|
Name |
Accession |
Description |
Interval |
E-value |
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
5-470 |
0e+00 |
|
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: 635.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 5 IIFGTDGWRAVMADQFTMENVRTVAKAIACYTEENGWIDRGIIVGYDTRFMGRMFAQEVVRVLTAHSILSFLVSEPTPTP 84
Cdd:cd05800 1 IKFGTDGWRGIIAEDFTFENVRRVAQAIADYLKEEGGGGRGVVVGYDTRFLSEEFARAVAEVLAANGIDVYLSDRPVPTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 85 VVAFGVKHFGVSGAVMLTASHNPAEYNGIKYIPEYAGPASPDITQRLEVLIQQIEASGEqvqtrsieEAKNGKLYQPIHL 164
Cdd:cd05800 81 AVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARLASGEPPGL--------EARAEGLIETIDP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 165 KPHYEAHIRRLIRMDVLQRANLTVVVDAMHGAGSGYMSALLQEAGVAVKSIREERDPLFGGGLPEPNEHHLAELSRQVLV 244
Cdd:cd05800 153 KPDYLEALRSLVDLEAIREAGLKVVVDPMYGAGAGYLEELLRGAGVDVEEIRAERDPLFGGIPPEPIEKNLGELAEAVKE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 245 ENADLGVANDGDADRFGVVDRQGRYLSPNEVLTLLTYHMVKNRNGQGKVIRTVATTHQLDRICEHYGLELIETPVGFKYI 324
Cdd:cd05800 233 GGADLGLATDGDADRIGAVDEKGNFLDPNQILALLLDYLLENKGLRGPVVKTVSTTHLIDRIAEKHGLPVYETPVGFKYI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 325 GAQMLRGNVLIGGEESGGASILGHIPEKDGILMNLLIAEMCAVEGKSLDEIKADIHRQFGRMYSSRLDIRFK--QKEAFL 402
Cdd:cd05800 313 AEKMLEEDVLIGGEESGGLGIRGHIPERDGILAGLLLLEAVAKTGKPLSELVAELEEEYGPSYYDRIDLRLTpaQKEAIL 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1343199007 403 LRFKEKPPHTIAGYAVEAIHTQDGFKLLLEGGHWVLIRPSGTEPLLRIYCEATGSEELERLKEAVRDW 470
Cdd:cd05800 393 EKLKNEPPLSIAGGKVDEVNTIDGVKLVLEDGSWLLIRPSGTEPLLRIYAEAPSPEKVEALLDAGKKL 460
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
1-473 |
2.57e-169 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 484.32 E-value: 2.57e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 1 MEKQIIFGTDGWRAVMADQFTMENVRTVAKAIACYTEENGwiDRGIIVGYDTRFMGRMFAQEVVRVLTAHSILSFLVsEP 80
Cdd:COG1109 1 MTYKKLFGTDGIRGIVGEELTPEFVLKLGRAFGTYLKEKG--GPKVVVGRDTRLSSPMLARALAAGLASAGIDVYDL-GL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 81 TPTPVVAFGVKHFGVSGAVMLTASHNPAEYNGIKYIPEYAGPASPDITQRLEVLIQQIEasgeqvqTRSIEEAKNGKLYQ 160
Cdd:COG1109 78 VPTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKED-------FRRAEAEEIGKVTR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 161 PIHLKPHYEAHIRRLIRmDVLQRANLTVVVDAMHGAGSGYMSALLQEAGVAVKSIREERDPLFGGGLPEPNEHHLAELSR 240
Cdd:COG1109 151 IEDVLEAYIEALKSLVD-EALRLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFPNHNPNPEPENLEDLIE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 241 QVLVENADLGVANDGDADRFGVVDRQGRYLSPNEVLTLLTYHMVKnRNGQGKVIRTVATTHQLDRICEHYGLELIETPVG 320
Cdd:COG1109 230 AVKETGADLGIAFDGDADRLGVVDEKGRFLDGDQLLALLARYLLE-KGPGGTVVVTVMSSLALEDIAEKHGGEVVRTKVG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 321 FKYIGAQMLRGNVLIGGEESGGASILGHIPEKDGILMNLLIAEMCAVEGKSLDEIKADIhrqfGRMYSSRLDIRFKQKEA 400
Cdd:COG1109 309 FKYIKEKMRETGAVLGGEESGGIIFPDFVPTDDGILAALLLLELLAKQGKSLSELLAEL----PRYPQPEINVRVPDEEK 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1343199007 401 FLL---RFKEKPPhtiagyAVEAIHTQDGFKLLLEGGHWVLIRPSGTEPLLRIYCEATGSEELERLKEAVRDWFEE 473
Cdd:COG1109 385 IGAvmeKLREAVE------DKEELDTIDGVKVDLEDGGWVLVRPSGTEPLLRVYAEAKDEEEAEELLAELAELVEE 454
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
7-465 |
2.09e-95 |
|
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: 296.73 E-value: 2.09e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 7 FGTDGWRAVMADQFTMENVRTVAKA---IACYTEENG--WIDRGIIVGYDTRFMGRMFAQEVVRVLTAHSILSFLVSEPT 81
Cdd:cd05799 4 FGTAGLRGKMGAGTNRMNDYTVRQAtqgLANYLKKKGpdAKNRGVVIGYDSRHNSREFAELTAAVLAANGIKVYLFDDLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 82 PTPVVAFGVKHFGVSGAVMLTASHNPAEYNGIK-Y-------IPEYAgpaspditqrlEVLIQQIEASGEQVQTRSIEEA 153
Cdd:cd05799 84 PTPLLSFAVRHLGADAGIMITASHNPKEYNGYKvYwedgaqiIPPHD-----------AEIAEEIEAVLEPLDIKFEEAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 154 KNGKL-YQPIHLKPHYEAHIRRLI-RMDVLQRANLTVVVDAMHGAGSGYMSALLQEAGVA-VKSIREER--DPLFGG-GL 227
Cdd:cd05799 153 DSGLIkYIGEEIDDAYLEAVKKLLvNPELNEGKDLKIVYTPLHGVGGKFVPRALKEAGFTnVIVVEEQAepDPDFPTvKF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 228 PEPNEHH---LA-ELSRQVlveNADLGVANDGDADRFGVVDRQG----RYLSPNEVLTLLTYHMVKNRNGQGK------V 293
Cdd:cd05799 233 PNPEEPGaldLAiELAKKV---GADLILATDPDADRLGVAVKDKdgewRLLTGNEIGALLADYLLEQRKEKGKlpknpvI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 294 IRTVATTHQLDRICEHYGLELIETPVGFKYIGAQMLR-----GNVLIGGEESGGASILGHIPEKDGILMNLLIAEMCAV- 367
Cdd:cd05799 310 VKTIVSSELLRKIAKKYGVKVEETLTGFKWIGNKIEElesggKKFLFGFEESIGYLVGPFVRDKDGISAAALLAEMAAYl 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 368 --EGKSLDEIKADIHRQFGRMYSSRLDIRFKQKE------AFLLRFKEKPphtiagyaveaihtqDGFKLLLEGGHWVLI 439
Cdd:cd05799 390 kaQGKTLLDRLDELYEKYGYYKEKTISITFEGKEgpekikAIMDRLRNNP---------------NVLTFYLEDGSRVTV 454
|
490 500
....*....|....*....|....*.
