|
Name |
Accession |
Description |
Interval |
E-value |
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
43-564 |
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: 685.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 43 NLEFGTGGLRGIMGAGTNRINRYTVGMATQGLSNYIKNCFRGRAGLAVAVAYDSRNNSREFAGITASVFASNGFRVYLFD 122
Cdd:cd05799 1 RLEFGTAGLRGKMGAGTNRMNDYTVRQATQGLANYLKKKGPDAKNRGVVIGYDSRHNSREFAELTAAVLAANGIKVYLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 123 ELRPTPVLSFAIRYYKCVAGVMITASHNPKEYNGYKAYWEDGAQITAPHDANIIAEVEKITDISMVRFKGENLD--IHLK 200
Cdd:cd05799 81 DLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAVLEPLDIKFEEALDSglIKYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 201 GQEIDDAYLKAVMSLTLSPEIVKKHNhFKIVYTPLHGTGVKIIPRALRELGFSNIINVPEQDVSDGNFPTVKSPNPEESA 280
Cdd:cd05799 161 GEEIDDAYLEAVKKLLVNPELNEGKD-LKIVYTPLHGVGGKFVPRALKEAGFTNVIVVEEQAEPDPDFPTVKFPNPEEPG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 281 TLEMALKKAEETSADLVMATDPDADRLGIAVRDLKGRLVLLNGNQTAAILSFYLLERWRELGKLSEGPnpsfYMVKTIVT 360
Cdd:cd05799 240 ALDLAIELAKKVGADLILATDPDADRLGVAVKDKDGEWRLLTGNEIGALLADYLLEQRKEKGKLPKNP----VIVKTIVS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 361 TDLLKSMAEIYGVEMIEVLTGFKYIAEVV-HRNEGKRTFIGGGEESYGFNAGEFVRDKDAVLACALVAEAAAWAEERGQS 439
Cdd:cd05799 316 SELLRKIAKKYGVKVEETLTGFKWIGNKIeELESGGKKFLFGFEESIGYLVGPFVRDKDGISAAALLAEMAAYLKAQGKT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 440 LYELLIEIYVRFGFYKEKLLSVTKKGIDGLEQIKNIMKGLRERPlqnlagsevvlihdynssesvdmisdlrfklnfpks 519
Cdd:cd05799 396 LLDRLDELYEKYGYYKEKTISITFEGKEGPEKIKAIMDRLRNNP------------------------------------ 439
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1309054204 520 DVLQFVSSDNSIVSVRPSGTEPKIKYYFGVKDTLNSADDFDKLND 564
Cdd:cd05799 440 NVLTFYLEDGSRVTVRPSGTEPKIKFYIEVVGKKTLEEAEKKLDA 484
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
8-546 |
3.13e-138 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 413.70 E-value: 3.13e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 8 RAQLWLDESYDEETRKEVKRMM-DENPAELEDSFYKNLEFGTGGLRGIMGAGTNRINRYTVGMATQGLSNYIKNCFrGRA 86
Cdd:PTZ00150 8 QVELWLKWDKDPETRKEIEELLaSKDEEELKRRFLKRMEFGTAGLRGKMGAGFNCMNDLTVQQTAQGLCAYVIETF-GQA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 87 GLA--VAVAYDSRNNSREFAGITASVFASNGFRVYLFDELRPTPVLSFAIRYYKCVAGVMITASHNPKEYNGYKAYWEDG 164
Cdd:PTZ00150 87 LKSrgVVIGYDGRYHSRRFAEITASVFLSKGFKVYLFGQTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVYWSNG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 165 AQITAPHDANIIAEV-----------EKITDISMVrfkgenlDIHlkgQEIDDAYLKAVMSlTLSPEiVKKHNHFKIVYT 233
Cdd:PTZ00150 167 AQIIPPHDKNISAKIlsnlepwssswEYLTETLVE-------DPL---AEVSDAYFATLKS-EYNPA-CCDRSKVKIVYT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 234 PLHGTGVKIIPRALRELGFSNIINVPEQDVSDGNFPTVKSPNPEESA-TLEMALKKAEETSADLVMATDPDADRLGIAVR 312
Cdd:PTZ00150 235 AMHGVGTRFVQKALHTVGLPNLLSVAQQAEPDPEFPTVTFPNPEEGKgALKLSMETAEAHGSTVVLANDPDADRLAVAEK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 313 dLKGRLVLLNGNQTAAILSFYLLERWRELGklseGPNPSFYMVKTIVTTDLLKSMAEIYGVEMIEVLTGFKYI---AEVV 389
Cdd:PTZ00150 315 -LNNGWKIFTGNELGALLAWWAMKRYRRQG----IDKSKCFFICTVVSSRMLKKMAEKEGFQYDETLTGFKWIgnkAIEL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 390 HRNEGKRTFIgGGEESYGFNAGEFVRDKDAVLACALVAEAAAWAEERGQSLYELLIEIYVRFGFYkekllsVTKKG---I 466
Cdd:PTZ00150 390 NAENGLTTLF-AYEEAIGFMLGTRVRDKDGVTAAAVVAEMALYLYERGKTLVEHLESLYKQYGYH------FTNNSyyiC 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 467 DGLEQIKNIMKGLRE--RPLQNLAGSEVVLIHD----YNSSEsvdmiSDLRFKLNF-PKSDVLQFVSSDNSIVSVRPSGT 539
Cdd:PTZ00150 463 YDPSRIVSIFNDIRNngSYPTKLGGYPVTRIRDlttgYDTAT-----PDGKPLLPVsASTQMITFYFENGAIITIRGSGT 537
|
....*..
