|
Name |
Accession |
Description |
Interval |
E-value |
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
4-440 |
0e+00 |
|
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: 698.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 4 YFGTDGVRGVANQELTPELAFKLGRYGGYVLAhnKGEKHPRVLVGRDTRVSGEMLESALIAGLISIGAEVMRLGIISTPG 83
Cdd:cd05802 1 LFGTDGIRGVANEPLTPELALKLGRAAGKVLG--KGGGRPKVLIGKDTRISGYMLESALAAGLTSAGVDVLLLGVIPTPA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 84 VAYLTRDMGAELGVMISASHNPVADNGIKFFGSDGFKLSDEQENEIEALLDQENPELPrpVGNDIVHYSDYFEGAQKYLS 163
Cdd:cd05802 79 VAYLTRKLRADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVEEEIEALIDKELELPP--TGEKIGRVYRIDDARGRYIE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 164 YLKSTVDVN-FEGLKIALDGANGSTSSLAPFLFGDLEADTETIGCSPDGYNINEKCGSTHPEKLAEKVVETESDFGLAFD 242
Cdd:cd05802 157 FLKSTFPKDlLSGLKIVLDCANGAAYKVAPEVFRELGAEVIVINNAPDGLNINVNCGSTHPESLQKAVLENGADLGIAFD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 243 GDGDRIIAVDENGQIVDGDQIMFIIGQEMHKNQELNNDMIVSTVMSNLGFYKALEQEGIKSNKTKVGDRYVVEEMRRGNY 322
Cdd:cd05802 237 GDADRVIAVDEKGNIVDGDQILAICARDLKERGRLKGNTVVGTVMSNLGLEKALKELGIKLVRTKVGDRYVLEEMLKHGA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 323 NLGGEQSGHIVMMDYNTTGDGLLTGIQLASVIKMTGKSLSELAGQMKKYPQSLINVRVTDKYRVEENVDVKEVMTKVEVE 402
Cdd:cd05802 317 NLGGEQSGHIIFLDHSTTGDGLLTALQLLAIMKRSGKSLSELASDMKLYPQVLVNVRVKDKKALLENPRVQAAIAEAEKE 396
|
410 420 430
....*....|....*....|....*....|....*...
gi 446443636 403 MNGEGRILVRPSGTEPLVRVMVEAATDEDAERFAQQIA 440
Cdd:cd05802 397 LGGEGRVLVRPSGTEPLIRVMVEGEDEELVEKLAEELA 434
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
5-445 |
0e+00 |
|
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: 592.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 5 FGTDGVRGVANQE-LTPELAFKLGRYGGYVLAHNKGEKHpRVLVGRDTRVSGEMLESALIAGLISIGAEVMRLGIISTPG 83
Cdd:TIGR01455 1 FGTDGVRGRAGQEpLTAELALLLGAAAGRVLRQGRDTAP-RVVIGKDTRLSGYMLENALAAGLNSAGVDVLLLGPLPTPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 84 VAYLTRDMGAELGVMISASHNPVADNGIKFFGSDGFKLSDEQENEIEALLDQENPeLPRPVGNDIVHYSDYFEGAQKYLS 163
Cdd:TIGR01455 80 VAYLTRTLRADAGVMISASHNPYEDNGIKFFGPGGFKLDDATEAAIEALLDEADP-LPRPESEGLGRVKRYPDAVGRYIE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 164 YLKSTV--DVNFEGLKIALDGANGSTSSLAPFLFGDLEADTETIGCSPDGYNINEKCGSTHPEKLAEKVVETESDFGLAF 241
Cdd:TIGR01455 159 FLKSTLprGLTLSGLKVVLDCANGAAYKVAPHVFRELGAEVIAIGVEPDGLNINDGCGSTHLDALQKAVREHGADLGIAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 242 DGDGDRIIAVDENGQIVDGDQIMFIIGQEMHKNQELNNDMIVSTVMSNLGFYKALEQEGIKSNKTKVGDRYVVEEMRRGN 321
Cdd:TIGR01455 239 DGDADRVLAVDANGRIVDGDQILYIIARALKESGELAGNTVVATVMSNLGLERALEKLGLTLIRTAVGDRYVLEEMRESG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 322 YNLGGEQSGHIVMMDYNTTGDGLLTGIQLASVIKMTGKSLSELAGQMKKYPQSLINVRVTD-KYRVEENVDVKEVMTKVE 400
Cdd:TIGR01455 319 YNLGGEQSGHIILLDYSTTGDGIVSALQVLTIMKKSGSTLSELAAEFVPYPQTLVNVRVADrKLAAAEAPAVKAAIEDAE 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 446443636 401 VEMNGEGRILVRPSGTEPLVRVMVEAATDEDAERFAQQIADVVQD 445
Cdd:TIGR01455 399 AELGGTGRILLRPSGTEPLIRVMVEAADEELVQQLADTLADVVSA 443
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
3-445 |
0e+00 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 533.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 3 KYFGTDGVRGVANQE-LTPELAFKLGRYGGYVLAHNKgekHPRVLVGRDTRVSGEMLESALIAGLISIGAEVMRLGIIST 81
Cdd:PRK10887 2 KYFGTDGIRGKVGQApITPDFVLKLGWAAGKVLARQG---RPKVLIGKDTRISGYMLESALEAGLAAAGVDVLLTGPMPT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 82 PGVAYLTRDMGAELGVMISASHNPVADNGIKFFGSDGFKLSDEQENEIEALLDQEnpelPRPVGNDIVHYSDYFEGAQ-K 160
Cdd:PRK10887 79 PAVAYLTRTLRAEAGIVISASHNPYYDNGIKFFSADGTKLPDEVELAIEAELDKP----LTCVESAELGKASRINDAAgR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 161 YLSYLKSTV--DVNFEGLKIALDGANGSTSSLAPFLFGDLEADTETIGCSPDGYNINEKCGSTHPEKLAEKVVETESDFG 238
Cdd:PRK10887 155 YIEFCKSTFpnELSLRGLKIVVDCANGATYHIAPNVFRELGAEVIAIGCEPNGLNINDECGATDPEALQAAVLAEKADLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 239 LAFDGDGDRIIAVDENGQIVDGDQIMFIIGQEMHKNQELNNDmIVSTVMSNLGFYKALEQEGIKSNKTKVGDRYVVEEMR 318
Cdd:PRK10887 235 IAFDGDGDRVIMVDHLGNLVDGDQLLYIIARDRLRRGQLRGG-VVGTLMSNMGLELALKQLGIPFVRAKVGDRYVLEKLQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 319 RGNYNLGGEQSGHIVMMDYNTTGDGLLTGIQLASVIKMTGKSLSELAGQMKKYPQSLINVRVTDKYRVE-ENVDVKEVMT 397
