|
Name |
Accession |
Description |
Interval |
E-value |
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
3-443 |
0e+00 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 841.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 3 KKYFGTDGIRGKVGEPPITADFLLKLGWATGRVFANERHDFVLVGKDTRISGYMFESALEAGLTAAGVDTRLLGPMPTPG 82
Cdd:PRK10887 1 RKYFGTDGIRGKVGQAPITPDFVLKLGWAAGKVLARQGRPKVLIGKDTRISGYMLESALEAGLAAAGVDVLLTGPMPTPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 83 IAYLTRTLRAQAGIVISASHNPYYDNGVKFFSVQGTKLPDDIEKEIEHYMDSPMTTVDSAHLGKAKRLEDAAGRYIEYCK 162
Cdd:PRK10887 81 VAYLTRTLRAEAGIVISASHNPYYDNGIKFFSADGTKLPDEVELAIEAELDKPLTCVESAELGKASRINDAAGRYIEFCK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 163 ASVPTRLDFDHMKIVVDCAHGATYHIAPHVFSEIGAEVISIGVQPNGLNINDNCGATKPEMLAATVLANHADLGIALDGD 242
Cdd:PRK10887 161 STFPNELSLRGLKIVVDCANGATYHIAPNVFRELGAEVIAIGCEPNGLNINDECGATDPEALQAAVLAEKADLGIAFDGD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 243 GDRLIMVDHKGEIVDGDELIYIIAKSRLSSGQMAGPVVGTLMTNLGMEHALAQLGIPLLRAKVGDRYVMELLTKHNGILG 322
Cdd:PRK10887 241 GDRVIMVDHLGNLVDGDQLLYIIARDRLRRGQLRGGVVGTLMSNMGLELALKQLGIPFVRAKVGDRYVLEKLQEKGWRLG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 323 GENSGHIICLDKTTTGDGIIAALQVLAEMQYSGQSLHELKSGMQKYPQILINIKTAKKVN--LDHyDGIQQAVKAVENKL 400
Cdd:PRK10887 321 GENSGHILCLDKTTTGDGIVAALQVLAAMVRSGMSLADLCSGMKLFPQVLINVRFKPGADdpLES-EAVKAALAEVEAEL 399
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 518703060 401 GDKGRVLLRTSGTEPLIRVMVEGEQGDAVNNYAQQLAEAVKSA 443
Cdd:PRK10887 400 GGRGRVLLRKSGTEPLIRVMVEGEDEAQVTALAERIADAVKAA 442
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
5-437 |
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: 720.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 5 YFGTDGIRGKVGEPpITADFLLKLGWATGRVFANERHD-FVLVGKDTRISGYMFESALEAGLTAAGVDTRLLGPMPTPGI 83
Cdd:cd05802 1 LFGTDGIRGVANEP-LTPELALKLGRAAGKVLGKGGGRpKVLIGKDTRISGYMLESALAAGLTSAGVDVLLLGVIPTPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 84 AYLTRTLRAQAGIVISASHNPYYDNGVKFFSVQGTKLPDDIEKEIEHYMDSPMTTV-DSAHLGKAKRLEDAAGRYIEYCK 162
Cdd:cd05802 80 AYLTRKLRADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVEEEIEALIDKELELPpTGEKIGRVYRIDDARGRYIEFLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 163 ASVPtRLDFDHMKIVVDCAHGATYHIAPHVFSEIGAEVISIGVQPNGLNINDNCGATKPEMLAATVLANHADLGIALDGD 242
Cdd:cd05802 160 STFP-KDLLSGLKIVLDCANGAAYKVAPEVFRELGAEVIVINNAPDGLNINVNCGSTHPESLQKAVLENGADLGIAFDGD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 243 GDRLIMVDHKGEIVDGDELIYIIAKSRLSSGQMAGP-VVGTLMTNLGMEHALAQLGIPLLRAKVGDRYVMELLTKHNGIL 321
Cdd:cd05802 239 ADRVIAVDEKGNIVDGDQILAICARDLKERGRLKGNtVVGTVMSNLGLEKALKELGIKLVRTKVGDRYVLEEMLKHGANL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 322 GGENSGHIICLDKTTTGDGIIAALQVLAEMQYSGQSLHELKSGMQKYPQILINIKTAKKVNLDHYDGIQQAVKAVENKLG 401
Cdd:cd05802 319 GGEQSGHIIFLDHSTTGDGLLTALQLLAIMKRSGKSLSELASDMKLYPQVLVNVRVKDKKALLENPRVQAAIAEAEKELG 398
|
410 420 430
....*....|....*....|....*....|....*.
gi 518703060 402 DKGRVLLRTSGTEPLIRVMVEGEQGDAVNNYAQQLA 437
Cdd:cd05802 399 GEGRVLVRPSGTEPLIRVMVEGEDEELVEKLAEELA 434
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
6-441 |
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: 636.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 6 FGTDGIRGKVGEPPITADFLLKLGWATGRVFA--NERHDFVLVGKDTRISGYMFESALEAGLTAAGVDTRLLGPMPTPGI 83
Cdd:TIGR01455 1 FGTDGVRGRAGQEPLTAELALLLGAAAGRVLRqgRDTAPRVVIGKDTRLSGYMLENALAAGLNSAGVDVLLLGPLPTPAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 84 AYLTRTLRAQAGIVISASHNPYYDNGVKFFSVQGTKLPDDIEKEIEHYMD--SPMTTVDSAHLGKAKRLEDAAGRYIEYC 161
Cdd:TIGR01455 81 AYLTRTLRADAGVMISASHNPYEDNGIKFFGPGGFKLDDATEAAIEALLDeaDPLPRPESEGLGRVKRYPDAVGRYIEFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 162 KASVPTRLDFDHMKIVVDCAHGATYHIAPHVFSEIGAEVISIGVQPNGLNINDNCGATKPEMLAATVLANHADLGIALDG 241
Cdd:TIGR01455 161 KSTLPRGLTLSGLKVVLDCANGAAYKVAPHVFRELGAEVIAIGVEPDGLNINDGCGSTHLDALQKAVREHGADLGIAFDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 242 DGDRLIMVDHKGEIVDGDELIYIIAKSRLSSGQMAGP-VVGTLMTNLGMEHALAQLGIPLLRAKVGDRYVMELLTKHNGI 320
Cdd:TIGR01455 241 DADRVLAVDANGRIVDGDQILYIIARALKESGELAGNtVVATVMSNLGLERALEKLGLTLIRTAVGDRYVLEEMRESGYN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 321 LGGENSGHIICLDKTTTGDGIIAALQVLAEMQYSGQSLHELKSGMQKYPQILINIKTA-KKVNLDHYDGIQQAVKAVENK 399
Cdd:TIGR01455 321 LGGEQSGHIILLDYSTTGDGIVSALQVLTIMKKSGSTLSELAAEFVPYPQTLVNVRVAdRKLAAAEAPAVKAAIEDAEAE 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 518703060 400 LGDKGRVLLRTSGTEPLIRVMVEGEQGDAVNNYAQQLAEAVK 441
Cdd:TIGR01455 401 LGGTGRILLRPSGTEPLIRVMVEAADEELVQQLADTLADVVS 442
|
|
| 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: 541.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 1 MT-KKYFGTDGIRGKVGEPpITADFLLKLGWATGRVFANERHDFVLVGKDTRISGYMFESALEAGLTAAGVDTRLLGPMP 79
Cdd:COG1109 1 MTyKKLFGTDGIRGIVGEE-LTPEFVLKLGRAFGTYLKEKGGPKVVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 80 TPGIAYLTRTLRAQAGIVISASHNPYYDNGVKFFSVQGTKLPDDIEKEIEHYMDSPM-TTVDSAHLGKAKRLEDAAGRYI 158
