|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15414 |
PRK15414 |
phosphomannomutase; |
1-456 |
0e+00 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 1006.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 1 MEKLTCFKAYDIRGKLGEELNEDIAWRIGRAYGEYLKPQTIVLGGDVRLTSVSLKLALAKGLQDAGVDVLDIGLSGTEEI 80
Cdd:PRK15414 1 MKKLTCFKAYDIRGKLGEELNEDIAWRIGRAYGEFLKPKTIVLGGDVRLTSETLKLALAKGLQDAGVDVLDIGMSGTEEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 81 YFATFHLGVDGGIEVTASHNPMDYNGMKLVRKGARPISGDTGLRDVQRLAEANDFPPVNEAKRGSYKKINLQKEYIDHLL 160
Cdd:PRK15414 81 YFATFHLGVDGGIEVTASHNPMDYNGMKLVREGARPISGDTGLRDVQRLAEANDFPPVDETKRGRYQQINLRDAYVDHLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 161 GYINVANLKPLKLVINSGNGAAGPVVDALEARFKALNVPVTFVKVHNTPDGNFPNGIPNPLLPECRDDTRNAVIEHGADM 240
Cdd:PRK15414 161 GYINVKNLTPLKLVINSGNGAAGPVVDAIEARFKALGAPVELIKVHNTPDGNFPNGIPNPLLPECRDDTRNAVIKHGADM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 241 GIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPGAKIIHDPRLSWNTVDVVSAAGGTPVMSKTGHAFIKERMRE 320
Cdd:PRK15414 241 GIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPGAKIIHDPRLSWNTVDVVTAAGGTPVMSKTGHAFIKERMRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 321 EDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVTELLCLKGQTLGELVRDRMAAFPASGEINSKLAQPAEAIARVEQHFAIH 400
Cdd:PRK15414 321 EDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELVCLKGKTLGELVRDRMAAFPASGEINSKLAQPVEAINRVEQHFSRE 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2181739291 401 ALEIDRTDGISMAFPQWRFNLRSSNTEPVVRLNVESRADTALMEARTKDILALLNQ 456
Cdd:PRK15414 401 ALAVDRTDGISMTFADWRFNLRSSNTEPVVRLNVESRGDVPLMEARTRTLLTLLNE 456
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
6-454 |
0e+00 |
|
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: 584.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 6 CFKAYDIRGKLGEELNEDIAWRIGRAYGEYLK---PQTIVLGGDVRLTSVSLKLALAKGLQDAGVDVLDIGLSGTEEIYF 82
Cdd:cd03089 1 IFRAYDIRGIAGEELTEEIAYAIGRAFGSWLLekgAKKVVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPVLYF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 83 ATFHLGVDGGIEVTASHNPMDYNGMKLVRkGARPISGDtGLRDVQRLAEANDFPPVNeaKRGSYKKINLQKEYIDHLLGY 162
Cdd:cd03089 81 ATFHLDADGGVMITASHNPPEYNGFKIVI-GGGPLSGE-DIQALRERAEKGDFAAAT--GRGSVEKVDILPDYIDRLLSD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 163 INVANlKPLKLVINSGNGAAGPVVDALEARFKAlnvpvTFVKVHNTPDGNFPNGIPNPLLPECRDDTRNAVIEHGADMGI 242
Cdd:cd03089 157 IKLGK-RPLKVVVDAGNGAAGPIAPQLLEALGC-----EVIPLFCEPDGTFPNHHPDPTDPENLEDLIAAVKENGADLGI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 243 AFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPGAKIIHDPRLSWNTVDVVSAAGGTPVMSKTGHAFIKERMREED 322
Cdd:cd03089 231 AFDGDGDRLGVVDEKGEIIWGDRLLALFARDILKRNPGATIVYDVKCSRNLYDFIEEAGGKPIMWKTGHSFIKAKMKETG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 323 AIYGGEMSAHHYFRD-FAYCDSGMIPWLLVTELLCLKGQTLGELVRDRMaAFPASGEINSKLAQ--PAEAIARVEQHFAI 399
Cdd:cd03089 311 ALLAGEMSGHIFFKDrWYGFDDGIYAALRLLELLSKSGKTLSELLADLP-KYFSTPEIRIPVTEedKFAVIERLKEHFEF 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2181739291 400 HALEIDRTDGISMAFPQWRFNLRSSNTEPVVRLNVESRADtALMEARTKDILALL 454
Cdd:cd03089 390 PGAEIIDIDGVRVDFEDGWGLVRASNTEPVLVLRFEADTE-EGLEEIKAELRKLL 443
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
1-456 |
7.20e-168 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 480.08 E-value: 7.20e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 1 MEKLTCFKAYDIRGKLGEELNEDIAWRIGRAYGEYLKPQ---TIVLGGDVRLTSVSLKLALAKGLQDAGVDVLDIGLSGT 77
Cdd:COG1109 1 MTYKKLFGTDGIRGIVGEELTPEFVLKLGRAFGTYLKEKggpKVVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 78 EEIYFATFHLGVDGGIEVTASHNPMDYNGMKLVRKGARPISGDTgLRDVQRLAEANDFPPVNEAKRGSYKKI-NLQKEYI 156
Cdd:COG1109 81 PALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEE-EKEIEALIEKEDFRRAEAEEIGKVTRIeDVLEAYI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 157 DHLLGYINVA-NLKPLKLVINSGNGAAGPVVDALearFKALNVPVtfVKVHNTPDGNFPNGIPNPLlPECRDDTRNAVIE 235
Cdd:COG1109 160 EALKSLVDEAlRLRGLKVVVDCGNGAAGGVAPRL---LRELGAEV--IVLNAEPDGNFPNHNPNPE-PENLEDLIEAVKE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 236 HGADMGIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPGAKIIHDPRLSWNTVDVVSAAGGTPVMSKTGHAFIK 315
Cdd:COG1109 234 TGADLGIAFDGDADRLGVVDEKGRFLDGDQLLALLARYLLEKGPGGTVVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 316 ERMREEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVTELLCLKGQTLGELVRDrMAAFPaSGEINSKLA---QPAEAIAR 392
