|
Name |
Accession |
Description |
Interval |
E-value |
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
6-560 |
0e+00 |
|
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: 1031.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 6 EIVATKPYEGQKPGTSGLRKKVKVFTQPNYTENFVQAILEANGAA-LAGSTLVVGGDGRFYCKEAAELIVRLSAANGVSK 84
Cdd:cd03085 1 QTVPTKPYEGQKPGTSGLRKKVKVFQQPNYLENFVQSIFNALPPEkLKGATLVVGGDGRYYNKEAIQIIIKIAAANGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 85 LLVGQNGILSTPAVSSLIRHNKALGGIVLTASHNPGGPENDFGIKFNCENGGPAPDAFTNHIYKITTEIKEYKLVRNLQI 164
Cdd:cd03085 81 VVVGQNGLLSTPAVSAVIRKRKATGGIILTASHNPGGPEGDFGIKYNTSNGGPAPESVTDKIYEITKKITEYKIADDPDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 165 DISKVGVTSFDiaGKPFTVEVIDSVANYVRHMEEIFDFAKLKDFVSGKatgkPLKMRIDAMNGVTGSYVREIFLNRLGAT 244
Cdd:cd03085 161 DLSKIGVTKFG--GKPFTVEVIDSVEDYVELMKEIFDFDAIKKLLSRK----GFKVRFDAMHGVTGPYAKKIFVEELGAP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 245 ESSVVHTTPLPDFGGLHPDPNLTYAKDLVDTVAQGDYDIGAAFDGDGDRNMIIGsKAFFVTPSDSLAVIAHYLEAIPYFQ 324
Cdd:cd03085 235 ESSVVNCTPLPDFGGGHPDPNLTYAKDLVELMKSGEPDFGAASDGDGDRNMILG-KGFFVTPSDSVAVIAANAKLIPYFY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 325 KNGVQGFARSMPTASAVDLVGRKLGKEVFEVPTGWKYFGNLMDAGRLCLCGEESFGTGSNHIREKDGIWAVLAWISVMQH 404
Cdd:cd03085 314 KGGLKGVARSMPTSGALDRVAKKLGIPLFETPTGWKFFGNLMDAGKLSLCGEESFGTGSDHIREKDGLWAVLAWLSILAH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 405 TGKGIEDILKQHWSVYGRNYFTRYDYEECASDPCNEMVATMEKTITAPEFVGKsysSGGKTYKVKEADNFSYTDPVDKSV 484
Cdd:cd03085 394 RNVSVEDIVKEHWQKYGRNFYTRYDYEEVDSEAANKMMDHLRALVSDLPGVGK---SGDKGYKVAKADDFSYTDPVDGSV 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12006791 485 ATKQGLRIVFEDGSRIVVRLSGTGSSGATVRLYIDSYEKEN--VLGQASVMLKPLIDIALEISQLPKFTGRNAPTVIT 560
Cdd:cd03085 471 SKKQGLRIIFEDGSRIIFRLSGTGSSGATIRLYIESYEKDPskYGLDAQVALKPLIEIALKLSKLKEFTGREEPTVIT 548
|
|
| PLN02307 |
PLN02307 |
phosphoglucomutase |
1-560 |
0e+00 |
|
phosphoglucomutase
Pssm-ID: 177942 [Multi-domain] Cd Length: 579 Bit Score: 820.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 1 MSLTVEIVATKPYEGQKPGTSGLRKKVKVFTQPNYTENFVQAILEANGAA-LAGSTLVVGGDGRFYCKEAAELIVRLSAA 79
Cdd:PLN02307 8 ASFKVSSVPTKPIEGQKPGTSGLRKKVKVFMQENYLANFVQALFNALPAEkVKGATLVLGGDGRYFNKEAIQIIIKIAAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 80 NGVSKLLVGQNGILSTPAVSSLIR---HNKALGGIVLTASHNPGGPENDFGIKFNCENGGPAPDAFTNHIYKITTEIKEY 156
Cdd:PLN02307 88 NGVRRVWVGQNGLLSTPAVSAVIRerdGSKANGGFILTASHNPGGPEEDFGIKYNYESGQPAPESITDKIYGNTLTIKEY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 157 KLVRNL-QIDISKVGVTSFDiAGKPFTVEVIDSVANYVRHMEEIFDFAKLKDFVSgkatgKP-LKMRIDAMNGVTGSYVR 234
Cdd:PLN02307 168 KMAEDIpDVDLSAVGVTKFG-GPEDFDVEVIDPVEDYVKLMKSIFDFELIKKLLS-----RPdFTFCFDAMHGVTGAYAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 235 EIFLNRLGATESSVVHTTPLPDFGGLHPDPNLTYAKDLVDTVAQGDY-------DIGAAFDGDGDRNMIIGSKaFFVTPS 307
Cdd:PLN02307 242 RIFVEELGAPESSLLNCVPKEDFGGGHPDPNLTYAKELVKRMGLGKTsygdeppEFGAASDGDGDRNMILGKR-FFVTPS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 308 DSLAVI-AHYLEAIPYFqKNGVQGFARSMPTASAVDLVGRKLGKEVFEVPTGWKYFGNLMDAGRLCLCGEESFGTGSNHI 386
Cdd:PLN02307 321 DSVAIIaANAQEAIPYF-SGGLKGVARSMPTSAALDVVAKKLNLPFFEVPTGWKFFGNLMDAGKLSICGEESFGTGSDHI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 387 REKDGIWAVLAWISVMQHTGK---------GIEDILKQHWSVYGRNYFTRYDYEECASDPCNEMVATMEKTITApefVGK 457
Cdd:PLN02307 400 REKDGIWAVLAWLSILAHKNKdvlpggklvTVEDIVREHWATYGRNFYSRYDYENVDSEAANKMMDHLRDLVNK---SKK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 458 SYSSGgkTYKVKEADNFSYTDPVDKSVATKQGLRIVFEDGSRIVVRLSGTGSSGATVRLYIDSYEKE--NVLGQASVMLK 535
Cdd:PLN02307 477 GIKYG--VYTLAFADDFEYTDPVDGSVSSKQGIRFLFTDGSRIIFRLSGTGSAGATIRLYIEQYEKDpsKHGRDAQEALK 554
|
570 580
....*....|....*....|....*
gi 12006791 536 PLIDIALEISQLPKFTGRNAPTVIT 560
Cdd:PLN02307 555 PLIDVALKLSKLKEFTGRSKPTVIT 579
|
|
| Pgm |
COG0033 |
Phosphoglucomutase/phosphomannomutase [Carbohydrate transport and metabolism]; |
4-544 |
0e+00 |
|
Phosphoglucomutase/phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 439803 Cd Length: 544 Bit Score: 581.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 4 TVEIVATKPYEGQKPGTSGLRKKV--KVFTQPNYTEnFVQAILEANGAALAGSTLVVGGDGRFYCKEAAELIVRLSAANG 81
Cdd:COG0033 26 TIKPDPTTPFQDVKFGTSGHRGSSlkGSFNEPHILA-ITQAIFDYRKAQGITGPLFLGGDTHALSEPAIQTALEVLAANG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 82 VSKLLVGQNGILSTPAVSSLIR-HNK----ALGGIVLTASHNPggPEnDFGIKFNCENGGPAPDAFTNHIYKITTEIKEY 156
Cdd:COG0033 105 VGVVIVGQGGYTPTPAVSHAILkYNRgtsgAADGIVLTPSHNP--PE-DGGIKYNPPNGGPADEDVTDAIEARANEILEY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 157 KLVrnlqiDISKVgvtSFDIAGKPFTVEVIDSVANYVRHMEEIFDFAKLKDfvSGkatgkpLKMRIDAMNGVTGSYVREI 236
Cdd:COG0033 182 GLA-----DVKRV---PLDRAGTAMTVEVIDPVADYVELLESVFDFDAIRA--AG------FRIGFDPLGGATGPYWKAI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 237 FlNRLGAtESSVVHTTPLPDF--------GGLHPDPNLTYAkdLVDTVAQGD-YDIGAAFDGDGDRNMIIGSKAFFVTPS 307
Cdd:COG0033 246 A-ERYGL-DLTVVNGVPDPDFrfmtldwdGGIRMDPSSPYA--MASLIAGKDaPDFAAANDGDGDRHGIVTPRGGLMNPN 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 308 DSLAVIAHYLEA-IP-YFQKNGVqgfARSMPTASAVDLVGRKLGKEVFEVPTGWKYFGNLMDAGRLCLCGEESFGT---- 381
Cdd:COG0033 322 HYLAVAIAYLFThRPgWAALAGV---GKTMVTSSAIDRVAAALGRPLYEVPVGFKWFVNGLDAGSLGFGGEESAGAsflr 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 382 --GSNHIREKDGIWAVLAWISVMQHTGKGIEDILKQHWSVYGRNYFTRYDYEecASDPCNEMVATMektitAPEFVGksy 459
Cdd:COG0033 399 rdGSVWTTDKDGLWAVLLAAEILAVTGKSPAEIYRELWARFGRPYYSRHDAE--ATDEQKARLAKL-----SGEQVG--- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 460 ssggkTYKVKEADNFSYTDPVDKSVATKQGLRIVFEDGsRIVVRLSGTgssGATVRLYIDSYE----KENVLGQAsvmlK 535
Cdd:COG0033 469 -----ATTLAGEDIFAYLDPAPGNGAAIGGLKVVTENG-WFAARPSGT---ETTYKIYAESFEgdehLHQIDAEA----A 535
|
....*....