Cdd:COG1109 80 TPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKEDfRRAEAEEIGKVTRIEDVLEAYI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 159 EYCKASVPTRLDFDHMKIVVDCAHGATYHIAPHVFSEIGAEVISIGVQPNGLNINDNCG--ATKPEMLAATVLANHADLG 236
Cdd:COG1109 160 EALKSLVDEALRLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFPNHNPNpePENLEDLIEAVKETGADLG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 237 IALDGDGDRLIMVDHKGEIVDGDELIYIIAKSRLSSGQmAGPVVGTLMTNLGMEHALAQLGIPLLRAKVGDRYVMELLTK 316
Cdd:COG1109 240 IAFDGDADRLGVVDEKGRFLDGDQLLALLARYLLEKGP-GGTVVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKMRE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 317 HNGILGGENSGHIICLDKTTTGDGIIAALQVLAEMQYSGQSLHELKSGMQKYPQILINIKTAKKVNLDH-YDGIQQAVKA 395
Cdd:COG1109 319 TGAVLGGEESGGIIFPDFVPTDDGILAALLLLELLAKQGKSLSELLAELPRYPQPEINVRVPDEEKIGAvMEKLREAVED 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 518703060 396 ---------VENKLGDKGRVLLRTSGTEPLIRVMVEGEQGDAVNNYAQQLAEAVKSAI 444
Cdd:COG1109 399 keeldtidgVKVDLEDGGWVLVRPSGTEPLLRVYAEAKDEEEAEELLAELAELVEEAL 456
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
3-444 |
3.78e-107 |
|
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: 324.08 E-value: 3.78e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 3 KKYFGTDGIRGKVGEPpITADFLLKLGWATGRVFaneRHDFVLVGKDTRISGYMFESALEAGLTAAGVDTRLLGPMPTPG 82
Cdd:TIGR03990 1 MLLFGTSGIRGIVGEE-LTPELALKVGKAFGTYL---RGGKVVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLGIAPTPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 83 IAYLTRTLRAQAGIVISASHNPYYDNGVKFFSVQGTKLPDDIEKEIEH-YMDSPMTTVDSAHLGKAKRLEDAAGRYIEYC 161
Cdd:TIGR03990 77 LQYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQEEEIEEiAESGDFERADWDEIGTVTSDEDAIDDYIEAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 162 KASVP-TRLDFDHMKIVVDCAHGATYHIAPHVFSEIGAEVISIGVQPNGLNINDNcgatkPE-------MLAATVLANHA 233
Cdd:TIGR03990 157 LDKVDvEAIRKKGFKVVVDCGNGAGSLTTPYLLRELGCKVITLNCQPDGTFPGRN-----PEptpenlkDLSALVKATGA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 234 DLGIALDGDGDRLIMVDHKGEIVDGDELIYIIAKSRLSSGqmAGPVVGTLMTNLGMEHALAQLGIPLLRAKVGDRYVMEL 313
Cdd:TIGR03990 232 DLGIAHDGDADRLVFIDEKGRFIGGDYTLALFAKYLLEHG--GGKVVTNVSSSRAVEDVAERHGGEVIRTKVGEVNVAEK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 314 LTKHNGILGGENSGHIICLDKTTTGDGIIAALQVLAEMQYSGQSLHELKSGMQKYPqiliNIKTakKVNLDHyDGIQQAV 393
Cdd:TIGR03990 310 MKEEGAVFGGEGNGGWIFPDHHYCRDGLMAAALFLELLAEEGKPLSELLAELPKYP----MSKE--KVELPD-EDKEEVM 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518703060 394 KAVENKL--------------GDKGRVLLRTSGTEPLIRVMVEGEQGDavnnYAQQLAEAVKSAI 444
Cdd:TIGR03990 383 EAVEEEFadaeidtidgvridFEDGWVLVRPSGTEPIVRIYAEAKTEE----RAEELLEEGRSLV 443
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
5-444 |
7.20e-102 |
|
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: 310.66 E-value: 7.20e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 5 YFGTDGIRGKVGEPpITADFLLKLGWATGRVFANERhdfVLVGKDTRISGYMFESALEAGLTAAGVDTRLLGPMPTPGIA 84
Cdd:cd03087 1 LFGTSGIRGVVGEE-LTPELALKVGKALGTYLGGGT---VVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDIGIVPTPALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 85 YLTRTlRAQAGIVISASHNPYYDNGVKFFSVQGTKLPDDIEKEIEHYMDSP-MTTVDSAHLGKAKRLEDAAGRYIEYCKA 163
Cdd:cd03087 77 YAVRK-LGDAGVMITASHNPPEYNGIKLVNPDGTEFSREQEEEIEEIIFSErFRRVAWDEVGSVRREDSAIDEYIEAILD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 164 SVPTRLDfDHMKIVVDCAHGATYHIAPHVFSEIGAEVISIGVQPNGL-------NINDNCgatkpEMLAATVLANHADLG 236
Cdd:cd03087 156 KVDIDGG-KGLKVVVDCGNGAGSLTTPYLLRELGCKVITLNANPDGFfpgrppePTPENL-----SELMELVRATGADLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 237 IALDGDGDRLIMVDHKGEIVDGDELIYIIAKSRLSSGqmAGPVVGTLMTNLGMEHALAQLGIPLLRAKVGDRYVMELLTK 316
Cdd:cd03087 230 IAHDGDADRAVFVDEKGRFIDGDKLLALLAKYLLEEG--GGKVVTPVDASMLVEDVVEEAGGEVIRTPVGDVHVAEEMIE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 317 HNGILGGENSGHIICLDKTTTGDGIIAALqVLAEMQYSGQSLHELKSGMQKYPQILINIKTAKkvnlDHYDGIQQAVKAV 396
Cdd:cd03087 308 NGAVFGGEPNGGWIFPDHQLCRDGIMTAA-LLLELLAEEKPLSELLDELPKYPLLREKVECPD----EKKEEVMEAVEEE 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518703060 397 ENKLGDK-------------GRVLLRTSGTEPLIRVMVEGEQGDAvnnyAQQLAEAVKSAI 444
Cdd:cd03087 383 LSDADEDvdtidgvrieyedGWVLIRPSGTEPKIRITAEAKTEER----AKELLEEGRSKV 439
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
5-440 |
5.86e-92 |
|
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: 282.32 E-value: 5.86e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 5 YFGTDGIRGKVGEPpITADFLLKLGWATGRVfanerhdfvlvgkdtrisgymfesaleagltaagvdtrllgpmptpgia 84
Cdd:cd03084 1 IFGTSGVRGVVGDD-ITPETAVALGQAIGST------------------------------------------------- 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 85 yltrtlraqAGIVISASHNPYYDNGVKFFSVQGTKLPDDIEKEIE-HYMDSPMTTVDSAHLGKAKRLEDAAGRYIEYCKA 163
Cdd:cd03084 31 ---------GGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEdLAEKEDEPSAVAYELGGSVKAVDILQRYFEALKK 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 164 SVPTR-LDFDHMKIVVDCAHGATYHIAPHVFSEIGAEVISIGVQPNGLNINDNCGATKPEMLA---ATVLANHADLGIAL 239
