|
Name |
Accession |
Description |
Interval |
E-value |
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
92-600 |
0e+00 |
|
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: 606.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 92 LTFGTAGIRGKFGLGEGRLNKFTIEKLALGLARYLNAQTN---SPTIVIHYDIRHLSTEFAQIIANVLANHQITVYLPDT 168
Cdd:cd05799 2 LEFGTAGLRGKMGAGTNRMNDYTVRQATQGLANYLKKKGPdakNRGVVIGYDSRHNSREFAELTAAVLAANGIKVYLFDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 169 YKTTPELSFAVRNLNTTAGIMITASHNPKDYNGIKVYGSDGAQLSTDASELASRYIEEVGDPLQIDIPISKQNtSYIKPF 248
Cdd:cd05799 82 LRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAVLEPLDIKFEEALDS-GLIKYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 249 PKSVTDDYMKHIQNMIGY---IPKSDLQVVFTSLHGTSVPIVPELLQSLNFNQFNLVEAQCKPDPNFSSVQSANPEDHRA 325
Cdd:cd05799 161 GEEIDDAYLEAVKKLLVNpelNEGKDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVVEEQAEPDPDFPTVKFPNPEEPGA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 326 FDQAVELANKSHADLLISTDPDADRLGIAERDAHGHITYFNGNQIGALLLNYRIQQTSQLR----HRLMIQSIVSSELTK 401
Cdd:cd05799 241 LDLAIELAKKVGADLILATDPDADRLGVAVKDKDGEWRLLTGNEIGALLADYLLEQRKEKGklpkNPVIVKTIVSSELLR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 402 SLARYNNVEYKEVLTGFKFIAQEIRQLD-DHQNMIFAFEESYGFLSEPFVRDKDAVQIVPLIIKYASELKLYGKTLKDEL 480
Cdd:cd05799 321 KIAKKYGVKVEETLTGFKWIGNKIEELEsGGKKFLFGFEESIGYLVGPFVRDKDGISAAALLAEMAAYLKAQGKTLLDRL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 481 EQIYQTVGRHEDTLFSHTLDGLEGKKKIESIMTHFRSNPpqeiqglkvkaiedyltsevyhldkdttsqinspksNVIRV 560
Cdd:cd05799 401 DELYEKYGYYKEKTISITFEGKEGPEKIKAIMDRLRNNP------------------------------------NVLTF 444
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 487709087 561 LFDEG-FIALRPSGTEPKIKLYVSLKCR-NFDDVAQKINAMI 600
Cdd:cd05799 445 YLEDGsRVTVRPSGTEPKIKFYIEVVGKkTLEEAEKKLDALK 486
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
83-600 |
1.36e-112 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 348.60 E-value: 1.36e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 83 EQREGFESKLTFGTAGIRGKFGLGEGRLNKFTIEKLALGLARYLNAQTN----SPTIVIHYDIRHLSTEFAQIIANVLAN 158
Cdd:PTZ00150 36 ELKRRFLKRMEFGTAGLRGKMGAGFNCMNDLTVQQTAQGLCAYVIETFGqalkSRGVVIGYDGRYHSRRFAEITASVFLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 159 HQITVYLPDTYKTTPELSFAVRNLNTTAGIMITASHNPKDYNGIKVYGSDGAQLSTDASELASRYIEEVGDPL-QIDIPI 237
Cdd:PTZ00150 116 KGFKVYLFGQTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVYWSNGAQIIPPHDKNISAKILSNLEPWsSSWEYL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 238 SKqnTSYIKPFpKSVTDDYMKHIqnMIGYIP----KSDLQVVFTSLHGTSVPIVPELLQSLNFNQFNLVEAQCKPDPNFS 313
Cdd:PTZ00150 196 TE--TLVEDPL-AEVSDAYFATL--KSEYNPaccdRSKVKIVYTAMHGVGTRFVQKALHTVGLPNLLSVAQQAEPDPEFP 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 314 SVQSANPEDHR-AFDQAVELANKSHADLLISTDPDADRLGIAERDAHG-HItyFNGNQIGALL----LNYRIQQTSQLRH 387
Cdd:PTZ00150 271 TVTFPNPEEGKgALKLSMETAEAHGSTVVLANDPDADRLAVAEKLNNGwKI--FTGNELGALLawwaMKRYRRQGIDKSK 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 388 RLMIQSIVSSELTKSLARYNNVEYKEVLTGFKFI---AQEIRQlDDHQNMIFAFEESYGFLSEPFVRDKDAVQIVPLIIK 464
Cdd:PTZ00150 349 CFFICTVVSSRMLKKMAEKEGFQYDETLTGFKWIgnkAIELNA-ENGLTTLFAYEEAIGFMLGTRVRDKDGVTAAAVVAE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 465 YASELKLYGKTLKDELEQIYQTVGRHedtlFSH-----TLDglegKKKIESIMTHFRSNP--PQEIQGLKVKAIEDyLTS 537
Cdd:PTZ00150 428 MALYLYERGKTLVEHLESLYKQYGYH----FTNnsyyiCYD----PSRIVSIFNDIRNNGsyPTKLGGYPVTRIRD-LTT 498
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487709087 538 EVYHLDKDTTSQIN-SPKSNVIRVLFDEGFIA-LRPSGTEPKIKLYVSLKCRNFDDVAQKINAMI 600
Cdd:PTZ00150 499 GYDTATPDGKPLLPvSASTQMITFYFENGAIItIRGSGTEPKLKWYAELSGTKDEAVEKELAALV 563