Cdd:PRK10887 314 EKGWRLGGENSGHILCLDKTTTGDGIVAALQVLAAMVRSGMSLADLCSGMKLFPQVLINVRFKPGADDPlESEAVKAALA 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 446443636 398 KVEVEMNGEGRILVRPSGTEPLVRVMVEAATDEDAERFAQQIADVVQD 445
Cdd:PRK10887 394 EVEAELGGRGRVLLRKSGTEPLIRVMVEGEDEAQVTALAERIADAVKA 441
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
2-447 |
0e+00 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 531.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 2 GKYFGTDGVRGVANQELTPELAFKLGRYGGYVLAHNKGekhPRVLVGRDTRVSGEMLESALIAGLISIGAEVMRLGIIST 81
Cdd:COG1109 4 KKLFGTDGIRGIVGEELTPEFVLKLGRAFGTYLKEKGG---PKVVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 82 PGVAYLTRDMGAELGVMISASHNPVADNGIKFFGSDGFKLSDEQENEIEALLDQEnpELPRPVGNDIVHYSDYFEGAQKY 161
Cdd:COG1109 81 PALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKE--DFRRAEAEEIGKVTRIEDVLEAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 162 LSYLKSTVD--VNFEGLKIALDGANGSTSSLAPFLFGDLEADTETIGCSPDGYNINEKCG--STHPEKLAEKVVETESDF 237
Cdd:COG1109 159 IEALKSLVDeaLRLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFPNHNPNpePENLEDLIEAVKETGADL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 238 GLAFDGDGDRIIAVDENGQIVDGDQIMFIIGQEMHKNQElnNDMIVSTVMSNLGFYKALEQEGIKSNKTKVGDRYVVEEM 317
Cdd:COG1109 239 GIAFDGDADRLGVVDEKGRFLDGDQLLALLARYLLEKGP--GGTVVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKM 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 318 RRGNYNLGGEQSGHIVMMDYNTTGDGLLTGIQLASVIKMTGKSLSELAGQMKKYPQSLINVRVTDKYRVEENVD-VKEVM 396
Cdd:COG1109 317 RETGAVLGGEESGGIIFPDFVPTDDGILAALLLLELLAKQGKSLSELLAELPRYPQPEINVRVPDEEKIGAVMEkLREAV 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 397 TK---------VEVEMNGEGRILVRPSGTEPLVRVMVEAATDEDAERFAQQIADVVQDKM 447
Cdd:COG1109 397 EDkeeldtidgVKVDLEDGGWVLVRPSGTEPLLRVYAEAKDEEEAEELLAELAELVEEAL 456
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
2-443 |
5.78e-121 |
|
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: 359.90 E-value: 5.78e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 2 GKYFGTDGVRGVANQELTPELAFKLGR-YGGYVlahnkgeKHPRVLVGRDTRVSGEMLESALIAGLISIGAEVMRLGIIS 80
Cdd:TIGR03990 1 MLLFGTSGIRGIVGEELTPELALKVGKaFGTYL-------RGGKVVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLGIAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 81 TPGVAYLTRDMGAELGVMISASHNPVADNGIKFFGSDGFKLSDEQENEIEALLDQENPELPR--PVGNdivhYSDYFEGA 158
Cdd:TIGR03990 74 TPTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQEEEIEEIAESGDFERADwdEIGT----VTSDEDAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 159 QKYLSYLKSTVDVNF---EGLKIALDGANGSTSSLAPFLFGDLEADTETIGCSPDGYNINEkcgstHPE-------KLAE 228
Cdd:TIGR03990 150 DDYIEAILDKVDVEAirkKGFKVVVDCGNGAGSLTTPYLLRELGCKVITLNCQPDGTFPGR-----NPEptpenlkDLSA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 229 KVVETESDFGLAFDGDGDRIIAVDENGQIVDGDQIMFIIGQEMHKNQElnnDMIVSTVMSNLGFYKALEQEGIKSNKTKV 308
Cdd:TIGR03990 225 LVKATGADLGIAHDGDADRLVFIDEKGRFIGGDYTLALFAKYLLEHGG---GKVVTNVSSSRAVEDVAERHGGEVIRTKV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 309 GDRYVVEEMRRGNYNLGGEQSGHIVMMDYNTTGDGLLTGIQLASVIKMTGKSLSELAGQMKKYPQSLINVRVTDKyrvee 388
Cdd:TIGR03990 302 GEVNVAEKMKEEGAVFGGEGNGGWIFPDHHYCRDGLMAAALFLELLAEEGKPLSELLAELPKYPMSKEKVELPDE----- 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446443636 389 nvDVKEVMTKVEVEMNGE--------------GRILVRPSGTEPLVRVMVEAATDEDAERFAQQIADVV 443
Cdd:TIGR03990 377 --DKEEVMEAVEEEFADAeidtidgvridfedGWVLVRPSGTEPIVRIYAEAKTEERAEELLEEGRSLV 443
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
4-443 |
4.27e-112 |
|
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: 336.85 E-value: 4.27e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 4 YFGTDGVRGVANQELTPELAFKLGR-YGGYVlahnkgeKHPRVLVGRDTRVSGEMLESALIAGLISIGAEVMRLGIISTP 82
Cdd:cd03087 1 LFGTSGIRGVVGEELTPELALKVGKaLGTYL-------GGGTVVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDIGIVPTP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 83 GVAYLTRDMGaELGVMISASHNPVADNGIKFFGSDGFKLSDEQENEIEALLDQENpelPRPVGNDIVHYSDYFEGA-QKY 161
Cdd:cd03087 74 ALQYAVRKLG-DAGVMITASHNPPEYNGIKLVNPDGTEFSREQEEEIEEIIFSER---FRRVAWDEVGSVRREDSAiDEY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 162 LSYLKSTVDVNF-EGLKIALDGANGSTSSLAPFLFGDLEADTETIGCSPDGYNInekcgSTHPE-------KLAEKVVET 233