Cdd:cd03084 102 LFDVAaLSNKKFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCEPDGNFGNINPDPGSETNLKqllAVVKAEKADFGVAF 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 240 DGDGDRLIMVDHKGEIVDGDELIYIIAKSRLSSGQMAGPVVGTLMTNLGMEHALAQLGIPLLRAKVGDRYVMELLTKHNG 319
Cdd:cd03084 182 DGDADRLIVVDENGGFLDGDELLALLAVELFLTFNPRGGVVKTVVSSGALDKVAKKLGIKVIRTKTGFKWVGEAMQEGDV 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 320 ILGGENSGHIICLDKTTTGDGIIAALQVLAEMQYSGQSLHELKSGMQKYPQILINIktakkvnldhydgiqqavkavenk 399
Cdd:cd03084 262 VLGGEESGGVIFPEFHPGRDGISAALLLLEILANLGKSLSELFSELPRYYYIRLKV------------------------ 317
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 518703060 400 lgdKGRVLLRTSGTEPLIRVMVEGEQGDAVNNYAQQLAEAV 440
Cdd:cd03084 318 ---RGWVLVRASGTEPAIRIYAEADTQEDVEQIKKEARELV 355
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
11-440 |
2.25e-78 |
|
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: 250.12 E-value: 2.25e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 11 IRGKVGEPpITADFLLKLGWATGRVFANERHDFVLVGKDTRISGYMFESALEAGLTAAGVDTRLLGPMPTPGIAYLTRTL 90
Cdd:cd03089 7 IRGIAGEE-LTEEIAYAIGRAFGSWLLEKGAKKVVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPVLYFATFHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 91 RAQAGIVISASHNPYYDNGVKFFSVQGTKLPDDIeKEIEHYMDSPMTTVDSAHlGKAKRLeDAAGRYIEYCKASVptRLD 170
Cdd:cd03089 86 DADGGVMITASHNPPEYNGFKIVIGGGPLSGEDI-QALRERAEKGDFAAATGR-GSVEKV-DILPDYIDRLLSDI--KLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 171 FDHMKIVVDCAHGATYHIAPHVFSEIGAEVISIGVQPNGLNINDNCGATKPEMLAAT---VLANHADLGIALDGDGDRLI 247
Cdd:cd03089 161 KRPLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCEPDGTFPNHHPDPTDPENLEDLiaaVKENGADLGIAFDGDGDRLG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 248 MVDHKGEIVDGDELIYIIAKsRLSSGQMAGPVVGTLMTNLGMEHALAQLGIPLLRAKVGDRYVMELLTKHNGILGGENSG 327
Cdd:cd03089 241 VVDEKGEIIWGDRLLALFAR-DILKRNPGATIVYDVKCSRNLYDFIEEAGGKPIMWKTGHSFIKAKMKETGALLAGEMSG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 328 HIIC------LDktttgDGIIAALQVLAEMQYSGQSLHELKSGMQKY---PQILINIKTAKK---------------VNL 383
Cdd:cd03089 320 HIFFkdrwygFD-----DGIYAALRLLELLSKSGKTLSELLADLPKYfstPEIRIPVTEEDKfavierlkehfefpgAEI 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 518703060 384 DHYDGIQqavkaVEnklGDKGRVLLRTSGTEPLIRVMVEGEQGDAVNNYAQQLAEAV 440
Cdd:cd03089 395 IDIDGVR-----VD---FEDGWGLVRASNTEPVLVLRFEADTEEGLEEIKAELRKLL 443
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
6-437 |
1.80e-64 |
|
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: 214.34 E-value: 1.80e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 6 FGTDGIRGKVGEPpITADFLLKLGWATGRVFANE--RHDFVLVGKDTRISGYMFESALEAGLTAAGVDTRLL-GPMPTPG 82
Cdd:cd05800 3 FGTDGWRGIIAED-FTFENVRRVAQAIADYLKEEggGGRGVVVGYDTRFLSEEFARAVAEVLAANGIDVYLSdRPVPTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 83 IAYLTRTLRAQAGIVISASHNPYYDNGVKFFSVQGTKLPDDIEKEIEHYMDSPMTTVDSAHLGKAKRLEDAAGRYIEYCK 162
Cdd:cd05800 82 VSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARLASGEPPGLEARAEGLIETIDPKPDYLEALR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 163 asvpTRLDFD-----HMKIVVDCAHGATYHIAPHVFSEIGAEVISI---------GVQPNGL--NINDncgatkpemLAA 226
Cdd:cd05800 162 ----SLVDLEaireaGLKVVVDPMYGAGAGYLEELLRGAGVDVEEIraerdplfgGIPPEPIekNLGE---------LAE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 227 TVLANHADLGIALDGDGDRLIMVDHKGEIVDGDELIYIIAKSRLSSGQMAGPVVGTLMTNlGMEHALAQ-LGIPLLRAKV 305
Cdd:cd05800 229 AVKEGGADLGLATDGDADRIGAVDEKGNFLDPNQILALLLDYLLENKGLRGPVVKTVSTT-HLIDRIAEkHGLPVYETPV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 306 GDRYVMELLTKHNGILGGENSGHIICLDKTTTGDGIIAALQVLAEMQYSGQSLHELksgmqkYPQIL----------INI 375
Cdd:cd05800 308 GFKYIAEKMLEEDVLIGGEESGGLGIRGHIPERDGILAGLLLLEAVAKTGKPLSEL------VAELEeeygpsyydrIDL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 376 KTA---KKVNLDHYD------GIQQAVKAVENK------LGDKGRVLLRTSGTEPLIRVMVEG---EQGDAVNNYAQQLA 437
Cdd:cd05800 382 RLTpaqKEAILEKLKnepplsIAGGKVDEVNTIdgvklvLEDGSWLLIRPSGTEPLLRIYAEApspEKVEALLDAGKKLA 461
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
10-440 |
7.67e-52 |
|
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: 180.58 E-value: 7.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 10 GIRGKVGE---PPITADFLLKLGWATGRVFANERhdfVLVGKDTRISGYMFESALEAGLTAAGVDTRLLGPMPTPGIAYL 86
Cdd:cd05803 6 GIRGIVGEgltPEVITRYVAAFATWQPERTKGGK---IVVGRDGRPSGPMLEKIVIGALLACGCDVIDLGIAPTPTVQVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 87 TRTLRAQAGIVISASHNPYYDNGVKFFSVQGTKL-PDDIEKEIEHYMDSPMTTVDSAHLGKAKRLEDAAGRYIEYCKASV 165
Cdd:cd05803 83 VRQSQASGGIIITASHNPPQWNGLKFIGPDGEFLtPDEGEEVLSCAEAGSAQKAGYDQLGEVTFSEDAIAEHIDKVLALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 166 P---TRLDFDHMKIVVDCAHGATYHIAPHVFSEIGAEVISIGVQPNGLNindncgATKPE-------MLAATVLANHADL 235
Cdd:cd05803 163 DvdvIKIRERNFKVAVDSVNGAGGLLIPRLLEKLGCEVIVLNCEPTGLF------PHTPEplpenltQLCAAVKESGADV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 236 GIALDGDGDRLIMVDHKGEIVdGDELIYIIA-KSRLSSGQMAGPVVGTLMTNLGMEHALAQLGIPLLRAKVGDRYVMELL 314
