|
Name |
Accession |
Description |
Interval |
E-value |
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
5-444 |
0e+00 |
|
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: 677.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 5 LFGTDGIRGLANRgEMSPEVAFRIGAAIAYQARKRtKHVPHIVVGKDTRLSGYLFETAVASGICALGGEVLLTGPLPTPA 84
Cdd:cd05802 1 LFGTDGIRGVANE-PLTPELALKLGRAAGKVLGKG-GGRPKVLIGKDTRISGYMLESALAAGLTSAGVDVLLLGVIPTPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 85 IAHLATSMRADAGVVISASHNPYQDNGIKIFGPDGFKLPDEMEIEIENLIFgsELDTDRPTGTRVGRAERQDDAPGRYVA 164
Cdd:cd05802 79 VAYLTRKLRADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVEEEIEALID--KELELPPTGEKIGRVYRIDDARGRYIE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 165 FVKASFPNDLtLEGVKIVVDAAHGAAYRTAPLVFSELGAVTYPIGVRPNGKNINHKVGALHPEACAREVQKRHADLGIAL 244
Cdd:cd05802 157 FLKSTFPKDL-LSGLKIVLDCANGAAYKVAPEVFRELGAEVIVINNAPDGLNINVNCGSTHPESLQKAVLENGADLGIAF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 245 DGDADRIIMIDEKGQEVDGDVIMALCATRMLRAKRLRQRTLVATVMSNLGLERAIENDNGKLLRCNVGDRYVVETMRNRG 324
Cdd:cd05802 236 DGDADRVIAVDEKGNIVDGDQILAICARDLKERGRLKGNTVVGTVMSNLGLEKALKELGIKLVRTKVGDRYVLEEMLKHG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 325 LNFGGEQSGHLIFLDHATTGDGLVAAMQVLAILCREQRPLSELAAQvMDRVPQVLVNVSLPERRPLDELPKTRRAIALAE 404
Cdd:cd05802 316 ANLGGEQSGHIIFLDHSTTGDGLLTALQLLAIMKRSGKSLSELASD-MKLYPQVLVNVRVKDKKALLENPRVQAAIAEAE 394
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 931474921 405 KTLGKDGRVLVRWSGTEPKLRVMIEGPRLEKIQTMADDIA 444
Cdd:cd05802 395 KELGGEGRVLVRPSGTEPLIRVMVEGEDEELVEKLAEELA 434
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
6-448 |
0e+00 |
|
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: 546.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 6 FGTDGIRGLANRGEMSPEVAFRIGAAIAYQARKRTKHVPHIVVGKDTRLSGYLFETAVASGICALGGEVLLTGPLPTPAI 85
Cdd:TIGR01455 1 FGTDGVRGRAGQEPLTAELALLLGAAAGRVLRQGRDTAPRVVIGKDTRLSGYMLENALAAGLNSAGVDVLLLGPLPTPAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 86 AHLATSMRADAGVVISASHNPYQDNGIKIFGPDGFKLPDEMEIEIENLIFGsELDTDRPTGTRVGRAERQDDAPGRYVAF 165
Cdd:TIGR01455 81 AYLTRTLRADAGVMISASHNPYEDNGIKFFGPGGFKLDDATEAAIEALLDE-ADPLPRPESEGLGRVKRYPDAVGRYIEF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 166 VKASFPNDLTLEGVKIVVDAAHGAAYRTAPLVFSELGAVTYPIGVRPNGKNINHKVGALHPEACAREVQKRHADLGIALD 245
Cdd:TIGR01455 160 LKSTLPRGLTLSGLKVVLDCANGAAYKVAPHVFRELGAEVIAIGVEPDGLNINDGCGSTHLDALQKAVREHGADLGIAFD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 246 GDADRIIMIDEKGQEVDGDVIMALCATRMLRAKRLRQRTLVATVMSNLGLERAIENDNGKLLRCNVGDRYVVETMRNRGL 325
Cdd:TIGR01455 240 GDADRVLAVDANGRIVDGDQILYIIARALKESGELAGNTVVATVMSNLGLERALEKLGLTLIRTAVGDRYVLEEMRESGY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 326 NFGGEQSGHLIFLDHATTGDGLVAAMQVLAILCREQRPLSELAAQvMDRVPQVLVNVS-LPERRPLDELPKTRRAIALAE 404
Cdd:TIGR01455 320 NLGGEQSGHIILLDYSTTGDGIVSALQVLTIMKKSGSTLSELAAE-FVPYPQTLVNVRvADRKLAAAEAPAVKAAIEDAE 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 931474921 405 KTLGKDGRVLVRWSGTEPKLRVMIEGPRLEKIQTMADDIAAAAQ 448
Cdd:TIGR01455 399 AELGGTGRILLRPSGTEPLIRVMVEAADEELVQQLADTLADVVS 442
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
3-446 |
0e+00 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 544.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 3 RKLFGTDGIRGLANRGEMSPEVAFRIGAAIAYQARKRTKhvPHIVVGKDTRLSGYLFETAVASGICALGGEVLLTGPLPT 82
Cdd:PRK10887 1 RKYFGTDGIRGKVGQAPITPDFVLKLGWAAGKVLARQGR--PKVLIGKDTRISGYMLESALEAGLAAAGVDVLLTGPMPT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 83 PAIAHLATSMRADAGVVISASHNPYQDNGIKIFGPDGFKLPDEMEIEIENLIfgseldtDRPTGT----RVGRAERQDDA 158
Cdd:PRK10887 79 PAVAYLTRTLRAEAGIVISASHNPYYDNGIKFFSADGTKLPDEVELAIEAEL-------DKPLTCvesaELGKASRINDA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 159 PGRYVAFVKASFPNDLTLEGVKIVVDAAHGAAYRTAPLVFSELGAVTYPIGVRPNGKNINHKVGALHPEACAREVQKRHA 238
Cdd:PRK10887 152 AGRYIEFCKSTFPNELSLRGLKIVVDCANGATYHIAPNVFRELGAEVIAIGCEPNGLNINDECGATDPEALQAAVLAEKA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 239 DLGIALDGDADRIIMIDEKGQEVDGDVIMALCATRMLRAKRLRQrTLVATVMSNLGLERAIENDNGKLLRCNVGDRYVVE 318
Cdd:PRK10887 232 DLGIAFDGDGDRVIMVDHLGNLVDGDQLLYIIARDRLRRGQLRG-GVVGTLMSNMGLELALKQLGIPFVRAKVGDRYVLE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 319 TMRNRGLNFGGEQSGHLIFLDHATTGDGLVAAMQVLAILCREQRPLSELAAQvMDRVPQVLVNVSLPERRPL-DELPKTR 397