gi 1343199007 440 RPSGTEPLLRIYCEATGSEELERLKE 465
Cdd:cd05799 455 RPSGTEPKIKFYIEVVGKKTLEEAEK 480
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
6-469 |
2.01e-94 |
|
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: 292.49 E-value: 2.01e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 6 IFGTDGWRAVMADQFTMENVRTVAKAIACYTEENGwidrgIIVGYDTRFMGRMFAQEVVRVLTA--HSILSFLVSeptPT 83
Cdd:TIGR03990 3 LFGTSGIRGIVGEELTPELALKVGKAFGTYLRGGK-----VVVGRDTRTSGPMLENAVIAGLLStgCDVVDLGIA---PT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 84 PVVAFGVKHFGVSGAVMLTASHNPAEYNGIKYIPEYAGPASPDITQRLEVLIQQIEAsgEQVQTRSIeeaknGKLYQPIH 163
Cdd:TIGR03990 75 PTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQEEEIEEIAESGDF--ERADWDEI-----GTVTSDED 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 164 LKPHYEAHIRRLIRMDVLQRANLTVVVDAMHGAGSGYMSALLQEAGVAVKSIREERDPLFGGGLPEPNEHHLAELSRQVL 243
Cdd:TIGR03990 148 AIDDYIEAILDKVDVEAIRKKGFKVVVDCGNGAGSLTTPYLLRELGCKVITLNCQPDGTFPGRNPEPTPENLKDLSALVK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 244 VENADLGVANDGDADRFGVVDRQGRYLSPNEVLTLLTYHMVknRNGQGKVIRTVATTHQLDRICEHYGLELIETPVGFKY 323
Cdd:TIGR03990 228 ATGADLGIAHDGDADRLVFIDEKGRFIGGDYTLALFAKYLL--EHGGGKVVTNVSSSRAVEDVAERHGGEVIRTKVGEVN 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 324 IGAQMLRGNVLIGGEESGGASILGHIPEKDGILMNLLIAEMCAVEGKSLDEIKADIHRQFgrMYSSRLDIRFKQKEAFLL 403
Cdd:TIGR03990 306 VAEKMKEEGAVFGGEGNGGWIFPDHHYCRDGLMAAALFLELLAEEGKPLSELLAELPKYP--MSKEKVELPDEDKEEVME 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1343199007 404 RFKEKpphtiagYAVEAIHTQDGFKLLLEGGhWVLIRPSGTEPLLRIYCEATGSEELERLKEAVRD 469
Cdd:TIGR03990 384 AVEEE-------FADAEIDTIDGVRIDFEDG-WVLVRPSGTEPIVRIYAEAKTEERAEELLEEGRS 441
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
7-469 |
2.67e-93 |
|
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: 289.47 E-value: 2.67e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 7 FGTDGWRAVMADQFTMENVRTVAKAIACYteengWIDRGIIVGYDTRFMGRMFAQEVVRVLTAHSILSFLVsEPTPTPVV 86
Cdd:cd03087 2 FGTSGIRGVVGEELTPELALKVGKALGTY-----LGGGTVVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDI-GIVPTPAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 87 AFGVKHFGVSGaVMLTASHNPAEYNGIKYIpeyagpaSPD---ITQRLEVLIQQIEASGeqvQTRSIEEAKNGKLYQPIH 163
Cdd:cd03087 76 QYAVRKLGDAG-VMITASHNPPEYNGIKLV-------NPDgteFSREQEEEIEEIIFSE---RFRRVAWDEVGSVRREDS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 164 LKPHYEAHIRRLIrmDVLQRANLTVVVDAMHGAGSGYMSALLQEAGVAVKSIREERDPLFGGGLPEPNEHHLAELSRQVL 243
Cdd:cd03087 145 AIDEYIEAILDKV--DIDGGKGLKVVVDCGNGAGSLTTPYLLRELGCKVITLNANPDGFFPGRPPEPTPENLSELMELVR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 244 VENADLGVANDGDADRFGVVDRQGRYLSPNEVLTLLTYHMVKNRNgqGKVIRTVATTHQLDRICEHYGLELIETPVGFKY 323
Cdd:cd03087 223 ATGADLGIAHDGDADRAVFVDEKGRFIDGDKLLALLAKYLLEEGG--GKVVTPVDASMLVEDVVEEAGGEVIRTPVGDVH 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 324 IGAQMLRGNVLIGGEESGGASILGHIPEKDGILMNLLIAEMCAvEGKSLDEIKADIHRQFgrMYSSRLDIRFKQKEAFLL 403
Cdd:cd03087 301 VAEEMIENGAVFGGEPNGGWIFPDHQLCRDGIMTAALLLELLA-EEKPLSELLDELPKYP--LLREKVECPDEKKEEVME 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1343199007 404 RFKEKPPHtiagyAVEAIHTQDGFKLLLEGGhWVLIRPSGTEPLLRIYCEATGSEELERLKEAVRD 469
Cdd:cd03087 378 AVEEELSD-----ADEDVDTIDGVRIEYEDG-WVLIRPSGTEPKIRITAEAKTEERAKELLEEGRS 437
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
7-466 |
1.16e-87 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 278.17 E-value: 1.16e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 7 FGTDGWR-AVMADQFTmEN-VRTVAKAIACYTEENGwIDRGIIVGYDTRFMGRMFAQEVVRVLTAHSILSFLVS--EPTP 82
Cdd:PRK07564 40 FGTSGHRgSSLQPSFN-ENhILAIFQAICEYRGKQG-ITGPLFVGGDTHALSEPAIQSALEVLAANGVGVVIVGrgGYTP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 83 TPVV-----AFGVKHFGVSGAVMLTASHNPAEYNGIKYIPEYAGPASPDITQRLEVLIQQIEASG-EQVQTRSIEEAKNG 156
Cdd:PRK07564 118 TPAVshailKYNGRGGGLADGIVITPSHNPPEDGGIKYNPPNGGPADTDVTDAIEARANELLAYGlKGVKRIPLDRALAS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 157 KLYQPIHLKPHYEAHIRRLIRMDVLQRANLTVVVDAMHGAGSGYMSALLQEAGVAVKSIREERDPLF--------GGGLP 228
Cdd:PRK07564 198 MTVEVIDPVADYVEDLENVFDFDAIRKAGLRLGVDPLGGATGPYWKAIAERYGLDLTVVNAPVDPTFnfmpldddGKIRM 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 229 EPN-EHHLAELsrqVLVENA-DLGVANDGDADRFGVVDRQGrYLSPNEVLTLLTYHMVKNRNG--QGKVI-RTVATTHQL 303
Cdd:PRK07564 278 DCSsPYAMAGL---LALKDAfDLAFANDPDGDRHGIVTPGG-LMNPNHYLAVAIAYLFHHRPGwrAGAGVgKTLVSSAMI 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 304 DRICEHYGLELIETPVGFKYIGAQMLRGNVLIGGEESGGASILG-----HIPEKDGILMNLLIAEMCAVEGKSLDEIKAD 378
Cdd:PRK07564 354 DRVAAKLGRKLYEVPVGFKWFVNGLDDGSLGFGGEESAGASFLRrdgsvWTTDKDGLIAVLLAAEILAVTGKSPSEIYRE 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 379 IHRQFGRMYSSRLD--IRFKQKEAFLLRFKEKPPHT-IAGYAVEAIHTQ--------DGFKLLLEGGhWVLIRPSGTEPL 447
Cdd:PRK07564 434 LWARFGRPYYSRHDapATPEQKAALRKLSPELVGATeLAGDPIDASLTEapgngaaiGGLKVVTENG-WFAARPSGTETT 512
|
490 500
....*....|....*....|.
