVME 313
Cdd:cd03088 230 VSTDGDGDRpLVA-DETGEWLRGDILGLLTARF------LGADTVVTPVSSN----SAIELSGFFKrvVRTRIGSPYVIA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 314 EMKR---------------GGYNLGGEQSGHIILLDYITTGDGMLSALQLVNIMKMTKKPLSELAGEMTK---------- 368
Cdd:cd03088 299 AMAEaaaagagrvvgyeanGGFLLGSDIERNGRTLKALPTRDAVLPILAVLAAAKEAGIPLSELVASLPArftasdrlqn 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 369 FPQ-----LLVNVRVTDKKLA-LENEKIKEIIRVveEEMNG------DGRIL-VRPSGTEPLIRVMAEAPTQEVCNAYVH 435
Cdd:cd03088 379 FPTeksqaLIARLSADPEARAaFFFALGGEVASI--DTTDGlrmtfaNGDIVhLRPSGNAPELRCYVEADSEERARELLA 456
|
...
gi 446443617 436 RIV 438
Cdd:cd03088 457 RGL 459
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
6-259 |
1.42e-30 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 124.01 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 6 GTDgVRGVANE-------ELTPELAFKIGR-FGGYVLTK----DTDRPKVIIGRDTRVSGHMLEGALVAGLLSTGAEVMR 73
Cdd:PLN02371 70 GSD-IRGVAVEgvegepvTLTPPAVEAIGAaFAEWLLEKkkadGSGELRVSVGRDPRISGPRLADAVFAGLASAGLDVVD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 74 LGVISTPGVAY--LTKALGAQAGVMISASHNPVQDNGIKFFGSDGfKLTdeqEAEIEALLDKEVDELPRPTGTNLGQVS- 150
Cdd:PLN02371 149 MGLATTPAMFMstLTEREDYDAPIMITASHLPYNRNGLKFFTKDG-GLG---KPDIKDILERAARIYKEWSDEGLLKSSs 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 151 ---------DYFEGGQKYL-QYIKQTV------EEDFSGLHIALDCAHGATSSLAPYLFADLEADIS-TMGTSPNGMNIN 213
Cdd:PLN02371 225 gassvvcrvDFMSTYAKHLrDAIKEGVghptnyETPLEGFKIVVDAGNGAGGFFAEKVLEPLGADTSgSLFLEPDGMFPN 304
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 446443617 214 AGVGSTHPEGLAEL---VKEKGADIGLAFDGDGDRLIAVDEKGNIVDGD 259
Cdd:PLN02371 305 HIPNPEDKAAMSATtqaVLANKADLGIIFDTDVDRSAVVDSSGREINRN 353
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
10-424 |
1.69e-30 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 122.75 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 10 VRGVANEELTPELAFKIGR-FGGYVltkdtdRPKVII-GRDTRVSGHMLEGALVAGLLSTGAEVMRLGVISTPGVAYLTK 87
Cdd:PRK15414 12 IRGKLGEELNEDIAWRIGRaYGEFL------KPKTIVlGGDVRLTSETLKLALAKGLQDAGVDVLDIGMSGTEEIYFATF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 88 ALGAQAGVMISASHNPVQDNGIKFF--------GSDGfkLTDEQEAEiEALLDKEVDELPRPTGTNLGQVSDYFEggqKY 159
Cdd:PRK15414 86 HLGVDGGIEVTASHNPMDYNGMKLVregarpisGDTG--LRDVQRLA-EANDFPPVDETKRGRYQQINLRDAYVD---HL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 160 LQYIKQtveEDFSGLHIALDCAHGATSSLAPYLFADLEA-----DISTMGTSPNGMNINAGVGSTHPEGLAEL---VKEK 231