Cdd:PRK10887 311 KLQEKGWRLGGENSGHILCLDKTTTGDGIVAALQVLAAMVRSGMSLADLCSG-MKLFPQVLINVRFKPGADDpLESEAVK 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 931474921 398 RAIALAEKTLGKDGRVLVRWSGTEPKLRVMIEGPRLEKIQTMADDIAAA 446
Cdd:PRK10887 390 AALAEVEAELGGRGRVLLRKSGTEPLIRVMVEGEDEAQVTALAERIADA 438
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
1-451 |
5.92e-175 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 497.80 E-value: 5.92e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 1 MT-RKLFGTDGIRGLANRgEMSPEVAFRIGAAIAYQARKRTKhvPHIVVGKDTRLSGYLFETAVASGICALGGEVLLTGP 79
Cdd:COG1109 1 MTyKKLFGTDGIRGIVGE-ELTPEFVLKLGRAFGTYLKEKGG--PKVVVGRDTRLSSPMLARALAAGLASAGIDVYDLGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 80 LPTPAIAHLATSMRADAGVVISASHNPYQDNGIKIFGPDGFKLPDEMEIEIENLIFgsELDTDRPTGTRVGRAERQDDAP 159
Cdd:COG1109 78 VPTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIE--KEDFRRAEAEEIGKVTRIEDVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 160 GRYVAFVKASFPNDLTLEGVKIVVDAAHGAAYRTAPLVFSELGAVTYPIGVRPNGKNINHKVG--ALHPEACAREVQKRH 237
Cdd:COG1109 156 EAYIEALKSLVDEALRLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFPNHNPNpePENLEDLIEAVKETG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 238 ADLGIALDGDADRIIMIDEKGQEVDGDVIMALCATRMLraKRLRQRTLVATVMSNLGLERAIENDNGKLLRCNVGDRYVV 317
Cdd:COG1109 236 ADLGIAFDGDADRLGVVDEKGRFLDGDQLLALLARYLL--EKGPGGTVVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 318 ETMRNRGLNFGGEQSGHLIFLDHATTGDGLVAAMQVLAILCREQRPLSELAAQvMDRVPQVLVNVSLPERRPLDEL---- 393
Cdd:COG1109 314 EKMRETGAVLGGEESGGIIFPDFVPTDDGILAALLLLELLAKQGKSLSELLAE-LPRYPQPEINVRVPDEEKIGAVmekl 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931474921 394 ------PKTRRAIALAEKTLGKDGRVLVRWSGTEPKLRVMIEGPRLEKIQTMADDIAAAAQKEV 451
Cdd:COG1109 393 reavedKEELDTIDGVKVDLEDGGWVLVRPSGTEPLLRVYAEAKDEEEAEELLAELAELVEEAL 456
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
4-446 |
2.77e-109 |
|
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: 330.24 E-value: 2.77e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 4 KLFGTDGIRGLANRgEMSPEVAFRIGAAIAYQARKRTkhvphIVVGKDTRLSGYLFETAVASGICALGGEVLLTGPLPTP 83
Cdd:TIGR03990 2 LLFGTSGIRGIVGE-ELTPELALKVGKAFGTYLRGGK-----VVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLGIAPTP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 84 AIAHLATSMRADAGVVISASHNPYQDNGIKIFGPDGFKLPDEMEIEIENLIFgsELDTDRPTGTRVGRAERQDDAPGRYV 163
Cdd:TIGR03990 76 TLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQEEEIEEIAE--SGDFERADWDEIGTVTSDEDAIDDYI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 164 AFVKASFP-NDLTLEGVKIVVDAAHGAAYRTAPLVFSELGAVTYPIGVRPNGKNINHkvgalHPE-------ACAREVQK 235
Cdd:TIGR03990 154 EAILDKVDvEAIRKKGFKVVVDCGNGAGSLTTPYLLRELGCKVITLNCQPDGTFPGR-----NPEptpenlkDLSALVKA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 236 RHADLGIALDGDADRIIMIDEKGQEVDGDVIMALCATRMLRAKRlrqRTLVATVMSNLGLERAIENDNGKLLRCNVGDRY 315
Cdd:TIGR03990 229 TGADLGIAHDGDADRLVFIDEKGRFIGGDYTLALFAKYLLEHGG---GKVVTNVSSSRAVEDVAERHGGEVIRTKVGEVN 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 316 VVETMRNRGLNFGGEQSGHLIFLDHATTGDGLVAAMQVLAILCREQRPLSELAAQvMDRVPQVLVNVSLPERRPLDELPK 395
Cdd:TIGR03990 306 VAEKMKEEGAVFGGEGNGGWIFPDHHYCRDGLMAAALFLELLAEEGKPLSELLAE-LPKYPMSKEKVELPDEDKEEVMEA 384
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 931474921 396 TRRAIALAE-------KTLGKDGRVLVRWSGTEPKLRVMIEGPRLEKIQTMADDIAAA 446
Cdd:TIGR03990 385 VEEEFADAEidtidgvRIDFEDGWVLVRPSGTEPIVRIYAEAKTEERAEELLEEGRSL 442
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
5-447 |
8.41e-104 |
|
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: 316.05 E-value: 8.41e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 5 LFGTDGIRGLANRgEMSPEVAFRIGAAIAYQARKRTkhvphIVVGKDTRLSGYLFETAVASGICALGGEVLLTGPLPTPA 84
Cdd:cd03087 1 LFGTSGIRGVVGE-ELTPELALKVGKALGTYLGGGT-----VVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDIGIVPTPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 85 IAHlATSMRADAGVVISASHNPYQDNGIKIFGPDGFKLPDEMEIEIENLIFGSelDTDRPTGTRVGRAERQDDAPGRYVA 164
Cdd:cd03087 75 LQY-AVRKLGDAGVMITASHNPPEYNGIKLVNPDGTEFSREQEEEIEEIIFSE--RFRRVAWDEVGSVRREDSAIDEYIE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 165 FVKASFpNDLTLEGVKIVVDAAHGAAYRTAPLVFSELGAVTYPIGVRPNGKNINHkvgalHPE-------ACAREVQKRH 237
Cdd:cd03087 152 AILDKV-DIDGGKGLKVVVDCGNGAGSLTTPYLLRELGCKVITLNANPDGFFPGR-----PPEptpenlsELMELVRATG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 238 ADLGIALDGDADRIIMIDEKGQEVDGDVIMALCATRMLRAkrlRQRTLVATVMSNLGLERAIENDNGKLLRCNVGDRYVV 317
