|
Name |
Accession |
Description |
Interval |
E-value |
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
32-522 |
4.70e-142 |
|
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: 418.45 E-value: 4.70e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 32 KFGTGGMRGLMRSGFNGINEVTCNLIGTELCRRFS---------SIVIGCDGRYNSLNYAMILRGIFKLNGKEAVLYSE- 101
Cdd:cd05799 3 EFGTAGLRGKMGAGTNRMNDYTVRQATQGLANYLKkkgpdaknrGVVIGYDSRHNSREFAELTAAVLAANGIKVYLFDDl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 102 VATPFLAFLVSRLGADAGIMVTASHNPKEYNGFKVYTSNGSQIGSPLDREIEESMEMLnltrlsGEEWygeifkrireen 181
Cdd:cd05799 83 RPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAV------LEPL------------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 182 dilggkippasrktnmansagiDFSRRDELVDCYNRWMFKGWSDSIVQAIKS--------AGSPVPVVFTGLCGVSGEFV 253
Cdd:cd05799 145 ----------------------DIKFEEALDSGLIKYIGEEIDDAYLEAVKKllvnpelnEGKDLKIVYTPLHGVGGKFV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 254 KKALEFYNLDgSMHFIDEECIPNPNFPRLPFPNPEVPETLARSKSSGL---GDIVFSCDPDGDRFGLSEKVG-GEWVDYN 329
Cdd:cd05799 203 PRALKEAGFT-NVIVVEEQAEPDPDFPTVKFPNPEEPGALDLAIELAKkvgADLILATDPDADRLGVAVKDKdGEWRLLT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 330 GNEIAAMFMDFFVENF-----APSDLAFINTYLCNGLMEKVCSIHGIEYLRTETGFKNVSRAVDSVEGKN---VFAYEDS 401
Cdd:cd05799 282 GNEIGALLADYLLEQRkekgkLPKNPVIVKTIVSSELLRKIAKKYGVKVEETLTGFKWIGNKIEELESGGkkfLFGFEES 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 402 LGFLFGN-GKEKDGIKCVVLMASMVQ------RELPSRTLKRMERYGCFSSVNIHIRCTEPDRiLEKVLRKFPAAKTEGK 474
Cdd:cd05799 362 IGYLVGPfVRDKDGISAAALLAEMAAylkaqgKTLLDRLDELYEKYGYYKEKTISITFEGKEG-PEKIKAIMDRLRNNPN 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1154491712 475 RSTVEFDD-YKVILRVSGTESVLKVYTssEVLSKGALTTAAKNFSDRYI 522
Cdd:cd05799 441 VLTFYLEDgSRVTVRPSGTEPKIKFYI--EVVGKKTLEEAEKKLDALKK 487
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
19-486 |
1.15e-79 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 260.39 E-value: 1.15e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 19 LEIYGEKDLLRL----VKFGTGGMRGLMRSGFNGINEVTC------------NLIGTELCRRfsSIVIGCDGRYNSLNYA 82
Cdd:PTZ00150 29 LASKDEEELKRRflkrMEFGTAGLRGKMGAGFNCMNDLTVqqtaqglcayviETFGQALKSR--GVVIGYDGRYHSRRFA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 83 MILRGIFKLNGKEAVLYSE-VATPFLAFLVSRLGADAGIMVTASHNPKEYNGFKVYTSNGSQIGSPLDREIEESMEMlNL 161
Cdd:PTZ00150 107 EITASVFLSKGFKVYLFGQtVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVYWSNGAQIIPPHDKNISAKILS-NL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 162 TRLSgEEWygEIFKRIREEnDILggkippasrktnmansagidfsrrDELVDCYNRWMfkgwsDSIVQAIKSAGSPVPVV 241
Cdd:PTZ00150 186 EPWS-SSW--EYLTETLVE-DPL------------------------AEVSDAYFATL-----KSEYNPACCDRSKVKIV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 242 FTGLCGVSGEFVKKALEFYNLDGSMHfIDEECIPNPNFPRLPFPNPEVP--------ETLARSKSSglgdIVFSCDPDGD 313
Cdd:PTZ00150 233 YTAMHGVGTRFVQKALHTVGLPNLLS-VAQQAEPDPEFPTVTFPNPEEGkgalklsmETAEAHGST----VVLANDPDAD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 314 RFGLSEKVGGEWVDYNGNEIAAMFMDFFVENF-----APSDLAFINTYLCNGLMEKVCSIHGIEYLRTETGFKNV-SRAV 387
Cdd:PTZ00150 308 RLAVAEKLNNGWKIFTGNELGALLAWWAMKRYrrqgiDKSKCFFICTVVSSRMLKKMAEKEGFQYDETLTGFKWIgNKAI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 388 DSVE---GKNVFAYEDSLGFLFGN-GKEKDGIKCVVLMASMVQrELPSRTLKRME-------RYGCFSSVNIHIRCTEPD 456
Cdd:PTZ00150 388 ELNAengLTTLFAYEEAIGFMLGTrVRDKDGVTAAAVVAEMAL-YLYERGKTLVEhleslykQYGYHFTNNSYYICYDPS 466
|
490 500 510
....*....|....*....|....*....|