Cdd:PRK15414 160 FGYINV---KNLTPLKLVINSGNGAAGPVVDAIEARFKAlgapvELIKVHNTPDGNFPNGIPNPLLPECRDDTrnaVIKH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 232 GADIGLAFDGDGDRLIAVDEKGNIVDGDQIMFICAKYMKETG---------QLKHNTVvstvmsnlgfyKALEANNITSD 302
Cdd:PRK15414 237 GADMGIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNpgakiihdpRLSWNTV-----------DVVTAAGGTPV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 303 KTAVGDRYVMEEMKRGGYNLGGEQSGHIILLDYITTGDGMLSALQLVNIMKMTKKPLSELAGE-MTKFPQL-LVNVRVTD 380
Cdd:PRK15414 306 MSKTGHAFIKERMRKEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELVCLKGKTLGELVRDrMAAFPASgEINSKLAQ 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 446443617 381 KKLALEN------EKIKEIIRVVEEEMN-GDGRILVRPSGTEPLIRVMAEA 424
Cdd:PRK15414 386 PVEAINRveqhfsREALAVDRTDGISMTfADWRFNLRSSNTEPVVRLNVES 436
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
38-441 |
1.07e-24 |
|
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: 106.52 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 38 TDRPKVIIGRDTRVSGHMLEGALVAGLLSTGAEVMRLGVISTPGVAYLTKAlgaqagvmisasHNpvqdngikffgsdgf 117
Cdd:cd03086 100 SVPANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYLVRA------------AN--------------- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 118 kltdeqeaeiealldkevdelprpTGTNLGQVSD--YFEGGQK-YLQYIKQTVEEDFSGLHIALDCAHG----ATSSLAP 190
Cdd:cd03086 153 ------------------------TEGAYGEPTEegYYEKLSKaFNELYNLLQDGGDEPEKLVVDCANGvgalKLKELLK 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 191 YLFADLEADISTMGTSPNGMnINAGVGsthpeglAELVK-EKGADIGL----------AFDGDGDRLIA--VDEKGN--I 255
Cdd:cd03086 209 RLKKGLSVKIINDGEEGPEL-LNDGCG-------ADYVKtKQKPPRGFelkppgvrccSFDGDADRLVYfyPDSSNKfhL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 256 VDGDQIMFICAKYMKE-----------------------------TGQLKHNTV-VSTVMSNL---------GFYkaLEA 296
Cdd:cd03086 281 LDGDKIATLFAKFIKEllkkageelkltigvvqtayangastkylEDVLKVPVVcTPTGVKHLhhaaeefdiGVY--FEA 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 297 NN----ITSDKTAVGDRYVMEemkrggynLGGEQSGHIILLDYI------TTGD---GMLSALQLVNIMKMTkkpLSELA 363
Cdd:cd03086 359 NGhgtvLFSESALAKIEENSS--------LSDEQEKAAKTLLAFsrlinqTVGDaisDMLAVELILAALGWS---PQDWD 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 364 GEMTKFPQLLVNVRVTDKKL---------ALE----NEKIKEIIRVVEeemngDGRILVRPSGTEPLIRVMAEAPTQEVC 430
Cdd:cd03086 428 NLYTDLPNRQLKVKVPDRSVikttdaerrLVEpkglQDKIDAIVAKYN-----NGRAFVRPSGTEDVVRVYAEAATQEEA 502
|
490
....*....|.