gi 1309054204 540 EPKIKYY 546
Cdd:PTZ00150 538 EPKLKWY 544
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
41-573 |
6.58e-123 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 369.92 E-value: 6.58e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 41 YKNLeFGTGGLRGImgAGTNrINRYTVGMATQGLSNYIKNCFRGRaglaVAVAYDSRNNSREFAGITASVFASNGFRVYL 120
Cdd:COG1109 3 YKKL-FGTDGIRGI--VGEE-LTPEFVLKLGRAFGTYLKEKGGPK----VVVGRDTRLSSPMLARALAAGLASAGIDVYD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 121 FdELRPTPVLSFAIRYYKCVAGVMITASHNPKEYNGYKAYWEDGAQITAPHDANIIAEVEKItDISMVRFKGENLDIHLk 200
Cdd:COG1109 75 L-GLVPTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKE-DFRRAEAEEIGKVTRI- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 201 gQEIDDAYLKAVMSltLSPEIVKKHNhFKIVYTPLHGTGVKIIPRALRELGFsNIINVPEQdvSDGNFPTVkSPNPEESA 280
Cdd:COG1109 152 -EDVLEAYIEALKS--LVDEALRLRG-LKVVVDCGNGAAGGVAPRLLRELGA-EVIVLNAE--PDGNFPNH-NPNPEPEN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 281 tLEMALKKAEETSADLVMATDPDADRLGIAVRdlKGRLVllNGNQTAAILSFYLLERwrelgklseGPNPsfYMVKTIVT 360
Cdd:COG1109 224 -LEDLIEAVKETGADLGIAFDGDADRLGVVDE--KGRFL--DGDQLLALLARYLLEK---------GPGG--TVVVTVMS 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 361 TDLLKSMAEIYGVEMIEVLTGFKYIAEVVHRNEgkrtFIGGGEESYGFNAGEFVRDKDAVLacaLVAEAAAWAEERGQSL 440
Cdd:COG1109 288 SLALEDIAEKHGGEVVRTKVGFKYIKEKMRETG----AVLGGEESGGIIFPDFVPTDDGIL---AALLLLELLAKQGKSL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 441 YELLIEIyvrfGFYKEKLLSVTkkgIDGLEQIKNIMKGLRERplqnlagsevvlihdYNSSESVDMISDLRFKLNfpksd 520
Cdd:COG1109 361 SELLAEL----PRYPQPEINVR---VPDEEKIGAVMEKLREA---------------VEDKEELDTIDGVKVDLE----- 413
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1309054204 521 vlqfvssDNSIVSVRPSGTEPKIKYYFGVKDtlnsADDFDKLNDELDQRLSAL 573
Cdd:COG1109 414 -------DGGWVLVRPSGTEPLLRVYAEAKD----EEEAEELLAELAELVEEA 455
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
45-546 |
1.73e-80 |
|
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: 260.18 E-value: 1.73e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 45 EFGTGGLRGIMGAGTNRINrytVGMATQGLSNYIKNcfRGRAGLAVAVAYDSRNNSREFAGITASVFASNGFRVYLFDEL 124
Cdd:cd05800 2 KFGTDGWRGIIAEDFTFEN---VRRVAQAIADYLKE--EGGGGRGVVVGYDTRFLSEEFARAVAEVLAANGIDVYLSDRP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 125 RPTPVLSFAIRYYKCVAGVMITASHNPKEYNGYKAYWEDGAqiTAPHDanIIAEVEKITDISMVRFKGENLDIHLKGQEI 204
Cdd:cd05800 77 VPTPAVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGG--SALPE--ITAAIEARLASGEPPGLEARAEGLIETIDP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 205 DDAYLKAVMSLtLSPEIVKKhNHFKIVYTPLHGTGVKIIPRALRELGFSNI-INvPEQDVS-DGNFPtvkSPNPEESATL 282
Cdd:cd05800 153 KPDYLEALRSL-VDLEAIRE-AGLKVVVDPMYGAGAGYLEELLRGAGVDVEeIR-AERDPLfGGIPP---EPIEKNLGEL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 283 EMALKkaeETSADLVMATDPDADRLGIAvrDLKGRLVllNGNQTAAILSFYLLER--WRelgklseGPnpsfyMVKTIVT 360
Cdd:cd05800 227 AEAVK---EGGADLGLATDGDADRIGAV--DEKGNFL--DPNQILALLLDYLLENkgLR-------GP-----VVKTVST 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 361 TDLLKSMAEIYGVEMIEVLTGFKYIAEVVHRnegKRTFIgGGEESYGFNAGEFVRDKDAVLacaLVAEAAAWAEERGQSL 440
Cdd:cd05800 288 THLIDRIAEKHGLPVYETPVGFKYIAEKMLE---EDVLI-GGEESGGLGIRGHIPERDGIL---AGLLLLEAVAKTGKPL 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 441 YELLIEIYVRFG--FYKEKLLSVTkkgidgLEQIKNIMKGLRERPLQNLAGSEvvlihdynssesVDMISDLrfklnfpk 518
Cdd:cd05800 361 SELVAELEEEYGpsYYDRIDLRLT------PAQKEAILEKLKNEPPLSIAGGK------------VDEVNTI-------- 414
|
490 500
....*....|....*....|....*...