gi 12006791 536 PLIDIALEI 544
Cdd:COG0033 536 DLVDAALAL 544
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
15-157 |
7.47e-45 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 155.07 E-value: 7.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 15 GQKPGTSGLRKKVKVFT-QPNYTENFVQAILEANGAALAGSTLVVGGDGRFYCKEAAELIVRLSAANGVSKLLVgqnGIL 93
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGElTPEFALKLGQAIASYLRAQGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVILL---GLL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12006791 94 STPAVSSLIRHNKALGGIVLTASHNPGGPEndfGIKFNCENGGPAPDAFTNHIYKITTEIKEYK 157
Cdd:pfam02878 78 PTPAVSFATRKLKADGGIMITASHNPPEYN---GIKVFDSNGGPIPPEVEKKIEAIIEKEDFYR 138
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
19-507 |
1.60e-25 |
|
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: 109.52 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 19 GTSGLRKKVkvftQPNYTENFVQAILEANGAALAGSTLVVGGDGRfyckEAAELIVRLsAANGVskLLVGQN----GILS 94
Cdd:TIGR03990 5 GTSGIRGIV----GEELTPELALKVGKAFGTYLRGGKVVVGRDTR----TSGPMLENA-VIAGL--LSTGCDvvdlGIAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 95 TPAVSSLIRHNKALGGIVLTASHNPggPE-NdfGIKFNCENGGPAPDAFTNHIYKItTEIKEYKLVrnlqiDISKVGvts 173
Cdd:TIGR03990 74 TPTLQYAVRELGADGGIMITASHNP--PEyN--GIKLLNSDGTELSREQEEEIEEI-AESGDFERA-----DWDEIG--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 174 fdiagkpfTVEVIDSVANYvrHMEEIfdfaklKDFVSGKA-TGKPLKMRIDAMNGVtGSYVREIFLNRLGATessvVHT- 251
Cdd:TIGR03990 141 --------TVTSDEDAIDD--YIEAI------LDKVDVEAiRKKGFKVVVDCGNGA-GSLTTPYLLRELGCK----VITl 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 252 --TPLPDFGGLHPDPNLTYAKDLVDTVAQGDYDIGAAFDGDGDRNMIIGSKAFFVTPSDSLAVIAHYLEaipyfqKNGVQ 329
Cdd:TIGR03990 200 ncQPDGTFPGRNPEPTPENLKDLSALVKATGADLGIAHDGDADRLVFIDEKGRFIGGDYTLALFAKYLL------EHGGG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 330 GFARSMPTASAVDLVGRKLGKEVFEVPTGWKYFGNLMDAGRLCLCGEESfgtGS----NHIREKDGIWAVLAWISVMQHT 405
Cdd:TIGR03990 274 KVVTNVSSSRAVEDVAERHGGEVIRTKVGEVNVAEKMKEEGAVFGGEGN---GGwifpDHHYCRDGLMAAALFLELLAEE 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 406 GKGIEDILKQHwsvygRNYFTRYDYEECASDPCNEMVATMEKTITapefvgksyssggktykvkeadnfsytdpvDKSVA 485
Cdd:TIGR03990 351 GKPLSELLAEL-----PKYPMSKEKVELPDEDKEEVMEAVEEEFA------------------------------DAEID 395
|
490 500
....*....|....*....|..
gi 12006791 486 TKQGLRIVFEDGsRIVVRLSGT 507
Cdd:TIGR03990 396 TIDGVRIDFEDG-WVLVRPSGT 416
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
6-560 |
0e+00 |
|
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: 1031.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 6 EIVATKPYEGQKPGTSGLRKKVKVFTQPNYTENFVQAILEANGAA-LAGSTLVVGGDGRFYCKEAAELIVRLSAANGVSK 84
Cdd:cd03085 1 QTVPTKPYEGQKPGTSGLRKKVKVFQQPNYLENFVQSIFNALPPEkLKGATLVVGGDGRYYNKEAIQIIIKIAAANGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 85 LLVGQNGILSTPAVSSLIRHNKALGGIVLTASHNPGGPENDFGIKFNCENGGPAPDAFTNHIYKITTEIKEYKLVRNLQI 164
Cdd:cd03085 81 VVVGQNGLLSTPAVSAVIRKRKATGGIILTASHNPGGPEGDFGIKYNTSNGGPAPESVTDKIYEITKKITEYKIADDPDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 165 DISKVGVTSFDiaGKPFTVEVIDSVANYVRHMEEIFDFAKLKDFVSGKatgkPLKMRIDAMNGVTGSYVREIFLNRLGAT 244
Cdd:cd03085 161 DLSKIGVTKFG--GKPFTVEVIDSVEDYVELMKEIFDFDAIKKLLSRK----GFKVRFDAMHGVTGPYAKKIFVEELGAP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 245 ESSVVHTTPLPDFGGLHPDPNLTYAKDLVDTVAQGDYDIGAAFDGDGDRNMIIGsKAFFVTPSDSLAVIAHYLEAIPYFQ 324
Cdd:cd03085 235 ESSVVNCTPLPDFGGGHPDPNLTYAKDLVELMKSGEPDFGAASDGDGDRNMILG-KGFFVTPSDSVAVIAANAKLIPYFY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 325 KNGVQGFARSMPTASAVDLVGRKLGKEVFEVPTGWKYFGNLMDAGRLCLCGEESFGTGSNHIREKDGIWAVLAWISVMQH 404
Cdd:cd03085 314 KGGLKGVARSMPTSGALDRVAKKLGIPLFETPTGWKFFGNLMDAGKLSLCGEESFGTGSDHIREKDGLWAVLAWLSILAH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 405 TGKGIEDILKQHWSVYGRNYFTRYDYEECASDPCNEMVATMEKTITAPEFVGKsysSGGKTYKVKEADNFSYTDPVDKSV 484
Cdd:cd03085 394 RNVSVEDIVKEHWQKYGRNFYTRYDYEEVDSEAANKMMDHLRALVSDLPGVGK---SGDKGYKVAKADDFSYTDPVDGSV 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12006791 485 ATKQGLRIVFEDGSRIVVRLSGTGSSGATVRLYIDSYEKEN--VLGQASVMLKPLIDIALEISQLPKFTGRNAPTVIT 560
