|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
22-618 |
0e+00 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 744.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 22 LDKAVSQWMTWDKNPLTREQIESLVQEGRVVELRRRLCSRMTFGTAGLRAAMGAGFARINDLTIIQSTQGLYKYLAKCF- 100
Cdd:PTZ00150 5 LEAQVELWLKWDKDPETRKEIEELLASKDEEELKRRFLKRMEFGTAGLRGKMGAGFNCMNDLTVQQTAQGLCAYVIETFg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 101 PDLKTRGLVVGYDTRAQassgctSERLAKLTAAVMLCKDVPVYLFSTYVPTPFVPYAVMKYGAAAGVMITASHNRKEDNG 180
Cdd:PTZ00150 85 QALKSRGVVIGYDGRYH------SRRFAEITASVFLSKGFKVYLFGQTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 181 YKVYWHNGAQIASPHDKEILHCIEESAEPWAESW---NEDLVEnsllkrDPLEDVCHWYM----EELNTLCFHRelnakS 253
Cdd:PTZ00150 159 YKVYWSNGAQIIPPHDKNISAKILSNLEPWSSSWeylTETLVE------DPLAEVSDAYFatlkSEYNPACCDR-----S 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 254 PLKFVHSSFHGVGHNYVQRAFQQFGFPPPIPVPEQKDPDPDFSTVSCPNPEEGESVLELSLRLAEREKARIVVATDPDAD 333
Cdd:PTZ00150 228 KVKIVYTAMHGVGTRFVQKALHTVGLPNLLSVAQQAEPDPEFPTVTFPNPEEGKGALKLSMETAEAHGSTVVLANDPDAD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 334 RLAVAEQNDNcGWKVFTGNELAALLGWWMlfnWKEAHPDPADTERVYMLATTVSSKILEAFARIEGFHFEETLPGFKWIG 413
Cdd:PTZ00150 308 RLAVAEKLNN-GWKIFTGNELGALLAWWA---MKRYRRQGIDKSKCFFICTVVSSRMLKKMAEKEGFQYDETLTGFKWIG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 414 NRIHELKKA-GKEVIFSFEESIGFLCGNMVLDKDGVSTAAVVAEMASYLHTKNLSLNQQLCNIYEIYGYHISRTSYVLCN 492
Cdd:PTZ00150 384 NKAIELNAEnGLTTLFAYEEAIGFMLGTRVRDKDGVTAAAVVAEMALYLYERGKTLVEHLESLYKQYGYHFTNNSYYICY 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 493 DPPTIHRIFSRLRNfggQGVYPTSCGDYCITHIRDVTTGYDSSQPDKKCVLPLSKSSQMLTFTFQNGIVATLRTSGTEPK 572
Cdd:PTZ00150 464 DPSRIVSIFNDIRN---NGSYPTKLGGYPVTRIRDLTTGYDTATPDGKPLLPVSASTQMITFYFENGAIITIRGSGTEPK 540
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 148596920 573 IKYYTEFCASpgerDISSLDEELRKVAAALVEEFLEPDKNDLLGRS 618
Cdd:PTZ00150 541 LKWYAELSGT----KDEAVEKELAALVDEVVEQLMQPEKYGLVPRK 582
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
61-600 |
0e+00 |
|
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The mammalian PGM2 is thought to be a phosphopentomutase that catalyzes the conversion of the nucleoside breakdown products, ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. PGM2L1 is thought to catalyze the 1,3-bisphosphoglycerate-dependent synthesis of glucose 1,6-bisphosphate and other aldose-bisphosphates that serve as cofactors for several sugar phosphomutases and possibly also as regulators of glycolytic enzymes. PGM2 and PGM2L1 belong to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100092 Cd Length: 487 Bit Score: 656.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 61 RMTFGTAGLRAAMGAGFARINDLTIIQSTQGLYKYLAKCFPDLKTRGLVVGYDTRAQassgctSERLAKLTAAVMLCKDV 140
Cdd:cd05799 1 RLEFGTAGLRGKMGAGTNRMNDYTVRQATQGLANYLKKKGPDAKNRGVVIGYDSRHN------SREFAELTAAVLAANGI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 141 PVYLFSTYVPTPFVPYAVMKYGAAAGVMITASHNRKEDNGYKVYWHNGAQIASPHDKEILHCIEESAEPWaESWNEDLVE 220
Cdd:cd05799 75 KVYLFDDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAVLEPL-DIKFEEALD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 221 NSLLKrDPLEDVCHWYMEELNTLCFHRELNAKSPLKFVHSSFHGVGHNYVQRAFQQFGFPPPIPVPEQKDPDPDFSTVSC 300
Cdd:cd05799 154 SGLIK-YIGEEIDDAYLEAVKKLLVNPELNEGKDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVVEEQAEPDPDFPTVKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 301 PNPEEgESVLELSLRLAEREKARIVVATDPDADRLAVAEQNDNCGWKVFTGNELAALLGWWMLFNWKEAHPDPadtERVY 380
Cdd:cd05799 233 PNPEE-PGALDLAIELAKKVGADLILATDPDADRLGVAVKDKDGEWRLLTGNEIGALLADYLLEQRKEKGKLP---KNPV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 381 MLATTVSSKILEAFARIEGFHFEETLPGFKWIGNRIHELKKAGKEVIFSFEESIGFLCGNMVLDKDGVSTAAVVAEMASY 460
Cdd:cd05799 309 IVKTIVSSELLRKIAKKYGVKVEETLTGFKWIGNKIEELESGGKKFLFGFEESIGYLVGPFVRDKDGISAAALLAEMAAY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 461 LHTKNLSLNQQLCNIYEIYGYHISRTSYVLC---NDPPTIHRIFSRLRNFGgqgvyptscgdycithirdvttgydssqp 537
