|
Name |
Accession |
Description |
Interval |
E-value |
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
88-550 |
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: 587.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 88 PLTFGTAGLRGPVRAGPNGMNRVVVRRAAAGLAAWLTAQGRSGEP--VVVGYDGRHGSAEFAHDSAAIFAAAGFDARLLP 165
Cdd:cd05799 1 RLEFGTAGLRGKMGAGTNRMNDYTVRQATQGLANYLKKKGPDAKNrgVVIGYDSRHNSREFAELTAAVLAANGIKVYLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 166 RLLPTPVLAFAVQHLGAAAGVMVTASHNPPQDNGYKVYVADGAQIAPPVDVEIEAAIRAVASARGVPLSD-----RYTVL 240
Cdd:cd05799 81 DLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAVLEPLDIKFEEaldsgLIKYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 241 GEDIVDAYVGAVAGLIGPGS----REVRIVHTAMHGVGTEVITKVFAAAGFAPMHGVPQQAAPDADFPTVSFPNPEETGA 316
Cdd:cd05799 161 GEEIDDAYLEAVKKLLVNPElnegKDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVVEEQAEPDPDFPTVKFPNPEEPGA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 317 LDLALALAREQDADLVIANDPDADRCAVAVPDASGEWRMLRGDQVGVLLADALLRK-------GVRGTYATTIVSSSMLG 389
Cdd:cd05799 241 LDLAIELAKKVGADLILATDPDADRLGVAVKDKDGEWRLLTGNEIGALLADYLLEQrkekgklPKNPVIVKTIVSSELLR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 390 AMAARNQVPYRETLTGFKWISRAAPDL-------VFGYEEALGYAVAPElVRDKDGISAALLVAELAAALKADGSSLTQR 462
Cdd:cd05799 321 KIAKKYGVKVEETLTGFKWIGNKIEELesggkkfLFGFEESIGYLVGPF-VRDKDGISAAALLAEMAAYLKAQGKTLLDR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 463 LEQLYAEYGRYATDQVSVRV---EDLALIAAMMQRLRARPptqllgrpvtvedllpdnDVLRLRWQ-GGRVVIRPSGTEP 538
Cdd:cd05799 400 LDELYEKYGYYKEKTISITFegkEGPEKIKAIMDRLRNNP------------------NVLTFYLEdGSRVTVRPSGTEP 461
|
490
....*....|..
gi 2416456659 539 KLKAYLEVIVPD 550
Cdd:cd05799 462 KIKFYIEVVGKK 473
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
78-548 |
7.29e-143 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 425.25 E-value: 7.29e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 78 EAELVDRFRGPLTFGTAGLRGPVRAGPNGMNRVVVRRAAAGLAAWL---TAQGRSGEPVVVGYDGRHGSAEFAHDSAAIF 154
Cdd:PTZ00150 34 EEELKRRFLKRMEFGTAGLRGKMGAGFNCMNDLTVQQTAQGLCAYVietFGQALKSRGVVIGYDGRYHSRRFAEITASVF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 155 AAAGFDARLLPRLLPTPVLAFAVQHLGAAAGVMVTASHNPPQDNGYKVYVADGAQIAPPVDVEIEAAIRAVASargvPLS 234
Cdd:PTZ00150 114 LSKGFKVYLFGQTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVYWSNGAQIIPPHDKNISAKILSNLE----PWS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 235 DRYTVLGED--------IVDAYVGAVAGLIGPGSRE---VRIVHTAMHGVGTEVITKVFAAAGFAPMHGVPQQAAPDADF 303
Cdd:PTZ00150 190 SSWEYLTETlvedplaeVSDAYFATLKSEYNPACCDrskVKIVYTAMHGVGTRFVQKALHTVGLPNLLSVAQQAEPDPEF 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 304 PTVSFPNPEET-GALDLALALAREQDADLVIANDPDADRCAVAVpDASGEWRMLRGDQVGVLLADALLRKGVRGTYAT-- 380
Cdd:PTZ00150 270 PTVTFPNPEEGkGALKLSMETAEAHGSTVVLANDPDADRLAVAE-KLNNGWKIFTGNELGALLAWWAMKRYRRQGIDKsk 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 381 -----TIVSSSMLGAMAARNQVPYRETLTGFKWISRAAPDL--------VFGYEEALGYAVApELVRDKDGISAALLVAE 447
Cdd:PTZ00150 349 cfficTVVSSRMLKKMAEKEGFQYDETLTGFKWIGNKAIELnaenglttLFAYEEAIGFMLG-TRVRDKDGVTAAAVVAE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 448 LAAALKADGSSLTQRLEQLYAEYGRYATDQVSVRVEDLALIAAMMQRLR--ARPPTQLLGRPVT-VEDL----------- 513
Cdd:PTZ00150 428 MALYLYERGKTLVEHLESLYKQYGYHFTNNSYYICYDPSRIVSIFNDIRnnGSYPTKLGGYPVTrIRDLttgydtatpdg 507
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2416456659 514 ------LPDNDVLRLRWQGGRVV-IRPSGTEPKLKAYLEVIV 548
Cdd:PTZ00150 508 kpllpvSASTQMITFYFENGAIItIRGSGTEPKLKWYAELSG 549
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
91-546 |
6.61e-116 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 351.81 E-value: 6.61e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 91 FGTAGLRGpvRAGPNgMNRVVVRRAAAGLAAWLTAQGRSGepVVVGYDGRHGSAEFAHDSAAIFAAAGFDARLLpRLLPT 170
Cdd:COG1109 7 FGTDGIRG--IVGEE-LTPEFVLKLGRAFGTYLKEKGGPK--VVVGRDTRLSSPMLARALAAGLASAGIDVYDL-GLVPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 171 PVLAFAVQHLGAAAGVMVTASHNPPQDNGYKVYVADGAQIAPPVDVEIEAAIRAVASARGVPLSDRYTVLGEDIVDAYVG 250