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
94-600 |
3.62e-111 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 340.64 E-value: 3.62e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 94 FGTAGIRGKFGLGegrLNKFTIEKLALGLARYLnAQTNSPTIVIHYDIRHLSTEFAQIIANVLANHQITVYLPDtYKTTP 173
Cdd:COG1109 7 FGTDGIRGIVGEE---LTPEFVLKLGRAFGTYL-KEKGGPKVVVGRDTRLSSPMLARALAAGLASAGIDVYDLG-LVPTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 174 ELSFAVRNLNTTAGIMITASHNPKDYNGIKVYGSDGAQLSTD-ASELASRYIEEvgdplQIDIPISKQNTSYIKpfPKSV 252
Cdd:COG1109 82 ALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEeEKEIEALIEKE-----DFRRAEAEEIGKVTR--IEDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 253 TDDYMKHIQNMIGY-IPKSDLQVVFTSLHGTSVPIVPELLQSLNfnqFNLVEAQCKPDPNFSSVqSANPEdHRAFDQAVE 331
Cdd:COG1109 155 LEAYIEALKSLVDEaLRLRGLKVVVDCGNGAAGGVAPRLLRELG---AEVIVLNAEPDGNFPNH-NPNPE-PENLEDLIE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 332 LANKSHADLLISTDPDADRLGIAerDAHGHItyFNGNQIGALLLNYRIQQTsqlRHRLMIQSIVSSELTKSLARYNNVEY 411
Cdd:COG1109 230 AVKETGADLGIAFDGDADRLGVV--DEKGRF--LDGDQLLALLARYLLEKG---PGGTVVVTVMSSLALEDIAEKHGGEV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 412 KEVLTGFKFIAQEIRQLddhqNMIFAFEESYGFLSEPFVRDKDAVQIVPLIIKYASElklYGKTLKDELEQIyqtvGRHE 491
Cdd:COG1109 303 VRTKVGFKYIKEKMRET----GAVLGGEESGGIIFPDFVPTDDGILAALLLLELLAK---QGKSLSELLAEL----PRYP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 492 DTLFSHTldgLEGKKKIESIMTHFRSnppqeiqglKVKAIEDYltsevyhldkdttsqinsPKSNVIRVLF-DEGFIALR 570
Cdd:COG1109 372 QPEINVR---VPDEEKIGAVMEKLRE---------AVEDKEEL------------------DTIDGVKVDLeDGGWVLVR 421
|
490 500 510
....*....|....*....|....*....|....*
gi 487709087 571 PSGTEPKIKLYVSLKCRN-----FDDVAQKINAMI 600
Cdd:COG1109 422 PSGTEPLLRVYAEAKDEEeaeelLAELAELVEEAL 456
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
93-582 |
1.39e-72 |
|
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily and is found in both archaea and bacteria. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four structural domains (subdomains) with a centrally located active site formed by four loops, one from each subdomain. All four subdomains are included in this alignment model.
Pssm-ID: 100093 Cd Length: 461 Bit Score: 240.15 E-value: 1.39e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 93 TFGTAGIRGKfgLGEGrlnkFT---IEKLALGLARYLNA-QTNSPTIVIHYDIRHLSTEFAQIIANVLANHQITVYLPDT 168
Cdd:cd05800 2 KFGTDGWRGI--IAED----FTfenVRRVAQAIADYLKEeGGGGRGVVVGYDTRFLSEEFARAVAEVLAANGIDVYLSDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 169 YKTTPELSFAVRNLNTTAGIMITASHNPKDYNGIKVYGSDGAQLSTDASELASRYIEEVGDPLQIDIPISKqnTSYIKPF 248
Cdd:cd05800 76 PVPTPAVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARLASGEPPGLEARAEGL--IETIDPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 249 PksvtdDYMKHIQNMIG--YIPKSDLQVVFTSLHGTSVPIVPELLQSLNfnqFNLVEAQCKPDPNFSSVqsaNPE-DHRA 325
Cdd:cd05800 154 P-----DYLEALRSLVDleAIREAGLKVVVDPMYGAGAGYLEELLRGAG---VDVEEIRAERDPLFGGI---PPEpIEKN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 326 FDQAVELANKSHADLLISTDPDADRLGIAerDAHGHitYFNGNQIGALLLNYRIqQTSQLRHRLmIQSIVSSELTKSLAR 405
Cdd:cd05800 223 LGELAEAVKEGGADLGLATDGDADRIGAV--DEKGN--FLDPNQILALLLDYLL-ENKGLRGPV-VKTVSTTHLIDRIAE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 406 YNNVEYKEVLTGFKFIAQEIRQlddhQNMIFAFEESYGFLSEPFVRDKDAVQIVPLIIKYASElklYGKTLKDELEQIYQ 485
Cdd:cd05800 297 KHGLPVYETPVGFKYIAEKMLE----EDVLIGGEESGGLGIRGHIPERDGILAGLLLLEAVAK---TGKPLSELVAELEE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 486 TVGRHEDTLFSHTLDglEGKKkiESIMTHFRSNPPQEIQGLKVKAIEDyltsevyhldkdttsqinspKSNVIRVLFDEG 565
Cdd:cd05800 370 EYGPSYYDRIDLRLT--PAQK--EAILEKLKNEPPLSIAGGKVDEVNT--------------------IDGVKLVLEDGS 425
|
490
....*....|....*..