Cdd:cd05799 389 LKAQGKTLLDRLDELYEKYGYYKEKTISITFegkEGPEKIKAIMDRLRNNP----------------------------- 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148596920 538 dkkcvlplskssQMLTFTFQNGIVATLRTSGTEPKIKYYTEFCaspGERDISSLDEELRKVAA 600
Cdd:cd05799 440 ------------NVLTFYLEDGSRVTVRPSGTEPKIKFYIEVV---GKKTLEEAEKKLDALKK 487
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
60-607 |
6.11e-86 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 275.54 E-value: 6.11e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 60 SRMTFGTAGLRAAMGAGfarINDLTIIQSTQGLYKYLAKCfpdlKTRGLVVGYDTRAqassgcTSERLAKLTAAVMLCKD 139
Cdd:COG1109 3 YKKLFGTDGIRGIVGEE---LTPEFVLKLGRAFGTYLKEK----GGPKVVVGRDTRL------SSPMLARALAAGLASAG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 140 VPVYLFsTYVPTPFVPYAVMKYGAAAGVMITASHNRKEDNGYKVYWHNGAQIASPHDKEILHCIEESAEPWAESwnedlV 219
Cdd:COG1109 70 IDVYDL-GLVPTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKEDFRRAEA-----E 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 220 ENSLLKRdpLEDVCHWYMEELNTLCfhRELNAKSPLKFVHSSFHGVGHNYVQRAFQQFGFpPPIPVPEQkdPDPDFSTVS 299
Cdd:COG1109 144 EIGKVTR--IEDVLEAYIEALKSLV--DEALRLRGLKVVVDCGNGAAGGVAPRLLRELGA-EVIVLNAE--PDGNFPNHN 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 300 cPNPEEGesVLELSLRLAEREKARIVVATDPDADRLAVAeqnDNCGwKVFTGNELAALLGWWMLfnwkEAHPDPAdterv 379
Cdd:COG1109 217 -PNPEPE--NLEDLIEAVKETGADLGIAFDGDADRLGVV---DEKG-RFLDGDQLLALLARYLL----EKGPGGT----- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 380 yMLATTVSSKILEAFARIEGFHFEETLPGFKWIGNRIHELKkagkeVIFSFEESIGFLCGNMVLDKDGVSTAAVVAEMAS 459
Cdd:COG1109 281 -VVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKMRETG-----AVLGGEESGGIIFPDFVPTDDGILAALLLLELLA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 460 YlhtKNLSLNQqlcnIYEIYGYHISRTSYVLCNDPPTIHRIFSRLRNFggqgvyptscgdycITHIRDVTTgydssqpdk 539
Cdd:COG1109 355 K---QGKSLSE----LLAELPRYPQPEINVRVPDEEKIGAVMEKLREA--------------VEDKEELDT--------- 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148596920 540 kcvlplsksSQMLTFTFQNGIVATLRTSGTEPKIKYYTEfcaSPGERDIssldEELRKVAAALVEEFL 607
Cdd:COG1109 405 ---------IDGVKVDLEDGGWVLVRPSGTEPLLRVYAE---AKDEEEA----EELLAELAELVEEAL 456
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
61-210 |
1.09e-37 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 136.20 E-value: 1.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 61 RMTFGTAGLRAAMGAGFarINDLTIIQSTQGLYKYLAKcfpDLKTRGLVVGYDTRAqassgcTSERLAKLTAAVMLCKDV 140
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGE--LTPEFALKLGQAIASYLRA---QGGGGKVVVGRDTRY------SSRELARALAAGLASNGV 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 141 PVYLFStYVPTPFVPYAVMKYGAAAGVMITASHNRKEDNGYKVYWHNGAQIASPHDKEILHCIEESAEPW 210
Cdd:pfam02878 70 EVILLG-LLPTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKEDFYR 138
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
109-578 |
9.71e-28 |
|
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: 116.46 E-value: 9.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 109 VVGYDTRAqassgcTSERLAKLTAAVMLCKDVPVYLFStYVPTPFVPYAVMKYGAAAGVMITASHNRKEDNGYKVYWHNG 188
Cdd:TIGR03990 39 VVGRDTRT------SGPMLENAVIAGLLSTGCDVVDLG-IAPTPTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 189 AQIASPHDKEILHCIEESAEPWAeSWNE--DLVENsllkRDPLEDvchwYMEE-LNTLCfhRELNAKSPLKFVHSSFHGV 265
Cdd:TIGR03990 112 TELSREQEEEIEEIAESGDFERA-DWDEigTVTSD----EDAIDD----YIEAiLDKVD--VEAIRKKGFKVVVDCGNGA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 266 GHNYVQRAFQQFGFpPPIPVPEQkdPDPDFSTvscPNPEEGESVLELSLRLAEREKARIVVATDPDADRLAVAEQNDNcg 345
Cdd:TIGR03990 181 GSLTTPYLLRELGC-KVITLNCQ--PDGTFPG---RNPEPTPENLKDLSALVKATGADLGIAHDGDADRLVFIDEKGR-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 346 wkVFTGNELAALLGWWMLfnwkEAHPDPadtervymLATTVS-SKILEAFARIEGFHFEETLpgfkwIG--NRIHELKKA 422