gi 1309054204 519 sDVLQFVSSDNSIVSVRPSGTEPKIKYY 546
Cdd:cd05800 415 -DGVKLVLEDGSWLLIRPSGTEPLLRIY 441
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
44-183 |
1.25e-48 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 165.48 E-value: 1.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 44 LEFGTGGLRGIMGAGTNriNRYTVGMATQGLSNYIKNCFRGRAglaVAVAYDSRNNSREFAGITASVFASNGFRVYLFdE 123
Cdd:pfam02878 2 QLFGTSGIRGKVGVGEL--TPEFALKLGQAIASYLRAQGGGGK---VVVGRDTRYSSRELARALAAGLASNGVEVILL-G 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 124 LRPTPVLSFAIRYYKCVAGVMITASHNPKEYNGYKAYWEDGAQITAPHDANIIAEVEKIT 183
Cdd:pfam02878 76 LLPTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKED 135
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
111-421 |
3.25e-42 |
|
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: 155.21 E-value: 3.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 111 FASNGFRVYLFDELRPTPVLSFAIRYYKcVAGVMITASHNPKEYNGYKAYWEDGAQITAPHDANIIAEVEKitdISMVRF 190
Cdd:cd03084 2 FGTSGVRGVVGDDITPETAVALGQAIGS-TGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEK---EDEPSA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 191 KGENLDIHLKGQEIDDAYLKAVMSLTlsPEIVKKHNHFKIVYTPLHGTGVKIIPRALRELGFSNIinvPEQDVSDGNFPt 270
Cdd:cd03084 78 VAYELGGSVKAVDILQRYFEALKKLF--DVAALSNKKFKVVVDSVNGVGGPIAPQLLEKLGAEVI---PLNCEPDGNFG- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 271 VKSPNPEESATLEMALKKAEETSADLVMATDPDADRLGIAvrDLKGRLVllNGNQTAAILSFYLLERWrelgklsegpNP 350
Cdd:cd03084 152 NINPDPGSETNLKQLLAVVKAEKADFGVAFDGDADRLIVV--DENGGFL--DGDELLALLAVELFLTF----------NP 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1309054204 351 SFYMVKTIVTTDLLKSMAEIYGVEMIEVLTGFKYIAEVVHrnegKRTFIGGGEESYGFNAGEFVRDKDAVL 421
Cdd:cd03084 218 RGGVVKTVVSSGALDKVAKKLGIKVIRTKTGFKWVGEAMQ----EGDVVLGGEESGGVIFPEFHPGRDGIS 284
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
46-546 |
4.97e-40 |
|
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: 151.51 E-value: 4.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 46 FGTGGLRGIMGAGTNRINRYTVGMAtqgLSNYIKncfRGRaglaVAVAYDSRNNSREFAGITASVFASNGFRVYLFDELr 125
Cdd:TIGR03990 4 FGTSGIRGIVGEELTPELALKVGKA---FGTYLR---GGK----VVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLGIA- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 126 PTPVLSFAIRYYKCVAGVMITASHNPKEYNGYKAYWEDGAQITAphdaniiAEVEKITDISmvrFKG--ENLDIHLKGQ- 202
Cdd:TIGR03990 73 PTPTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSR-------EQEEEIEEIA---ESGdfERADWDEIGTv 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 203 ----EIDDAYLKAVMSlTLSPEIVKKHNhFKIVYTPLHGTGVKIIPRALRELGfSNIINVPEQdvSDGNFPTVKS-PNPE 277
Cdd:TIGR03990 143 tsdeDAIDDYIEAILD-KVDVEAIRKKG-FKVVVDCGNGAGSLTTPYLLRELG-CKVITLNCQ--PDGTFPGRNPePTPE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 278 esaTLEMALKKAEETSADLVMATDPDADRLgIAVrDLKGRLVllNGNQTAAILSFYLLErwrelgklsegpNPSFYMVKT 357
Cdd:TIGR03990 218 ---NLKDLSALVKATGADLGIAHDGDADRL-VFI-DEKGRFI--GGDYTLALFAKYLLE------------HGGGKVVTN 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 358 IVTTDLLKSMAEIYGVEMIEVLTGFKYIAEVVHRNEGkrtfIGGGEESYGFNAGEFVRDKDAVLacaLVAEAAAWAEERG 437
Cdd:TIGR03990 279 VSSSRAVEDVAERHGGEVIRTKVGEVNVAEKMKEEGA----VFGGEGNGGWIFPDHHYCRDGLM---AAALFLELLAEEG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 438 QSLYELLIEI--YVRfgfYKEKL-LSVTKKgidgleqiKNIMKGLRERplqnlagsevvlihdyNSSESVDMISDLRfkl 514
Cdd:TIGR03990 352 KPLSELLAELpkYPM---SKEKVeLPDEDK--------EEVMEAVEEE----------------FADAEIDTIDGVR--- 401
|
490 500 510
....*....|....*....|....*....|..
gi 1309054204 515 nfpksdvlqfVSSDNSIVSVRPSGTEPKIKYY 546
Cdd:TIGR03990 402 ----------IDFEDGWVLVRPSGTEPIVRIY 423
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
46-546 |
7.46e-35 |
|
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: 136.55 E-value: 7.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 46 FGTGGLRGIMGAGTNRINRYTVGMAtqgLSNYIKNcfrGRaglaVAVAYDSRNNSREFAGITASVFASNGFRVYLFDELr 125
Cdd:cd03087 2 FGTSGIRGVVGEELTPELALKVGKA---LGTYLGG---GT----VVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDIGIV- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 126 PTPVLSFAIRYYKcVAGVMITASHNPKEYNGYKAYWEDGAQITAPHDaniiAEVEKItdISMVRFKGENLDiHLKGQEID 205
Cdd:cd03087 71 PTPALQYAVRKLG-DAGVMITASHNPPEYNGIKLVNPDGTEFSREQE----EEIEEI--IFSERFRRVAWD-EVGSVRRE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 206 DA----YLKAVMSLTlspeIVKKHNHFKIVYTPLHGTGVKIIPRALRELGfSNIINVPEQdvSDGNFPTVKS-PNPEesa 280
Cdd:cd03087 143 DSaideYIEAILDKV----DIDGGKGLKVVVDCGNGAGSLTTPYLLRELG-CKVITLNAN--PDGFFPGRPPePTPE--- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 281 TLEMALKKAEETSADLVMATDPDADRLgIAVrDLKGRLVllNGNQTAAILSFYLLErwrelgklsEGPnpsfymvKTIVT 360
Cdd:cd03087 213 NLSELMELVRATGADLGIAHDGDADRA-VFV-DEKGRFI--DGDKLLALLAKYLLE---------EGG-------GKVVT 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 361 T----DLLKSMAEIYGVEMIEVLTGFKYIAEVVHRNEGkrTFigGGEESYGFNAGEFVRDKDAVLacalVAEAAAWAEER 436
Cdd:cd03087 273 PvdasMLVEDVVEEAGGEVIRTPVGDVHVAEEMIENGA--VF--GGEPNGGWIFPDHQLCRDGIM----TAALLLELLAE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 437 GQSLYELLIEIYVRFgFYKEKL-LSVTKKgidgleqiKNIMKGLRERplqnlagsevvlIHDynSSESVDMISDLRfkln 515
Cdd:cd03087 345 EKPLSELLDELPKYP-LLREKVeCPDEKK--------EEVMEAVEEE------------LSD--ADEDVDTIDGVR---- 397
|
490 500 510
....*....|....*....|....*....|.
