|
Name |
Accession |
Description |
Interval |
E-value |
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
7-450 |
0e+00 |
|
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars (e.g. between mannose-1-phosphate and mannose-6-phosphate or glucose-1-phosphate and glucose-6-phosphate) via a bisphosphorylated sugar intermediate. The reaction involves two phosphoryl transfers, with an intervening 180 degree reorientation of the reaction intermediate during catalysis. Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is thus, a simple example of processivity, as defined by multiple rounds of catalysis without release of substrate. Glucose-6-phosphate and glucose-1-phosphate are known to be utilized for energy metabolism and cell surface construction, respectively. PMM/PGM belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the phosphoglucomutases (PGM1 and PGM2). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100091 Cd Length: 443 Bit Score: 613.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 7 IFREYDIRGVVGTEITHRFAYELGRAYGTMAEAQGAQKIVIGYDGRLSSPDLVMGLQEGLKKSGRAVINVGLGPTPMVYF 86
Cdd:cd03089 1 IFRAYDIRGIAGEELTEEIAYAIGRAFGSWLLEKGAKKVVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPVLYF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 87 AQRALNADGAIMITGSHNPAHMNGFKMMLKGVSFFGDNIQKLYKTLTQSDFF--ENAGSIEEVAFEGAYVEYLLEDFKth 164
Cdd:cd03089 81 ATFHLDADGGVMITASHNPPEYNGFKIVIGGGPLSGEDIQALRERAEKGDFAaaTGRGSVEKVDILPDYIDRLLSDIK-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 165 yETSRPLRVVWDVGNGAMGNALQRLLKKMPGEHIVLNGTIDGHFPAHHPDPTVPENLVELQQTVLSRKADLGIAFDGDGD 244
Cdd:cd03089 159 -LGKRPLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCEPDGTFPNHHPDPTDPENLEDLIAAVKENGADLGIAFDGDGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 245 RLGVVDETAQIIWGDQLLILFAEEVLKTHPGATVLADVKASQVLFDKIKEMGGNPLMSRTGHSLIKTKMKELSSPLAGEM 324
Cdd:cd03089 238 RLGVVDEKGEIIWGDRLLALFARDILKRNPGATIVYDVKCSRNLYDFIEEAGGKPIMWKTGHSFIKAKMKETGALLAGEM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 325 SGHVFFGDRNFGFDDALYAALRLCGIVGMKEKPLSAWRLSLPKTYATPELHIQAQDVDKFKVIQSIRVELEKNNIDFIDV 404
Cdd:cd03089 318 SGHIFFKDRWYGFDDGIYAALRLLELLSKSGKTLSELLADLPKYFSTPEIRIPVTEEDKFAVIERLKEHFEFPGAEIIDI 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1189039216 405 DGVRVVKKNGWWLLRASNTQEILVGRVEALSEKVLGELKDDLESHL 450
Cdd:cd03089 398 DGVRVDFEDGWGLVRASNTEPVLVLRFEADTEEGLEEIKAELRKLL 443
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
1-453 |
3.83e-160 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 460.44 E-value: 3.83e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 1 MSYPqKIFREYDIRGVVGTEITHRFAYELGRAYGTMAEAQGAQKIVIGYDGRLSSPDLVMGLQEGLKKSGRAVINVGLGP 80
Cdd:COG1109 1 MTYK-KLFGTDGIRGIVGEELTPEFVLKLGRAFGTYLKEKGGPKVVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 81 TPMVYFAQRALNADGAIMITGSHNPAHMNGFKMML-KGVSFFGDNIQKLYKTLTQSDFF----ENAGSIEEVA-FEGAYV 154
Cdd:COG1109 80 TPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDaDGGKLSPEEEKEIEALIEKEDFRraeaEEIGKVTRIEdVLEAYI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 155 EYLLEDFKTHyETSRPLRVVWDVGNGAMGNALQRLLKKMPGEHIVLNGTIDGHFPAHHPDPTvPENLVELQQTVLSRKAD 234
Cdd:COG1109 160 EALKSLVDEA-LRLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFPNHNPNPE-PENLEDLIEAVKETGAD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 235 LGIAFDGDGDRLGVVDETAQIIWGDQLLILFAEEVLKTHPGATVLADVKASQVLFDKIKEMGGNPLMSRTGHSLIKTKMK 314
Cdd:COG1109 238 LGIAFDGDADRLGVVDEKGRFLDGDQLLALLARYLLEKGPGGTVVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKMR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 315 ELSSPLAGEMSGHVFFGDrNFGFDDALYAALRLCGIVGMKEKPLSAWRLSLPKtYATPELHIQAQDVDKF-KVIQSIRVE 393
Cdd:COG1109 318 ETGAVLGGEESGGIIFPD-FVPTDDGILAALLLLELLAKQGKSLSELLAELPR-YPQPEINVRVPDEEKIgAVMEKLREA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189039216 394 LEKnNIDFIDVDGVRVVKKNG-WWLLRASNTQEILVGRVEALSEKVLGELKDDLESHLKNY 453