Cdd:TIGR03990 253 --FIGGDYTLALFAKYLL----EHGGGK--------VVTNVSsSRAVEDVAERHGGEVIRTK-----VGevNVAEKMKEE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 423 GkeVIFSFEESIGFLCGNMVLDKDGVSTAAVVAEMasyLHTKNLSLNQQlcnIYEIYGYHISRTSYVLCNDPPtiHRIFS 502
Cdd:TIGR03990 314 G--AVFGGEGNGGWIFPDHHYCRDGLMAAALFLEL---LAEEGKPLSEL---LAELPKYPMSKEKVELPDEDK--EEVME 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148596920 503 RLRnfggqgvypTSCGDYCITHIRDVTTGYDSSQpdkkcVLplskssqmltftfqngivatLRTSGTEPKIKYYTE 578
Cdd:TIGR03990 384 AVE---------EEFADAEIDTIDGVRIDFEDGW-----VL--------------------VRPSGTEPIVRIYAE 425
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
22-618 |
0e+00 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 744.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 22 LDKAVSQWMTWDKNPLTREQIESLVQEGRVVELRRRLCSRMTFGTAGLRAAMGAGFARINDLTIIQSTQGLYKYLAKCF- 100
Cdd:PTZ00150 5 LEAQVELWLKWDKDPETRKEIEELLASKDEEELKRRFLKRMEFGTAGLRGKMGAGFNCMNDLTVQQTAQGLCAYVIETFg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 101 PDLKTRGLVVGYDTRAQassgctSERLAKLTAAVMLCKDVPVYLFSTYVPTPFVPYAVMKYGAAAGVMITASHNRKEDNG 180
Cdd:PTZ00150 85 QALKSRGVVIGYDGRYH------SRRFAEITASVFLSKGFKVYLFGQTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 181 YKVYWHNGAQIASPHDKEILHCIEESAEPWAESW---NEDLVEnsllkrDPLEDVCHWYM----EELNTLCFHRelnakS 253
Cdd:PTZ00150 159 YKVYWSNGAQIIPPHDKNISAKILSNLEPWSSSWeylTETLVE------DPLAEVSDAYFatlkSEYNPACCDR-----S 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 254 PLKFVHSSFHGVGHNYVQRAFQQFGFPPPIPVPEQKDPDPDFSTVSCPNPEEGESVLELSLRLAEREKARIVVATDPDAD 333
Cdd:PTZ00150 228 KVKIVYTAMHGVGTRFVQKALHTVGLPNLLSVAQQAEPDPEFPTVTFPNPEEGKGALKLSMETAEAHGSTVVLANDPDAD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 334 RLAVAEQNDNcGWKVFTGNELAALLGWWMlfnWKEAHPDPADTERVYMLATTVSSKILEAFARIEGFHFEETLPGFKWIG 413
Cdd:PTZ00150 308 RLAVAEKLNN-GWKIFTGNELGALLAWWA---MKRYRRQGIDKSKCFFICTVVSSRMLKKMAEKEGFQYDETLTGFKWIG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 414 NRIHELKKA-GKEVIFSFEESIGFLCGNMVLDKDGVSTAAVVAEMASYLHTKNLSLNQQLCNIYEIYGYHISRTSYVLCN 492
Cdd:PTZ00150 384 NKAIELNAEnGLTTLFAYEEAIGFMLGTRVRDKDGVTAAAVVAEMALYLYERGKTLVEHLESLYKQYGYHFTNNSYYICY 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 493 DPPTIHRIFSRLRNfggQGVYPTSCGDYCITHIRDVTTGYDSSQPDKKCVLPLSKSSQMLTFTFQNGIVATLRTSGTEPK 572
Cdd:PTZ00150 464 DPSRIVSIFNDIRN---NGSYPTKLGGYPVTRIRDLTTGYDTATPDGKPLLPVSASTQMITFYFENGAIITIRGSGTEPK 540
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 148596920 573 IKYYTEFCASpgerDISSLDEELRKVAAALVEEFLEPDKNDLLGRS 618
Cdd:PTZ00150 541 LKWYAELSGT----KDEAVEKELAALVDEVVEQLMQPEKYGLVPRK 582
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
61-600 |
0e+00 |
|
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The mammalian PGM2 is thought to be a phosphopentomutase that catalyzes the conversion of the nucleoside breakdown products, ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. PGM2L1 is thought to catalyze the 1,3-bisphosphoglycerate-dependent synthesis of glucose 1,6-bisphosphate and other aldose-bisphosphates that serve as cofactors for several sugar phosphomutases and possibly also as regulators of glycolytic enzymes. PGM2 and PGM2L1 belong to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100092 Cd Length: 487 Bit Score: 656.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 61 RMTFGTAGLRAAMGAGFARINDLTIIQSTQGLYKYLAKCFPDLKTRGLVVGYDTRAQassgctSERLAKLTAAVMLCKDV 140
Cdd:cd05799 1 RLEFGTAGLRGKMGAGTNRMNDYTVRQATQGLANYLKKKGPDAKNRGVVIGYDSRHN------SREFAELTAAVLAANGI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 141 PVYLFSTYVPTPFVPYAVMKYGAAAGVMITASHNRKEDNGYKVYWHNGAQIASPHDKEILHCIEESAEPWaESWNEDLVE 220
Cdd:cd05799 75 KVYLFDDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAVLEPL-DIKFEEALD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 221 NSLLKrDPLEDVCHWYMEELNTLCFHRELNAKSPLKFVHSSFHGVGHNYVQRAFQQFGFPPPIPVPEQKDPDPDFSTVSC 300
Cdd:cd05799 154 SGLIK-YIGEEIDDAYLEAVKKLLVNPELNEGKDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVVEEQAEPDPDFPTVKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 301 PNPEEgESVLELSLRLAEREKARIVVATDPDADRLAVAEQNDNCGWKVFTGNELAALLGWWMLFNWKEAHPDPadtERVY 380