Cdd:cd03087 226 ADLGIAHDGDADRAVFVDEKGRFIDGDKLLALLAKYLLEE---GGGKVVTPVDASMLVEDVVEEAGGEVIRTPVGDVHVA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 318 ETMRNRGLNFGGEQSGHLIFLDHATTGDGLVAAMQVLAILCREqRPLSELAaqvmDRVPQ-VLVNVSLPerRPLDELPKT 396
Cdd:cd03087 303 EEMIENGAVFGGEPNGGWIFPDHQLCRDGIMTAALLLELLAEE-KPLSELL----DELPKyPLLREKVE--CPDEKKEEV 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931474921 397 RRAIALAEKTLG-------------KDGRVLVRWSGTEPKLRVMIEGPRLEKIQTMADDIAAAA 447
Cdd:cd03087 376 MEAVEEELSDADedvdtidgvrieyEDGWVLIRPSGTEPKIRITAEAKTEERAKELLEEGRSKV 439
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
11-439 |
8.22e-75 |
|
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: 241.26 E-value: 8.22e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 11 IRGLANRgEMSPEVAFRIGAAIAYQARKRTKhvPHIVVGKDTRLSGYLFETAVASGICALGGEVLLTGPLPTPAiAHLAT 90
Cdd:cd03089 7 IRGIAGE-ELTEEIAYAIGRAFGSWLLEKGA--KKVVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPV-LYFAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 91 SM-RADAGVVISASHNPYQDNGIKIFGPDGFKLPDEMEiEIENLIfgSELDTDRPTGTrvGRAERQDDAPgRYVAFVKAS 169
Cdd:cd03089 83 FHlDADGGVMITASHNPPEYNGFKIVIGGGPLSGEDIQ-ALRERA--EKGDFAAATGR--GSVEKVDILP-DYIDRLLSD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 170 FpnDLTLEGVKIVVDAAHGAAYRTAPLVFSELGAVTYPIGVRPNGKNINHkvgalHP--------EACAREVQKRHADLG 241
Cdd:cd03089 157 I--KLGKRPLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCEPDGTFPNH-----HPdptdpenlEDLIAAVKENGADLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 242 IALDGDADRIIMIDEKGQEVDGDVIMALCATRMLraKRLRQRTLVATVMSNLGLERAIENDNGKLLRCNVGDRYVVETMR 321
Cdd:cd03089 230 IAFDGDGDRLGVVDEKGEIIWGDRLLALFARDIL--KRNPGATIVYDVKCSRNLYDFIEEAGGKPIMWKTGHSFIKAKMK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 322 NRGLNFGGEQSGHLIF------LDhattgDGLVAAMQVLAILCREQRPLSELAAQVMDRVPQVLVNVSLPERRPLDELPK 395
Cdd:cd03089 308 ETGALLAGEMSGHIFFkdrwygFD-----DGIYAALRLLELLSKSGKTLSELLADLPKYFSTPEIRIPVTEEDKFAVIER 382
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 931474921 396 TRRAIALAEKTL---------GKDGRVLVRWSGTEPKLRVMIEGP---RLEKIQTM 439
Cdd:cd03089 383 LKEHFEFPGAEIididgvrvdFEDGWGLVRASNTEPVLVLRFEADteeGLEEIKAE 438
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
5-430 |
3.15e-69 |
|
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: 224.16 E-value: 3.15e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 5 LFGTDGIRGLANRGeMSPEVAFRIGAAIAYQArkrtkhvphivvgkdtrlsgylfetavasgicalggevlltgplptpa 84
Cdd:cd03084 1 IFGTSGVRGVVGDD-ITPETAVALGQAIGSTG------------------------------------------------ 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 85 iahlatsmradaGVVISASHNPYQDNGIKIFGPDGFKLPDEMEIEIENLIFgsELDTDRPTGTRVGRAERQDDAPGRYVA 164
Cdd:cd03084 32 ------------GIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAE--KEDEPSAVAYELGGSVKAVDILQRYFE 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 165 FVKASFPNDLT-LEGVKIVVDAAHGAAYRTAPLVFSELGAVTYPIGVRPNGKNinhkvGALHPEACARE--------VQK 235
Cdd:cd03084 98 ALKKLFDVAALsNKKFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCEPDGNF-----GNINPDPGSETnlkqllavVKA 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 236 RHADLGIALDGDADRIIMIDEKGQEVDGDVIMALCATRMLRaKRLRQRTLVATVMSNLGLERAIENDNGKLLRCNVGDRY 315
Cdd:cd03084 173 EKADFGVAFDGDADRLIVVDENGGFLDGDELLALLAVELFL-TFNPRGGVVKTVVSSGALDKVAKKLGIKVIRTKTGFKW 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 316 VVETMRNRGLNFGGEQSGHLIFLDHATTGDGLVAAMQVLAILCREQRPLSELAAQvMDRVPQVLVNVSlperrpldelpk 395
Cdd:cd03084 252 VGEAMQEGDVVLGGEESGGVIFPEFHPGRDGISAALLLLEILANLGKSLSELFSE-LPRYYYIRLKVR------------ 318
|
410 420 430
....*....|....*....|....*....|....*
gi 931474921 396 trraialaektlgkdGRVLVRWSGTEPKLRVMIEG 430
Cdd:cd03084 319 ---------------GWVLVRASGTEPAIRIYAEA 338
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
6-439 |
1.19e-62 |
|
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: 210.10 E-value: 1.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 6 FGTDGIRGLANRgEMSPEVAFRIGAAIAYQARKRTKHVPHIVVGKDTRLSGYLFETAVASGICALGGEVLLT-GPLPTPA 84
Cdd:cd05800 3 FGTDGWRGIIAE-DFTFENVRRVAQAIADYLKEEGGGGRGVVVGYDTRFLSEEFARAVAEVLAANGIDVYLSdRPVPTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 85 IAHLATSMRADAGVVISASHNPYQDNGIKIFGPDGFKLPDEMEIEIENLIfgSELDTDRPTGTRVGRAERQDDAPGrYVA 164
Cdd:cd05800 82 VSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARL--ASGEPPGLEARAEGLIETIDPKPD-YLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 165 FVKASFpnDLTL---EGVKIVVDAAHGAAYRTAPLVFSELGAVTYPI---------GVRPN--GKNInhkvgalhpEACA 230