Cdd:cd05803 237 GFAVDPDADRLALVDEDGRPI-GEEYTLALAvDYVLKYGGRKGPVVVNLSTSRALEDIARKHGVPVFRSAVGEANVVEKM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 315 TKHNGILGGENSGHIICLDKTTTGDGIIAALQVLAEMQYSGQSLHELKSGmqkYPQILI---NIKTAKKVNLDHYDGIQQ 391
Cdd:cd05803 316 KEVDAVIGGEGNGGVILPDVHYGRDSLVGIALVLQLLAASGKPLSEIVDE---LPQYYIsktKVTIAGEALERLLKKLEA 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 518703060 392 AVK-AVENKLG------DKGRVLLRTSGTEPLIRVMVEGEQGDAvnnyAQQLAEAV 440
Cdd:cd05803 393 YFKdAEASTLDglrldsEDSWVHVRPSNTEPIVRIIAEAPTQDE----AEALADRF 444
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
3-129 |
1.94e-50 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 167.40 E-value: 1.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 3 KKYFGTDGIRGKVGEPPITADFLLKLGWATGRVFANERHD-FVLVGKDTRISGYMFESALEAGLTAAGVDTRLLGPMPTP 81
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGELTPEFALKLGQAIASYLRAQGGGgKVVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 518703060 82 GIAYLTRTLRAQAGIVISASHNPYYDNGVKFFSVQGTKLPDDIEKEIE 129
Cdd:pfam02878 81 AVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIE 128
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
257-368 |
1.34e-40 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 140.66 E-value: 1.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 257 DGDELIYIIAKSRLSSGQMAG--PVVGTLMTNLGMEHALAQLGIPLLRAKVGDRYVMELLTKHNGILGGENSGHIICLDK 334
Cdd:pfam02880 1 DGDQILALLAKYLLEQGKLPPgaGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLDH 80
|
90 100 110
....*....|....*....|....*....|....*
gi 518703060 335 TTTGDGIIAALQVLAEMQYSGQSLHEL-KSGMQKY 368
Cdd:pfam02880 81 ATTKDGILAALLVLEILARTGKSLSELlEELPEKY 115
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
11-429 |
3.33e-36 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 138.19 E-value: 3.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 11 IRGKVGEPpITADFLLKLGWATGRVFANERHDFVLVGKDTRISGYMFESALEAGLTAAGVDTRLLGPMPTPGIAYLTRTL 90
Cdd:PRK09542 6 VRGVVGEQ-IDEDLVRDVGAAFARLMRAEGATTVVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIGLASTDQLYFASGLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 91 RAqAGIVISASHNPYYDNGVKFFSV------QGTKLP---DDIEKEIEHYMDSPMTTVDsahlgkakrlEDAAGRYIEYC 161
Cdd:PRK09542 85 DC-PGAMFTASHNPAAYNGIKLCRAgakpvgQDTGLAairDDLIAGVPAYDGPPGTVTE----------RDVLADYAAFL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 162 KASVPTRlDFDHMKIVVDCAHGATYHIAPHVFSEIGAEVISI-----GVQPNG-------LNINDncgatkpemLAATVL 229
Cdd:PRK09542 154 RSLVDLS-GIRPLKVAVDAGNGMGGHTVPAVLGGLPITLLPLyfeldGTFPNHeanpldpANLVD---------LQAFVR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 230 ANHADLGIALDGDGDRLIMVDHKGEIVDGDELIYIIAKSRLSSGqMAGPVVGTLMTNLGMEHALAQLGIPLLRAKVGDRY 309
Cdd:PRK09542 224 ETGADIGLAFDGDADRCFVVDERGQPVSPSAVTALVAARELARE-PGATIIHNLITSRAVPELVAERGGTPVRTRVGHSF 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 310 VMELLTKHNGILGGENSGHIICLDKTTTGDGIIAALQVLAEMQYSGQSLHELKSGMQKY-------------PQILINIK 376
Cdd:PRK09542 303 IKALMAETGAIFGGEHSAHYYFRDFWGADSGMLAALHVLAALGEQDRPLSELMADYQRYaasgeinstvadaPARMEAVL 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 518703060 377 TA---KKVNLDHYDGIqqavkAVEnkLGDKGRVLLRTSGTEPLIRVMVEGEQGDAV 429
Cdd:PRK09542 383 KAfadRIVSVDHLDGV-----TVD--LGDGSWFNLRASNTEPLLRLNVEARTEEEV 431
|
|
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
6-438 |
3.39e-36 |
|
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: 138.15 E-value: 3.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 6 FGTDGIRGKV-GEppITADFLLKLGWATGRVFanERHDFVLVGKDTRISGYMFESALEAGLTAAGVDTRLLGPMPTPGIA 84
Cdd:cd05805 2 FGGRGVSGLInVD--ITPEFATRLGAAYGSTL--PPGSTVTVSRDASRASRMLKRALISGLLSTGVNVRDLGALPLPVAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 85 YLTRTLRAQAGIVISAShnpYYDNG---VKFFSVQGTKLPDDIEKEIEH-YMDSPMTTVDSAHLGKAKRLEDAAGRYIE- 159
Cdd:cd05805 78 YAIRFLGASGGIHVRTS---PDDPDkveIEFFDSRGLNISRAMERKIENaFFREDFRRAHVDEIGDITEPPDFVEYYIRg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 160 YCKASVPTRLDFDHMKIVVDCAHGATYHIAPHVFSEIGAEVISigvqpngLNINDNCGATKP--------EMLAATVLAN 231
Cdd:cd05805 155 LLRALDTSGLKKSGLKVVIDYAYGVAGIVLPGLLSRLGCDVVI-------LNARLDEDAPRTdterqrslDRLGRIVKAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 232 HADLGIALDGDGDRLIMVDHKGEIVDGDELIYIIAKSRLSSGQmAGPVVGTLMTNLGMEHALAQLGIPLLRAKVGDRYVM 311
Cdd:cd05805 228 GADFGVIIDPNGERLILVDEAGRVISDDLLTALVSLLVLKSEP-GGTVVVPVTAPSVIEQLAERYGGRVIRTKTSPQALM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 312 ELLTKhNGILGGENSGHIICLDKTTTGDGIIAALQVLAEMQYSGQSLHELKSGMqkyPQILIN----------------- 374
Cdd:cd05805 307 EAALE-NVVLAGDGDGGFIFPEFHPGFDAIAALVKILEMLARTNISLSQIVDEL---PRFYVLhkevpcpweakgrvmrr 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518703060 375 -IKTAKKVNLDHYDGiqqaVKAVEnklgDKGRVLLRTSGTEPLIRVMVEGEQGDavnnYAQQLAE 438
Cdd:cd05805 383 lIEEAPDKSIELIDG----VKIYE----DDGWVLVLPDADEPLCHIYAEGSDQE----RAEELTE 435
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
6-444 |
4.51e-33 |
|
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: 130.32 E-value: 4.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 6 FGTDGIRGKVGEPP-------IT------ADFLLKLGWAtgrvfANERHdfVLVGKDTRISGYMFesALEAG--LTAAGV 70