Cdd:cd03085 471 SKKQGLRIIFEDGSRIIFRLSGTGSSGATIRLYIESYEKDPskYGLDAQVALKPLIEIALKLSKLKEFTGREEPTVIT 548
|
|
| PLN02307 |
PLN02307 |
phosphoglucomutase |
1-560 |
0e+00 |
|
phosphoglucomutase
Pssm-ID: 177942 [Multi-domain] Cd Length: 579 Bit Score: 820.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 1 MSLTVEIVATKPYEGQKPGTSGLRKKVKVFTQPNYTENFVQAILEANGAA-LAGSTLVVGGDGRFYCKEAAELIVRLSAA 79
Cdd:PLN02307 8 ASFKVSSVPTKPIEGQKPGTSGLRKKVKVFMQENYLANFVQALFNALPAEkVKGATLVLGGDGRYFNKEAIQIIIKIAAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 80 NGVSKLLVGQNGILSTPAVSSLIR---HNKALGGIVLTASHNPGGPENDFGIKFNCENGGPAPDAFTNHIYKITTEIKEY 156
Cdd:PLN02307 88 NGVRRVWVGQNGLLSTPAVSAVIRerdGSKANGGFILTASHNPGGPEEDFGIKYNYESGQPAPESITDKIYGNTLTIKEY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 157 KLVRNL-QIDISKVGVTSFDiAGKPFTVEVIDSVANYVRHMEEIFDFAKLKDFVSgkatgKP-LKMRIDAMNGVTGSYVR 234
Cdd:PLN02307 168 KMAEDIpDVDLSAVGVTKFG-GPEDFDVEVIDPVEDYVKLMKSIFDFELIKKLLS-----RPdFTFCFDAMHGVTGAYAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 235 EIFLNRLGATESSVVHTTPLPDFGGLHPDPNLTYAKDLVDTVAQGDY-------DIGAAFDGDGDRNMIIGSKaFFVTPS 307
Cdd:PLN02307 242 RIFVEELGAPESSLLNCVPKEDFGGGHPDPNLTYAKELVKRMGLGKTsygdeppEFGAASDGDGDRNMILGKR-FFVTPS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 308 DSLAVI-AHYLEAIPYFqKNGVQGFARSMPTASAVDLVGRKLGKEVFEVPTGWKYFGNLMDAGRLCLCGEESFGTGSNHI 386
Cdd:PLN02307 321 DSVAIIaANAQEAIPYF-SGGLKGVARSMPTSAALDVVAKKLNLPFFEVPTGWKFFGNLMDAGKLSICGEESFGTGSDHI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 387 REKDGIWAVLAWISVMQHTGK---------GIEDILKQHWSVYGRNYFTRYDYEECASDPCNEMVATMEKTITApefVGK 457
Cdd:PLN02307 400 REKDGIWAVLAWLSILAHKNKdvlpggklvTVEDIVREHWATYGRNFYSRYDYENVDSEAANKMMDHLRDLVNK---SKK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 458 SYSSGgkTYKVKEADNFSYTDPVDKSVATKQGLRIVFEDGSRIVVRLSGTGSSGATVRLYIDSYEKE--NVLGQASVMLK 535
Cdd:PLN02307 477 GIKYG--VYTLAFADDFEYTDPVDGSVSSKQGIRFLFTDGSRIIFRLSGTGSAGATIRLYIEQYEKDpsKHGRDAQEALK 554
|
570 580
....*....|....*....|....*
gi 12006791 536 PLIDIALEISQLPKFTGRNAPTVIT 560
Cdd:PLN02307 555 PLIDVALKLSKLKEFTGRSKPTVIT 579
|
|
| Pgm |
COG0033 |
Phosphoglucomutase/phosphomannomutase [Carbohydrate transport and metabolism]; |
4-544 |
0e+00 |
|
Phosphoglucomutase/phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 439803 Cd Length: 544 Bit Score: 581.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 4 TVEIVATKPYEGQKPGTSGLRKKV--KVFTQPNYTEnFVQAILEANGAALAGSTLVVGGDGRFYCKEAAELIVRLSAANG 81
Cdd:COG0033 26 TIKPDPTTPFQDVKFGTSGHRGSSlkGSFNEPHILA-ITQAIFDYRKAQGITGPLFLGGDTHALSEPAIQTALEVLAANG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 82 VSKLLVGQNGILSTPAVSSLIR-HNK----ALGGIVLTASHNPggPEnDFGIKFNCENGGPAPDAFTNHIYKITTEIKEY 156
Cdd:COG0033 105 VGVVIVGQGGYTPTPAVSHAILkYNRgtsgAADGIVLTPSHNP--PE-DGGIKYNPPNGGPADEDVTDAIEARANEILEY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 157 KLVrnlqiDISKVgvtSFDIAGKPFTVEVIDSVANYVRHMEEIFDFAKLKDfvSGkatgkpLKMRIDAMNGVTGSYVREI 236
Cdd:COG0033 182 GLA-----DVKRV---PLDRAGTAMTVEVIDPVADYVELLESVFDFDAIRA--AG------FRIGFDPLGGATGPYWKAI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 237 FlNRLGAtESSVVHTTPLPDF--------GGLHPDPNLTYAkdLVDTVAQGD-YDIGAAFDGDGDRNMIIGSKAFFVTPS 307
Cdd:COG0033 246 A-ERYGL-DLTVVNGVPDPDFrfmtldwdGGIRMDPSSPYA--MASLIAGKDaPDFAAANDGDGDRHGIVTPRGGLMNPN 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 308 DSLAVIAHYLEA-IP-YFQKNGVqgfARSMPTASAVDLVGRKLGKEVFEVPTGWKYFGNLMDAGRLCLCGEESFGT---- 381
Cdd:COG0033 322 HYLAVAIAYLFThRPgWAALAGV---GKTMVTSSAIDRVAAALGRPLYEVPVGFKWFVNGLDAGSLGFGGEESAGAsflr 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 382 --GSNHIREKDGIWAVLAWISVMQHTGKGIEDILKQHWSVYGRNYFTRYDYEecASDPCNEMVATMektitAPEFVGksy 459
Cdd:COG0033 399 rdGSVWTTDKDGLWAVLLAAEILAVTGKSPAEIYRELWARFGRPYYSRHDAE--ATDEQKARLAKL-----SGEQVG--- 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 460 ssggkTYKVKEADNFSYTDPVDKSVATKQGLRIVFEDGsRIVVRLSGTgssGATVRLYIDSYE----KENVLGQAsvmlK 535
Cdd:COG0033 469 -----ATTLAGEDIFAYLDPAPGNGAAIGGLKVVTENG-WFAARPSGT---ETTYKIYAESFEgdehLHQIDAEA----A 535
|
....*....