gi 487709087 566 FIALRPSGTEPKIKLYV 582
Cdd:cd05800 426 WLLIRPSGTEPLLRIYA 442
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
91-226 |
8.27e-50 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 168.94 E-value: 8.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 91 KLTFGTAGIRGKFGLGEgrLNKFTIEKLALGLARYLNAQTNSPTIVIHYDIRHLSTEFAQIIANVLANHQITVYLPDtYK 170
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGE--LTPEFALKLGQAIASYLRAQGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVILLG-LL 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 487709087 171 TTPELSFAVRNLNTTAGIMITASHNPKDYNGIKVYGSDGAQLSTDASELASRYIEE 226
Cdd:pfam02878 78 PTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEK 133
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
184-486 |
1.60e-41 |
|
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: 153.67 E-value: 1.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 184 TTAGIMITASHNPKDYNGIKVYGSDGAQLSTDASELASRYIEEVGDPLQIDIPISKQNtsyikpFPKSVTDDYMKHIQNM 263
Cdd:cd03084 29 STGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSAVAYELGGSV------KAVDILQRYFEALKKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 264 I--GYIPKSDLQVVFTSLHGTSVPIVPELLQSLNfnqFNLVEAQCKPDPNFSsvqSANPEDHRAFD--QAVELANKSHAD 339
Cdd:cd03084 103 FdvAALSNKKFKVVVDSVNGVGGPIAPQLLEKLG---AEVIPLNCEPDGNFG---NINPDPGSETNlkQLLAVVKAEKAD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 340 LLISTDPDADRLGIAERDAhghiTYFNGNQIGALLLNYRIQQtSQLRHRlMIQSIVSSELTKSLARYNNVEYKEVLTGFK 419
Cdd:cd03084 177 FGVAFDGDADRLIVVDENG----GFLDGDELLALLAVELFLT-FNPRGG-VVKTVVSSGALDKVAKKLGIKVIRTKTGFK 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487709087 420 FIAQEIRQlddhQNMIFAFEESYGFLSEPFVRDKDAVQIVPLIIKYASELKLYGKTLKDELEQIYQT 486
Cdd:cd03084 251 WVGEAMQE----GDVVLGGEESGGVIFPEFHPGRDGISAALLLLEILANLGKSLSELFSELPRYYYI 313
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
99-580 |
5.15e-38 |
|
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: 146.12 E-value: 5.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 99 IRGKFGlgeGRLNKFTIEKLALGLARYLNAQTNsPTIVIHYDIRHLSTEFAQIIANVLANHQITVYL----PdtyktTPE 174
Cdd:cd03089 7 IRGIAG---EELTEEIAYAIGRAFGSWLLEKGA-KKVVVGRDGRLSSPELAAALIEGLLAAGCDVIDiglvP-----TPV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 175 LSFAVRNLNTTAGIMITASHNPKDYNGIKVYGSDGAQLSTDASELASRYieevgdpLQIDIPISKQNTSYIKpfpKSVTD 254
Cdd:cd03089 78 LYFATFHLDADGGVMITASHNPPEYNGFKIVIGGGPLSGEDIQALRERA-------EKGDFAAATGRGSVEK---VDILP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 255 DYMKHIQNMIGyIPKSDLQVVFTSLHGTSVPIVPELLQSLNFNqfnlVEAQ-CKPDPNFSSvQSANPEDHRAFDQAVELA 333
Cdd:cd03089 148 DYIDRLLSDIK-LGKRPLKVVVDAGNGAAGPIAPQLLEALGCE----VIPLfCEPDGTFPN-HHPDPTDPENLEDLIAAV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 334 NKSHADLLISTDPDADRLGIAerDAHGHItyFNGNQIGALLLnyriqqtsqlrhRLMIQS------IVSSELTKSLARY- 406
Cdd:cd03089 222 KENGADLGIAFDGDGDRLGVV--DEKGEI--IWGDRLLALFA------------RDILKRnpgatiVYDVKCSRNLYDFi 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 407 -----NNVEYKevlTGFKFIAQEIRQLddhqNMIFAFEES-YGFLSEPFVRDKDAVQIVPLIIKYASELklyGKTLKDEL 480
Cdd:cd03089 286 eeaggKPIMWK---TGHSFIKAKMKET----GALLAGEMSgHIFFKDRWYGFDDGIYAALRLLELLSKS---GKTLSELL 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 481 EQIYQTVGRHEdtlFSHTLDGLEGKKKIESIMTHFRSNPPqeiqglkvkaiedyltsEVYHLDKdttsqinspksnvIRV 560
Cdd:cd03089 356 ADLPKYFSTPE---IRIPVTEEDKFAVIERLKEHFEFPGA-----------------EIIDIDG-------------VRV 402
|
490 500
....*....|....*....|
gi 487709087 561 LFDEGFIALRPSGTEPKIKL 580
Cdd:cd03089 403 DFEDGWGLVRASNTEPVLVL 422
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
91-582 |
9.29e-37 |
|
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: 142.27 E-value: 9.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 91 KLTFGTAGIRGKFGlgEGrLNKFTIEKLALGLARYLNAqtnsPTIVIHYDIRhLSTE-FAQIIANVLANHQITVYLPDtY 169
Cdd:TIGR03990 1 MLLFGTSGIRGIVG--EE-LTPELALKVGKAFGTYLRG----GKVVVGRDTR-TSGPmLENAVIAGLLSTGCDVVDLG-I 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 170 KTTPELSFAVRNLNTTAGIMITASHNPKDYNGIKVYGSDGAQLSTDA-SELASRYIEEVGDPLQIDipiskqNTSYIKPF 248
Cdd:TIGR03990 72 APTPTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQeEEIEEIAESGDFERADWD------EIGTVTSD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 249 PkSVTDDYMKHIQNMIG--YIPKSDLQVVFTSLHGTSVPIVPELLQSLNFNQFNLveaQCKPDPNFSsvqSANPE---DH 323
Cdd:TIGR03990 146 E-DAIDDYIEAILDKVDveAIRKKGFKVVVDCGNGAGSLTTPYLLRELGCKVITL---NCQPDGTFP---GRNPEptpEN 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 324 RAfdQAVELANKSHADLLISTDPDADRLGIAerDAHGhiTYFNGNQIGALLLNYRIQQTSqlrhrlmiQSIV----SSEL 399
Cdd:TIGR03990 219 LK--DLSALVKATGADLGIAHDGDADRLVFI--DEKG--RFIGGDYTLALFAKYLLEHGG--------GKVVtnvsSSRA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 400 TKSLARYNNVEYkeVLT--GFKFIAQEIRQLDDhqnmIFAFEESYGFLSEPFVRDKDAVQIVPLIIKYASElklYGKTLK 477
Cdd:TIGR03990 285 VEDVAERHGGEV--IRTkvGEVNVAEKMKEEGA----VFGGEGNGGWIFPDHHYCRDGLMAAALFLELLAE---EGKPLS 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 478 DELEQI--YQTVgrhedtlfshtldglegKKKIesimthfrsnppqEIQGLKVKAIEDYLTSEVYHLDKDTTSQinspks 555
Cdd:TIGR03990 356 ELLAELpkYPMS-----------------KEKV-------------ELPDEDKEEVMEAVEEEFADAEIDTIDG------ 399
|
490 500
....*....|....*....|....*..