Cdd:cd05799 4 FGTAGLRGKMGAGTnrmndytVRqatqglANYLKKKGPD-----AKNRG--VVIGYDSRHNSREF--AELTAavLAANGI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 71 DTRLL-GPMPTPGIAYLTRTLRAQAGIVISASHNPYYDNGVKFFSVQGTKLPDDIEKEIEHYMDS--PMTTVDSAHLGKA 147
Cdd:cd05799 75 KVYLFdDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAvlEPLDIKFEEALDS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 148 KRLEDAA----GRYIEYCKASVPTRLDFDH--MKIVVDCAHGATYHIAPHVFSEIGAE-VISIGVQ------------PN 208
Cdd:cd05799 155 GLIKYIGeeidDAYLEAVKKLLVNPELNEGkdLKIVYTPLHGVGGKFVPRALKEAGFTnVIVVEEQaepdpdfptvkfPN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 209 glnindncgatkPEMLAATVLA------NHADLGIALDGDGDRL-IMV-DHKGE--IVDGDE----LIYIIAKSRLSSGQ 274
Cdd:cd05799 235 ------------PEEPGALDLAielakkVGADLILATDPDADRLgVAVkDKDGEwrLLTGNEigalLADYLLEQRKEKGK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 275 MAGP--VVGTLMTNlgmehalaqlgiPLLR--AKVGDRYVMELLT---------------KHNGILGGENS-GHII---C 331
Cdd:cd05799 303 LPKNpvIVKTIVSS------------ELLRkiAKKYGVKVEETLTgfkwignkieelesgGKKFLFGFEESiGYLVgpfV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 332 LDKtttgDGIIAALqVLAEMQY----SGQSLHE-LKSGMQKYPQILINIKTakkVNLDHYDGIQQAVKAVEN-------- 398
Cdd:cd05799 371 RDK----DGISAAA-LLAEMAAylkaQGKTLLDrLDELYEKYGYYKEKTIS---ITFEGKEGPEKIKAIMDRlrnnpnvl 442
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 518703060 399 --KLGDKGRVLLRTSGTEPLIRVMVEgeqgdAVNNYAQQLAEAVKSAI 444
Cdd:cd05799 443 tfYLEDGSRVTVRPSGTEPKIKFYIE-----VVGKKTLEEAEKKLDAL 485
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
44-442 |
5.34e-30 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 122.47 E-value: 5.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 44 VLVGKDTRISGYMFESALEAGLTAAGVDTRLLGPMPTPGIAYLTRTLRAQ--AGIVISASHNPYYDNGVKFFSVQGTKLP 121
Cdd:PLN02371 118 VSVGRDPRISGPRLADAVFAGLASAGLDVVDMGLATTPAMFMSTLTEREDydAPIMITASHLPYNRNGLKFFTKDGGLGK 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 122 DDIEKEIE------------------HYMDSPMTTVD-----SAHLGKAKRleDAAGRYIEYCKasvPTRldfdHMKIVV 178
Cdd:PLN02371 198 PDIKDILEraariykewsdegllkssSGASSVVCRVDfmstyAKHLRDAIK--EGVGHPTNYET---PLE----GFKIVV 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 179 DCAHGATYHIAPHVFSEIGAEVI-SIGVQPNGLNINDNCGATKPEMLAAT---VLANHADLGIALDGDGDRLIMVDHKGE 254
Cdd:PLN02371 269 DAGNGAGGFFAEKVLEPLGADTSgSLFLEPDGMFPNHIPNPEDKAAMSATtqaVLANKADLGIIFDTDVDRSAVVDSSGR 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 255 IVDGDELIYIIAK--SRLSSGQMagpVVGTLMTNLGMEHALAQLGIPLLRAKVGDRYVMELLTKHN--GI---LGGENSG 327
Cdd:PLN02371 349 EINRNRLIALMSAivLEEHPGTT---IVTDSVTSDGLTTFIEKKGGKHHRFKRGYKNVIDKGVRLNsdGEethLMIETSG 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 328 HII-----CLDktttgDGIIAALQVLAEM-----QYSGQSLHELKSGMQKYPQ-------ILINIKTAKKVNLDHYDGIQ 390
Cdd:PLN02371 426 HGAlkenhFLD-----DGAYLAVKIIIELvrmraAGAGGGLGDLIEDLEEPLEavelrlkILDEGKDFKAYGEEVLEHLR 500
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518703060 391 QAVKAVEN----------------KLGDKGRVLLRTSGTEPLIRVMVEGEQGDAVNNYAQQLAEAVKS 442
Cdd:PLN02371 501 NSIESDGKlegapvnyegvrvsdeGEGFGGWFLLRQSLHDPVIPLNIESSSPGGAQKMALVVLTWLKE 568
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
11-427 |
6.20e-30 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 120.82 E-value: 6.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 11 IRGKVGEPpITADFLLKLGWATGRVFaneRHDFVLVGKDTRISGYMFESALEAGLTAAGVDTRLLGPMPTPGIAYLTRTL 90
Cdd:PRK15414 12 IRGKLGEE-LNEDIAWRIGRAYGEFL---KPKTIVLGGDVRLTSETLKLALAKGLQDAGVDVLDIGMSGTEEIYFATFHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 91 RAQAGIVISASHNPYYDNGVKFFS-----VQGTKLPDDIEKEIEhYMDSPmtTVDSAHLGKAKR--LEDAagrYIEYCKA 163
Cdd:PRK15414 88 GVDGGIEVTASHNPMDYNGMKLVRegarpISGDTGLRDVQRLAE-ANDFP--PVDETKRGRYQQinLRDA---YVDHLFG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 164 SVPTRlDFDHMKIVVDCAHGATYHIAPHV---FSEIGA--EVISIGVQPNGLNINDNCGATKPEMLAAT---VLANHADL 235
Cdd:PRK15414 162 YINVK-NLTPLKLVINSGNGAAGPVVDAIearFKALGApvELIKVHNTPDGNFPNGIPNPLLPECRDDTrnaVIKHGADM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 236 GIALDGDGDRLIMVDHKGEIVDGDELIYIIAKSRLSSGQMAGPVVGTLMTNLGMEHALAQLGIPLLrAKVGDRYVMELLT 315
Cdd:PRK15414 241 GIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPGAKIIHDPRLSWNTVDVVTAAGGTPVM-SKTGHAFIKERMR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 316 KHNGILGGENSGHIICLDKTTTGDGIIAALQVLAEMQYSGQSLHEL-KSGMQKYPQI-LINIKTAKKV------------ 381
Cdd:PRK15414 320 KEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELVCLKGKTLGELvRDRMAAFPASgEINSKLAQPVeainrveqhfsr 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 518703060 382 ---NLDHYDGIQQAVKavenklgdKGRVLLRTSGTEPLIRVMVEgEQGD 427
Cdd:PRK15414 400 ealAVDRTDGISMTFA--------DWRFNLRSSNTEPVVRLNVE-SRGD 439
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
157-253 |
4.91e-17 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 76.18 E-value: 4.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 157 YIEYCKASVPTRLDF-DHMKIVVDCAHGATYHIAPHVFSEIGAEVISIGVQPNGLNINdncGATKPE------MLAATVL 229
Cdd:pfam02879 2 YIDHLLELVDSEALKkRGLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDPDFPT---RAPNPEepealaLLIELVK 78
|
90 100
....*....|....*....|....