gi 1309054204 516 fpksdvlqfVSSDNSIVSVRPSGTEPKIKYY 546
Cdd:cd03087 398 ---------IEYEDGWVLIRPSGTEPKIRIT 419
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
82-337 |
1.68e-31 |
|
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: 127.24 E-value: 1.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 82 FRGRAGLAVAVAYDSRNNSREFAGITASVFASNGFRVYLFdELRPTPVLSFAIRYYKCVAGVMITASHNPKEYNGYKAYW 161
Cdd:cd03089 31 LLEKGAKKVVVGRDGRLSSPELAAALIEGLLAAGCDVIDI-GLVPTPVLYFATFHLDADGGVMITASHNPPEYNGFKIVI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 162 E----DGAQITAphdanIIAEVEKItdismvRFKGENLDIHLKGQEIDDAYLKAVMSltlspEIVKKHNHFKIVYTPLHG 237
Cdd:cd03089 110 GggplSGEDIQA-----LRERAEKG------DFAAATGRGSVEKVDILPDYIDRLLS-----DIKLGKRPLKVVVDAGNG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 238 TGVKIIPRALRELGFsniiNVPEQDV-SDGNFPTvKSPNPEESATLEmALKKA-EETSADLVMATDPDADRLGIAvrDLK 315
Cdd:cd03089 174 AAGPIAPQLLEALGC----EVIPLFCePDGTFPN-HHPDPTDPENLE-DLIAAvKENGADLGIAFDGDGDRLGVV--DEK 245
|
250 260
....*....|....*....|..
gi 1309054204 316 GRLVllNGNQTAAILSFYLLER 337
Cdd:cd03089 246 GEII--WGDRLLALFARDILKR 265
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
50-401 |
5.42e-31 |
|
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: 125.50 E-value: 5.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 50 GLRGIMGAGTN--RINRYTVGMATQglsnyiknCFRGRAGLAVAVAYDSRNNSREFAGITASVFASNGFRVYLFDeLRPT 127
Cdd:cd05803 6 GIRGIVGEGLTpeVITRYVAAFATW--------QPERTKGGKIVVGRDGRPSGPMLEKIVIGALLACGCDVIDLG-IAPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 128 PVLSFAIRYYKCVAGVMITASHNPKEYNGYKAYWEDGAQITAphdaniiAEVEKITDISmvrFKGENLDIH----LKGQE 203
Cdd:cd05803 77 PTVQVLVRQSQASGGIIITASHNPPQWNGLKFIGPDGEFLTP-------DEGEEVLSCA---EAGSAQKAGydqlGEVTF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 204 IDDA---YLKAVMSLTLSPEIVKKHNHFKIVYTPLHGTGVKIIPRALRELGFSNII--NVPeqdvsDGNFPTVKSPNPEE 278
Cdd:cd05803 147 SEDAiaeHIDKVLALVDVDVIKIRERNFKVAVDSVNGAGGLLIPRLLEKLGCEVIVlnCEP-----TGLFPHTPEPLPEN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 279 SATLEMALKKAeetSADLVMATDPDADRLgiAVRDLKGRLVllnGNQTAAILSFYLLerWRELGKlsEGPnpsfyMVKTI 358
Cdd:cd05803 222 LTQLCAAVKES---GADVGFAVDPDADRL--ALVDEDGRPI---GEEYTLALAVDYV--LKYGGR--KGP-----VVVNL 284
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1309054204 359 VTTDLLKSMAEIYGVEMIEVLTGfkyIAEVVHRNEGKRTFIGG 401
Cdd:cd05803 285 STSRALEDIARKHGVPVFRSAVG---EANVVEKMKEVDAVIGG 324
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
46-405 |
2.46e-26 |
|
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: 111.81 E-value: 2.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 46 FGTGGLRGImgAGTNrinrYTVGMATQgLSNYIKNCFRGRAGLA-VAVAYDSRNNSREFAGITASVFASNGFRVYLFDEL 124
Cdd:cd05802 2 FGTDGIRGV--ANEP----LTPELALK-LGRAAGKVLGKGGGRPkVLIGKDTRISGYMLESALAAGLTSAGVDVLLLGVI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 125 rPTPVLSFAIRYYKCVAGVMITASHNPKEYNGYKAYWEDGAQITaphDAnIIAEVEK-ITDISMVRFKGENLDihlKGQE 203
Cdd:cd05802 75 -PTPAVAYLTRKLRADAGVVISASHNPFEDNGIKFFSSDGYKLP---DE-VEEEIEAlIDKELELPPTGEKIG---RVYR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 204 IDDA---YLKAVMSlTLSPEIVKKhnhFKIVYTPLHGTGVKIIPRALRELGfSNII---NVPeqdvsDG-----NfptVK 272
Cdd:cd05802 147 IDDArgrYIEFLKS-TFPKDLLSG---LKIVLDCANGAAYKVAPEVFRELG-AEVIvinNAP-----DGlninvN---CG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 273 SPNPEesatlemALKKA-EETSADLVMATDPDADRLgIAVrDLKGRLVllNGNQTAAILSFYLLERwrelGKLSEGpnps 351
Cdd:cd05802 214 STHPE-------SLQKAvLENGADLGIAFDGDADRV-IAV-DEKGNIV--DGDQILAICARDLKER----GRLKGN---- 274
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1309054204 352 fymvkTIVTT-----DLLKSMAEIyGVEMIEVLTGFKYIAEVVHRNEgkrtFIGGGEES 405
Cdd:cd05802 275 -----TVVGTvmsnlGLEKALKEL-GIKLVRTKVGDRYVLEEMLKHG----ANLGGEQS 323
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
207-310 |
2.06e-25 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 100.44 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 207 AYLKAVMSlTLSPEIVKKhNHFKIVYTPLHGTGVKIIPRALRELGFsniINVPEQDVSDGNFPTvKSPNPEESATLEMAL 286
Cdd:pfam02879 1 AYIDHLLE-LVDSEALKK-RGLKVVYDPLHGVGGGYLPELLKRLGC---DVVEENCEPDPDFPT-RAPNPEEPEALALLI 74
|
90 100
....*....|....*....|....
