|
Name |
Accession |
Description |
Interval |
E-value |
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
8-446 |
0e+00 |
|
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: 634.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 8 LFGTSGIRGEIGSEVTGELALNVGKSLSYYLGNeGTVVLGYDTRTTSKMLNQAITAGLVESGVNVIKVGMVPTPLVGYAT 87
Cdd:cd03087 1 LFGTSGIRGVVGEELTPELALKVGKALGTYLGG-GTVVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDIGIVPTPALQYAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 88 DRLGaDAGIMITASHNPSKYNGIKIWDKNGMAYTPEQESEIEDIYLNKKYVNVGWDKIGSITENNEIKKVYMDDLLSMVN 167
Cdd:cd03087 80 RKLG-DAGVMITASHNPPEYNGIKLVNPDGTEFSREQEEEIEEIIFSERFRRVAWDEVGSVRREDSAIDEYIEAILDKVD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 168 IEP--GFKVVIDCASGAGSEISPIVFRRAGCEVITLNSQVDGFFPGRNPEPNDANLGSLKKVVKATGADLGIAHDGDADR 245
Cdd:cd03087 159 IDGgkGLKVVVDCGNGAGSLTTPYLLRELGCKVITLNANPDGFFPGRPPEPTPENLSELMELVRATGADLGIAHDGDADR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 246 MMAVDETGKVVNFDKLLALVA----SEFGGTVVTTVDAGFIMDEELEKVCGNVLRTPVGDVAVADGILKNNASFGGEPSG 321
Cdd:cd03087 239 AVFVDEKGRFIDGDKLLALLAkyllEEGGGKVVTPVDASMLVEDVVEEAGGEVIRTPVGDVHVAEEMIENGAVFGGEPNG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 322 TWLHPDFCMCPDGLLSGLRLADIVSHKGPLSKLLDQMPDYPNIREKVTCSKEDKVKIMENMDEELENAFDDikeINTIDG 401
Cdd:cd03087 319 GWIFPDHQLCRDGIMTAALLLELLAEEKPLSELLDELPKYPLLREKVECPDEKKEEVMEAVEEELSDADED---VDTIDG 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2630008627 402 VRISLNDGsWVLVRPSGTENYIRITLEAKTEEKANEIKNICLDII 446
Cdd:cd03087 396 VRIEYEDG-WVLIRPSGTEPKIRITAEAKTEERAKELLEEGRSKV 439
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
6-446 |
0e+00 |
|
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: 591.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 6 KKLFGTSGIRGEIGSEVTGELALNVGKSLSYYLGnEGTVVLGYDTRTTSKMLNQAITAGLVESGVNVIKVGMVPTPLVGY 85
Cdd:TIGR03990 1 MLLFGTSGIRGIVGEELTPELALKVGKAFGTYLR-GGKVVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLGIAPTPTLQY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 86 ATDRLGADAGIMITASHNPSKYNGIKIWDKNGMAYTPEQESEIEDIYLNKKYVNVGWDKIGSITENNEIKKVYMDDLLSM 165
Cdd:TIGR03990 80 AVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQEEEIEEIAESGDFERADWDEIGTVTSDEDAIDDYIEAILDK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 166 VNIEP----GFKVVIDCASGAGSEISPIVFRRAGCEVITLNSQVDGFFPGRNPEPNDANLGSLKKVVKATGADLGIAHDG 241
Cdd:TIGR03990 160 VDVEAirkkGFKVVVDCGNGAGSLTTPYLLRELGCKVITLNCQPDGTFPGRNPEPTPENLKDLSALVKATGADLGIAHDG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 242 DADRMMAVDETGKVVNFDKLLALVASEF----GGTVVTTVDAGFIMDEELEKVCGNVLRTPVGDVAVADGILKNNASFGG 317
Cdd:TIGR03990 240 DADRLVFIDEKGRFIGGDYTLALFAKYLlehgGGKVVTNVSSSRAVEDVAERHGGEVIRTKVGEVNVAEKMKEEGAVFGG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 318 EPSGTWLHPDFCMCPDGLLSGLRLADIVSHKG-PLSKLLDQMPDYPNIREKVTCSKEDKVKIMENMDEELENAfddikEI 396
Cdd:TIGR03990 320 EGNGGWIFPDHHYCRDGLMAAALFLELLAEEGkPLSELLAELPKYPMSKEKVELPDEDKEEVMEAVEEEFADA-----EI 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2630008627 397 NTIDGVRISLNDGsWVLVRPSGTENYIRITLEAKTEEKANEIKNICLDII 446
Cdd:TIGR03990 395 DTIDGVRIDFEDG-WVLVRPSGTEPIVRIYAEAKTEERAEELLEEGRSLV 443
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
1-450 |
0e+00 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 524.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 1 MASvgKKLFGTSGIRGEIGSEVTGELALNVGKSLSYYLGNEG--TVVLGYDTRTTSKMLNQAITAGLVESGVNVIKVGMV 78
Cdd:COG1109 1 MTY--KKLFGTDGIRGIVGEELTPEFVLKLGRAFGTYLKEKGgpKVVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 79 PTPLVGYATDRLGADAGIMITASHNPSKYNGIKIWDKNGMAYTPEQESEIEDIYLNKKYVNVGWDKIGSITENNEIKKVY 158
Cdd:COG1109 79 PTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKEDFRRAEAEEIGKVTRIEDVLEAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 159 MDDLLSMVN---IEPGFKVVIDCASGAGSEISPIVFRRAGCEVITLNSQVDGFFPGRNPEPNDANLGSLKKVVKATGADL 235
Cdd:COG1109 159 IEALKSLVDealRLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFPNHNPNPEPENLEDLIEAVKETGADL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 236 GIAHDGDADRMMAVDETGKVVNFDKLLALVASEF-----GGTVVTTVDAGFIMDEELEKVCGNVLRTPVGDVAVADGILK 310
Cdd:COG1109 239 GIAFDGDADRLGVVDEKGRFLDGDQLLALLARYLlekgpGGTVVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKMRE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 311 NNASFGGEPSGTWLHPDFCMCPDGLLSGLRLADIVSHKG-PLSKLLDQMPDYPNIREKVTCskEDKVKIMENMdEELENA 389
Cdd:COG1109 319 TGAVLGGEESGGIIFPDFVPTDDGILAALLLLELLAKQGkSLSELLAELPRYPQPEINVRV--PDEEKIGAVM-EKLREA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2630008627 390 FDDIKEINTIDGVRISLNDGSWVLVRPSGTENYIRITLEAKTEEKANEIKNICLDIINSHL 450
Cdd:COG1109 396 VEDKEELDTIDGVKVDLEDGGWVLVRPSGTEPLLRVYAEAKDEEEAEELLAELAELVEEAL 456
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
8-438 |
1.53e-130 |
|