Cdd:cd03087 150 IEAILDKVDIDGgKGLKVVVDCGNGAGSLTTPYLLRELGCKVITLNANPDGFFP-----GRPPEptpenlsELMELVRAT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 234 ESDFGLAFDGDGDRIIAVDENGQIVDGDQIMFIIGQEMHKNQelnNDMIVSTVMSNLGFYKALEQEGIKSNKTKVGDRYV 313
Cdd:cd03087 225 GADLGIAHDGDADRAVFVDEKGRFIDGDKLLALLAKYLLEEG---GGKVVTPVDASMLVEDVVEEAGGEVIRTPVGDVHV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 314 VEEMRRGNYNLGGEQSGHIVMMDYNTTGDGLLTGiqlASVIKM--TGKSLSELAGQMKKYPQSLINVRVTDKYRVEENVD 391
Cdd:cd03087 302 AEEMIENGAVFGGEPNGGWIFPDHQLCRDGIMTA---ALLLELlaEEKPLSELLDELPKYPLLREKVECPDEKKEEVMEA 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446443636 392 VKEVMTKVEVEMN---------GEGRILVRPSGTEPLVRVMVEAATDEDAERFAQQIADVV 443
Cdd:cd03087 379 VEEELSDADEDVDtidgvrieyEDGWVLIRPSGTEPKIRITAEAKTEERAKELLEEGRSKV 439
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
10-443 |
1.70e-88 |
|
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: 276.32 E-value: 1.70e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 10 VRGVANQELTPELAFKLGR-YGGYVLAHNKgekhPRVLVGRDTRVSGEMLESALIAGLISIGAEVMRLGIISTPGVAYLT 88
Cdd:cd03089 7 IRGIAGEELTEEIAYAIGRaFGSWLLEKGA----KKVVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPVLYFAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 89 RDMGAELGVMISASHNPVADNGIKFFGSDGfKLSDEQENEIEALLDQENPELPRPVGNDIVHysDYFEgaqKYLSYLKST 168
Cdd:cd03089 83 FHLDADGGVMITASHNPPEYNGFKIVIGGG-PLSGEDIQALRERAEKGDFAAATGRGSVEKV--DILP---DYIDRLLSD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 169 VDVNFEGLKIALDGANGSTSSLAPFLFGDLEADTETIGCSPDGYNINEkcgstHP--------EKLAEKVVETESDFGLA 240
Cdd:cd03089 157 IKLGKRPLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCEPDGTFPNH-----HPdptdpenlEDLIAAVKENGADLGIA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 241 FDGDGDRIIAVDENGQIVDGDQIMFIIGQEMHKNQElnNDMIVSTVMSNLGFYKALEQEGIKSNKTKVGDRYVVEEMRRG 320
Cdd:cd03089 232 FDGDGDRLGVVDEKGEIIWGDRLLALFARDILKRNP--GATIVYDVKCSRNLYDFIEEAGGKPIMWKTGHSFIKAKMKET 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 321 NYNLGGEQSGHIVMMD-YNTTGDGLLTGIQLASVIKMTGKSLSELAGQMKKYPQSL-INVRVTDKY------RVEENVDV 392
Cdd:cd03089 310 GALLAGEMSGHIFFKDrWYGFDDGIYAALRLLELLSKSGKTLSELLADLPKYFSTPeIRIPVTEEDkfavieRLKEHFEF 389
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 446443636 393 KEV-MTKVE---VEMnGEGRILVRPSGTEPLVRVMVEAATDEDAERFAQQIADVV 443
Cdd:cd03089 390 PGAeIIDIDgvrVDF-EDGWGLVRASNTEPVLVLRFEADTEEGLEEIKAELRKLL 443
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
4-434 |
1.67e-74 |
|
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: 237.64 E-value: 1.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 4 YFGTDGVRGVANQELTPELAFKLGRyggyvlahnkgekhprvlvgrdtrvsgemlesaliaglisigaevmrlgiistpg 83
Cdd:cd03084 1 IFGTSGVRGVVGDDITPETAVALGQ------------------------------------------------------- 25
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 84 vAYLTRDmgaelGVMISASHNPVADNGIKFFGSDGFKLSDEQENEIEALLDQEnpELPRPVG---NDIVHYSDYfegAQK 160
Cdd:cd03084 26 -AIGSTG-----GIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKE--DEPSAVAyelGGSVKAVDI---LQR 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 161 YLSYLKSTVDV---NFEGLKIALDGANGSTSSLAPFLFGDLEADTETIGCSPDGY--NINEKCGS-THPEKLAEKVVETE 234
Cdd:cd03084 95 YFEALKKLFDVaalSNKKFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCEPDGNfgNINPDPGSeTNLKQLLAVVKAEK 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 235 SDFGLAFDGDGDRIIAVDENGQIVDGDQIMFIIGQEMhkNQELNNDM-IVSTVMSNLGFYKALEQEGIKSNKTKVGDRYV 313
Cdd:cd03084 175 ADFGVAFDGDADRLIVVDENGGFLDGDELLALLAVEL--FLTFNPRGgVVKTVVSSGALDKVAKKLGIKVIRTKTGFKWV 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 314 VEEMRRGNYNLGGEQSGHIVMMDYNTTGDGLLTGIQLASVIKMTGKSLSELAGQMKKYPQSLINVRvtdkyrveenvdvk 393
Cdd:cd03084 253 GEAMQEGDVVLGGEESGGVIFPEFHPGRDGISAALLLLEILANLGKSLSELFSELPRYYYIRLKVR-------------- 318
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 446443636 394 evmtkvevemngeGRILVRPSGTEPLVRVMVEAATDEDAER 434
Cdd:cd03084 319 -------------GWVLVRASGTEPAIRIYAEADTQEDVEQ 346
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
5-440 |
7.38e-66 |
|
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: 218.19 E-value: 7.38e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 5 FGTDGVRGVANQELTPE----LAFKLGRYggyvlAHNKGEKHPRVLVGRDTRVSGEmlESALIAglisigAEVMR-LGI- 78