gi 1309054204 287 KKAEETSADLVMATDPDADRLGIA 310
Cdd:pfam02879 75 ELVKSVGADLGIATDGDADRLGVV 98
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
46-405 |
6.27e-20 |
|
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: 92.81 E-value: 6.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 46 FGTGGLRGimgagtnRINRY-TVGMATQGLSNYIKNCFRGRAGLA--VAVAYDSRNNSREFAGITASVFASNGFRVYLFD 122
Cdd:TIGR01455 1 FGTDGVRG-------RAGQEpLTAELALLLGAAAGRVLRQGRDTAprVVIGKDTRLSGYMLENALAAGLNSAGVDVLLLG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 123 ELrPTPVLSFAIRYYKCVAGVMITASHNPKEYNGYKAYWEDGAQITAPHDANIIAEVEKITDISMVrfKGENLDIHLKGQ 202
Cdd:TIGR01455 74 PL-PTPAVAYLTRTLRADAGVMISASHNPYEDNGIKFFGPGGFKLDDATEAAIEALLDEADPLPRP--ESEGLGRVKRYP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 203 EIDDAYLKAVMS-----LTLSpeivkkhnHFKIVYTPLHGTGVKIIPRALRELGfsniinvpEQDVSDGNFPTVKSPNPE 277
Cdd:TIGR01455 151 DAVGRYIEFLKStlprgLTLS--------GLKVVLDCANGAAYKVAPHVFRELG--------AEVIAIGVEPDGLNINDG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 278 ESATLEMALKKA-EETSADLVMATDPDADRLgIAVrDLKGRLVllNGNQTAAILSFYLLERwrelGKLsegpnPSFYMVK 356
Cdd:TIGR01455 215 CGSTHLDALQKAvREHGADLGIAFDGDADRV-LAV-DANGRIV--DGDQILYIIARALKES----GEL-----AGNTVVA 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1309054204 357 TIVTT-DLLKSMAEIyGVEMIEVLTGFKYIAEVVHRNEGKRtfigGGEES 405
Cdd:TIGR01455 282 TVMSNlGLERALEKL-GLTLIRTAVGDRYVLEEMRESGYNL----GGEQS 326
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
31-546 |
2.29e-17 |
|
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: 85.38 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 31 ENPAEledsfykNLEFGTGGLRGIMGAGTnrINRYTVGMATQGLSNYIKN------CFRGRaglavavayDSRNNSrEFA 104
Cdd:cd05801 15 SNPAQ-------RVAFGTSGHRGSSLKGS--FNEAHILAISQAICDYRKSqgitgpLFLGK---------DTHALS-EPA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 105 GITA-SVFASNGFRVYLFDELR--PTPVLSFAI------RYYKCVAGVMITASHNPKEYNGYKAYWEDGAqitaPHDANI 175
Cdd:cd05801 76 FISAlEVLAANGVEVIIQQNDGytPTPVISHAIltynrgRTEGLADGIVITPSHNPPEDGGFKYNPPHGG----PADTDI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 176 IAEVEKI------TDISMVR-------FKGENLDIH-LKGQEIDDayLKAVMSLtlspEIVKKHNhFKIVYTPLHGTGVK 241
Cdd:cd05801 152 TRWIEKRanallaNGLKGVKripleaaLASGYTHRHdFVTPYVAD--LGNVIDM----DAIRKSG-LRLGVDPLGGASVP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 242 IIPRALRELGFS-NIINvPEQDvsdgnfPTVKSPNPEESATLEM------------ALKKaeetSADLVMATDPDADRLG 308
Cdd:cd05801 225 YWQPIAEKYGLNlTVVN-PKVD------PTFRFMTLDHDGKIRMdcsspyamagllKLKD----KFDLAFANDPDADRHG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 309 IAVRDLKgrlvLLNGNQTAAILSFYLLER---WRELGKLSegpnpsfymvKTIVTTDLLKSMAEIYGVEMIEVLTGFKYI 385
Cdd:cd05801 294 IVTPSAG----LMNPNHYLSVAIDYLFTHrplWNKSAGVG----------KTLVSSSMIDRVAAALGRKLYEVPVGFKWF 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 386 AEVVHrnEGKRTFigGGEESYG-----FNAGEFVRDKDAVLACALVAEAAAWAEERGQSLYELLIEiyvRFG--FYKEKL 458
Cdd:cd05801 360 VDGLL--DGSLGF--GGEESAGasflrRDGTVWTTDKDGIIMCLLAAEILAVTGKDPGQLYQELTE---RFGepYYARID 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 459 LSVTkkgidgLEQiKNIMKGLRERPLQ--NLAGSEV--VLIHDYNSSESVDMISdlrfklnfpksdvlqfVSSDNSIVSV 534
Cdd:cd05801 433 APAT------PEQ-KARLKKLSPEQVTatELAGDPIlaKLTRAPGNGASIGGLK----------------VTTANGWFAA 489
|
570
....*....|..
