|
Name |
Accession |
Description |
Interval |
E-value |
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
4-444 |
0e+00 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 791.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 4 RKYFGTDGVRGEVGGPVINAEFALRLGYAAGRVLARehavrgGSRPQVVIGKDTRISGYMLESALEAGLSAAGIDVLLAG 83
Cdd:PRK10887 1 RKYFGTDGIRGKVGQAPITPDFVLKLGWAAGKVLAR------QGRPKVLIGKDTRISGYMLESALEAGLAAAGVDVLLTG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 84 PVPTPAVAYLTRALRLVAGIVISASHNPYHDNGIKFFSAQGMKLPDEIEADIEAALDEPLGCVASEGLGRARRMGDAQGR 163
Cdd:PRK10887 75 PMPTPAVAYLTRTLRAEAGIVISASHNPYYDNGIKFFSADGTKLPDEVELAIEAELDKPLTCVESAELGKASRINDAAGR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 164 YIEFCKSTFPNDLDLNGMSIVVDAAHGAAYNIAPHVFRELGAEVHAIGVHPDGFNINKGVGALHPELLAKEVSARGAQLG 243
Cdd:PRK10887 155 YIEFCKSTFPNELSLRGLKIVVDCANGATYHIAPNVFRELGAEVIAIGCEPNGLNINDECGATDPEALQAAVLAEKADLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 244 IALDGDADRLQMVDGDGRIYNGDELMYAIVRERMQRGK-VDGVVGTLMTNFGFEREMKRLGVGFERANVGDRYVLEQMQA 322
Cdd:PRK10887 235 IAFDGDGDRVIMVDHLGNLVDGDQLLYIIARDRLRRGQlRGGVVGTLMSNMGLELALKQLGIPFVRAKVGDRYVLEKLQE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 323 RGWLYGGESSGHLLCLDCHSTGDGIVAALQVLTALRRNAVGLSEWVSDLRMYPQKMINVPLAPGLDWK-THAGLTAARKA 401
Cdd:PRK10887 315 KGWRLGGENSGHILCLDKTTTGDGIVAALQVLAAMVRSGMSLADLCSGMKLFPQVLINVRFKPGADDPlESEAVKAALAE 394
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1011865136 402 VEADLDGRGRILIRASGTEPKLRLMVEAEDEALAVASAEKLAA 444
Cdd:PRK10887 395 VEAELGGRGRVLLRKSGTEPLIRVMVEGEDEAQVTALAERIAD 437
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
6-443 |
0e+00 |
|
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the alpha-D-phosphohexomutase superfamily. It is required for the interconversion of glucosamine-6-phosphate and glucosamine-1-phosphate in the biosynthetic pathway of UDP-N-acetylglucosamine, an essential precursor to components of the cell envelope. In order to be active, GlmM must be phosphorylated, which can occur via autophosphorylation or by the Ser/Thr kinase StkP. GlmM functions in a classical ping-pong bi-bi mechanism with glucosamine-1,6-diphosphate as an intermediate. Other members of the alpha-D-phosphohexomutase superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100095 Cd Length: 434 Bit Score: 686.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 6 YFGTDGVRGEVGGPvINAEFALRLGYAAGRVLARehavrGGSRPQVVIGKDTRISGYMLESALEAGLSAAGIDVLLAGPV 85
Cdd:cd05802 1 LFGTDGIRGVANEP-LTPELALKLGRAAGKVLGK-----GGGRPKVLIGKDTRISGYMLESALAAGLTSAGVDVLLLGVI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 86 PTPAVAYLTRALRLVAGIVISASHNPYHDNGIKFFSAQGMKLPDEIEADIEAALDEPLGCVA-SEGLGRARRMGDAQGRY 164
Cdd:cd05802 75 PTPAVAYLTRKLRADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVEEEIEALIDKELELPPtGEKIGRVYRIDDARGRY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 165 IEFCKSTFPNDLdLNGMSIVVDAAHGAAYNIAPHVFRELGAEVHAIGVHPDGFNINKGVGALHPELLAKEVSARGAQLGI 244
Cdd:cd05802 155 IEFLKSTFPKDL-LSGLKIVLDCANGAAYKVAPEVFRELGAEVIVINNAPDGLNINVNCGSTHPESLQKAVLENGADLGI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 245 ALDGDADRLQMVDGDGRIYNGDELMYAIVRERMQRG--KVDGVVGTLMTNFGFEREMKRLGVGFERANVGDRYVLEQMQA 322
Cdd:cd05802 234 AFDGDADRVIAVDEKGNIVDGDQILAICARDLKERGrlKGNTVVGTVMSNLGLEKALKELGIKLVRTKVGDRYVLEEMLK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 323 RGWLYGGESSGHLLCLDCHSTGDGIVAALQVLTALRRNAVGLSEWVSDLRMYPQKMINVPLAPGLDWKTHAGLTAARKAV 402
Cdd:cd05802 314 HGANLGGEQSGHIIFLDHSTTGDGLLTALQLLAIMKRSGKSLSELASDMKLYPQVLVNVRVKDKKALLENPRVQAAIAEA 393
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1011865136 403 EADLDGRGRILIRASGTEPKLRLMVEAEDEALAVASAEKLA 443
Cdd:cd05802 394 EKELGGEGRVLVRPSGTEPLIRVMVEGEDEELVEKLAEELA 434
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
7-443 |
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: 561.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 7 FGTDGVRGEVGGPVINAEFALRLGYAAGRVLARehavRGGSRPQVVIGKDTRISGYMLESALEAGLSAAGIDVLLAGPVP 86
Cdd:TIGR01455 1 FGTDGVRGRAGQEPLTAELALLLGAAAGRVLRQ----GRDTAPRVVIGKDTRLSGYMLENALAAGLNSAGVDVLLLGPLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 87 TPAVAYLTRALRLVAGIVISASHNPYHDNGIKFFSAQGMKLPDEIEADIEAALDE--PLGCVASEGLGRARRMGDAQGRY 164
Cdd:TIGR01455 77 TPAVAYLTRTLRADAGVMISASHNPYEDNGIKFFGPGGFKLDDATEAAIEALLDEadPLPRPESEGLGRVKRYPDAVGRY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 165 IEFCKSTFPNDLDLNGMSIVVDAAHGAAYNIAPHVFRELGAEVHAIGVHPDGFNINKGVGALHPELLAKEVSARGAQLGI 244
Cdd:TIGR01455 157 IEFLKSTLPRGLTLSGLKVVLDCANGAAYKVAPHVFRELGAEVIAIGVEPDGLNINDGCGSTHLDALQKAVREHGADLGI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 245 ALDGDADRLQMVDGDGRIYNGDELMYAIVRERMQRG--KVDGVVGTLMTNFGFEREMKRLGVGFERANVGDRYVLEQMQA 322
Cdd:TIGR01455 237 AFDGDADRVLAVDANGRIVDGDQILYIIARALKESGelAGNTVVATVMSNLGLERALEKLGLTLIRTAVGDRYVLEEMRE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 323 RGWLYGGESSGHLLCLDCHSTGDGIVAALQVLTALRRNAVGLSEWVSDLRMYPQKMINVPLA-PGLDWKTHAGLTAARKA 401