gi 1154491712 457 RIlEKVLRKFpaaKTEGKRSTvEFDDYKVI 486
Cdd:PTZ00150 467 RI-VSIFNDI---RNNGSYPT-KLGGYPVT 491
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
33-499 |
2.04e-70 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 232.78 E-value: 2.04e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 33 FGTGGMRGLMRSGFNgiNEVTCNL---IGTELCRRF-SSIVIGCDGRYNSLNYAMILRGIFKLNGKEAVLYSEVATPFLA 108
Cdd:COG1109 7 FGTDGIRGIVGEELT--PEFVLKLgraFGTYLKEKGgPKVVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVPTPALA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 109 FLVSRLGADAGIMVTASHNPKEYNGFKVYTSNGSQIGSPLDREIEESMEMLNLTRLSGEEWygeifkrireendilgGKI 188
Cdd:COG1109 85 FAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKEDFRRAEAEEI----------------GKV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 189 ppasrktnmansagidfSRRDELVDCYnrwmfkgwSDSIVQAI--KSAGSPVPVVFTGLCGVSGEFVKKALEfyNLDGSM 266
Cdd:COG1109 149 -----------------TRIEDVLEAY--------IEALKSLVdeALRLRGLKVVVDCGNGAAGGVAPRLLR--ELGAEV 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 267 HFIDEEciPNPNFP-RLPFPNPEVPETLARS-KSSGLgDIVFSCDPDGDRFGLsekvggewVD-----YNGNEIAAMFMD 339
Cdd:COG1109 202 IVLNAE--PDGNFPnHNPNPEPENLEDLIEAvKETGA-DLGIAFDGDADRLGV--------VDekgrfLDGDQLLALLAR 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 340 FFVENFAPSdlAFINTYLCNGLMEKVCSIHGIEYLRTETGFKNVSRAVdsVEGKNVFAYEDSLGFLFG-NGKEKDGIKCV 418
Cdd:COG1109 271 YLLEKGPGG--TVVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKM--RETGAVLGGEESGGIIFPdFVPTDDGILAA 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 419 VLMASMVQRElpSRTLKRM-ERYGCFSSVNIHIRCTE---PDRILEKVLRKFPAAKTEGKRSTVEF---DDYKVILRVSG 491
Cdd:COG1109 347 LLLLELLAKQ--GKSLSELlAELPRYPQPEINVRVPDeekIGAVMEKLREAVEDKEELDTIDGVKVdleDGGWVLVRPSG 424
|
....*...
gi 1154491712 492 TESVLKVY 499
Cdd:COG1109 425 TEPLLRVY 432
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
31-517 |
3.69e-38 |
|
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: 145.77 E-value: 3.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 31 VKFGTGGMRGLMRSGFNGIN-----EVTCNLIGTELcRRFSSIVIGCDGRYNSLNYAMILRGIFKLNGKEAVLYSE-VAT 104
Cdd:cd05800 1 IKFGTDGWRGIIAEDFTFENvrrvaQAIADYLKEEG-GGGRGVVVGYDTRFLSEEFARAVAEVLAANGIDVYLSDRpVPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 105 PFLAFLVSRLGADAGIMVTASHNPKEYNGFKVYTSNGSQIGSPLDREIEESMEMLNLTRLSGEEWyGEIfkrirEENDIL 184
Cdd:cd05800 80 PAVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARLASGEPPGLEARAE-GLI-----ETIDPK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 185 GGKippasrktnmansagidFSRRDELVDcynrwmfkgwsdsiVQAIKSAGspVPVVFTGLCGVSGEFVKKALEFYNLDg 264
Cdd:cd05800 154 PDY-----------------LEALRSLVD--------------LEAIREAG--LKVVVDPMYGAGAGYLEELLRGAGVD- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 265 sMHFIDEEciPNPNFPRLPfPNPeVPETLA------RSKSSGLGdIVFscDPDGDRFGLSEKvGGEWVDynGNEIAAMFM 338
Cdd:cd05800 200 -VEEIRAE--RDPLFGGIP-PEP-IEKNLGelaeavKEGGADLG-LAT--DGDADRIGAVDE-KGNFLD--PNQILALLL 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 339 DFFVE----------NFAPSDlafintylcngLMEKVCSIHGIEYLRTETGFKNVSRAVDsvEGKNVFAYEDSLGFLFGN 408
Cdd:cd05800 269 DYLLEnkglrgpvvkTVSTTH-----------LIDRIAEKHGLPVYETPVGFKYIAEKML--EEDVLIGGEESGGLGIRG 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 409 G-KEKDGIKCVVLMASMVQREL--PSRTLKR-MERYGCFSSVNIHIRCTEPD--RILEKVLRKFPAAKTEGK-RSTVEFD 481
Cdd:cd05800 336 HiPERDGILAGLLLLEAVAKTGkpLSELVAElEEEYGPSYYDRIDLRLTPAQkeAILEKLKNEPPLSIAGGKvDEVNTID 415
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1154491712 482 DYKVIL--------RVSGTESVLKVYTSSEVLSK-GALTTAAKNF 517