gi 1309054204 535 RPSGTEPKIKYY 546
Cdd:cd05801 490 RPSGTEDVYKIY 501
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
46-421 |
1.37e-16 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 82.88 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 46 FGTGGLRGIMGAGT---NRInrytvgMA-TQGLSNYikncfRGRAGLAVA--VAYDSRNNSREfAGITA-SVFASNGFRV 118
Cdd:PRK07564 40 FGTSGHRGSSLQPSfneNHI------LAiFQAICEY-----RGKQGITGPlfVGGDTHALSEP-AIQSAlEVLAANGVGV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 119 YL--FDELRPTPVLSFAIRYYKCVA-----GVMITASHNPKEYNGYKaYwedgaqitaphdaNII----AEvEKITDIsm 187
Cdd:PRK07564 108 VIvgRGGYTPTPAVSHAILKYNGRGggladGIVITPSHNPPEDGGIK-Y-------------NPPnggpAD-TDVTDA-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 188 vrfkgenldIHLKGQEIDDAYLKAVMSLTLS---------------------PEIVK----KHNHFKIVYTPLHGTGV-- 240
Cdd:PRK07564 171 ---------IEARANELLAYGLKGVKRIPLDralasmtvevidpvadyvedlENVFDfdaiRKAGLRLGVDPLGGATGpy 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 241 --KIIPRALRELgfsNIINvPEQDvSDGNFPTVKS-------PNPEESATLEMALKKAeetsADLVMATDPDADRLGIAv 311
Cdd:PRK07564 242 wkAIAERYGLDL---TVVN-APVD-PTFNFMPLDDdgkirmdCSSPYAMAGLLALKDA----FDLAFANDPDGDRHGIV- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 312 rdlkGRLVLLNGNQTAAILSFYLLER---WRElgKLSEGpnpsfymvKTIVTTDLLKSMAEIYGVEMIEVLTGFKYIAEV 388
Cdd:PRK07564 312 ----TPGGLMNPNHYLAVAIAYLFHHrpgWRA--GAGVG--------KTLVSSAMIDRVAAKLGRKLYEVPVGFKWFVNG 377
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1309054204 389 VHrnEGKRTFigGGEESYG-----FNAGEFVRDKD---AVL 421
Cdd:PRK07564 378 LD--DGSLGF--GGEESAGasflrRDGSVWTTDKDgliAVL 414
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
322-451 |
1.39e-16 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 75.95 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 322 NGNQTAAILSFYLLERwrelGKLSEGPnpsfYMVKTIVTTDLLKSMAEIYGVEMIEVLTGFKYIAEVVHRNEgkrtFIGG 401
Cdd:pfam02880 1 DGDQILALLAKYLLEQ----GKLPPGA----GVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEG----ALFG 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1309054204 402 GEESYGFNAGEFVRDKDAVLacaLVAEAAAWAEERGQSLYELLIEIYVRF 451
Cdd:pfam02880 69 GEESGHIIFLDHATTKDGIL---AALLVLEILARTGKSLSELLEELPEKY 115
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
83-336 |
9.15e-13 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 70.86 E-value: 9.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 83 RGRAGLAVAVAYDSRNNSREFAGITASVFASNGFRVYLFDeLRPTPVLSFAIRY--YKCVAGVMITASHNPKEYNGYKAY 160
Cdd:PLN02371 111 DGSGELRVSVGRDPRISGPRLADAVFAGLASAGLDVVDMG-LATTPAMFMSTLTerEDYDAPIMITASHLPYNRNGLKFF 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 161 WEDGAqITAPhdaniiaEVEKITDISMVRFKGENLDIHLKGQEIDDAYLKAV--MSL---TLSPEIVKKHNHFKIVYTPL 235
Cdd:PLN02371 190 TKDGG-LGKP-------DIKDILERAARIYKEWSDEGLLKSSSGASSVVCRVdfMSTyakHLRDAIKEGVGHPTNYETPL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 236 hgTGVKIIPRA------------LRELGfsniinvpeQDVS-------DGNFPTvKSPNPEESATLEMALKKAEETSADL 296
Cdd:PLN02371 262 --EGFKIVVDAgngaggffaekvLEPLG---------ADTSgslflepDGMFPN-HIPNPEDKAAMSATTQAVLANKADL 329
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1309054204 297 VMATDPDADRlgIAVRDLKGRlvLLNGNQTAAILSFYLLE 336
Cdd:PLN02371 330 GIIFDTDVDR--SAVVDSSGR--EINRNRLIALMSAIVLE 365
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
46-306 |
2.58e-12 |
|
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: 69.15 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 46 FGTGGLRGIMGAGTNR-INRYTVGmatqglsnYIKNCFRGRAGLAVAVAYDSRNNSREFAGITASVFASNGFRVYLFDEL 124
Cdd:cd03088 2 FGTSGLRGLVTDLTDEvCYAYTRA--------FLQHLESKFPGDTVAVGRDLRPSSPRIAAACAAALRDAGFRVVDCGAV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 125 rPTPVLSFAIRYYKCvAGVMITASHNPKEYNGYKAYWEDGaQITAPHDANIIAEVEKITDISMVRfKGENLDIHLKGQei 204
Cdd:cd03088 74 -PTPALALYAMKRGA-PAIMVTGSHIPADRNGLKFYRPDG-EITKADEAAILAALVELPEALFDP-AGALLPPDTDAA-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 205 dDAYLKAVMSL----TLSPEIVKKHNHFK----IVYTPLHGTGVKIIPralreLGFSNI-INVPEQDVSDgnfptvkspn 275
Cdd:cd03088 148 -DAYIARYTDFfgagALKGLRIGVYQHSSvgrdLLVRILEALGAEVVP-----LGRSDTfIPVDTEAVRP---------- 211
|
250 260 270
....*....|....*....|....*....|.