Cdd:COG1109 396 VED-KEELDTIDGVKVDLEDGgWVLVRPSGTEPLLRVYAEAKDEEEAEELLAELAELVEEA 455
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
6-448 |
1.50e-113 |
|
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: 341.03 E-value: 1.50e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 6 KIFREYDIRGVVGTEITHRFAYELGRAYGTMAeaqGAQKIVIGYDGRLSSPDLVMGLQEGLKKSGRAVINVGLGPTPMVY 85
Cdd:TIGR03990 2 LLFGTSGIRGIVGEELTPELALKVGKAFGTYL---RGGKVVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLGIAPTPTLQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 86 FAQRALNADGAIMITGSHNPAHMNGFKMMLK-GVSFFGDNIQKLYKTLTQSDFF----ENAGSIEEVA-FEGAYVEYLLE 159
Cdd:TIGR03990 79 YAVRELGADGGIMITASHNPPEYNGIKLLNSdGTELSREQEEEIEEIAESGDFEradwDEIGTVTSDEdAIDDYIEAILD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 160 DFKTHYETSRPLRVVWDVGNGAMGNALQRLLKKMPGEHIVLNGTIDGHFPAHHPDPTvPENLVELQQTVLSRKADLGIAF 239
Cdd:TIGR03990 159 KVDVEAIRKKGFKVVVDCGNGAGSLTTPYLLRELGCKVITLNCQPDGTFPGRNPEPT-PENLKDLSALVKATGADLGIAH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 240 DGDGDRLGVVDETAQIIWGDQLLILFAEEVLKtHPGATVLADVKASQVLFDKIKEMGGNPLMSRTGHSLIKTKMKELSSP 319
Cdd:TIGR03990 238 DGDADRLVFIDEKGRFIGGDYTLALFAKYLLE-HGGGKVVTNVSSSRAVEDVAERHGGEVIRTKVGEVNVAEKMKEEGAV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 320 LAGEMSGHVFFGDRNFGfDDALYAALRLCGIVGMKEKPLSAWRLSLPKtYATPELHIQAQDVDKFKVIQSIRVELEKNNI 399
Cdd:TIGR03990 317 FGGEGNGGWIFPDHHYC-RDGLMAAALFLELLAEEGKPLSELLAELPK-YPMSKEKVELPDEDKEEVMEAVEEEFADAEI 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1189039216 400 DFIdvDGVRVVKKNGWWLLRASNTQEILVGRVEALSEKVLGELKDDLES 448
Cdd:TIGR03990 395 DTI--DGVRIDFEDGWVLVRPSGTEPIVRIYAEAKTEERAEELLEEGRS 441
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
13-448 |
3.76e-90 |
|
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: 281.00 E-value: 3.76e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 13 IRGVVGTEITHRFAYELGRAYGTMAeaqGAQKIVIGYDGRLSSPDLVMGLQEGLKKSGRAVINVGLGPTPMVYFAQRALN 92
Cdd:cd03087 7 IRGVVGEELTPELALKVGKALGTYL---GGGTVVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDIGIVPTPALQYAVRKLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 93 aDGAIMITGSHNPAHMNGFKMMLK-GVSFFGDNIQKLYKTLTQSDF----FENAGSIEEVafEGA---YVEYLLEDFKTh 164
Cdd:cd03087 84 -DAGVMITASHNPPEYNGIKLVNPdGTEFSREQEEEIEEIIFSERFrrvaWDEVGSVRRE--DSAideYIEAILDKVDI- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 165 yETSRPLRVVWDVGNGAMGNALQRLLKKMPGEHIVLNGTIDGHFPAHHPDPTvPENLVELQQTVLSRKADLGIAFDGDGD 244
Cdd:cd03087 160 -DGGKGLKVVVDCGNGAGSLTTPYLLRELGCKVITLNANPDGFFPGRPPEPT-PENLSELMELVRATGADLGIAHDGDAD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 245 RLGVVDETAQIIWGDQLLILFAEEVLKTHPGATVLAdVKASQVLFDKIKEMGGNPLMSRTGHSLIKTKMKELSSPLAGEM 324
Cdd:cd03087 238 RAVFVDEKGRFIDGDKLLALLAKYLLEEGGGKVVTP-VDASMLVEDVVEEAGGEVIRTPVGDVHVAEEMIENGAVFGGEP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 325 SGHVFFGDRNFGFDDAlYAALRLCGIVGmKEKPLSAWRLSLPKtYATPELHIQAQDVDKFKVIQSIRVELEKNNIDFIDV 404
Cdd:cd03087 317 NGGWIFPDHQLCRDGI-MTAALLLELLA-EEKPLSELLDELPK-YPLLREKVECPDEKKEEVMEAVEEELSDADEDVDTI 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1189039216 405 DGVRVVKKNGWWLLRASNTQEILVGRVEALSEKVLGELKDDLES 448
Cdd:cd03087 394 DGVRIEYEDGWVLIRPSGTEPKIRITAEAKTEERAKELLEEGRS 437
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
8-446 |
1.19e-81 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 259.14 E-value: 1.19e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 8 FREYDIRGVVGTEITHRFAYELGRAYGTMAEAQGAQKIVIGYDGRLSSPDLVMGLQEGLKKSGRAVINVGLGPTPMVYFA 87
Cdd:PRK09542 1 IKAYDVRGVVGEQIDEDLVRDVGAAFARLMRAEGATTVVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIGLASTDQLYFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 88 QRALNADGAiMITGSHNPAHMNGFKMMLKGVSFFG-----DNIQKLyktLTQS--DFFENAGSIEEVAFEGAYVEYLLED 160
Cdd:PRK09542 81 SGLLDCPGA-MFTASHNPAAYNGIKLCRAGAKPVGqdtglAAIRDD---LIAGvpAYDGPPGTVTERDVLADYAAFLRSL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 161 FKThyETSRPLRVVWDVGNGAMGNALQRLLKKMPGEHIVLNGTIDGHFPAHHPDPTVPENLVELQQTVLSRKADLGIAFD 240