gi 518703060 230 ANHADLGIALDGDGDRLIMVDHKG 253
Cdd:pfam02879 79 SVGADLGIATDGDADRLGVVDERG 102
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
6-361 |
4.72e-16 |
|
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: 79.94 E-value: 4.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 6 FGTDGIRGKVGE--PPITADFLLKLGWATGRVFANerhDFVLVGKDTRISGYMFESALEAGLTAAGVDTRLLGPMPTPGI 83
Cdd:cd03088 2 FGTSGLRGLVTDltDEVCYAYTRAFLQHLESKFPG---DTVAVGRDLRPSSPRIAAACAAALRDAGFRVVDCGAVPTPAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 84 AYLTRTlRAQAGIVISASHNPYYDNGVKFFSVQGTKLPDDiEKEIEHYMDSPMTTVDSAHLGKAKRLEDAAGRYIE-YCK 162
Cdd:cd03088 79 ALYAMK-RGAPAIMVTGSHIPADRNGLKFYRPDGEITKAD-EAAILAALVELPEALFDPAGALLPPDTDAADAYIArYTD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 163 ASVPTRLdfDHMKIVVDCAHGATYHIAPHVFSEIGAEVISIG------------VQPnglnindncgATKpEMLAATVLA 230
Cdd:cd03088 157 FFGAGAL--KGLRIGVYQHSSVGRDLLVRILEALGAEVVPLGrsdtfipvdteaVRP----------EDR-ALAAAWAAE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 231 NHADLGIALDGDGDRLIMVDHKGEIVDGDELIYIIAKSrLSSGQMAGPVVgtlmTNLGMEhaLAQLGIPLLRAKVGDRYV 310
Cdd:cd03088 224 HGLDAIVSTDGDGDRPLVADETGEWLRGDILGLLTARF-LGADTVVTPVS----SNSAIE--LSGFFKRVVRTRIGSPYV 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518703060 311 ---MELLTKHNG--ILGGE-NSGHI----ICLDKTT-----TGDGIIAALQVLAEMQYSGQSLHEL 361
Cdd:cd03088 297 iaaMAEAAAAGAgrVVGYEaNGGFLlgsdIERNGRTlkalpTRDAVLPILAVLAAAKEAGIPLSEL 362
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
372-441 |
1.42e-14 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 68.45 E-value: 1.42e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518703060 372 LINIKTAKKVNLDHYDGIQQAVKAVENKLGDKGRVL-LRTSGTEPLIRVMVEGEQGDAVNNYAQQLAEAVK 441
Cdd:pfam00408 1 LINVRVAEKKKLAALAAILKVFADAEKILGEDGRRLdVRPSGTEPVLRVMVEGDSDEELARLADEIADLLE 71
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
44-442 |
4.15e-14 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 74.30 E-value: 4.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 44 VLVGKDTRISGYMFESALEAGLTAAGVDT-RLLGPMPTPGIAYLTRtlRAQAGivisaSHNPYYDNGVKFFSvqgtklpd 122
Cdd:PTZ00302 155 VHVGRDTRPSSPELVSALLRGLKLLIGSNvRNFGIVTTPQLHFLVA--FANGL-----GVDVVESSDELYYA-------- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 123 diekEIEHYMDSPMTTVDSAHLGkakrledaagryieyckasvpTRLDFDHMKIVVDCAHG-ATYHIAP--HVFSEIGAE 199
Cdd:PTZ00302 220 ----YLLAAFKELYRTLQEGGPV---------------------DLTQNNSKILVVDCANGvGGYKIKRffEALKQLGIE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 200 VI--SIGVQPNGLnINDNCGA--TKPEMLAATVLANHADLGI----ALDGDGDRLI--MVDHKGE----IVDGDELIYII 265
Cdd:PTZ00302 275 IIpiNINCDEEEL-LNDKCGAdyVQKTRKPPRAMKEWPGDEEtrvaSFDGDADRLVyfFPDKDGDdkwvLLDGDRIAILY 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 266 AKsrlssgqmagpVVGTLMTNLGMEHAL-------------------AQLG-IPLLRAKVGDRYVMELLTKHN-GILgGE 324
Cdd:PTZ00302 354 AM-----------LIKKLLGKIQLKKKLdigvvqtayangastnylnELLGrLRVYCAPTGVKNLHPKAHKYDiGIY-FE 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 325 NSGH--II----CLDK--------------------------TTTGDGIIAALQVLAEMQYSGQSLHELKSGMQKYPQIL 372
Cdd:PTZ00302 422 ANGHgtVLfnekALAEwakflakqnalnsacrqlekflrlfnQTIGDAISDLLAVELALAFLGLSFQDWLNLYTDLPSRQ 501
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518703060 373 INIKTAKKVNLDHYD---------GIQQAVKAVENKLGDKGRVLLRTSGTEPLIRVMVEGEQGDAVNNYAQQLAEAVKS 442
Cdd:PTZ00302 502 DKVTVKDRTLITNTEdetrllepkGLQDKIDAIVSKYDNAARAFIRPSGTEPVVRVYAEAPTLEQADELANEVKGLVLR 580
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
6-266 |
6.11e-14 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 73.95 E-value: 6.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 6 FGTDGIRGKVGeppitADF-----LLKLGWATG------RVFANERHDF-VLVGKDTRISGYMFESALEAGLTAAGVDTR 73
Cdd:PTZ00150 47 FGTAGLRGKMG-----AGFncmndLTVQQTAQGlcayviETFGQALKSRgVVIGYDGRYHSRRFAEITASVFLSKGFKVY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 74 LLGPM-PTPGIAYLTRTLRAQAGIVISASHNPYYDNGVKFFSVQGTKLPDDIEKEIEHYMDSPMTTVDSAHLG-KAKRLE 151
Cdd:PTZ00150 122 LFGQTvPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVYWSNGAQIIPPHDKNISAKILSNLEPWSSSWEYlTETLVE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 152 DA-AGRYIEYCKA----SVPTRLDFDHMKIVVDCAHGATYHIAPHVFSEIG-AEVISIGVQ--PNG-------LNINDNC 216
Cdd:PTZ00150 202 DPlAEVSDAYFATlkseYNPACCDRSKVKIVYTAMHGVGTRFVQKALHTVGlPNLLSVAQQaePDPefptvtfPNPEEGK 281
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 518703060 217 GATKPEMlaATVLANHADLGIALDGDGDRLIMV---DHKGEIVDGDELIYIIA 266