Cdd:cd05799 233 PNPEE-PGALDLAIELAKKVGADLILATDPDADRLGVAVKDKDGEWRLLTGNEIGALLADYLLEQRKEKGKLP---KNPV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 381 MLATTVSSKILEAFARIEGFHFEETLPGFKWIGNRIHELKKAGKEVIFSFEESIGFLCGNMVLDKDGVSTAAVVAEMASY 460
Cdd:cd05799 309 IVKTIVSSELLRKIAKKYGVKVEETLTGFKWIGNKIEELESGGKKFLFGFEESIGYLVGPFVRDKDGISAAALLAEMAAY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 461 LHTKNLSLNQQLCNIYEIYGYHISRTSYVLC---NDPPTIHRIFSRLRNFGgqgvyptscgdycithirdvttgydssqp 537
Cdd:cd05799 389 LKAQGKTLLDRLDELYEKYGYYKEKTISITFegkEGPEKIKAIMDRLRNNP----------------------------- 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148596920 538 dkkcvlplskssQMLTFTFQNGIVATLRTSGTEPKIKYYTEFCaspGERDISSLDEELRKVAA 600
Cdd:cd05799 440 ------------NVLTFYLEDGSRVTVRPSGTEPKIKFYIEVV---GKKTLEEAEKKLDALKK 487
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
60-607 |
6.11e-86 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 275.54 E-value: 6.11e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 60 SRMTFGTAGLRAAMGAGfarINDLTIIQSTQGLYKYLAKCfpdlKTRGLVVGYDTRAqassgcTSERLAKLTAAVMLCKD 139
Cdd:COG1109 3 YKKLFGTDGIRGIVGEE---LTPEFVLKLGRAFGTYLKEK----GGPKVVVGRDTRL------SSPMLARALAAGLASAG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 140 VPVYLFsTYVPTPFVPYAVMKYGAAAGVMITASHNRKEDNGYKVYWHNGAQIASPHDKEILHCIEESAEPWAESwnedlV 219
Cdd:COG1109 70 IDVYDL-GLVPTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKEDFRRAEA-----E 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 220 ENSLLKRdpLEDVCHWYMEELNTLCfhRELNAKSPLKFVHSSFHGVGHNYVQRAFQQFGFpPPIPVPEQkdPDPDFSTVS 299
Cdd:COG1109 144 EIGKVTR--IEDVLEAYIEALKSLV--DEALRLRGLKVVVDCGNGAAGGVAPRLLRELGA-EVIVLNAE--PDGNFPNHN 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 300 cPNPEEGesVLELSLRLAEREKARIVVATDPDADRLAVAeqnDNCGwKVFTGNELAALLGWWMLfnwkEAHPDPAdterv 379
Cdd:COG1109 217 -PNPEPE--NLEDLIEAVKETGADLGIAFDGDADRLGVV---DEKG-RFLDGDQLLALLARYLL----EKGPGGT----- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 380 yMLATTVSSKILEAFARIEGFHFEETLPGFKWIGNRIHELKkagkeVIFSFEESIGFLCGNMVLDKDGVSTAAVVAEMAS 459
Cdd:COG1109 281 -VVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKMRETG-----AVLGGEESGGIIFPDFVPTDDGILAALLLLELLA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 460 YlhtKNLSLNQqlcnIYEIYGYHISRTSYVLCNDPPTIHRIFSRLRNFggqgvyptscgdycITHIRDVTTgydssqpdk 539
Cdd:COG1109 355 K---QGKSLSE----LLAELPRYPQPEINVRVPDEEKIGAVMEKLREA--------------VEDKEELDT--------- 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148596920 540 kcvlplsksSQMLTFTFQNGIVATLRTSGTEPKIKYYTEfcaSPGERDIssldEELRKVAAALVEEFL 607
Cdd:COG1109 405 ---------IDGVKVDLEDGGWVLVRPSGTEPLLRVYAE---AKDEEEA----EELLAELAELVEEAL 456
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
153-490 |
4.34e-71 |
|
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: 233.40 E-value: 4.34e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 153 FVPYAVMKYGAAA----GVMITASHNRKEDNGYKVYWHNGAQIASPHDKEILHCIEESAEPWAESWNEDLVEnsllKRDP 228
Cdd:cd03084 15 ITPETAVALGQAIgstgGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSAVAYELGGSV----KAVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 229 LEDVchwYMEELNTLCFHRELNaKSPLKFVHSSFHGVGHNYVQRAFQQFGFPppiPVPEQKDPDPDFSTVScPNPEEGES 308
Cdd:cd03084 91 ILQR---YFEALKKLFDVAALS-NKKFKVVVDSVNGVGGPIAPQLLEKLGAE---VIPLNCEPDGNFGNIN-PDPGSETN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 309 VLELSLRLaEREKARIVVATDPDADRLAVAEQNdncgWKVFTGNELAALLGWWMLFNWKeahpdpadtERVYMLATTVSS 388
Cdd:cd03084 163 LKQLLAVV-KAEKADFGVAFDGDADRLIVVDEN----GGFLDGDELLALLAVELFLTFN---------PRGGVVKTVVSS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 389 KILEAFARIEGFHFEETLPGFKWIGNRIHElkkagKEVIFSFEESIGFLCGNMVLDKDGVSTAAVVAEMASYLHtknLSL 468
Cdd:cd03084 229 GALDKVAKKLGIKVIRTKTGFKWVGEAMQE-----GDVVLGGEESGGVIFPEFHPGRDGISAALLLLEILANLG---KSL 300
|
330 340
....*....|....*....|..