Cdd:PRK09542 157 VDL--SGIRPLKVAVDAGNGMGGHTVPAVLGGLPITLLPLYFELDGTFPNHEANPLDPANLVDLQAFVRETGADIGLAFD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 241 GDGDRLGVVDETAQIIWGDQLLILFAEEVLKTHPGATVLADVKASQVLFDKIKEMGGNPLMSRTGHSLIKTKMKELSSPL 320
Cdd:PRK09542 235 GDADRCFVVDERGQPVSPSAVTALVAARELAREPGATIIHNLITSRAVPELVAERGGTPVRTRVGHSFIKALMAETGAIF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 321 AGEMSGHVFFGDRnFGFDDALYAALRLCGIVGMKEKPLSAWRLSLPKTYATPELHIQAQDVDkfKVIQSIRVELEKNNID 400
Cdd:PRK09542 315 GGEHSAHYYFRDF-WGADSGMLAALHVLAALGEQDRPLSELMADYQRYAASGEINSTVADAP--ARMEAVLKAFADRIVS 391
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1189039216 401 FIDVDGVRVVKKNGWWL-LRASNTQEILVGRVEALSEKVLGELKDDL 446
Cdd:PRK09542 392 VDHLDGVTVDLGDGSWFnLRASNTEPLLRLNVEARTEEEVDALVDEV 438
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
8-443 |
8.39e-70 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 228.68 E-value: 8.39e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 8 FREYDIRGVVGTEITHRFAYELGRAYGtmaEAQGAQKIVIGYDGRLSSPDLVMGLQEGLKKSGRAVINVGLGPTPMVYFA 87
Cdd:PRK15414 7 FKAYDIRGKLGEELNEDIAWRIGRAYG---EFLKPKTIVLGGDVRLTSETLKLALAKGLQDAGVDVLDIGMSGTEEIYFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 88 QRALNADGAIMITGSHNPAHMNGFKMMLKGVS-FFGDNIQKLYKTLTQSDFF-----ENAGSIEEVAFEGAYVEYLLEdf 161
Cdd:PRK15414 84 TFHLGVDGGIEVTASHNPMDYNGMKLVREGARpISGDTGLRDVQRLAEANDFppvdeTKRGRYQQINLRDAYVDHLFG-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 162 KTHYETSRPLRVVWDVGNGAMG---NALQRLLKKM--PGEHIVLNGTIDGHFPAHHPDPTVPENLVELQQTVLSRKADLG 236
Cdd:PRK15414 162 YINVKNLTPLKLVINSGNGAAGpvvDAIEARFKALgaPVELIKVHNTPDGNFPNGIPNPLLPECRDDTRNAVIKHGADMG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 237 IAFDGDGDRLGVVDETAQIIWGDQLLILFAEEVLKTHPGATVLADVKASQVLFDKIKEMGGNPLMSRTGHSLIKTKMKEL 316
Cdd:PRK15414 242 IAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPGAKIIHDPRLSWNTVDVVTAAGGTPVMSKTGHAFIKERMRKE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 317 SSPLAGEMSGHVFFgdRNFGF-DDALYAALRLCGIVGMKEKPLSawRLSLPKTYATPEL-HIQAQDVDKFKVIQSIRVEL 394
Cdd:PRK15414 322 DAIYGGEMSAHHYF--RDFAYcDSGMIPWLLVAELVCLKGKTLG--ELVRDRMAAFPASgEINSKLAQPVEAINRVEQHF 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1189039216 395 EKNNIDFIDVDGVRVVKKNGWWLLRASNTQEILVGRVEALSEKVLGELK 443
Cdd:PRK15414 398 SREALAVDRTDGISMTFADWRFNLRSSNTEPVVRLNVESRGDVPLMEAR 446
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
13-444 |
3.61e-63 |
|
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate guanyltransferase domain in a protein of unknown function that is found in both prokaryotes and eukaryotes. This domain belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100096 Cd Length: 445 Bit Score: 211.01 E-value: 3.61e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 13 IRGVVGTEITHRFAYELGRAYGTMAEAQGAQK-IVIGYDGRLSSPDLVMGLQEGLKKSGRAVINVGLGPTPMVYFAQRAL 91
Cdd:cd05803 7 IRGIVGEGLTPEVITRYVAAFATWQPERTKGGkIVVGRDGRPSGPMLEKIVIGALLACGCDVIDLGIAPTPTVQVLVRQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 92 NADGAIMITGSHNPAHMNGFKMMLKGVSFF-GDNIQKLYKTLTQSDFF----ENAGSIeeVAFEGAYVEYLLEDFKTHY- 165
Cdd:cd05803 87 QASGGIIITASHNPPQWNGLKFIGPDGEFLtPDEGEEVLSCAEAGSAQkagyDQLGEV--TFSEDAIAEHIDKVLALVDv 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 166 ----ETSRPLRVVWDVGNGAMGNALQRLLKKMPGEHIVLNGTIDGHFPaHHPDPTvPENLVELQQTVLSRKADLGIAFDG 241
Cdd:cd05803 165 dvikIRERNFKVAVDSVNGAGGLLIPRLLEKLGCEVIVLNCEPTGLFP-HTPEPL-PENLTQLCAAVKESGADVGFAVDP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 242 DGDRLGVVDETAQIIWGDQLLILFAEEVLKTHPGAT-VLADVKASQVLFDKIKEMGGNPLMSRTGHSLIKTKMKELSSPL 320
Cdd:cd05803 243 DADRLALVDEDGRPIGEEYTLALAVDYVLKYGGRKGpVVVNLSTSRALEDIARKHGVPVFRSAVGEANVVEKMKEVDAVI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 321 AGEMSGHVFFGDRNFGFDDALYAALRLCGIVGMkEKPLSAWRLSLPKTYatpelhIQAQDVD-KFKVIQSIRVELEKNNI 399