gi 487709087 556 nvIRVLFDEGFIALRPSGTEPKIKLYV 582
Cdd:TIGR03990 400 --VRIDFEDGWVLVRPSGTEPIVRIYA 424
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
94-582 |
8.93e-35 |
|
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: 136.55 E-value: 8.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 94 FGTAGIRGKFGlgegrlNKFTIE---KLALGLARYLNAqtnsPTIVIHYDIRHLSTEFAQIIANVLANHQITVY----LP 166
Cdd:cd03087 2 FGTSGIRGVVG------EELTPElalKVGKALGTYLGG----GTVVVGRDTRTSGPMLKNAVIAGLLSAGCDVIdigiVP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 167 dtyktTPELSFAVRNLNTtAGIMITASHNPKDYNGIKVYGSDGAQLSTDA-SELASRYIEEVGDPlqidIPISKQNTSYI 245
Cdd:cd03087 72 -----TPALQYAVRKLGD-AGVMITASHNPPEYNGIKLVNPDGTEFSREQeEEIEEIIFSERFRR----VAWDEVGSVRR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 246 kpfPKSVTDDYMKHIQNMIGYIPKSDLQVVFTSLHGTSVPIVPELLQSLNFNQFNLveaQCKPDPNFSSVQS-ANPEDHR 324
Cdd:cd03087 142 ---EDSAIDEYIEAILDKVDIDGGKGLKVVVDCGNGAGSLTTPYLLRELGCKVITL---NANPDGFFPGRPPePTPENLS 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 325 AFDQAVElanKSHADLLISTDPDADRLGIAerDAHGhiTYFNGNQIGALLLNYRIQQTSQLrhrlmiqsIV-----SSEL 399
Cdd:cd03087 216 ELMELVR---ATGADLGIAHDGDADRAVFV--DEKG--RFIDGDKLLALLAKYLLEEGGGK--------VVtpvdaSMLV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 400 TKSLARYN-NVEYKEVltGFKFIAQEIRQlddhQNMIFAFEESYGFLSEPFVRDKDAVQIVPLIIKYASElklyGKTLKD 478
Cdd:cd03087 281 EDVVEEAGgEVIRTPV--GDVHVAEEMIE----NGAVFGGEPNGGWIFPDHQLCRDGIMTAALLLELLAE----EKPLSE 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 479 ELEQI--YQTVgrhedtlfshtldglegKKKIESimthfrsnpPQEIQGLKVKAIEDYLTSEVYhlDKDTTSQinspksn 556
Cdd:cd03087 351 LLDELpkYPLL-----------------REKVEC---------PDEKKEEVMEAVEEELSDADE--DVDTIDG------- 395
|
490 500
....*....|....*....|....*.
gi 487709087 557 vIRVLFDEGFIALRPSGTEPKIKLYV 582
Cdd:cd03087 396 -VRIEYEDGWVLIRPSGTEPKIRITA 420
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
255-355 |
2.88e-28 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 108.53 E-value: 2.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 255 DYMKHIQNMIG--YIPKSDLQVVFTSLHGTSVPIVPELLQSLNFNqfnLVEAQCKPDPNFSSvQSANPEDHRAFDQAVEL 332
Cdd:pfam02879 1 AYIDHLLELVDseALKKRGLKVVYDPLHGVGGGYLPELLKRLGCD---VVEENCEPDPDFPT-RAPNPEEPEALALLIEL 76
|
90 100
....*....|....*....|...
gi 487709087 333 ANKSHADLLISTDPDADRLGIAE 355
Cdd:pfam02879 77 VKSVGADLGIATDGDADRLGVVD 99
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
94-578 |
1.99e-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: 103.33 E-value: 1.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 94 FGTAGIRGKFGLGegrLNKFTIEKLALGLARYLNAQTNSPTIVIHYDIRHLSTEFAQIIANVLANHQITVYL----Pdty 169
Cdd:cd05802 2 FGTDGIRGVANEP---LTPELALKLGRAAGKVLGKGGGRPKVLIGKDTRISGYMLESALAAGLTSAGVDVLLlgviP--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 170 ktTPELSFAVRNLNTTAGIMITASHNPKDYNGIKVYGSDGAQLStDASELAsryIEE-VGDPLQIDIPISKQNTSYIKPF 248
Cdd:cd05802 76 --TPAVAYLTRKLRADAGVVISASHNPFEDNGIKFFSSDGYKLP-DEVEEE---IEAlIDKELELPPTGEKIGRVYRIDD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 249 PKsvtDDYMKHIQNMIGYIPKSDLQVVFTSLHGTSVPIVPELLQSLNfnqFNLVEAQCKPDP---NfSSVQSANPEdhra 325
Cdd:cd05802 150 AR---GRYIEFLKSTFPKDLLSGLKIVLDCANGAAYKVAPEVFRELG---AEVIVINNAPDGlniN-VNCGSTHPE---- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 326 fdQAVELANKSHADLLISTDPDADRLgIAErDAHGHItyFNGNQIGALLLNYRiqqtsQLRHRLMIQSIVSSE-----LT 400
Cdd:cd05802 219 --SLQKAVLENGADLGIAFDGDADRV-IAV-DEKGNI--VDGDQILAICARDL-----KERGRLKGNTVVGTVmsnlgLE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 401 KSLARyNNVEYKEVLTGFKFIAQEIRQLD--------DHqnMIFafeesygflsepfvRDKD--------AVQIVpliik 464
Cdd:cd05802 288 KALKE-LGIKLVRTKVGDRYVLEEMLKHGanlggeqsGH--IIF--------------LDHSttgdglltALQLL----- 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 465 yaSELKLYGKTLKDELEQIyqtvgrhedTLFSHTLDGLEGKKKiesimthfrsNPPQEIQGLKvKAIEDyltsevyhldk 544
Cdd:cd05802 346 --AIMKRSGKSLSELASDM---------KLYPQVLVNVRVKDK----------KALLENPRVQ-AAIAE----------- 392
|
490 500 510
....*....|....*....|....*....|....