gi 1343199007 448 LRIYCEA-TGSEELERL-KEA 466
Cdd:PRK07564 513 YKIYAESfEGDEHLHQIqKEA 533
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
81-469 |
6.19e-86 |
|
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: 267.69 E-value: 6.19e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 81 TPTPVVAFGVKhFGVSGAVMLTASHNPAEYNGIKYIPEYAGPASPDITQRLEVLIQQIEASGEQvqtrsiEEAKNGKLYQ 160
Cdd:cd03084 16 TPETAVALGQA-IGSTGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSAV------AYELGGSVKA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 161 PIHLKPHYEAhIRRLIRMDVLQRANLTVVVDAMHGAGSGYMSALLQEAGVAVKSIREERDPLFGGGLPEPN-EHHLAELS 239
Cdd:cd03084 89 VDILQRYFEA-LKKLFDVAALSNKKFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCEPDGNFGNINPDPGsETNLKQLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 240 RQVLVENADLGVANDGDADRFGVVDRQGRYLSPNEVLTLLTYHMVKNRNGQGKVIRTVATTHQLDRICEHYGLELIETPV 319
Cdd:cd03084 168 AVVKAEKADFGVAFDGDADRLIVVDENGGFLDGDELLALLAVELFLTFNPRGGVVKTVVSSGALDKVAKKLGIKVIRTKT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 320 GFKYIGAQMLRGNVLIGGEESGGASILGHIPEKDGILMNLLIAEMCAVEGKSLDEIKADIHRQFGRmyssrldirfkqke 399
Cdd:cd03084 248 GFKWVGEAMQEGDVVLGGEESGGVIFPEFHPGRDGISAALLLLEILANLGKSLSELFSELPRYYYI-------------- 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 400 afllrfkekpPHTIAGyaveaihtqdgfklllegghWVLIRPSGTEPLLRIYCEATGSEELERLKEAVRD 469
Cdd:cd03084 314 ----------RLKVRG--------------------WVLVRASGTEPAIRIYAEADTQEDVEQIKKEARE 353
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
2-470 |
1.19e-73 |
|
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: 241.00 E-value: 1.19e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 2 EKQIIFGTDGWR-AVMADQFTMENVRTVAKAIACYTEENGwIDRGIIVGYDTRFMGRMFAQEVVRVLTAHSILSFLVSE- 79
Cdd:cd05801 18 AQRVAFGTSGHRgSSLKGSFNEAHILAISQAICDYRKSQG-ITGPLFLGKDTHALSEPAFISALEVLAANGVEVIIQQNd 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 80 -PTPTPVVAFGV----KHF--GVSGAVMLTASHNPAEYNGIKYIPEYAGPASPDITQRLEVLIQQIEASGEQ-VQTRSIE 151
Cdd:cd05801 97 gYTPTPVISHAIltynRGRteGLADGIVITPSHNPPEDGGFKYNPPHGGPADTDITRWIEKRANALLANGLKgVKRIPLE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 152 EAKNGKLYQPIHLKPHYEAHIRRLIRMDVLQRANLTVVVDAMHGAGSGYMSALLQEAGVAVKSIREERDPLFG------G 225
Cdd:cd05801 177 AALASGYTHRHDFVTPYVADLGNVIDMDAIRKSGLRLGVDPLGGASVPYWQPIAEKYGLNLTVVNPKVDPTFRfmtldhD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 226 GLPEPN---EHHLAELSRqvLVENADLGVANDGDADRFGVVDRQGRYLSPNEVLTLLTYHMVKNRNGQGKVI---RTVAT 299
Cdd:cd05801 257 GKIRMDcssPYAMAGLLK--LKDKFDLAFANDPDADRHGIVTPSAGLMNPNHYLSVAIDYLFTHRPLWNKSAgvgKTLVS 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 300 THQLDRICEHYGLELIETPVGFKYIGAQMLRGNVLIGGEESGGASILGH-----IPEKDGILMNLLIAEMCAVEGKSLDE 374
Cdd:cd05801 335 SSMIDRVAAALGRKLYEVPVGFKWFVDGLLDGSLGFGGEESAGASFLRRdgtvwTTDKDGIIMCLLAAEILAVTGKDPGQ 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 375 IKADIHRQFGRMYSSRLD--IRFKQKEAFL-LRFKEKPPHTIAGYAVEAIHTQ--------DGFKLLLEGGhWVLIRPSG 443
Cdd:cd05801 415 LYQELTERFGEPYYARIDapATPEQKARLKkLSPEQVTATELAGDPILAKLTRapgngasiGGLKVTTANG-WFAARPSG 493
|
490 500
....*....|....*....|....*...