Cdd:cd05803 323 GGEGNGGVILPDVHYGRDSLVGIALVLQLLAAS-GKPLSEIVDELPQYY------ISKTKVTiAGEALERLLKKLEAYFK 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1189039216 400 DF-ID-VDGVRVVKKNGWWLLRASNTQEILVGRVEALSEKVLGELKD 444
Cdd:cd05803 396 DAeAStLDGLRLDSEDSWVHVRPSNTEPIVRIIAEAPTQDEAEALAD 442
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
13-446 |
2.51e-61 |
|
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: 205.80 E-value: 2.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 13 IRGVVGTEITHRFAYELGRAYGTM-AEAQGAQKIVIGYDGRLSSPDLVMGLQEGLKKSGRAVINVGLGPTPMVYFAQRAL 91
Cdd:cd05802 7 IRGVANEPLTPELALKLGRAAGKVlGKGGGRPKVLIGKDTRISGYMLESALAAGLTSAGVDVLLLGVIPTPAVAYLTRKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 92 NADGAIMITGSHNPAHMNGFKmmlkgvsFFGDNIQKLyktltqSDFFENA------------------GSIEEVAF-EGA 152
Cdd:cd05802 87 RADAGVVISASHNPFEDNGIK-------FFSSDGYKL------PDEVEEEiealidkelelpptgekiGRVYRIDDaRGR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 153 YVEYLLEDFKTHYETSrpLRVVWDVGNGAMGNALQRLLKKMPGEHIVLNGTIDG-----HFPAHHPDPtvpenlveLQQT 227
Cdd:cd05802 154 YIEFLKSTFPKDLLSG--LKIVLDCANGAAYKVAPEVFRELGAEVIVINNAPDGlninvNCGSTHPES--------LQKA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 228 VLSRKADLGIAFDGDGDRLGVVDETAQIIWGDQLLILFAEEVLKTH--PGATVLADVKASQVLFDKIKEMGGNPLMSRTG 305
Cdd:cd05802 224 VLENGADLGIAFDGDADRVIAVDEKGNIVDGDQILAICARDLKERGrlKGNTVVGTVMSNLGLEKALKELGIKLVRTKVG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 306 HSLIKTKMKELSSPLAGEMSGHVFFGDRNF-GfdDALYAALRLCGIVGMKEKPLSAWRLSLPKtyaTPELHIQAQDVDKF 384
Cdd:cd05802 304 DRYVLEEMLKHGANLGGEQSGHIIFLDHSTtG--DGLLTALQLLAIMKRSGKSLSELASDMKL---YPQVLVNVRVKDKK 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189039216 385 KVIQSIRVELEKNNIDFIDVDGVRVvkkngwwLLRASNTqEILVgRV--EALSEKVLGELKDDL 446
Cdd:cd05802 379 ALLENPRVQAAIAEAEKELGGEGRV-------LVRPSGT-EPLI-RVmvEGEDEELVEKLAEEL 433
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
7-444 |
7.19e-59 |
|
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: 197.19 E-value: 7.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 7 IFREYDIRGVVGTEITHRFAYELGRAYGTMaeaqgaqkivigydgrlsspdlvmglqeglkksgravinvglgptpmvyf 86
Cdd:cd03084 1 IFGTSGVRGVVGDDITPETAVALGQAIGST-------------------------------------------------- 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 87 aqralnadGAIMITGSHNPAHMNGFKMML-KGVSFFGDNIQKLYKTLTQSDFF-----ENAGSIEEVAFEGAYVEYLLED 160
Cdd:cd03084 31 --------GGIMITASHNPPEDNGIKFVDpDGEPIASEEEKAIEDLAEKEDEPsavayELGGSVKAVDILQRYFEALKKL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 161 FKTHYETSRPLRVVWDVGNGAMGNALQRLLKKMPGEHIVLNGTIDGHFPAHHPDPTVPENLVELQQTVLSRKADLGIAFD 240
Cdd:cd03084 103 FDVAALSNKKFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCEPDGNFGNINPDPGSETNLKQLLAVVKAEKADFGVAFD 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 241 GDGDRLGVVDETAQIIWGDQLLILFAEEVLKTH-PGATVLADVKASQVLFDKIKEMGGNPLMSRTGHSLIKTKMKELSSP 319
Cdd:cd03084 183 GDADRLIVVDENGGFLDGDELLALLAVELFLTFnPRGGVVKTVVSSGALDKVAKKLGIKVIRTKTGFKWVGEAMQEGDVV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 320 LAGEMSGHVFFGDrNFGFDDALYAALRLCGIVGMKEKPLSAWRLSLPKTYATPelhiqaqdvdkfkviqsirveleknni 399
Cdd:cd03084 263 LGGEESGGVIFPE-FHPGRDGISAALLLLEILANLGKSLSELFSELPRYYYIR--------------------------- 314
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1189039216 400 dfidvdgvrvVKKNGWWLLRASNTQEILVGRVEALSEKVLGELKD 444
Cdd:cd03084 315 ----------LKVRGWVLVRASGTEPAIRIYAEADTQEDVEQIKK 349
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
14-450 |
3.05e-52 |
|
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: 182.37 E-value: 3.05e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 14 RGVVGTEIT----HRFAyelgRAYGTM--AEAQGAQKIVIGYDGRLSSPDLVMGLQEGLKKSGravINVGLG----PTPM 83
Cdd:cd05800 9 RGIIAEDFTfenvRRVA----QAIADYlkEEGGGGRGVVVGYDTRFLSEEFARAVAEVLAANG---IDVYLSdrpvPTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 84 VYFAQRALNADGAIMITGSHNPAHMNGFKmmLKGvsFFG--------DNIQKLYKTLTQSDFFE-NAGSIEEVAFEGAYV 154