Cdd:cd05800 3 FGTDGWRGIIAEDFTFEnvrrVAQAIADY-----LKEEGGGGRGVVVGYDTRFLSE--EFARAV------AEVLAaNGId 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 79 -------ISTPGVAYLTRDMGAELGVMISASHNPVADNGIKFFGSDGFKLSDEQENEIEALLDQENPELPRPVGNDIVHY 151
Cdd:cd05800 70 vylsdrpVPTPAVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARLASGEPPGLEARAEGLIET 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 152 SDYFEGaqkYLSYLKSTVDVNF---EGLKIALDGANGSTSSLAPFLFGDLEADTETIGCSPDGYninekCGSTHPE---- 224
Cdd:cd05800 150 IDPKPD---YLEALRSLVDLEAireAGLKVVVDPMYGAGAGYLEELLRGAGVDVEEIRAERDPL-----FGGIPPEpiek 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 225 ---KLAEKVVETESDFGLAFDGDGDRIIAVDENGQIVDGDQIMFIIGQEMHKNQELNNDmIVSTV-MSNLgFYKALEQEG 300
Cdd:cd05800 222 nlgELAEAVKEGGADLGLATDGDADRIGAVDEKGNFLDPNQILALLLDYLLENKGLRGP-VVKTVsTTHL-IDRIAEKHG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 301 IKSNKTKVGDRYVVEEMRRGNYNLGGEQSGHIVMMDYNTTGDGLLTGIQLASVIKMTGKSLSELAGQ-MKKYPQSL---I 376
Cdd:cd05800 300 LPVYETPVGFKYIAEKMLEEDVLIGGEESGGLGIRGHIPERDGILAGLLLLEAVAKTGKPLSELVAElEEEYGPSYydrI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 377 NVRVTD------KYRVEENVD-------VKEVMTK--VEVEMNGEGRILVRPSGTEPLVRVMVEAATDEDAER---FAQQ 438
Cdd:cd05800 380 DLRLTPaqkeaiLEKLKNEPPlsiaggkVDEVNTIdgVKLVLEDGSWLLIRPSGTEPLLRIYAEAPSPEKVEAlldAGKK 459
|
..
gi 446443636 439 IA 440
Cdd:cd05800 460 LA 461
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
9-438 |
1.66e-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: 203.69 E-value: 1.66e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 9 GVRGVANQELTPELAFKLGR-YGGYVLAHNKGekhPRVLVGRDTRVSGEMLESALIAGLISIGAEVMRLGIISTPGVAYL 87
Cdd:cd05803 6 GIRGIVGEGLTPEVITRYVAaFATWQPERTKG---GKIVVGRDGRPSGPMLEKIVIGALLACGCDVIDLGIAPTPTVQVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 88 TRDMGAELGVMISASHNPVADNGIKFFGSDGFKLSDEQENEIEALLdqENPELPrPVGND----IVHYSDYFegaQKYLS 163
Cdd:cd05803 83 VRQSQASGGIIITASHNPPQWNGLKFIGPDGEFLTPDEGEEVLSCA--EAGSAQ-KAGYDqlgeVTFSEDAI---AEHID 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 164 YLKSTVDVNFEG-----LKIALDGANGSTSSLAPFLFGDLEADTETIGCSPDGyninekcGSTH-PEKLAE-------KV 230
Cdd:cd05803 157 KVLALVDVDVIKirernFKVAVDSVNGAGGLLIPRLLEKLGCEVIVLNCEPTG-------LFPHtPEPLPEnltqlcaAV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 231 VETESDFGLAFDGDGDRIIAVDENG--------QIVDGDQIMFIIGQEMHknqelnndmIVSTVMSNLGFYKALEQEGIK 302
Cdd:cd05803 230 KESGADVGFAVDPDADRLALVDEDGrpigeeytLALAVDYVLKYGGRKGP---------VVVNLSTSRALEDIARKHGVP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 303 SNKTKVGDRYVVEEMRRGNYNLGGEQSGHIVMMDYNTTGDGlLTGIQLA-SVIKMTGKSLSELAGQMKKYPQSLINVRVT 381
Cdd:cd05803 301 VFRSAVGEANVVEKMKEVDAVIGGEGNGGVILPDVHYGRDS-LVGIALVlQLLAASGKPLSEIVDELPQYYISKTKVTIA 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446443636 382 DKYR------VEENVDVKEVMTKVEVEMNGE-GRILVRPSGTEPLVRVMVEAATDEDAERFAQQ 438
Cdd:cd05803 380 GEALerllkkLEAYFKDAEASTLDGLRLDSEdSWVHVRPSNTEPIVRIIAEAPTQDEAEALADR 443
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
2-136 |
5.88e-52 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 171.64 E-value: 5.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 2 GKYFGTDGVRGVANQ-ELTPELAFKLGR-YGGYVLAHNKGekhPRVLVGRDTRVSGEMLESALIAGLISIGAEVMRLGII 79
Cdd:pfam02878 1 RQLFGTSGIRGKVGVgELTPEFALKLGQaIASYLRAQGGG---GKVVVGRDTRYSSRELARALAAGLASNGVEVILLGLL 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 446443636 80 STPGVAYLTRDMGAELGVMISASHNPVADNGIKFFGSDGFKLSDEQENEIEALLDQE 136
Cdd:pfam02878 78 PTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKE 134
|
|
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
5-443 |
1.93e-46 |
|
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: 166.27 E-value: 1.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 5 FGTDGVRGVANQELTPELAFKLGRYGGYVLahnkgEKHPRVLVGRDTRVSGEMLESALIAGLISIGAEVMRLGIISTPGV 84
Cdd:cd05805 2 FGGRGVSGLINVDITPEFATRLGAAYGSTL-----PPGSTVTVSRDASRASRMLKRALISGLLSTGVNVRDLGALPLPVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 85 AYLTRDMGAELGVMISAShnpVADNG---IKFFGSDGFKLSDEQENEIEALLDQEnpELPRPVGNDIVHYSDYFEGAQKY 161
Cdd:cd05805 77 RYAIRFLGASGGIHVRTS---PDDPDkveIEFFDSRGLNISRAMERKIENAFFRE--DFRRAHVDEIGDITEPPDFVEYY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 162 LSYLKSTVD---VNFEGLKIALDGANGSTSSLAPFLFGDLEADTETIGCSPDGYN---INEKCGSThpEKLAEKVVETES 235