Cdd:COG1109 81 PALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKEDFRRAEAEEIGKVTRIEDVLEAYIE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 251 AVAGLIGPGSRE--VRIVHTAMHGVGTEVITKVFAAAGFAPmhgVPQQAAPDADFPTVsFPNPEETgALDLALALAREQD 328
Cdd:COG1109 161 ALKSLVDEALRLrgLKVVVDCGNGAAGGVAPRLLRELGAEV---IVLNAEPDGNFPNH-NPNPEPE-NLEDLIEAVKETG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 329 ADLVIANDPDADRCAVAvpDASGewRMLRGDQVGVLLADALLRKGVRGTYATTIVSSSMLGAMAARNQVPYRETLTGFKW 408
Cdd:COG1109 236 ADLGIAFDGDADRLGVV--DEKG--RFLDGDQLLALLARYLLEKGPGGTVVVTVMSSLALEDIAEKHGGEVVRTKVGFKY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 409 ISRAA--PDLVFGYEEALGYAVaPELVRDKDGISaallvaelaaalkadgSSLT---------QRLEQLYAEYGRYATDQ 477
Cdd:COG1109 312 IKEKMreTGAVLGGEESGGIIF-PDFVPTDDGIL----------------AALLllellakqgKSLSELLAELPRYPQPE 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 478 VSVRVEDLALIAAMMQRLRARpptqllgrpVTVEDLLPDNDVLRLRW-QGGRVVIRPSGTEPKLKAYLEV 546
Cdd:COG1109 375 INVRVPDEEKIGAVMEKLREA---------VEDKEELDTIDGVKVDLeDGGWVLVRPSGTEPLLRVYAEA 435
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
90-545 |
2.09e-75 |
|
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: 246.70 E-value: 2.09e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 90 TFGTAGLRGPVRAGPNGMNrvvVRRAAAGLAAWLTAQGRSGEPVVVGYDGRHGSAEFAHDSAAIFAAAGFDARLLPRLLP 169
Cdd:cd05800 2 KFGTDGWRGIIAEDFTFEN---VRRVAQAIADYLKEEGGGGRGVVVGYDTRFLSEEFARAVAEVLAANGIDVYLSDRPVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 170 TPVLAFAVQHLGAAAGVMVTASHNPPQDNGYKVYVADGAQIAPPVDVEIEAAIrAVASARGVPLSDRYTVLGEDIVDAYV 249
Cdd:cd05800 79 TPAVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARL-ASGEPPGLEARAEGLIETIDPKPDYL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 250 GAVAGLIGP---GSREVRIVHTAMHGVGTEVITKVFAAAGF--APMHGvpqqaAPDADFPTVSfPNPEETgALDLALALA 324
Cdd:cd05800 158 EALRSLVDLeaiREAGLKVVVDPMYGAGAGYLEELLRGAGVdvEEIRA-----ERDPLFGGIP-PEPIEK-NLGELAEAV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 325 REQDADLVIANDPDADRcaVAVPDASGEWrmLRGDQVGVLLADALLR-KGVRGTYATTIVSSSMLGAMAARNQVPYRETL 403
Cdd:cd05800 231 KEGGADLGLATDGDADR--IGAVDEKGNF--LDPNQILALLLDYLLEnKGLRGPVVKTVSTTHLIDRIAEKHGLPVYETP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 404 TGFKWISRA--APDLVFGYEEALGYAVaPELVRDKDGISAALLVAELAAALkadGSSLTQRLEQLYAEYGRYATDQVSVR 481
Cdd:cd05800 307 VGFKYIAEKmlEEDVLIGGEESGGLGI-RGHIPERDGILAGLLLLEAVAKT---GKPLSELVAELEEEYGPSYYDRIDLR 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2416456659 482 VEDlALIAAMMQRLRARPPTQLLGRPVTVEDLLpdnDVLRLRWQ-GGRVVIRPSGTEPKLKAYLE 545
Cdd:cd05800 383 LTP-AQKEAILEKLKNEPPLSIAGGKVDEVNTI---DGVKLVLEdGSWLLIRPSGTEPLLRIYAE 443
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
153-545 |
6.41e-51 |
|
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: 178.70 E-value: 6.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 153 IFAAAGFDARLLPRLLPTPVLAFAvQHLGAAAGVMVTASHNPPQDNGYKVYVADGAQIAPPVDVEIEAAIRAVASARGVP 232
Cdd:cd03084 1 IFGTSGVRGVVGDDITPETAVALG-QAIGSTGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSAVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 233 LSDRYTVLGEDIVDAYVGAVAGLI---GPGSREVRIVHTAMHGVGTEVITKVFAAAGfAPMhgVPQQAAPDADFPTVSFP 309
Cdd:cd03084 80 YELGGSVKAVDILQRYFEALKKLFdvaALSNKKFKVVVDSVNGVGGPIAPQLLEKLG-AEV--IPLNCEPDGNFGNINPD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 310 NPEETGALDLALALAREQdADLVIANDPDADRCAVAVPdasgEWRMLRGDQVGVLLADALLRK-GVRGTYATTIVSSSML 388
Cdd:cd03084 157 PGSETNLKQLLAVVKAEK-ADFGVAFDGDADRLIVVDE----NGGFLDGDELLALLAVELFLTfNPRGGVVKTVVSSGAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 389 GAMAARNQVPYRETLTGFKWISRAA--PDLVFGYEEALGYAVaPELVRDKDGISaalLVAELAAALKADGSSLTQRLEQL 466
Cdd:cd03084 232 DKVAKKLGIKVIRTKTGFKWVGEAMqeGDVVLGGEESGGVIF-PEFHPGRDGIS---AALLLLEILANLGKSLSELFSEL 307
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2416456659 467 YAEYGRyatdqvsvrvedlaliaammqRLRARpptqllgrpvtvedllpdndvlrlrwqgGRVVIRPSGTEPKLKAYLE 545
Cdd:cd03084 308 PRYYYI---------------------RLKVR----------------------------GWVLVRASGTEPAIRIYAE 337