Cdd:cd05800 82 VSWAVKKLGAAGGVMITASHNPPEYNGVK--VKP--AFGgsalpeitAAIEARLASGEPPGLEArAEGLIETIDPKPDYL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 155 EYLLEDFKTHYETSRPLRVVWDVGNGAMGNALQRLLKKMPGEHIVLNGTIDGHFPAHHPDPTvPENLVELQQTVLSRKAD 234
Cdd:cd05800 158 EALRSLVDLEAIREAGLKVVVDPMYGAGAGYLEELLRGAGVDVEEIRAERDPLFGGIPPEPI-EKNLGELAEAVKEGGAD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 235 LGIAFDGDGDRLGVVDETAQIIWGDQLLILFAEEVLKT--HPGA---TVladvkASQVLFDKIKEMGGNPLM-SRTGHSL 308
Cdd:cd05800 237 LGLATDGDADRIGAVDEKGNFLDPNQILALLLDYLLENkgLRGPvvkTV-----STTHLIDRIAEKHGLPVYeTPVGFKY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 309 IKTKMKELSSPLAGEMSGHVFFGD----RnfgfdDALYAALRLCGIVGMKEKPLSAWRLSL-----PKTYATPELHIQAQ 379
Cdd:cd05800 312 IAEKMLEEDVLIGGEESGGLGIRGhipeR-----DGILAGLLLLEAVAKTGKPLSELVAELeeeygPSYYDRIDLRLTPA 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189039216 380 DVDKFKVIQSIRVELEKNN---IDFIDVDGVRVVKKNGWWLL-RASNTQEILvgRV--EALSEKVLGELKDDLESHL 450
Cdd:cd05800 387 QKEAILEKLKNEPPLSIAGgkvDEVNTIDGVKLVLEDGSWLLiRPSGTEPLL--RIyaEAPSPEKVEALLDAGKKLA 461
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
13-446 |
3.31e-49 |
|
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: 174.09 E-value: 3.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 13 IRGVVGTE-ITHRFAYELGRAYGTMAEAQ--GAQKIVIGYDGRLSSPDLVMGLQEGLKKSGRAVINVGLGPTPMVYFAQR 89
Cdd:TIGR01455 6 VRGRAGQEpLTAELALLLGAAAGRVLRQGrdTAPRVVIGKDTRLSGYMLENALAAGLNSAGVDVLLLGPLPTPAVAYLTR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 90 ALNADGAIMITGSHNPAHMNGFKmmlkgvsFFGDNIQKLYKTLTQS--------DFFENAGS------IEEVAFEGAYVE 155
Cdd:TIGR01455 86 TLRADAGVMISASHNPYEDNGIK-------FFGPGGFKLDDATEAAiealldeaDPLPRPESeglgrvKRYPDAVGRYIE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 156 YLLEDFkTHYETSRPLRVVWDVGNGAMGNALQRLLKKMPGEHIVLNGTIDG-----HFPAHHPDPtvpenlveLQQTVLS 230
Cdd:TIGR01455 159 FLKSTL-PRGLTLSGLKVVLDCANGAAYKVAPHVFRELGAEVIAIGVEPDGlnindGCGSTHLDA--------LQKAVRE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 231 RKADLGIAFDGDGDRLGVVDETAQIIWGDQLLILFAEEVLKTH--PGATVLADVKASQVLFDKIKEMGGNPLMSRTGHSL 308
Cdd:TIGR01455 230 HGADLGIAFDGDADRVLAVDANGRIVDGDQILYIIARALKESGelAGNTVVATVMSNLGLERALEKLGLTLIRTAVGDRY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 309 IKTKMKELSSPLAGEMSGHVFFGDRNFGfDDALYAALRLCGIVGMKEKPLSAwrlslpktyATPELHIQAQdvdkfkVIQ 388
Cdd:TIGR01455 310 VLEEMRESGYNLGGEQSGHIILLDYSTT-GDGIVSALQVLTIMKKSGSTLSE---------LAAEFVPYPQ------TLV 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189039216 389 SIRVELEKNNIDFID------VDGVRVVKKNGWWLLRASNTQEILVGRVEALSEKVLGELKDDL 446
Cdd:TIGR01455 374 NVRVADRKLAAAEAPavkaaiEDAEAELGGTGRILLRPSGTEPLIRVMVEAADEELVQQLADTL 437
|
|
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
7-417 |
9.83e-43 |
|
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: 156.25 E-value: 9.83e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 7 IFREYDIRGVVGTEITHRFAYELGRAYGTMAEAqGAqKIVIGYDGRLSSPDLVMGLQEGLKKSGRAVINVGLGPTPMVYF 86
Cdd:cd05805 1 LFGGRGVSGLINVDITPEFATRLGAAYGSTLPP-GS-TVTVSRDASRASRMLKRALISGLLSTGVNVRDLGALPLPVARY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 87 AQRALNADGAIMI-TGSHNPAHMNgfkmmlkgVSFF---GDNIQ-----KLYKTLTQSDF----FENAGSIEEVA-FEGA 152
Cdd:cd05805 79 AIRFLGASGGIHVrTSPDDPDKVE--------IEFFdsrGLNISramerKIENAFFREDFrrahVDEIGDITEPPdFVEY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 153 YVEYLLEDFKTHYETSRPLRVVWDVGNGAMGNALQRLLKKMPGEHIVLNGTIDghFPAHHPDPTVPENLVELQQTVLSRK 232
Cdd:cd05805 151 YIRGLLRALDTSGLKKSGLKVVIDYAYGVAGIVLPGLLSRLGCDVVILNARLD--EDAPRTDTERQRSLDRLGRIVKALG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 233 ADLGIAFDGDGDRLGVVDETAQIIWGDQLLILFAEEVLKTHPGATVLADVKASQVLFDKIKEMGGNPLMSRTGHSLIKTK 312
Cdd:cd05805 229 ADFGVIIDPNGERLILVDEAGRVISDDLLTALVSLLVLKSEPGGTVVVPVTAPSVIEQLAERYGGRVIRTKTSPQALMEA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 313 MKElSSPLAGEMSGHVFFGDRNFGFdDALYAALRLCGIVGMKEKPLSAWRLSLPKTY-ATPELHIQAQdvDKFKVIQSIR 391
Cdd:cd05805 309 ALE-NVVLAGDGDGGFIFPEFHPGF-DAIAALVKILEMLARTNISLSQIVDELPRFYvLHKEVPCPWE--AKGRVMRRLI 384
|
410 420
....*....|....*....|....*.