Cdd:cd05805 152 IRGLLRALDtsgLKKSGLKVVIDYAYGVAGIVLPGLLSRLGCDVVILNARLDEDAprtDTERQRSL--DRLGRIVKALGA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 236 DFGLAFDGDGDRIIAVDENGQIVDGDQIMFIIGqEMHKNQELNNDMIV----STVMSNLgfykaLEQEGIKSNKTKVGDR 311
Cdd:cd05805 230 DFGVIIDPNGERLILVDEAGRVISDDLLTALVS-LLVLKSEPGGTVVVpvtaPSVIEQL-----AERYGGRVIRTKTSPQ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 312 YVVEEMRRGNYNLGGEQSGHIVMMdYNTTGDGLLTgiqLASVIKM---TGKSLSELAGQMKKYpqSLINVRV----TDKY 384
Cdd:cd05805 304 ALMEAALENVVLAGDGDGGFIFPE-FHPGFDAIAA---LVKILEMlarTNISLSQIVDELPRF--YVLHKEVpcpwEAKG 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446443636 385 RV-----EENVDvKEVMTKVEVEMNGE-GRILVRPSGTEPLVRVMVEAATDEDAERFAQQIADVV 443
Cdd:cd05805 378 RVmrrliEEAPD-KSIELIDGVKIYEDdGWVLVLPDADEPLCHIYAEGSDQERAEELTEFYVEKV 441
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
10-443 |
2.75e-44 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 160.53 E-value: 2.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 10 VRGVANQELTPELAFKLGRYGGYVLahnKGEKHPRVLVGRDTRVSGEMLESALIAGLISIGAEVMRLGIISTPGVAYLTR 89
Cdd:PRK09542 6 VRGVVGEQIDEDLVRDVGAAFARLM---RAEGATTVVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIGLASTDQLYFASG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 90 DMGAElGVMISASHNPVADNGIKF-------FGSD-GFklsdeqeNEIEALLDQENPELPRPVGNdiVHYSDYFEGaqkY 161
Cdd:PRK09542 83 LLDCP-GAMFTASHNPAAYNGIKLcragakpVGQDtGL-------AAIRDDLIAGVPAYDGPPGT--VTERDVLAD---Y 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 162 LSYLKSTVDV-NFEGLKIALDGANGSTSSLAPFLFGDLEADTETIGCSPDGYNINEKCGSTHPEKLAE---KVVETESDF 237
Cdd:PRK09542 150 AAFLRSLVDLsGIRPLKVAVDAGNGMGGHTVPAVLGGLPITLLPLYFELDGTFPNHEANPLDPANLVDlqaFVRETGADI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 238 GLAFDGDGDRIIAVDENGQIVDGDQIMFIIGQemhknQELNNDmIVSTVMSNLGFYKA----LEQEGIKSNKTKVGDRYV 313
Cdd:PRK09542 230 GLAFDGDADRCFVVDERGQPVSPSAVTALVAA-----RELARE-PGATIIHNLITSRAvpelVAERGGTPVRTRVGHSFI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 314 VEEMRRGNYNLGGEQSGHIVMMDYNTTGDGLLTGIQLASVIKMTGKSLSELAGQMKKYPQS-LINVRVTDK----YRVEE 388
Cdd:PRK09542 304 KALMAETGAIFGGEHSAHYYFRDFWGADSGMLAALHVLAALGEQDRPLSELMADYQRYAASgEINSTVADAparmEAVLK 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 389 -----NVDVKEvMTKVEVEMNGEGRILVRPSGTEPLVRVMVEAATDEDAERFAQQIADVV 443
Cdd:PRK09542 384 afadrIVSVDH-LDGVTVDLGDGSWFNLRASNTEPLLRLNVEARTEEEVDALVDEVLAII 442
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
259-371 |
2.73e-42 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 145.28 E-value: 2.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 259 DGDQIMFIIGQEMHKNQELNND-MIVSTVMSNLGFYKALEQEGIKSNKTKVGDRYVVEEMRRGNYNLGGEQSGHIVMMDY 337
Cdd:pfam02880 1 DGDQILALLAKYLLEQGKLPPGaGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLDH 80
|
90 100 110
....*....|....*....|....*....|....*
gi 446443636 338 NTTGDGLLTGIQLASVIKMTGKSLSELAGQ-MKKY 371
Cdd:pfam02880 81 ATTKDGILAALLVLEILARTGKSLSELLEElPEKY 115
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
10-429 |
7.35e-35 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 135.07 E-value: 7.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 10 VRGVANQELTPELAFKLGR-YGGYVlahnkgeKHPRVLVGRDTRVSGEMLESALIAGLISIGAEVMRLGIISTPGVAYLT 88
Cdd:PRK15414 12 IRGKLGEELNEDIAWRIGRaYGEFL-------KPKTIVLGGDVRLTSETLKLALAKGLQDAGVDVLDIGMSGTEEIYFAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 89 RDMGAELGVMISASHNPVADNGIKFFGSDGFKLS-DEQENEIEALldQENPELPrPVGNDIVHYSDYFEGAQKYLSYLKS 167
Cdd:PRK15414 85 FHLGVDGGIEVTASHNPMDYNGMKLVREGARPISgDTGLRDVQRL--AEANDFP-PVDETKRGRYQQINLRDAYVDHLFG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 168 TVDV-NFEGLKIALDGANGSTSSLAPFL---FGDLEADTETIGC--SPDGYNINEKCGSTHPEKLAEK---VVETESDFG 238
Cdd:PRK15414 162 YINVkNLTPLKLVINSGNGAAGPVVDAIearFKALGAPVELIKVhnTPDGNFPNGIPNPLLPECRDDTrnaVIKHGADMG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 239 LAFDGDGDRIIAVDENGQIVDGDQIMFIIGQ---EMHKNQELNNDMIVS--TVmsnlgfyKALEQEGIKSNKTKVGDRYV 313
Cdd:PRK15414 242 IAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEaflEKNPGAKIIHDPRLSwnTV-------DVVTAAGGTPVMSKTGHAFI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 314 VEEMRRGNYNLGGEQSGHIVMMDYNTTGDGLLTGIQLASVIKMTGKSLSEL-AGQMKKYPQS-LINVRVTDKY----RVE 387
Cdd:PRK15414 315 KERMRKEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELVCLKGKTLGELvRDRMAAFPASgEINSKLAQPVeainRVE 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 446443636 388 ENV--DVKEVMTKVEVEMN-GEGRILVRPSGTEPLVRVMVEAATD 429