gi 148596920 469 NQQLCNIYEIYGYHISRTSYVL 490
Cdd:cd03084 301 SELFSELPRYYYIRLKVRGWVL 322
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
62-578 |
1.57e-59 |
|
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: 205.86 E-value: 1.57e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 62 MTFGTAGLRAAMGAGFARINdLTIIqsTQGLYKYLAKCFPDlkTRGLVVGYDTRAqassgcTSERLAKLTAAVMLCKDVP 141
Cdd:cd05800 1 IKFGTDGWRGIIAEDFTFEN-VRRV--AQAIADYLKEEGGG--GRGVVVGYDTRF------LSEEFARAVAEVLAANGID 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 142 VYLFSTYVPTPFVPYAVMKYGAAAGVMITASHNRKEDNGYKVYWHNGAqiasPHDKEILHCIEESAEPWAESWNEDLVEN 221
Cdd:cd05800 70 VYLSDRPVPTPAVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGG----SALPEITAAIEARLASGEPPGLEARAEG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 222 SLLKRDPLEDvchwYMEELNTLcFHRELNAKSPLKFVHSSFHGVGHNYVQRAFQQFGfpppIPVPE-QKDPDPDFSTVsC 300
Cdd:cd05800 146 LIETIDPKPD----YLEALRSL-VDLEAIREAGLKVVVDPMYGAGAGYLEELLRGAG----VDVEEiRAERDPLFGGI-P 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 301 PNPEEGesVLELSLRLAEREKARIVVATDPDADRLAVAEQNDNCgwkvFTGNELAALLGWWMLFN--WKEAhpdpadter 378
Cdd:cd05800 216 PEPIEK--NLGELAEAVKEGGADLGLATDGDADRIGAVDEKGNF----LDPNQILALLLDYLLENkgLRGP--------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 379 vymLATTVS-SKILEAFARIEGFHFEETLPGFKWIGNRIHElkkagKEVIFSFEESIGFLCGNMVLDKDGVSTAAVVAEM 457
Cdd:cd05800 281 ---VVKTVStTHLIDRIAEKHGLPVYETPVGFKYIAEKMLE-----EDVLIGGEESGGLGIRGHIPERDGILAGLLLLEA 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 458 ASYlhtKNLSLNQQLCNIYEIYGYHIS-RTSYVLcnDPPTIHRIFSRLRNFggqgvYPTSCGDYCITHIRDVtTGYdssq 536
Cdd:cd05800 353 VAK---TGKPLSELVAELEEEYGPSYYdRIDLRL--TPAQKEAILEKLKNE-----PPLSIAGGKVDEVNTI-DGV---- 417
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 148596920 537 pdKkcvlplskssqmltFTFQNGIVATLRTSGTEPKIKYYTE 578
Cdd:cd05800 418 --K--------------LVLEDGSWLLIRPSGTEPLLRIYAE 443
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
61-210 |
1.09e-37 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 136.20 E-value: 1.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 61 RMTFGTAGLRAAMGAGFarINDLTIIQSTQGLYKYLAKcfpDLKTRGLVVGYDTRAqassgcTSERLAKLTAAVMLCKDV 140
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGE--LTPEFALKLGQAIASYLRA---QGGGGKVVVGRDTRY------SSRELARALAAGLASNGV 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 141 PVYLFStYVPTPFVPYAVMKYGAAAGVMITASHNRKEDNGYKVYWHNGAQIASPHDKEILHCIEESAEPW 210
Cdd:pfam02878 70 EVILLG-LLPTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKEDFYR 138
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
109-578 |
9.71e-28 |
|
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: 116.46 E-value: 9.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 109 VVGYDTRAqassgcTSERLAKLTAAVMLCKDVPVYLFStYVPTPFVPYAVMKYGAAAGVMITASHNRKEDNGYKVYWHNG 188
Cdd:TIGR03990 39 VVGRDTRT------SGPMLENAVIAGLLSTGCDVVDLG-IAPTPTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 189 AQIASPHDKEILHCIEESAEPWAeSWNE--DLVENsllkRDPLEDvchwYMEE-LNTLCfhRELNAKSPLKFVHSSFHGV 265
Cdd:TIGR03990 112 TELSREQEEEIEEIAESGDFERA-DWDEigTVTSD----EDAIDD----YIEAiLDKVD--VEAIRKKGFKVVVDCGNGA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 266 GHNYVQRAFQQFGFpPPIPVPEQkdPDPDFSTvscPNPEEGESVLELSLRLAEREKARIVVATDPDADRLAVAEQNDNcg 345
Cdd:TIGR03990 181 GSLTTPYLLRELGC-KVITLNCQ--PDGTFPG---RNPEPTPENLKDLSALVKATGADLGIAHDGDADRLVFIDEKGR-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 346 wkVFTGNELAALLGWWMLfnwkEAHPDPadtervymLATTVS-SKILEAFARIEGFHFEETLpgfkwIG--NRIHELKKA 422
Cdd:TIGR03990 253 --FIGGDYTLALFAKYLL----EHGGGK--------VVTNVSsSRAVEDVAERHGGEVIRTK-----VGevNVAEKMKEE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 423 GkeVIFSFEESIGFLCGNMVLDKDGVSTAAVVAEMasyLHTKNLSLNQQlcnIYEIYGYHISRTSYVLCNDPPtiHRIFS 502
Cdd:TIGR03990 314 G--AVFGGEGNGGWIFPDHHYCRDGLMAAALFLEL---LAEEGKPLSEL---LAELPKYPMSKEKVELPDEDK--EEVME 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148596920 503 RLRnfggqgvypTSCGDYCITHIRDVTTGYDSSQpdkkcVLplskssqmltftfqngivatLRTSGTEPKIKYYTE 578