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: 383.76 E-value: 1.53e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 8 LFGTSGIRGEIGSEVTGELALNVGKSLSYYLGNEG---TVVLGYDTRTTSKMLNQAITAGLVESGVNVIKVGMVPTPLVG 84
Cdd:cd05802 1 LFGTDGIRGVANEPLTPELALKLGRAAGKVLGKGGgrpKVLIGKDTRISGYMLESALAAGLTSAGVDVLLLGVIPTPAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 85 YATDRLGADAGIMITASHNPSKYNGIKIWDKNGMAYTPEQESEIEDIYLNKKYVNVGWDKIGSITENNEIKKVYMDDLLS 164
Cdd:cd05802 81 YLTRKLRADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVEEEIEALIDKELELPPTGEKIGRVYRIDDARGRYIEFLKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 165 MVNIE--PGFKVVIDCASGAGSEISPIVFRRAGCEVITLNSQVDGFfpgrnpepN-DANLGS-----LKKVVKATGADLG 236
Cdd:cd05802 161 TFPKDllSGLKIVLDCANGAAYKVAPEVFRELGAEVIVINNAPDGL--------NiNVNCGSthpesLQKAVLENGADLG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 237 IAHDGDADRMMAVDETGKVVNFDKLLALVASEF-------GGTVVTTVDAGFIMDEELEKVCGNVLRTPVGDVAVADGIL 309
Cdd:cd05802 233 IAFDGDADRVIAVDEKGNIVDGDQILAICARDLkergrlkGNTVVGTVMSNLGLEKALKELGIKLVRTKVGDRYVLEEML 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 310 KNNASFGGEPSGTWLHPDFCMCPDGLLSGLRLADIVSHKG-PLSKLLDQMPDYP----NIREKvtcskeDKVKIMENmdE 384
Cdd:cd05802 313 KHGANLGGEQSGHIIFLDHSTTGDGLLTALQLLAIMKRSGkSLSELASDMKLYPqvlvNVRVK------DKKALLEN--P 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2630008627 385 ELENAFDDIKEIntidgvrisLNDGSWVLVRPSGTENYIRITLEAKTEEKANEI 438
Cdd:cd05802 385 RVQAAIAEAEKE---------LGGEGRVLVRPSGTEPLIRVMVEGEDEELVEKL 429
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
8-446 |
1.01e-118 |
|
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: 354.13 E-value: 1.01e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 8 LFGTSGIRGEIGSEVTGELALNVGKSLSYYLGNEG--TVVLGYDTRTTSKMLNQAITAGLVESGVNVIKVGMVPTPLVGY 85
Cdd:cd03089 1 IFRAYDIRGIAGEELTEEIAYAIGRAFGSWLLEKGakKVVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPVLYF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 86 ATDRLGADAGIMITASHNPSKYNGIKIWdKNGMAYTPEQESEIEDIYLNKKYVNVgwDKIGSITENNeIKKVYMDDLLSM 165
Cdd:cd03089 81 ATFHLDADGGVMITASHNPPEYNGFKIV-IGGGPLSGEDIQALRERAEKGDFAAA--TGRGSVEKVD-ILPDYIDRLLSD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 166 VNIEP-GFKVVIDCASGAGSEISPIVFRRAGCEVITLNSQVDGFFPGRNPEP-NDANLGSLKKVVKATGADLGIAHDGDA 243
Cdd:cd03089 157 IKLGKrPLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCEPDGTFPNHHPDPtDPENLEDLIAAVKENGADLGIAFDGDG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 244 DRMMAVDETGKVVNFDKLLALVASEF-----GGTVVTTVDAGFIMDEELEKVCGNVLRTPVGDVAVADGILKNNASFGGE 318
Cdd:cd03089 237 DRLGVVDEKGEIIWGDRLLALFARDIlkrnpGATIVYDVKCSRNLYDFIEEAGGKPIMWKTGHSFIKAKMKETGALLAGE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 319 PSG------TWLHPDfcmcpDGLLSGLRLADIVSHKG-PLSKLLDQMPDYPNIRE-KVTCSKEDKVKIMenmdEELENAF 390
Cdd:cd03089 317 MSGhiffkdRWYGFD-----DGIYAALRLLELLSKSGkTLSELLADLPKYFSTPEiRIPVTEEDKFAVI----ERLKEHF 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2630008627 391 DDI-KEINTIDGVRISLNDGsWVLVRPSGTENYIRITLEAKTEEKANEIKNICLDII 446
Cdd:cd03089 388 EFPgAEIIDIDGVRVDFEDG-WGLVRASNTEPVLVLRFEADTEEGLEEIKAELRKLL 443
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
12-438 |
5.19e-101 |
|
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: 308.85 E-value: 5.19e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 12 SGIRGEIGSEVTGELALNVGKSLSYYL---GNEGTVVLGYDTRTTSKMLNQAITAGLVESGVNVIKVGMVPTPLVGYATD 88
Cdd:cd05803 5 SGIRGIVGEGLTPEVITRYVAAFATWQperTKGGKIVVGRDGRPSGPMLEKIVIGALLACGCDVIDLGIAPTPTVQVLVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 89 RLGADAGIMITASHNPSKYNGIKIWDKNGMAYTPEQESEIEDIYLNKKYVNVGWDKIGSITENNEIKKVYMDDLLSMVNI 168
Cdd:cd05803 85 QSQASGGIIITASHNPPQWNGLKFIGPDGEFLTPDEGEEVLSCAEAGSAQKAGYDQLGEVTFSEDAIAEHIDKVLALVDV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 169 EP------GFKVVIDCASGAGSEISPIVFRRAGCEVITLNSQVDGFFPgRNPEPNDANLGSLKKVVKATGADLGIAHDGD 242
Cdd:cd05803 165 DVikirerNFKVAVDSVNGAGGLLIPRLLEKLGCEVIVLNCEPTGLFP-HTPEPLPENLTQLCAAVKESGADVGFAVDPD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 243 ADRMMAVDETGKVVNFDKLLALvASEF-------GGTVVTTVDAGFIMDEELEKVCGNVLRTPVGDVAVADGILKNNASF 315
Cdd:cd05803 244 ADRLALVDEDGRPIGEEYTLAL-AVDYvlkyggrKGPVVVNLSTSRALEDIARKHGVPVFRSAVGEANVVEKMKEVDAVI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 316 GGEPSGTWLHPDFCMCPDGLLS-GLRLADIVSHKGPLSKLLDQMPDYPNIREKVTCSKEDkvkiMENMDEELENAFDDiK 394
Cdd:cd05803 323 GGEGNGGVILPDVHYGRDSLVGiALVLQLLAASGKPLSEIVDELPQYYISKTKVTIAGEA----LERLLKKLEAYFKD-A 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2630008627 395 EINTIDGVRISLNDgSWVLVRPSGTENYIRITLEAKTEEKANEI 438
Cdd:cd05803 398 EASTLDGLRLDSED-SWVHVRPSNTEPIVRIIAEAPTQDEAEAL 440
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
9-438 |
4.97e-96 |
|
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: 296.39 E-value: 4.97e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 9 FGTSGIRGEIGSEVTGE----LALNVGKSLSYYLGNEGTVVLGYDTRTTSKMLNQAITAGLVESGVNVIKV-GMVPTPLV 83