Cdd:cd05800 159 ALRSLV--DLEAireAGLKVVVDPMYGAGAGYLEELLRGAGVDVEEIraerdplfgGIPPEpiEKNL---------GELA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 231 REVQKRHADLGIALDGDADRIIMIDEKGQEVDGDVIMALCATRMLRAKRLRQRtLVATV-MSNLgLERAIENDNGKLLRC 309
Cdd:cd05800 228 EAVKEGGADLGLATDGDADRIGAVDEKGNFLDPNQILALLLDYLLENKGLRGP-VVKTVsTTHL-IDRIAEKHGLPVYET 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 310 NVGDRYVVETMRNRGLNFGGEQSGHLIFLDHATTGDGLVAAMQVLAILCREQRPLSELAAQVMDRVP---QVLVNVSLPE 386
Cdd:cd05800 306 PVGFKYIAEKMLEEDVLIGGEESGGLGIRGHIPERDGILAGLLLLEAVAKTGKPLSELVAELEEEYGpsyYDRIDLRLTP 385
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 931474921 387 -------RRPLDELPKTRRAIALAEKT--------LGKDGRVLVRWSGTEPKLRVMIEGPRLEKIQTM 439
Cdd:cd05800 386 aqkeailEKLKNEPPLSIAGGKVDEVNtidgvklvLEDGSWLLIRPSGTEPLLRIYAEAPSPEKVEAL 453
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
3-135 |
5.50e-51 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 168.94 E-value: 5.50e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 3 RKLFGTDGIRGLANRGEMSPEVAFRIGAAIAYQARKRTKhVPHIVVGKDTRLSGYLFETAVASGICALGGEVLLTGPLPT 82
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGELTPEFALKLGQAIASYLRAQGG-GGKVVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPT 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 931474921 83 PAIAHLATSMRADAGVVISASHNPYQDNGIKIFGPDGFKLPDEMEIEIENLIF 135
Cdd:pfam02878 80 PAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIE 132
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
10-441 |
7.48e-48 |
|
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: 170.18 E-value: 7.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 10 GIRGLANRGeMSPEVAFRIGAAIAYQARKRTKHvPHIVVGKDTRLSGYLFETAVASGICALGGEVLLTGPLPTPAIAHLA 89
Cdd:cd05803 6 GIRGIVGEG-LTPEVITRYVAAFATWQPERTKG-GKIVVGRDGRPSGPMLEKIVIGALLACGCDVIDLGIAPTPTVQVLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 90 TSMRADAGVVISASHNPYQDNGIKIFGPDGFKLPDEmeiEIENLIFGSELDTDRPTGTR-VGRAERQDDAPGRYVAFVKA 168
Cdd:cd05803 84 RQSQASGGIIITASHNPPQWNGLKFIGPDGEFLTPD---EGEEVLSCAEAGSAQKAGYDqLGEVTFSEDAIAEHIDKVLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 169 SfpNDLTLEGV-----KIVVDAAHGAAYRTAPLVFSELGAVTYPIGVRPNGKNinhkvgALHPEACA-------REVQKR 236
Cdd:cd05803 161 L--VDVDVIKIrernfKVAVDSVNGAGGLLIPRLLEKLGCEVIVLNCEPTGLF------PHTPEPLPenltqlcAAVKES 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 237 HADLGIALDGDADRIIMIDEKGQEVDGDVIMALCATRMLRAKRLRqrtlvATVMSNLGLERAIEN----DNGKLLRCNVG 312
Cdd:cd05803 233 GADVGFAVDPDADRLALVDEDGRPIGEEYTLALAVDYVLKYGGRK-----GPVVVNLSTSRALEDiarkHGVPVFRSAVG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 313 DRYVVETMRNRGLNFGGEQSGHLIFLDHATTGDGLVAAMQVLAILCREQRPLSELAAQvmdrVPQVLV---NVSLPeRRP 389
Cdd:cd05803 308 EANVVEKMKEVDAVIGGEGNGGVILPDVHYGRDSLVGIALVLQLLAASGKPLSEIVDE----LPQYYIsktKVTIA-GEA 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 390 LDELPKTRRAIALAEKTLGKDG--------RVLVRWSGTEPKLRVMIEGPRLEKIQTMAD 441
Cdd:cd05803 383 LERLLKKLEAYFKDAEASTLDGlrldsedsWVHVRPSNTEPIVRIIAEAPTQDEAEALAD 442
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
262-374 |
4.41e-44 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 150.29 E-value: 4.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 262 DGDVIMALCATRMLRAKRLRQ-RTLVATVMSNLGLERAIENDNGKLLRCNVGDRYVVETMRNRGLNFGGEQSGHLIFLDH 340
Cdd:pfam02880 1 DGDQILALLAKYLLEQGKLPPgAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLDH 80
|
90 100 110
....*....|....*....|....*....|....
gi 931474921 341 ATTGDGLVAAMQVLAILCREQRPLSELAAQVMDR 374
Cdd:pfam02880 81 ATTKDGILAALLVLEILARTGKSLSELLEELPEK 114
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
11-445 |
9.84e-40 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 148.21 E-value: 9.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 11 IRGLANRgEMSPEVAFRIGAAIAyqARKRTKHVPHIVVGKDTRLSGYLFETAVASGICALGGEVLLTGPLPTPAIAHLAT 90
Cdd:PRK09542 6 VRGVVGE-QIDEDLVRDVGAAFA--RLMRAEGATTVVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIGLASTDQLYFASG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 91 SMRAdAGVVISASHNPYQDNGIKI-------FGPD-GFKlpdemeiEIENLIFGSELDTDRPTGTRVGRaerqdDAPGRY 162
Cdd:PRK09542 83 LLDC-PGAMFTASHNPAAYNGIKLcragakpVGQDtGLA-------AIRDDLIAGVPAYDGPPGTVTER-----DVLADY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 163 VAFVKaSFPNDLTLEGVKIVVDAAHGAAYRTAPLVFSELgavtyPIGVRP-----NGKNINHKVGALHPeACAREVQKR- 236