Cdd:TIGR01455 317 SGYNLGGEQSGHIILLDYSTTGDGIVSALQVLTIMKKSGSTLSELAAEFVPYPQTLVNVRVAdRKLAAAEAPAVKAAIED 396
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1011865136 402 VEADLDGRGRILIRASGTEPKLRLMVEAEDEALAVASAEKLA 443
Cdd:TIGR01455 397 AEAELGGTGRILLRPSGTEPLIRVMVEAADEELVQQLADTLA 438
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
1-444 |
0e+00 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 514.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 1 MIRRKYFGTDGVRGEVGgPVINAEFALRLGYAAGRVLAREhavrggSRPQVVIGKDTRISGYMLESALEAGLSAAGIDVL 80
Cdd:COG1109 1 MTYKKLFGTDGIRGIVG-EELTPEFVLKLGRAFGTYLKEK------GGPKVVVGRDTRLSSPMLARALAAGLASAGIDVY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 81 LAGPVPTPAVAYLTRALRLVAGIVISASHNPYHDNGIKFFSAQGMKLPDEIEADIEAALDEP-LGCVASEGLGRARRMGD 159
Cdd:COG1109 74 DLGLVPTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKEdFRRAEAEEIGKVTRIED 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 160 AQGRYIEFCKSTFPNDLDLNGMSIVVDAAHGAAYNIAPHVFRELGAEVHAIGVHPDGFNINKGVG--ALHPELLAKEVSA 237
Cdd:COG1109 154 VLEAYIEALKSLVDEALRLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFPNHNPNpePENLEDLIEAVKE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 238 RGAQLGIALDGDADRLQMVDGDGRIYNGDELMYAIVRERMQRGKVDGVVGTLMTNFGFEREMKRLGVGFERANVGDRYVL 317
Cdd:COG1109 234 TGADLGIAFDGDADRLGVVDEKGRFLDGDQLLALLARYLLEKGPGGTVVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 318 EQMQARGWLYGGESSGHLLCLDCHSTGDGIVAALQVLTALRRNAVGLSEWVSDLRMYPQKMINVPLAPGLDW-KTHAGLT 396
Cdd:COG1109 314 EKMRETGAVLGGEESGGIIFPDFVPTDDGILAALLLLELLAKQGKSLSELLAELPRYPQPEINVRVPDEEKIgAVMEKLR 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1011865136 397 AARKA---------VEADLDGRGRILIRASGTEPKLRLMVEAEDEALAVASAEKLAA 444
Cdd:COG1109 394 EAVEDkeeldtidgVKVDLEDGGWVLVRPSGTEPLLRVYAEAKDEEEAEELLAELAE 450
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
5-446 |
8.18e-99 |
|
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: 302.89 E-value: 8.18e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 5 KYFGTDGVRGEVGGPvINAEFALRLGYAAGRVLarehavRGGSrpqVVIGKDTRISGYMLESALEAGLSAAGIDVLLAGP 84
Cdd:TIGR03990 2 LLFGTSGIRGIVGEE-LTPELALKVGKAFGTYL------RGGK---VVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 85 VPTPAVAYLTRALRLVAGIVISASHNPYHDNGIKFFSAQGMKLPDEIEADIEAALDEPLGCVAS-EGLGRARRMGDAQGR 163
Cdd:TIGR03990 72 APTPTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQEEEIEEIAESGDFERADwDEIGTVTSDEDAIDD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 164 YIEFCKSTFP-NDLDLNGMSIVVDAAHGAAYNIAPHVFRELGAEVHAIGVHPDGFNINKgvgalHPE-------LLAKEV 235
Cdd:TIGR03990 152 YIEAILDKVDvEAIRKKGFKVVVDCGNGAGSLTTPYLLRELGCKVITLNCQPDGTFPGR-----NPEptpenlkDLSALV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 236 SARGAQLGIALDGDADRLQMVDGDGRIYNGDELMYAIVRERMQRGKvDGVVGTLMTNFGFEREMKRLGVGFERANVGDRY 315
Cdd:TIGR03990 227 KATGADLGIAHDGDADRLVFIDEKGRFIGGDYTLALFAKYLLEHGG-GKVVTNVSSSRAVEDVAERHGGEVIRTKVGEVN 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 316 VLEQMQARGWLYGGESSGHLLCLDCHSTGDGIVAALQVLTALRRNAVGLSEWVSDLRMYPQKMINVPLaPGLDWKthagl 395
Cdd:TIGR03990 306 VAEKMKEEGAVFGGEGNGGWIFPDHHYCRDGLMAAALFLELLAEEGKPLSELLAELPKYPMSKEKVEL-PDEDKE----- 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1011865136 396 tAARKAVEA--------DLDG------RGRILIRASGTEPKLRLMVEAEDEALAVASAEKLAASL 446
Cdd:TIGR03990 380 -EVMEAVEEefadaeidTIDGvridfeDGWVLVRPSGTEPIVRIYAEAKTEERAEELLEEGRSLV 443
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
6-446 |
8.18e-94 |
|
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100089 Cd Length: 439 Bit Score: 289.86 E-value: 8.18e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 6 YFGTDGVRGEVGgPVINAEFALRLGYAAGrvlarehAVRGGSRpqVVIGKDTRISGYMLESALEAGLSAAGIDVLLAGPV 85
Cdd:cd03087 1 LFGTSGIRGVVG-EELTPELALKVGKALG-------TYLGGGT--VVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDIGIV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 86 PTPAVAYLTRALRLvAGIVISASHNPYHDNGIKFFSAQGMKLPDEIEADIEAALDEPLGCVAS-EGLGRARRMGDAQGRY 164
Cdd:cd03087 71 PTPALQYAVRKLGD-AGVMITASHNPPEYNGIKLVNPDGTEFSREQEEEIEEIIFSERFRRVAwDEVGSVRREDSAIDEY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 165 IEFCKSTFPNDLDLnGMSIVVDAAHGAAYNIAPHVFRELGAEVHAIGVHPDGFNINKgvgalHPE-------LLAKEVSA 237
Cdd:cd03087 150 IEAILDKVDIDGGK-GLKVVVDCGNGAGSLTTPYLLRELGCKVITLNANPDGFFPGR-----PPEptpenlsELMELVRA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 238 RGAQLGIALDGDADRLQMVDGDGRIYNGDELMyAIVRERMQRGKVDGVVGTLMTNFGFEREMKRLGVGFERANVGDRYVL 317
Cdd:cd03087 224 TGADLGIAHDGDADRAVFVDEKGRFIDGDKLL-ALLAKYLLEEGGGKVVTPVDASMLVEDVVEEAGGEVIRTPVGDVHVA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 318 EQMQARGWLYGGESSGHLLCLDCHSTGDGIVAALqVLTALRRNAVGLSEWVSDLRMYPQKMINVPLaPGLDWKthagltA 397