Cdd:PRK15414 395 QHFsrEALAVDRTDGISMTfADWRFNLRSSNTEPVVRLNVESRGD 439
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
5-444 |
1.31e-33 |
|
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: 131.86 E-value: 1.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 5 FGTDGVRGV----ANQ--ELT-PELAFKLGRYggyVLAHNKGEKHPRVLVGRDTRVSGEM--LESALIagLISIGAEVMR 75
Cdd:cd05799 4 FGTAGLRGKmgagTNRmnDYTvRQATQGLANY---LKKKGPDAKNRGVVIGYDSRHNSREfaELTAAV--LAANGIKVYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 76 L-GIISTPGVAYLTRDMGAELGVMISASHNPVADNGIKFFGSDGFKLSDEQENEIEALLDQ------------ENPELPR 142
Cdd:cd05799 79 FdDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEAvlepldikfeeaLDSGLIK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 143 PVGNDIvhYSDYFEGAQKYLSYLKSTVDVNfegLKIALDGANGSTSSLAPFLFGDLEADTETIG---CSPDGY------- 212
Cdd:cd05799 159 YIGEEI--DDAYLEAVKKLLVNPELNEGKD---LKIVYTPLHGVGGKFVPRALKEAGFTNVIVVeeqAEPDPDfptvkfp 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 213 NINEKCGSTHPEKLAEKVvetESDFGLAFDGDGDRI-IAV-DENG--QIVDGDQIMFIIG----QEMHKNQELNND--MI 282
Cdd:cd05799 234 NPEEPGALDLAIELAKKV---GADLILATDPDADRLgVAVkDKDGewRLLTGNEIGALLAdyllEQRKEKGKLPKNpvIV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 283 VSTVMSNLGfyKAL-EQEGIKSNKTKVGDRY---VVEEMRRGNYNL--GGEQS-GHIVmMDYNTTGDGLLTGIQLASVI- 354
Cdd:cd05799 311 KTIVSSELL--RKIaKKYGVKVEETLTGFKWignKIEELESGGKKFlfGFEESiGYLV-GPFVRDKDGISAAALLAEMAa 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 355 --KMTGKSLSE-LAGQMKKY---PQSLINVRVTDKYRVEEnvdVKEVMTK-------VEVEMNGEGRILVRPSGTEPLVR 421
Cdd:cd05799 388 ylKAQGKTLLDrLDELYEKYgyyKEKTISITFEGKEGPEK---IKAIMDRlrnnpnvLTFYLEDGSRVTVRPSGTEPKIK 464
|
490 500
....*....|....*....|...
gi 446443636 422 VMVEAATDEDAERFAQQIADVVQ 444
Cdd:cd05799 465 FYIEVVGKKTLEEAEKKLDALKK 487
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
6-450 |
1.55e-30 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 124.01 E-value: 1.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 6 GTDgVRGVANQ-------ELTPELAFKLGRYGGYVLAHNK---GEKHPRVLVGRDTRVSGEMLESALIAGLISIGAEVMR 75
Cdd:PLN02371 70 GSD-IRGVAVEgvegepvTLTPPAVEAIGAAFAEWLLEKKkadGSGELRVSVGRDPRISGPRLADAVFAGLASAGLDVVD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 76 LGIISTPGVAYLTRDMGAEL--GVMISASHNPVADNGIKFFGSDGfKLSDEqenEIEALLDQ----------ENPELPRP 143
Cdd:PLN02371 149 MGLATTPAMFMSTLTEREDYdaPIMITASHLPYNRNGLKFFTKDG-GLGKP---DIKDILERaariykewsdEGLLKSSS 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 144 VGNDIVHYSDYFEgaqKYLSYLKSTV--DVNF--------EGLKIALDGANGSTSSLAPFLFGDLEADTE-TIGCSPDGY 212
Cdd:PLN02371 225 GASSVVCRVDFMS---TYAKHLRDAIkeGVGHptnyetplEGFKIVVDAGNGAGGFFAEKVLEPLGADTSgSLFLEPDGM 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 213 NINekcGSTHPEK------LAEKVVETESDFGLAFDGDGDRIIAVDENGQIVDGDQ---IMFIIGQEMHKNQelnndMIV 283
Cdd:PLN02371 302 FPN---HIPNPEDkaamsaTTQAVLANKADLGIIFDTDVDRSAVVDSSGREINRNRliaLMSAIVLEEHPGT-----TIV 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 284 STVMSNLGFYKALEQEGIKSNKTKVGDRYVVEEMRRGN-----YNLGGEQSGHIVMMDYNTTGDGLLTGIQLasVIKMTG 358
Cdd:PLN02371 374 TDSVTSDGLTTFIEKKGGKHHRFKRGYKNVIDKGVRLNsdgeeTHLMIETSGHGALKENHFLDDGAYLAVKI--IIELVR 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 359 KSLSELAGQMKKYPQSLINVRVTDKYRV---EENVDVKEVMTKVE------------------------VEMNGEGR--- 408
Cdd:PLN02371 452 MRAAGAGGGLGDLIEDLEEPLEAVELRLkilDEGKDFKAYGEEVLehlrnsiesdgklegapvnyegvrVSDEGEGFggw 531
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 446443636 409 ILVRPSGTEPLVRVMVEAATDEDAERFAQQIADVVQDKMGLD 450
Cdd:PLN02371 532 FLLRQSLHDPVIPLNIESSSPGGAQKMALVVLTWLKEFAALD 573
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
43-443 |
8.71e-27 |
|
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: 112.69 E-value: 8.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 43 PRVLVGRDTRVSGEMLESALIAGLISIGAEVMRLGIISTPGVAYLTRdmgaelgvmisaSHNpvadngikffgsdgfkls 122
Cdd:cd03086 103 ANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYLVR------------AAN------------------ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 123 deqeneiealldqenpELPRPVGNDIVHYSDYFEGAQKYLSYLKSTVDVNFEGLKIalDGANGstsslapflFGDLEADt 202
Cdd:cd03086 153 ----------------TEGAYGEPTEEGYYEKLSKAFNELYNLLQDGGDEPEKLVV--DCANG---------VGALKLK- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 203 ETIGCSPDGYNIN-EKCGSTHPEKLAEKV----VETE----SDFGL--------AFDGDGDRIIA--VDENGQ--IVDGD 261