Cdd:cd05800 3 FGTDGWRGIIAEDFTFEnvrrVAQAIADYLKEEGGGGRGVVVGYDTRFLSEEFARAVAEVLAANGIDVYLSdRPVPTPAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 84 GYATDRLGADAGIMITASHNPSKYNGIKIWDKNGMAYTPEQESEIEDiYLNKKYVNVGWDKIGSITENNEIKKVYMDDLL 163
Cdd:cd05800 83 SWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEA-RLASGEPPGLEARAEGLIETIDPKPDYLEALR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 164 SMVNIEP----GFKVVIDCASGAGSEISPIVFRRAGCEVITLNSQVDGFFPGRNPEPNDANLGSLKKVVKATGADLGIAH 239
Cdd:cd05800 162 SLVDLEAireaGLKVVVDPMYGAGAGYLEELLRGAGVDVEEIRAERDPLFGGIPPEPIEKNLGELAEAVKEGGADLGLAT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 240 DGDADRMMAVDETGKVVNFDKLLALVAS---EFGGT---VVTTVDAGFIMDEELEKVCGNVLRTPVGDVAVADGILKNNA 313
Cdd:cd05800 242 DGDADRIGAVDEKGNFLDPNQILALLLDyllENKGLrgpVVKTVSTTHLIDRIAEKHGLPVYETPVGFKYIAEKMLEEDV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 314 SFGGEPSG--TWLH--PDfcmcPDGLLSGLRLADIVSHKG-PLSKLLDQMPD-----YPNiREKVTCSKEDKVKIMENMD 383
Cdd:cd05800 322 LIGGEESGglGIRGhiPE----RDGILAGLLLLEAVAKTGkPLSELVAELEEeygpsYYD-RIDLRLTPAQKEAILEKLK 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2630008627 384 EE--LENAFDDIKEINTIDGVRISLNDGSWVLVRPSGTENYIRITLEAKTEEKANEI 438
Cdd:cd05800 397 NEppLSIAGGKVDEVNTIDGVKLVLEDGSWLLIRPSGTEPLLRIYAEAPSPEKVEAL 453
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
9-446 |
1.31e-94 |
|
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: 292.35 E-value: 1.31e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 9 FGTSGIRGEIGSE-VTGELALNVGKSLSYYLGNEGT----VVLGYDTRTTSKMLNQAITAGLVESGVNVIKVGMVPTPLV 83
Cdd:TIGR01455 1 FGTDGVRGRAGQEpLTAELALLLGAAAGRVLRQGRDtaprVVIGKDTRLSGYMLENALAAGLNSAGVDVLLLGPLPTPAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 84 GYATDRLGADAGIMITASHNPSKYNGIKIWDKNGMAYTPEQESEIEDIYLNKKYVN-VGWDKIGSITENNEIKKVYMDDL 162
Cdd:TIGR01455 81 AYLTRTLRADAGVMISASHNPYEDNGIKFFGPGGFKLDDATEAAIEALLDEADPLPrPESEGLGRVKRYPDAVGRYIEFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 163 LSMVNIEP---GFKVVIDCASGAGSEISPIVFRRAGCEVITLNSQVDGFfpGRNPEPNDANLGSLKKVVKATGADLGIAH 239
Cdd:TIGR01455 161 KSTLPRGLtlsGLKVVLDCANGAAYKVAPHVFRELGAEVIAIGVEPDGL--NINDGCGSTHLDALQKAVREHGADLGIAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 240 DGDADRMMAVDETGKVVNFDKLLALVASEF-------GGTVVTTVDAGFIMDEELEKVCGNVLRTPVGDVAVADGILKNN 312
Cdd:TIGR01455 239 DGDADRVLAVDANGRIVDGDQILYIIARALkesgelaGNTVVATVMSNLGLERALEKLGLTLIRTAVGDRYVLEEMRESG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 313 ASFGGEPSGTWLHPDFCMCPDGLLSGLRLADIVSHKG-PLSKLLDQMPDYPNIREKVtCSKEDKVKIMEnmDEELENAFD 391
Cdd:TIGR01455 319 YNLGGEQSGHIILLDYSTTGDGIVSALQVLTIMKKSGsTLSELAAEFVPYPQTLVNV-RVADRKLAAAE--APAVKAAIE 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2630008627 392 DikeintidgVRISLNDGSWVLVRPSGTENYIRITLEAKTEEKANEIKNICLDII 446
Cdd:TIGR01455 396 D---------AEAELGGTGRILLRPSGTEPLIRVMVEAADEELVQQLADTLADVV 441
|
|
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
8-446 |
1.70e-77 |
|
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: 247.93 E-value: 1.70e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 8 LFGTSGIRGEIGSEVTGELALNVGKSLSYYLGNEGTVVLGYDTRTTSKMLNQAITAGLVESGVNVIKVGMVPTPLVGYAT 87
Cdd:cd05805 1 LFGGRGVSGLINVDITPEFATRLGAAYGSTLPPGSTVTVSRDASRASRMLKRALISGLLSTGVNVRDLGALPLPVARYAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 88 DRLGADAGIMITASHNPSKYNGIKIWDKNGMAYTPEQESEIEDIYLNKKYVNVGWDKIGSITENNEIKKVYMDDLLSMVN 167
Cdd:cd05805 81 RFLGASGGIHVRTSPDDPDKVEIEFFDSRGLNISRAMERKIENAFFREDFRRAHVDEIGDITEPPDFVEYYIRGLLRALD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 168 IEP----GFKVVIDCASGAGSEISPIVFRRAGCEVITLNSQVDGFFPgRNPEPNDANLGSLKKVVKATGADLGIAHDGDA 243
Cdd:cd05805 161 TSGlkksGLKVVIDYAYGVAGIVLPGLLSRLGCDVVILNARLDEDAP-RTDTERQRSLDRLGRIVKALGADFGVIIDPNG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 244 DRMMAVDETGKVVNFDKLLALV-----ASEFGGTVVTTVDAGFIMDEELEKVCGNVLRTPVGDVAVADGILKNNAsFGGE 318
Cdd:cd05805 240 ERLILVDEAGRVISDDLLTALVsllvlKSEPGGTVVVPVTAPSVIEQLAERYGGRVIRTKTSPQALMEAALENVV-LAGD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 319 PSGTWLHPDFCMCPDGLLSGLRLADIVSHKG-PLSKLLDQMPDYPNIREKVTCSKEDKVKIMENMDEELENafddiKEIN 397
Cdd:cd05805 319 GDGGFIFPEFHPGFDAIAALVKILEMLARTNiSLSQIVDELPRFYVLHKEVPCPWEAKGRVMRRLIEEAPD-----KSIE 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2630008627 398 TIDGVRISLNDGsWVLVRPSGTENYIRITLEAKTEEKANEIKNICLDII 446
Cdd:cd05805 394 LIDGVKIYEDDG-WVLVLPDADEPLCHIYAEGSDQERAEELTEFYVEKV 441
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
74-446 |
1.18e-74 |
|
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: 238.02 E-value: 1.18e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 74 KVGMVPTPLVGYATDR-LGADAGIMITASHNPSKYNGIKIWDKNGMAYTPEQESEIEDIYL-NKKYVNVGWDkIGSITEN 151