Cdd:cd03087 303 EEMIENGAVFGGEPNGGWIFPDHQLCRDGIMTAA-LLLELLAEEKPLSELLDELPKYPLLREKVEC-PDEKKE------E 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1011865136 398 ARKAVEADLDGRG---------RI-------LIRASGTEPKLRLMVEAEDEALAVASAEKLAASL 446
Cdd:cd03087 375 VMEAVEEELSDADedvdtidgvRIeyedgwvLIRPSGTEPKIRITAEAKTEERAKELLEEGRSKV 439
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
81-443 |
2.36e-84 |
|
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: 262.68 E-value: 2.36e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 81 LAGPVPTPAVAY-LTRALRLVAGIVISASHNPYHDNGIKFFSAQGMKLPDEIEADIEAALDEPLGCVAS-EGLGRARRMG 158
Cdd:cd03084 10 VVGDDITPETAVaLGQAIGSTGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSAVaYELGGSVKAV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 159 DAQGRYIEFCKSTFPNDLDLN-GMSIVVDAAHGAAYNIAPHVFRELGAEVHAIGVHPDGFNinkgvGALHPE-------- 229
Cdd:cd03084 90 DILQRYFEALKKLFDVAALSNkKFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCEPDGNF-----GNINPDpgsetnlk 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 230 LLAKEVSARGAQLGIALDGDADRLQMVDGDGRIYNGDELMYAIVRERMQRGKVDG-VVGTLMTNFGFEREMKRLGVGFER 308
Cdd:cd03084 165 QLLAVVKAEKADFGVAFDGDADRLIVVDENGGFLDGDELLALLAVELFLTFNPRGgVVKTVVSSGALDKVAKKLGIKVIR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 309 ANVGDRYVLEQMQARGWLYGGESSGHLLCLDCHSTGDGIVAALQVLTALRRNAVGLSEWVSDLRMYPQKMINVplapgld 388
Cdd:cd03084 245 TKTGFKWVGEAMQEGDVVLGGEESGGVIFPEFHPGRDGISAALLLLEILANLGKSLSELFSELPRYYYIRLKV------- 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1011865136 389 wkthagltaarkaveadldgRGRILIRASGTEPKLRLMVEAeDEALAVASAEKLA 443
Cdd:cd03084 318 --------------------RGWVLVRASGTEPAIRIYAEA-DTQEDVEQIKKEA 351
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
12-435 |
4.02e-71 |
|
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: 231.25 E-value: 4.02e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 12 VRGEVGGPvINAEFALRLGYAAGRVLAREHAvrggsrPQVVIGKDTRISGYMLESALEAGLSAAGIDVLLAGPVPTPAVA 91
Cdd:cd03089 7 IRGIAGEE-LTEEIAYAIGRAFGSWLLEKGA------KKVVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPVLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 92 YLTRALRLVAGIVISASHNPYHDNGIKFFSAQGMKLPDEIEADIEAALDEPLgcVASEGLGRARRMgDAQGRYIEFCKST 171
Cdd:cd03089 80 FATFHLDADGGVMITASHNPPEYNGFKIVIGGGPLSGEDIQALRERAEKGDF--AAATGRGSVEKV-DILPDYIDRLLSD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 172 FpnDLDLNGMSIVVDAAHGAAYNIAPHVFRELGAEVHAIGVHPDG-F-NinkgvgalH---PEL------LAKEVSARGA 240
Cdd:cd03089 157 I--KLGKRPLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCEPDGtFpN--------HhpdPTDpenledLIAAVKENGA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 241 QLGIALDGDADRLQMVDGDGRIYNGDELMYAIVRERMQRGKVDGVVGTLMTNFGFEREMKRLGVGFERANVGDRYVLEQM 320
Cdd:cd03089 227 DLGIAFDGDGDRLGVVDEKGEIIWGDRLLALFARDILKRNPGATIVYDVKCSRNLYDFIEEAGGKPIMWKTGHSFIKAKM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 321 QARGWLYGGESSGHL------LCLDchstgDGIVAALQVLTALRRNAVGLSEWVSDLRMYPQK-MINVPLApglDWKTHA 393
Cdd:cd03089 307 KETGALLAGEMSGHIffkdrwYGFD-----DGIYAALRLLELLSKSGKTLSELLADLPKYFSTpEIRIPVT---EEDKFA 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1011865136 394 GLTAARKAVEA------DLDG------RGRILIRASGTEPKLRLMVEAEDEALA 435
Cdd:cd03089 379 VIERLKEHFEFpgaeiiDIDGvrvdfeDGWGLVRASNTEPVLVLRFEADTEEGL 432
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
7-443 |
5.22e-67 |
|
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: 221.27 E-value: 5.22e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 7 FGTDGVRGevggpVINAEFA----LRLGYAAGRVLAREhavRGGSRPqVVIGKDTRisgYMLESALEA---GLSAAGIDV 79
Cdd:cd05800 3 FGTDGWRG-----IIAEDFTfenvRRVAQAIADYLKEE---GGGGRG-VVVGYDTR---FLSEEFARAvaeVLAANGIDV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 80 LLA-GPVPTPAVAYLTRALRLVAGIVISASHNPYHDNGIKFFSAQGMKLPDEIEADIEAALDEPLGCVASEGLGRARRMG 158
Cdd:cd05800 71 YLSdRPVPTPAVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARLASGEPPGLEARAEGLIETI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 159 DAQGRYIEFCKSTFpnDLDLN---GMSIVVDAAHGAAYNIAPHVFRELGAEVHAIGVHPD-GFninkgvGALHPE----- 229
Cdd:cd05800 151 DPKPDYLEALRSLV--DLEAIreaGLKVVVDPMYGAGAGYLEELLRGAGVDVEEIRAERDpLF------GGIPPEpiekn 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 230 --LLAKEVSARGAQLGIALDGDADRLQMVDGDGRIYNGDE----LMYAIVRERMQRGkvdGVVGTLMTNFGFEREMKRLG 303
Cdd:cd05800 223 lgELAEAVKEGGADLGLATDGDADRIGAVDEKGNFLDPNQilalLLDYLLENKGLRG---PVVKTVSTTHLIDRIAEKHG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 304 VGFERANVGDRYVLEQMQARGWLYGGESSGHLLCLDCHSTGDGIVAALQVLTALRRNAVGLSEWVSDL-----RMYPQKm 378
Cdd:cd05800 300 LPVYETPVGFKYIAEKMLEEDVLIGGEESGGLGIRGHIPERDGILAGLLLLEAVAKTGKPLSELVAELeeeygPSYYDR- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 379 INVPLAPGLDWKTHAGLTAARKAVEA--------DLDG-------RGRILIRASGTEPKLRLMVEAEDEALAVA---SAE 440
Cdd:cd05800 379 IDLRLTPAQKEAILEKLKNEPPLSIAggkvdevnTIDGvklvledGSWLLIRPSGTEPLLRIYAEAPSPEKVEAlldAGK 458
|
...