gi 12006791 536 PLIDIALEI 544
Cdd:COG0033 536 DLVDAALAL 544
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
4-540 |
0e+00 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 535.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 4 TVEIVATKPYEGQKPGTSGLRKKVkvfTQPNYTENFVQAILEA----NGAALAGSTLVVGGDGRFYCKEAAELIVRLSAA 79
Cdd:PRK07564 26 TLKPDPTNPFQDVKFGTSGHRGSS---LQPSFNENHILAIFQAiceyRGKQGITGPLFVGGDTHALSEPAIQSALEVLAA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 80 NGVSKLLVGQNGILSTPAVSSLIR-HNK----ALGGIVLTASHNPggPEnDFGIKFNCENGGPAPDAFTNHIYKITTEIK 154
Cdd:PRK07564 103 NGVGVVIVGRGGYTPTPAVSHAILkYNGrgggLADGIVITPSHNP--PE-DGGIKYNPPNGGPADTDVTDAIEARANELL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 155 EYKLVrnlqiDISKVGvtsFDIAGKPFTVEVIDSVANYVRHMEEIFDFAKLKDfvSGkatgkpLKMRIDAMNGVTGSYVR 234
Cdd:PRK07564 180 AYGLK-----GVKRIP---LDRALASMTVEVIDPVADYVEDLENVFDFDAIRK--AG------LRLGVDPLGGATGPYWK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 235 EIF------LNRLGATESSVVHTTPLPDFGGLHPDPNLTYAkdLVDTVAQGD-YDIGAAFDGDGDRNMIIGsKAFFVTPS 307
Cdd:PRK07564 244 AIAerygldLTVVNAPVDPTFNFMPLDDDGKIRMDCSSPYA--MAGLLALKDaFDLAFANDPDGDRHGIVT-PGGLMNPN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 308 DSLAVIAHYLEA-IP-YFQKNGVqgfARSMPTASAVDLVGRKLGKEVFEVPTGWKYFGNLMDAGRLCLCGEESFGT---- 381
Cdd:PRK07564 321 HYLAVAIAYLFHhRPgWRAGAGV---GKTLVSSAMIDRVAAKLGRKLYEVPVGFKWFVNGLDDGSLGFGGEESAGAsflr 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 382 --GSNHIREKDGIWAVLAWISVMQHTGKGIEDILKQHWSVYGRNYFTRYDYEECASDpcnemVATMEKT----ITAPEFV 455
Cdd:PRK07564 398 rdGSVWTTDKDGLIAVLLAAEILAVTGKSPSEIYRELWARFGRPYYSRHDAPATPEQ-----KAALRKLspelVGATELA 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 456 GksyssggktykvkeadnfsytDPVDKSVATKQ-------GLRIVFEDGsRIVVRLSGTgssGATVRLYIDSYE----KE 524
Cdd:PRK07564 473 G---------------------DPIDASLTEAPgngaaigGLKVVTENG-WFAARPSGT---ETTYKIYAESFEgdehLH 527
|
570
....*....|....*.
gi 12006791 525 NVLGQASVMLKPLIDI 540
Cdd:PRK07564 528 QIQKEAQEIVADLIAA 543
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
19-507 |
6.67e-74 |
|
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily and is found in both archaea and bacteria. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four structural domains (subdomains) with a centrally located active site formed by four loops, one from each subdomain. All four subdomains are included in this alignment model.
Pssm-ID: 100093 Cd Length: 461 Bit Score: 242.46 E-value: 6.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 19 GTSGLRKKV-KVFTQPNytenfVQAILEANGAALA-----GSTLVVGGDGRFYCKEAAELIVRLSAANGVSKLLVgqNGI 92
Cdd:cd05800 4 GTDGWRGIIaEDFTFEN-----VRRVAQAIADYLKeegggGRGVVVGYDTRFLSEEFARAVAEVLAANGIDVYLS--DRP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 93 LSTPAVSSLIRHNKALGGIVLTASHNPGgpeNDFGIKFNCENGGPAPDAFTNHIYKITTEIKEYKLVrnlqidiskvgvt 172
Cdd:cd05800 77 VPTPAVSWAVKKLGAAGGVMITASHNPP---EYNGVKVKPAFGGSALPEITAAIEARLASGEPPGLE------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 173 sfdiAGKPFTVEVIDSVANYVRHMEEIFDFAKLKdfvsgkatGKPLKMRIDAMNGVTGSYVREIFlnRLGATESSVVHTT 252
Cdd:cd05800 141 ----ARAEGLIETIDPKPDYLEALRSLVDLEAIR--------EAGLKVVVDPMYGAGAGYLEELL--RGAGVDVEEIRAE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 253 PLPDFGGLHPDPNLTYAKDLVDTVAQGDYDIGAAFDGDGDRNMIIGSKAFFVTPSDSLAVIAHYLeaipyFQKNGVQG-F 331
Cdd:cd05800 207 RDPLFGGIPPEPIEKNLGELAEAVKEGGADLGLATDGDADRIGAVDEKGNFLDPNQILALLLDYL-----LENKGLRGpV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 332 ARSMPTASAVDLVGRKLGKEVFEVPTGWKYFGNLMDAGRLCLCGEESFGTG-SNHIREKDGIWAVLAWISVMQHTGKGIE 410
Cdd:cd05800 282 VKTVSTTHLIDRIAEKHGLPVYETPVGFKYIAEKMLEEDVLIGGEESGGLGiRGHIPERDGILAGLLLLEAVAKTGKPLS 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 411 DILKQHWSVYGRNYFTRYDYeecasdPCNEMV--ATMEK-TITAPEFVGKsyssggktYKVKEadnfsytdpvdksVATK 487
Cdd:cd05800 362 ELVAELEEEYGPSYYDRIDL------RLTPAQkeAILEKlKNEPPLSIAG--------GKVDE-------------VNTI 414
|
490 500
....*....|....*....|
gi 12006791 488 QGLRIVFEDGSRIVVRLSGT 507
Cdd:cd05800 415 DGVKLVLEDGSWLLIRPSGT 434
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
19-524 |
6.48e-65 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 218.53 E-value: 6.48e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 19 GTSGLRKKVKVftqpNYTENFVQAIleanGAALA-------GSTLVVGGDGRFYCKEAAELIVRLSAANGVSKLLVGqng 91
Cdd:COG1109 8 GTDGIRGIVGE----ELTPEFVLKL----GRAFGtylkekgGPKVVVGRDTRLSSPMLARALAAGLASAGIDVYDLG--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 92 ILSTPAVSSLIRHNKALGGIVLTASHNPggPEnDFGIKFNCENGGPAPDAftnHIYKITTEIKEYKLVRnlqIDISKVGv 171
Cdd:COG1109 77 LVPTPALAFAVRHLGADGGIMITASHNP--PE-YNGIKFFDADGGKLSPE---EEKEIEALIEKEDFRR---AEAEEIG- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 172 tsfdiagkpfTVEVIDSVAN-YVRHmeeifdfakLKDFVSGKATGKPLKMRIDAMNGVTGSYVREIFlNRLGAtESSVVH 250
Cdd:COG1109 147 ----------KVTRIEDVLEaYIEA---------LKSLVDEALRLRGLKVVVDCGNGAAGGVAPRLL-RELGA-EVIVLN 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 251 TTPLPDFGGLHPDPNLTYAKDLVDTVAQGDYDIGAAFDGDGDRNMIIGSKAFFVTPSDSLAVIAHYLEaipyfQKNGVQG 330
Cdd:COG1109 206 AEPDGNFPNHNPNPEPENLEDLIEAVKETGADLGIAFDGDADRLGVVDEKGRFLDGDQLLALLARYLL-----EKGPGGT 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 331 FARSMPTASAVDLVGRKLGKEVFEVPTGWKYFGNLMDAGRLCLCGEESFGTG-SNHIREKDGIWAVLAWISVMQHTGKGI 409
Cdd:COG1109 281 VVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKMRETGAVLGGEESGGIIfPDFVPTDDGILAALLLLELLAKQGKSL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 410 EDILKQhwsvYGRNYFTRYDYeECASDpcNEMVATMEKTITapefvgksyssggktyKVKEADNFSYTDpvdksvatkqG 489
Cdd:COG1109 361 SELLAE----LPRYPQPEINV-RVPDE--EKIGAVMEKLRE----------------AVEDKEELDTID----------G 407
|
490 500 510