gi 446443617 431 NAYVHRIVEVV 441
Cdd:cd03086 503 DELANEVAELV 513
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
373-442 |
5.80e-19 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 80.78 E-value: 5.80e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446443617 373 LVNVRVTDKKLALENEKIKEIIRVVEEEMNGDGRIL-VRPSGTEPLIRVMAEAPTQEVCNAYVHRIVEVVK 442
Cdd:pfam00408 1 LINVRVAEKKKLAALAAILKVFADAEKILGEDGRRLdVRPSGTEPVLRVMVEGDSDEELARLADEIADLLE 71
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
42-446 |
1.66e-18 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 87.79 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 42 KVIIGRDTRVSGHMLEGALVAGL-LSTGAEVMRLGVISTPGVAYLTkalgaqagvmisASHNPvqdngikfFGSDGFKLT 120
Cdd:PTZ00302 154 KVHVGRDTRPSSPELVSALLRGLkLLIGSNVRNFGIVTTPQLHFLV------------AFANG--------LGVDVVESS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 121 DEQEAEiealldkevdelprptgtnlgQVSDYFEGGQKYLQYIKQTVEEDFSGLHIALDCAHGATS-SLAPYL--FADLE 197
Cdd:PTZ00302 214 DELYYA---------------------YLLAAFKELYRTLQEGGPVDLTQNNSKILVVDCANGVGGyKIKRFFeaLKQLG 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 198 ADISTM---GTSPNGMNINAG-----VGSTHPEGLaelvKEKGADIGL---AFDGDGDRLIA--VDEKGN----IVDGDQ 260
Cdd:PTZ00302 273 IEIIPIninCDEEELLNDKCGadyvqKTRKPPRAM----KEWPGDEETrvaSFDGDADRLVYffPDKDGDdkwvLLDGDR 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 261 IMFICAKYMKE---TGQLKHN---TVVSTVMSNLGFYKALEAN----NITSDKTAV------GDRY-------------- 310
Cdd:PTZ00302 349 IAILYAMLIKKllgKIQLKKKldiGVVQTAYANGASTNYLNELlgrlRVYCAPTGVknlhpkAHKYdigiyfeanghgtv 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 311 -----VMEEMKRGGYNLGGEQSGHIILLDYI-----TTGDGM--LSALQLV-NIMKMTkkpLSELAGEMTKFPQLLVNVR 377
Cdd:PTZ00302 429 lfnekALAEWAKFLAKQNALNSACRQLEKFLrlfnqTIGDAIsdLLAVELAlAFLGLS---FQDWLNLYTDLPSRQDKVT 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 378 VTDKKL---------ALE----NEKIKEIIRVVEEEmngdGRILVRPSGTEPLIRVMAEAPTQEVCNAYVHRIVEVVKAE 444
Cdd:PTZ00302 506 VKDRTLitntedetrLLEpkglQDKIDAIVSKYDNA----ARAFIRPSGTEPVVRVYAEAPTLEQADELANEVKGLVLRY 581
|
..
gi 446443617 445 VG 446
Cdd:PTZ00302 582 CS 583
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
159-253 |
2.13e-14 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 68.86 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 159 YLQYIKQTVEEDF---SGLHIALDCAHGATSSLAPYLFADLEADISTMGTSPNGmniNAGVGSTHPEG------LAELVK 229
Cdd:pfam02879 2 YIDHLLELVDSEAlkkRGLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDP---DFPTRAPNPEEpealalLIELVK 78
|
90 100
....*....|....*....|....