Cdd:cd05800 416 GVKLVLedgswlliRPSGTEPLLRIYAEAPSPEKvEALLDAGKKL 460
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
33-499 |
1.01e-36 |
|
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: 141.17 E-value: 1.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 33 FGTGGMRGLmrsgfngINE-VTCNL---IGTELCRRF--SSIVIGCDGRYNS--LNYAMI--LRGIfklnGKEAVLYSEV 102
Cdd:cd03087 2 FGTSGIRGV-------VGEeLTPELalkVGKALGTYLggGTVVVGRDTRTSGpmLKNAVIagLLSA----GCDVIDIGIV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 103 ATPFLAFLVSRLGaDAGIMVTASHNPKEYNGFKVYTSNGSQIGSPLDREIEESMEMLNLTRLSGEEWyGEI--FKRIREE 180
Cdd:cd03087 71 PTPALQYAVRKLG-DAGVMITASHNPPEYNGIKLVNPDGTEFSREQEEEIEEIIFSERFRRVAWDEV-GSVrrEDSAIDE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 181 --NDILgGKIP-PASRKTNMAnsagidfsrrdelVDCYNrwmfkgwsdsivqaikSAGSPV-PVVFTGL-CGVsgefvkk 255
Cdd:cd03087 149 yiEAIL-DKVDiDGGKGLKVV-------------VDCGN----------------GAGSLTtPYLLRELgCKV------- 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 256 alefynldgsmhfIDEECIPNPNFP-RLPFPNPEVPETLARS-KSSGLgDIVFSCDPDGDR--FgLSEKvgGEWVDynGN 331
Cdd:cd03087 192 -------------ITLNANPDGFFPgRPPEPTPENLSELMELvRATGA-DLGIAHDGDADRavF-VDEK--GRFID--GD 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 332 EIAAMFMDFFVENFAPSDLAFINTYLCnglMEKVCSIHGIEYLRTETGFKNVSRAVDSVEGknVFAYEDSLGFLFGN-GK 410
Cdd:cd03087 253 KLLALLAKYLLEEGGGKVVTPVDASML---VEDVVEEAGGEVIRTPVGDVHVAEEMIENGA--VFGGEPNGGWIFPDhQL 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 411 EKDGIKCVVLMASMVQR---------ELPSRTLKRmerygcfssVNIHIRCTEPDRILEKVLRKFPAAK-----TEGKRs 476
Cdd:cd03087 328 CRDGIMTAALLLELLAEekplselldELPKYPLLR---------EKVECPDEKKEEVMEAVEEELSDADedvdtIDGVR- 397
|
490 500
....*....|....*....|...
gi 1154491712 477 tVEFDDYKVILRVSGTESVLKVY 499
Cdd:cd03087 398 -IEYEDGWVLIRPSGTEPKIRIT 419
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
33-500 |
2.15e-35 |
|
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: 137.64 E-value: 2.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 33 FGTGGMRGLmrsgfngINE-VTCNL-------IGTELcrRFSSIVIGCDGRYNSLNYAMILRGIFKLNGKEAVLYSEVAT 104
Cdd:TIGR03990 4 FGTSGIRGI-------VGEeLTPELalkvgkaFGTYL--RGGKVVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLGIAPT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 105 PFLAFLVSRLGADAGIMVTASHNPKEYNGFKVYTSNGSQIGSPLDREIEESMEmlnltrlSGE----EWYGeiFKRIREE 180
Cdd:TIGR03990 75 PTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQEEEIEEIAE-------SGDferaDWDE--IGTVTSD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 181 NDILGGKIppasrkTNMANSAGIDFSRRDEL---VDCYNrwmfkgwsdsivqaikSAGSPV-PVVFTGLcGVsgefvkKA 256
Cdd:TIGR03990 146 EDAIDDYI------EAILDKVDVEAIRKKGFkvvVDCGN----------------GAGSLTtPYLLREL-GC------KV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 257 LEFYnldgsmhfideeCIPNPNFP-RLPFPNPEVPETLARS-KSSGLgDIVFSCDPDGDRFGL-SEKvgGEWVDynGNEI 333
Cdd:TIGR03990 197 ITLN------------CQPDGTFPgRNPEPTPENLKDLSALvKATGA-DLGIAHDGDADRLVFiDEK--GRFIG--GDYT 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 334 AAMFMDFFVENfaPSDlAFINTYLCNGLMEKVCSIHGIEYLRTETGFKNVSRAVdsVEGKNVFAYEDSLGFLF-GNGKEK 412
Cdd:TIGR03990 260 LALFAKYLLEH--GGG-KVVTNVSSSRAVEDVAERHGGEVIRTKVGEVNVAEKM--KEEGAVFGGEGNGGWIFpDHHYCR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 413 DGIKCVVLMASMVQRE--LPSRTLKRMERYgCFSSVNIHIRCTEPDRILEKVLRKFPAAK---TEGKRstVEFDDYKVIL 487
Cdd:TIGR03990 335 DGLMAAALFLELLAEEgkPLSELLAELPKY-PMSKEKVELPDEDKEEVMEAVEEEFADAEidtIDGVR--IDFEDGWVLV 411
|
490
....*....|...