Cdd:cd03084 10 VVGDDITPETAVALGQaIGSTGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEkEDEPSAVAYE-LGGSVKA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 152 NEIKKVYMDDLLSMVNI----EPGFKVVIDCASGAGSEISPIVFRRAGCEVITLNSQVDGFFPGRNPEPN-DANLGSLKK 226
Cdd:cd03084 89 VDILQRYFEALKKLFDVaalsNKKFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCEPDGNFGNINPDPGsETNLKQLLA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 227 VVKATGADLGIAHDGDADRMMAVDETGKVVNFDKLLALVASEF------GGTVVTTVDAGFIMDEELEKVCGNVLRTPVG 300
Cdd:cd03084 169 VVKAEKADFGVAFDGDADRLIVVDENGGFLDGDELLALLAVELfltfnpRGGVVKTVVSSGALDKVAKKLGIKVIRTKTG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 301 DVAVADGILKNNASFGGEPSGTWLHPDFCMCPDGLLSGLRLADIVSHKGP-LSKLLDQMPDYPNIREKVTcskedkvkim 379
Cdd:cd03084 249 FKWVGEAMQEGDVVLGGEESGGVIFPEFHPGRDGISAALLLLEILANLGKsLSELFSELPRYYYIRLKVR---------- 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2630008627 380 enmdeelenafddikeintidgvrislndgSWVLVRPSGTENYIRITLEAKTEEKANEIKNICLDII 446
Cdd:cd03084 319 ------------------------------GWVLVRASGTEPAIRIYAEADTQEDVEQIKKEARELV 355
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
6-437 |
1.01e-72 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 235.42 E-value: 1.01e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 6 KKLFGTSGIRGEIGSE-VTGELALNVGKSLSYYLGNEG--TVVLGYDTRTTSKMLNQAITAGLVESGVNVIKVGMVPTPL 82
Cdd:PRK10887 1 RKYFGTDGIRGKVGQApITPDFVLKLGWAAGKVLARQGrpKVLIGKDTRISGYMLESALEAGLAAAGVDVLLTGPMPTPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 83 VGYATDRLGADAGIMITASHNPSKYNGIKIWDKNGMAYTPEQESEIEDIyLNKKYVNVGWDKIGSITENNEIKKVYmddl 162
Cdd:PRK10887 81 VAYLTRTLRAEAGIVISASHNPYYDNGIKFFSADGTKLPDEVELAIEAE-LDKPLTCVESAELGKASRINDAAGRY---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 163 lsmvnIE------P------GFKVVIDCASGAGSEISPIVFRRAGCEVITLNSQVDGFfpGRNPEPNDANLGSLKKVVKA 230
Cdd:PRK10887 156 -----IEfckstfPnelslrGLKIVVDCANGATYHIAPNVFRELGAEVIAIGCEPNGL--NINDECGATDPEALQAAVLA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 231 TGADLGIAHDGDADRMMAVDETGKVVNFDKLLALVASE------FGGTVVTTVDAGFIMDEELEKVCGNVLRTPVGDVAV 304
Cdd:PRK10887 229 EKADLGIAFDGDGDRVIMVDHLGNLVDGDQLLYIIARDrlrrgqLRGGVVGTLMSNMGLELALKQLGIPFVRAKVGDRYV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 305 ADGILKNNASFGGEPSGTWLHPDFCMCPDGLLSGLR-LADIVSHKGPLSKLLDQMPDYPNIREKVTCSKedkvkimeNMD 383
Cdd:PRK10887 309 LEKLQEKGWRLGGENSGHILCLDKTTTGDGIVAALQvLAAMVRSGMSLADLCSGMKLFPQVLINVRFKP--------GAD 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2630008627 384 EELENafDDIKEIntIDGVRISLNDGSWVLVRPSGTENYIRITLEAKTEEKANE 437
Cdd:PRK10887 381 DPLES--EAVKAA--LAEVEAELGGRGRVLLRKSGTEPLIRVMVEGEDEAQVTA 430
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
14-449 |
1.57e-62 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 209.07 E-value: 1.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 14 IRGEIGSEVTGELALNVGKSLSYYLGNEG--TVVLGYDTRTTSKMLNQAITAGLVESGVNVIKVGMVPTPLVGYATDRLG 91
Cdd:PRK09542 6 VRGVVGEQIDEDLVRDVGAAFARLMRAEGatTVVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIGLASTDQLYFASGLLD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 92 AdAGIMITASHNPSKYNGIK--------IWDKNGMAytpeqesEIEDIYLNKkyVNVGWDKIGSITENNEIKKvYMDDLL 163
Cdd:PRK09542 86 C-PGAMFTASHNPAAYNGIKlcragakpVGQDTGLA-------AIRDDLIAG--VPAYDGPPGTVTERDVLAD-YAAFLR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 164 SMVN---IEPgFKVVIDCASGAGSEISPIVFRRAGCEVITLNSQVDGFFPGRNPEPND-ANLGSLKKVVKATGADLGIAH 239
Cdd:PRK09542 155 SLVDlsgIRP-LKVAVDAGNGMGGHTVPAVLGGLPITLLPLYFELDGTFPNHEANPLDpANLVDLQAFVRETGADIGLAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 240 DGDADRMMAVDETGKVVNFDKLLALVAS-----EFGGTVVTTVDAGFIMDEELEKVCGNVLRTPVGDVAVADGILKNNAS 314
Cdd:PRK09542 234 DGDADRCFVVDERGQPVSPSAVTALVAArelarEPGATIIHNLITSRAVPELVAERGGTPVRTRVGHSFIKALMAETGAI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 315 FGGEPSGTWLHPDFCMCPDGLLSGLR-LADIVSHKGPLSKLLDQMPDYP---NIREKVtcskEDKVKIMenmdEELENAF 390
Cdd:PRK09542 314 FGGEHSAHYYFRDFWGADSGMLAALHvLAALGEQDRPLSELMADYQRYAasgEINSTV----ADAPARM----EAVLKAF 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 391 -DDIKEINTIDGVRISLNDGSWVLVRPSGTENYIRITLEAKTEEKANEIKNICLDIINSH 449
Cdd:PRK09542 386 aDRIVSVDHLDGVTVDLGDGSWFNLRASNTEPLLRLNVEARTEEEVDALVDEVLAIIRAQ 445
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
6-134 |
1.92e-50 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 167.40 E-value: 1.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 6 KKLFGTSGIRGEIGS-EVTGELALNVGKSLSYYLGNE---GTVVLGYDTRTTSKMLNQAITAGLVESGVNVIKVGMVPTP 81
Cdd:pfam02878 1 RQLFGTSGIRGKVGVgELTPEFALKLGQAIASYLRAQgggGKVVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2630008627 82 LVGYATDRLGADAGIMITASHNPSKYNGIKIWDKNGMAYTPEQESEIEDIYLN 134
Cdd:pfam02878 81 AVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEK 133
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
9-447 |
5.88e-46 |
|