gi 446443617 230 EKGADIGLAFDGDGDRLIAVDEKG 253
Cdd:pfam02879 79 SVGADLGIATDGDADRLGVVDERG 102
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
43-285 |
6.43e-13 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 70.48 E-value: 6.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 43 VIIGRDTRVsgHMLEGALVAG--LLSTGAEVMRLG-VISTPGVAYLTKALGAQAGVMISASHNPVQDNGIKFFGSDGFKL 119
Cdd:PTZ00150 92 VVIGYDGRY--HSRRFAEITAsvFLSKGFKVYLFGqTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVYWSNGAQI 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 120 TDEQEAEIEALLDKEVDELPRP-TGTNLGQVSD-YFEGGQKYLQYIKQTV---EEDFSGLHIALDCAHG----------A 184
Cdd:PTZ00150 170 IPPHDKNISAKILSNLEPWSSSwEYLTETLVEDpLAEVSDAYFATLKSEYnpaCCDRSKVKIVYTAMHGvgtrfvqkalH 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 185 TSSLAPYLFADLEA----DISTMgTSPNgmninagvgsthPEGLA-------ELVKEKGADIGLAFDGDGDRLiAVDEKG 253
Cdd:PTZ00150 250 TVGLPNLLSVAQQAepdpEFPTV-TFPN------------PEEGKgalklsmETAEAHGSTVVLANDPDADRL-AVAEKL 315
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446443617 254 N----IVDGDQIMFICA-----KYMKETGQLKH----NTVVSTVM 285
Cdd:PTZ00150 316 NngwkIFTGNELGALLAwwamkRYRRQGIDKSKcffiCTVVSSRM 360
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
71-446 |
6.77e-13 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 70.44 E-value: 6.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 71 VMRLGVIStpgvAYLTKALGAQAGVMISASHNPVQDNGIKFFGSDGFKLT----------------DEQEAEIEALLDKE 134
Cdd:PLN02895 42 VFRVGILA----ALRSLKTGAATGLMITASHNPVSDNGVKIVDPSGGMLPqawepfadalanapdpDALVQLIREFVKKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 135 ----VDELP----------RPTG------------------TNLGQV--------------------SDYFEGGQKY--- 159
Cdd:PLN02895 118 nipaVGGNPpaevllgrdtRPSGpallaaalkgvraigaraVDMGILttpqlhwmvraankgmkateSDYFEQLSSSfra 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 160 -LQYIKQTVEEDFSGLHIALDCAHGA----TSSLAPyLFADLEADISTMGTSPNGMnINAGVGS-------THPEGLAEL 227
Cdd:PLN02895 198 lLDLIPNGSGDDRADDKLVVDGANGVgaekLETLKK-ALGGLDLEVRNSGKEGEGV-LNEGVGAdfvqkekVPPTGFASK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 228 vkekgaDIGL---AFDGDGDRLIAVDEKGN-----IVDGDQIMFICAKYMKE-------TGQLKHNT------VVSTVMS 286
Cdd:PLN02895 276 ------DVGLrcaSLDGDADRLVYFYVSSAgskidLLDGDKIASLFALFIKEqlrilngNGNEKPEEllvrlgVVQTAYA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 287 N----------LGFYKALeannitsdkTAVGDRYVMEEMKrgGYNLG--GEQSGH-IIL-----LDYITTGDGMLSAL-- 346
Cdd:PLN02895 350 NgastaylkqvLGLEVVC---------TPTGVKYLHEAAA--EFDIGvyFEANGHgTVLfserfLDWLEAAAAELSSKak 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 347 ---------------QLVN---------------IMKMTKKPLSELAGEMTKFPQLLVNVRVTDK---------KLALEN 387
Cdd:PLN02895 419 gseahkaarrllavsRLINqavgdalsglllveaILQYRGWSLAEWNALYQDLPSRQLKVKVADRtaitttdaeTVVVRP 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 446443617 388 EKIKEIIRVVEEEMNGdGRILVRPSGTEPLIRVMAEAPTQEVCNAYVHRIVEVVKAEVG 446
Cdd:PLN02895 499 AGLQDAIDAEVAKYPR-GRAFVRPSGTEDVVRVYAEASTQEAADSLAREVARLVYDLLG 556
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
68-423 |