Cdd:COG1109 314 EKMRETGAVLGGEESGGIIFPDFVPTDDGILAALLLLELLAKQGKSLSELLAE-LPRYP-QPEINVRVPdeeKIGAVMEK 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181739291 393 VEQHFAiHALEIDRTDGISMAFPQW-RFNLRSSNTEPVVRLNVESRaDTALMEARTKDILALLNQ 456
Cdd:COG1109 392 LREAVE-DKEELDTIDGVKVDLEDGgWVLVRPSGTEPLLRVYAEAK-DEEEAEELLAELAELVEE 454
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
7-437 |
3.06e-105 |
|
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: 319.84 E-value: 3.06e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 7 FKAYDIRGKLGEELNEDIAWRIGRAYGEYLKPQTIVLGGDVRLTSVSLKLALAKGLQDAGVDVLDIGLSGTEEIYFATFH 86
Cdd:TIGR03990 4 FGTSGIRGIVGEELTPELALKVGKAFGTYLRGGKVVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLGIAPTPTLQYAVRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 87 LGVDGGIEVTASHNPMDYNGMKLVRKGARPISGDTGlRDVQRLAEANDFPPVNEAKRGSYKKI-NLQKEYIDHLLGYINV 165
Cdd:TIGR03990 84 LGADGGIMITASHNPPEYNGIKLLNSDGTELSREQE-EEIEEIAESGDFERADWDEIGTVTSDeDAIDDYIEAILDKVDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 166 ANL--KPLKLVINSGNGAAGPVVDALearFKALNVPVtfVKVHNTPDGNFPNGIPNPlLPECRDDTRNAVIEHGADMGIA 243
Cdd:TIGR03990 163 EAIrkKGFKVVVDCGNGAGSLTTPYL---LRELGCKV--ITLNCQPDGTFPGRNPEP-TPENLKDLSALVKATGADLGIA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 244 FDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKnPGAKIIhdprlswNTV-------DVVSAAGGTPVMSKTGHAFIKE 316
Cdd:TIGR03990 237 HDGDADRLVFIDEKGRFIGGDYTLALFAKYLLEH-GGGKVV-------TNVsssraveDVAERHGGEVIRTKVGEVNVAE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 317 RMREEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVTELLCLKGQTLGELVrDRMAAFPAS-GEINSKLAQPAEAIARVEQ 395
Cdd:TIGR03990 309 KMKEEGAVFGGEGNGGWIFPDHHYCRDGLMAAALFLELLAEEGKPLSELL-AELPKYPMSkEKVELPDEDKEEVMEAVEE 387
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2181739291 396 HFAihALEIDRTDGISMAFPQWRFNLRSSNTEPVVRLNVESR 437
Cdd:TIGR03990 388 EFA--DAEIDTIDGVRIDFEDGWVLVRPSGTEPIVRIYAEAK 427
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
7-136 |
1.50e-38 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 136.20 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 7 FKAYDIRGKLG-EELNEDIAWRIGRAYGEYLKPQ----TIVLGGDVRLTSVSLKLALAKGLQDAGVDVLDIGLSGTEEIY 81
Cdd:pfam02878 4 FGTSGIRGKVGvGELTPEFALKLGQAIASYLRAQggggKVVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTPAVS 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2181739291 82 FATFHLGVDGGIEVTASHNPMDYNGMKLVRKGARPISGDTgLRDVQRLAEANDFP 136
Cdd:pfam02878 84 FATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEV-EKKIEAIIEKEDFY 137
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15414 |
PRK15414 |
phosphomannomutase; |
1-456 |
0e+00 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 1006.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 1 MEKLTCFKAYDIRGKLGEELNEDIAWRIGRAYGEYLKPQTIVLGGDVRLTSVSLKLALAKGLQDAGVDVLDIGLSGTEEI 80
Cdd:PRK15414 1 MKKLTCFKAYDIRGKLGEELNEDIAWRIGRAYGEFLKPKTIVLGGDVRLTSETLKLALAKGLQDAGVDVLDIGMSGTEEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 81 YFATFHLGVDGGIEVTASHNPMDYNGMKLVRKGARPISGDTGLRDVQRLAEANDFPPVNEAKRGSYKKINLQKEYIDHLL 160
Cdd:PRK15414 81 YFATFHLGVDGGIEVTASHNPMDYNGMKLVREGARPISGDTGLRDVQRLAEANDFPPVDETKRGRYQQINLRDAYVDHLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 161 GYINVANLKPLKLVINSGNGAAGPVVDALEARFKALNVPVTFVKVHNTPDGNFPNGIPNPLLPECRDDTRNAVIEHGADM 240
Cdd:PRK15414 161 GYINVKNLTPLKLVINSGNGAAGPVVDAIEARFKALGAPVELIKVHNTPDGNFPNGIPNPLLPECRDDTRNAVIKHGADM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 241 GIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPGAKIIHDPRLSWNTVDVVSAAGGTPVMSKTGHAFIKERMRE 320
Cdd:PRK15414 241 GIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPGAKIIHDPRLSWNTVDVVTAAGGTPVMSKTGHAFIKERMRK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 321 EDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVTELLCLKGQTLGELVRDRMAAFPASGEINSKLAQPAEAIARVEQHFAIH 400
Cdd:PRK15414 321 EDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELVCLKGKTLGELVRDRMAAFPASGEINSKLAQPVEAINRVEQHFSRE 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2181739291 401 ALEIDRTDGISMAFPQWRFNLRSSNTEPVVRLNVESRADTALMEARTKDILALLNQ 456
Cdd:PRK15414 401 ALAVDRTDGISMTFADWRFNLRSSNTEPVVRLNVESRGDVPLMEARTRTLLTLLNE 456
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