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
88-229 |
3.65e-46 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 158.93 E-value: 3.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 88 PLTFGTAGLRGPVRAGPNgmNRVVVRRAAAGLAAWLTAQGRSGePVVVGYDGRHGSAEFAHDSAAIFAAAGFDARLLPrL 167
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGEL--TPEFALKLGQAIASYLRAQGGGG-KVVVGRDTRYSSRELARALAAGLASNGVEVILLG-L 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2416456659 168 LPTPVLAFAVQHLGAAAGVMVTASHNPPQDNGYKVYVADGAQIAPPVDVEIEAAIRAVASAR 229
Cdd:pfam02878 77 LPTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKEDFYR 138
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
111-372 |
3.28e-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: 3.28e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 111 VVRRAAAGLAAWLTAQGRSgePVVVGYDGRHGSAEFAHDSAAIFAAAGFDARLLpRLLPTPVLAFAVQHLGAAAGVMVTA 190
Cdd:cd03089 19 IAYAIGRAFGSWLLEKGAK--KVVVGRDGRLSSPELAAALIEGLLAAGCDVIDI-GLVPTPVLYFATFHLDADGGVMITA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 191 SHNPPQDNGYKVYVADGaqiaPPVDVEIEAAIRAVASARGVPLSDRYTVLGEDIVDAYVGAVAGLIGPGSREVRIVHTAM 270
Cdd:cd03089 96 SHNPPEYNGFKIVIGGG----PLSGEDIQALRERAEKGDFAAATGRGSVEKVDILPDYIDRLLSDIKLGKRPLKVVVDAG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 271 HGVGTEVITKVFAAAGFapmHGVPQQAAPDADFPTvSFPNPEETGALDLALALAREQDADLVIANDPDADRCAVAvpDAS 350
Cdd:cd03089 172 NGAAGPIAPQLLEALGC---EVIPLFCEPDGTFPN-HHPDPTDPENLEDLIAAVKENGADLGIAFDGDGDRLGVV--DEK 245
|
250 260
....*....|....*....|..
gi 2416456659 351 GewRMLRGDQVGVLLADALLRK 372
Cdd:cd03089 246 G--EIIWGDRLLALFARDILKR 265
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
91-545 |
6.48e-38 |
|
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: 145.35 E-value: 6.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 91 FGTAGLRGPVragPNGMNRVVVRRAAAGLAAWLtaqgRSGEpVVVGYDGRHGSAEFAHDSAAIFAAAGFDARLLPrLLPT 170
Cdd:TIGR03990 4 FGTSGIRGIV---GEELTPELALKVGKAFGTYL----RGGK-VVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLG-IAPT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 171 PVLAFAVQHLGAAAGVMVTASHNPPQDNGYKVYVADGAQIAPPVDVEIEAAIRAvASARGVPLSDRYTVL-GEDIVDAYV 249
Cdd:TIGR03990 75 PTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQEEEIEEIAES-GDFERADWDEIGTVTsDEDAIDDYI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 250 GAVAGLIGP---GSREVRIVHTAMHGVGTEVITKVFAAAGfapMHGVPQQAAPDADFPT-VSFPNPEETGaldLALALAR 325
Cdd:TIGR03990 154 EAILDKVDVeaiRKKGFKVVVDCGNGAGSLTTPYLLRELG---CKVITLNCQPDGTFPGrNPEPTPENLK---DLSALVK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 326 EQDADLVIANDPDADRCAVAvpDASGewRMLRGDQVGVLLADALLRKGvRGTYATTIVSSSMLGAMAARNQVPYRETLTG 405
Cdd:TIGR03990 228 ATGADLGIAHDGDADRLVFI--DEKG--RFIGGDYTLALFAKYLLEHG-GGKVVTNVSSSRAVEDVAERHGGEVIRTKVG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 406 FKWISRA--APDLVFGYEEALGYaVAPELVRDKDGISAALLVAELAaalkadgSSLTQRLEQLYAEYGRYATDQVSVRVE 483
Cdd:TIGR03990 303 EVNVAEKmkEEGAVFGGEGNGGW-IFPDHHYCRDGLMAAALFLELL-------AEEGKPLSELLAELPKYPMSKEKVELP 374
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2416456659 484 DLALiAAMMQRLRARPPTqllGRPVTVedllpdnDVLRLRWQGGRVVIRPSGTEPKLKAYLE 545
Cdd:TIGR03990 375 DEDK-EEVMEAVEEEFAD---AEIDTI-------DGVRIDFEDGWVLVRPSGTEPIVRIYAE 425
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
91-545 |
9.81e-38 |
|
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: 144.64 E-value: 9.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 91 FGTAGLRGPVragPNGMNRVVVRRAAAGLAAWltaqgRSGEPVVVGYDGRHGSAEFAHDSAAIFAAAGFDARLLPrLLPT 170
Cdd:cd03087 2 FGTSGIRGVV---GEELTPELALKVGKALGTY-----LGGGTVVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDIG-IVPT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 171 PVLAFAVQHLGAAaGVMVTASHNPPQDNGYKVYVADGAQIAPPVDVEIEAAI----------RAVASARGVplsdrytvl 240
Cdd:cd03087 73 PALQYAVRKLGDA-GVMITASHNPPEYNGIKLVNPDGTEFSREQEEEIEEIIfserfrrvawDEVGSVRRE--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 241 gEDIVDAYVGAVAGLIG-PGSREVRIVHTAMHGVGTEVITKVFAAAGfapMHGVPQQAAPDADFPT-VSFPNPEETGald 318