....*....|....*....|....*....|....*
gi 12006791 490 LRIVFEDGSRIVVRLSGTGSSgatVRLYIDSYEKE 524
Cdd:COG1109 408 VKVDLEDGGWVLVRPSGTEPL---LRVYAEAKDEE 439
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
17-424 |
3.67e-64 |
|
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this family include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). These enzymes play important and diverse roles in carbohydrate metabolism in organisms from bacteria to humans. Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100086 [Multi-domain] Cd Length: 355 Bit Score: 213.76 E-value: 3.67e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 17 KPGTSGLRKKVKVFTQPNYTENFVQAILEangaalagstlvvggdgrfyckeaaelivrlsaangvskllvgqngilstp 96
Cdd:cd03084 1 IFGTSGVRGVVGDDITPETAVALGQAIGS--------------------------------------------------- 29
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 97 avsslirhnkaLGGIVLTASHNPGGpenDFGIKFNCENGGPAPDAFTNHIYKITTEIKEYKLVRNLQIDIskvgvtsfdi 176
Cdd:cd03084 30 -----------TGGIMITASHNPPE---DNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSAVAYELGGS---------- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 177 agkpftVEVIDSVANYVRHMEEIFDFAKLKdfvsgkatGKPLKMRIDAMNGVTGSYVREIFlNRLGAtESSVVHTTPLPD 256
Cdd:cd03084 86 ------VKAVDILQRYFEALKKLFDVAALS--------NKKFKVVVDSVNGVGGPIAPQLL-EKLGA-EVIPLNCEPDGN 149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 257 FGGLHPDPN-LTYAKDLVDTVAQGDYDIGAAFDGDGDRNMIIGSKAFFVTPSDSLAVIAhyLEAIPYFQKNGvqGFARSM 335
Cdd:cd03084 150 FGNINPDPGsETNLKQLLAVVKAEKADFGVAFDGDADRLIVVDENGGFLDGDELLALLA--VELFLTFNPRG--GVVKTV 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 336 PTASAVDLVGRKLGKEVFEVPTGWKYFGNLMDAGRLCLCGEESFGTGSNHI-REKDGIWAVLAWISVMQHTGKGIEDILK 414
Cdd:cd03084 226 VSSGALDKVAKKLGIKVIRTKTGFKWVGEAMQEGDVVLGGEESGGVIFPEFhPGRDGISAALLLLEILANLGKSLSELFS 305
|
410
....*....|
gi 12006791 415 QHWSVYGRNY 424
Cdd:cd03084 306 ELPRYYYIRL 315
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
15-157 |
7.47e-45 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 155.07 E-value: 7.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 15 GQKPGTSGLRKKVKVFT-QPNYTENFVQAILEANGAALAGSTLVVGGDGRFYCKEAAELIVRLSAANGVSKLLVgqnGIL 93
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGElTPEFALKLGQAIASYLRAQGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVILL---GLL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12006791 94 STPAVSSLIRHNKALGGIVLTASHNPGGPEndfGIKFNCENGGPAPDAFTNHIYKITTEIKEYK 157
Cdd:pfam02878 78 PTPAVSFATRKLKADGGIMITASHNPPEYN---GIKVFDSNGGPIPPEVEKKIEAIIEKEDFYR 138
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
19-507 |
4.40e-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: 132.24 E-value: 4.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 19 GTSGLRKKVKV-FTQPN-YTenfVQAI-------LEANGAALAGSTLVVGGDGRFYCKEAAELIVRLSAANGVSKLLVgq 89
Cdd:cd05799 5 GTAGLRGKMGAgTNRMNdYT---VRQAtqglanyLKKKGPDAKNRGVVIGYDSRHNSREFAELTAAVLAANGIKVYLF-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 90 NGILSTPAVSSLIRHNKALGGIVLTASHNPggPEnDFGIKFNCENGG--PAPDAftnhiykitTEIKEYklvrnlqidIS 167
Cdd:cd05799 80 DDLRPTPLLSFAVRHLGADAGIMITASHNP--KE-YNGYKVYWEDGAqiIPPHD---------AEIAEE---------IE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 168 KVGvtsfDIAGKPFTVEVIDSVANYVRhmEEIFD--FAKLKDFVSGKATGKPLKMRI--DAMNGVTGSYVREIfLNRLGA 243
Cdd:cd05799 139 AVL----EPLDIKFEEALDSGLIKYIG--EEIDDayLEAVKKLLVNPELNEGKDLKIvyTPLHGVGGKFVPRA-LKEAGF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 244 TESSVV--HTTPLPDFGGLhPDPN------LTYAKDLVDTVaqgDYDIGAAFDGDGDRNMI---IGSKAFFVTPSDSLAV 312
Cdd:cd05799 212 TNVIVVeeQAEPDPDFPTV-KFPNpeepgaLDLAIELAKKV---GADLILATDPDADRLGVavkDKDGEWRLLTGNEIGA 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 313 I-AHYL----EAIPYFQKNGVqgFARSMPTASAVDLVGRKLGKEVFEVPTGWKYFGNLM-----DAGRLCLCGEESFG-T 381
Cdd:cd05799 288 LlADYLleqrKEKGKLPKNPV--IVKTIVSSELLRKIAKKYGVKVEETLTGFKWIGNKIeelesGGKKFLFGFEESIGyL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 382 GSNHIREKDGIWAVLAWISVMQH---TGKGIEDILKQHWSVYGRnYFTRYDYEEC-ASDPCNEMVATMEKTITAPefvgk 457
Cdd:cd05799 366 VGPFVRDKDGISAAALLAEMAAYlkaQGKTLLDRLDELYEKYGY-YKEKTISITFeGKEGPEKIKAIMDRLRNNP----- 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 12006791 458 syssggktykvkeadnfsytdpvdksvatkQGLRIVFEDGSRIVVRLSGT 507
Cdd:cd05799 440 ------------------------------NVLTFYLEDGSRVTVRPSGT 459
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
78-507 |
9.07e-31 |
|
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: 125.82 E-value: 9.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 78 AANGVSKLLVGQNGILSTPAVS-SLIRHNKALG-----GIVLTASHNPggPEnDFGIKFNCENGGPAPDAFTNHIYKITT 151
Cdd:cd05801 84 AANGVEVIIQQNDGYTPTPVIShAILTYNRGRTegladGIVITPSHNP--PE-DGGFKYNPPHGGPADTDITRWIEKRAN 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 152 EIkeyklvrnLQIDISKVGVTSFDIAGKPFTVEVIDSVANYVRHMEEIFDFAKLKDfvSGkatgkpLKMRIDAMNGVTGS 231
Cdd:cd05801 161 AL--------LANGLKGVKRIPLEAALASGYTHRHDFVTPYVADLGNVIDMDAIRK--SG------LRLGVDPLGGASVP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 232 YVREIF-LNRLGATessVVHTTPLPDFGGLHPD--------PNLTYA-KDLVDTvaQGDYDIGAAFDGDGDRNMIIGSKA 301
Cdd:cd05801 225 YWQPIAeKYGLNLT---VVNPKVDPTFRFMTLDhdgkirmdCSSPYAmAGLLKL--KDKFDLAFANDPDADRHGIVTPSA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 302 FFVTPSDSLAVIAHYLEAIPYFQKNGVqGFARSMPTASAVDLVGRKLGKEVFEVPTGWKYFGNLMDAGRLCLCGEESFGT 381
Cdd:cd05801 300 GLMNPNHYLSVAIDYLFTHRPLWNKSA-GVGKTLVSSSMIDRVAAALGRKLYEVPVGFKWFVDGLLDGSLGFGGEESAGA 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 382 ------GSNHIREKDGIWAVLAWISVMQHTGKGIEDILKQHWSVYGRNYFTRYDYeecASDPCNE--MVATMEKTITAPE 453
Cdd:cd05801 379 sflrrdGTVWTTDKDGIIMCLLAAEILAVTGKDPGQLYQELTERFGEPYYARIDA---PATPEQKarLKKLSPEQVTATE 455