Cdd:PRK09542 150 AAFLR-SLVDLSGIRPLKVAVDAGNGMGGHTVPAVLGGL-----PITLLPlyfelDGTFPNHEANPLDP-ANLVDLQAFv 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 237 ---HADLGIALDGDADRIIMIDEKGQEVDGDVIMALCATRMLrakrlrQRTLVATVMSNLGLERA----IENDNGKLLRC 309
Cdd:PRK09542 223 retGADIGLAFDGDADRCFVVDERGQPVSPSAVTALVAAREL------AREPGATIIHNLITSRAvpelVAERGGTPVRT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 310 NVGDRYVVETMRNRGLNFGGEQSGHLIFLDHATTGDGLVAAMQVLAILCREQRPLSELAAQVMDRVPQVLVNVSlperrp 389
Cdd:PRK09542 297 RVGHSFIKALMAETGAIFGGEHSAHYYFRDFWGADSGMLAALHVLAALGEQDRPLSELMADYQRYAASGEINST------ 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 390 LDELPKTRRAI--ALAEKT------------LGKDGRVLVRWSGTEPKLRVMIEGPRLEKIQTMADDIAA 445
Cdd:PRK09542 371 VADAPARMEAVlkAFADRIvsvdhldgvtvdLGDGSWFNLRASNTEPLLRLNVEARTEEEVDALVDEVLA 440
|
|
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
5-442 |
6.75e-34 |
|
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: 131.99 E-value: 6.75e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 5 LFGTDGIRGLANrGEMSPEVAFRIGAAIAYQARKRTKhvphIVVGKDTRLSGYLFETAVASGICALGGEVLLTGPLPTPA 84
Cdd:cd05805 1 LFGGRGVSGLIN-VDITPEFATRLGAAYGSTLPPGST----VTVSRDASRASRMLKRALISGLLSTGVNVRDLGALPLPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 85 IAHLATSMRADAGVVISAShnpYQDNG---IKIFGPDGFKLPDEMEIEIENlIFGSElDTDRPTGTRVGRAErqddAPGR 161
Cdd:cd05805 76 ARYAIRFLGASGGIHVRTS---PDDPDkveIEFFDSRGLNISRAMERKIEN-AFFRE-DFRRAHVDEIGDIT----EPPD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 162 YVAFVKASFPNDLTLEGV-----KIVVDAAHGAAYRTAPLVFSELG--AVTYPIGVRPNGKNINHKVGALHPEAcAREVQ 234
Cdd:cd05805 147 FVEYYIRGLLRALDTSGLkksglKVVIDYAYGVAGIVLPGLLSRLGcdVVILNARLDEDAPRTDTERQRSLDRL-GRIVK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 235 KRHADLGIALDGDADRIIMIDEKGQEVDGDviMALCATRMLRAKRLRQRTLVATVMSNLGLERAIENDNGKLLRCNVGDR 314
Cdd:cd05805 226 ALGADFGVIIDPNGERLILVDEAGRVISDD--LLTALVSLLVLKSEPGGTVVVPVTAPSVIEQLAERYGGRVIRTKTSPQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 315 YVVETMRNrGLNFGGEQSGHLIFLDHATTGDGLVAAMQVLAILCREQRPLSELAaqvmDRVPQVLVN---VSLPE----- 386
Cdd:cd05805 304 ALMEAALE-NVVLAGDGDGGFIFPEFHPGFDAIAALVKILEMLARTNISLSQIV----DELPRFYVLhkeVPCPWeakgr 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 387 --RRPLDELPktRRAIALAE--KTLGKDGRVLVRWSGTEPKLRVMIEGPRLEKIQTMADD 442
Cdd:cd05805 379 vmRRLIEEAP--DKSIELIDgvKIYEDDGWVLVLPDADEPLCHIYAEGSDQERAEELTEF 436
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
6-429 |
9.52e-34 |
|
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The mammalian PGM2 is thought to be a phosphopentomutase that catalyzes the conversion of the nucleoside breakdown products, ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. PGM2L1 is thought to catalyze the 1,3-bisphosphoglycerate-dependent synthesis of glucose 1,6-bisphosphate and other aldose-bisphosphates that serve as cofactors for several sugar phosphomutases and possibly also as regulators of glycolytic enzymes. PGM2 and PGM2L1 belong to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100092 Cd Length: 487 Bit Score: 132.24 E-value: 9.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 6 FGTDGIRGL--ANRGEMSPEVAFRIGAAIAY--QARKRTKHVPHIVVGKDTRLSGYLFETAVASGICALGGEV-LLTGPL 80
Cdd:cd05799 4 FGTAGLRGKmgAGTNRMNDYTVRQATQGLANylKKKGPDAKNRGVVIGYDSRHNSREFAELTAAVLAANGIKVyLFDDLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 81 PTPAIAHLATSMRADAGVVISASHNPYQDNGIKIFGPDGFKLPDEMEIEIENLI------FGSELDTDRPTGTRVGRAER 154
Cdd:cd05799 84 PTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIeavlepLDIKFEEALDSGLIKYIGEE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 155 QDDApgrYVAFVKA--SFPNDLTLEGVKIVVDAAHGAAYRTAPLVFSELGaVTYPIGVR----PNG-----KNINhkvga 223
Cdd:cd05799 164 IDDA---YLEAVKKllVNPELNEGKDLKIVYTPLHGVGGKFVPRALKEAG-FTNVIVVEeqaePDPdfptvKFPN----- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 224 lhPE-----ACAREVQKRH-ADLGIALDGDADRI-IMI---DEKGQEVDGDVIMAL----CATRMLRAKRLRQRTLVA-- 287
Cdd:cd05799 235 --PEepgalDLAIELAKKVgADLILATDPDADRLgVAVkdkDGEWRLLTGNEIGALladyLLEQRKEKGKLPKNPVIVkt 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 288 TVMSNLgLERAIENDNGKLLRCNVGDRYVVETMRNR-----GLNFGGEQS-GHLiFLDHATTGDGLVAAMQVLAILCreq 361
Cdd:cd05799 313 IVSSEL-LRKIAKKYGVKVEETLTGFKWIGNKIEELesggkKFLFGFEESiGYL-VGPFVRDKDGISAAALLAEMAA--- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 362 rplsELAAQVMDrVPQVL------------VNVSLpERRPLDELPKTRRAIA-LAEK------TLGKDGRVLVRWSGTEP 422
Cdd:cd05799 388 ----YLKAQGKT-LLDRLdelyekygyykeKTISI-TFEGKEGPEKIKAIMDrLRNNpnvltfYLEDGSRVTVRPSGTEP 461
|
....*..