gi 1343199007 444 TEPLLRIYCEATGSEE-LERLKEAVRDW 470
Cdd:cd05801 494 TEDVYKIYAESFLSEEhLKKIQKEAQEI 521
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
13-471 |
2.38e-72 |
|
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: 235.49 E-value: 2.38e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 13 RAVMADQFTMENVRTVAKAIACYTEENGWIDrgIIVGYDTRFMGRMFAQEVVRVLTAHSILSFLVSEpTPTPVVAFGVKH 92
Cdd:cd03089 8 RGIAGEELTEEIAYAIGRAFGSWLLEKGAKK--VVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGL-VPTPVLYFATFH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 93 FGVSGAVMLTASHNPAEYNGIKYIPEYAGPASPDITQRLEVLIQQIEASGEQvqtrsieeakNGKlYQPIHLKPHYEAHI 172
Cdd:cd03089 85 LDADGGVMITASHNPPEYNGFKIVIGGGPLSGEDIQALRERAEKGDFAAATG----------RGS-VEKVDILPDYIDRL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 173 RRLIRMDVLqraNLTVVVDAMHGAGSGYMSALLQEAGVAVKSIREERDPLFGGGLPEP-NEHHLAELSRQVLVENADLGV 251
Cdd:cd03089 154 LSDIKLGKR---PLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCEPDGTFPNHHPDPtDPENLEDLIAAVKENGADLGI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 252 ANDGDADRFGVVDRQGRYLSPNEVLTLLTYHMVKNRNGqGKVIRTVATTHQLDRICEHYGLELIETPVGFKYIGAQMLRG 331
Cdd:cd03089 231 AFDGDGDRLGVVDEKGEIIWGDRLLALFARDILKRNPG-ATIVYDVKCSRNLYDFIEEAGGKPIMWKTGHSFIKAKMKET 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 332 NVLIGGEESggasilGHIPEK-------DGILMNLLIAEMCAVEGKSLDEIKADIhrqfgRMYSSRLDIRFK----QKEA 400
Cdd:cd03089 310 GALLAGEMS------GHIFFKdrwygfdDGIYAALRLLELLSKSGKTLSELLADL-----PKYFSTPEIRIPvteeDKFA 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1343199007 401 FLLRFKEKpphtiAGYAVEAIHTQDGFKLLLEGGhWVLIRPSGTEPLLRIYCEATGSEELERLKEAVRDWF 471
Cdd:cd03089 379 VIERLKEH-----FEFPGAEIIDIDGVRVDFEDG-WGLVRASNTEPVLVLRFEADTEEGLEEIKAELRKLL 443
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
6-463 |
1.57e-62 |
|
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: 209.26 E-value: 1.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 6 IFGTDGWRAVMADQFTMENVRTVAKAIACYTEENGwiDRG-IIVGYDTRFMGRMFAQEVVRVLTAHSILSFLVSePTPTP 84
Cdd:cd05802 1 LFGTDGIRGVANEPLTPELALKLGRAAGKVLGKGG--GRPkVLIGKDTRISGYMLESALAAGLTSAGVDVLLLG-VIPTP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 85 VVAFGVKHFGVSGAVMLTASHNPAEYNGIKYIPEYAGPASPDITQRLEVLIQQ---IEASGEQV-QTRSIEEAKNgklyq 160
Cdd:cd05802 78 AVAYLTRKLRADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVEEEIEALIDKeleLPPTGEKIgRVYRIDDARG----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 161 pihlkpHYEAHIRRLIRMDVLQraNLTVVVDAMHGAGSGYMSALLQEAGVAVKSIREERDplfggGLpEPNEH----HLA 236
Cdd:cd05802 153 ------RYIEFLKSTFPKDLLS--GLKIVLDCANGAAYKVAPEVFRELGAEVIVINNAPD-----GL-NINVNcgstHPE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 237 ELSRQVLVENADLGVANDGDADRFGVVDRQGRYLSPNEVLTLLTYHMvKNRNG--QGKVIRTVATTHQLDRICEHYGLEL 314
Cdd:cd05802 219 SLQKAVLENGADLGIAFDGDADRVIAVDEKGNIVDGDQILAICARDL-KERGRlkGNTVVGTVMSNLGLEKALKELGIKL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 315 IETPVGFKYIGAQMLRGNVLIGGEESGGASILGHIPEKDGILMNLLIAEMCAVEGKSLDEIKADIHrqfgrMYSSRL-DI 393
Cdd:cd05802 298 VRTKVGDRYVLEEMLKHGANLGGEQSGHIIFLDHSTTGDGLLTALQLLAIMKRSGKSLSELASDMK-----LYPQVLvNV 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 394 RFKQKEAFLlrfkekpphTIAGYAvEAIhtQDGFKLLLEGGHwVLIRPSGTEPLLRIYCEATGSEELERL 463
Cdd:cd05802 373 RVKDKKALL---------ENPRVQ-AAI--AEAEKELGGEGR-VLVRPSGTEPLIRVMVEGEDEELVEKL 429
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
6-468 |
1.12e-60 |
|
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: 204.85 E-value: 1.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 6 IFGTDGWRAVMADQFTMENVRTVAKAIACYTEENGWIDRgIIVGYDTRFMGRMFAQEVVRVLTAHSIlSFLVSEPTPTPV 85
Cdd:cd05803 1 IISISGIRGIVGEGLTPEVITRYVAAFATWQPERTKGGK-IVVGRDGRPSGPMLEKIVIGALLACGC-DVIDLGIAPTPT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 86 VAFGVKHFGVSGAVMLTASHNPAEYNGIKYIpeyaGPASPDITQrlevliqqieASGEQVQtrsieEAKNGKLYQPIHLK 165
Cdd:cd05803 79 VQVLVRQSQASGGIIITASHNPPQWNGLKFI----GPDGEFLTP----------DEGEEVL-----SCAEAGSAQKAGYD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 166 P---------HYEAHIRRLIRMDVLQRA-----NLTVVVDAMHGAGSGYMSALLQEAGVAVKSIREERDPLFGGgLPEPN 231
Cdd:cd05803 140 QlgevtfsedAIAEHIDKVLALVDVDVIkirerNFKVAVDSVNGAGGLLIPRLLEKLGCEVIVLNCEPTGLFPH-TPEPL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 232 EHHLAELSRQVLVENADLGVANDGDADRFGVVDRQGRYLSPNEVLTLLTYHMVKNRNGQGKVIRTVATTHQLDRICEHYG 311