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: 165.76 E-value: 5.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 9 FGTSGIRGEIGSevtGELALN---VGK---SLSYYLGNEG------TVVLGYDTRTTSKMLnqAITAGLVESGvNVIKV- 75
Cdd:cd05799 4 FGTAGLRGKMGA---GTNRMNdytVRQatqGLANYLKKKGpdaknrGVVIGYDSRHNSREF--AELTAAVLAA-NGIKVy 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 76 ---GMVPTPLVGYATDRLGADAGIMITASHNPSKYNGIKIWDKNGMAYTPEQESEIED-IYLNKKYVNVGWD---KIGSI 148
Cdd:cd05799 78 lfdDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEeIEAVLEPLDIKFEealDSGLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 149 TE-NNEIKKVYMDDLLSMV-----NIEPGFKVVIDCASGAGSEISPIVFRRAGCE-VITLNSQ--VDGFFPG-RNPEPND 218
Cdd:cd05799 158 KYiGEEIDDAYLEAVKKLLvnpelNEGKDLKIVYTPLHGVGGKFVPRALKEAGFTnVIVVEEQaePDPDFPTvKFPNPEE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 219 AnlGSLKKVVK---ATGADLGIAHDGDADRM-MAV------------DETG------------KVVNFDKLLALVAsefg 270
Cdd:cd05799 238 P--GALDLAIElakKVGADLILATDPDADRLgVAVkdkdgewrlltgNEIGalladylleqrkEKGKLPKNPVIVK---- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 271 gTVVTTvdagfimdEELEKVC----GNVLRTPVG---DVAVADGILKNNAS--FGGEPS-GtwlhpdFCMCP-----DGL 335
Cdd:cd05799 312 -TIVSS--------ELLRKIAkkygVKVEETLTGfkwIGNKIEELESGGKKflFGFEESiG------YLVGPfvrdkDGI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 336 LSGLRLADIVSH-----KGPLSKLLDQMPDYPNIREK---VTCSKEDKVKIMENMDEELENAFddikeintiDGVRISLN 407
Cdd:cd05799 377 SAAALLAEMAAYlkaqgKTLLDRLDELYEKYGYYKEKtisITFEGKEGPEKIKAIMDRLRNNP---------NVLTFYLE 447
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2630008627 408 DGSWVLVRPSGTENYIRITLEAKTEEKANEIKNICLDIIN 447
Cdd:cd05799 448 DGSRVTVRPSGTEPKIKFYIEVVGKKTLEEAEKKLDALKK 487
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
9-441 |
3.09e-44 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 160.50 E-value: 3.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 9 FGTSGIRGEIGSEVTGELALNVGKSLSYYLGNEgTVVLGYDTRTTSKMLNQAITAGLVESGVNVIKVGMVPTPLVGYATD 88
Cdd:PRK15414 7 FKAYDIRGKLGEELNEDIAWRIGRAYGEFLKPK-TIVLGGDVRLTSETLKLALAKGLQDAGVDVLDIGMSGTEEIYFATF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 89 RLGADAGIMITASHNPSKYNGIKIWDKNGMAYTPEQE-SEIEDIYLNKKYVNVGWDKIGSITENNeIKKVYMDDLLSMVN 167
Cdd:PRK15414 86 HLGVDGGIEVTASHNPMDYNGMKLVREGARPISGDTGlRDVQRLAEANDFPPVDETKRGRYQQIN-LRDAYVDHLFGYIN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 168 IE--PGFKVVIDCASGAGSEISPIVFRR-----AGCEVITLNSQVDGFFPGRNPEP------NDAnlgslKKVVKATGAD 234
Cdd:PRK15414 165 VKnlTPLKLVINSGNGAAGPVVDAIEARfkalgAPVELIKVHNTPDGNFPNGIPNPllpecrDDT-----RNAVIKHGAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 235 LGIAHDGDADRMMAVDETGKVVNFDKLLALVASEFggtVVTTVDAGFIMDEEL----EKVCGNVLRTPV----GDVAVAD 306
Cdd:PRK15414 240 MGIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAF---LEKNPGAKIIHDPRLswntVDVVTAAGGTPVmsktGHAFIKE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 307 GILKNNASFGGEPSGTWLHPDFCMCPDGLLSGLRLADIVSHKG-PLSKLL-DQMPDYPNIREKVTCSKEDKVKImenmdE 384
Cdd:PRK15414 317 RMRKEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELVCLKGkTLGELVrDRMAAFPASGEINSKLAQPVEAI-----N 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2630008627 385 ELENAF-DDIKEINTIDGVRISLNDGSWVLvRPSGTENYIRITLEAK-----TEEKANEIKNI 441
Cdd:PRK15414 392 RVEQHFsREALAVDRTDGISMTFADWRFNL-RSSNTEPVVRLNVESRgdvplMEARTRTLLTL 453
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
9-443 |
1.48e-31 |
|
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: 125.78 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 9 FGTSGIRGEIgSEVTGELALNVGKSLSYYLGNE---GTVVLGYDTRTTSKMLNQAITAGLVESGVNVIKVGMVPTPLVGY 85
Cdd:cd03088 2 FGTSGLRGLV-TDLTDEVCYAYTRAFLQHLESKfpgDTVAVGRDLRPSSPRIAAACAAALRDAGFRVVDCGAVPTPALAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 86 ATDRLGAdAGIMITASHNPSKYNGIKIwdkngmaYTP------EQESEIEDIYLNKKYVNVGwDKIGSITENNEIKKVYM 159
Cdd:cd03088 81 YAMKRGA-PAIMVTGSHIPADRNGLKF-------YRPdgeitkADEAAILAALVELPEALFD-PAGALLPPDTDAADAYI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 160 DDLLSMVNIEP--GFKVVIDCASGAGSEISPIVFRRAGCEVITLnsqvdgffpGRNPE----------PNDANLgsLKKV 227
Cdd:cd03088 152 ARYTDFFGAGAlkGLRIGVYQHSSVGRDLLVRILEALGAEVVPL---------GRSDTfipvdteavrPEDRAL--AAAW 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 228 VKATGADLGIAHDGDADRMMAVDETGKVVNFDKLLALVASEFG-GTVVTTV-------DAGFIMdeelekvcgNVLRTPV 299
Cdd:cd03088 221 AAEHGLDAIVSTDGDGDRPLVADETGEWLRGDILGLLTARFLGaDTVVTPVssnsaieLSGFFK---------RVVRTRI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 300 GD----VAVADGILKN-NASFGGEPSGTWLHPDFCMCPDGLLSGL--R---------LADIVSHKGPLSKLLDQMPdypn 363
Cdd:cd03088 292 GSpyviAAMAEAAAAGaGRVVGYEANGGFLLGSDIERNGRTLKALptRdavlpilavLAAAKEAGIPLSELVASLP---- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 364 irEKVTCSkeDKVK------------IMENMDEELENAFDD----IKEINTIDGVRISLNDGSWVLVRPSGTENYIRITL 427
Cdd:cd03088 368 --ARFTAS--DRLQnfpteksqaliaRLSADPEARAAFFFAlggeVASIDTTDGLRMTFANGDIVHLRPSGNAPELRCYV 443
|
490
....*....|....*.