gi 1154491712 488 RVSGTESVLKVYT 500
Cdd:TIGR03990 412 RPSGTEPIVRIYA 424
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
104-499 |
7.68e-35 |
|
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: 134.41 E-value: 7.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 104 TPFLAFLVSRLGADAGIMVTASHNPKEYNGFKVYTSNGSQIGSPLDREIEESMEMLNLTRLSGEEWYGEifkrireendi 183
Cdd:cd03084 17 PETAVALGQAIGSTGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSAVAYELGGS----------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 184 lggkippasrktnmansagidfSRRDELVDCYnrwmFKGWSDSIVQAIKSaGSPVPVVFTGLCGVSGEFVKKALEFYNLD 263
Cdd:cd03084 86 ----------------------VKAVDILQRY----FEALKKLFDVAALS-NKKFKVVVDSVNGVGGPIAPQLLEKLGAE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 264 gsmhFIDEECIPNPNFPRLpFPNPEVPETL----ARSKSSGLgDIVFSCDPDGDRFGLSEKvGGEWVdyNGNEIAAMFMD 339
Cdd:cd03084 139 ----VIPLNCEPDGNFGNI-NPDPGSETNLkqllAVVKAEKA-DFGVAFDGDADRLIVVDE-NGGFL--DGDELLALLAV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 340 FFVENFAPsDLAFINTYLCNGLMEKVCSIHGIEYLRTETGFKNVSRAVDsvEGKNVFAYEDSLGFLF-GNGKEKDGIKCV 418
Cdd:cd03084 210 ELFLTFNP-RGGVVKTVVSSGALDKVAKKLGIKVIRTKTGFKWVGEAMQ--EGDVVLGGEESGGVIFpEFHPGRDGISAA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 419 VLMASMV-QREL-PSRTLKRMERYgcfssvnIHIRCTEPDRILekvlrkfpaaktegkrstvefddykviLRVSGTESVL 496
Cdd:cd03084 287 LLLLEILaNLGKsLSELFSELPRY-------YYIRLKVRGWVL---------------------------VRASGTEPAI 332
|
...
gi 1154491712 497 KVY 499
Cdd:cd03084 333 RIY 335
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
31-157 |
5.71e-31 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 116.94 E-value: 5.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 31 VKFGTGGMRGLMrsgfnGINEVTCNL-------IGTEL--CRRFSSIVIGCDGRYNSLNYAMILRGIFKLNGKEAVLYSE 101
Cdd:pfam02878 2 QLFGTSGIRGKV-----GVGELTPEFalklgqaIASYLraQGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVILLGL 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1154491712 102 VATPFLAFLVSRLGADAGIMVTASHNPKEYNGFKVYTSNGSQIGSPLDREIEESME 157
Cdd:pfam02878 77 LPTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIE 132
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
49-496 |
2.11e-29 |
|
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: 120.70 E-value: 2.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 49 INEVTCNLIGTELCRRF-----SSIVIGCDGRYNS--LNYAMIlRGIFKLnGKEAVLYSEVATPFLAFLVSRLGADAGIM 121
Cdd:cd03089 15 LTEEIAYAIGRAFGSWLlekgaKKVVVGRDGRLSSpeLAAALI-EGLLAA-GCDVIDIGLVPTPVLYFATFHLDADGGVM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 122 VTASHNPKEYNGFKVYTSNGSqigspldreieesmemlnltrLSGEEWYgEIFKRIrEENDILGGKIPPASRKTNMansa 201
Cdd:cd03089 93 ITASHNPPEYNGFKIVIGGGP---------------------LSGEDIQ-ALRERA-EKGDFAAATGRGSVEKVDI---- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 202 gidfsrrdelVDCYnrwmfkgwSDSIVQAIKSAGSPVPVVFTGLCGVSGEFVKKALEFYNLD-GSMHfideeCIPNPNFP 280
Cdd:cd03089 146 ----------LPDY--------IDRLLSDIKLGKRPLKVVVDAGNGAAGPIAPQLLEALGCEvIPLF-----CEPDGTFP 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 281 RLPfPNPEVPETLA------RSKSSGLGdIVFscDPDGDRFGLSEKVGGEwvdYNGNEIAAMFMDFFVENFAPSDlaFIN 354
Cdd:cd03089 203 NHH-PDPTDPENLEdliaavKENGADLG-IAF--DGDGDRLGVVDEKGEI---IWGDRLLALFARDILKRNPGAT--IVY 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 355 TYLCNGLMEKVCSIHGIEYLRTETGFKNVSRAVdsVEGKNVFAYEDSLGFLFgngKEK-----DGIKCVVLMASMVQREL 429
Cdd:cd03089 274 DVKCSRNLYDFIEEAGGKPIMWKTGHSFIKAKM--KETGALLAGEMSGHIFF---KDRwygfdDGIYAALRLLELLSKSG 348
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1154491712 430 --PSRTLKRMERYgcFSSVNIHIRCTE--PDRILEKVLRKFPAAK-----TEGKRstVEFDDYKVILRVSGTESVL 496
Cdd:cd03089 349 ktLSELLADLPKY--FSTPEIRIPVTEedKFAVIERLKEHFEFPGaeiidIDGVR--VDFEDGWGLVRASNTEPVL 420
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
223-322 |
3.32e-18 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 80.03 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 223 WSDSIVQAIKS---AGSPVPVVFTGLCGVSGEFVKKALEFYNLDgsmhFIDEECIPNPNFPRlPFPNPEVPETLARS--- 296
Cdd:pfam02879 2 YIDHLLELVDSealKKRGLKVVYDPLHGVGGGYLPELLKRLGCD----VVEENCEPDPDFPT-RAPNPEEPEALALLiel 76
|
90 100
....*....|....*....|....*..