6-454 |
0e+00 |
|
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: 584.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 6 CFKAYDIRGKLGEELNEDIAWRIGRAYGEYLK---PQTIVLGGDVRLTSVSLKLALAKGLQDAGVDVLDIGLSGTEEIYF 82
Cdd:cd03089 1 IFRAYDIRGIAGEELTEEIAYAIGRAFGSWLLekgAKKVVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPVLYF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 83 ATFHLGVDGGIEVTASHNPMDYNGMKLVRkGARPISGDtGLRDVQRLAEANDFPPVNeaKRGSYKKINLQKEYIDHLLGY 162
Cdd:cd03089 81 ATFHLDADGGVMITASHNPPEYNGFKIVI-GGGPLSGE-DIQALRERAEKGDFAAAT--GRGSVEKVDILPDYIDRLLSD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 163 INVANlKPLKLVINSGNGAAGPVVDALEARFKAlnvpvTFVKVHNTPDGNFPNGIPNPLLPECRDDTRNAVIEHGADMGI 242
Cdd:cd03089 157 IKLGK-RPLKVVVDAGNGAAGPIAPQLLEALGC-----EVIPLFCEPDGTFPNHHPDPTDPENLEDLIAAVKENGADLGI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 243 AFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPGAKIIHDPRLSWNTVDVVSAAGGTPVMSKTGHAFIKERMREED 322
Cdd:cd03089 231 AFDGDGDRLGVVDEKGEIIWGDRLLALFARDILKRNPGATIVYDVKCSRNLYDFIEEAGGKPIMWKTGHSFIKAKMKETG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 323 AIYGGEMSAHHYFRD-FAYCDSGMIPWLLVTELLCLKGQTLGELVRDRMaAFPASGEINSKLAQ--PAEAIARVEQHFAI 399
Cdd:cd03089 311 ALLAGEMSGHIFFKDrWYGFDDGIYAALRLLELLSKSGKTLSELLADLP-KYFSTPEIRIPVTEedKFAVIERLKEHFEF 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2181739291 400 HALEIDRTDGISMAFPQWRFNLRSSNTEPVVRLNVESRADtALMEARTKDILALL 454
Cdd:cd03089 390 PGAEIIDIDGVRVDFEDGWGLVRASNTEPVLVLRFEADTE-EGLEEIKAELRKLL 443
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
1-456 |
7.20e-168 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 480.08 E-value: 7.20e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 1 MEKLTCFKAYDIRGKLGEELNEDIAWRIGRAYGEYLKPQ---TIVLGGDVRLTSVSLKLALAKGLQDAGVDVLDIGLSGT 77
Cdd:COG1109 1 MTYKKLFGTDGIRGIVGEELTPEFVLKLGRAFGTYLKEKggpKVVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 78 EEIYFATFHLGVDGGIEVTASHNPMDYNGMKLVRKGARPISGDTgLRDVQRLAEANDFPPVNEAKRGSYKKI-NLQKEYI 156
Cdd:COG1109 81 PALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEE-EKEIEALIEKEDFRRAEAEEIGKVTRIeDVLEAYI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 157 DHLLGYINVA-NLKPLKLVINSGNGAAGPVVDALearFKALNVPVtfVKVHNTPDGNFPNGIPNPLlPECRDDTRNAVIE 235
Cdd:COG1109 160 EALKSLVDEAlRLRGLKVVVDCGNGAAGGVAPRL---LRELGAEV--IVLNAEPDGNFPNHNPNPE-PENLEDLIEAVKE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 236 HGADMGIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPGAKIIHDPRLSWNTVDVVSAAGGTPVMSKTGHAFIK 315
Cdd:COG1109 234 TGADLGIAFDGDADRLGVVDEKGRFLDGDQLLALLARYLLEKGPGGTVVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 316 ERMREEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVTELLCLKGQTLGELVRDrMAAFPaSGEINSKLA---QPAEAIAR 392
Cdd:COG1109 314 EKMRETGAVLGGEESGGIIFPDFVPTDDGILAALLLLELLAKQGKSLSELLAE-LPRYP-QPEINVRVPdeeKIGAVMEK 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2181739291 393 VEQHFAiHALEIDRTDGISMAFPQW-RFNLRSSNTEPVVRLNVESRaDTALMEARTKDILALLNQ 456
Cdd:COG1109 392 LREAVE-DKEELDTIDGVKVDLEDGgWVLVRPSGTEPLLRVYAEAK-DEEEAEELLAELAELVEE 454
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
7-453 |
7.39e-135 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 395.50 E-value: 7.39e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 7 FKAYDIRGKLGEELNEDIAWRIGRAYGEYLKPQ---TIVLGGDVRLTSVSLKLALAKGLQDAGVDVLDIGLSGTEEIYFA 83
Cdd:PRK09542 1 IKAYDVRGVVGEQIDEDLVRDVGAAFARLMRAEgatTVVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIGLASTDQLYFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 84 TFHLGVDGGIeVTASHNPMDYNGMKLVRKGARPISGDTGLRDVQRLAEANdFPPVnEAKRGSYKKINLQKEYIDHLLGYI 163
Cdd:PRK09542 81 SGLLDCPGAM-FTASHNPAAYNGIKLCRAGAKPVGQDTGLAAIRDDLIAG-VPAY-DGPPGTVTERDVLADYAAFLRSLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 164 NVANLKPLKLVINSGNGAAGPVVDALearFKALnvPVTFVKVHNTPDGNFPNGIPNPLLPECRDDTRNAVIEHGADMGIA 243
Cdd:PRK09542 158 DLSGIRPLKVAVDAGNGMGGHTVPAV---LGGL--PITLLPLYFELDGTFPNHEANPLDPANLVDLQAFVRETGADIGLA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 244 FDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPGAKIIHDPRLSWNTVDVVSAAGGTPVMSKTGHAFIKERMREEDA 323
Cdd:PRK09542 233 FDGDADRCFVVDERGQPVSPSAVTALVAARELAREPGATIIHNLITSRAVPELVAERGGTPVRTRVGHSFIKALMAETGA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 324 IYGGEMSAHHYFRDFAYCDSGMIPWLLVTELLCLKGQTLGELVRDrMAAFPASGEINSKLAQPAEAIARVEQHFAIHALE 403