gi 2630008627 428 EAKTEEKANEIKNICL 443
Cdd:cd03088 444 EADSEERARELLARGL 459
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
158-253 |
2.12e-30 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 113.15 E-value: 2.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 158 YMDDLLSMVNIEP----GFKVVIDCASGAGSEISPIVFRRAGCEVITLNSQVDGFFPGRNPEP-NDANLGSLKKVVKATG 232
Cdd:pfam02879 2 YIDHLLELVDSEAlkkrGLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDPDFPTRAPNPeEPEALALLIELVKSVG 81
|
90 100
....*....|....*....|.
gi 2630008627 233 ADLGIAHDGDADRMMAVDETG 253
Cdd:pfam02879 82 ADLGIATDGDADRLGVVDERG 102
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
43-275 |
1.14e-28 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 118.62 E-value: 1.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 43 TVVLGYDTRTTSKMLNQAITAGLVESGVNVIKVGMVPTPLVGYAT--DRLGADAGIMITASHNPSKYNGIKIWDKNGMAY 120
Cdd:PLN02371 117 RVSVGRDPRISGPRLADAVFAGLASAGLDVVDMGLATTPAMFMSTltEREDYDAPIMITASHLPYNRNGLKFFTKDGGLG 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 121 TPEqeseIEDIYLN--KKYVNVGWDKI--GSITENNEIKKV-----YMDDLLSMV--------NIE-P--GFKVVIDCAS 180
Cdd:PLN02371 197 KPD----IKDILERaaRIYKEWSDEGLlkSSSGASSVVCRVdfmstYAKHLRDAIkegvghptNYEtPleGFKIVVDAGN 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 181 GAGSEISPIVFRRAGceVITLNSQV---DGFFPGRNPEPND-ANLGSLKKVVKATGADLGIAHDGDADRMMAVDETGKVV 256
Cdd:PLN02371 273 GAGGFFAEKVLEPLG--ADTSGSLFlepDGMFPNHIPNPEDkAAMSATTQAVLANKADLGIIFDTDVDRSAVVDSSGREI 350
|
250 260
....*....|....*....|....
gi 2630008627 257 NFDKLLALVASEF-----GGTVVT 275
Cdd:PLN02371 351 NRNRLIALMSAIVleehpGTTIVT 374
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
259-360 |
2.06e-21 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 89.05 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 259 DKLLALVASEF--------GGTVVTTVDAGFIMDEELEKVCGNVLRTPVGDVAVADGILKNNASFGGEPSGTWLHPDFCM 330
Cdd:pfam02880 3 DQILALLAKYLleqgklppGAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLDHAT 82
|
90 100 110
....*....|....*....|....*....|.
gi 2630008627 331 CPDGLLSGLRLADIVSHKG-PLSKLLDQMPD 360
Cdd:pfam02880 83 TKDGILAALLVLEILARTGkSLSELLEELPE 113
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
9-266 |
7.57e-21 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 95.14 E-value: 7.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 9 FGTSGIRGEIGSevtGELALNV------GKSLSYYLGN-------EGTVVLGYDTRTTSKMLNQaITAGLVES-GVNVIK 74
Cdd:PTZ00150 47 FGTAGLRGKMGA---GFNCMNDltvqqtAQGLCAYVIEtfgqalkSRGVVIGYDGRYHSRRFAE-ITASVFLSkGFKVYL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 75 VG-MVPTPLVGYATDRLGADAGIMITASHNPSKYNGIKIWDKNGMAYTPEQESEIED-IYLNKKYVNVGWDkigSITEN- 151
Cdd:PTZ00150 123 FGqTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVYWSNGAQIIPPHDKNISAkILSNLEPWSSSWE---YLTETl 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 152 -----NEIKKVYMDDLLSMVNI----EPGFKVVIDCASGAGSEISPIVFRRAGC-EVITLNSQV--DGFFPG---RNPEP 216
Cdd:PTZ00150 200 vedplAEVSDAYFATLKSEYNPaccdRSKVKIVYTAMHGVGTRFVQKALHTVGLpNLLSVAQQAepDPEFPTvtfPNPEE 279
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2630008627 217 NDANLGSLKKVVKATGADLGIAHDGDADRmMAVDE----TGKVVNFDKLLALVA 266
Cdd:PTZ00150 280 GKGALKLSMETAEAHGSTVVLANDPDADR-LAVAEklnnGWKIFTGNELGALLA 332
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
9-438 |
9.54e-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: 79.21 E-value: 9.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 9 FGTSGIRGEIGSEVTGEL-ALNVGKSLSYY---LGNEGTVVLGYDTRTTSK-MLNQAITAgLVESGVNVI---KVGMVPT 80
Cdd:cd05801 23 FGTSGHRGSSLKGSFNEAhILAISQAICDYrksQGITGPLFLGKDTHALSEpAFISALEV-LAANGVEVIiqqNDGYTPT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 81 PLVGYAT-----DRLGADA-GIMITASHNPSKYNGIKIWDKNGMAYTPEQESEIEDI---YLNKKYVNV-------GWDK 144
Cdd:cd05801 102 PVISHAIltynrGRTEGLAdGIVITPSHNPPEDGGFKYNPPHGGPADTDITRWIEKRanaLLANGLKGVkripleaALAS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 145 iGSITENNEIKKvYMDDLLSMVNIE----PGFKVVIDCASGAGSEISPIVFRRAGCEVITLNSQVD---GFFP----GR- 212
Cdd:cd05801 182 -GYTHRHDFVTP-YVADLGNVIDMDairkSGLRLGVDPLGGASVPYWQPIAEKYGLNLTVVNPKVDptfRFMTldhdGKi 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 213 ----NPEPNDANLGSLKKvvkatGADLGIAHDGDADRMMAVDETGKVVNFDKLLAlVASEF--------------GGTVV 274
Cdd:cd05801 260 rmdcSSPYAMAGLLKLKD-----KFDLAFANDPDADRHGIVTPSAGLMNPNHYLS-VAIDYlfthrplwnksagvGKTLV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 275 TTVdagfIMDEELEKVCGNVLRTPVGDVAVADGILKNNASFGGEPSG--TWLHPD---FCMCPDGLLSGLRLADI--VSH 347
Cdd:cd05801 334 SSS----MIDRVAAALGRKLYEVPVGFKWFVDGLLDGSLGFGGEESAgaSFLRRDgtvWTTDKDGIIMCLLAAEIlaVTG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 348 KGPlSKLLDQM------PDYPniREKVTCSKEDKVKIMENMDEEL---ENAFDDIKEINT--------IDGVRISLNDGs 410
Cdd:cd05801 410 KDP-GQLYQELterfgePYYA--RIDAPATPEQKARLKKLSPEQVtatELAGDPILAKLTrapgngasIGGLKVTTANG- 485
|
490 500 510
....*....|....*....|....*....|....*.