gi 1011865136 441 KLA 443
Cdd:cd05800 459 KLA 461
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
11-441 |
8.24e-60 |
|
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: 201.77 E-value: 8.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 11 GVRGEVGGPvINAEFALRLGYAAGRVLAREhavrgGSRPQVVIGKDTRISGYMLESALEAGLSAAGIDVLLAGPVPTPAV 90
Cdd:cd05803 6 GIRGIVGEG-LTPEVITRYVAAFATWQPER-----TKGGKIVVGRDGRPSGPMLEKIVIGALLACGCDVIDLGIAPTPTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 91 AYLTRALRLVAGIVISASHNPYHDNGIKFFSAQGMKL-PDEIEADIEAALDEPLGCVASEGLGRARRMGDAQGRYIEFCK 169
Cdd:cd05803 80 QVLVRQSQASGGIIITASHNPPQWNGLKFIGPDGEFLtPDEGEEVLSCAEAGSAQKAGYDQLGEVTFSEDAIAEHIDKVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 170 STFPNDLDLNG---MSIVVDAAHGAAYNIAPHVFRELGAEVHAIGVHPDG-FninkgvgALHPE-------LLAKEVSAR 238
Cdd:cd05803 160 ALVDVDVIKIRernFKVAVDSVNGAGGLLIPRLLEKLGCEVIVLNCEPTGlF-------PHTPEplpenltQLCAAVKES 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 239 GAQLGIALDGDADRLQMVDGDGRiYNGDELMYA-IVRERMQRGKVDG-VVGTLMTNFGFEREMKRLGVGFERANVGDRYV 316
Cdd:cd05803 233 GADVGFAVDPDADRLALVDEDGR-PIGEEYTLAlAVDYVLKYGGRKGpVVVNLSTSRALEDIARKHGVPVFRSAVGEANV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 317 LEQMQARGWLYGGESSGHLLCLDCHSTGDGIVAALQVLTALRRNAVGLSEWVSDL---RMYPQKMINVPLAPGLDWKTHA 393
Cdd:cd05803 312 VEKMKEVDAVIGGEGNGGVILPDVHYGRDSLVGIALVLQLLAASGKPLSEIVDELpqyYISKTKVTIAGEALERLLKKLE 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1011865136 394 GLtaARKAVEADLDG------RGRILIRASGTEPKLRLMVEAEDEALAVASAEK 441
Cdd:cd05803 392 AY--FKDAEASTLDGlrldseDSWVHVRPSNTEPIVRIIAEAPTQDEAEALADR 443
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
4-141 |
3.22e-52 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 172.02 E-value: 3.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 4 RKYFGTDGVRGEVGGPVINAEFALRLGYAAGRVLAREhavrgGSRPQVVIGKDTRISGYMLESALEAGLSAAGIDVLLAG 83
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGELTPEFALKLGQAIASYLRAQ-----GGGGKVVVGRDTRYSSRELARALAAGLASNGVEVILLG 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1011865136 84 PVPTPAVAYLTRALRLVAGIVISASHNPYHDNGIKFFSAQGMKLPDEIEADIEAALDE 141
Cdd:pfam02878 76 LLPTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEK 133
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
7-444 |
1.85e-40 |
|
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: 150.73 E-value: 1.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 7 FGTDGVRGEVG-GP-------VINAefalrlgyAAGrvLAR--EHAVRGGSRPQVVIGKDTRISGYmlESALEAG--LSA 74
Cdd:cd05799 4 FGTAGLRGKMGaGTnrmndytVRQA--------TQG--LANylKKKGPDAKNRGVVIGYDSRHNSR--EFAELTAavLAA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 75 AGIDV-LLAGPVPTPAVAYLTRALRLVAGIVISASHNPYHDNGIKFFSAQGMKLPDEIEADIEAALD---EPLGCVASEG 150
Cdd:cd05799 72 NGIKVyLFDDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEavlEPLDIKFEEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 151 L--GRARRMGDAQ-GRYIEFCKS--TFPNDLDLNGMSIVVDAAHGAAYNIAPHVFRELGAEvHAIGV----HPDG-Fnin 220
Cdd:cd05799 152 LdsGLIKYIGEEIdDAYLEAVKKllVNPELNEGKDLKIVYTPLHGVGGKFVPRALKEAGFT-NVIVVeeqaEPDPdF--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 221 KGVGALHPE---------LLAKEVsarGAQLGIALDGDADRLQMV----DGDGRIYNGDE----LMYAIVRERMQRGKVD 283
Cdd:cd05799 228 PTVKFPNPEepgaldlaiELAKKV---GADLILATDPDADRLGVAvkdkDGEWRLLTGNEigalLADYLLEQRKEKGKLP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 284 G---VVGTLMT---------NFGFerEMKRLGVGFEraNVGDRYVLEQMQARGWLYGGESS-GHLLCLDCHSTgDGIVAA 350
Cdd:cd05799 305 KnpvIVKTIVSsellrkiakKYGV--KVEETLTGFK--WIGNKIEELESGGKKFLFGFEESiGYLVGPFVRDK-DGISAA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 351 LQVLT-ALRRNAVGLSewVSDL--RMYPQ------KMINVPLaPGLDW--KTHAGLTAARKA---VEADLDGRGRILIRA 416
Cdd:cd05799 380 ALLAEmAAYLKAQGKT--LLDRldELYEKygyykeKTISITF-EGKEGpeKIKAIMDRLRNNpnvLTFYLEDGSRVTVRP 456
|
490 500
....*....|....*....|....*...