Cdd:PRK09542 313 IFGGEHSAHYYFRDFWGADSGMLAALHVLAALGEQDRPLSELMAD-YQRYAASGEINSTVADAPARMEAVLKAFADRIVS 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2181739291 404 IDRTDG--ISMAFPQWrFNLRSSNTEPVVRLNVESRaDTALMEARTKDILAL 453
Cdd:PRK09542 392 VDHLDGvtVDLGDGSW-FNLRASNTEPLLRLNVEAR-TEEEVDALVDEVLAI 441
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
7-437 |
3.06e-105 |
|
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: 319.84 E-value: 3.06e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 7 FKAYDIRGKLGEELNEDIAWRIGRAYGEYLKPQTIVLGGDVRLTSVSLKLALAKGLQDAGVDVLDIGLSGTEEIYFATFH 86
Cdd:TIGR03990 4 FGTSGIRGIVGEELTPELALKVGKAFGTYLRGGKVVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLGIAPTPTLQYAVRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 87 LGVDGGIEVTASHNPMDYNGMKLVRKGARPISGDTGlRDVQRLAEANDFPPVNEAKRGSYKKI-NLQKEYIDHLLGYINV 165
Cdd:TIGR03990 84 LGADGGIMITASHNPPEYNGIKLLNSDGTELSREQE-EEIEEIAESGDFERADWDEIGTVTSDeDAIDDYIEAILDKVDV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 166 ANL--KPLKLVINSGNGAAGPVVDALearFKALNVPVtfVKVHNTPDGNFPNGIPNPlLPECRDDTRNAVIEHGADMGIA 243
Cdd:TIGR03990 163 EAIrkKGFKVVVDCGNGAGSLTTPYL---LRELGCKV--ITLNCQPDGTFPGRNPEP-TPENLKDLSALVKATGADLGIA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 244 FDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKnPGAKIIhdprlswNTV-------DVVSAAGGTPVMSKTGHAFIKE 316
Cdd:TIGR03990 237 HDGDADRLVFIDEKGRFIGGDYTLALFAKYLLEH-GGGKVV-------TNVsssraveDVAERHGGEVIRTKVGEVNVAE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 317 RMREEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVTELLCLKGQTLGELVrDRMAAFPAS-GEINSKLAQPAEAIARVEQ 395
Cdd:TIGR03990 309 KMKEEGAVFGGEGNGGWIFPDHHYCRDGLMAAALFLELLAEEGKPLSELL-AELPKYPMSkEKVELPDEDKEEVMEAVEE 387
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2181739291 396 HFAihALEIDRTDGISMAFPQWRFNLRSSNTEPVVRLNVESR 437
Cdd:TIGR03990 388 EFA--DAEIDTIDGVRIDFEDGWVLVRPSGTEPIVRIYAEAK 427
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
12-448 |
1.35e-80 |
|
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: 255.96 E-value: 1.35e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 12 IRGKLGEELNEDIAWRIGRAYGEYLKPQTIVLGGDVRLTSVSLKLALAKGLQDAGVDVLDIGLSGTEEIYFATFHLGvDG 91
Cdd:cd03087 7 IRGVVGEELTPELALKVGKALGTYLGGGTVVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDIGIVPTPALQYAVRKLG-DA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 92 GIEVTASHNPMDYNGMKLVRKGARPISGDTgLRDVQRLAEANDFPPVNEAKRGSYKKIN-LQKEYIDHLLGYINVANLKP 170
Cdd:cd03087 86 GVMITASHNPPEYNGIKLVNPDGTEFSREQ-EEEIEEIIFSERFRRVAWDEVGSVRREDsAIDEYIEAILDKVDIDGGKG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 171 LKLVINSGNGAAG---PVVdalearFKALNVPVTFVKVHntPDGNFPNGIPNPlLPECRDDTRNAVIEHGADMGIAFDGD 247
Cdd:cd03087 165 LKVVVDCGNGAGSlttPYL------LRELGCKVITLNAN--PDGFFPGRPPEP-TPENLSELMELVRATGADLGIAHDGD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 248 FDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPGaKIIHDPRLSWNTVDVVSAAGGTPVMSKTGHAFIKERMREEDAIYGG 327
Cdd:cd03087 236 ADRAVFVDEKGRFIDGDKLLALLAKYLLEEGGG-KVVTPVDASMLVEDVVEEAGGEVIRTPVGDVHVAEEMIENGAVFGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 328 EMSAHHYFRDFAYCDSGMIPWLLVTELLClKGQTLGELVrDRMAAFPASGE-INSKLAQPAEAIARVEQHFAIHALEIDR 406
Cdd:cd03087 315 EPNGGWIFPDHQLCRDGIMTAALLLELLA-EEKPLSELL-DELPKYPLLREkVECPDEKKEEVMEAVEEELSDADEDVDT 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2181739291 407 TDGISMAFPQWRFNLRSSNTEPVVRLNVES----RADTALMEARTK 448
Cdd:cd03087 393 IDGVRIEYEDGWVLIRPSGTEPKIRITAEAkteeRAKELLEEGRSK 438
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
12-450 |
7.36e-67 |
|
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: 220.05 E-value: 7.36e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 12 IRGKLGEELNEDIAWRIGRAYGEYLK----PQTIVLGGDVRLTSVSLKLALAKGLQDAGVDVLDIGLSGTEEIYFATFHL 87
Cdd:cd05802 7 IRGVANEPLTPELALKLGRAAGKVLGkgggRPKVLIGKDTRISGYMLESALAAGLTSAGVDVLLLGVIPTPAVAYLTRKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 88 GVDGGIEVTASHNPMDYNGMKLVRKGARPISGDTGLRdVQRLAEANDFPPVNEAKRGSYKKI-NLQKEYIDHLLGYINVA 166
Cdd:cd05802 87 RADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVEEE-IEALIDKELELPPTGEKIGRVYRIdDARGRYIEFLKSTFPKD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 167 NLKPLKLVINSGNGAA---GPVVdalearFKALNVPVtfVKVHNTPDG-NfpngI--------PNPLlpecrddtRNAVI 234