gi 1189039216 392 VELEKNNIDFIdvDGVRVVKKNGWWL 417
Cdd:cd05805 385 EEAPDKSIELI--DGVKIYEDDGWVL 408
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
12-445 |
1.34e-40 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 152.90 E-value: 1.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 12 DIRGVV--GTE-----ITHRFAYELGRAYG------TMAEAQGAQKIVIGYDGRLSSPDLVMGLQEGLKKSGRAVINVGL 78
Cdd:PLN02371 72 DIRGVAveGVEgepvtLTPPAVEAIGAAFAewllekKKADGSGELRVSVGRDPRISGPRLADAVFAGLASAGLDVVDMGL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 79 GPTPMVYFAQRA--LNADGAIMITGSHNPAHMNGFKMMLKG-------VSFFGDNIQKLYK----TLTQSDFFENAGSIE 145
Cdd:PLN02371 152 ATTPAMFMSTLTerEDYDAPIMITASHLPYNRNGLKFFTKDgglgkpdIKDILERAARIYKewsdEGLLKSSSGASSVVC 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 146 EVAFEGAYVEYLLEDFK------THYETsrPLR---VVWDVGNGAMGNALQRLLKKMpgehivlnGTI---------DGH 207
Cdd:PLN02371 232 RVDFMSTYAKHLRDAIKegvghpTNYET--PLEgfkIVVDAGNGAGGFFAEKVLEPL--------GADtsgslflepDGM 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 208 FPAHHPDPTVPENLVELQQTVLSRKADLGIAFDGDGDRLGVVDETAQIIWGDQLLILFAEEVLKTHPGATVLADVKASQV 287
Cdd:PLN02371 302 FPNHIPNPEDKAAMSATTQAVLANKADLGIIFDTDVDRSAVVDSSGREINRNRLIALMSAIVLEEHPGTTIVTDSVTSDG 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 288 LFDKIKEMGGNPLMSRTGHSLIKTKMKELS-----SPLAGEMSGHVFFGDrNFGFDDALY---------AALRLCG---- 349
Cdd:PLN02371 382 LTTFIEKKGGKHHRFKRGYKNVIDKGVRLNsdgeeTHLMIETSGHGALKE-NHFLDDGAYlavkiiielVRMRAAGaggg 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 350 ----IVGMKEKPLSA-WRLslpKTYATPElHIQA---QDVDKFKviQSIRvELEKNNIDFIDVDGVRVVKKN----GWWL 417
Cdd:PLN02371 461 lgdlIEDLEEPLEAVeLRL---KILDEGK-DFKAygeEVLEHLR--NSIE-SDGKLEGAPVNYEGVRVSDEGegfgGWFL 533
|
490 500 510
....*....|....*....|....*....|....*.