Cdd:cd03087 143 -DSAIDEYIEAILDKVDiDGGKGLKVVVDCGNGAGSLTTPYLLRELG---CKVITLNANPDGFFPGrPPEPTPENLS--- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 319 LALALAREQDADLVIANDPDADRcAVAVpDASGewRMLRGDQVGVLLADALLRKGvRGTYATTIVSSSMLGAMAARNQVP 398
Cdd:cd03087 216 ELMELVRATGADLGIAHDGDADR-AVFV-DEKG--RFIDGDKLLALLAKYLLEEG-GGKVVTPVDASMLVEDVVEEAGGE 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 399 YRETLTGFKWISRAA--PDLVFGYEEALGYaVAPELVRDKDGISAALLVAELaaalkadgSSLTQRLEQLYAEYGRYATD 476
Cdd:cd03087 291 VIRTPVGDVHVAEEMieNGAVFGGEPNGGW-IFPDHQLCRDGIMTAALLLEL--------LAEEKPLSELLDELPKYPLL 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2416456659 477 QVSVRVEDLALiAAMMQRLRARpptqLLGRPVTVEDLlpdnDVLRLRWQGGRVVIRPSGTEPKLKAYLE 545
Cdd:cd03087 362 REKVECPDEKK-EEVMEAVEEE----LSDADEDVDTI----DGVRIEYEDGWVLIRPSGTEPKIRITAE 421
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
91-545 |
5.31e-29 |
|
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: 119.78 E-value: 5.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 91 FGTAGLRGPVRAGPNGMNRVVVRRAAAGLaawLTAQGRSGEP-VVVGYDGRHGSAEFAHDSAAIFAAAGFDARLLPrLLP 169
Cdd:TIGR01455 1 FGTDGVRGRAGQEPLTAELALLLGAAAGR---VLRQGRDTAPrVVIGKDTRLSGYMLENALAAGLNSAGVDVLLLG-PLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 170 TPVLAFAVQHLGAAAGVMVTASHNPPQDNGYKVYVADGAQIAPPVDVEIEAAIRAVA-----SARGVPLSDRYtvlgEDI 244
Cdd:TIGR01455 77 TPAVAYLTRTLRADAGVMISASHNPYEDNGIKFFGPGGFKLDDATEAAIEALLDEADplprpESEGLGRVKRY----PDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 245 VDAYVGAVAGLIGPGS--REVRIVHTAMHGVGTEVITKVFAAAG---FApMHGVPQQAAPDADfptVSFPNPEetgaldL 319
Cdd:TIGR01455 153 VGRYIEFLKSTLPRGLtlSGLKVVLDCANGAAYKVAPHVFRELGaevIA-IGVEPDGLNINDG---CGSTHLD------A 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 320 ALALAREQDADLVIANDPDADRCaVAVpDASGewRMLRGDQVGVLLADALLRKG--VRGTYATTIVSSsmLGAMAARNQ- 396
Cdd:TIGR01455 223 LQKAVREHGADLGIAFDGDADRV-LAV-DANG--RIVDGDQILYIIARALKESGelAGNTVVATVMSN--LGLERALEKl 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 397 -VPYRETLTGFKWISRA--APDLVFGYEEAlGYAVAPELVRDKDGIsaaLLVAELAAALKADGSSltqrLEQLYAEYGRY 473
Cdd:TIGR01455 297 gLTLIRTAVGDRYVLEEmrESGYNLGGEQS-GHIILLDYSTTGDGI---VSALQVLTIMKKSGST----LSELAAEFVPY 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2416456659 474 ATDQVSVRVEDLALIAAMMQRLRArpptqllgRPVTVEDLLPDNdvlrlrwqgGRVVIRPSGTEPKLKAYLE 545
Cdd:TIGR01455 369 PQTLVNVRVADRKLAAAEAPAVKA--------AIEDAEAELGGT---------GRILLRPSGTEPLIRVMVE 423
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
91-540 |
2.23e-28 |
|
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: 117.59 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 91 FGTAGLRGpvRAGpNGMN-RVVVRRAAAglAAWLTAQGRSGEPVVVGYDGRHGSAEFAHDSAAIFAAAGFDARLLPrLLP 169
Cdd:cd05802 2 FGTDGIRG--VAN-EPLTpELALKLGRA--AGKVLGKGGGRPKVLIGKDTRISGYMLESALAAGLTSAGVDVLLLG-VIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 170 TPVLAFAVQHLGAAAGVMVTASHNPPQDNGYKVYVADGAQIAPPVDVEIEAAIRA----VASARGVPLSDRYtvlgEDIV 245
Cdd:cd05802 76 TPAVAYLTRKLRADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVEEEIEALIDKelelPPTGEKIGRVYRI----DDAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 246 DAYVGAVAGLIGPGS-REVRIVHTAMHGVGTEVITKVFAAAGfapMHGVPQQAAPDADfptvsfpN---------PEEtg 315
Cdd:cd05802 152 GRYIEFLKSTFPKDLlSGLKIVLDCANGAAYKVAPEVFRELG---AEVIVINNAPDGL-------NinvncgsthPES-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 316 aldlALALAREQDADLVIANDPDADRCaVAVpDASGewRMLRGDQVGVLLADALLRKGVRGTyaTTIVSSSM--LG---A 390
Cdd:cd05802 220 ----LQKAVLENGADLGIAFDGDADRV-IAV-DEKG--NIVDGDQILAICARDLKERGRLKG--NTVVGTVMsnLGlekA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 391 MAARNqVPYRETLTGFKWIsraapdlvfgYEE--ALGYAVAPE-----LVRDK----DGIsaallvaelaaalkadgssL 459
Cdd:cd05802 290 LKELG-IKLVRTKVGDRYV----------LEEmlKHGANLGGEqsghiIFLDHsttgDGL-------------------L 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 460 T------------QRLEQLYAEYGRYATDQVSVRVED---LALIAAMMQRLRArpptqllgrpvtVEDLLPDNdvlrlrw 524
Cdd:cd05802 340 TalqllaimkrsgKSLSELASDMKLYPQVLVNVRVKDkkaLLENPRVQAAIAE------------AEKELGGE------- 400
|
490
....*....|....*.