gi 931474921 423 KLRVMIE 429
Cdd:cd05799 462 KIKFYIE 468
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
3-335 |
1.88e-30 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 124.01 E-value: 1.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 3 RKLFGTDGIRGLANRGE------MSPEVAFRIGAAIAYQARKRTKHVPH----IVVGKDTRLSGYLFETAVASGICALGG 72
Cdd:PLN02371 65 RKLQNGSDIRGVAVEGVegepvtLTPPAVEAIGAAFAEWLLEKKKADGSgelrVSVGRDPRISGPRLADAVFAGLASAGL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 73 EVLLTGPLPTPAIAH--LATSMRADAGVVISASHNPYQDNGIKIFGPD-GFKLPDemeieIENLIFGSELDTDRPTGTRV 149
Cdd:PLN02371 145 DVVDMGLATTPAMFMstLTEREDYDAPIMITASHLPYNRNGLKFFTKDgGLGKPD-----IKDILERAARIYKEWSDEGL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 150 GRAERQDDAPGRYVAF---------------VKASFPNDLTLEGVKIVVDAAHGAAYRTAPLVFSELGA-VTYPIGVRPN 213
Cdd:PLN02371 220 LKSSSGASSVVCRVDFmstyakhlrdaikegVGHPTNYETPLEGFKIVVDAGNGAGGFFAEKVLEPLGAdTSGSLFLEPD 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 214 GKNINHKVGALHPEACA---REVQKRHADLGIALDGDADRIIMIDEKGQEVDGDVIMALCATRMLRAkrlRQRTLVAT-- 288
Cdd:PLN02371 300 GMFPNHIPNPEDKAAMSattQAVLANKADLGIIFDTDVDRSAVVDSSGREINRNRLIALMSAIVLEE---HPGTTIVTds 376
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 931474921 289 VMSNlGLERAIENDNGKLLRCNVGDRYVVEtmRNRGLNFGGEQSgHL 335
Cdd:PLN02371 377 VTSD-GLTTFIEKKGGKHHRFKRGYKNVID--KGVRLNSDGEET-HL 419
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
6-448 |
9.76e-30 |
|
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: 120.77 E-value: 9.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 6 FGTDGIRGLAnrGEMSPEVAFrigaaiAYqARKRTKHVPH------IVVGKDTRLSGYLFETAVASGICALGGEVLLTGP 79
Cdd:cd03088 2 FGTSGLRGLV--TDLTDEVCY------AY-TRAFLQHLESkfpgdtVAVGRDLRPSSPRIAAACAAALRDAGFRVVDCGA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 80 LPTPAIAHLAtsMRADAG-VVISASHNPYQDNGIKIFGPDG-FKLPDEMEIEIENLIFGSELDTDRPTGtrvgrAERQDD 157
Cdd:cd03088 73 VPTPALALYA--MKRGAPaIMVTGSHIPADRNGLKFYRPDGeITKADEAAILAALVELPEALFDPAGAL-----LPPDTD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 158 APGRYVAFVKASFPNDlTLEGVKIVVDAaHGAAYRTAPL-VFSELGAVTYPIGvRPNgKNINHKVGALHPEACARE---V 233
Cdd:cd03088 146 AADAYIARYTDFFGAG-ALKGLRIGVYQ-HSSVGRDLLVrILEALGAEVVPLG-RSD-TFIPVDTEAVRPEDRALAaawA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 234 QKRHADLGIALDGDADRIIMIDEKGQEVDGDVIMALCAtRMLRAKrlrqrTLVATVMSNLGLERAieNDNGKLLRCNVGD 313
Cdd:cd03088 222 AEHGLDAIVSTDGDGDRPLVADETGEWLRGDILGLLTA-RFLGAD-----TVVTPVSSNSAIELS--GFFKRVVRTRIGS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 314 RYVVETM-----RNRGLNFGGEQSGHLIFLDHATTGDGLVAAM----QVLAILC------REQRPLSELAAQ------VM 372
Cdd:cd03088 294 PYVIAAMaeaaaAGAGRVVGYEANGGFLLGSDIERNGRTLKALptrdAVLPILAvlaaakEAGIPLSELVASlparftAS 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 373 DRVPQVLVNVSlpeRRPLDEL--PKTRRAIALAE---------KTLG-----KDGRVL-VRWSGTEPKLRVMIEgprlek 435
Cdd:cd03088 374 DRLQNFPTEKS---QALIARLsaDPEARAAFFFAlggevasidTTDGlrmtfANGDIVhLRPSGNAPELRCYVE------ 444
|
490
....*....|...
gi 931474921 436 iqtmADDIAAAAQ 448
Cdd:cd03088 445 ----ADSEERARE 453
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
11-429 |
9.18e-29 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 117.74 E-value: 9.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 11 IRGLANRgEMSPEVAFRIGAAIAYQARKRTkhvphIVVGKDTRLSGYLFETAVASGICALGGEVLLTGPLPTPAIAHLAT 90
Cdd:PRK15414 12 IRGKLGE-ELNEDIAWRIGRAYGEFLKPKT-----IVLGGDVRLTSETLKLALAKGLQDAGVDVLDIGMSGTEEIYFATF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 91 SMRADAGVVISASHNPYQDNGIK--------IFGPDGFKlpdemeiEIENLifgSELDTDRPTGTRVGRAERQDDAPGRY 162
Cdd:PRK15414 86 HLGVDGGIEVTASHNPMDYNGMKlvregarpISGDTGLR-------DVQRL---AEANDFPPVDETKRGRYQQINLRDAY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 163 VAFVkASFPNDLTLEGVKIVVDAAHGAAyrtAPLV------FSELGAVTYPIGVR--PNGKNINHKVGALHPEACA---R 231
Cdd:PRK15414 156 VDHL-FGYINVKNLTPLKLVINSGNGAA---GPVVdaiearFKALGAPVELIKVHntPDGNFPNGIPNPLLPECRDdtrN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 232 EVQKRHADLGIALDGDADRIIMIDEKGQEVDGDVIMALCATRMLR----AKRLRQRTLvatvmsNLGLERAIENDNGKLL 307
Cdd:PRK15414 232 AVIKHGADMGIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEknpgAKIIHDPRL------SWNTVDVVTAAGGTPV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 308 RCNVGDRYVVETMRNRGLNFGGEQSGHLIFLDHATTGDGLVAAMQVLAILCREQRPLSELAAQVMDRVPQV-LVNVSLPE 386
Cdd:PRK15414 306 MSKTGHAFIKERMRKEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELVCLKGKTLGELVRDRMAAFPASgEINSKLAQ 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 931474921 387 rrPLDELPKTRRAI---ALA-EKTLG-----KDGRVLVRWSGTEPKLRVMIE 429
Cdd:PRK15414 386 --PVEAINRVEQHFsreALAvDRTDGismtfADWRFNLRSSNTEPVVRLNVE 435
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
6-449 |
2.80e-15 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 77.87 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 6 FGTDGIRGLANRGemspevAFR------IGAAIAYQARKRTKHVPhIVVGKDTRlsgYLFETAVASGI---CALGGEVLL 76
Cdd:PRK07564 40 FGTSGHRGSSLQP------SFNenhilaIFQAICEYRGKQGITGP-LFVGGDTH---ALSEPAIQSALevlAANGVGVVI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 77 T---GPLPTPAIAHL------ATSMRADaGVVISASHNPYQDNGIKIFGPDGFKLPDEMEIEIEN----LIFGSELDTDR 143
Cdd:PRK07564 110 VgrgGYTPTPAVSHAilkyngRGGGLAD-GIVITPSHNPPEDGGIKYNPPNGGPADTDVTDAIEAraneLLAYGLKGVKR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 144 PTGTRVGRAERQD--DAPGRYVAFVKASFpnDLTL---EGVKIVVDAAHGA----AYRTAPLVFSELGAVTYPIGVRPNG 214
Cdd:PRK07564 189 IPLDRALASMTVEviDPVADYVEDLENVF--DFDAirkAGLRLGVDPLGGAtgpyWKAIAERYGLDLTVVNAPVDPTFNF 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 215 KNINHKvGALHPE-----ACAREVQKRHA-DLGIALDGDADRiIMIDEKGQEVDGDVIMALCATrmlRAKRLRQ------ 282
Cdd:PRK07564 267 MPLDDD-GKIRMDcsspyAMAGLLALKDAfDLAFANDPDGDR-HGIVTPGGLMNPNHYLAVAIA---YLFHHRPgwraga 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 283 ---RTLVATVMsnlgLERAIENDNGKLLRCNVGDRYVVETMRNRGLNFGGEQSGHLIFL-----DHATTGDGLVAAMQVL 354
Cdd:PRK07564 342 gvgKTLVSSAM----IDRVAAKLGRKLYEVPVGFKWFVNGLDDGSLGFGGEESAGASFLrrdgsVWTTDKDGLIAVLLAA 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 355 AILCREQRPLSELAAQVMDR-------------VPQVLVNVS--LPERRPLDEL------------PKTRRAIA-LaeKT 406
Cdd:PRK07564 418 EILAVTGKSPSEIYRELWARfgrpyysrhdapaTPEQKAALRklSPELVGATELagdpidaslteaPGNGAAIGgL--KV 495
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 931474921 407 LGKDGRVLVRWSGTEPKLRVMIE----GPRLEKIQTMADDIAAAAQK 449
Cdd:PRK07564 496 VTENGWFAARPSGTETTYKIYAEsfegDEHLHQIQKEAQEIVADLIA 542
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
162-258 |
1.37e-14 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 69.24 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 162 YVAFVKASFPND-LTLEGVKIVVDAAHGAAYRTAPLVFSELGAVTYPIGVRPNGKNINHKVGALHPEACAR---EVQKRH 237
Cdd:pfam02879 2 YIDHLLELVDSEaLKKRGLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDPDFPTRAPNPEEPEALALlieLVKSVG 81
|
90 100
....*....|....*....|.