gi 1309054204 276 peesATLEMALKKAEETSADLVMATDPDADR 306
Cdd:cd03088 212 ----EDRALAAAWAAEHGLDAIVSTDGDGDR 238
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
126-347 |
2.64e-10 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 62.85 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 126 PTPVLSFAIRYYKCVAGVMITASHNPKEYNGYKAYWEDGAQITAPHDANIIAEVEKitDISMVrfKGENLDihlKGQEID 205
Cdd:PRK10887 77 PTPAVAYLTRTLRAEAGIVISASHNPYYDNGIKFFSADGTKLPDEVELAIEAELDK--PLTCV--ESAELG---KASRIN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 206 DA------YLKAVM--SLTLspeivkkhNHFKIVYTPLHGTGVKIIPRALRELGfSNIINVpeqdvsdGNFPTVKSPNPE 277
Cdd:PRK10887 150 DAagryieFCKSTFpnELSL--------RGLKIVVDCANGATYHIAPNVFRELG-AEVIAI-------GCEPNGLNINDE 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309054204 278 ESATLEMALKKA-EETSADLVMATDPDADRLgIAVrDLKGRLVllNGNQtaaILsfYLLER-WRELGKLSEG 347
Cdd:PRK10887 214 CGATDPEALQAAvLAEKADLGIAFDGDGDRV-IMV-DHLGNLV--DGDQ---LL--YIIARdRLRRGQLRGG 276
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
47-421 |
1.07e-08 |
|
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: 58.00 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 47 GTGGLRgimgagtnriNRYTVGMATQGLSNYIKNCF-----RGRAGLAVAVAYDSRNNSREFAGITASVFASNGFRVYLF 121
Cdd:cd03085 14 GTSGLR----------KKVKVFQQPNYLENFVQSIFnalppEKLKGATLVVGGDGRYYNKEAIQIIIKIAAANGVGKVVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 122 --DELRPTPVLSFAIRYYKCVAGVMITASHNP---KEYNGYKAYWEDGA----QITaphDAnIIAEVEKITDISMVrfKG 192
Cdd:cd03085 84 gqNGLLSTPAVSAVIRKRKATGGIILTASHNPggpEGDFGIKYNTSNGGpapeSVT---DK-IYEITKKITEYKIA--DD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 193 ENLDIHLKG-QEIDD---------------AYLKAVMSLTLSPEIVkKHNHFKIVYTPLHG-TG---VKIIpraLRELGF 252
Cdd:cd03085 158 PDVDLSKIGvTKFGGkpftvevidsvedyvELMKEIFDFDAIKKLL-SRKGFKVRFDAMHGvTGpyaKKIF---VEELGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 253 --SNIIN-VPEQDVSdGNFPtvkSPNPEESATLEMALKKAEetsADLVMATDPDADRLGIAvrdlkGRLVLLNGNQTAAI 329
Cdd:cd03085 234 peSSVVNcTPLPDFG-GGHP---DPNLTYAKDLVELMKSGE---PDFGAASDGDGDRNMIL-----GKGFFVTPSDSVAV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 330 LSFYLLERwrelgklsegpnPSFY------MVKTIVTTDLLKSMAEIYGVEMIEVLTGFKYIAEVVhrNEGKRTFIggGE 403
Cdd:cd03085 302 IAANAKLI------------PYFYkgglkgVARSMPTSGALDRVAKKLGIPLFETPTGWKFFGNLM--DAGKLSLC--GE 365
|
410 420
....*....|....*....|.
gi 1309054204 404 ESYGfNAGEFVRDKD---AVL 421
Cdd:cd03085 366 ESFG-TGSDHIREKDglwAVL 385
|
|
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
90-410 |
1.89e-08 |
|
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: 56.87 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 90 VAVAYDSRNNSREF-----AGITASvfasnGFRVYLFDELrPTPVLSFAIRYYKCVAGVMITASHNPKEYNGYKAYWEDG 164
Cdd:cd05805 37 VTVSRDASRASRMLkraliSGLLST-----GVNVRDLGAL-PLPVARYAIRFLGASGGIHVRTSPDDPDKVEIEFFDSRG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 165 AQITAPHDANIiaevEKI---TDISMVRFkGENLDIHLKGQEIdDAYLKAVMSlTLSPEIVKKhNHFKIVYTPLHGTGVK 241
Cdd:cd05805 111 LNISRAMERKI----ENAffrEDFRRAHV-DEIGDITEPPDFV-EYYIRGLLR-ALDTSGLKK-SGLKVVIDYAYGVAGI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 242 IIPRALRELGFSNIInVPEQDVSDGnfptVKSPNPEESATLEMAlKKAEETSADLVMATDPDADRLGIAvrDLKGRLVLl 321
Cdd:cd05805 183 VLPGLLSRLGCDVVI-LNARLDEDA----PRTDTERQRSLDRLG-RIVKALGADFGVIIDPNGERLILV--DEAGRVIS- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 322 nGNQTAAILSfYLLERWRELGKLsegpnpsfymVKTIVTTDLLKSMAEIYGVEMIEVLTGFKYIAEVVHRN----EGKRT 397
Cdd:cd05805 254 -DDLLTALVS-LLVLKSEPGGTV----------VVPVTAPSVIEQLAERYGGRVIRTKTSPQALMEAALENvvlaGDGDG 321
|
330
....*....|...