gi 2416456659 525 qgGRVVIRPSGTEPKL 540
Cdd:cd05802 401 --GRVLVRPSGTEPLI 414
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
91-550 |
1.26e-23 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 104.83 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 91 FGTAGLRGPVRAGPNGMNRVV-VRRAAAGLAAwltAQGRSGePVVVGYDGRHGSAEfAHDSA-AIFAAAGFDARLLPR-- 166
Cdd:PRK07564 40 FGTSGHRGSSLQPSFNENHILaIFQAICEYRG---KQGITG-PLFVGGDTHALSEP-AIQSAlEVLAANGVGVVIVGRgg 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 167 LLPTPVLAFAV-----QHLGAAAGVMVTASHNPPQDNGYKVYVADGAqiapPVDVEIEAAI--RA-------VASARGVP 232
Cdd:PRK07564 115 YTPTPAVSHAIlkyngRGGGLADGIVITPSHNPPEDGGIKYNPPNGG----PADTDVTDAIeaRAnellaygLKGVKRIP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 233 LSD---RYTVLGEDIVDAYVGAVAGLI------GPGsreVRIVHTAMHGVGTEVitkvfaAAGFAPMHGVPQQ---AAPD 300
Cdd:PRK07564 191 LDRalaSMTVEVIDPVADYVEDLENVFdfdairKAG---LRLGVDPLGGATGPY------WKAIAERYGLDLTvvnAPVD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 301 adfPTVSF------------PNPEETgaldLALALAREQDADLVIANDPDADR---------------CAVAVPDASG-- 351
Cdd:PRK07564 262 ---PTFNFmpldddgkirmdCSSPYA----MAGLLALKDAFDLAFANDPDGDRhgivtpgglmnpnhyLAVAIAYLFHhr 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 352 -EWRmlrgDQVGVlladallrkgvrgtyATTIVSSSMLGAMAARNQVPYRETLTGFKWISR--AAPDLVFGYEEALGyav 428
Cdd:PRK07564 335 pGWR----AGAGV---------------GKTLVSSAMIDRVAAKLGRKLYEVPVGFKWFVNglDDGSLGFGGEESAG--- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 429 APEL-------VRDKDGISAALLVAELAAALkadGSSLTQRLEQLYAEYGR--YAtdqvsvRVeDLALIAAMMQRLRARP 499
Cdd:PRK07564 393 ASFLrrdgsvwTTDKDGLIAVLLAAEILAVT---GKSPSEIYRELWARFGRpyYS------RH-DAPATPEQKAALRKLS 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2416456659 500 P-----TQLLGRPVT-VEDLLPDNDV----LRLRWQGGRVVIRPSGTEPKLKAYLEVIVPD 550
Cdd:PRK07564 463 PelvgaTELAGDPIDaSLTEAPGNGAaiggLKVVTENGWFAARPSGTETTYKIYAESFEGD 523
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
95-545 |
1.56e-23 |
|
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: 103.54 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 95 GLRGPVragPNGMNRVVVRRAAAGLAAWLTaQGRSGEPVVVGYDGRHGSAEFAHDSAAIFAAAGFDARLLPrLLPTPVLA 174
Cdd:cd05803 6 GIRGIV---GEGLTPEVITRYVAAFATWQP-ERTKGGKIVVGRDGRPSGPMLEKIVIGALLACGCDVIDLG-IAPTPTVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 175 FAVQHLGAAAGVMVTASHNPPQDNGYKVYVADGAQIaPPVDVE--IEAAIRAVASARGVPLSDRYTVLgEDIVDAYVGAV 252
Cdd:cd05803 81 VLVRQSQASGGIIITASHNPPQWNGLKFIGPDGEFL-TPDEGEevLSCAEAGSAQKAGYDQLGEVTFS-EDAIAEHIDKV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 253 AGL-----IGPGSREVRIVHTAMHGVGTEVITKVFAAAG--FAPMHGVpqqaaPDADFPTVSFPNPEETGaldLALALAR 325
Cdd:cd05803 159 LALvdvdvIKIRERNFKVAVDSVNGAGGLLIPRLLEKLGceVIVLNCE-----PTGLFPHTPEPLPENLT---QLCAAVK 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 326 EQDADLVIANDPDADRCAVAVPD--ASGEWRMLrgdqvgVLLADALLRK-GVRGTYATTIVSSSMLGAMAARNQVPYRET 402
Cdd:cd05803 231 ESGADVGFAVDPDADRLALVDEDgrPIGEEYTL------ALAVDYVLKYgGRKGPVVVNLSTSRALEDIARKHGVPVFRS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 403 LTG-----FKWISRAApdlVFGyEEALGYAVAPELVRDKDGISAALLVAELAAALKADGSSLTQRLEQLYaeygrYATDQ 477
Cdd:cd05803 305 AVGeanvvEKMKEVDA---VIG-GEGNGGVILPDVHYGRDSLVGIALVLQLLAASGKPLSEIVDELPQYY-----ISKTK 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2416456659 478 VSVRVEDLALIAammQRLRARPPTQLLGRpvtvedllpdNDVLRLRWQGGRVVIRPSGTEPKLKAYLE 545
Cdd:cd05803 376 VTIAGEALERLL---KKLEAYFKDAEAST----------LDGLRLDSEDSWVHVRPSNTEPIVRIIAE 430
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
247-345 |
5.25e-19 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 82.34 E-value: 5.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 247 AYVGAVAGLIGP---GSREVRIVHTAMHGVGTEVITKVFAAAGFAPmhgVPQQAAPDADFPTvSFPNPEETGALDLALAL 323
Cdd:pfam02879 1 AYIDHLLELVDSealKKRGLKVVYDPLHGVGGGYLPELLKRLGCDV---VEENCEPDPDFPT-RAPNPEEPEALALLIEL 76
|
90 100
....*....|....*....|..