gi 2630008627 411 WVLVRPSGTENYIRITLE--------AKTEEKANEI 438
Cdd:cd05801 486 WFAARPSGTEDVYKIYAEsflseehlKKIQKEAQEI 521
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
9-428 |
1.30e-14 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 75.94 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 9 FGTSGIRGeigsevtgelalnvgKSLSY-YL------------------GNEGTVVLGYDTRTTSKMLNQAITAGLVESG 69
Cdd:PRK07564 40 FGTSGHRG---------------SSLQPsFNenhilaifqaiceyrgkqGITGPLFVGGDTHALSEPAIQSALEVLAANG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 70 VNVIKV---GMVPTPLV-----GYATDRLGADAGIMITASHNPSKYNGIKiwdkngmaYTP--------EQESEIEDI-- 131
Cdd:PRK07564 105 VGVVIVgrgGYTPTPAVshailKYNGRGGGLADGIVITPSHNPPEDGGIK--------YNPpnggpadtDVTDAIEARan 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 132 -YLNKKYVNV---GWDKIGSITENNEIKKV--YMDDLLSMVNIE----PGFKVVIDCASGAGSEISPIVFRRAGCEVITL 201
Cdd:PRK07564 177 eLLAYGLKGVkriPLDRALASMTVEVIDPVadYVEDLENVFDFDairkAGLRLGVDPLGGATGPYWKAIAERYGLDLTVV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 202 NSQVD---GFFP-----GRNPEPNDANlgSLKKVVKATGA-DLGIAHDGDADRMMAVDETGkVVNFDKLLAlVASEF--- 269
Cdd:PRK07564 257 NAPVDptfNFMPldddgKIRMDCSSPY--AMAGLLALKDAfDLAFANDPDGDRHGIVTPGG-LMNPNHYLA-VAIAYlfh 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 270 -----------GGTVVTT--VDagfimdeeleKVCG----NVLRTPVGDVAVADGILKNNASFGGEPS-GT-WLHPD--- 327
Cdd:PRK07564 333 hrpgwragagvGKTLVSSamID----------RVAAklgrKLYEVPVGFKWFVNGLDDGSLGFGGEESaGAsFLRRDgsv 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 328 FCMCPDGLLSGLRLADIVSHKG-PLSKLLDQM------P-----DYPNIRekvtcskEDKVKImENMDEEL----ENAFD 391
Cdd:PRK07564 403 WTTDKDGLIAVLLAAEILAVTGkSPSEIYRELwarfgrPyysrhDAPATP-------EQKAAL-RKLSPELvgatELAGD 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2630008627 392 DIKEINT--------IDGVRISLNDGsWVLVRPSGTENYIRITLE 428
Cdd:PRK07564 475 PIDASLTeapgngaaIGGLKVVTENG-WFAARPSGTETTYKIYAE 518
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
40-446 |
4.41e-11 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 64.67 E-value: 4.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 40 NEGTVVLGYDTRTTSKMLNQAITAGLVES-GVNVIKVGMVPTPLVGYatdrlgadagimITASHNpskyNGIKIWDKNgm 118
Cdd:PTZ00302 151 SKAKVHVGRDTRPSSPELVSALLRGLKLLiGSNVRNFGIVTTPQLHF------------LVAFAN----GLGVDVVES-- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 119 aytpEQESEIEDI--YLNKKYVNVGWDKIGSITENNEIKkvymddllsmvniepgfkVVIDCASGAGSE-ISPI--VFRR 193
Cdd:PTZ00302 213 ----SDELYYAYLlaAFKELYRTLQEGGPVDLTQNNSKI------------------LVVDCANGVGGYkIKRFfeALKQ 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 194 AGCEVITLNSQVDgffpgrnpEPNDANLG-------SLKKVVKATGADLGIAH------DGDADRMMA--VDETG--KVV 256
Cdd:PTZ00302 271 LGIEIIPININCD--------EEELLNDKcgadyvqKTRKPPRAMKEWPGDEEtrvasfDGDADRLVYffPDKDGddKWV 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 257 --NFDKLLALVASEFG--------------GTVVTT-VDAGFI--MDEELEKVcgNVLRTPVG-----------DVAV-- 304
Cdd:PTZ00302 343 llDGDRIAILYAMLIKkllgkiqlkkkldiGVVQTAyANGASTnyLNELLGRL--RVYCAPTGvknlhpkahkyDIGIyf 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 305 -ADG----ILKNNASFGGEPSGTWLHPDFCMCPdgLLSGLRL----------ADIVSHKGPLSKL-------LDQMPDYP 362
Cdd:PTZ00302 421 eANGhgtvLFNEKALAEWAKFLAKQNALNSACR--QLEKFLRlfnqtigdaiSDLLAVELALAFLglsfqdwLNLYTDLP 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 363 NIREKVTCSKEDKVKIMENMDEELENAfdDIKEinTIDGVRISLNDGSWVLVRPSGTENYIRITLEAKTEEKANEIKNIC 442
Cdd:PTZ00302 499 SRQDKVTVKDRTLITNTEDETRLLEPK--GLQD--KIDAIVSKYDNAARAFIRPSGTEPVVRVYAEAPTLEQADELANEV 574
|
....