Cdd:TIGR03990 384 AVE---------EEFADAEIDTIDGVRIDFEDGW-----VL--------------------VRPSGTEPIVRIYAE 425
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
236-345 |
6.05e-27 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 105.07 E-value: 6.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 236 YMEELNTLCFhRELNAKSPLKFVHSSFHGVGHNYVQRAFQQFGFpppIPVPEQKDPDPDFSTVScPNPEEGEsVLELSLR 315
Cdd:pfam02879 2 YIDHLLELVD-SEALKKRGLKVVYDPLHGVGGGYLPELLKRLGC---DVVEENCEPDPDFPTRA-PNPEEPE-ALALLIE 75
|
90 100 110
....*....|....*....|....*....|
gi 148596920 316 LAEREKARIVVATDPDADRLAVAeqnDNCG 345
Cdd:pfam02879 76 LVKSVGADLGIATDGDADRLGVV---DERG 102
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
109-488 |
4.11e-25 |
|
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: 108.43 E-value: 4.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 109 VVGYDTRAqassgcTSERLAKLTAAVMLCKDVPVYLFSTyVPTPFVPYAVMKYGAAaGVMITASHNRKEDNGYKVYWHNG 188
Cdd:cd03087 37 VVGRDTRT------SGPMLKNAVIAGLLSAGCDVIDIGI-VPTPALQYAVRKLGDA-GVMITASHNPPEYNGIKLVNPDG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 189 AQIASPHDKEILHCIEESAEPWAeSWNE--DLVENSLLKRDpledvchwYMEELNTlcfHRELNAKSPLKFVHSSFHGVG 266
Cdd:cd03087 109 TEFSREQEEEIEEIIFSERFRRV-AWDEvgSVRREDSAIDE--------YIEAILD---KVDIDGGKGLKVVVDCGNGAG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 267 HNYVQRAFQQFGFpPPIPVPEQkdPDPDFSTvscPNPEEGESVLELSLRLAEREKARIVVATDPDADRLAVAeqnDNCGw 346
Cdd:cd03087 177 SLTTPYLLRELGC-KVITLNAN--PDGFFPG---RPPEPTPENLSELMELVRATGADLGIAHDGDADRAVFV---DEKG- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 347 KVFTGNELAALLGWWMLfnwkEAHPDpadteRVYmlaTTVS-SKILEAFARIEGFHFEETLPGFKWIGNRIhelkkAGKE 425
Cdd:cd03087 247 RFIDGDKLLALLAKYLL----EEGGG-----KVV---TPVDaSMLVEDVVEEAGGEVIRTPVGDVHVAEEM-----IENG 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148596920 426 VIFSFEESIGFLCGNMVLDKDGVSTAAVVAEMASylHTKNLSlnqQLcnIYEIYGYHISRTSY 488
Cdd:cd03087 310 AVFGGEPNGGWIFPDHQLCRDGIMTAALLLELLA--EEKPLS---EL--LDELPKYPLLREKV 365
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
94-358 |
3.42e-19 |
|
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: 90.65 E-value: 3.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 94 KYLAKCFPDLKTRGLVVGYDTRAqassgcTSERLAKLTAAVMLCKDVPVYLFSTyVPTPFVPYAVMKYGAAAGVMITASH 173
Cdd:cd03089 25 RAFGSWLLEKGAKKVVVGRDGRL------SSPELAAALIEGLLAAGCDVIDIGL-VPTPVLYFATFHLDADGGVMITASH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 174 NRKEDNGYKVYWHNGAqiASPHD-KEILHCIEESAEPWAESwnedlvENSLLKRDPLEDvchwYMEELNTLCFHrelnAK 252
Cdd:cd03089 98 NPPEYNGFKIVIGGGP--LSGEDiQALRERAEKGDFAAATG------RGSVEKVDILPD----YIDRLLSDIKL----GK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 253 SPLKFVHSSFHGVGHNYVQRAFQQFGFpppIPVPEQKDPDPDFSTVScPNPEEGESVLELSLRLAErEKARIVVATDPDA 332
Cdd:cd03089 162 RPLKVVVDAGNGAAGPIAPQLLEALGC---EVIPLFCEPDGTFPNHH-PDPTDPENLEDLIAAVKE-NGADLGIAFDGDG 236
|
250 260
....*....|....*....|....*.
gi 148596920 333 DRLAVAeqnDNCGwKVFTGNELAALL 358
Cdd:cd03089 237 DRLGVV---DEKG-EIIWGDRLLALF 258
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
109-337 |
3.32e-15 |
|
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: 78.12 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 109 VVGYDTRAqassgcTSERLAKLT-AAVMLC-KDVpVYLfsTYVPTPFVPYAVMKYGAAAGVMITASHNRKEDNGYKVYWH 186
Cdd:cd05803 41 VVGRDGRP------SGPMLEKIViGALLACgCDV-IDL--GIAPTPTVQVLVRQSQASGGIIITASHNPPQWNGLKFIGP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 187 NGAQIASPHDKEILHCIEESAEPWA-----------ESWNEDLVENsLLKRDPLEdvchwymeelntlcfhRELNAKSPL 255
Cdd:cd05803 112 DGEFLTPDEGEEVLSCAEAGSAQKAgydqlgevtfsEDAIAEHIDK-VLALVDVD----------------VIKIRERNF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 256 KFVHSSFHGVGHNYVQRAFQQFGFPPPIPVPEqkdPDPDFSTVSCPNPeegESVLELSlRLAEREKARIVVATDPDADRL 335
Cdd:cd05803 175 KVAVDSVNGAGGLLIPRLLEKLGCEVIVLNCE---PTGLFPHTPEPLP---ENLTQLC-AAVKESGADVGFAVDPDADRL 247
|
..