Cdd:cd05802 166 LLSGLKIVLDCANGAAykvAPEV------FRELGAEV--IVINNAPDGlN----InvncgsthPESL--------QKAVL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 235 EHGADMGIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNpgakiihdpRLSWNTVdVV------------SAAGG 302
Cdd:cd05802 226 ENGADLGIAFDGDADRVIAVDEKGNIVDGDQILAICARDLKERG---------RLKGNTV-VGtvmsnlglekalKELGI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 303 TPVMSKTGHAFIKERMREEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVTELLCLKGQTLGELVRDrMAAFP-------- 374
Cdd:cd05802 296 KLVRTKVGDRYVLEEMLKHGANLGGEQSGHIIFLDHSTTGDGLLTALQLLAIMKRSGKSLSELASD-MKLYPqvlvnvrv 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2181739291 375 ASGEINSKLAQPAEAIARVEQHFAihaleidrTDGismafpqwRFNLRSSNTEPVVRLNVESrADTALMEARTKDI 450
Cdd:cd05802 375 KDKKALLENPRVQAAIAEAEKELG--------GEG--------RVLVRPSGTEPLIRVMVEG-EDEELVEKLAEEL 433
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
12-441 |
2.80e-63 |
|
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: 211.01 E-value: 2.80e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 12 IRGKLGEELNEDIAWRIGRAYGEYL----KPQTIVLGGDVRLTSVSLKLALAKGLQDAGVDVLDIGLSGTEEIYFATFHL 87
Cdd:cd05803 7 IRGIVGEGLTPEVITRYVAAFATWQpertKGGKIVVGRDGRPSGPMLEKIVIGALLACGCDVIDLGIAPTPTVQVLVRQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 88 GVDGGIEVTASHNPMDYNGMKLVRKGARPISGDTGLRdVQRLAEANDFPPVNEAKRGSYKKI-NLQKEYIDHLLGYINVA 166
Cdd:cd05803 87 QASGGIIITASHNPPQWNGLKFIGPDGEFLTPDEGEE-VLSCAEAGSAQKAGYDQLGEVTFSeDAIAEHIDKVLALVDVD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 167 NLKP----LKLVINSGNGAAGPVVDALearFKALNVPVTFvkVHNTPDGNFPNgIPNPlLPECRDDTRNAVIEHGADMGI 242
Cdd:cd05803 166 VIKIrernFKVAVDSVNGAGGLLIPRL---LEKLGCEVIV--LNCEPTGLFPH-TPEP-LPENLTQLCAAVKESGADVGF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 243 AFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPG-AKIIHDPRLSWNTVDVVSAAGGTPVMSKTGHAFIKERMREE 321
Cdd:cd05803 239 AVDPDADRLALVDEDGRPIGEEYTLALAVDYVLKYGGRkGPVVVNLSTSRALEDIARKHGVPVFRSAVGEANVVEKMKEV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 322 DAIYGGE------MSAHHYFRDfAYcdSGMIpwlLVTELLCLKGQTLGELVrdrmAAFPASGEINSKLAQPAEAIARVEQ 395
Cdd:cd05803 319 DAVIGGEgnggviLPDVHYGRD-SL--VGIA---LVLQLLAASGKPLSEIV----DELPQYYISKTKVTIAGEALERLLK 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2181739291 396 HFAIHA--LEIDRTDGISMAFPQWRFNLRSSNTEPVVRLNVESRA-DTA 441
Cdd:cd05803 389 KLEAYFkdAEASTLDGLRLDSEDSWVHVRPSNTEPIVRIIAEAPTqDEA 437
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
13-437 |
7.45e-46 |
|
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: 165.42 E-value: 7.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 13 RGKLGEELNEDIAWRIGRAYGEYLK-----PQTIVLGGDVRLTSVSLKLALAKGLQDAGVDVLdigLSG----TEEIYFA 83
Cdd:cd05800 9 RGIIAEDFTFENVRRVAQAIADYLKeegggGRGVVVGYDTRFLSEEFARAVAEVLAANGIDVY---LSDrpvpTPAVSWA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 84 TFHLGVDGGIEVTASHNPMDYNGMKLVRKGARPISGDTgLRDVQRLAEANDFPPVNEAKRGSYKKINLQKEYIDHLLGYI 163
Cdd:cd05800 86 VKKLGAAGGVMITASHNPPEYNGVKVKPAFGGSALPEI-TAAIEARLASGEPPGLEARAEGLIETIDPKPDYLEALRSLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 164 NVANLKP--LKLVINSGNGAAGPVVDALearFKALNVPVTFVkvHNTPDGNFPNGIPNPLLPECrDDTRNAVIEHGADMG 241
Cdd:cd05800 165 DLEAIREagLKVVVDPMYGAGAGYLEEL---LRGAGVDVEEI--RAERDPLFGGIPPEPIEKNL-GELAEAVKEGGADLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 242 IAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLE----KNPGAKIIHDPRLswntVDVVSAAGG-----TPVmsktGHA 312
Cdd:cd05800 239 LATDGDADRIGAVDEKGNFLDPNQILALLLDYLLEnkglRGPVVKTVSTTHL----IDRIAEKHGlpvyeTPV----GFK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 313 FIKERMREEDAIYGGEMS-----AHHY-FRDfaycdsGMIPWLLVTELLCLKGQTLGELVRDRMAAFPAS--GEINSKL- 383
Cdd:cd05800 311 YIAEKMLEEDVLIGGEESgglgiRGHIpERD------GILAGLLLLEAVAKTGKPLSELVAELEEEYGPSyyDRIDLRLt 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2181739291 384 -AQPAEAIARVEQH-FAIHAL----EIDRTDGIsmafpQWRFN------LRSSNTEPVVRLNVESR 437
Cdd:cd05800 385 pAQKEAILEKLKNEpPLSIAGgkvdEVNTIDGV-----KLVLEdgswllIRPSGTEPLLRIYAEAP 445
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
7-445 |
1.42e-44 |
|
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: 159.06 E-value: 1.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 7 FKAYDIRGKLGEELNEDIAWRIGRAYGEYlkpqtivlggdvrltsvslklalakglqdagvdvldiglsgteeiyfatfh 86