6.89e-13 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 70.55 E-value: 6.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 68 GAEVM---RLGVISTPGV-----AYLTKALGAQAGVMISASHNPVQDNGIKFFGSDG----FKLTDEQEAEIEALLDKEV 135
Cdd:PRK07564 104 GVGVVivgRGGYTPTPAVshailKYNGRGGGLADGIVITPSHNPPEDGGIKYNPPNGgpadTDVTDAIEARANELLAYGL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 136 DELPRPTGTNLGQ---------VSDYFEGGQKYLqyikqtveeDF-----SGLHIALDCAHGATSSLAPYLFADLEADIS 201
Cdd:PRK07564 184 KGVKRIPLDRALAsmtvevidpVADYVEDLENVF---------DFdairkAGLRLGVDPLGGATGPYWKAIAERYGLDLT 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 202 TMGTSP----NGMNI-NAGVG-----STHpeGLAELVKEKGA-DIGLAFDGDGDRliavdekgN-IVDGDQIM------F 263
Cdd:PRK07564 255 VVNAPVdptfNFMPLdDDGKIrmdcsSPY--AMAGLLALKDAfDLAFANDPDGDR--------HgIVTPGGLMnpnhylA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 264 ICAKYmketgqLKHN------------TVVSTVMSNlgfyKALEANNITSDKTAVGDRYVMEEMKRGGYNLGGEQS-GHI 330
Cdd:PRK07564 325 VAIAY------LFHHrpgwragagvgkTLVSSAMID----RVAAKLGRKLYEVPVGFKWFVNGLDDGSLGFGGEESaGAS 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 331 ILL----DYITTGDGMLSALQLVNIMKMTKKPLSELAGEMT---------------------KFPQLLVNVrVTDKKLAl 385
Cdd:PRK07564 395 FLRrdgsVWTTDKDGLIAVLLAAEILAVTGKSPSEIYRELWarfgrpyysrhdapatpeqkaALRKLSPEL-VGATELA- 472
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 446443617 386 eNEKIKEI-------------IRVVEEemngDGRILVRPSGTEPLIRVMAE 423
Cdd:PRK07564 473 -GDPIDASlteapgngaaiggLKVVTE----NGWFAARPSGTETTYKIYAE 518
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
75-245 |
5.07e-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: 54.92 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 75 GVISTPGVAYLTKALGAQAGVMISASHNP---VQDNGIKFFGSDGF----KLTD---EQEAEIEALL---DKEVDelprp 141
Cdd:cd03085 87 GLLSTPAVSAVIRKRKATGGIILTASHNPggpEGDFGIKYNTSNGGpapeSVTDkiyEITKKITEYKiadDPDVD----- 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 142 tgtnLGQVSDY-FEGG----------QKYLQYIKQTVeeDF---------SGLHIALDCAHGATSSLAPYLFAD-LEADI 200
Cdd:cd03085 162 ----LSKIGVTkFGGKpftvevidsvEDYVELMKEIF--DFdaikkllsrKGFKVRFDAMHGVTGPYAKKIFVEeLGAPE 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446443617 201 ST-MGTSP----NGM----NInagvgsTHPEGLAELVKEKGADIGLAFDGDGDR 245
Cdd:cd03085 236 SSvVNCTPlpdfGGGhpdpNL------TYAKDLVELMKSGEPDFGAASDGDGDR 283
|
|
| PLN02307 |
PLN02307 |
phosphoglucomutase |
75-245 |
2.53e-04 |
|
phosphoglucomutase
Pssm-ID: 177942 [Multi-domain] Cd Length: 579 Bit Score: 43.49 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 75 GVISTPGVAYLTKA---LGAQAGVMISASHN---PVQDNGIKFFGSDGF----KLTD---EQEAEIEALldKEVDELPR- 140
Cdd:PLN02307 99 GLLSTPAVSAVIRErdgSKANGGFILTASHNpggPEEDFGIKYNYESGQpapeSITDkiyGNTLTIKEY--KMAEDIPDv 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443617 141 ----PTGTNLGQVSDY----FEGGQKYLQYIKQTVeeDFSGLHIAL---------DCAHGATSSLAPYLFADleadisTM 203
Cdd:PLN02307 177 dlsaVGVTKFGGPEDFdvevIDPVEDYVKLMKSIF--DFELIKKLLsrpdftfcfDAMHGVTGAYAKRIFVE------EL 248
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446443617 204 GTSPNgmNINAGV-----GSTHPEG----LAELVK----------EKGADIGLAFDGDGDR 245
Cdd:PLN02307 249 GAPES--SLLNCVpkedfGGGHPDPnltyAKELVKrmglgktsygDEPPEFGAASDGDGDR 307
|
|
| |