gi 148596920 336 AV 337
Cdd:cd05803 248 AL 249
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
350-479 |
7.27e-15 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 70.94 E-value: 7.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 350 TGNELAALLGWWMLFNwKEAHPDPAdtervymLATTV-SSKILEAFARIEGFHFEETLPGFKWIGNRIHELKkagkeVIF 428
Cdd:pfam02880 1 DGDQILALLAKYLLEQ-GKLPPGAG-------VVKTVmSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEG-----ALF 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 148596920 429 SFEESIGFLCGNMVLDKDGVSTAAVVAEMasyLHTKNLSLNQQLCNIYEIY 479
Cdd:pfam02880 68 GGEESGHIIFLDHATTKDGILAALLVLEI---LARTGKSLSELLEELPEKY 115
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
61-578 |
7.67e-13 |
|
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: 71.12 E-value: 7.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 61 RMTFGTAGLR-AAMGAGFariNDLTIIQSTQGLYKYLAK------CFpdlktrglvVGYDTRAQASSGCTS--ERLAKLT 131
Cdd:cd05801 20 RVAFGTSGHRgSSLKGSF---NEAHILAISQAICDYRKSqgitgpLF---------LGKDTHALSEPAFISalEVLAANG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 132 AAVMLCKDvpvylfSTYVPTPFVPYAVMKY------GAAAGVMITASHNRKEDNGYKVYWHNGAqiasPHDKEILHCIEE 205
Cdd:cd05801 88 VEVIIQQN------DGYTPTPVISHAILTYnrgrteGLADGIVITPSHNPPEDGGFKYNPPHGG----PADTDITRWIEK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 206 SAepwaeswNEDLVEN-SLLKRDPLED------------VCHwYMEELNTlCFHRELNAKSPLKFVHSSFHGVGHNYVQR 272
Cdd:cd05801 158 RA-------NALLANGlKGVKRIPLEAalasgythrhdfVTP-YVADLGN-VIDMDAIRKSGLRLGVDPLGGASVPYWQP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 273 AFQQFGFPPPIPVPEQkdpDPDFSTVS----------CPNPEEGESVLELslrlaeREKARIVVATDPDADRLAVAEQnd 342
Cdd:cd05801 229 IAEKYGLNLTVVNPKV---DPTFRFMTldhdgkirmdCSSPYAMAGLLKL------KDKFDLAFANDPDADRHGIVTP-- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 343 ncGWKVFTGNE-LAALLgwWMLF----NWKeahpdpadtERVYMLATTVSSKILEAFARIEGFHFEETLPGFKWIGNRIH 417
Cdd:cd05801 298 --SAGLMNPNHyLSVAI--DYLFthrpLWN---------KSAGVGKTLVSSSMIDRVAAALGRKLYEVPVGFKWFVDGLL 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 418 ELKKAgkeviFSFEESIG--FLCGN-MV--LDKDGVSTAAVVAEMASyLHTKNLS-LNQQLCNIYEIYGYhiSRTsyvlc 491
Cdd:cd05801 365 DGSLG-----FGGEESAGasFLRRDgTVwtTDKDGIIMCLLAAEILA-VTGKDPGqLYQELTERFGEPYY--ARI----- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 492 nDPPTIHRIFSRLRNFGGQGVYPTSCGDYCITHIRDVTTGYDSSqpdkkcvlplskssqM--LTFTFQNGIVAtLRTSGT 569
Cdd:cd05801 432 -DAPATPEQKARLKKLSPEQVTATELAGDPILAKLTRAPGNGAS---------------IggLKVTTANGWFA-ARPSGT 494
|
....*....
gi 148596920 570 EPKIKYYTE 578
Cdd:cd05801 495 EDVYKIYAE 503
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
64-456 |
6.00e-12 |
|
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: 68.16 E-value: 6.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 64 FGTAGLRAAmgAGFARINDLTIIQSTQGLYKYLAKCFPdlkTRGLVV-GYDTRAqasSGctsERLAKLTAAVMLCKDVPV 142
Cdd:TIGR01455 1 FGTDGVRGR--AGQEPLTAELALLLGAAAGRVLRQGRD---TAPRVViGKDTRL---SG---YMLENALAAGLNSAGVDV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 143 YLFSTyVPTPFVPYAVMKYGAAAGVMITASHNRKEDNGYKVYWHNGAQIASPHDKEILHCIEESAE---PWAESWNEdlv 219
Cdd:TIGR01455 70 LLLGP-LPTPAVAYLTRTLRADAGVMISASHNPYEDNGIKFFGPGGFKLDDATEAAIEALLDEADPlprPESEGLGR--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 220 enslLKRDPleDVCHWYMEEL-NTLCFHRELnakSPLKFVHSSFHGVGHNYVQRAFQQFGfPPPIPVPEqkdpDPDFSTV 298
Cdd:TIGR01455 146 ----VKRYP--DAVGRYIEFLkSTLPRGLTL---SGLKVVLDCANGAAYKVAPHVFRELG-AEVIAIGV----EPDGLNI 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 299 scpNPEEGESVLElSLRLAERE-KARIVVATDPDADR-LAVAEQNDncgwkVFTGNELAALLGwwmlFNWKEAHPDPADT 376
Cdd:TIGR01455 212 ---NDGCGSTHLD-ALQKAVREhGADLGIAFDGDADRvLAVDANGR-----IVDGDQILYIIA----RALKESGELAGNT 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 377 ervyMLATTVSSKILEAFARIEGFHFEETLPGFKWIGNRIHElkkagKEVIFSFEESIGFLCGNMVLDKDGVSTAAVVAE 456
Cdd:TIGR01455 279 ----VVATVMSNLGLERALEKLGLTLIRTAVGDRYVLEEMRE-----SGYNLGGEQSGHIILLDYSTTGDGIVSALQVLT 349
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
109-205 |
2.71e-10 |
|
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: 62.89 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 109 VVGYDTRAqaSSGCTSERLAK-LTAAVMLCKDVPVylfstyVPTPFVPYAVMKYGAAAGVMITASHNRKEDNGYKVYWHN 187
Cdd:cd05802 41 LIGKDTRI--SGYMLESALAAgLTSAGVDVLLLGV------IPTPAVAYLTRKLRADAGVVISASHNPFEDNGIKFFSSD 112
|
90
....*....|....*...