gi 2416456659 324 AREQDADLVIANDPDADRCAVA 345
Cdd:pfam02879 77 VKSVGADLGIATDGDADRLGVV 98
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
91-545 |
1.67e-18 |
|
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: 88.41 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 91 FGTAGLRGPVRAgpngMNRVVVRRAAAGLAAWLtAQGRSGEPVVVGYDGRHGSAEFAHDSAAIFAAAGFDARLLPRLlPT 170
Cdd:cd03088 2 FGTSGLRGLVTD----LTDEVCYAYTRAFLQHL-ESKFPGDTVAVGRDLRPSSPRIAAACAAALRDAGFRVVDCGAV-PT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 171 PVLAFAVQHLGAAAgVMVTASHNPPQDNGYKVYVADGaqiappvdvEI----EAAIRA-VASARGVPLSDRYTVL--GED 243
Cdd:cd03088 76 PALALYAMKRGAPA-IMVTGSHIPADRNGLKFYRPDG---------EItkadEAAILAaLVELPEALFDPAGALLppDTD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 244 IVDAYVGAVAGLIGPGSREVRIV----HTAmhgVGTEVITKVFAAAG-----------FAPmhgVPQQAAPDADfptvsf 308
Cdd:cd03088 146 AADAYIARYTDFFGAGALKGLRIgvyqHSS---VGRDLLVRILEALGaevvplgrsdtFIP---VDTEAVRPED------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 309 pnpeetgaLDLALALAREQDADLVIANDPDADRCAVAvpDASGEWrmLRGDQVGVLLADALLRKGVrgtyATTIVSSSML 388
Cdd:cd03088 214 --------RALAAAWAAEHGLDAIVSTDGDGDRPLVA--DETGEW--LRGDILGLLTARFLGADTV----VTPVSSNSAI 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 389 GAMAARNQV-------PYreTLTGFKWISRAAPDLVFGYEEALGYAVAPELVRD---------KDGISAALLVAELAAAL 452
Cdd:cd03088 278 ELSGFFKRVvrtrigsPY--VIAAMAEAAAAGAGRVVGYEANGGFLLGSDIERNgrtlkalptRDAVLPILAVLAAAKEA 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 453 KADGSSLTQRLEQLYAeygryatdqVSVRVEDL--ALIAAMMQRLRARP------PTQLLGRPVTVEDLlpdnDVLRLRW 524
Cdd:cd03088 356 GIPLSELVASLPARFT---------ASDRLQNFptEKSQALIARLSADPearaafFFALGGEVASIDTT----DGLRMTF 422
|
490 500
....*....|....*....|..
gi 2416456659 525 QGGRVV-IRPSGTEPKLKAYLE 545
Cdd:cd03088 423 ANGDIVhLRPSGNAPELRCYVE 444
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
90-545 |
1.87e-16 |
|
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: 82.29 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 90 TFGTAGLRGpvRAGPNGMNRVVVRRAAAGLAAWLTAQGRSGePVVVGYDgRHGSAEFAHDSA-AIFAAAGFDARLLPRLL 168
Cdd:cd05801 22 AFGTSGHRG--SSLKGSFNEAHILAISQAICDYRKSQGITG-PLFLGKD-THALSEPAFISAlEVLAANGVEVIIQQNDG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 169 --PTPVLAFAV------QHLGAAAGVMVTASHNPPQDNGYKVYVADGAqiapPVDVEIEAAIRAVASA---------RGV 231
Cdd:cd05801 98 ytPTPVISHAIltynrgRTEGLADGIVITPSHNPPEDGGFKYNPPHGG----PADTDITRWIEKRANAllanglkgvKRI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 232 PLSDRY---TVLGEDIVDAYVGAVAGLI------GPGsreVRIVHTAMHGVGTEVITKVfaaagfAPMHGVPQQAA-PDA 301
Cdd:cd05801 174 PLEAALasgYTHRHDFVTPYVADLGNVIdmdairKSG---LRLGVDPLGGASVPYWQPI------AEKYGLNLTVVnPKV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 302 DfPTVSFPNPEETGA--------LDLALALAREQDADLVIANDPDADRCAVAVPDAsgewrmlrgdqvGVL-----LADA 368
Cdd:cd05801 245 D-PTFRFMTLDHDGKirmdcsspYAMAGLLKLKDKFDLAFANDPDADRHGIVTPSA------------GLMnpnhyLSVA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 369 ---LL--RKGVRGTYAT--TIVSSSMLGAMAARNQVPYRETLTGFKWISR--AAPDLVFGYEEALGyavAPELVR----- 434
Cdd:cd05801 312 idyLFthRPLWNKSAGVgkTLVSSSMIDRVAAALGRKLYEVPVGFKWFVDglLDGSLGFGGEESAG---ASFLRRdgtvw 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 435 --DKDGIsaaLLVAELAAALKADGSSLTQRLEQLYAEYGR--YATDQVSVRVEDLALIAammqRLRAR--PPTQLLGRPV 508
Cdd:cd05801 389 ttDKDGI---IMCLLAAEILAVTGKDPGQLYQELTERFGEpyYARIDAPATPEQKARLK----KLSPEqvTATELAGDPI 461
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2416456659 509 T-VEDLLPDNDV----LRLRWQGGRVVIRPSGTEPKLKAYLE 545
Cdd:cd05801 462 LaKLTRAPGNGAsiggLKVTTANGWFAARPSGTEDVYKIYAE 503
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
97-344 |
1.99e-13 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 72.32 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 97 RGPVragPNGMNRVVVRRAAAGLAAWLTAQGrsGEPVVVGYDGRHGSAEFAHDSAAIFAAAGFDARLLPrLLPTPVLAFA 176
Cdd:PRK09542 7 RGVV---GEQIDEDLVRDVGAAFARLMRAEG--ATTVVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIG-LASTDQLYFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 177 VQHLGAAaGVMVTASHNPPQDNGYKVYVAdGAQiapPVDVEIE-AAIRAVASArGVPLSD--RYTVLGEDIVDAYVGAVA 253
Cdd:PRK09542 81 SGLLDCP-GAMFTASHNPAAYNGIKLCRA-GAK---PVGQDTGlAAIRDDLIA-GVPAYDgpPGTVTERDVLADYAAFLR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 254 GLIGP-GSREVRIVHTAMHGVGTEVITKVFAAagfAPMHGVPQQAAPDADFPTVSfPNPEETGALDLALALAREQDADLV 332
Cdd:PRK09542 155 SLVDLsGIRPLKVAVDAGNGMGGHTVPAVLGG---LPITLLPLYFELDGTFPNHE-ANPLDPANLVDLQAFVRETGADIG 230
|
250
....*....|..