gi 1154491712 297 -KSSGLgDIVFSCDPDGDRFGLSEKVG 322
Cdd:pfam02879 77 vKSVGA-DLGIATDGDADRLGVVDERG 102
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
66-503 |
7.39e-17 |
|
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: 83.13 E-value: 7.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 66 SSIVIGCDGRYNSLNYAMILRGIFKLNGKEAVLYSEVATPFLAFLVSRLGADAGIMVTASHNPKEYNGFKVYTSNGsqig 145
Cdd:cd05803 38 GKIVVGRDGRPSGPMLEKIVIGALLACGCDVIDLGIAPTPTVQVLVRQSQASGGIIITASHNPPQWNGLKFIGPDG---- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 146 spldreieesmemLNLTRLSGEewygEIFKRIREendilggkippasrktNMANSAGID-FSRRDELVDCYNRWMFKGWS 224
Cdd:cd05803 114 -------------EFLTPDEGE----EVLSCAEA----------------GSAQKAGYDqLGEVTFSEDAIAEHIDKVLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 225 DSIVQAIKSAGSPVPVVFTGLCGVSGEFVKKALEfyNLDGSMHFIDeeCIPNPNFPRLPFPNPE-VPETLARSKSSGlGD 303
Cdd:cd05803 161 LVDVDVIKIRERNFKVAVDSVNGAGGLLIPRLLE--KLGCEVIVLN--CEPTGLFPHTPEPLPEnLTQLCAAVKESG-AD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 304 IVFSCDPDGDRFGLsekvggewVDYNGNEIA-----AMFMDF----------FVENFAPSDlafintylcngLMEKVCSI 368
Cdd:cd05803 236 VGFAVDPDADRLAL--------VDEDGRPIGeeytlALAVDYvlkyggrkgpVVVNLSTSR-----------ALEDIARK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 369 HGIEYLRTETGFKNVsrAVDSVEGKNVFAYEdslgflfGNGKEKD-----------GIKCVV-LMASMvQRELpSRTLKR 436
Cdd:cd05803 297 HGVPVFRSAVGEANV--VEKMKEVDAVIGGE-------GNGGVILpdvhygrdslvGIALVLqLLAAS-GKPL-SEIVDE 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 437 MERYgCFSSVNIHIRCTEPDRILEKVLRKFPAAKTE---GKRstVEFDDYKVILRVSGTESVLKVYTSSE 503
Cdd:cd05803 366 LPQY-YISKTKVTIAGEALERLLKKLEAYFKDAEAStldGLR--LDSEDSWVHVRPSNTEPIVRIIAEAP 432
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
31-502 |
4.51e-16 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 80.95 E-value: 4.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 31 VKFGTGGMRG-LMRSGFNG--INEVTCNLIGTELCRRFSS-IVIGCDGRYnsLN---YAMILRgIFKLNGKEAVLYSE-- 101
Cdd:PRK07564 38 VKFGTSGHRGsSLQPSFNEnhILAIFQAICEYRGKQGITGpLFVGGDTHA--LSepaIQSALE-VLAANGVGVVIVGRgg 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 102 -VATPflafLVSRL---------GADAGIMVTASHNPKEYNGFKVYTSNGsqiGsPLDREIeesmemlnlTrlsgeEWyg 171
Cdd:PRK07564 115 yTPTP----AVSHAilkyngrggGLADGIVITPSHNPPEDGGIKYNPPNG---G-PADTDV---------T-----DA-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 172 eIFKRIRE--ENDILGGKIPPASRKTNMANSAGIDFsrrdelVDCYNRWMfkgwsDSIV--QAIKSAGspVPVVFTGLCG 247
Cdd:PRK07564 171 -IEARANEllAYGLKGVKRIPLDRALASMTVEVIDP------VADYVEDL-----ENVFdfDAIRKAG--LRLGVDPLGG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 248 VSGEFVKKALEFYNLDgsmhfidEECIpNP------NFPRLPF-----PNPEVPETLARS-KSSGLGDIVFSCDPDGDRF 315
Cdd:PRK07564 237 ATGPYWKAIAERYGLD-------LTVV-NApvdptfNFMPLDDdgkirMDCSSPYAMAGLlALKDAFDLAFANDPDGDRH 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 316 GLSEKVGgewvdyngneiaamFMDffvenfaPSD-LAFINTYLCN------------------GLMEKVCSIHGIEYLRT 376
Cdd:PRK07564 309 GIVTPGG--------------LMN-------PNHyLAVAIAYLFHhrpgwragagvgktlvssAMIDRVAAKLGRKLYEV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 377 ETGFKNVSRAVDSveGKNVFAYEDSLG--FLFGNGK----EKDGIKCVVLMASM--VQRELPSRTLKRM-ERYGCFSSVN 447
Cdd:PRK07564 368 PVGFKWFVNGLDD--GSLGFGGEESAGasFLRRDGSvwttDKDGLIAVLLAAEIlaVTGKSPSEIYRELwARFGRPYYSR 445
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1154491712 448 IHIRCTEPDR-ILEKVLRKFPAAKT------EGKRST------------VEFDDYKVILRVSGTESVLKVYTSS 502
Cdd:PRK07564 446 HDAPATPEQKaALRKLSPELVGATElagdpiDASLTEapgngaaigglkVVTENGWFAARPSGTETTYKIYAES 519
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
33-498 |
2.17e-15 |
|