gi 1189039216 418 LRAS--------NTQEILVGRVEALSEKVLGELKDD 445
Cdd:PLN02371 534 LRQSlhdpviplNIESSSPGGAQKMALVVLTWLKEF 569
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
6-137 |
6.07e-36 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 129.65 E-value: 6.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 6 KIFREYDIRGVVG-TEITHRFAYELGRAYGT-MAEAQGAQKIVIGYDGRLSSPDLVMGLQEGLKKSGRAVINVGLGPTPM 83
Cdd:pfam02878 2 QLFGTSGIRGKVGvGELTPEFALKLGQAIASyLRAQGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTPA 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1189039216 84 VYFAQRALNADGAIMITGSHNPAHMNGFKMMLK-GVSFFGDNIQKLYKTLTQSDF 137
Cdd:pfam02878 82 VSFATRKLKADGGIMITASHNPPEYNGIKVFDSnGGPIPPEVEKKIEAIIEKEDF 136
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
13-272 |
5.00e-31 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 124.09 E-value: 5.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 13 IRGVVGTE-ITHRFAYELGRAYGTMAEAQGAQKIVIGYDGRLSSPDLVMGLQEGLKKSGRAVINVGLGPTPMVYFAQRAL 91
Cdd:PRK10887 9 IRGKVGQApITPDFVLKLGWAAGKVLARQGRPKVLIGKDTRISGYMLESALEAGLAAAGVDVLLTGPMPTPAVAYLTRTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 92 NADGAIMITGSHNPAHMNGFKmmlkgvsFFG-------DNIQ-----KLYKTLT--QSDFFENAGSIEEVAfeGAYVEYL 157
Cdd:PRK10887 89 RAEAGIVISASHNPYYDNGIK-------FFSadgtklpDEVElaieaELDKPLTcvESAELGKASRINDAA--GRYIEFC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 158 LEDFKTHYeTSRPLRVVWDVGNGAMGNALQRLLKKMPGEHIVLNGTIDG-----HFPAHHPDptvpenlvELQQTVLSRK 232
Cdd:PRK10887 160 KSTFPNEL-SLRGLKIVVDCANGATYHIAPNVFRELGAEVIAIGCEPNGlnindECGATDPE--------ALQAAVLAEK 230
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1189039216 233 ADLGIAFDGDGDRLGVVDETAQIIWGDQLLILFAEEVLKT 272
Cdd:PRK10887 231 ADLGIAFDGDGDRVIMVDHLGNLVDGDQLLYIIARDRLRR 270
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
152-251 |
7.10e-30 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 112.00 E-value: 7.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 152 AYVEYLLEDFKTHYETSRPLRVVWDVGNGAMGNALQRLLKKMPGEHIVLNGTIDGHFPAHHPDPTVPENLVELQQTVLSR 231
Cdd:pfam02879 1 AYIDHLLELVDSEALKKRGLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDPDFPTRAPNPEEPEALALLIELVKSV 80
|
90 100
....*....|....*....|
gi 1189039216 232 KADLGIAFDGDGDRLGVVDE 251
Cdd:pfam02879 81 GADLGIATDGDADRLGVVDE 100
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
257-369 |
2.96e-27 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 105.22 E-value: 2.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 257 WGDQLLILFAEEVLKT---HPGATVLADVKASQVLFDKIKEMGGNPLMSRTGHSLIKTKMKELSSPLAGEMSGHVFFGDR 333
Cdd:pfam02880 1 DGDQILALLAKYLLEQgklPPGAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLDH 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 1189039216 334 NFgFDDALYAALRLCGIVGMKEKPLSAWRLSLPKTY 369
Cdd:pfam02880 81 AT-TKDGILAALLVLEILARTGKSLSELLEELPEKY 115
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
13-271 |
6.95e-21 |
|
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: 94.88 E-value: 6.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 13 IRGVVG-----------TEITHRFAYELGRAYGtmaeAQGAQKIVIGYDGRLSSPD------LVMgLQEGLKksgrAVIN 75
Cdd:cd05799 9 LRGKMGagtnrmndytvRQATQGLANYLKKKGP----DAKNRGVVIGYDSRHNSREfaeltaAVL-AANGIK----VYLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 76 VGLGPTPMVYFAQRALNADGAIMITGSHNPAHMNGFKMMLKG----VSFFGDNIQK-----LYKTLTQSDFFENAGSIEE 146
Cdd:cd05799 80 DDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDgaqiIPPHDAEIAEeieavLEPLDIKFEEALDSGLIKY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 147 VAFE--GAYVEYLLED-FKTHYETSRPLRVVWDVGNGAMGNALQRLLKKMPGEHIVL---NGTIDGHFP-AHHPDPTVPE 219
Cdd:cd05799 160 IGEEidDAYLEAVKKLlVNPELNEGKDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVveeQAEPDPDFPtVKFPNPEEPG 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1189039216 220 NLVELQQTVLSRKADLGIAFDGDGDRLGVV----DETAQIIWGDQLLILFAEEVLK 271
Cdd:cd05799 240 ALDLAIELAKKVGADLILATDPDADRLGVAvkdkDGEWRLLTGNEIGALLADYLLE 295
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
36-245 |
5.78e-13 |
|
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: 70.71 E-value: 5.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 36 MAEAQGAQKIVIGYDGRLSSPdlvmglqeglkkSGRAVInvglgptpmvyfaqRALNADGAIMITGSHNPAHMNG-Fkmm 114
Cdd:cd03085 72 IAAANGVGKVVVGQNGLLSTP------------AVSAVI--------------RKRKATGGIILTASHNPGGPEGdF--- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 115 lkGVSF-----------FGDNIQKLYKTLTQSDFFENA----GSIEEVAFEG------------AYVEYLLE--DFKT-- 163
Cdd:cd03085 123 --GIKYntsnggpapesVTDKIYEITKKITEYKIADDPdvdlSKIGVTKFGGkpftvevidsveDYVELMKEifDFDAik 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 164 HYETSRPLRVVWDVGNGAMGNALQRLLKKMPG--EHIVLNGTIDGHFPAHHPDPtvpeNLV---ELQQTVLSRKADLGIA 238
Cdd:cd03085 201 KLLSRKGFKVRFDAMHGVTGPYAKKIFVEELGapESSVVNCTPLPDFGGGHPDP----NLTyakDLVELMKSGEPDFGAA 276
|
....*..