gi 2416456659 333 IANDPDADRCAV 344
Cdd:PRK09542 231 LAFDGDADRCFV 242
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
358-439 |
8.07e-12 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 62.08 E-value: 8.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 358 GDQVGVLLADALLRKGVRGTYA---TTIVSSSMLGAMAARNQVPYRETLTGFKWISRA--APDLVFGYEEAlGYAVAPEL 432
Cdd:pfam02880 2 GDQILALLAKYLLEQGKLPPGAgvvKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKmrEEGALFGGEES-GHIIFLDH 80
|
....*..
gi 2416456659 433 VRDKDGI 439
Cdd:pfam02880 81 ATTKDGI 87
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
91-229 |
1.25e-11 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 66.70 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 91 FGTAGLRGPVRAGPngMNRVVVRRA--AAGLAawLTAQGRSgePVVVGYDGRHGSAEFahDSA--AIFAAAGFDARLL-P 165
Cdd:PRK10887 4 FGTDGIRGKVGQAP--ITPDFVLKLgwAAGKV--LARQGRP--KVLIGKDTRISGYML--ESAleAGLAAAGVDVLLTgP 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2416456659 166 rlLPTPVLAFAVQHLGAAAGVMVTASHNPPQDNGYKVYVADGAQIAPPVDVEIEAAIRA----VASAR 229
Cdd:PRK10887 76 --MPTPAVAYLTRTLRAEAGIVISASHNPYYDNGIKFFSADGTKLPDEVELAIEAELDKpltcVESAE 141
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
133-372 |
1.38e-11 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 66.89 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 133 VVVGYDGRHGSAEFAHDSAAIFAAAGFDArLLPRLLPTPVLAFAVQHLGAAAGVMVTASHNPPQDNGYKVyVADGAQiap 212
Cdd:PRK15414 41 IVLGGDVRLTSETLKLALAKGLQDAGVDV-LDIGMSGTEEIYFATFHLGVDGGIEVTASHNPMDYNGMKL-VREGAR--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 213 PV--DVEIEAAIRaVASARGVPLSD-----RYTVLgeDIVDAYVGAVAGLIGPGS-REVRIVHTAMHGVGTEVITKV--- 281
Cdd:PRK15414 116 PIsgDTGLRDVQR-LAEANDFPPVDetkrgRYQQI--NLRDAYVDHLFGYINVKNlTPLKLVINSGNGAAGPVVDAIear 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 282 FAAAGfAPMHGVPQQAAPDADFPTvSFPNPEETGALDLALALAREQDADLVIANDPDADRCAVAvpDASGEWrmLRGDQV 361
Cdd:PRK15414 193 FKALG-APVELIKVHNTPDGNFPN-GIPNPLLPECRDDTRNAVIKHGADMGIAFDGDFDRCFLF--DEKGQF--IEGYYI 266
|
250
....*....|.
gi 2416456659 362 GVLLADALLRK 372
Cdd:PRK15414 267 VGLLAEAFLEK 277
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
116-386 |
1.07e-10 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 64.31 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 116 AAGLAAWLTAQGR---SGEP-VVVGYDGRHGSAEFAHDSAAIFAAAGFDArLLPRLLPTPVLAFAVQHLGAA--AGVMVT 189
Cdd:PLN02371 97 GAAFAEWLLEKKKadgSGELrVSVGRDPRISGPRLADAVFAGLASAGLDV-VDMGLATTPAMFMSTLTEREDydAPIMIT 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 190 ASHNPPQDNGYKVYVADGAQIAPPVDVEIEAAIRA---------VASARG-------VPLSDRYTVLGEDIVDAYVGAVA 253
Cdd:PLN02371 176 ASHLPYNRNGLKFFTKDGGLGKPDIKDILERAARIykewsdeglLKSSSGassvvcrVDFMSTYAKHLRDAIKEGVGHPT 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 254 GLIGPgSREVRIVHTAMHGVGTEVITKVFAAAGfAPMHGvPQQAAPDADFPTVSfPNPEETGALDLALALAREQDADLVI 333
Cdd:PLN02371 256 NYETP-LEGFKIVVDAGNGAGGFFAEKVLEPLG-ADTSG-SLFLEPDGMFPNHI-PNPEDKAAMSATTQAVLANKADLGI 331
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2416456659 334 ANDPDADRCAVAvpDASGewRMLRGDQVGVLLADALLRK--GvrgtyaTTIVSSS 386
Cdd:PLN02371 332 IFDTDVDRSAVV--DSSG--REINRNRLIALMSAIVLEEhpG------TTIVTDS 376
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
157-212 |
3.15e-07 |
|
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: 52.98 E-value: 3.15e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2416456659 157 AGF--DARLLPR-LLPTPVLA--FAVQHLGAAAGVMVTASHNPPQDNGYKVYVADGAQIAP 212
Cdd:cd03086 5 AGFrtKAELLDSvVFRVGILAalRSKKLGGKTIGVMITASHNPVEDNGVKIVDPDGEMLEE 65
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
184-212 |
2.27e-05 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 47.34 E-value: 2.27e-05
10 20
....*....|....*....|....*....