Cdd:PTZ00150 282 GALKLSM--ETAEAHGSTVVLANDPDADRLAVAeklNNGWKIFTGNELGALLA 332
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
6-361 |
3.52e-13 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 71.32 E-value: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 6 FGTDGIRGKVGEPPITADFLLKLGWATGRVFANERHDFVL-VGKDTR-ISGYMFESALEAgLTAAGVDTRL---LGPMPT 80
Cdd:PRK07564 40 FGTSGHRGSSLQPSFNENHILAIFQAICEYRGKQGITGPLfVGGDTHaLSEPAIQSALEV-LAANGVGVVIvgrGGYTPT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 81 PGI-----AYLTRTLRAQAGIVISASHNPYYDNGVKFFSVQG----TKLPDDIE---KEIEHYMDSPMTTVDSAHLGKAK 148
Cdd:PRK07564 119 PAVshailKYNGRGGGLADGIVITPSHNPPEDGGIKYNPPNGgpadTDVTDAIEaraNELLAYGLKGVKRIPLDRALASM 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 149 RLE--DAAGRYIEyckaSVPTRLDFD-----HMKIVVDCAHGATYHIAPHVFSEIG--AEVISIGVQP--NGLNIND--- 214
Cdd:PRK07564 199 TVEviDPVADYVE----DLENVFDFDairkaGLRLGVDPLGGATGPYWKAIAERYGldLTVVNAPVDPtfNFMPLDDdgk 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 215 ---NCgaTKPEMLAATV-LANHADLGIALDGDGDR---------------L-IMVDHKGEIVDGdeliY----IIAKSRL 270
Cdd:PRK07564 275 irmDC--SSPYAMAGLLaLKDAFDLAFANDPDGDRhgivtpgglmnpnhyLaVAIAYLFHHRPG----WragaGVGKTLV 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 271 SSgQMAGPVVgtlmtnlgmehalAQLGIPLLRAKVGDRYVMELLTKHNGILGGENSGHIICLDK-----TTTGDGIIAAL 345
Cdd:PRK07564 349 SS-AMIDRVA-------------AKLGRKLYEVPVGFKWFVNGLDDGSLGFGGEESAGASFLRRdgsvwTTDKDGLIAVL 414
|
410
....*....|....*....
gi 518703060 346 ---QVLAEmqySGQSLHEL 361
Cdd:PRK07564 415 laaEILAV---TGKSPSEI 430
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
44-440 |
1.48e-12 |
|
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: 69.16 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 44 VLVGKDTRISGYMFESALEAGLTAAGVDTRLLGPMPTPGIAYLTRTLRAQaGIVISASHNPYYDNGVKFFSvQGTKLPDD 123
Cdd:cd03086 105 VFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYLVRAANTE-GAYGEPTEEGYYEKLSKAFN-ELYNLLQD 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 124 IEKEIEhymdspmttvdsahlgkakrledaagryieyckasvptrldfdhmKIVVDCAHG-ATYHI---APHVFSEIGAE 199
Cdd:cd03086 183 GGDEPE---------------------------------------------KLVVDCANGvGALKLkelLKRLKKGLSVK 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 200 VISIGVQPNGLnINDNCGA------TKP----EMLAATVLAnhadlgIALDGDGDRLI--MVDHKG--EIVDGDELIYII 265
Cdd:cd03086 218 IINDGEEGPEL-LNDGCGAdyvktkQKPprgfELKPPGVRC------CSFDGDADRLVyfYPDSSNkfHLLDGDKIATLF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 266 A---KSRLSSGQMAGP----VVGTLMTN----------LGMEHALAQLGIPLLRAK-----VG--------------DRY 309
Cdd:cd03086 291 AkfiKELLKKAGEELKltigVVQTAYANgastkyledvLKVPVVCTPTGVKHLHHAaeefdIGvyfeanghgtvlfsESA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 310 VMELltKHNGILGGENSGHIICLDK------TTTGDGIIAALQVLAEMQYSGQSLHELKSGMQKYPQILINIKTAKK--- 380
Cdd:cd03086 371 LAKI--EENSSLSDEQEKAAKTLLAfsrlinQTVGDAISDMLAVELILAALGWSPQDWDNLYTDLPNRQLKVKVPDRsvi 448
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518703060 381 VNLDHYD------GIQQAVKAVENKLgDKGRVLLRTSGTEPLIRVMVEGEQGDAVNNYAQQLAEAV 440
Cdd:cd03086 449 KTTDAERrlvepkGLQDKIDAIVAKY-NNGRAFVRPSGTEDVVRVYAEAATQEEADELANEVAELV 513
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
7-245 |
1.48e-09 |
|
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate (G-1-P) and glucose-6-phosphate (G-6-P) via a glucose 1,6-diphosphate intermediate, an important metabolic step in prokaryotes and eukaryotes. In one direction, G-1-P produced from sucrose catabolism is converted to G-6-P, the first intermediate in glycolysis. In the other direction, conversion of G-6-P to G-1-P generates a substrate for synthesis of UDP-glucose which is required for synthesis of a variety of cellular constituents including cell wall polymers and glycoproteins. The PGM1 family also includes a non-enzymatic PGM-related protein (PGM-RP) thought to play a structural role in eukaryotes, as well as pp63/parafusin, a phosphoglycoprotein that plays an important role in calcium-regulated exocytosis in ciliated protozoans. PGM1 belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100087 [Multi-domain] Cd Length: 548 Bit Score: 59.93 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 7 GTDGIRGKVGE---PPITADFLLKLGWATGRVFANErhDFVLVGKDTRIsgYMFESALEAGLTAA--GVdTRLL----GP 77