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12006791 454 FVGksyssggktykvkeadnfsytDPVDKSVATKQ-------GLRIVFEDGsRIVVRLSGT 507
Cdd:cd05801 456 LAG---------------------DPILAKLTRAPgngasigGLKVTTANG-WFAARPSGT 494
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
36-507 |
1.40e-29 |
|
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: 121.47 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 36 TENFVQAIleanGAALA-------GSTLVVGGDGRFYCKEAAELIVR-LSAAnGVSKLLVGqngILSTPAVSSLIRHNKA 107
Cdd:cd03089 16 TEEIAYAI----GRAFGswllekgAKKVVVGRDGRLSSPELAAALIEgLLAA-GCDVIDIG---LVPTPVLYFATFHLDA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 108 LGGIVLTASHNPGgpeNDFGIKFnCENGGPapdaftnhIYKitTEIKE-YKLVRNLQidiskvgvtsFDIAGKPFTVEVI 186
Cdd:cd03089 88 DGGVMITASHNPP---EYNGFKI-VIGGGP--------LSG--EDIQAlRERAEKGD----------FAAATGRGSVEKV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 187 DSVANYVRHMEEIFDFAKlkdfvsgkatgKPLKMRIDAMNGVTGSYVREIFlNRLGAtESSVVHTTPLPDFGGLHPDP-- 264
Cdd:cd03089 144 DILPDYIDRLLSDIKLGK-----------RPLKVVVDAGNGAAGPIAPQLL-EALGC-EVIPLFCEPDGTFPNHHPDPtd 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 265 --NLtyaKDLVDTVAQGDYDIGAAFDGDGDRNMIIGSKAFFVTPsDSLAVIahyleaipyfqkngvqgFARSM----PTA 338
Cdd:cd03089 211 peNL---EDLIAAVKENGADLGIAFDGDGDRLGVVDEKGEIIWG-DRLLAL-----------------FARDIlkrnPGA 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 339 SAV----------DLVgRKLGKEVFEVPTGWKYFGNLM-DAGRLcLCGEEsfgtgSNHI--REK-----DGIWAVLAWIS 400
Cdd:cd03089 270 TIVydvkcsrnlyDFI-EEAGGKPIMWKTGHSFIKAKMkETGAL-LAGEM-----SGHIffKDRwygfdDGIYAALRLLE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 401 VMQHTGKGIEDILKQhwsvygrnyftrydyeecasdpcnemvatMEKTITAPEFvgksyssggkTYKVKEADNFSYTDPV 480
Cdd:cd03089 343 LLSKSGKTLSELLAD-----------------------------LPKYFSTPEI----------RIPVTEEDKFAVIERL 383
|
490 500 510
....*....|....*....|....*....|....
gi 12006791 481 DKSVATKQ-------GLRIVFEDGsRIVVRLSGT 507
Cdd:cd03089 384 KEHFEFPGaeiididGVRVDFEDG-WGLVRASNT 416
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
310-420 |
2.89e-27 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 105.99 E-value: 2.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 310 LAVIAHYLEAipYFQKNGVQGFARSMPTASAVDLVGRKLGKEVFEVPTGWKYFGNLMDAGRLCLCGEESfGTGSN--HIR 387
Cdd:pfam02880 6 LALLAKYLLE--QGKLPPGAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEES-GHIIFldHAT 82
|
90 100 110
....*....|....*....|....*....|...
gi 12006791 388 EKDGIWAVLAWISVMQHTGKGIEDILKQHWSVY 420
Cdd:pfam02880 83 TKDGILAALLVLEILARTGKSLSELLEELPEKY 115
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
19-507 |
1.60e-25 |
|
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: 109.52 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 19 GTSGLRKKVkvftQPNYTENFVQAILEANGAALAGSTLVVGGDGRfyckEAAELIVRLsAANGVskLLVGQN----GILS 94
Cdd:TIGR03990 5 GTSGIRGIV----GEELTPELALKVGKAFGTYLRGGKVVVGRDTR----TSGPMLENA-VIAGL--LSTGCDvvdlGIAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 95 TPAVSSLIRHNKALGGIVLTASHNPggPE-NdfGIKFNCENGGPAPDAFTNHIYKItTEIKEYKLVrnlqiDISKVGvts 173
Cdd:TIGR03990 74 TPTLQYAVRELGADGGIMITASHNP--PEyN--GIKLLNSDGTELSREQEEEIEEI-AESGDFERA-----DWDEIG--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 174 fdiagkpfTVEVIDSVANYvrHMEEIfdfaklKDFVSGKA-TGKPLKMRIDAMNGVtGSYVREIFLNRLGATessvVHT- 251
Cdd:TIGR03990 141 --------TVTSDEDAIDD--YIEAI------LDKVDVEAiRKKGFKVVVDCGNGA-GSLTTPYLLRELGCK----VITl 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 252 --TPLPDFGGLHPDPNLTYAKDLVDTVAQGDYDIGAAFDGDGDRNMIIGSKAFFVTPSDSLAVIAHYLEaipyfqKNGVQ 329
Cdd:TIGR03990 200 ncQPDGTFPGRNPEPTPENLKDLSALVKATGADLGIAHDGDADRLVFIDEKGRFIGGDYTLALFAKYLL------EHGGG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 330 GFARSMPTASAVDLVGRKLGKEVFEVPTGWKYFGNLMDAGRLCLCGEESfgtGS----NHIREKDGIWAVLAWISVMQHT 405
Cdd:TIGR03990 274 KVVTNVSSSRAVEDVAERHGGEVIRTKVGEVNVAEKMKEEGAVFGGEGN---GGwifpDHHYCRDGLMAAALFLELLAEE 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 406 GKGIEDILKQHwsvygRNYFTRYDYEECASDPCNEMVATMEKTITapefvgksyssggktykvkeadnfsytdpvDKSVA 485
Cdd:TIGR03990 351 GKPLSELLAEL-----PKYPMSKEKVELPDEDKEEVMEAVEEEFA------------------------------DAEID 395
|
490 500
....*....|....*....|..
gi 12006791 486 TKQGLRIVFEDGsRIVVRLSGT 507
Cdd:TIGR03990 396 TIDGVRIDFEDG-WVLVRPSGT 416
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
19-415 |
3.97e-23 |
|
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: 102.18 E-value: 3.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 19 GTSGLRKKVKVFTqpnyTENFVQAILEANGAALA----GSTLVVGGDGRF--YCKEAAeLIVRLSAAnGVSKLLVGqngI 92
Cdd:cd05802 3 GTDGIRGVANEPL----TPELALKLGRAAGKVLGkgggRPKVLIGKDTRIsgYMLESA-LAAGLTSA-GVDVLLLG---V 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 93 LSTPAVSSLIRHNKALGGIVLTASHNPggPEnDFGIKFNCENGGPAPDAFTNHIykitteikEYKLVRNLQIDISKVGVt 172
Cdd:cd05802 74 IPTPAVAYLTRKLRADAGVVISASHNP--FE-DNGIKFFSSDGYKLPDEVEEEI--------EALIDKELELPPTGEKI- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 173 sfdiaGKpfTVEVIDSVANYVRHMEEIFDFAKLKDfvsgkatgkpLKMRIDAMNGVTGSYVREIFlNRLGAtESSVVHTT 252
Cdd:cd05802 142 -----GR--VYRIDDARGRYIEFLKSTFPKDLLSG----------LKIVLDCANGAAYKVAPEVF-RELGA-EVIVINNA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 253 plPD-------FGGLHPDPnltyakdLVDTVAQGDYDIGAAFDGDGDRNMIIGSKAFFVTPSDSLAVIAHYLEAIPYFQK 325
Cdd:cd05802 203 --PDglninvnCGSTHPES-------LQKAVLENGADLGIAFDGDADRVIAVDEKGNIVDGDQILAICARDLKERGRLKG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 326 NGV-------QGFARSMptasavdlvgRKLGKEVFEVPTGWKYFGNLMDAGRLCLCGEESfGtgsnHI--REK----DGI 392
Cdd:cd05802 274 NTVvgtvmsnLGLEKAL----------KELGIKLVRTKVGDRYVLEEMLKHGANLGGEQS-G----HIifLDHsttgDGL 338
|
410 420
....*....|....*....|...