Cdd:cd05803 219 PENLTQLCAAVKESGADVGFAVDPDADRLALVDEDGRPIGEEYTLALAVDYVLKYGGRKGPVVVNLSTSRALEDIARKHG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 312 LELIETPVGFKYIGAQMLRGNVLIGGEESGGAsILGHI-PEKDGILMNLLIAEMCAVEGKSLDEIKADIHRQFgrMYSSR 390
Cdd:cd05803 299 VPVFRSAVGEANVVEKMKEVDAVIGGEGNGGV-ILPDVhYGRDSLVGIALVLQLLAASGKPLSEIVDELPQYY--ISKTK 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1343199007 391 LDIRFKQKEAFLLRFKEKpphtiagYAVEAIHTQDGFKLLLEGGhWVLIRPSGTEPLLRIYCEATGSEELERLKEAVR 468
Cdd:cd05803 376 VTIAGEALERLLKKLEAY-------FKDAEASTLDGLRLDSEDS-WVHVRPSNTEPIVRIIAEAPTQDEAEALADRFI 445
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
7-469 |
4.64e-56 |
|
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: 192.58 E-value: 4.64e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 7 FGTDGWRAVmADQF--TMENVRTVAKAIACYTEENGWIDRGIIVGYDTRFMGRMFAQEVVRVLTAHSILSFLVSePTPTP 84
Cdd:TIGR01455 1 FGTDGVRGR-AGQEplTAELALLLGAAAGRVLRQGRDTAPRVVIGKDTRLSGYMLENALAAGLNSAGVDVLLLG-PLPTP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 85 VVAFGVKHFGVSGAVMLTASHNPAEYNGIKYIPEYAGPASPDITQRLEVLIQqieasgEQVQTRSIEEAKNGKLYQPIHL 164
Cdd:TIGR01455 79 AVAYLTRTLRADAGVMISASHNPYEDNGIKFFGPGGFKLDDATEAAIEALLD------EADPLPRPESEGLGRVKRYPDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 165 KPHYEAHIRR-LIRMDVLQraNLTVVVDAMHGAGSGYMSALLQEAGVAVKSIREERDPLfggglpEPNEH----HLAELS 239
Cdd:TIGR01455 153 VGRYIEFLKStLPRGLTLS--GLKVVLDCANGAAYKVAPHVFRELGAEVIAIGVEPDGL------NINDGcgstHLDALQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 240 RQVLVENADLGVANDGDADRFGVVDRQGRYLSPNEVLTLLTYHMV-KNRNGQGKVIRTVATTHQLDRICEHYGLELIETP 318
Cdd:TIGR01455 225 KAVREHGADLGIAFDGDADRVLAVDANGRIVDGDQILYIIARALKeSGELAGNTVVATVMSNLGLERALEKLGLTLIRTA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 319 VGFKYIGAQMLRGNVLIGGEESGGASILGHIPEKDGILMNLLIAEMCAVEGKSLDEIKADIHrqfgrMYSSRL-DIRFKQ 397
Cdd:TIGR01455 305 VGDRYVLEEMRESGYNLGGEQSGHIILLDYSTTGDGIVSALQVLTIMKKSGSTLSELAAEFV-----PYPQTLvNVRVAD 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1343199007 398 KEAFLLrfkEKPP--HTIAGYAVEaihtqdgfkllLEGGHWVLIRPSGTEPLLRIYCEATGSEELERLKEAVRD 469
Cdd:TIGR01455 380 RKLAAA---EAPAvkAAIEDAEAE-----------LGGTGRILLRPSGTEPLIRVMVEAADEELVQQLADTLAD 439
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
2-465 |
4.37e-48 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 174.10 E-value: 4.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 2 EKQIIFGTDGWRAVMADQFTMENVRTV---AKAIACYTEE---NGWIDRGIIVGYDTRFMGRMFAQEVVRVLTAHSILSF 75
Cdd:PTZ00150 42 LKRMEFGTAGLRGKMGAGFNCMNDLTVqqtAQGLCAYVIEtfgQALKSRGVVIGYDGRYHSRRFAEITASVFLSKGFKVY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 76 LVSEPTPTPVVAFGVKHFGVSGAVMLTASHNPAEYNGIKYipeYAG-------PASPDITQRLEVLIQQIEASGEQVQTR 148
Cdd:PTZ00150 122 LFGQTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKV---YWSngaqiipPHDKNISAKILSNLEPWSSSWEYLTET 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 149 SIEEAkngklYQPIHlkPHYEAHIRRLIRMDVLQRANLTVVVDAMHGAGSGYMSALLQEAGV-AVKSIRE--ERDPLFGG 225
Cdd:PTZ00150 199 LVEDP-----LAEVS--DAYFATLKSEYNPACCDRSKVKIVYTAMHGVGTRFVQKALHTVGLpNLLSVAQqaEPDPEFPT 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 226 -GLPEPNEHHLA-ELSRQVL-VENADLGVANDGDADRFGVVDRQG---RYLSPNEVLTLLTYHMVKNRNGQGK------V 293
Cdd:PTZ00150 272 vTFPNPEEGKGAlKLSMETAeAHGSTVVLANDPDADRLAVAEKLNngwKIFTGNELGALLAWWAMKRYRRQGIdkskcfF 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 294 IRTVATTHQLDRICEHYGLELIETPVGFKYIG--AQMLRGN----VLIGGEESGGASILGHIPEKDGILMNLLIAEMC-- 365
Cdd:PTZ00150 352 ICTVVSSRMLKKMAEKEGFQYDETLTGFKWIGnkAIELNAEngltTLFAYEEAIGFMLGTRVRDKDGVTAAAVVAEMAly 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 366 -AVEGKSLDEIKADIHRQFGRMYS----------SRLDIRFKQkeaflLRFKEKPPHTIAGYAVEAIH---------TQD 425
Cdd:PTZ00150 432 lYERGKTLVEHLESLYKQYGYHFTnnsyyicydpSRIVSIFND-----IRNNGSYPTKLGGYPVTRIRdlttgydtaTPD 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1343199007 426 GFKLL------------LEGGHWVLIRPSGTEPLLRIYCEATGSEELERLKE 465
Cdd:PTZ00150 507 GKPLLpvsastqmitfyFENGAIITIRGSGTEPKLKWYAELSGTKDEAVEKE 558
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
5-139 |
8.54e-43 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 148.14 E-value: 8.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 5 IIFGTDGWRAVM-ADQFTMENVRTVAKAIACYTEENGwIDRGIIVGYDTRFMGRMFAQEVVRVLTAHSILSFLVsEPTPT 83
Cdd:pfam02878 2 QLFGTSGIRGKVgVGELTPEFALKLGQAIASYLRAQG-GGGKVVVGRDTRYSSRELARALAAGLASNGVEVILL-GLLPT 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1343199007 84 PVVAFGVKHFGVSGAVMLTASHNPAEYNGIKYIPEYAGPASPDITQRLEVLIQQIE 139