Cdd:cd03084 2 FGTSGVRGVVGDDITPETAVALGQAIGST--------------------------------------------------- 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 87 lgvdGGIEVTASHNPMDYNGMKLVRKGARPISGDTgLRDVQRLAEANDFP-PVNEAKRGSYKKINLQKEYIDHLLGYINV 165
Cdd:cd03084 31 ----GGIMITASHNPPEDNGIKFVDPDGEPIASEE-EKAIEDLAEKEDEPsAVAYELGGSVKAVDILQRYFEALKKLFDV 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 166 A--NLKPLKLVINSGNGAAGPVVDALearFKALNVPVtfVKVHNTPDGNFPNGIPNPLLPECRDDTRNAVIEHGADMGIA 243
Cdd:cd03084 106 AalSNKKFKVVVDSVNGVGGPIAPQL---LEKLGAEV--IPLNCEPDGNFGNINPDPGSETNLKQLLAVVKAEKADFGVA 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 244 FDGDFDRCFLFDEKGQFIEGYYIVGLLA-EAFLEKNPGAKIIHDPRLSWNTVDVVSAAGGTPVMSKTGHAFIKERMREED 322
Cdd:cd03084 181 FDGDADRLIVVDENGGFLDGDELLALLAvELFLTFNPRGGVVKTVVSSGALDKVAKKLGIKVIRTKTGFKWVGEAMQEGD 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 323 AIYGGEMSAHHYFRDFAYCDSGMIPWLLVTELLCLKGQTLGELVrdrmaafpasgeinsklaqpaEAIARVEQhfaihal 402
Cdd:cd03084 261 VVLGGEESGGVIFPEFHPGRDGISAALLLLEILANLGKSLSELF---------------------SELPRYYY------- 312
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2181739291 403 eiDRTDGIsmafpqWRFNLRSSNTEPVVRLNVESRADTALMEA 445
Cdd:cd03084 313 --IRLKVR------GWVLVRASGTEPAIRIYAEADTQEDVEQI 347
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
11-436 |
1.13e-41 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 155.98 E-value: 1.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 11 DIRGKL--GEE-----LNEDIAWRIGRAYGEYL---------KPQTIVLGGDVRLTSVSLKLALAKGLQDAGVDVLDIGL 74
Cdd:PLN02371 72 DIRGVAveGVEgepvtLTPPAVEAIGAAFAEWLlekkkadgsGELRVSVGRDPRISGPRLADAVFAGLASAGLDVVDMGL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 75 SGTEEIYFATFHLGVDG--GIEVTASHNPMDYNGMKLVRK----GARPISgDTGLRDVQRLAEAND--FPPVNEAKRGSY 146
Cdd:PLN02371 152 ATTPAMFMSTLTEREDYdaPIMITASHLPYNRNGLKFFTKdgglGKPDIK-DILERAARIYKEWSDegLLKSSSGASSVV 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 147 KKINLQKEYIDHLLGYI--NVAN-------LKPLKLVINSGNGAAG----PVVDALEArfkalnvpVTFVKVHNTPDGNF 213
Cdd:PLN02371 231 CRVDFMSTYAKHLRDAIkeGVGHptnyetpLEGFKIVVDAGNGAGGffaeKVLEPLGA--------DTSGSLFLEPDGMF 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 214 PNGIPNPLLPECRDDTRNAVIEHGADMGIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPGAKIIHDPRLSWNT 293
Cdd:PLN02371 303 PNHIPNPEDKAAMSATTQAVLANKADLGIIFDTDVDRSAVVDSSGREINRNRLIALMSAIVLEEHPGTTIVTDSVTSDGL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 294 VDVVSAAGGTPVMSKTGHA-FIKERMR----EEDAIYGGEMSAH------HYFRDFAYCDSGMIPwLLVTELLCLKGQTL 362
Cdd:PLN02371 383 TTFIEKKGGKHHRFKRGYKnVIDKGVRlnsdGEETHLMIETSGHgalkenHFLDDGAYLAVKIII-ELVRMRAAGAGGGL 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 363 GELVRDrMAAFPASGEINSKLAQPA----EAIARVEQHFAIH-----ALEID-------RTDGISMAFPQWrFNLRSSNT 426
Cdd:PLN02371 462 GDLIED-LEEPLEAVELRLKILDEGkdfkAYGEEVLEHLRNSiesdgKLEGApvnyegvRVSDEGEGFGGW-FLLRQSLH 539
|
490
....*....|
gi 2181739291 427 EPVVRLNVES 436
Cdd:PLN02371 540 DPVIPLNIES 549
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
7-136 |
1.50e-38 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 136.20 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 7 FKAYDIRGKLG-EELNEDIAWRIGRAYGEYLKPQ----TIVLGGDVRLTSVSLKLALAKGLQDAGVDVLDIGLSGTEEIY 81
Cdd:pfam02878 4 FGTSGIRGKVGvGELTPEFALKLGQAIASYLRAQggggKVVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTPAVS 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2181739291 82 FATFHLGVDGGIEVTASHNPMDYNGMKLVRKGARPISGDTgLRDVQRLAEANDFP 136
Cdd:pfam02878 84 FATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEV-EKKIEAIIEKEDFY 137
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
262-373 |
8.00e-37 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 131.03 E-value: 8.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 262 EGYYIVGLLAEAFLE---KNPGAKIIHDPRLSWNTVDVVSAAGGTPVMSKTGHAFIKERMREEDAIYGGEMSAHHYFRDF 338
Cdd:pfam02880 1 DGDQILALLAKYLLEqgkLPPGAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLDH 80
|
90 100 110
....*....|....*....|....*....|....*
gi 2181739291 339 AYCDSGMIPWLLVTELLCLKGQTLGELVRDRMAAF 373
Cdd:pfam02880 81 ATTKDGILAALLVLEILARTGKSLSELLEELPEKY 115
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
12-445 |
5.03e-27 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 112.54 E-value: 5.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 12 IRGKLGEE-LNEDIAWRIGRAYGEYLKPQ---TIVLGGDVRLTSVSLKLALAKGLQDAGVDVLDIGLSGTEEIYFATFHL 87