gi 931474921 238 ADLGIALDGDADRIIMIDEKG 258
Cdd:pfam02879 82 ADLGIATDGDADRLGVVDERG 102
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
379-446 |
2.21e-12 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 62.29 E-value: 2.21e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 931474921 379 LVNVSLPERRPLDELPKTRRAIALAEKTLGKDGRVL-VRWSGTEPKLRVMIEGPRLEKIQTMADDIAAA 446
Cdd:pfam00408 1 LINVRVAEKKKLAALAAILKVFADAEKILGEDGRRLdVRPSGTEPVLRVMVEGDSDEELARLADEIADL 69
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
96-449 |
7.64e-12 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 67.37 E-value: 7.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 96 AGVVISASHNPYQDNGIKIFGPDGFKLPDEMEIEIENLI-------FGSEL----------------------------- 139
Cdd:PTZ00302 77 VGVMITASHNPIQDNGVKIIDPDGGMLEESWEKICTDFAnartgedLVSVLmdcltehgiklsnlkldlnksncskakvh 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 140 ---DTdRPTGTR-------------------------------VGRAERQDDAPGR-----YVAFVKASF---------- 170
Cdd:PTZ00302 157 vgrDT-RPSSPElvsallrglklligsnvrnfgivttpqlhflVAFANGLGVDVVEssdelYYAYLLAAFkelyrtlqeg 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 171 -PNDLTLEGV-KIVVDAAHG-AAYRTAPL--VFSELGAVTYPI-GVRPNGKNINHKVGALH------PEACAREVQKRHA 238
Cdd:PTZ00302 236 gPVDLTQNNSkILVVDCANGvGGYKIKRFfeALKQLGIEIIPInINCDEEELLNDKCGADYvqktrkPPRAMKEWPGDEE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 239 DLGIALDGDADRII--MIDEKGQEV----DGD---VIMALCATRMLRAKRLRQR---TLVATVMSN----------LGLE 296
Cdd:PTZ00302 316 TRVASFDGDADRLVyfFPDKDGDDKwvllDGDriaILYAMLIKKLLGKIQLKKKldiGVVQTAYANgastnylnelLGRL 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 297 RA------IENDNGKLLRCNVGDRY-----------------VVETMRNRG-LNFGGEQSGHLIFLDHATTGDGLVAAMQ 352
Cdd:PTZ00302 396 RVycaptgVKNLHPKAHKYDIGIYFeanghgtvlfnekalaeWAKFLAKQNaLNSACRQLEKFLRLFNQTIGDAISDLLA 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 353 VLAILCREQRPLSELAAQVMDRvPQVLVNVSLPERR----PLDElpktRRAIA---LAEK------TLGKDGRVLVRWSG 419
Cdd:PTZ00302 476 VELALAFLGLSFQDWLNLYTDL-PSRQDKVTVKDRTlitnTEDE----TRLLEpkgLQDKidaivsKYDNAARAFIRPSG 550
|
490 500 510
....*....|....*....|....*....|
gi 931474921 420 TEPKLRVMIEGPRLEKIQTMADDIAAAAQK 449
Cdd:PTZ00302 551 TEPVVRVYAEAPTLEQADELANEVKGLVLR 580
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
46-250 |
1.43e-11 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 66.25 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 46 IVVGKDTRLSGYLFETAVASGICALGGEVLLTGPL-PTPAIAHLATSMRADAGVVISASHNPYQDNGIKIFGPDGFKLPD 124
Cdd:PTZ00150 92 VVIGYDGRYHSRRFAEITASVFLSKGFKVYLFGQTvPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVYWSNGAQIIP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 125 EMEIEI-----ENLIFGSELDTD-RPTGTRVGRAERQDDapgrYVAFVKASF-PNDLTLEGVKIVVDAAHGAAYRTAPLV 197
Cdd:PTZ00150 172 PHDKNIsakilSNLEPWSSSWEYlTETLVEDPLAEVSDA----YFATLKSEYnPACCDRSKVKIVYTAMHGVGTRFVQKA 247
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931474921 198 FSELG------------------AVTYPigvrpngkNINHKVGALhpeACAREVQKRH-ADLGIALDGDADR 250
Cdd:PTZ00150 248 LHTVGlpnllsvaqqaepdpefpTVTFP--------NPEEGKGAL---KLSMETAEAHgSTVVLANDPDADR 308
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
97-444 |
3.29e-11 |
|
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: 65.31 E-value: 3.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 97 GVVISASHNPYQDNGIKIFGPDGFKLP---------------DEMEIEIENLIFGSEL--------------DTdRPTG- 146
Cdd:cd03086 38 GVMITASHNPVEDNGVKIVDPDGEMLEeswepyatqlanasdDELLVLVLMLISVKELnidlsvpanvfvgrDT-RPSGp 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 147 -----------------------------------TRVGRAERQDDApgRYVAFVKASF------PNDLTLEGVKIVVDA 185
Cdd:cd03086 117 allqalldglkalggnvidyglvttpqlhylvraaNTEGAYGEPTEE--GYYEKLSKAFnelynlLQDGGDEPEKLVVDC 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 186 AHG-AAYRTAPlvFSELGAVTYPIGVRPNGK----NINHKVGA----------LHPEACAREVqkRHAdlgiALDGDADR 250
Cdd:cd03086 195 ANGvGALKLKE--LLKRLKKGLSVKIINDGEegpeLLNDGCGAdyvktkqkppRGFELKPPGV--RCC----SFDGDADR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 251 II--MIDEKGQ--EVDGDVI---MALCATRMLRAKRLRQR---TLVATVMSNLGLERAIEndngKLLRCNV-----GDRY 315
Cdd:cd03086 267 LVyfYPDSSNKfhLLDGDKIatlFAKFIKELLKKAGEELKltiGVVQTAYANGASTKYLE----DVLKVPVvctptGVKH 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 316 VVETMRNR--GLNFggEQSGH--LIFLDHA------------------------------TTGDGLVAAMQVLAILCREQ 361
Cdd:cd03086 343 LHHAAEEFdiGVYF--EANGHgtVLFSESAlakieensslsdeqekaaktllafsrlinqTVGDAISDMLAVELILAALG 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 362 RPLSELAAQVMDrVPQVLVNVSLPERRpldeLPKT----RRAI----------ALAEKTlgKDGRVLVRWSGTEPKLRVM 427
Cdd:cd03086 421 WSPQDWDNLYTD-LPNRQLKVKVPDRS----VIKTtdaeRRLVepkglqdkidAIVAKY--NNGRAFVRPSGTEDVVRVY 493
|
490
....*....|....*..