gi 487709087 545 dttsqinspksnVIRVLFDEGFIALRPSGTEPKI 578
Cdd:cd05802 393 ------------AEKELGGEGRVLVRPSGTEPLI 414
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
98-353 |
4.41e-22 |
|
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: 99.30 E-value: 4.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 98 GIRGKfgLGEGrLNKFTIEKLALGLARYLNAQTNSPTIVIHYDIRHLSTEFAQIIANVLANHQITVYLPDTyKTTPELSF 177
Cdd:cd05803 6 GIRGI--VGEG-LTPEVITRYVAAFATWQPERTKGGKIVVGRDGRPSGPMLEKIVIGALLACGCDVIDLGI-APTPTVQV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 178 AVRNLNTTAGIMITASHNPKDYNGIKVYGSDGAQLS-TDASELASRYIEEVGDPLQIDIPISKQNTSyikpfpkSVTDDY 256
Cdd:cd05803 82 LVRQSQASGGIIITASHNPPQWNGLKFIGPDGEFLTpDEGEEVLSCAEAGSAQKAGYDQLGEVTFSE-------DAIAEH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 257 MKHI-----QNMIGyIPKSDLQVVFTSLHGTSVPIVPELLQSLNfnqFNLVEAQCKPDPNFSSVQSANPEDHRAFDQAVE 331
Cdd:cd05803 155 IDKVlalvdVDVIK-IRERNFKVAVDSVNGAGGLLIPRLLEKLG---CEVIVLNCEPTGLFPHTPEPLPENLTQLCAAVK 230
|
250 260
....*....|....*....|..
gi 487709087 332 lanKSHADLLISTDPDADRLGI 353
Cdd:cd05803 231 ---ESGADVGFAVDPDADRLAL 249
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
94-396 |
3.11e-21 |
|
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: 96.67 E-value: 3.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 94 FGTAGIRGKfgLGEGRLNKFTIEKLALGLARYLNAQ-TNSPTIVIHYDIRHLSTEFAQIIANVLANHQITVY----LPdt 168
Cdd:TIGR01455 1 FGTDGVRGR--AGQEPLTAELALLLGAAAGRVLRQGrDTAPRVVIGKDTRLSGYMLENALAAGLNSAGVDVLllgpLP-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 169 yktTPELSFAVRNLNTTAGIMITASHNPKDYNGIKVYGSDGAQLStDASELAsryIEevgDPLQIDIPISKQNTSYIKPF 248
Cdd:TIGR01455 77 ---TPAVAYLTRTLRADAGVMISASHNPYEDNGIKFFGPGGFKLD-DATEAA---IE---ALLDEADPLPRPESEGLGRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 249 pKSVTDDYMKHIQNMIGYIPK----SDLQVVFTSLHGTSVPIVPELLQSLNfnqFNLVEAQCKPDP-NFS-SVQSANPED 322
Cdd:TIGR01455 147 -KRYPDAVGRYIEFLKSTLPRgltlSGLKVVLDCANGAAYKVAPHVFRELG---AEVIAIGVEPDGlNINdGCGSTHLDA 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487709087 323 HRAfdqAVElanKSHADLLISTDPDADRLGIAerDAHGHITyfNGNQIGALLLNYRiQQTSQLRHRLMIQSIVS 396
Cdd:TIGR01455 223 LQK---AVR---EHGADLGIAFDGDADRVLAV--DANGRIV--DGDQILYIIARAL-KESGELAGNTVVATVMS 285
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
69-581 |
7.99e-21 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 96.36 E-value: 7.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 69 DSLVKHFYEQQSDIEQREgfeSKLTFGTAGIRGKfglgeGRLNKFT---IEKLALGLARYLNAQTNSPTIVIHYDIRHLS 145
Cdd:PRK07564 18 PRLVSAYYTLKPDPTNPF---QDVKFGTSGHRGS-----SLQPSFNenhILAIFQAICEYRGKQGITGPLFVGGDTHALS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 146 TEFAQIIANVLANHQITV-------YLPdtyktTPELSFAVRNLNTTA-----GIMITASHNPKDYNGIKVYGSDGAQLS 213
Cdd:PRK07564 90 EPAIQSALEVLAANGVGVvivgrggYTP-----TPAVSHAILKYNGRGggladGIVITPSHNPPEDGGIKYNPPNGGPAD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 214 TD--------ASELASRYIEEVGdplqiDIPISKQNTS-------YIKPFpksVTDdyMKHIQNMiGYIPKSDLQVVFTS 278
Cdd:PRK07564 165 TDvtdaiearANELLAYGLKGVK-----RIPLDRALASmtvevidPVADY---VED--LENVFDF-DAIRKAGLRLGVDP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 279 LHGTSVPIVPELLQSLNFNQfNLVEAqcKPDPNFSSVqsanPEDH----R-----AFDQAVELANKSHADLLISTDPDAD 349
Cdd:PRK07564 234 LGGATGPYWKAIAERYGLDL-TVVNA--PVDPTFNFM----PLDDdgkiRmdcssPYAMAGLLALKDAFDLAFANDPDGD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 350 RLGIAERdaHGhitYFNGNQIGALLLNYRIQQTSQLRHRLMI-QSIVSSELTKSLARYNNVEYKEVLTGFKFIAQeirQL 428
Cdd:PRK07564 307 RHGIVTP--GG---LMNPNHYLAVAIAYLFHHRPGWRAGAGVgKTLVSSAMIDRVAAKLGRKLYEVPVGFKWFVN---GL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 429 DDhqNMI-FAFEESYG--FLSE---PFVRDKDAVQIVPLiikyASElkLYGKTLKDeLEQIYQ----TVGRH-------E 491
Cdd:PRK07564 379 DD--GSLgFGGEESAGasFLRRdgsVWTTDKDGLIAVLL----AAE--ILAVTGKS-PSEIYRelwaRFGRPyysrhdaP 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 492 DTlfshtldgLEGKKKIESI------MTHFRSNPpqeiqglkvkaIEDYLtsevyhldkdTTSQINSPKSNVIRVLFDEG 565
Cdd:PRK07564 450 AT--------PEQKAALRKLspelvgATELAGDP-----------IDASL----------TEAPGNGAAIGGLKVVTENG 500
|
570
....*....|....*.