gi 1011865136 417 SGTEPKLRLMVEAEDEALAVASAEKLAA 444
Cdd:cd05799 457 SGTEPKIKFYIEVVGKKTLEEAEKKLDA 484
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
12-433 |
8.61e-33 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 128.95 E-value: 8.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 12 VRGEVGGPvINAEFALRLGYAAGRVLAREHAvrggsrPQVVIGKDTRISGYMLESALEAGLSAAGIDVLLAGPVPTPAVA 91
Cdd:PRK09542 6 VRGVVGEQ-IDEDLVRDVGAAFARLMRAEGA------TTVVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIGLASTDQLY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 92 YLTRALRLvAGIVISASHNPYHDNGIKFFSA------QGMKLpDEIEADIEA---ALDEPLGCVASEGLGRArrmgdaqg 162
Cdd:PRK09542 79 FASGLLDC-PGAMFTASHNPAAYNGIKLCRAgakpvgQDTGL-AAIRDDLIAgvpAYDGPPGTVTERDVLAD-------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 163 rYIEFCKSTfpndLDLNG---MSIVVDAAHGAAYNIAPHVFRELGAEVHAIGVHPDGFNINKGVGALHPELLA---KEVS 236
Cdd:PRK09542 149 -YAAFLRSL----VDLSGirpLKVAVDAGNGMGGHTVPAVLGGLPITLLPLYFELDGTFPNHEANPLDPANLVdlqAFVR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 237 ARGAQLGIALDGDADRLQMVDGDGRIYNGDELMyAIVRER-MQRGKVDGVVGTLMTNFGFEREMKRLGVGFERANVGDRY 315
Cdd:PRK09542 224 ETGADIGLAFDGDADRCFVVDERGQPVSPSAVT-ALVAAReLAREPGATIIHNLITSRAVPELVAERGGTPVRTRVGHSF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 316 VLEQMQARGWLYGGESSGHLLCLDCHSTGDGIVAALQVLTALRRNAVGLSEWVSDLRMYPQK-MIN--VPLAPGldwKTH 392
Cdd:PRK09542 303 IKALMAETGAIFGGEHSAHYYFRDFWGADSGMLAALHVLAALGEQDRPLSELMADYQRYAASgEINstVADAPA---RME 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1011865136 393 AGLTA-ARKAVEAD-LDGRGRIL-------IRASGTEPKLRLMVEAEDEA 433
Cdd:PRK09542 380 AVLKAfADRIVSVDhLDGVTVDLgdgswfnLRASNTEPLLRLNVEARTEE 429
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
264-371 |
9.15e-33 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 119.86 E-value: 9.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 264 NGDELMYAIVRERMQRGKV---DGVVGTLMTNFGFEREMKRLGVGFERANVGDRYVLEQMQARGWLYGGESSGHLLCLDC 340
Cdd:pfam02880 1 DGDQILALLAKYLLEQGKLppgAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLDH 80
|
90 100 110
....*....|....*....|....*....|.
gi 1011865136 341 HSTGDGIVAALQVLTALRRNAVGLSEWVSDL 371
Cdd:pfam02880 81 ATTKDGILAALLVLEILARTGKSLSELLEEL 111
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
9-275 |
4.76e-31 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 125.55 E-value: 4.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 9 TDGVRGEvggPVINAEFALR-LGYAAGRVLAREHAVRGGSRPQVVIGKDTRISGYMLESALEAGLSAAGIDVLLAGPVPT 87
Cdd:PLN02371 78 VEGVEGE---PVTLTPPAVEaIGAAFAEWLLEKKKADGSGELRVSVGRDPRISGPRLADAVFAGLASAGLDVVDMGLATT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 88 PAVAYLTRALR--LVAGIVISASHNPYHDNGIKFFSAQGMKLPDEIEADIEAALDEPLGCVASEGLGRARRMGDAQGR-- 163
Cdd:PLN02371 155 PAMFMSTLTERedYDAPIMITASHLPYNRNGLKFFTKDGGLGKPDIKDILERAARIYKEWSDEGLLKSSSGASSVVCRvd 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 164 YIEFCKST----------FPNDLD--LNGMSIVVDAAHGAAYNIAPHVFRELGAEVHAiGVH--PDGFNINkgvGALHPE 229
Cdd:PLN02371 235 FMSTYAKHlrdaikegvgHPTNYEtpLEGFKIVVDAGNGAGGFFAEKVLEPLGADTSG-SLFlePDGMFPN---HIPNPE 310
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1011865136 230 ------LLAKEVSARGAQLGIALDGDADRLQMVDGDGRIYNGDE---LMYAIVRE 275
Cdd:PLN02371 311 dkaamsATTQAVLANKADLGIIFDTDVDRSAVVDSSGREINRNRliaLMSAIVLE 365
|
|
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
7-371 |
1.57e-30 |
|
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: 122.36 E-value: 1.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 7 FGTDGVRGEVGGPvINAEFALRLGYAAGRVLARehavrgGSRpqVVIGKDTRISGYMLESALEAGLSAAGIDVLLAGPVP 86
Cdd:cd05805 2 FGGRGVSGLINVD-ITPEFATRLGAAYGSTLPP------GST--VTVSRDASRASRMLKRALISGLLSTGVNVRDLGALP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 87 TPAVAYLTRALRLVAGIVISAShnPYHDNG--IKFFSAQGMKLPDEIEADIEAAL-DEPLGCVASEGLGRARRMGDAQGR 163
Cdd:cd05805 73 LPVARYAIRFLGASGGIHVRTS--PDDPDKveIEFFDSRGLNISRAMERKIENAFfREDFRRAHVDEIGDITEPPDFVEY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 164 YIE-FCKSTFPNDLDLNGMSIVVDAAHGAAYNIAPHVFRELGAEVHAI------GVHPDGFNINKGVgalhpELLAKEVS 236
Cdd:cd05805 151 YIRgLLRALDTSGLKKSGLKVVIDYAYGVAGIVLPGLLSRLGCDVVILnarldeDAPRTDTERQRSL-----DRLGRIVK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 237 ARGAQLGIALDGDADRLQMVDGDGRIYNGDEL---MYAIVRERMQRGKVdgVVGTLMTNFgFEREMKRLGVGFERANVGD 313
Cdd:cd05805 226 ALGADFGVIIDPNGERLILVDEAGRVISDDLLtalVSLLVLKSEPGGTV--VVPVTAPSV-IEQLAERYGGRVIRTKTSP 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1011865136 314 RYVLEQMqARGWLYGGESSGHLLCLDCHSTGDGIVAALQVLTALRRNAVGLSEWVSDL 371