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: 78.30 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 33 FGTGGMRGLmrsgFNgiNEVTCNL-------IGTELCRRFS--SIVIGCDGRYNS--LNYAMIlRGIfKLNGKEAVLYSE 101
Cdd:cd05802 2 FGTDGIRGV----AN--EPLTPELalklgraAGKVLGKGGGrpKVLIGKDTRISGymLESALA-AGL-TSAGVDVLLLGV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 102 VATPFLAFLVSRLGADAGIMVTASHNPKEYNGFKVYTSNGSQigspLDREIEESMEMLnltrLSGEEWYGEIFKRIreen 181
Cdd:cd05802 74 IPTPAVAYLTRKLRADAGVVISASHNPFEDNGIKFFSSDGYK----LPDEVEEEIEAL----IDKELELPPTGEKI---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 182 dilgGKIppasrkTNMANSAG--IDF----SRRDEL------VDCYNrwmfkGWSDSIVQAI-KSAGSPVPVVFTGLCGV 248
Cdd:cd05802 142 ----GRV------YRIDDARGryIEFlkstFPKDLLsglkivLDCAN-----GAAYKVAPEVfRELGAEVIVINNAPDGL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 249 SgefvkkalefYNLD-GSMHfideecipnpnfprlpfpnpevPETLARS-KSSGLgDIVFSCDPDGDR--Fglsekvgge 324
Cdd:cd05802 207 N----------INVNcGSTH----------------------PESLQKAvLENGA-DLGIAFDGDADRviA--------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 325 wVDYNGNEI------AAMFMDFFVENFAPSDLAfINTYLCNGLMEKVCSIHGIEYLRTETGFKNVSRAVdsVEGKNVFAY 398
Cdd:cd05802 245 -VDEKGNIVdgdqilAICARDLKERGRLKGNTV-VGTVMSNLGLEKALKELGIKLVRTKVGDRYVLEEM--LKHGANLGG 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 399 EDSLGFLFGN----GkekDGIKCVV-LMASMVQRELPSRTLKR-MERYgcfSSVNIHIRCTEPDRILEkvLRKFPAAKTE 472
Cdd:cd05802 321 EQSGHIIFLDhsttG---DGLLTALqLLAIMKRSGKSLSELASdMKLY---PQVLVNVRVKDKKALLE--NPRVQAAIAE 392
|
490 500
....*....|....*....|....*..
gi 1154491712 473 GKRstvEFDD-YKVILRVSGTESVLKV 498
Cdd:cd05802 393 AEK---ELGGeGRVLVRPSGTEPLIRV 416
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
67-502 |
7.34e-13 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 70.74 E-value: 7.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 67 SIVIGCDGRYNSLNYAMILRGIFKLNGKEAVLYSEVATPFLAFLVSRLGADAGIMVTASHNPKEYNGFKVYTSNGSQIgs 146
Cdd:PRK15414 40 TIVLGGDVRLTSETLKLALAKGLQDAGVDVLDIGMSGTEEIYFATFHLGVDGGIEVTASHNPMDYNGMKLVREGARPI-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 147 pldreieesmemlnltrlSGEEWYGEIfKRIREENDilggkIPPasrktnmANSAGIDFSRRDELVDCYNRWMFkGWSDs 226
Cdd:PRK15414 118 ------------------SGDTGLRDV-QRLAEAND-----FPP-------VDETKRGRYQQINLRDAYVDHLF-GYIN- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 227 iVQAIKsagsPVPVVFTGLCGVSGEFVkKALE--FYNLDGSMHFIDEECIPNPNFPRlPFPNPEVPETLARSKSSGL--- 301
Cdd:PRK15414 165 -VKNLT----PLKLVINSGNGAAGPVV-DAIEarFKALGAPVELIKVHNTPDGNFPN-GIPNPLLPECRDDTRNAVIkhg 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 302 GDIVFSCDPDGDR-FGLSEKvgGEWVDynGNEIAAMFMDFFVENFAPSDLafINTYLCNGLMEKVCSIHGIEYLRTETG- 379
Cdd:PRK15414 238 ADMGIAFDGDFDRcFLFDEK--GQFIE--GYYIVGLLAEAFLEKNPGAKI--IHDPRLSWNTVDVVTAAGGTPVMSKTGh 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 380 --FKNVSRAVDSVEGKNV--------FAYEDSlgflfgngkekdGIKCVVLMASMVQreLPSRTLKRM--ERYGCF-SSV 446
Cdd:PRK15414 312 afIKERMRKEDAIYGGEMsahhyfrdFAYCDS------------GMIPWLLVAELVC--LKGKTLGELvrDRMAAFpASG 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1154491712 447 NIHIRCTEPDRILEKVLRKFPAAKTEGKRS---TVEFDDYKVILRVSGTESVLKVYTSS 502
Cdd:PRK15414 378 EINSKLAQPVEAINRVEQHFSREALAVDRTdgiSMTFADWRFNLRSSNTEPVVRLNVES 436
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
329-440 |
1.72e-11 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 61.31 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 329 NGNEIAAMFMDFFVENFA-PSDLAFINTYLCNGLMEKVCSIHGIEYLRTETGFKNVSRAVDsvEGKNVFAYEDSLGFLFG 407
Cdd:pfam02880 1 DGDQILALLAKYLLEQGKlPPGAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMR--EEGALFGGEESGHIIFL 78
|
90 100 110
....*....|....*....|....*....|....*..