Cdd:cd03086 205 ELLKRLKKGLSVKiINDGEEGPELLNDGCgadyVKTKqkppRGFELkppgvrccSFDGDADRLVYfyPDSSNKfhLLDGD 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 262 QI-----MFIigQEMHKNQELNNDM---IVSTVMSNLGFYKALEQE-GIKSNKTKVGDRYVVEEMRR---GNY------- 322
Cdd:cd03086 285 KIatlfaKFI--KELLKKAGEELKLtigVVQTAYANGASTKYLEDVlKVPVVCTPTGVKHLHHAAEEfdiGVYfeanghg 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 323 ----------------NLGGEQSGHIVMMDY------NTTGDGLlTGIQLASVI-KMTGKSLSELAGQMKKYPQSLINVR 379
Cdd:cd03086 363 tvlfsesalakieensSLSDEQEKAAKTLLAfsrlinQTVGDAI-SDMLAVELIlAALGWSPQDWDNLYTDLPNRQLKVK 441
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446443636 380 VTDKyRVEENVDVKEVMTK---------VEVEMNGEGRILVRPSGTEPLVRVMVEAATDEDAERFAQQIADVV 443
Cdd:cd03086 442 VPDR-SVIKTTDAERRLVEpkglqdkidAIVAKYNNGRAFVRPSGTEDVVRVYAEAATQEEADELANEVAELV 513
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
5-438 |
8.79e-27 |
|
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: 111.91 E-value: 8.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 5 FGTDGVRGVANqELTPELAFklgrygGYVLA-------HNKGEKhprVLVGRDTRVSGEMLESALIAGLISIGAEVMRLG 77
Cdd:cd03088 2 FGTSGLRGLVT-DLTDEVCY------AYTRAflqhlesKFPGDT---VAVGRDLRPSSPRIAAACAAALRDAGFRVVDCG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 78 IISTPGVAY--LTRDMGAelgVMISASHNPVADNGIKFFGSDGfKLSDEQENEIEALLDQENPELPRPVGNDIVH----- 150
Cdd:cd03088 72 AVPTPALALyaMKRGAPA---IMVTGSHIPADRNGLKFYRPDG-EITKADEAAILAALVELPEALFDPAGALLPPdtdaa 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 151 ------YSDYF-EGAQKYLS---YLKSTV--DVN---FEGLkialdGAN----GSTSSLAPFlfgDLEA-DTETIgcspd 210
Cdd:cd03088 148 dayiarYTDFFgAGALKGLRigvYQHSSVgrDLLvriLEAL-----GAEvvplGRSDTFIPV---DTEAvRPEDR----- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 211 gyninekcgsthpEKLAEKVVETESDFGLAFDGDGDRIIAVDENGQIVDGDqIMFIIGQemhknQELNNDMIVSTVMSNl 290
Cdd:cd03088 215 -------------ALAAAWAAEHGLDAIVSTDGDGDRPLVADETGEWLRGD-ILGLLTA-----RFLGADTVVTPVSSN- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 291 gfyKALEQEGIKSN--KTKVGDRYVVEEMRRgnynLGGEQSGHIVMMDYN-------------------TTGDGLLTGIQ 349
Cdd:cd03088 275 ---SAIELSGFFKRvvRTRIGSPYVIAAMAE----AAAAGAGRVVGYEANggfllgsdierngrtlkalPTRDAVLPILA 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 350 LASVIKMTGKSLSELAGQmkkYPQslinvRVTDKYRVeENVDVK-------------EVMTKVEVEMNGE---------- 406
Cdd:cd03088 348 VLAAAKEAGIPLSELVAS---LPA-----RFTASDRL-QNFPTEksqaliarlsadpEARAAFFFALGGEvasidttdgl 418
|
490 500 510
....*....|....*....|....*....|....*....
gi 446443636 407 ------GRIL-VRPSGTEPLVRVMVEAATDEDAERFAQQ 438
Cdd:cd03088 419 rmtfanGDIVhLRPSGNAPELRCYVEADSEERARELLAR 457
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
35-448 |
1.91e-21 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 97.02 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 35 AHNKGEKHPRVLVGRDTRVSGEMLESALIAGLISIGAEVMRLGIISTPgvayltrdmgaELGVMISASHNPVADngikff 114
Cdd:PLN02895 120 PAVGGNPPAEVLLGRDTRPSGPALLAAALKGVRAIGARAVDMGILTTP-----------QLHWMVRAANKGMKA------ 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 115 gsdgfklsdeqeneiealldqenpelprpvgndivHYSDYFEGAQKYLSYLKSTVD----VNFEGLKIALDGANG----S 186
Cdd:PLN02895 183 -----------------------------------TESDYFEQLSSSFRALLDLIPngsgDDRADDKLVVDGANGvgaeK 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 187 TSSLAPfLFGDLEADTETIGCSPDGyNINEKCGSTHPEKlaEKVVETE---SDFGL---AFDGDGDRIIAVDENG----- 255
Cdd:PLN02895 228 LETLKK-ALGGLDLEVRNSGKEGEG-VLNEGVGADFVQK--EKVPPTGfasKDVGLrcaSLDGDADRLVYFYVSSagski 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 256 QIVDGDQIMFI----IGQEMHKNQELNNDM---------IVSTVMSNLGFYKALEQE-GIKSNKTKVGDRYVVEEMRRgn 321
Cdd:PLN02895 304 DLLDGDKIASLfalfIKEQLRILNGNGNEKpeellvrlgVVQTAYANGASTAYLKQVlGLEVVCTPTGVKYLHEAAAE-- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 322 YNLG--GEQSGH--IVMMDY------------------------------------NTTGDGLlTGIQLASVI-KMTGKS 360
Cdd:PLN02895 382 FDIGvyFEANGHgtVLFSERfldwleaaaaelsskakgseahkaarrllavsrlinQAVGDAL-SGLLLVEAIlQYRGWS 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 361 LSELAGQMKKYPQSLINVRVTDK---------YRVEENVDVKEVMTKvEVEMNGEGRILVRPSGTEPLVRVMVEAATDED 431
Cdd:PLN02895 461 LAEWNALYQDLPSRQLKVKVADRtaitttdaeTVVVRPAGLQDAIDA-EVAKYPRGRAFVRPSGTEDVVRVYAEASTQEA 539
|
490
....*....|....*..