gi 1309054204 398 FIGGGEESYGFNA 410
Cdd:cd05805 322 GFIFPEFHPGFDA 334
|
|
| PLN02307 |
PLN02307 |
phosphoglucomutase |
47-421 |
2.00e-08 |
|
phosphoglucomutase
Pssm-ID: 177942 [Multi-domain] Cd Length: 579 Bit Score: 56.97 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 47 GTGGLRgimgagtnriNRYTVGMATQGLSNYIKNCF-----RGRAGLAVAVAYDSRNNSREFAGITASVFASNGFRVYLF 121
Cdd:PLN02307 26 GTSGLR----------KKVKVFMQENYLANFVQALFnalpaEKVKGATLVLGGDGRYFNKEAIQIIIKIAAANGVRRVWV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 122 --DELRPTPVLSFAIR---YYKCVAGVMITASHN---PKEYNGYKAYWEDGAqiTAPHDAN--IIAEVEKIT-------- 183
Cdd:PLN02307 96 gqNGLLSTPAVSAVIRerdGSKANGGFILTASHNpggPEEDFGIKYNYESGQ--PAPESITdkIYGNTLTIKeykmaedi 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 184 ---DISMV---RFKG-ENLDIhlkgqEIDDAY------LKAVMSLTLSPEIVKKHNhFKIVYTPLHG-TGVKIIPRALRE 249
Cdd:PLN02307 174 pdvDLSAVgvtKFGGpEDFDV-----EVIDPVedyvklMKSIFDFELIKKLLSRPD-FTFCFDAMHGvTGAYAKRIFVEE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 250 LGF--SNIIN-VPEQDVSDGNfptvksPNP------EESATLEMALKKAEETSADLVMATDPDADRLGIAvrdlkGR--- 317
Cdd:PLN02307 248 LGApeSSLLNcVPKEDFGGGH------PDPnltyakELVKRMGLGKTSYGDEPPEFGAASDGDGDRNMIL-----GKrff 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 318 ------LVLLNGNQTAAILSFyllerwrelgklSEGPNPsfyMVKTIVTTDLLKSMAEIYGVEMIEVLTGFKYIAEVVhr 391
Cdd:PLN02307 317 vtpsdsVAIIAANAQEAIPYF------------SGGLKG---VARSMPTSAALDVVAKKLNLPFFEVPTGWKFFGNLM-- 379
|
410 420 430
....*....|....*....|....*....|...
gi 1309054204 392 nEGKRTFIgGGEESYGfNAGEFVRDKD---AVL 421
Cdd:PLN02307 380 -DAGKLSI-CGEESFG-TGSDHIREKDgiwAVL 409
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
83-306 |
7.70e-08 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 54.99 E-value: 7.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 83 RGRAGLAVAVAYDSRNNSREFAGITASVFASNGFRVYLFDeLRPTPVLSFAIRYYKCvAGVMITASHNPKEYNGYKaYWE 162
Cdd:PRK09542 31 RAEGATTVVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIG-LASTDQLYFASGLLDC-PGAMFTASHNPAAYNGIK-LCR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 163 DGAQitaP--HD---ANIIAEVEK-----------ITDISMVRFKGenldihlkgqeiddAYLKAVMSLT-LSPeivkkh 225
Cdd:PRK09542 108 AGAK---PvgQDtglAAIRDDLIAgvpaydgppgtVTERDVLADYA--------------AFLRSLVDLSgIRP------ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 226 nhFKIVYTPLHGTGVKIIPRALRELgfsNIINVPEQDVSDGNFPTVKSpNPEESATLEMALKKAEETSADLVMATDPDAD 305
Cdd:PRK09542 165 --LKVAVDAGNGMGGHTVPAVLGGL---PITLLPLYFELDGTFPNHEA-NPLDPANLVDLQAFVRETGADIGLAFDGDAD 238
|
.
gi 1309054204 306 R 306
Cdd:PRK09542 239 R 239
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
127-416 |
6.31e-06 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 48.79 E-value: 6.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 127 TPVLSFAIRYYKCVAGVMITASHNPKEYNGYKAYWEDGAQI---TAPHDANIIAEVEKITDISMVRfKGENLDIHLKgqe 203
Cdd:PRK15414 77 TEEIYFATFHLGVDGGIEVTASHNPMDYNGMKLVREGARPIsgdTGLRDVQRLAEANDFPPVDETK-RGRYQQINLR--- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 204 idDAYLKAVMSLTlspeIVKKHNHFKIVYTPLHGTG---VKIIPRALRELG----FSNIINVPeqdvsDGNFPTvKSPNP 276
Cdd:PRK15414 153 --DAYVDHLFGYI----NVKNLTPLKLVINSGNGAAgpvVDAIEARFKALGapveLIKVHNTP-----DGNFPN-GIPNP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 277 EESATLEMALKKAEETSADLVMATDPDADRLGIAvrDLKGRLVllNGNQTAAILSFYLLERwRELGKLSEGPNPSFYMVK 356
Cdd:PRK15414 221 LLPECRDDTRNAVIKHGADMGIAFDGDFDRCFLF--DEKGQFI--EGYYIVGLLAEAFLEK-NPGAKIIHDPRLSWNTVD 295
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 357 TIVTTDLLKSMAEiygvemievlTGFKYIAEVVHRNEGkrtfIGGGEESygfnAGEFVRD 416
Cdd:PRK15414 296 VVTAAGGTPVMSK----------TGHAFIKERMRKEDA----IYGGEMS----AHHYFRD 337
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
116-158 |
7.48e-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: 7.48e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1309054204 116 FRVYLFDELRPtpvlsfaiRYYKC-VAGVMITASHNPKEYNGYK 158
Cdd:cd03086 19 FRVGILAALRS--------KKLGGkTIGVMITASHNPVEDNGVK 54
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
115-236 |
3.38e-04 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 43.49 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309054204 115 GFRVYLFDELRPTPVLSFAIRYYKCVAGVMITASHNPKEYNGYKAYWEDGAQI------------TAPHDANIIAEVEKI 182
Cdd:PTZ00302 51 AYRVGILAALRSFLYGGKRAKRGNKSVGVMITASHNPIQDNGVKIIDPDGGMLeeswekictdfaNARTGEDLVSVLMDC 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1309054204 183 ---TDISMVRFKGENLDIHLK------GQEIDDAYLKAVMSL--TLSPEIVKKHNHFKIVYTP-LH 236
Cdd:PTZ00302 131 lteHGIKLSNLKLDLNKSNCSkakvhvGRDTRPSSPELVSALlrGLKLLIGSNVRNFGIVTTPqLH 196
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
107-158 |
3.39e-04 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 43.47 E-value: 3.39e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1309054204 107 TASVFASNGFRVYLFDELRptpvlSFAIRYykcVAGVMITASHNPKEYNGYK 158
Cdd:PLN02895 34 DASLLESTVFRVGILAALR-----SLKTGA---ATGLMITASHNPVSDNGVK 77
|
|
| |