gi 1154491712 408 N-GKEKDGIKCVVLMASMVQRE---LPSRTLKRMERY 440
Cdd:pfam02880 79 DhATTKDGILAALLVLEILARTgksLSELLEELPEKY 115
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
32-141 |
1.29e-08 |
|
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: 57.21 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 32 KFGTGGMRGLmrsgfngINEVTCNLIGT---------ELCRRFSSIVIGCDGRYNSLNYAMILRGIFKLNGKEAVLYSEV 102
Cdd:cd03088 1 KFGTSGLRGL-------VTDLTDEVCYAytraflqhlESKFPGDTVAVGRDLRPSSPRIAAACAAALRDAGFRVVDCGAV 73
|
90 100 110
....*....|....*....|....*....|....*....
gi 1154491712 103 ATPFLAFLVSRLGAdAGIMVTASHNPKEYNGFKVYTSNG 141
Cdd:cd03088 74 PTPALALYAMKRGA-PAIMVTGSHIPADRNGLKFYRPDG 111
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
93-333 |
2.00e-08 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 56.99 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 93 GKEAVLYSEVATP--FLAFLVSRLGADAGIMVTASHNPKEYNGFKVYTSNGSqIGSPldrEIEesmemlnltrlsgeewy 170
Cdd:PLN02371 143 GLDVVDMGLATTPamFMSTLTEREDYDAPIMITASHLPYNRNGLKFFTKDGG-LGKP---DIK----------------- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 171 gEIFKRireendilggkippASRKTNMANSAGIDFSRR-DELVDCYNRWMfKGWSDSIVQAIK-SAGSPV----P----- 239
Cdd:PLN02371 202 -DILER--------------AARIYKEWSDEGLLKSSSgASSVVCRVDFM-STYAKHLRDAIKeGVGHPTnyetPlegfk 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 240 -VVFTGlCGVSGEFVKKALEFYNLD--GSMHFideecIPNPNFPRLPfPNPEVPETLA------RSKSSGLGdIVFscDP 310
Cdd:PLN02371 266 iVVDAG-NGAGGFFAEKVLEPLGADtsGSLFL-----EPDGMFPNHI-PNPEDKAAMSattqavLANKADLG-IIF--DT 335
|
250 260
....*....|....*....|...
gi 1154491712 311 DGDRFGLsekvggewVDYNGNEI 333
Cdd:PLN02371 336 DVDRSAV--------VDSSGREI 350
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
104-157 |
1.65e-06 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 50.52 E-value: 1.65e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1154491712 104 TPFLAFLVSRLGADAGIMVTASHNPKEYNGFKVYTSNGSQigspLDREIEESME 157
Cdd:PRK10887 78 TPAVAYLTRTLRAEAGIVISASHNPYYDNGIKFFSADGTK----LPDEVELAIE 127
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
107-144 |
5.53e-06 |
|
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: 49.13 E-value: 5.53e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1154491712 107 LAFLVSRL--GADAGIMVTASHNPKEYNGFKVYTSNGSQI 144
Cdd:cd03086 24 LAALRSKKlgGKTIGVMITASHNPVEDNGVKIVDPDGEML 63
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
66-415 |
1.51e-04 |
|
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: 44.52 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 66 SSIVIGCDGRYNSLNYAMIlrgIFKL---NGKEAVLYSE---VATPFLAFLVSRLGADAGIMVTASHNP---KEYNGFKV 136
Cdd:cd03085 50 ATLVVGGDGRYYNKEAIQI---IIKIaaaNGVGKVVVGQnglLSTPAVSAVIRKRKATGGIILTASHNPggpEGDFGIKY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 137 YTSNGSQIGSPLDREI-EESMEM----------LNLTRLSGEEWYGEIFkrireENDIlggkIPPASRKTNMANSAgIDF 205
Cdd:cd03085 127 NTSNGGPAPESVTDKIyEITKKIteykiaddpdVDLSKIGVTKFGGKPF-----TVEV----IDSVEDYVELMKEI-FDF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 206 srrdelvdcynrwmfkgwsdsivQAIKS--AGSPVPVVFTGLCGVSGEFVKKAlefynldgsmhFIDE---------ECI 274
Cdd:cd03085 197 -----------------------DAIKKllSRKGFKVRFDAMHGVTGPYAKKI-----------FVEElgapessvvNCT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 275 PNPNFPRL-PFPNPEVPETLARSKSSGLGDIVFSCDPDGDRfglsekvggewvdyngNEIAAmfMDFFVenfAPSD-LAF 352
Cdd:cd03085 243 PLPDFGGGhPDPNLTYAKDLVELMKSGEPDFGAASDGDGDR----------------NMILG--KGFFV---TPSDsVAV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 353 I--NTYLC-----NGL------------MEKVCSIHGIEYLRTETGFKNVSRAVDSveGKNVFAYEDSlgflFGNG---- 409
Cdd:cd03085 302 IaaNAKLIpyfykGGLkgvarsmptsgaLDRVAKKLGIPLFETPTGWKFFGNLMDA--GKLSLCGEES----FGTGsdhi 375
|
....*.