Cdd:cd05805 303 QALMEAA-LENVVLAGDGDGGFIFPEFHPGFDAIAALVKILEMLARTNISLSQIVDEL 359
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
12-446 |
1.48e-26 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 111.19 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 12 VRGEVGGPvINAEFALRLGYAAGRVLarehavrggsRPQ-VVIGKDTRISGYMLESALEAGLSAAGIDVLLAGPVPTPAV 90
Cdd:PRK15414 12 IRGKLGEE-LNEDIAWRIGRAYGEFL----------KPKtIVLGGDVRLTSETLKLALAKGLQDAGVDVLDIGMSGTEEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 91 AYLTRALRLVAGIVISASHNPYHDNGIKFFSAQGMKLP-DEIEADIE---AALDEPLGCVASEGLGRARRMGDAqgrYIE 166
Cdd:PRK15414 81 YFATFHLGVDGGIEVTASHNPMDYNGMKLVREGARPISgDTGLRDVQrlaEANDFPPVDETKRGRYQQINLRDA---YVD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 167 FCKStFPNDLDLNGMSIVVDAAHGAAYNIAPHV---FRELGAEVHAIGVH--PDGFNINKGVGALHPELLA---KEVSAR 238
Cdd:PRK15414 158 HLFG-YINVKNLTPLKLVINSGNGAAGPVVDAIearFKALGAPVELIKVHntPDGNFPNGIPNPLLPECRDdtrNAVIKH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 239 GAQLGIALDGDADRLQMVDGDGRIYNGDELMYAIVRERMQRGKVDGVVGTLMTNFGFEREMKRLGVGFERANVGDRYVLE 318
Cdd:PRK15414 237 GADMGIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPGAKIIHDPRLSWNTVDVVTAAGGTPVMSKTGHAFIKE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 319 QMQARGWLYGGESSGHLLCLDCHSTGDGIVAALQV--LTALRRNAVGlsEWVSDlRM--YPQK-MINVPLAPGLDWKTHA 393
Cdd:PRK15414 317 RMRKEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVaeLVCLKGKTLG--ELVRD-RMaaFPASgEINSKLAQPVEAINRV 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1011865136 394 GLTAARKAVEAD-LDGRG------RILIRASGTEPKLRLMVEAE-DEALAVASAEKLAASL 446
Cdd:PRK15414 394 EQHFSREALAVDrTDGISmtfadwRFNLRSSNTEPVVRLNVESRgDVPLMEARTRTLLTLL 454
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
7-435 |
2.50e-24 |
|
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: 104.98 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 7 FGTDGVRGEVggpvinAEFALRLGYAAGRVLAR--EHAVRGGSrpqVVIGKDTRISGYMLESALEAGLSAAGIDVLLAGP 84
Cdd:cd03088 2 FGTSGLRGLV------TDLTDEVCYAYTRAFLQhlESKFPGDT---VAVGRDLRPSSPRIAAACAAALRDAGFRVVDCGA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 85 VPTPAVAYLTRAlRLVAGIVISASHNPYHDNGIKFFSAQGmklpdEI----EADIEAALDEPLGCVASEGLGRARRMGDA 160
Cdd:cd03088 73 VPTPALALYAMK-RGAPAIMVTGSHIPADRNGLKFYRPDG-----EItkadEAAILAALVELPEALFDPAGALLPPDTDA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 161 QGRYIEFCKSTFPNDLdLNGMSIVVDAAHGAAYNIAPHVFRELGAEVHAIGvHPDGFnINKGVGALHPE---LLAKEVSA 237
Cdd:cd03088 147 ADAYIARYTDFFGAGA-LKGLRIGVYQHSSVGRDLLVRILEALGAEVVPLG-RSDTF-IPVDTEAVRPEdraLAAAWAAE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 238 RGAQLGIALDGDADRLQMVDGDGRIYNGDeLMYAIVRERMQrgkVDGVVGTLMTNFGFEremkrLGVGFE---RANVGDR 314
Cdd:cd03088 224 HGLDAIVSTDGDGDRPLVADETGEWLRGD-ILGLLTARFLG---ADTVVTPVSSNSAIE-----LSGFFKrvvRTRIGSP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 315 YVLEQMQA-----RGWLYGGESS-GHLLCLDCHS---------TGDGIVAALQVLTALRRNAVGLSEWVSDLR---MYPQ 376
Cdd:cd03088 295 YVIAAMAEaaaagAGRVVGYEANgGFLLGSDIERngrtlkalpTRDAVLPILAVLAAAKEAGIPLSELVASLParfTASD 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1011865136 377 KMINVPLAPGL--------DWKTHAGLTAARKAVEA---DLDG------RGRIL-IRASGTEPKLRLMVEAEDEALA 435
Cdd:cd03088 375 RLQNFPTEKSQaliarlsaDPEARAAFFFALGGEVAsidTTDGlrmtfaNGDIVhLRPSGNAPELRCYVEADSEERA 451
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
3-433 |
2.12e-17 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 84.74 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 3 RRKYFGTDGVRGEVGGpvinaefalrlGYAAGRVLAREHAVRG------------GSRPQVVIGKDTRISGYMLESALEA 70
Cdd:PTZ00150 43 KRMEFGTAGLRGKMGA-----------GFNCMNDLTVQQTAQGlcayvietfgqaLKSRGVVIGYDGRYHSRRFAEITAS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 71 GLSAAGIDVLLAGP-VPTPAVAYLTRALRLVAGIVISASHNPYHDNGIKFFSAQGMKLPDEIEADIEAALD---EPLGCV 146
Cdd:PTZ00150 112 VFLSKGFKVYLFGQtVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVYWSNGAQIIPPHDKNISAKILsnlEPWSSS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 147 ---ASEGL--GRARRMGDAqgrYIEFCKSTF-PNDLDLNGMSIVVDAAHGAAYNIAPHVFRELGAEVH---AIGVHPDG- 216
Cdd:PTZ00150 192 weyLTETLveDPLAEVSDA---YFATLKSEYnPACCDRSKVKIVYTAMHGVGTRFVQKALHTVGLPNLlsvAQQAEPDPe 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 217 F------NINKGVGALHpelLAKEVSAR-GAQLGIALDGDADRL---QMVDGDGRIYNGDEL-----MYAIVRERMQRGK 281
Cdd:PTZ00150 269 FptvtfpNPEEGKGALK---LSMETAEAhGSTVVLANDPDADRLavaEKLNNGWKIFTGNELgallaWWAMKRYRRQGID 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 282 VD------GVVGTLMTNFGFEREmkrlGVGFERANVGDRYV----LEQMQARGW--LYGGESS-GHllCLDCHSTG-DGI 347