Cdd:pfam02878 80 PAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKED 135
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
272-379 |
1.08e-35 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 128.34 E-value: 1.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 272 PNEVLTLLTYHMVKNR--NGQGKVIRTVATTHQLDRICEHYGLELIETPVGFKYIGAQMLRGNVLIGGEESGGASILGHI 349
Cdd:pfam02880 2 GDQILALLAKYLLEQGklPPGAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLDHA 81
|
90 100 110
....*....|....*....|....*....|
gi 1343199007 350 PEKDGILMNLLIAEMCAVEGKSLDEIKADI 379
Cdd:pfam02880 82 TTKDGILAALLVLEILARTGKSLSELLEEL 111
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
46-453 |
2.10e-34 |
|
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: 135.43 E-value: 2.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 46 IIVGYDTRFMGRMFAQEVVRVLTAHSILSFLVSEPT--PTPVVAFGVKHFGVSGAVMLTASHNPAEYN---GIKYIPEYA 120
Cdd:cd03085 52 LVVGGDGRYYNKEAIQIIIKIAAANGVGKVVVGQNGllSTPAVSAVIRKRKATGGIILTASHNPGGPEgdfGIKYNTSNG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 121 GPASPDITQRlevlIQQIEASGEQVQTRSIEEAKNGKL-YQPIHLKP----------HYEAHIRRLIRMD----VLQRAN 185
Cdd:cd03085 132 GPAPESVTDK----IYEITKKITEYKIADDPDVDLSKIgVTKFGGKPftvevidsveDYVELMKEIFDFDaikkLLSRKG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 186 LTVVVDAMHGAGSGYMSALL-QEAGVAVKSIREErDPL--FGGGLPEPNEHHLAELSRQVLVENADLGVANDGDADRFGV 262
Cdd:cd03085 208 FKVRFDAMHGVTGPYAKKIFvEELGAPESSVVNC-TPLpdFGGGHPDPNLTYAKDLVELMKSGEPDFGAASDGDGDRNMI 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 263 VDRqGRYLSPNEVLTLLTYHMVK----NRNGQGKVIRTVATTHQLDRICEHYGLELIETPVGFKYIGAQMLRGNVLIGGE 338
Cdd:cd03085 287 LGK-GFFVTPSDSVAVIAANAKLipyfYKGGLKGVARSMPTSGALDRVAKKLGIPLFETPTGWKFFGNLMDAGKLSLCGE 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 339 ES-GGASilGHIPEKDGILMNLLIAEMCAVEGKSLDEIKADIHRQFGRMYSSRLDIR----------FKQKEAFLLRFKE 407
Cdd:cd03085 366 ESfGTGS--DHIREKDGLWAVLAWLSILAHRNVSVEDIVKEHWQKYGRNFYTRYDYEevdseaankmMDHLRALVSDLPG 443
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1343199007 408 KPPHTIAGYAVE-------------AIHTQDGFKLLLEGGHWVLIRPSGTE---PLLRIYCE 453
Cdd:cd03085 444 VGKSGDKGYKVAkaddfsytdpvdgSVSKKQGLRIIFEDGSRIIFRLSGTGssgATIRLYIE 505
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
13-467 |
2.39e-34 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 133.57 E-value: 2.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 13 RAVMADQFTMENVRTVAKAIACYTEENGwiDRGIIVGYDTRFMGRMFAQEVVRVLTAHS---ILSFLVSeptpTPVVAFG 89
Cdd:PRK09542 7 RGVVGEQIDEDLVRDVGAAFARLMRAEG--ATTVVIGHDMRDSSPELAAAFAEGVTAQGldvVRIGLAS----TDQLYFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 90 VKHFGVSGAvMLTASHNPAEYNGIKYIPEYAGPASPD--ITQRLEVLIQQIEASGEQVQTRSIEEakngklyqpihLKPH 167
Cdd:PRK09542 81 SGLLDCPGA-MFTASHNPAAYNGIKLCRAGAKPVGQDtgLAAIRDDLIAGVPAYDGPPGTVTERD-----------VLAD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 168 YEAHIRRLIrmDVLQRANLTVVVDAMHGAGSGYMSALLQEAGVAVKSIREERDPLFggglpePNeH--------HLAELS 239
Cdd:PRK09542 149 YAAFLRSLV--DLSGIRPLKVAVDAGNGMGGHTVPAVLGGLPITLLPLYFELDGTF------PN-HeanpldpaNLVDLQ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 240 RQVLVENADLGVANDGDADRFGVVDRQGRYLSPNEVLTLLTYHMVKNRNGqGKVIRTVATTHQLDRICEHYGLELIETPV 319
Cdd:PRK09542 220 AFVRETGADIGLAFDGDADRCFVVDERGQPVSPSAVTALVAARELAREPG-ATIIHNLITSRAVPELVAERGGTPVRTRV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 320 GFKYIGAQMLRGNVLIGGEESggasilGHIPEKD------GILMNL-LIAEMCAvEGKSLDEIKADIHRQFGrmySSRLD 392
Cdd:PRK09542 299 GHSFIKALMAETGAIFGGEHS------AHYYFRDfwgadsGMLAALhVLAALGE-QDRPLSELMADYQRYAA---SGEIN 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1343199007 393 IRFKQKEAFLLRFKEkpphTIAGYAVEAIHTqDGFKLLLEGGHWVLIRPSGTEPLLRIYCEATGSEELERLKEAV 467
Cdd:PRK09542 369 STVADAPARMEAVLK----AFADRIVSVDHL-DGVTVDLGDGSWFNLRASNTEPLLRLNVEARTEEEVDALVDEV 438
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
46-469 |
2.45e-31 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 125.25 E-value: 2.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 46 IIVGYDTRFMGRMFAQEVVRVLTAHSILSFLVSePTPTPVVAFGVKHFGVSGAVMLTASHNPAEYNGIKYIpeyagpaSP 125
Cdd:PRK10887 42 VLIGKDTRISGYMLESALEAGLAAAGVDVLLTG-PMPTPAVAYLTRTLRAEAGIVISASHNPYYDNGIKFF-------SA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 126 DITQrlevLIQQIEASgeqvqtrsIEEAkngkLYQPIHLKPHYE-AHIRRLIrmDVLQR---------------ANLTVV 189