gi 12006791 393 WAVLAWISVMQHTGKGIEDILKQ 415
Cdd:cd05802 339 LTALQLLAIMKRSGKSLSELASD 361
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
21-358 |
6.95e-21 |
|
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: 95.45 E-value: 6.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 21 SGLRKKVKVFTQPNYTENFVQAILEANGAALAGSTLVVGGDGRFYCKEAAELIVRLSAANGVSkllVGQNGILSTPAVSS 100
Cdd:cd05803 5 SGIRGIVGEGLTPEVITRYVAAFATWQPERTKGGKIVVGRDGRPSGPMLEKIVIGALLACGCD---VIDLGIAPTPTVQV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 101 LIRHNKALGGIVLTASHNPggPE-NdfGIKFNCENGGPAPDAFTNHIYKITTEiKEYKLVRNLQIDIskvgVTSFDIAGK 179
Cdd:cd05803 82 LVRQSQASGGIIITASHNP--PQwN--GLKFIGPDGEFLTPDEGEEVLSCAEA-GSAQKAGYDQLGE----VTFSEDAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 180 PftvevidsvanyvrHMEEIFdfaKLKDFVSGKATGKPLKMRIDAMNGVTGSYVREiFLNRLGATESsVVHTTPLPDFgg 259
Cdd:cd05803 153 E--------------HIDKVL---ALVDVDVIKIRERNFKVAVDSVNGAGGLLIPR-LLEKLGCEVI-VLNCEPTGLF-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 260 LH-PDP---NLTyakDLVDTVAQGDYDIGAAFDGDGDRNMIIGSKAFFVTPSDSLAVIAHYLEAIPyfqknGVQG-FARS 334
Cdd:cd05803 212 PHtPEPlpeNLT---QLCAAVKESGADVGFAVDPDADRLALVDEDGRPIGEEYTLALAVDYVLKYG-----GRKGpVVVN 283
|
330 340
....*....|....*....|....
gi 12006791 335 MPTASAVDLVGRKLGKEVFEVPTG 358
Cdd:cd05803 284 LSTSRALEDIARKHGVPVFRSAVG 307
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
19-317 |
3.59e-20 |
|
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: 93.02 E-value: 3.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 19 GTSGLRKKVkvftQPNYTENFVQAILEANGAALAGSTLVVGGDGRfyckEAAELIVR-----LSAAnGVSKLLVGqngIL 93
Cdd:cd03087 3 GTSGIRGVV----GEELTPELALKVGKALGTYLGGGTVVVGRDTR----TSGPMLKNaviagLLSA-GCDVIDIG---IV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 94 STPAVSSLIRhNKALGGIVLTASHNPggPEnDFGIKFNCENGGPAPDAFTNHIYKITTEiKEYKLVrnlqiDISKVGvts 173
Cdd:cd03087 71 PTPALQYAVR-KLGDAGVMITASHNP--PE-YNGIKLVNPDGTEFSREQEEEIEEIIFS-ERFRRV-----AWDEVG--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 174 fdiagkpfTVEVIDSVANYvrHMEEIFDFAKLKdfvsgkaTGKPLKMRIDAMNGVtGSYVREIFLNRLGATessvVHT-- 251
Cdd:cd03087 138 --------SVRREDSAIDE--YIEAILDKVDID-------GGKGLKVVVDCGNGA-GSLTTPYLLRELGCK----VITln 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12006791 252 -TPLPDFGGLHPDPNLTYAKDLVDTVAQGDYDIGAAFDGDGDRNMIIGSKAFFVTPSDSLAVIAHYL 317
Cdd:cd03087 196 aNPDGFFPGRPPEPTPENLSELMELVRATGADLGIAHDGDADRAVFVDEKGRFIDGDKLLALLAKYL 262
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
192-297 |
2.22e-17 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 77.72 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 192 YVRHMEEIFDFAKLKdfvsgkatGKPLKMRIDAMNGVTGSYVREIfLNRLGAtESSVVHTTPLPDFGGLHPDP-NLTYAK 270
Cdd:pfam02879 2 YIDHLLELVDSEALK--------KRGLKVVYDPLHGVGGGYLPEL-LKRLGC-DVVEENCEPDPDFPTRAPNPeEPEALA 71
|
90 100
....*....|....*....|....*..
gi 12006791 271 DLVDTVAQGDYDIGAAFDGDGDRNMII 297
Cdd:pfam02879 72 LLIELVKSVGADLGIATDGDADRLGVV 98
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
19-507 |
3.93e-15 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 78.19 E-value: 3.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 19 GTSGLRKKVKV-FTQPN------YTENFVQAILEANGAALAGSTLVVGGDGRFYCKEAAELIVRLSAANGVSKLLVGQng 91
Cdd:PTZ00150 48 GTAGLRGKMGAgFNCMNdltvqqTAQGLCAYVIETFGQALKSRGVVIGYDGRYHSRRFAEITASVFLSKGFKVYLFGQ-- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 92 ILSTPAVSSLIRHNKALGGIVLTASHNpggPENDFGIKFNCENGG---PAPDAftnhiyKITTEIKEyklvrNLqidisk 168
Cdd:PTZ00150 126 TVPTPFVPYAVRKLKCLAGVMVTASHN---PKEDNGYKVYWSNGAqiiPPHDK------NISAKILS-----NL------ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 169 vgvTSFDIAGKPFTVE-VIDSVAnyvrhmeEIFD--FAKLK-DFVSGKATGKPLKMRIDAMNGVTGSYVREIF----LNR 240
Cdd:PTZ00150 186 ---EPWSSSWEYLTETlVEDPLA-------EVSDayFATLKsEYNPACCDRSKVKIVYTAMHGVGTRFVQKALhtvgLPN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 241 LGATESSVvhtTPLPDFGGL-HPDPN-----LTYAKDLVDTVAQGdydIGAAFDGDGDRNMIIGSKA--FFVTPSDSLAV 312
Cdd:PTZ00150 256 LLSVAQQA---EPDPEFPTVtFPNPEegkgaLKLSMETAEAHGST---VVLANDPDADRLAVAEKLNngWKIFTGNELGA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 313 IAHYLEAIPYFQKNGVQG---FARSMPTASAVDLVGRKLGKEVFEVPTGWKYFGN----LMDAG--RLCLCGEESFGTG- 382
Cdd:PTZ00150 330 LLAWWAMKRYRRQGIDKSkcfFICTVVSSRMLKKMAEKEGFQYDETLTGFKWIGNkaieLNAENglTTLFAYEEAIGFMl 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 383 SNHIREKDGIWAVLAWISV---MQHTGKGIEDILKQHWSVYGRnYFTRYDYEECaSDPcNEMVATMEKTITApefvGKSY 459
Cdd:PTZ00150 410 GTRVRDKDGVTAAAVVAEMalyLYERGKTLVEHLESLYKQYGY-HFTNNSYYIC-YDP-SRIVSIFNDIRNN----GSYP 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 12006791 460 SSGGKtYKVKE----ADNFSYTDPVDKSV----ATKQGLRIVFEDGSRIVVRLSGT 507
Cdd:PTZ00150 483 TKLGG-YPVTRirdlTTGYDTATPDGKPLlpvsASTQMITFYFENGAIITIRGSGT 537
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
36-314 |