gi 931474921 428 IEGPRLEKIQTMADDIA 444
Cdd:cd03086 494 AEAATQEEADELANEVA 510
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
6-375 |
2.22e-10 |
|
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: 62.65 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 6 FGTDGIRGLANRGEMSPEVAFRIGAAIAyQARKRTKHVPHIVVGKDTR-LSGYLFETA----VASGIcalggEVLLT--- 77
Cdd:cd05801 23 FGTSGHRGSSLKGSFNEAHILAISQAIC-DYRKSQGITGPLFLGKDTHaLSEPAFISAlevlAANGV-----EVIIQqnd 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 78 GPLPTPAIAHL-------ATSMRADaGVVISASHNPYQDNGIKIFGPDGFklPDEMEI-----EIENLIFGSEL-DTDRP 144
Cdd:cd05801 97 GYTPTPVISHAiltynrgRTEGLAD-GIVITPSHNPPEDGGFKYNPPHGG--PADTDItrwieKRANALLANGLkGVKRI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 145 TGTRV---GRAERQDdapgrYVAFVKASFPNDLTLE-----GVKIVVDAAHGAayrtaplvfselgAVTY--PIGVRPnG 214
Cdd:cd05801 174 PLEAAlasGYTHRHD-----FVTPYVADLGNVIDMDairksGLRLGVDPLGGA-------------SVPYwqPIAEKY-G 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 215 KNI---NHKV------------GALH-----PEACAREVQ-KRHADLGIALDGDADRIIMIDEKGQEVDGD-----VIMA 268
Cdd:cd05801 235 LNLtvvNPKVdptfrfmtldhdGKIRmdcssPYAMAGLLKlKDKFDLAFANDPDADRHGIVTPSAGLMNPNhylsvAIDY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 269 LCATRMLRAKRLR-QRTLVATVMsnlgLERAIENDNGKLLRCNVGDRYVVETMRNRGLNFGGEQSGHLIFLDHA----TT 343
Cdd:cd05801 315 LFTHRPLWNKSAGvGKTLVSSSM----IDRVAAALGRKLYEVPVGFKWFVDGLLDGSLGFGGEESAGASFLRRDgtvwTT 390
|
410 420 430
....*....|....*....|....*....|...
gi 931474921 344 G-DGLVAAMQVLAILCREQRPLSELAAQVMDRV 375
Cdd:cd05801 391 DkDGIIMCLLAAEILAVTGKDPGQLYQELTERF 423
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
45-261 |
1.50e-07 |
|
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: 53.76 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 45 HIVVGKDTRLsgYLFET-------AVASGIcalgGEVLL--TGPLPTPAIAHLATSMRADAGVVISASHNP---YQDNGI 112
Cdd:cd03085 51 TLVVGGDGRY--YNKEAiqiiikiAAANGV----GKVVVgqNGLLSTPAVSAVIRKRKATGGIILTASHNPggpEGDFGI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 113 KiF-----GPDGFKLPDEM-----EIEIENLIFGSELDTDRPTGTRVGRAERQ---DDAPGRYVAFVKASFPND-----L 174
Cdd:cd03085 125 K-YntsngGPAPESVTDKIyeitkKITEYKIADDPDVDLSKIGVTKFGGKPFTvevIDSVEDYVELMKEIFDFDaikklL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 175 TLEGVKIVVDAAHGAAYRTAPLVF-SELGAvtypigvrPNGKNINHKV----GALHP-------EACAREVQKRHADLGI 242
Cdd:cd03085 204 SRKGFKVRFDAMHGVTGPYAKKIFvEELGA--------PESSVVNCTPlpdfGGGHPdpnltyaKDLVELMKSGEPDFGA 275
|
250
....*....|....*....
gi 931474921 243 ALDGDADRiIMIDEKGQEV 261
Cdd:cd03085 276 ASDGDGDR-NMILGKGFFV 293
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
97-274 |
6.04e-07 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 51.56 E-value: 6.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 97 GVVISASHNPYQDNGIKIFGPDGFKLPDEME----------------------IEIENLIFGSEL---------DTdRPT 145
Cdd:PLN02895 61 GLMITASHNPVSDNGVKIVDPSGGMLPQAWEpfadalanapdpdalvqlirefVKKENIPAVGGNppaevllgrDT-RPS 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 146 GTRVGRAERQ-------------------------------DDAPGRYVAFVKASF-------PND--LTLEGVKIVVDA 185
Cdd:PLN02895 140 GPALLAAALKgvraigaravdmgilttpqlhwmvraankgmKATESDYFEQLSSSFralldliPNGsgDDRADDKLVVDG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931474921 186 AHGAAYRTAPLVFSELGAVtyPIGVRPNGKN----INHKVGALHpeacareVQKRH--------ADLGI---ALDGDADR 250
Cdd:PLN02895 220 ANGVGAEKLETLKKALGGL--DLEVRNSGKEgegvLNEGVGADF-------VQKEKvpptgfasKDVGLrcaSLDGDADR 290
|
250 260
....*....|....*....|....*....
gi 931474921 251 IIMIDEKGQE-----VDGDVIMALCATRM 274
Cdd:PLN02895 291 LVYFYVSSAGskidlLDGDKIASLFALFI 319
|
|
| |