Cdd:PRK10887 114 DGTK----LPDEVELA--------IEAE----LDKPLTCVESAElGKASRIN--DAAGRyiefckstfpnelslRGLKIV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 190 VDAMHGAGsgYMSA--LLQEAGVAVKSIREERDplfggGLpEPNEH----HLAELSRQVLVENADLGVANDGDADRFGVV 263
Cdd:PRK10887 176 VDCANGAT--YHIApnVFRELGAEVIAIGCEPN-----GL-NINDEcgatDPEALQAAVLAEKADLGIAFDGDGDRVIMV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 264 DRQGRYLSPNEVLTLLTYHMVKNRNGQGKVIRTVATTHQLDRICEHYGLELIETPVGFKYIGAQMLRGNVLIGGEESGGA 343
Cdd:PRK10887 248 DHLGNLVDGDQLLYIIARDRLRRGQLRGGVVGTLMSNMGLELALKQLGIPFVRAKVGDRYVLEKLQEKGWRLGGENSGHI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 344 SILGHIPEKDGILMNLLIAEMCAVEGKSLDEIKADIhrqfgRMYSSRL-DIRFKQKEAFLLrfkEKPPHTIAGYAVEAIh 422
Cdd:PRK10887 328 LCLDKTTTGDGIVAALQVLAAMVRSGMSLADLCSGM-----KLFPQVLiNVRFKPGADDPL---ESEAVKAALAEVEAE- 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1343199007 423 tqdgfkllLEGGHWVLIRPSGTEPLLRIYCEATGSEEL----ERLKEAVRD 469
Cdd:PRK10887 399 --------LGGRGRVLLRKSGTEPLIRVMVEGEDEAQVtalaERIADAVKA 441
|
|
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
46-463 |
3.16e-31 |
|
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: 125.05 E-value: 3.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 46 IIVGYDTRFMGRMFAqevvrvltaHSILSFLVS--------EPTPTPVVAFGVKHFGVSGAVMLTASHNPAEYNGIKYIP 117
Cdd:cd05805 37 VTVSRDASRASRMLK---------RALISGLLStgvnvrdlGALPLPVARYAIRFLGASGGIHVRTSPDDPDKVEIEFFD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 118 EYAGPASPDiTQRlevliqQIEASGEQVQTRSIEEAKNGKLYQPIHLKPHYEAHIRRLIRMDVLQRANLTVVVDAMHGAG 197
Cdd:cd05805 108 SRGLNISRA-MER------KIENAFFREDFRRAHVDEIGDITEPPDFVEYYIRGLLRALDTSGLKKSGLKVVIDYAYGVA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 198 SGYMSALLQEAG---VAVKSIREERDPlfggglPEPNEHH--LAELSRQVLVENADLGVANDGDADRFGVVDRQGRYLSP 272
Cdd:cd05805 181 GIVLPGLLSRLGcdvVILNARLDEDAP------RTDTERQrsLDRLGRIVKALGADFGVIIDPNGERLILVDEAGRVISD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 273 nEVLTLLTYHMVKNRNGQGKVIRTVATTHQLDRICEHYGLELIETPVGFKYIGAQMLRGNVLiGGEESGGASILGHIPEK 352
Cdd:cd05805 255 -DLLTALVSLLVLKSEPGGTVVVPVTAPSVIEQLAERYGGRVIRTKTSPQALMEAALENVVL-AGDGDGGFIFPEFHPGF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 353 DGILMNLLIAEMCAVEGKSLDEIKADIHRQFgrMYSSRLDIRFKQKEAFLLRFKEKPPHtiagyavEAIHTQDGFKLLLE 432
Cdd:cd05805 333 DAIAALVKILEMLARTNISLSQIVDELPRFY--VLHKEVPCPWEAKGRVMRRLIEEAPD-------KSIELIDGVKIYED 403
|
410 420 430
....*....|....*....|....*....|.
gi 1343199007 433 GGhWVLIRPSGTEPLLRIYCEATGSEELERL 463
Cdd:cd05805 404 DG-WVLVLPDADEPLCHIYAEGSDQERAEEL 433
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
83-460 |
4.21e-29 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 119.28 E-value: 4.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 83 TPVVAFGVKHFGVSGAVMLTASHNPAEYNGIKYIPEYAGPASPDITQRlevliqQIEASGEQVQTRSIEEAKNGKlYQPI 162
Cdd:PRK15414 77 TEEIYFATFHLGVDGGIEVTASHNPMDYNGMKLVREGARPISGDTGLR------DVQRLAEANDFPPVDETKRGR-YQQI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 163 HLKPHYEAHIRRLIrmDVLQRANLTVVVDAMHGAGSGYMSAL---LQEAGVAVKSIREERDP--LFGGGLPEPNEHHLAE 237
Cdd:PRK15414 150 NLRDAYVDHLFGYI--NVKNLTPLKLVINSGNGAAGPVVDAIearFKALGAPVELIKVHNTPdgNFPNGIPNPLLPECRD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 238 LSRQVLVEN-ADLGVANDGDADRFGVVDRQGRYLSPNEVLTLLTYHMVKNRNGqGKVIRTVATTHQLDRICEHYGLELIE 316
Cdd:PRK15414 228 DTRNAVIKHgADMGIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPG-AKIIHDPRLSWNTVDVVTAAGGTPVM 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 317 TPVGFKYIGAQMLRGNVLIGGEESGGASILGHIPEKDGILMNLLIAEMCAVEGKSLDEIKADihRQFGRMYSSRLDIRFK 396
Cdd:PRK15414 307 SKTGHAFIKERMRKEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELVCLKGKTLGELVRD--RMAAFPASGEINSKLA 384
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1343199007 397 QKEAFLLRFKEKpphtiagYAVEAIHTQDGFKLLLEGGHWVL-IRPSGTEPLLRIYCEATGSEEL 460
Cdd:PRK15414 385 QPVEAINRVEQH-------FSREALAVDRTDGISMTFADWRFnLRSSNTEPVVRLNVESRGDVPL 442
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
168-267 |
8.27e-29 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 109.30 E-value: 8.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 168 YEAHIRRLIRMDVLQRANLTVVVDAMHGAGSGYMSALLQEAGVAVKSIREERDPLFGGGLPEPNEH-HLAELSRQVLVEN 246
Cdd:pfam02879 2 YIDHLLELVDSEALKKRGLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDPDFPTRAPNPEEPeALALLIELVKSVG 81
|
90 100
....*....|....*....|.