Cdd:PRK10887 9 IRGKVGQApITPDFVLKLGWAAGKVLARQgrpKVLIGKDTRISGYMLESALEAGLAAAGVDVLLTGPMPTPAVAYLTRTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 88 GVDGGIEVTASHNPMDYNGMKLvrkgarpISGD-TGLRD-VQRLAEA---NDFPPVNEAKRGSYKKINlqkeyiDHLLGY 162
Cdd:PRK10887 89 RAEAGIVISASHNPYYDNGIKF-------FSADgTKLPDeVELAIEAeldKPLTCVESAELGKASRIN------DAAGRY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 163 I--------NVANLKPLKLVINSGNGAA---GPVVdalearFKALNVPVtfVKVHNTPDG---NFPNGIPNPllpecrDD 228
Cdd:PRK10887 156 IefckstfpNELSLRGLKIVVDCANGATyhiAPNV------FRELGAEV--IAIGCEPNGlniNDECGATDP------EA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 229 TRNAVIEHGADMGIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPgakiihdprlswntvdVVSAAGGTpVMS- 307
Cdd:PRK10887 222 LQAAVLAEKADLGIAFDGDGDRVIMVDHLGNLVDGDQLLYIIARDRLRRGQ----------------LRGGVVGT-LMSn 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 308 -----------------KTGHAFIKERMREEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVTELLCLKGQTLGELvRDRM 370
Cdd:PRK10887 285 mglelalkqlgipfvraKVGDRYVLEKLQEKGWRLGGENSGHILCLDKTTTGDGIVAALQVLAAMVRSGMSLADL-CSGM 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 371 AAFPA-------SGEINSKLAQPA--EAIARVEQHFAIHAleidrtdgismafpqwRFNLRSSNTEPVVRLNVESRaDTA 441
Cdd:PRK10887 364 KLFPQvlinvrfKPGADDPLESEAvkAALAEVEAELGGRG----------------RVLLRKSGTEPLIRVMVEGE-DEA 426
|
....
gi 2181739291 442 LMEA 445
Cdd:PRK10887 427 QVTA 430
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
154-258 |
6.06e-26 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 101.21 E-value: 6.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 154 EYIDHLLGYINVANLK--PLKLVINSGNGAAGPVVDALEARFKalnvpVTFVKVHNTPDGNFPNGIPNPLLPECRDDTRN 231
Cdd:pfam02879 1 AYIDHLLELVDSEALKkrGLKVVYDPLHGVGGGYLPELLKRLG-----CDVVEENCEPDPDFPTRAPNPEEPEALALLIE 75
|
90 100
....*....|....*....|....*..
gi 2181739291 232 AVIEHGADMGIAFDGDFDRCFLFDEKG 258
Cdd:pfam02879 76 LVKSVGADLGIATDGDADRLGVVDERG 102
|
|
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
7-436 |
2.44e-24 |
|
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: 104.64 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 7 FKAYDIRGKLGEELNEDIAWRIGRAYGEYLKPQTIV-LGGDVRLTSVSLKLALAKGLQDAGVDVLDIGLSGTEEIYFATF 85
Cdd:cd05805 2 FGGRGVSGLINVDITPEFATRLGAAYGSTLPPGSTVtVSRDASRASRMLKRALISGLLSTGVNVRDLGALPLPVARYAIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 86 HLGVDGGIEV-TASHNP-------MDYNGMKLVRKGARPISGDTGLRDVQRlAEANDFPPVNEakrgsykKINLQKEYID 157
Cdd:cd05805 82 FLGASGGIHVrTSPDDPdkveiefFDSRGLNISRAMERKIENAFFREDFRR-AHVDEIGDITE-------PPDFVEYYIR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 158 HLLGYINVANLK--PLKLVINSGNGAAGPVVDALearFKALNVPVTFVKVHNTPDGnfpngiPNPLLPECRDDTR--NAV 233
Cdd:cd05805 154 GLLRALDTSGLKksGLKVVIDYAYGVAGIVLPGL---LSRLGCDVVILNARLDEDA------PRTDTERQRSLDRlgRIV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 234 IEHGADMGIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPGAKIIhdprLSWNTVDVVSAA----GGTPVMSKT 309
Cdd:cd05805 225 KALGADFGVIIDPNGERLILVDEAGRVISDDLLTALVSLLVLKSEPGGTVV----VPVTAPSVIEQLaeryGGRVIRTKT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 310 GHAFIKERMReEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVTELLCLKGQTLGELVRDrmaaFPASGEINSKLAQPAEA 389
Cdd:cd05805 301 SPQALMEAAL-ENVVLAGDGDGGFIFPEFHPGFDAIAALVKILEMLARTNISLSQIVDE----LPRFYVLHKEVPCPWEA 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2181739291 390 IARVEQHFAIHA--LEIDRTDGISMAFPQ-WRFNLRSSNtEPVVRLNVES 436
Cdd:cd05805 376 KGRVMRRLIEEApdKSIELIDGVKIYEDDgWVLVLPDAD-EPLCHIYAEG 424
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
12-251 |
2.23e-19 |
|
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: 90.26 E-value: 2.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 12 IRGKLGE---ELNEDIAWRIGRAYGEYLK-------PQTIVLGGDVRLTSVSLKLALAKGLQDAGVDV--LDiGLSGTEE 79
Cdd:cd05799 9 LRGKMGAgtnRMNDYTVRQATQGLANYLKkkgpdakNRGVVIGYDSRHNSREFAELTAAVLAANGIKVylFD-DLRPTPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 80 IYFATFHLGVDGGIEVTASHNPMDYNGMKL-VRKGARPISG-DTGLRD-VQRLAEANDFPPVNEAKRGSYKKIN--LQKE 154
Cdd:cd05799 88 LSFAVRHLGADAGIMITASHNPKEYNGYKVyWEDGAQIIPPhDAEIAEeIEAVLEPLDIKFEEALDSGLIKYIGeeIDDA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 155 YIDHLLGYI---NVANLKPLKLVINSGNGAAGPVVDALearFKALNVP-VTFVKVHNTPDGNFPN-GIPNPLLPECRDdt 229
Cdd:cd05799 168 YLEAVKKLLvnpELNEGKDLKIVYTPLHGVGGKFVPRA---LKEAGFTnVIVVEEQAEPDPDFPTvKFPNPEEPGALD-- 242
|
250 260
....*....|....*....|....*.