Cdd:PTZ00150 346 KSkcfficTVVSSRMLKKMAEKE----GFQYDETLTGFKWIgnkaIELNAENGLttLFAYEEAiGF--MLGTRVRDkDGV 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 348 VAA---LQVLTALRRNAVGLSEWVSDLR--------------------------------MYPQKMINVP------LAPG 386
Cdd:PTZ00150 420 TAAavvAEMALYLYERGKTLVEHLESLYkqygyhftnnsyyicydpsrivsifndirnngSYPTKLGGYPvtrirdLTTG 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1011865136 387 LDwkTHAGLTAARKAVEAD-------LDGRGRILIRASGTEPKLRLMVE---AEDEA 433
Cdd:PTZ00150 500 YD--TATPDGKPLLPVSAStqmitfyFENGAIITIRGSGTEPKLKWYAElsgTKDEA 554
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
164-260 |
3.17e-15 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 71.17 E-value: 3.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 164 YIEFCKSTFPNDLDLN-GMSIVVDAAHGAAYNIAPHVFRELGAEVHAIGVHPDGFNINKGVGALHPE---LLAKEVSARG 239
Cdd:pfam02879 2 YIDHLLELVDSEALKKrGLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDPDFPTRAPNPEEPEalaLLIELVKSVG 81
|
90 100
....*....|....*....|.
gi 1011865136 240 AQLGIALDGDADRLQMVDGDG 260
Cdd:pfam02879 82 ADLGIATDGDADRLGVVDERG 102
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
7-252 |
1.64e-12 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 69.39 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 7 FGTDGVRGEVGGPVINAEFALrlgyAAGRVLAREHAVRGGSRPqVVIGKDTR-ISGYMLESALEAgLSAAGIDVLLA--- 82
Cdd:PRK07564 40 FGTSGHRGSSLQPSFNENHIL----AIFQAICEYRGKQGITGP-LFVGGDTHaLSEPAIQSALEV-LAANGVGVVIVgrg 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 83 GPVPTPAV-----AYLTRALRLVAGIVISASHNPYHDNGIKFFSAQGMKLPDEIEADIEAA----LDEPLGCVASEGLGR 153
Cdd:PRK07564 114 GYTPTPAVshailKYNGRGGGLADGIVITPSHNPPEDGGIKYNPPNGGPADTDVTDAIEARanelLAYGLKGVKRIPLDR 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 154 ARRMG-----DAQGRYIEFCKSTFpnDLDL---NGMSIVVDAAHGA----AYNIAPHVFRE---LGAEVHAI--GVHPDG 216
Cdd:PRK07564 194 ALASMtveviDPVADYVEDLENVF--DFDAirkAGLRLGVDPLGGAtgpyWKAIAERYGLDltvVNAPVDPTfnFMPLDD 271
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1011865136 217 FninkgvGALHPE-----LLAKEVSARGA-QLGIALDGDADR 252
Cdd:PRK07564 272 D------GKIRMDcsspyAMAGLLALKDAfDLAFANDPDGDR 307
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
378-446 |
4.20e-12 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 61.13 E-value: 4.20e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 378 MINVPLAPGLDWKTHAGLTAARKAVEADLDGRGRIL-IRASGTEPKLRLMVEAEDEALAVASAEKLAASL 446
Cdd:pfam00408 1 LINVRVAEKKKLAALAAILKVFADAEKILGEDGRRLdVRPSGTEPVLRVMVEGDSDEELARLADEIADLL 70
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
50-435 |
5.38e-12 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 67.76 E-value: 5.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 50 QVVIGKDTRISGYMLESALEAGLSAA-GIDVLLAGPVPTPAVAYLTralrlvagivisASHNPYHDNGIKFFSAQGMklp 128
Cdd:PTZ00302 154 KVHVGRDTRPSSPELVSALLRGLKLLiGSNVRNFGIVTTPQLHFLV------------AFANGLGVDVVESSDELYY--- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 129 deieADIEAALDEPLGCVASEGLGRARRMGDAQgryiefckstfpndldlngmsIVVDAAHG-AAYNIAP--HVFRELGA 205
Cdd:PTZ00302 219 ----AYLLAAFKELYRTLQEGGPVDLTQNNSKI---------------------LVVDCANGvGGYKIKRffEALKQLGI 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 206 EVHAIGVHPDGFNI-NKGVGALH------PELLAKEVSARGAQLGIALDGDADRL----QMVDGDG--RIYNGDEL--MY 270
Cdd:PTZ00302 274 EIIPININCDEEELlNDKCGADYvqktrkPPRAMKEWPGDEETRVASFDGDADRLvyffPDKDGDDkwVLLDGDRIaiLY 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 271 A-IVRERMQRGKVD-----GVVGTLMTNFGF----EREMKRL---------------------GVGFErANvGDRYVL-- 317
Cdd:PTZ00302 354 AmLIKKLLGKIQLKkkldiGVVQTAYANGAStnylNELLGRLrvycaptgvknlhpkahkydiGIYFE-AN-GHGTVLfn 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 318 --------EQMQARGWLYGGESS-GHLLCLDCHSTGDGIVAALQVLTALRrnAVGLS--EWvsdLRMY---PQKMINVPL 383
Cdd:PTZ00302 432 ekalaewaKFLAKQNALNSACRQlEKFLRLFNQTIGDAISDLLAVELALA--FLGLSfqDW---LNLYtdlPSRQDKVTV 506
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1011865136 384 APGLDWKTH---------AGLTAARKAVEADLDGRGRILIRASGTEPKLRLMVEAEDEALA 435
Cdd:PTZ00302 507 KDRTLITNTedetrllepKGLQDKIDAIVSKYDNAARAFIRPSGTEPVVRVYAEAPTLEQA 567
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
46-443 |
8.97e-11 |
|
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: 63.77 E-value: 8.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 46 GSRPQVVIGKDTRISGYMLESALEAGLSAAGIDVLLAGPVPTPAVAYLTRALRLVaGIVISASHNPYHDNGIKFFSaqgm 125
Cdd:cd03086 100 SVPANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYLVRAANTE-GAYGEPTEEGYYEKLSKAFN---- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 126 KLpdeieadieaaldeplgcvaseglgrarrmgdaqgryiefckSTFPNDLDLNGMSIVVDAAHG-AAYNIAPhvFRELG 204