gi 1343199007 247 ADLGVANDGDADRFGVVDRQG 267
Cdd:pfam02879 82 ADLGIATDGDADRLGVVDERG 102
|
|
| PLN02307 |
PLN02307 |
phosphoglucomutase |
46-392 |
3.00e-27 |
|
phosphoglucomutase
Pssm-ID: 177942 [Multi-domain] Cd Length: 579 Bit Score: 114.75 E-value: 3.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 46 IIVGYDTRFMGRMFAQEVVRVLTAHSILSFLVSEPT--PTPVVAFGVK---HFGVSGAVMLTASHNPA---EYNGIKYIP 117
Cdd:PLN02307 64 LVLGGDGRYFNKEAIQIIIKIAAANGVRRVWVGQNGllSTPAVSAVIRerdGSKANGGFILTASHNPGgpeEDFGIKYNY 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 118 EYAGPASPDITQRL--------EVLIQQ----IEASGEQVQTRSIEEAKNGKLYQPI--HLKPHYEAHIRRLIRmDVLQR 183
Cdd:PLN02307 144 ESGQPAPESITDKIygntltikEYKMAEdipdVDLSAVGVTKFGGPEDFDVEVIDPVedYVKLMKSIFDFELIK-KLLSR 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 184 ANLTVVVDAMHGAGSGYMSALL-QEAGVAVKSIREErDPL--FGGGLPEPNEHHLAEL-------SRQVLVENADLGVAN 253
Cdd:PLN02307 223 PDFTFCFDAMHGVTGAYAKRIFvEELGAPESSLLNC-VPKedFGGGHPDPNLTYAKELvkrmglgKTSYGDEPPEFGAAS 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 254 DGDADRFGVVDRqGRYLSPNEVLTLLTYHMVKN----RNGQGKVIRTVATTHQLDRICEHYGLELIETPVGFKYIGAQML 329
Cdd:PLN02307 302 DGDGDRNMILGK-RFFVTPSDSVAIIAANAQEAipyfSGGLKGVARSMPTSAALDVVAKKLNLPFFEVPTGWKFFGNLMD 380
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1343199007 330 RGNVLIGGEES-GGASilGHIPEKDGIL-----MNLLiaeMCAVEGKSLDEIK---ADIHRQ----FGRMYSSRLD 392
Cdd:PLN02307 381 AGKLSICGEESfGTGS--DHIREKDGIWavlawLSIL---AHKNKDVLPGGKLvtvEDIVREhwatYGRNFYSRYD 451
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
46-279 |
4.39e-17 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 83.95 E-value: 4.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 46 IIVGYDTRFMGRMFAQEVVRVLTAHSILSFLVSEPTpTPVVAFGVKHFGVSG--AVMLTASHNPAEYNGIKYIPEYAGPA 123
Cdd:PLN02371 118 VSVGRDPRISGPRLADAVFAGLASAGLDVVDMGLAT-TPAMFMSTLTEREDYdaPIMITASHLPYNRNGLKFFTKDGGLG 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 124 SPDITQRLEVLIQQIEASGEQVQTRSieEAKNGKLYQPIHLKPHYEAHIRRLIRMDVLQRAN-------LTVVVDAMHGA 196
Cdd:PLN02371 197 KPDIKDILERAARIYKEWSDEGLLKS--SSGASSVVCRVDFMSTYAKHLRDAIKEGVGHPTNyetplegFKIVVDAGNGA 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 197 GSGYMSALLQEAGVAVK-SIREERDPLFGGGLPEPnEHHLA-ELSRQVLVEN-ADLGVANDGDADRFGVVDRQGRYLSPN 273
Cdd:PLN02371 275 GGFFAEKVLEPLGADTSgSLFLEPDGMFPNHIPNP-EDKAAmSATTQAVLANkADLGIIFDTDVDRSAVVDSSGREINRN 353
|
....*.
gi 1343199007 274 EVLTLL 279
Cdd:PLN02371 354 RLIALM 359
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
82-459 |
4.87e-16 |
|
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: 79.94 E-value: 4.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 82 PTPVVAFGVKHFGVsGAVMLTASHNPAEYNGIKYipeYagpaSPD--ITQRLEVLIQQIEasgeqVQTRSIEEAKNGKLy 159
Cdd:cd03088 74 PTPALALYAMKRGA-PAIMVTGSHIPADRNGLKF---Y----RPDgeITKADEAAILAAL-----VELPEALFDPAGAL- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 160 qPIHLKPHYEAHIRRLIRM---DVLqrANLTVVVDAMHGAGSGYMSALLQEAGVAVKSIReeRDPLFgggLP---EPNEH 233
Cdd:cd03088 140 -LPPDTDAADAYIARYTDFfgaGAL--KGLRIGVYQHSSVGRDLLVRILEALGAEVVPLG--RSDTF---IPvdtEAVRP 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 234 HLAELSRQVLVENA-DLGVANDGDADRFGVVDRQGRYLsPNEVLTLLTYHMVknrngQGKVIRT-VATTHQLDRICehYG 311
Cdd:cd03088 212 EDRALAAAWAAEHGlDAIVSTDGDGDRPLVADETGEWL-RGDILGLLTARFL-----GADTVVTpVSSNSAIELSG--FF 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 312 LELIETPVGFKYIGAQMLR---------------GNVLIGGEESGGASILGHIPEKDGILmnLLIAEMCAV--EGKSLDE 374
Cdd:cd03088 284 KRVVRTRIGSPYVIAAMAEaaaagagrvvgyeanGGFLLGSDIERNGRTLKALPTRDAVL--PILAVLAAAkeAGIPLSE 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 375 IKADIHRQFgrMYSSRL-DIRFKQKEAFLLRFKEkPPHTIAGY------AVEAIHTQDGFKLLLEGGHWVLIRPSGTEPL 447
Cdd:cd03088 362 LVASLPARF--TASDRLqNFPTEKSQALIARLSA-DPEARAAFffalggEVASIDTTDGLRMTFANGDIVHLRPSGNAPE 438
|
410
....*....|..
gi 1343199007 448 LRIYCEAtGSEE 459
Cdd:cd03088 439 LRCYVEA-DSEE 449
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
402-469 |
1.60e-11 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 59.59 E-value: 1.60e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1343199007 402 LLRFKEKPPHTIAgyAVEAIH--TQDGFKLLLEGGHWVLIRPSGTEPLLRIYCEATGSEELERLKEAVRD 469
Cdd:pfam00408 1 LINVRVAEKKKLA--ALAAILkvFADAEKILGEDGRRLDVRPSGTEPVLRVMVEGDSDEELARLADEIAD 68
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
439-469 |
5.96e-05 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 45.41 E-value: 5.96e-05
10 20 30
....*....|....*....|....*....|.
gi 1343199007 439 IRPSGTEPLLRIYCEATGSEELERLKEAVRD 469
Cdd:PTZ00302 546 IRPSGTEPVVRVYAEAPTLEQADELANEVKG 576
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
439-469 |
1.73e-04 |
|
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: 44.12 E-value: 1.73e-04
10 20 30
....*....|....*....|....*....|.
gi 1343199007 439 IRPSGTEPLLRIYCEATGSEELERLKEAVRD 469
Cdd:cd03086 481 VRPSGTEDVVRVYAEAATQEEADELANEVAE 511
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
99-114 |
7.05e-04 |
|
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: 42.20 E-value: 7.05e-04
|
| |