Cdd:cd03085 14 GTSGLRKKVKVfqqPNYLENFVQSIFNALPPEKLKG--ATLVVGGDGRY--YNKEAIQIIIKIAAanGV-GKVVvgqnGL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 78 MPTPGIAYLTRTLRAQAGIVISASHNP---YYDNGVKFFSVQGTKLPDDI-------EKEIEHYMDSPMTTVDSAHLGKA 147
Cdd:cd03085 89 LSTPAVSAVIRKRKATGGIILTASHNPggpEGDFGIKYNTSNGGPAPESVtdkiyeiTKKITEYKIADDPDVDLSKIGVT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 148 K--------RLEDAAGRYIEYCKasvpTRLDFD---------HMKIVVDCAHGATYHIAPHVF-SEIGAeviSIGVQPNG 209
Cdd:cd03085 169 KfggkpftvEVIDSVEDYVELMK----EIFDFDaikkllsrkGFKVRFDAMHGVTGPYAKKIFvEELGA---PESSVVNC 241
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 518703060 210 LNINDNCGA------TKPEMLAATVLANHADLGIALDGDGDR 245
Cdd:cd03085 242 TPLPDFGGGhpdpnlTYAKDLVELMKSGEPDFGAASDGDGDR 283
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
46-351 |
1.16e-08 |
|
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: 57.26 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 46 VGKDTR-ISGYMFESALEAgLTAAGVDTRL---LGPMPTPGI--AYLT----RTLRAQAGIVISASHNPYYDNGVKFFSV 115
Cdd:cd05801 64 LGKDTHaLSEPAFISALEV-LAANGVEVIIqqnDGYTPTPVIshAILTynrgRTEGLADGIVITPSHNPPEDGGFKYNPP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 116 QG----TKLPDDIEKEIEHYMDSPMTTVDSAHLGKAKRLE-----DAAGRYIeyckASVPTRLDFD-----HMKIVVDCA 181
Cdd:cd05801 143 HGgpadTDITRWIEKRANALLANGLKGVKRIPLEAALASGythrhDFVTPYV----ADLGNVIDMDairksGLRLGVDPL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 182 HGATYH----IAPHVfsEIGAEVISIGVQP---------NGLnINDNCgaTKPEMLAATV-LANHADLGIALDGDGDRLI 247
Cdd:cd05801 219 GGASVPywqpIAEKY--GLNLTVVNPKVDPtfrfmtldhDGK-IRMDC--SSPYAMAGLLkLKDKFDLAFANDPDADRHG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 248 MVDHKGEIVDGDEliYIIA------KSRLSSGQMAGpvVG-TLMTNLGMEHALAQLGIPLLRAKVGDRYVMELLtkHNGI 320
Cdd:cd05801 294 IVTPSAGLMNPNH--YLSVaidylfTHRPLWNKSAG--VGkTLVSSSMIDRVAAALGRKLYEVPVGFKWFVDGL--LDGS 367
|
330 340 350
....*....|....*....|....*....|....*...
gi 518703060 321 LG--GENSGHIICLDK-----TTTGDGIIAALqVLAEM 351
Cdd:cd05801 368 LGfgGEESAGASFLRRdgtvwTTDKDGIIMCL-LAAEI 404
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
44-445 |
1.95e-08 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 56.57 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 44 VLVGKDTRISGYMFESALEAGLTAAGVDTRLLGPMPTPGIAYLTRtlraqagivisASHNPyydngvkffsvqgtklpdd 123
Cdd:PLN02895 130 VLLGRDTRPSGPALLAAALKGVRAIGARAVDMGILTTPQLHWMVR-----------AANKG------------------- 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 124 iekeiehymdspmttVDSAHLGKAKRLEDAAGRYIEYCKASVPTRLDFDhmKIVVDCAHGATY----HIAPhVFSEIGAE 199
Cdd:PLN02895 180 ---------------MKATESDYFEQLSSSFRALLDLIPNGSGDDRADD--KLVVDGANGVGAekleTLKK-ALGGLDLE 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 200 VISIGVQPNGLnINDNCGA--TKPEMLAATVLANhADLGI---ALDGDGDRLI---MVDHKGEI--VDGDELIYIIA--- 266
Cdd:PLN02895 242 VRNSGKEGEGV-LNEGVGAdfVQKEKVPPTGFAS-KDVGLrcaSLDGDADRLVyfyVSSAGSKIdlLDGDKIASLFAlfi 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 267 KSRLSSGQMAGP-----------VVGTLMTN----------LGMEHALAQLGIPLLRAKV-------------------G 306
Cdd:PLN02895 320 KEQLRILNGNGNekpeellvrlgVVQTAYANgastaylkqvLGLEVVCTPTGVKYLHEAAaefdigvyfeanghgtvlfS 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 307 DRYVMELLTKHNGILGG--ENSGHIICLDKTTT--------GDGIIAALQVLAEMQYSGQSLHELKSGMQKYPQILINIK 376
Cdd:PLN02895 400 ERFLDWLEAAAAELSSKakGSEAHKAARRLLAVsrlinqavGDALSGLLLVEAILQYRGWSLAEWNALYQDLPSRQLKVK 479
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518703060 377 TAKKVNLDHYD---------GIQQAV-KAVENKlgDKGRVLLRTSGTEPLIRVMVEGEQGDAVNNYAQQLAEAVKSAIG 445
Cdd:PLN02895 480 VADRTAITTTDaetvvvrpaGLQDAIdAEVAKY--PRGRAFVRPSGTEDVVRVYAEASTQEAADSLAREVARLVYDLLG 556
|
|
| PLN02307 |
PLN02307 |
phosphoglucomutase |
76-245 |
7.20e-06 |
|
phosphoglucomutase
Pssm-ID: 177942 [Multi-domain] Cd Length: 579 Bit Score: 48.11 E-value: 7.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 76 GPMPTPGIAYLTR---TLRAQAGIVISASHN---PYYDNGVKFFSVQGTKLPDDIEKEI--------EHYMDSPMTTVDS 141
Cdd:PLN02307 99 GLLSTPAVSAVIRerdGSKANGGFILTASHNpggPEEDFGIKYNYESGQPAPESITDKIygntltikEYKMAEDIPDVDL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518703060 142 AHLGKAK---------RLEDAAGRYIEYCKaSVptrLDFDHMK---------IVVDCAHGATYHIAPHVF-SEIGAEVIS 202
Cdd:PLN02307 179 SAVGVTKfggpedfdvEVIDPVEDYVKLMK-SI---FDFELIKkllsrpdftFCFDAMHGVTGAYAKRIFvEELGAPESS 254
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 518703060 203 IgvqPNGLNIND-NCGATKPEM-----------LAATVLANHA-DLGIALDGDGDR 245
Cdd:PLN02307 255 L---LNCVPKEDfGGGHPDPNLtyakelvkrmgLGKTSYGDEPpEFGAASDGDGDR 307
|
|
| |