gi 1154491712 410 KEKDGI 415
Cdd:cd03085 376 REKDGL 381
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
114-159 |
2.75e-04 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 43.47 E-value: 2.75e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1154491712 114 LGADAGIMVTASHNPKEYNGFKVYTSNGSQigspLDREIEESMEML 159
Cdd:PLN02895 56 TGAATGLMITASHNPVSDNGVKIVDPSGGM----LPQAWEPFADAL 97
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
118-144 |
3.49e-04 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 43.49 E-value: 3.49e-04
10 20
....*....|....*....|....*..
gi 1154491712 118 AGIMVTASHNPKEYNGFKVYTSNGSQI 144
Cdd:PTZ00302 77 VGVMITASHNPIQDNGVKIIDPDGGML 103
|
|
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
33-440 |
1.41e-03 |
|
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: 41.08 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 33 FGTGGMRGLmrsgfngIN-EVTCNLIgTEL-------CRRFSSIVIGCDGRYNS--LNYAMIlRGIFkLNGKEAVLYSEV 102
Cdd:cd05805 2 FGGRGVSGL-------INvDITPEFA-TRLgaaygstLPPGSTVTVSRDASRASrmLKRALI-SGLL-STGVNVRDLGAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 103 ATPFLAFLVSRLGADAGIMVTASHNPKEYNGFKVYTSNGSQIGSPLDREIEESmemlnltrLSGEEwygeiFKRIReend 182
Cdd:cd05805 72 PLPVARYAIRFLGASGGIHVRTSPDDPDKVEIEFFDSRGLNISRAMERKIENA--------FFRED-----FRRAH---- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 183 ilGGKIPPASRKTNMansagIDFSRRDeLVDCYNRWMFKGWSDSIVqaIKSAGSPVPVVftgLCGVSGEFVKKALEFYNL 262
Cdd:cd05805 135 --VDEIGDITEPPDF-----VEYYIRG-LLRALDTSGLKKSGLKVV--IDYAYGVAGIV---LPGLLSRLGCDVVILNAR 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 263 DgsmhfideecipNPNFPRLPFPNPEVPETLARSKSSGLGDIVFSCDPDGDRFGLsekvggewVDYNGNEI-----AAMF 337
Cdd:cd05805 202 L------------DEDAPRTDTERQRSLDRLGRIVKALGADFGVIIDPNGERLIL--------VDEAGRVIsddllTALV 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 338 MD----------FFVENFAPSdlafintylcngLMEKVCSIHGIEYLRTETGFKNVSRAVDSV-----EGKNVFAY-EDS 401
Cdd:cd05805 262 SLlvlksepggtVVVPVTAPS------------VIEQLAERYGGRVIRTKTSPQALMEAALENvvlagDGDGGFIFpEFH 329
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1154491712 402 LGFlfgngkekDGIKCVV-LMASMVQRELP-SRTLKRMERY 440
Cdd:cd05805 330 PGF--------DAIAALVkILEMLARTNISlSQIVDELPRF 362
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
56-135 |
2.09e-03 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 40.73 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 56 LIGTELCrrfSSIVIGCDGRYNS--LNYAMIlRGIFKlNGKEAVLYSEVATPFLAFLVSRLGAdAGIMVTASHNPKEYNG 133
Cdd:PRK09542 29 LMRAEGA---TTVVIGHDMRDSSpeLAAAFA-EGVTA-QGLDVVRIGLASTDQLYFASGLLDC-PGAMFTASHNPAAYNG 102
|
..
gi 1154491712 134 FK 135
Cdd:PRK09542 103 IK 104
|
|
| PLN02307 |
PLN02307 |
phosphoglucomutase |
66-141 |
3.76e-03 |
|
phosphoglucomutase
Pssm-ID: 177942 [Multi-domain] Cd Length: 579 Bit Score: 40.02 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1154491712 66 SSIVIGCDGRYNSLNYAMILRGIFKLNGKEAVLYSE---VATPFL-AFLVSRLG--ADAGIMVTASHN---PKEYNGFKV 136
Cdd:PLN02307 62 ATLVLGGDGRYFNKEAIQIIIKIAAANGVRRVWVGQnglLSTPAVsAVIRERDGskANGGFILTASHNpggPEEDFGIKY 141
|
....*
gi 1154491712 137 YTSNG 141
Cdd:PLN02307 142 NYESG 146
|
|
| |