gi 2416456659 184 AGVMVTASHNPPQDNGYKVYVADGAQIAP 212
Cdd:PTZ00302 77 VGVMITASHNPIQDNGVKIIDPDGGMLEE 105
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
92-536 |
7.00e-05 |
|
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: 45.68 E-value: 7.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 92 GTAGLRGPVRA--GPNGMNRVVvrraAAGLAAwLTAQGRSGEPVVVGYDGRHGSAEFAHDSAAIFAAAGFdARLL---PR 166
Cdd:cd03085 14 GTSGLRKKVKVfqQPNYLENFV----QSIFNA-LPPEKLKGATLVVGGDGRYYNKEAIQIIIKIAAANGV-GKVVvgqNG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 167 LLPTPVLAFAVQHLGAAAGVMVTASHNP--P-QDNGYKVYVADGA--------------------QIAPPVDVEIeaair 223
Cdd:cd03085 88 LLSTPAVSAVIRKRKATGGIILTASHNPggPeGDFGIKYNTSNGGpapesvtdkiyeitkkiteyKIADDPDVDL----- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 224 avaSARGVPLSDRYTVLGE--DIVDAYV---------GAVAGLIGPGSREVRIvhTAMHGV----GTEVITKVFAAAGFA 288
Cdd:cd03085 163 ---SKIGVTKFGGKPFTVEviDSVEDYVelmkeifdfDAIKKLLSRKGFKVRF--DAMHGVtgpyAKKIFVEELGAPESS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 289 PMHGVPqqaAPDadfptvsF----PNPEETGALDLALALAREqDADLVIANDPDADRcavavpdasgewRMLRG------ 358
Cdd:cd03085 238 VVNCTP---LPD-------FggghPDPNLTYAKDLVELMKSG-EPDFGAASDGDGDR------------NMILGkgffvt 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 359 --DQVGVLLADALL-----RKGVRGtYATTIVSSSMLGAMAARNQVPYRETLTGFKWISRA--APDLVFGYEEALGyaVA 429
Cdd:cd03085 295 psDSVAVIAANAKLipyfyKGGLKG-VARSMPTSGALDRVAKKLGIPLFETPTGWKFFGNLmdAGKLSLCGEESFG--TG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 430 PELVRDKDGI-------SAALLVaelaaalkadGSSLTQRLEQLYAEYGR-YAT--DQVSVrveDLALIAAMMQRLRAR- 498
Cdd:cd03085 372 SDHIREKDGLwavlawlSILAHR----------NVSVEDIVKEHWQKYGRnFYTryDYEEV---DSEAANKMMDHLRALv 438
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2416456659 499 --PPTQLLGRPVT--------------VEDLLPDNDVLRLRWQGG-RVVIRPSGT 536
Cdd:cd03085 439 sdLPGVGKSGDKGykvakaddfsytdpVDGSVSKKQGLRIIFEDGsRIIFRLSGT 493
|
|
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
133-440 |
1.12e-04 |
|
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: 44.93 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 133 VVVGYDGRHGSAEFAHDSAAIFAAAGFDARLLpRLLPTPVLAFAVQHLGAAAGVMVTASHNPPQDNGYKVYVADGAQIAP 212
Cdd:cd05805 37 VTVSRDASRASRMLKRALISGLLSTGVNVRDL-GALPLPVARYAIRFLGASGGIHVRTSPDDPDKVEIEFFDSRGLNISR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 213 PVDVEIEAA-IR-AVASARGVPLSDRYTVlgEDIVDAYVGAVAGLIGP---GSREVRIVHTAMHGVGTEVITKVFAAAGF 287
Cdd:cd05805 116 AMERKIENAfFReDFRRAHVDEIGDITEP--PDFVEYYIRGLLRALDTsglKKSGLKVVIDYAYGVAGIVLPGLLSRLGC 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416456659 288 APMhgvpqqAAPDADFPTVSFPNPEETGALDLALALAREQDADLVIANDPDADRcaVAVPDASGewRMLRGDQVGVLLAD 367
Cdd:cd05805 194 DVV------ILNARLDEDAPRTDTERQRSLDRLGRIVKALGADFGVIIDPNGER--LILVDEAG--RVISDDLLTALVSL 263
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2416456659 368 ALLRKGVRGTYATTIVSSSMLGAMAARNQVPYRETLTGFK-WISRAAPDLVFGYEEALGYAVaPELVRDKDGIS 440
Cdd:cd05805 264 LVLKSEPGGTVVVPVTAPSVIEQLAERYGGRVIRTKTSPQaLMEAALENVVLAGDGDGGFIF-PEFHPGFDAIA 336
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
180-207 |
5.98e-04 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 42.70 E-value: 5.98e-04
10 20
....*....|....*....|....*...
gi 2416456659 180 LGAAAGVMVTASHNPPQDNGYKVYVADG 207
Cdd:PLN02895 56 TGAATGLMITASHNPVSDNGVKIVDPSG 83
|
|
| |