gi 2181739291 230 rnAVIE----HGADMGIAFDGDFDRC 251
Cdd:cd05799 243 --LAIElakkVGADLILATDPDADRL 266
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
13-453 |
1.28e-14 |
|
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: 75.70 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 13 RGkLGEELNEDIAWRIGRAYGEYL----KPQTIVLGGDVRLTSVSLKLALAKGLQDAGVDVLDIGLSGTEEIYFATFHLG 88
Cdd:cd03088 8 RG-LVTDLTDEVCYAYTRAFLQHLeskfPGDTVAVGRDLRPSSPRIAAACAAALRDAGFRVVDCGAVPTPALALYAMKRG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 89 VdGGIEVTASHNPMDYNGMKLVRKGAR-------PISGDTGLRDVQRLAEANDFPPVNEAKRGSYkkinlQKEYIDHLLG 161
Cdd:cd03088 87 A-PAIMVTGSHIPADRNGLKFYRPDGEitkadeaAILAALVELPEALFDPAGALLPPDTDAADAY-----IARYTDFFGA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 162 yinvANLKPLKLVINSGNGAAGpvvDALEARFKALNVPV-------TFVKVhNTpdgnfpngipNPLLPECRDDTRNAVI 234
Cdd:cd03088 161 ----GALKGLRIGVYQHSSVGR---DLLVRILEALGAEVvplgrsdTFIPV-DT----------EAVRPEDRALAAAWAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 235 EHGADMGIAFDGDFDRCFLFDEKGQFIEGyYIVGLLAEAFLeknpGAKIIHDPrLSWNTvdVVSAAGGTPVMSKT--GHA 312
Cdd:cd03088 223 EHGLDAIVSTDGDGDRPLVADETGEWLRG-DILGLLTARFL----GADTVVTP-VSSNS--AIELSGFFKRVVRTriGSP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 313 FIKERMREEDA-----IYGGEMSAHHYFRDFAYCDSGMIPWLL----VTELLCL------KGQTLGELVR---------D 368
Cdd:cd03088 295 YVIAAMAEAAAagagrVVGYEANGGFLLGSDIERNGRTLKALPtrdaVLPILAVlaaakeAGIPLSELVAslparftasD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 369 RMAAFP--ASGEINSKLAQPAEAIARVEQHFAIHALEIDRTDGISMAFPQWRF-NLRSSNTEPVVRLNVEsrADTalmEA 445
Cdd:cd03088 375 RLQNFPteKSQALIARLSADPEARAAFFFALGGEVASIDTTDGLRMTFANGDIvHLRPSGNAPELRCYVE--ADS---EE 449
|
....*...
gi 2181739291 446 RTKDILAL 453
Cdd:cd03088 450 RARELLAR 457
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
378-454 |
1.01e-08 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 51.89 E-value: 1.01e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2181739291 378 EINSKLAQPaEAIARVEQHFA--IHALEIDRTDGismafpqWRFNLRSSNTEPVVRLNVESRaDTALMEARTKDILALL 454
Cdd:pfam00408 1 LINVRVAEK-KKLAALAAILKvfADAEKILGEDG-------RRLDVRPSGTEPVLRVMVEGD-SDEELARLADEIADLL 70
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
33-250 |
1.77e-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: 47.22 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 33 GEYLKPQTIVLGGDVR-----LTSVSLKLALAkglqdAGVDVLDIGLSGteeiYFAT-------FHLGVDGGIEVTASHN 100
Cdd:cd03085 44 PEKLKGATLVVGGDGRyynkeAIQIIIKIAAA-----NGVGKVVVGQNG----LLSTpavsaviRKRKATGGIILTASHN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 101 P--------MDYNgmklVRKGArP--------ISGDTglrdvQRLAEAN--DFPPVNEAKRGSYKKI--NLQKEYIDHLL 160
Cdd:cd03085 115 PggpegdfgIKYN----TSNGG-PapesvtdkIYEIT-----KKITEYKiaDDPDVDLSKIGVTKFGgkPFTVEVIDSVE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 161 GYINVA-------------NLKPLKLVINSGNGAAGPVVDALearF-KALNVPVTFVkVHNTPDGNFPNGIPNPLLPECR 226
Cdd:cd03085 185 DYVELMkeifdfdaikkllSRKGFKVRFDAMHGVTGPYAKKI---FvEELGAPESSV-VNCTPLPDFGGGHPDPNLTYAK 260
|
250 260
....*....|....*....|....
gi 2181739291 227 DdTRNAVIEHGADMGIAFDGDFDR 250
Cdd:cd03085 261 D-LVELMKSGEPDFGAASDGDGDR 283
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
32-250 |
6.91e-05 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 45.06 E-value: 6.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 32 YGEYLKPQTIVLGGDVRLTSVSLKLALAKGLQDAGVDVLDIG-LSGTEEIYFATFHLGVDGGIEVTASHNPMDYNGMKLV 110
Cdd:PTZ00150 83 FGQALKSRGVVIGYDGRYHSRRFAEITASVFLSKGFKVYLFGqTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVY 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181739291 111 -RKGARPIS------GDTGLRDVQRLAEANDfpPVNEAK-RGSYKKINlqKEYIDHLLGYINVA--NLKPLKLVINSGNG 180
Cdd:PTZ00150 163 wSNGAQIIPphdkniSAKILSNLEPWSSSWE--YLTETLvEDPLAEVS--DAYFATLKSEYNPAccDRSKVKIVYTAMHG 238
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2181739291 181 AAGPVVdalEARFKALNVP-VTFVKVHNTPDGNFPN-GIPNpllPECRDDTRNAVIE----HGADMGIAFDGDFDR 250
Cdd:PTZ00150 239 VGTRFV---QKALHTVGLPnLLSVAQQAEPDPEFPTvTFPN---PEEGKGALKLSMEtaeaHGSTVVLANDPDADR 308
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
92-110 |
1.51e-03 |
|
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: 41.04 E-value: 1.51e-03
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