gi 148596920 188 GAQIasPHDKEILhcIEE 205
Cdd:cd05802 113 GYKL--PDEVEEE--IEA 126
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
60-447 |
2.87e-09 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 59.76 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 60 SRMTFGTAGLR-AAMGAGFariNDLTIIQSTQGLYKYLAKCFPDLKtrgLVVGYDTRAqassgcTSERlAKLTAAVMLC- 137
Cdd:PRK07564 36 QDVKFGTSGHRgSSLQPSF---NENHILAIFQAICEYRGKQGITGP---LFVGGDTHA------LSEP-AIQSALEVLAa 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 138 KDVPVYLFST--YVPTPFVPYAVMKY-----GAAAGVMITASHNRKEDNGYKVYWHNGAqiasPHDKEILHCIEESAE-- 208
Cdd:PRK07564 103 NGVGVVIVGRggYTPTPAVSHAILKYngrggGLADGIVITPSHNPPEDGGIKYNPPNGG----PADTDVTDAIEARANel 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 209 -----------PWAESWNEDLVEnsllKRDPLEDvchwYMEELNTLcFHRELNAKSPLKFVHSSFHGVGHNYVQRAFQQF 277
Cdd:PRK07564 179 layglkgvkriPLDRALASMTVE----VIDPVAD----YVEDLENV-FDFDAIRKAGLRLGVDPLGGATGPYWKAIAERY 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 278 GF------PPPIPV----PEQKD----PDPDfstvscpnpeegeSVLELSLRLAEREKARIVVATDPDADR--------- 334
Cdd:PRK07564 250 GLdltvvnAPVDPTfnfmPLDDDgkirMDCS-------------SPYAMAGLLALKDAFDLAFANDPDGDRhgivtpggl 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 335 ------LAVAEQNdncgwkvftgnelaallgwwmLFNWKEAHPDPADTERvymlaTTVSSKILEAFARIEGFHFEETLPG 408
Cdd:PRK07564 317 mnpnhyLAVAIAY---------------------LFHHRPGWRAGAGVGK-----TLVSSAMIDRVAAKLGRKLYEVPVG 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 148596920 409 FKWIGNRIHelkkAGKeviFSF--EESIG--FL---CGNMVLDKDG 447
Cdd:PRK07564 371 FKWFVNGLD----DGS---LGFggEESAGasFLrrdGSVWTTDKDG 409
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
162-213 |
7.58e-05 |
|
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: 45.66 E-value: 7.58e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 148596920 162 GAAAGVMITASHNRKEDNGYKVYWHNGAQiasphdkeilhcIEESAEPWAES 213
Cdd:cd03086 34 GKTIGVMITASHNPVEDNGVKIVDPDGEM------------LEESWEPYATQ 73
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
64-184 |
1.09e-04 |
|
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: 44.88 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148596920 64 FGTAGLRAAMGAgfarINDLTIIQSTQGLYKYLAKCFPDlktRGLVVGYDTRAqassgcTSERLAKLTA-AVMLCKDVPV 142
Cdd:cd03088 2 FGTSGLRGLVTD----LTDEVCYAYTRAFLQHLESKFPG---DTVAVGRDLRP------SSPRIAAACAaALRDAGFRVV 68
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 148596920 143 YLfsTYVPTPFVPYAVMKYGAAAgVMITASHNRKEDNGYKVY 184
Cdd:cd03088 69 DC--GAVPTPALALYAMKRGAPA-IMVTGSHIPADRNGLKFY 107
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
159-183 |
2.56e-04 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 43.86 E-value: 2.56e-04
10 20
....*....|....*....|....*
gi 148596920 159 MKYGAAAGVMITASHNRKEDNGYKV 183
Cdd:PLN02895 54 LKTGAATGLMITASHNPVSDNGVKI 78
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
149-182 |
3.13e-04 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 43.59 E-value: 3.13e-04
10 20 30
....*....|....*....|....*....|....
gi 148596920 149 VPTPFVPYAVMKYGAAAGVMITASHNRKEDNGYK 182
Cdd:PRK10887 76 MPTPAVAYLTRTLRAEAGIVISASHNPYYDNGIK 109
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
549-604 |
1.67e-03 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 37.25 E-value: 1.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 148596920 549 SQMLTFTFQNGIVATLRTSGTEPKIKYYTEfcASPgerdisslDEELRKVAAALVE 604
Cdd:pfam00408 23 ADAEKILGEDGRRLDVRPSGTEPVLRVMVE--GDS--------DEELARLADEIAD 68
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
165-213 |
2.67e-03 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 40.79 E-value: 2.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 148596920 165 AGVMITASHNRKEDNGYKVYWHNGAQiasphdkeilhcIEESAEPWAES 213
Cdd:PTZ00302 77 VGVMITASHNPIQDNGVKIIDPDGGM------------LEESWEKICTD 113
|
|
| |