Cdd:cd03086 175 EL------------------------------------------YNLLQDGGDEPEKLVVDCANGvGALKLKE--LLKRL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 205 AEVHAIGVHPDGF----NINKGVGALH-------PELLAKEVS-ARGAqlgiALDGDADRL-----------QMVDGDgR 261
Cdd:cd03086 211 KKGLSVKIINDGEegpeLLNDGCGADYvktkqkpPRGFELKPPgVRCC----SFDGDADRLvyfypdssnkfHLLDGD-K 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 262 IyngdELMYAI-VRERMQRGKVD-----GVVGT-------------------LMTNFGfereMKRL---------GVGFE 307
Cdd:cd03086 286 I----ATLFAKfIKELLKKAGEElkltiGVVQTayangastkyledvlkvpvVCTPTG----VKHLhhaaeefdiGVYFE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 308 rANvGDRYVLEQMQARGWLYGGESSGHLLCLDCHS-----------TGDGIVAALQVLTALRRNAVGLSEWvsdLRMY-- 374
Cdd:cd03086 358 -AN-GHGTVLFSESALAKIEENSSLSDEQEKAAKTllafsrlinqtVGDAISDMLAVELILAALGWSPQDW---DNLYtd 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 375 -PQKMINVPLAPGLDWKThaglTAA-RKAVE------------ADLDGrGRILIRASGTEPKLRLMVEAEDealaVASAE 440
Cdd:cd03086 433 lPNRQLKVKVPDRSVIKT----TDAeRRLVEpkglqdkidaivAKYNN-GRAFVRPSGTEDVVRVYAEAAT----QEEAD 503
|
...
gi 1011865136 441 KLA 443
Cdd:cd03086 504 ELA 506
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
7-157 |
1.59e-09 |
|
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100094 [Multi-domain] Cd Length: 522 Bit Score: 59.95 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 7 FGTDGVRGEvggpvinaefALRLGYAAGRVLAREHAV------RGGSRPqVVIGKDTR-ISGYMLESALEAgLSAAGIDV 79
Cdd:cd05801 23 FGTSGHRGS----------SLKGSFNEAHILAISQAIcdyrksQGITGP-LFLGKDTHaLSEPAFISALEV-LAANGVEV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 80 LLA---GPVPTPAV--AYLT----RALRLVAGIVISASHNPYHDNGIKFFSAQGMKLPDEIEADIEAALDEPLgcvaSEG 150
Cdd:cd05801 91 IIQqndGYTPTPVIshAILTynrgRTEGLADGIVITPSHNPPEDGGFKYNPPHGGPADTDITRWIEKRANALL----ANG 166
|
....*..
gi 1011865136 151 LGRARRM 157
Cdd:cd05801 167 LKGVKRI 173
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
52-260 |
3.66e-09 |
|
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate (G-1-P) and glucose-6-phosphate (G-6-P) via a glucose 1,6-diphosphate intermediate, an important metabolic step in prokaryotes and eukaryotes. In one direction, G-1-P produced from sucrose catabolism is converted to G-6-P, the first intermediate in glycolysis. In the other direction, conversion of G-6-P to G-1-P generates a substrate for synthesis of UDP-glucose which is required for synthesis of a variety of cellular constituents including cell wall polymers and glycoproteins. The PGM1 family also includes a non-enzymatic PGM-related protein (PGM-RP) thought to play a structural role in eukaryotes, as well as pp63/parafusin, a phosphoglycoprotein that plays an important role in calcium-regulated exocytosis in ciliated protozoans. PGM1 belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100087 [Multi-domain] Cd Length: 548 Bit Score: 58.77 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 52 VIGKDTRIsgYMLESALE-AGLSAA-GIDVLLAGP---VPTPAVAYLTRALRLVAGIVISASHNP---YHDNGIKFFSAQ 123
Cdd:cd03085 53 VVGGDGRY--YNKEAIQIiIKIAAAnGVGKVVVGQnglLSTPAVSAVIRKRKATGGIILTASHNPggpEGDFGIKYNTSN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 124 GMKLPDEI------------EADIEAALDEPLGCVASEGLGRAR---RMGDAQGRYIEFCKSTFPND-----LDLNGMSI 183
Cdd:cd03085 131 GGPAPESVtdkiyeitkkitEYKIADDPDVDLSKIGVTKFGGKPftvEVIDSVEDYVELMKEIFDFDaikklLSRKGFKV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011865136 184 VVDAAHGAAYNIAPHVF-RELGAE----VHAI------GVHPDgfninkgvgalhPEL-----LAKEVSARGAQLGIALD 247
Cdd:cd03085 211 RFDAMHGVTGPYAKKIFvEELGAPessvVNCTplpdfgGGHPD------------PNLtyakdLVELMKSGEPDFGAASD 278
|
250
....*....|...
gi 1011865136 248 GDADRlQMVDGDG 260
Cdd:cd03085 279 GDGDR-NMILGKG 290
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
95-133 |
2.89e-03 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 40.01 E-value: 2.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1011865136 95 RALRL--VAGIVISASHNPYHDNGIKFFSAQGMKLPDEIEA 133
Cdd:PLN02895 52 RSLKTgaATGLMITASHNPVSDNGVKIVDPSGGMLPQAWEP 92
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
35-96 |
3.53e-03 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 39.62 E-value: 3.53e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1011865136 35 RVLAREHAVRGGSRP-QVVIGKDTRISGYMLESALEAGLSAAGIDVLLAGPVPTPAVAYLTRA 96
Cdd:PLN02895 113 FVKKENIPAVGGNPPaEVLLGRDTRPSGPALLAAALKGVRAIGARAVDMGILTTPQLHWMVRA 175
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