gi 487709087 566 FIALRPSGTEPKIKLY 581
Cdd:PRK07564 501 WFAARPSGTETTYKIY 516
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
69-581 |
5.17e-19 |
|
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: 90.38 E-value: 5.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 69 DSLVKHFYEQQSDIEQREgfeSKLTFGTAGIRGKFGLGEgrLNKFTIEKLALGLARYLNAQTNSPTIVIHYDIRHLStEF 148
Cdd:cd05801 1 PRLITAYYTLKPDPSNPA---QRVAFGTSGHRGSSLKGS--FNEAHILAISQAICDYRKSQGITGPLFLGKDTHALS-EP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 149 AQIIA-NVLANHQITVYLP--DTYKTTPELSFAVRNLNTTA------GIMITASHNPKDYNGIKVYGSDGAQLSTDasel 219
Cdd:cd05801 75 AFISAlEVLAANGVEVIIQqnDGYTPTPVISHAILTYNRGRtegladGIVITPSHNPPEDGGFKYNPPHGGPADTD---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 220 ASRYIEE-----VGDPLQIDIPISKQN---TSYIKPFpksvtdDYMKHIQNMIGYIpkSDLQVVFTS--------LHGTS 283
Cdd:cd05801 151 ITRWIEKranalLANGLKGVKRIPLEAalaSGYTHRH------DFVTPYVADLGNV--IDMDAIRKSglrlgvdpLGGAS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 284 VPIVPELLQSLNFNqFNLVEAQCkpDPNFSSVqsanPEDH----R-------AFDQAVELanKSHADLLISTDPDADRLG 352
Cdd:cd05801 223 VPYWQPIAEKYGLN-LTVVNPKV--DPTFRFM----TLDHdgkiRmdcsspyAMAGLLKL--KDKFDLAFANDPDADRHG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 353 IAERDAhGHItyfNGNQIGALLLNYRIQQTSQLRHRLMI-QSIVSSELTKSLARYNNVEYKEVLTGFKFIAQEIRqlddH 431
Cdd:cd05801 294 IVTPSA-GLM---NPNHYLSVAIDYLFTHRPLWNKSAGVgKTLVSSSMIDRVAAALGRKLYEVPVGFKWFVDGLL----D 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 432 QNMIFAFEESYG--FL---SEPFVRDKDAvqIVPLIIkyASE-LKLYGKTLKDELEQIYQTVGRH----EDTLFSHtldg 501
Cdd:cd05801 366 GSLGFGGEESAGasFLrrdGTVWTTDKDG--IIMCLL--AAEiLAVTGKDPGQLYQELTERFGEPyyarIDAPATP---- 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 502 lEGKKKIESImthfrsNPPQ----EIQGLKVKAIEdyltsevyhldkdTTSQINSPKSNVIRVLFDEGFIALRPSGTEPK 577
Cdd:cd05801 438 -EQKARLKKL------SPEQvtatELAGDPILAKL-------------TRAPGNGASIGGLKVTTANGWFAARPSGTEDV 497
|
....
gi 487709087 578 IKLY 581
Cdd:cd05801 498 YKIY 501
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
366-486 |
2.09e-14 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 69.79 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 366 NGNQIGALLLNYRIQQTSQLRHRLMIQSIVSSELTKSLARYNNVEYKEVLTGFKFIAQEIRQLddhqNMIFAFEESYGFL 445
Cdd:pfam02880 1 DGDQILALLAKYLLEQGKLPPGAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREE----GALFGGEESGHII 76
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 487709087 446 SEPFVRDKDAVQIVPLIikyASELKLYGKTLKDELEQIYQT 486
Cdd:pfam02880 77 FLDHATTKDGILAALLV---LEILARTGKSLSELLEELPEK 114
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
134-582 |
2.56e-13 |
|
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: 72.64 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 134 TIVIHYDIRHLSTEFAQIIANVLANHQITVYL--PDTYKTTPELSFAVRNLNTTAGIMITASHNP----KDYnGIKVYGS 207
Cdd:cd03085 51 TLVVGGDGRYYNKEAIQIIIKIAAANGVGKVVvgQNGLLSTPAVSAVIRKRKATGGIILTASHNPggpeGDF-GIKYNTS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 208 DG--AQLS-TDASELASRYIEE--VGDPLQIDIPISKQNTSYIKPFPKSVTD---DYMKHIQNMI------GYIPKSDLQ 273
Cdd:cd03085 130 NGgpAPESvTDKIYEITKKITEykIADDPDVDLSKIGVTKFGGKPFTVEVIDsveDYVELMKEIFdfdaikKLLSRKGFK 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 274 VVFTSLHGTSVPIVPELL-QSLNFNQFNLVEAQ-------CKPDPNFSSVQSanpedhrafdqAVELANKSHADLLISTD 345
Cdd:cd03085 210 VRFDAMHGVTGPYAKKIFvEELGAPESSVVNCTplpdfggGHPDPNLTYAKD-----------LVELMKSGEPDFGAASD 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 346 PDADR---LG-------------IAErDAHgHITYFNGNQIGALLlnyRIQQTSQLRHRlmiqsivsseltksLARYNNV 409
Cdd:cd03085 279 GDGDRnmiLGkgffvtpsdsvavIAA-NAK-LIPYFYKGGLKGVA---RSMPTSGALDR--------------VAKKLGI 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 410 EYKEVLTGFKFIAqeirQLDDHQNMIFAFEESYGFLSEpFVRDKDAVQIVpliIKYASELKLYGKTLKDELEQIYQTVGR 489
Cdd:cd03085 340 PLFETPTGWKFFG----NLMDAGKLSLCGEESFGTGSD-HIREKDGLWAV---LAWLSILAHRNVSVEDIVKEHWQKYGR 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 490 HedtLFS-HTLDGLEGKKKiESIMTHFR---SNPPQEIQ----GLKVKAIEDYltseVYH--LDKDTTsqinspKSNVIR 559
Cdd:cd03085 412 N---FYTrYDYEEVDSEAA-NKMMDHLRalvSDLPGVGKsgdkGYKVAKADDF----SYTdpVDGSVS------KKQGLR 477
|
490 500
....*....|....*....|....*..