gi 1189039216 239 FDGDGDR 245
Cdd:cd03085 277 SDGDGDR 283
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
14-112 |
3.90e-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: 68.00 E-value: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 14 RGVVgTEITHRFAYELGRAYGT-MAEAQGAQKIVIGYDGRLSSPDLVMGLQEGLKKSGRAVINVGLGPTPMVYFAQRALN 92
Cdd:cd03088 8 RGLV-TDLTDEVCYAYTRAFLQhLESKFPGDTVAVGRDLRPSSPRIAAACAAALRDAGFRVVDCGAVPTPALALYAMKRG 86
|
90 100
....*....|....*....|
gi 1189039216 93 AdGAIMITGSHNPAHMNGFK 112
Cdd:cd03088 87 A-PAIMVTGSHIPADRNGLK 105
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
35-266 |
4.86e-11 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 64.70 E-value: 4.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 35 TMAEAQGAQKIVIGYDGRLSSPDL------VMgLQEGLKKS--GRAVinvglgPTPMVYFAQRALNADGAIMITGSHNPA 106
Cdd:PTZ00150 82 TFGQALKSRGVVIGYDGRYHSRRFaeitasVF-LSKGFKVYlfGQTV------PTPFVPYAVRKLKCLAGVMVTASHNPK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 107 HMNGFKM-----------MLKGVSFFgdnIQKLYKTLTQSDFFENAGSIEEVAFE--GAYVEYLLEDFKTHYETSRPLRV 173
Cdd:PTZ00150 155 EDNGYKVywsngaqiippHDKNISAK---ILSNLEPWSSSWEYLTETLVEDPLAEvsDAYFATLKSEYNPACCDRSKVKI 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 174 VWDvgngAMGNALQRLLKKMpgEHIV-LNGTI--------DGHFPA-HHPDPTVPENLVELQ-QTVLSRKADLGIAFDGD 242
Cdd:PTZ00150 232 VYT----AMHGVGTRFVQKA--LHTVgLPNLLsvaqqaepDPEFPTvTFPNPEEGKGALKLSmETAEAHGSTVVLANDPD 305
|
250 260
....*....|....*....|....*..
gi 1189039216 243 GDRLGVV---DETAQIIWGDQLLILFA 266
Cdd:PTZ00150 306 ADRLAVAeklNNGWKIFTGNELGALLA 332
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
44-266 |
2.14e-07 |
|
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: 52.98 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 44 KIVIGYDGRLSSPDLVMGLQEGLKKSGRAVINVGLGPTPMVYFAQRALNADGAimitgshnpahmngfkmmlkgvsFFGD 123
Cdd:cd03086 104 NVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYLVRAANTEGA-----------------------YGEP 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 124 NIQKLYKTLTQsdffenagsieevAFEGAYveYLLEDFKTHYETsrplrVVWDVGNGAMGNALQRLLKKMPGEHIV--LN 201
Cdd:cd03086 161 TEEGYYEKLSK-------------AFNELY--NLLQDGGDEPEK-----LVVDCANGVGALKLKELLKRLKKGLSVkiIN 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 202 GTIDGHFP------AHHpdptvpenlVELQQT-----VLSRKADLGIAFDGDGDRLgvV------DETAQIIWGDQLLIL 264
Cdd:cd03086 221 DGEEGPELlndgcgADY---------VKTKQKpprgfELKPPGVRCCSFDGDADRL--VyfypdsSNKFHLLDGDKIATL 289
|
..
gi 1189039216 265 FA 266
Cdd:cd03086 290 FA 291
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
44-267 |
3.69e-07 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 52.35 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 44 KIVIGYDGRLSSPDLVMGLQEGLKKSGRA-VINVGLGPTPMVYFAQRALNA---DGAIMITGSHNPAHMNGFKMMLKGVS 119
Cdd:PTZ00302 154 KVHVGRDTRPSSPELVSALLRGLKLLIGSnVRNFGIVTTPQLHFLVAFANGlgvDVVESSDELYYAYLLAAFKELYRTLQ 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 120 FfgdniqklyktLTQSDFFENagsieevafegayveylledfkthyetsRPLRVVWDVGNGAMGNALQRL---LKKMPGE 196
Cdd:PTZ00302 234 E-----------GGPVDLTQN----------------------------NSKILVVDCANGVGGYKIKRFfeaLKQLGIE 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 197 HIVLNGTIDGHFP------AHHPDPT--VPENLVELQQTVLSRKAdlgiAFDGDGDRL------GVVDETAQIIWGDQLL 262
Cdd:PTZ00302 275 IIPININCDEEELlndkcgADYVQKTrkPPRAMKEWPGDEETRVA----SFDGDADRLvyffpdKDGDDKWVLLDGDRIA 350
|
....*
gi 1189039216 263 ILFAE 267
Cdd:PTZ00302 351 ILYAM 355
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
405-451 |
1.79e-05 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 42.64 E-value: 1.79e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1189039216 405 DGVRVVKKNGWWL-LRASNTQEILVGRVEALSEKVLGELKDDLESHLK 451
Cdd:pfam00408 24 DAEKILGEDGRRLdVRPSGTEPVLRVMVEGDSDEELARLADEIADLLE 71
|
|
| 2A0601 |
TIGR00914 |
heavy metal efflux pump, CzcA family; This model represents a family of H+/heavy metal cation ... |
243-389 |
2.05e-03 |
|
heavy metal efflux pump, CzcA family; This model represents a family of H+/heavy metal cation antiporters. This family is one of several subfamilies within the scope of pfam00873. [Cellular processes, Detoxification, Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 129992 [Multi-domain] Cd Length: 1051 Bit Score: 40.90 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189039216 243 GDRLGVVDETAQIIwgdqllilfaEEVLKTHPGATvlaDVKASQ--------VLFDKIKemggnplMSRTGHSlIKTKMK 314
Cdd:TIGR00914 690 GDDLDDLDATAEKI----------SAVLKGVPGAA---DVKVEQttglpyltVEIDREK-------AARYGLT-VGDVQD 748
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189039216 315 ELSSPLAGEMSGHVFFGDRNFGFddalyaALRLCGIVGMKEKPLSAWRLSLPKTYATPELHIQAQDVDKFKVIQS 389
Cdd:TIGR00914 749 TVATAVGGRMSGETFEGDRRFDI------VIRLPESLRESPQALRQLPIPLPLSEDARKQFIPLSDVADLRVSPG 817
|
|
| |