4.34e-11 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 65.00 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 36 TENFVQAIleanGAALA-------GSTLVVGGDGRFYCKEAAELIVRLSAANGVSkllVGQNGILSTPAV---SSLIRhn 105
Cdd:PRK09542 15 DEDLVRDV----GAAFArlmraegATTVVIGHDMRDSSPELAAAFAEGVTAQGLD---VVRIGLASTDQLyfaSGLLD-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 106 kaLGGIVLTASHNPggPENDfGIKFnCEnGGPAPdaftnhIYKIT--TEIKeyklvrnlqiDISKVGVTSFDiaGKPFTV 183
Cdd:PRK09542 86 --CPGAMFTASHNP--AAYN-GIKL-CR-AGAKP------VGQDTglAAIR----------DDLIAGVPAYD--GPPGTV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 184 EVIDSVANYVRHMEEIFDFAKLKdfvsgkatgkPLKMRIDAMNGVTGSYVREIFlnrlGATESSVVhttPLP-DFGGLHP 262
Cdd:PRK09542 141 TERDVLADYAAFLRSLVDLSGIR----------PLKVAVDAGNGMGGHTVPAVL----GGLPITLL---PLYfELDGTFP 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12006791 263 -------DPnltyaKDLVD----TVAQGDyDIGAAFDGDGDRNMIIGSKAFFVTPSDSLAVIA 314
Cdd:PRK09542 204 nheanplDP-----ANLVDlqafVRETGA-DIGLAFDGDADRCFVVDERGQPVSPSAVTALVA 260
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
19-414 |
3.08e-09 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 59.38 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 19 GTSGLRKKVKVFtqpNYTENFVQAILEANGAALAGS---TLVVGGDGRF--YCKEAAeLIVRLSAAnGVSKLLVGQngiL 93
Cdd:PRK10887 5 GTDGIRGKVGQA---PITPDFVLKLGWAAGKVLARQgrpKVLIGKDTRIsgYMLESA-LEAGLAAA-GVDVLLTGP---M 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 94 STPAVSSLIRHNKALGGIVLTASHNpggPENDFGIKFNCENGGPAPDAFTNHIykitteikEYKLVRNLQIdiskvgVTS 173
Cdd:PRK10887 77 PTPAVAYLTRTLRAEAGIVISASHN---PYYDNGIKFFSADGTKLPDEVELAI--------EAELDKPLTC------VES 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 174 FDIaGKpfTVEVIDSVANYVrhmeeifDFAKlKDFVSGkATGKPLKMRIDAMNGVT----GSYVREiflnrLGAtESSVV 249
Cdd:PRK10887 140 AEL-GK--ASRINDAAGRYI-------EFCK-STFPNE-LSLRGLKIVVDCANGATyhiaPNVFRE-----LGA-EVIAI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 250 HTTplPD-------FGGLHPdpnltyaKDLVDTVAQGDYDIGAAFDGDGDRNMIIGSKAFFVTPSDSLAVIA-HYLEAIP 321
Cdd:PRK10887 202 GCE--PNglnindeCGATDP-------EALQAAVLAEKADLGIAFDGDGDRVIMVDHLGNLVDGDQLLYIIArDRLRRGQ 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 322 yfQKNGVQGfaRSMpTASAVDLVGRKLGKEVFEVPTGWKYFGNLMDAGRLCLCGEesfgtGSNHI--REK----DGIWAV 395
Cdd:PRK10887 273 --LRGGVVG--TLM-SNMGLELALKQLGIPFVRAKVGDRYVLEKLQEKGWRLGGE-----NSGHIlcLDKtttgDGIVAA 342
|
410
....*....|....*....
gi 12006791 396 LAWISVMQHTGKGIEDILK 414
Cdd:PRK10887 343 LQVLAAMVRSGMSLADLCS 361
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
37-321 |
5.14e-09 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 58.80 E-value: 5.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 37 ENFVQAILEANGAALAGSTLVVGGDGRFyCKEAAELIVRLSAAN-GVSKLLVGQNGilsTPAVSSLIRHNKALGGIVLTA 115
Cdd:PRK15414 22 EDIAWRIGRAYGEFLKPKTIVLGGDVRL-TSETLKLALAKGLQDaGVDVLDIGMSG---TEEIYFATFHLGVDGGIEVTA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 116 SHNPggpeNDF-GIKFNCENGGP-APDAFTNHIYKITTE-----IKEYKLVRNLQIDISKVgvtsfdiagkpftvevids 188
Cdd:PRK15414 98 SHNP----MDYnGMKLVREGARPiSGDTGLRDVQRLAEAndfppVDETKRGRYQQINLRDA------------------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 189 vanYVRHMEEIFDFAKLKdfvsgkatgkPLKMRIDAMNGVTGSYVR--EIFLNRLGA-TESSVVHTTPLPDFGGLHPDPN 265
Cdd:PRK15414 155 ---YVDHLFGYINVKNLT----------PLKLVINSGNGAAGPVVDaiEARFKALGApVELIKVHNTPDGNFPNGIPNPL 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 266 LTYAKDlvDT---VAQGDYDIGAAFDGDGDRNMIIGSKAFFVTPSDSLAVIAH-YLEAIP 321
Cdd:PRK15414 222 LPECRD--DTrnaVIKHGADMGIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEaFLEKNP 279
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
33-300 |
2.52e-06 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 50.44 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 33 PNYTENFVQAILEANGAALAGS---------TLVVGGDGRFyckEAAELIVRLSAANGVSKLLVGQNGILSTPAV--SSL 101
Cdd:PLN02371 86 VTLTPPAVEAIGAAFAEWLLEKkkadgsgelRVSVGRDPRI---SGPRLADAVFAGLASAGLDVVDMGLATTPAMfmSTL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 102 IRHNKALGGIVLTASHNPggpENDFGIKFNCENGG-PAPDaftnhIYKI-TTEIKEYKLVRNLQIDISKvgvtsfdiAGK 179
Cdd:PLN02371 163 TEREDYDAPIMITASHLP---YNRNGLKFFTKDGGlGKPD-----IKDIlERAARIYKEWSDEGLLKSS--------SGA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12006791 180 PFTVEVIDSVANYVRHMEEIfdfakLKDFVSGKATG-KPLK-MRI--DAMNGVTGSYVREIfLNRLGATESSVVHTTPLP 255
Cdd:PLN02371 227 SSVVCRVDFMSTYAKHLRDA-----IKEGVGHPTNYeTPLEgFKIvvDAGNGAGGFFAEKV-LEPLGADTSGSLFLEPDG 300
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 12006791 256 DFGGLHPDPNLTYAKDL-VDTVAQGDYDIGAAFDGDGDRNMIIGSK 300
Cdd:PLN02371 301 MFPNHIPNPEDKAAMSAtTQAVLANKADLGIIFDTDVDRSAVVDSS 346
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
467-524 |
3.14e-05 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 42.26 E-value: 3.14e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 12006791 467 KVKEADNFSYTDPVDKSVATKQGLRIVFEDGSRIVVRLSGTGSSgatVRLYIDSYEKE 524
Cdd:pfam00408 3 NVRVAEKKKLAALAAILKVFADAEKILGEDGRRLDVRPSGTEPV---LRVMVEGDSDE 57
|
|
| |