gi 487709087 560 VLFDEGF-IALRPSGTEPK---IKLYV 582
Cdd:cd03085 478 IIFEDGSrIIFRLSGTGSSgatIRLYI 504
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
90-350 |
2.28e-12 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 69.20 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 90 SKLT-FGTAGIRGKfgLGEgRLNkftiEKLALGLARYLNAQTNSPTIVIHYDIRHLSTEFAQIIANVLANHQITVyLPDT 168
Cdd:PRK15414 2 KKLTcFKAYDIRGK--LGE-ELN----EDIAWRIGRAYGEFLKPKTIVLGGDVRLTSETLKLALAKGLQDAGVDV-LDIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 169 YKTTPELSFAVRNLNTTAGIMITASHNPKDYNGIKVYGSDGAQLSTDASELASRYIEEVGDPLQIDipiSKQNTSYIKpf 248
Cdd:PRK15414 74 MSGTEEIYFATFHLGVDGGIEVTASHNPMDYNGMKLVREGARPISGDTGLRDVQRLAEANDFPPVD---ETKRGRYQQ-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 249 pKSVTDDYMKHiqnMIGYIPKSDL---QVVFTSLHGTSVPIVPEL---LQSLNFnQFNLVEAQCKPDPNFSSvQSANPED 322
Cdd:PRK15414 149 -INLRDAYVDH---LFGYINVKNLtplKLVINSGNGAAGPVVDAIearFKALGA-PVELIKVHNTPDGNFPN-GIPNPLL 222
|
250 260
....*....|....*....|....*...
gi 487709087 323 HRAFDQAVELANKSHADLLISTDPDADR 350
Cdd:PRK15414 223 PECRDDTRNAVIKHGADMGIAFDGDFDR 250
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
94-370 |
1.00e-10 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 64.00 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 94 FGTAGIRGKFGLGegrlnKFTIE---KLALGLARYLnAQTNSPTIVIHYDIR--------HLSTEFAQIIANVLanhqIT 162
Cdd:PRK10887 4 FGTDGIRGKVGQA-----PITPDfvlKLGWAAGKVL-ARQGRPKVLIGKDTRisgymlesALEAGLAAAGVDVL----LT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 163 VYLPdtyktTPELSFAVRNLNTTAGIMITASHNPKDYNGIKVYGSDGAQLStDASELAsryIEEvgdplQIDIPISKQNT 242
Cdd:PRK10887 74 GPMP-----TPAVAYLTRTLRAEAGIVISASHNPYYDNGIKFFSADGTKLP-DEVELA---IEA-----ELDKPLTCVES 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 243 S--------------YI----KPFPKSVTDDYMKhiqnmigyipksdlqVVFTSLHGTSVPIVPELLQSLNfnqFNLVEA 304
Cdd:PRK10887 140 AelgkasrindaagrYIefckSTFPNELSLRGLK---------------IVVDCANGATYHIAPNVFRELG---AEVIAI 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487709087 305 QCKPDP---NfSSVQSANPEdhrAFDQAVeLANKshADLLISTDPDADRLGIAerDAHGHItyFNGNQI 370
Cdd:PRK10887 202 GCEPNGlniN-DECGATDPE---ALQAAV-LAEK--ADLGIAFDGDGDRVIMV--DHLGNL--VDGDQL 259
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
186-374 |
3.73e-08 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 56.22 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 186 AGIMITASHNPKDYNGIKVYGSDGAQLSTDASEL----ASRYIEEVgdplqiDIPISKQnTSYIKPFPKSVtdDYM---- 257
Cdd:PLN02371 170 APIMITASHLPYNRNGLKFFTKDGGLGKPDIKDIleraARIYKEWS------DEGLLKS-SSGASSVVCRV--DFMstya 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 258 KHIQNMI----GYIPKSD-----LQVVFTSLHGTSVPIVPELLQSLNFN----QFnlveaqCKPDPNFSSvQSANPEDHR 324
Cdd:PLN02371 241 KHLRDAIkegvGHPTNYEtplegFKIVVDAGNGAGGFFAEKVLEPLGADtsgsLF------LEPDGMFPN-HIPNPEDKA 313
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 487709087 325 AFD---QAVeLANKshADLLISTDPDADRLGIAerDAHGHitYFNGNQIGALL 374
Cdd:PLN02371 314 AMSattQAV-LANK--ADLGIIFDTDVDRSAVV--DSSGR--EINRNRLIALM 359
|
|
| PLN02307 |
PLN02307 |
phosphoglucomutase |
95-490 |
5.27e-08 |
|
phosphoglucomutase
Pssm-ID: 177942 [Multi-domain] Cd Length: 579 Bit Score: 55.82 E-value: 5.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 95 GTAGIRGKFGL--GEGRLNKFtIEKLALGLArylNAQTNSPTIVIHYDIRHLSTEFAQIIANVLANHQI-TVYLP-DTYK 170
Cdd:PLN02307 26 GTSGLRKKVKVfmQENYLANF-VQALFNALP---AEKVKGATLVLGGDGRYFNKEAIQIIIKIAAANGVrRVWVGqNGLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 171 TTPELSFAVRN---LNTTAGIMITASHNP----KDYnGIKV-YGSDG-AQLS-TDASELASRYIEEVgdPLQIDIP---I 237
Cdd:PLN02307 102 STPAVSAVIRErdgSKANGGFILTASHNPggpeEDF-GIKYnYESGQpAPESiTDKIYGNTLTIKEY--KMAEDIPdvdL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 238 SKQN-TSYIKPFPKSV-----TDDYMKHIQNMI------GYIPKSDLQVVFTSLHGTSVP-----IVPELLQS----LNF 296
Cdd:PLN02307 179 SAVGvTKFGGPEDFDVevidpVEDYVKLMKSIFdfelikKLLSRPDFTFCFDAMHGVTGAyakriFVEELGAPesslLNC 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 297 N---QFNlveaQCKPDPNFSS----VQSANPEDHRAFDQAVELANKShadllistDPDADR---LG-------------I 353
Cdd:PLN02307 259 VpkeDFG----GGHPDPNLTYakelVKRMGLGKTSYGDEPPEFGAAS--------DGDGDRnmiLGkrffvtpsdsvaiI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 354 AErDAHGHITYFNGNQIGalllnyriqqtsqlrhrlMIQSIVSSELTKSLARYNNVEYKEVLTGFKFIAqeirQLDDHQN 433
Cdd:PLN02307 327 AA-NAQEAIPYFSGGLKG------------------VARSMPTSAALDVVAKKLNLPFFEVPTGWKFFG----NLMDAGK 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487709087 434 MIFAFEESYGFLSEpFVRDKD---AVQIVPLIIKYASELKLYGKTL---KDELEQIYQTVGRH 490