gi 2630008627 443 LDII 446
Cdd:PTZ00302 575 KGLV 578
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
41-247 |
8.80e-10 |
|
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: 60.70 E-value: 8.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 41 EGTVVLGYDTRTTSKMLNQAITAGLVESGVNVIKVG---MVPTPLVGYATDRLGADAGIMITASHNPSKYN---GIKIWD 114
Cdd:cd03085 49 GATLVVGGDGRYYNKEAIQIIIKIAAANGVGKVVVGqngLLSTPAVSAVIRKRKATGGIILTASHNPGGPEgdfGIKYNT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 115 KNGmayTPEQESEIEDIYLNKK---------YVNVGWDKIGSITENN-----EI-----------KKVYMDDLL-SMVNi 168
Cdd:cd03085 129 SNG---GPAPESVTDKIYEITKkiteykiadDPDVDLSKIGVTKFGGkpftvEVidsvedyvelmKEIFDFDAIkKLLS- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 169 EPGFKVVIDCASG-AGSEISPIVFRRAGC-EVITLNSQVDGFFPGRNPEPNDANLGSLKKVVKATGADLGIAHDGDADRM 246
Cdd:cd03085 205 RKGFKVRFDAMHGvTGPYAKKIFVEELGApESSVVNCTPLPDFGGGHPDPNLTYAKDLVELMKSGEPDFGAASDGDGDRN 284
|
.
gi 2630008627 247 M 247
Cdd:cd03085 285 M 285
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
375-439 |
1.12e-09 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 54.58 E-value: 1.12e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2630008627 375 KVKIMENMDEElenAFDDIKEiNTIDGVRISLNDGSWVLVRPSGTENYIRITLEAKTEEKANEIK 439
Cdd:pfam00408 3 NVRVAEKKKLA---ALAAILK-VFADAEKILGEDGRRLDVRPSGTEPVLRVMVEGDSDEELARLA 63
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
19-438 |
2.38e-08 |
|
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: 56.06 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 19 GSEVTGELALNVGKSLSYYLGNEGTVVLGYDTRTTSKMLNQAITAGLVESGVNVIKVGMVPTPLVGYatdrlgadagimI 98
Cdd:cd03086 80 DELLVLVLMLISVKELNIDLSVPANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHY------------L 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 99 TASHNPSKYNGikiwdkngmaytpeqESEIEDIYlnKKYVNvGWDKIGSITENNEIKKvymddllsmvniepgFKVVIDC 178
Cdd:cd03086 148 VRAANTEGAYG---------------EPTEEGYY--EKLSK-AFNELYNLLQDGGDEP---------------EKLVVDC 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 179 ASGAGS-------EISP----IVFRRAGCEVIT-LNSQVDGFF------PGRNPEPNDANlgslKKVVkatgadlgiAHD 240
Cdd:cd03086 195 ANGVGAlklkellKRLKkglsVKIINDGEEGPElLNDGCGADYvktkqkPPRGFELKPPG----VRCC---------SFD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 241 GDADRMMA--VDETGKVVNFD--KLLALVA-------------SEFGGTVVTTVDAG-----FImdEELEKVcgNVLRTP 298
Cdd:cd03086 262 GDADRLVYfyPDSSNKFHLLDgdKIATLFAkfikellkkageeLKLTIGVVQTAYANgastkYL--EDVLKV--PVVCTP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 299 VG-----------DVAV---ADG---ILKNNASFGGEPSGTWLHPDFCMCPDGLLSGLRL---------AD------IVS 346
Cdd:cd03086 338 TGvkhlhhaaeefDIGVyfeANGhgtVLFSESALAKIEENSSLSDEQEKAAKTLLAFSRLinqtvgdaiSDmlavelILA 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 347 HKG-PLSKLLDQMPDYPNIREKVTCSKEDKVKImenMDEE--------LENAFDDIkeintidgvrISLNDGSWVLVRPS 417
Cdd:cd03086 418 ALGwSPQDWDNLYTDLPNRQLKVKVPDRSVIKT---TDAErrlvepkgLQDKIDAI----------VAKYNNGRAFVRPS 484
|
490 500
....*....|....*....|.
gi 2630008627 418 GTENYIRITLEAKTEEKANEI 438
Cdd:cd03086 485 GTEDVVRVYAEAATQEEADEL 505
|
|
| PLN02307 |
PLN02307 |
phosphoglucomutase |
10-247 |
1.33e-07 |
|
phosphoglucomutase
Pssm-ID: 177942 [Multi-domain] Cd Length: 579 Bit Score: 53.89 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 10 GTSGIRGEIgSEVTGELAL-NVGKSLSYYLGNE----GTVVLGYDTRTTSKMLNQAITAGLVESGVNVIKVG---MVPTP 81
Cdd:PLN02307 26 GTSGLRKKV-KVFMQENYLaNFVQALFNALPAEkvkgATLVLGGDGRYFNKEAIQIIIKIAAANGVRRVWVGqngLLSTP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 82 LVGYAT---DRLGADAGIMITASHNPSKYN---GIKIWDKNGmayTPEQESEIEDIYLNKKYVN---------------V 140
Cdd:PLN02307 105 AVSAVIrerDGSKANGGFILTASHNPGGPEedfGIKYNYESG---QPAPESITDKIYGNTLTIKeykmaedipdvdlsaV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2630008627 141 GWDKIGSITENN-EIKKVYMDDLLSMVNI-----------EPGFKVVIDCASG-AGSEISPIVFRRAGC-EVITLNSQVD 206
Cdd:PLN02307 182 GVTKFGGPEDFDvEVIDPVEDYVKLMKSIfdfelikkllsRPDFTFCFDAMHGvTGAYAKRIFVEELGApESSLLNCVPK 261
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2630008627 207 GFFPGRNPEPN-------DANLGSLKKVVKATGADLGIAHDGDADRMM 247
Cdd:PLN02307 262 EDFGGGHPDPNltyakelVKRMGLGKTSYGDEPPEFGAASDGDGDRNM 309
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
95-117 |
1.38e-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: 50.67 E-value: 1.38e-06
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
90-117 |
5.28e-06 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 48.87 E-value: 5.28e-06
10 20
....*....|....*....|....*...
gi 2630008627 90 LGADAGIMITASHNPSKYNGIKIWDKNG 117
Cdd:PLN02895 56 TGAATGLMITASHNPVSDNGVKIVDPSG 83
|
|
| |