Cdd:PLN02307 384 LSICGEESFGTGSD-HIREKDgiwAVLAWLSILAHKNKDVLPGGKLvtvEDIVREHWATYGRN 445
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
94-360 |
2.15e-07 |
|
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: 53.74 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 94 FGTAGIRGKFGlgegRLNKFTIEKLALGLARYLNAQTNSPTIVIHYDIRHLSTEFAQIIANVLANHQITV----YLPdty 169
Cdd:cd03088 2 FGTSGLRGLVT----DLTDEVCYAYTRAFLQHLESKFPGDTVAVGRDLRPSSPRIAAACAAALRDAGFRVvdcgAVP--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 170 ktTPELSFAVRNLNTtAGIMITASHNPKDYNGIKVYGSDGAQLSTDASELASRYIE---EVGDPLQIDIPISKQNTS--- 243
Cdd:cd03088 75 --TPALALYAMKRGA-PAIMVTGSHIPADRNGLKFYRPDGEITKADEAAILAALVElpeALFDPAGALLPPDTDAADayi 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 244 --YIKPFPK--------------SVTDDYMKHIQNMIG--YIP--KSDlqvVFtslhgtsVPIVPEllqslnfnqfnlve 303
Cdd:cd03088 152 arYTDFFGAgalkglrigvyqhsSVGRDLLVRILEALGaeVVPlgRSD---TF-------IPVDTE-------------- 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 487709087 304 aqckpdpnfssvqsANPEDHRAfdQAVELANKSHADLLISTDPDADRLGIAerDAHG 360
Cdd:cd03088 208 --------------AVRPEDRA--LAAAWAAEHGLDAIVSTDGDGDRPLVA--DETG 246
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
133-350 |
1.12e-06 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 51.14 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 133 PTIVIHYDIRHLSTEFAQIIAN-VLANHQITVYLPDTykTTPELSFAVRNLNTtAGIMITASHNPKDYNGIKVYGSdGAQ 211
Cdd:PRK09542 36 TTVVIGHDMRDSSPELAAAFAEgVTAQGLDVVRIGLA--STDQLYFASGLLDC-PGAMFTASHNPAAYNGIKLCRA-GAK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 212 LSTDASELAsryieEVGDPLQIDIPiskqntSYIKPfPKSVTD-----DYMKHIQNMIGYIPKSDLQVVFTSLHGTSVPI 286
Cdd:PRK09542 112 PVGQDTGLA-----AIRDDLIAGVP------AYDGP-PGTVTErdvlaDYAAFLRSLVDLSGIRPLKVAVDAGNGMGGHT 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487709087 287 VPELLQSLNFN----QFNLveaqckpDPNFSSvQSANPedhraFDQA--VELANK---SHADLLISTDPDADR 350
Cdd:PRK09542 180 VPAVLGGLPITllplYFEL-------DGTFPN-HEANP-----LDPAnlVDLQAFvreTGADIGLAFDGDADR 239
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
185-220 |
3.75e-06 |
|
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: 49.90 E-value: 3.75e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 487709087 185 TAGIMITASHNPKDYNGIKVYGSDGAQLSTD----ASELA 220
Cdd:cd03086 36 TIGVMITASHNPVEDNGVKIVDPDGEMLEESwepyATQLA 75
|
|
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
172-484 |
4.10e-06 |
|
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: 49.55 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 172 TPELSFAVRNLNTTAGIMITASHNPKDYNGIKVYGSDGAQLSTDaselASRYIE-----------EVGDPLQIdIPISKQ 240
Cdd:cd05805 73 LPVARYAIRFLGASGGIHVRTSPDDPDKVEIEFFDSRGLNISRA----MERKIEnaffredfrraHVDEIGDI-TEPPDF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 241 NTSYIKPFPKSVTDDYMKhiqnmigyipKSDLQVVFTSLHGTSVPIVPELLQSLNFnqfnLVEAqckpdpNFSSVQSANP 320
Cdd:cd05805 148 VEYYIRGLLRALDTSGLK----------KSGLKVVIDYAYGVAGIVLPGLLSRLGC----DVVI------LNARLDEDAP 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 321 ----EDHRAFDQAVELANKSHADLLISTDPDADRLGIAerDAHGHItyFNGNQIGAL--LLNYRIQQTSQLrhrlmIQSI 394
Cdd:cd05805 208 rtdtERQRSLDRLGRIVKALGADFGVIIDPNGERLILV--DEAGRV--ISDDLLTALvsLLVLKSEPGGTV-----VVPV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487709087 395 VSSELTKSLARYNNVEYKEVLTGFKFIAQEIR----QLDDHQNMIFAFEESYGFlsepfvrdkDAVQIVPLIIKYASELK 470
Cdd:cd05805 279 TAPSVIEQLAERYGGRVIRTKTSPQALMEAALenvvLAGDGDGGFIFPEFHPGF---------DAIAALVKILEMLARTN 349
|
330
....*....|....
gi 487709087 471 LYGKTLKDELEQIY 484
Cdd:cd05805 350 ISLSQIVDELPRFY 363
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
178-220 |
2.00e-05 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 47.33 E-value: 2.00e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 487709087 178 AVRNLNTTA--GIMITASHNPKDYNGIKVYGSDGAQLSTD----ASELA 220
Cdd:PLN02895 50 ALRSLKTGAatGLMITASHNPVSDNGVKIVDPSGGMLPQAwepfADALA 98
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
183-224 |
5.21e-05 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 46.19 E-value: 5.21e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 487709087 183 NTTAGIMITASHNPKDYNGIKVYGSDGAQLSTDASELASRYI 224
Cdd:PTZ00302 74 NKSVGVMITASHNPIQDNGVKIIDPDGGMLEESWEKICTDFA 115
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
543-582 |
2.04e-04 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 39.94 E-value: 2.04e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 487709087 543 DKDTTSQINSPKSNVI---RVLFDEG-FIALRPSGTEPKIKLYV 582
Cdd:pfam00408 8 EKKKLAALAAILKVFAdaeKILGEDGrRLDVRPSGTEPVLRVMV 51
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