gi 446443636 432 AERFAQQIADVVQDKMG 448
Cdd:PLN02895 540 ADSLAREVARLVYDLLG 556
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
375-444 |
4.48e-19 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 81.16 E-value: 4.48e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446443636 375 LINVRVTDKYRVEENVDVKEVMTKVEVEMNGEGRIL-VRPSGTEPLVRVMVEAATDEDAERFAQQIADVVQ 444
Cdd:pfam00408 1 LINVRVAEKKKLAALAAILKVFADAEKILGEDGRRLdVRPSGTEPVLRVMVEGDSDEELARLADEIADLLE 71
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
45-448 |
2.59e-15 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 78.16 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 45 VLVGRDTRVSGEMLESALIAGL-ISIGAEVMRLGIISTPGVAYLTRdmgaelgvmisashnpvADNGikfFGSDGFKLSD 123
Cdd:PTZ00302 155 VHVGRDTRPSSPELVSALLRGLkLLIGSNVRNFGIVTTPQLHFLVA-----------------FANG---LGVDVVESSD 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 124 EQeneiealldqenpelprpvgndivhYSDYFEGAQKYLSYLKSTVDVNFEG----LKIALDGANGSTS-SLAPFL--FG 196
Cdd:PTZ00302 215 EL-------------------------YYAYLLAAFKELYRTLQEGGPVDLTqnnsKILVVDCANGVGGyKIKRFFeaLK 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 197 DLEADTETIGCSPDGYNI-NEKCGSTHPEK---LAEKVVETESDFGL---AFDGDGDRIIA--VDENG----QIVDGDQI 263
Cdd:PTZ00302 270 QLGIEIIPININCDEEELlNDKCGADYVQKtrkPPRAMKEWPGDEETrvaSFDGDADRLVYffPDKDGddkwVLLDGDRI 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 264 -----MFIigQEMHKNQELNNDM---IVSTVMSNLGFYKALEQE-----------GIK----------------SN---- 304
Cdd:PTZ00302 350 ailyaMLI--KKLLGKIQLKKKLdigVVQTAYANGASTNYLNELlgrlrvycaptGVKnlhpkahkydigiyfeANghgt 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 305 ---KTKVGDRYVVEEMRRGNYNLGGEQSGHIVMMDYNTTGDGL--LTGIQLA-SVIKMTGKslsELAGQMKKYPQSLINV 378
Cdd:PTZ00302 428 vlfNEKALAEWAKFLAKQNALNSACRQLEKFLRLFNQTIGDAIsdLLAVELAlAFLGLSFQ---DWLNLYTDLPSRQDKV 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 379 RVTDKYRVEENVDVKEVMT----------KVEVEMNGeGRILVRPSGTEPLVRVMVEAATDEDAERFAQQIADVVQDKMG 448
Cdd:PTZ00302 505 TVKDRTLITNTEDETRLLEpkglqdkidaIVSKYDNA-ARAFIRPSGTEPVVRVYAEAPTLEQADELANEVKGLVLRYCS 583
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
161-255 |
5.56e-14 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 67.70 E-value: 5.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 161 YLSYLKSTVDVNFE---GLKIALDGANGSTSSLAPFLFGDLEADTETIGCSPDGYNinekcGSTHPE--------KLAEK 229
Cdd:pfam02879 2 YIDHLLELVDSEALkkrGLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDPDF-----PTRAPNpeepealaLLIEL 76
|
90 100
....*....|....*....|....*.
gi 446443636 230 VVETESDFGLAFDGDGDRIIAVDENG 255
Cdd:pfam02879 77 VKSVGADLGIATDGDADRLGVVDERG 102
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
5-322 |
6.05e-09 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 58.16 E-value: 6.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 5 FGTDGVRG-----------VANQELTPELAfklgrygGYVLAHNKGEKHPR-VLVGRDTRVSGEMLESALIAGLISIGAE 72
Cdd:PTZ00150 47 FGTAGLRGkmgagfncmndLTVQQTAQGLC-------AYVIETFGQALKSRgVVIGYDGRYHSRRFAEITASVFLSKGFK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 73 VMRLG-IISTPGVAYLTRDMGAELGVMISASHNPVADNGIKFFGSDGFKLSDEQENEIEALLDqENPElPRPVGNDIVHY 151
Cdd:PTZ00150 120 VYLFGqTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVYWSNGAQIIPPHDKNISAKIL-SNLE-PWSSSWEYLTE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 152 SD----YFEGAQKYLSYLKSTVDVN-FEG--LKI---ALDGANG-------STSSLAPFLFGDLEADtetigcsPDGY-- 212
Cdd:PTZ00150 198 TLvedpLAEVSDAYFATLKSEYNPAcCDRskVKIvytAMHGVGTrfvqkalHTVGLPNLLSVAQQAE-------PDPEfp 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 213 -----NINEKCGSThpeKLAEKVVETE-SDFGLAFDGDGDRI-IAVDENG--QIVDGDQIMFIIG-QEMHKNQELNNDM- 281
Cdd:PTZ00150 271 tvtfpNPEEGKGAL---KLSMETAEAHgSTVVLANDPDADRLaVAEKLNNgwKIFTGNELGALLAwWAMKRYRRQGIDKs 347
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 446443636 282 ---IVSTVMSNLGFYKALEQEGIKSNKTKVGDRYV---VEEMRRGNY 322
Cdd:PTZ00150 348 kcfFICTVVSSRMLKKMAEKEGFQYDETLTGFKWIgnkAIELNAENG 394
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
77-247 |
1.09e-08 |
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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: 57.23 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 77 GIISTPGVAYLTRDMGAELGVMISASHNP---VADNGIKFFGSDG--------------------FKLSDEQENEIEALL 133
Cdd:cd03085 87 GLLSTPAVSAVIRKRKATGGIILTASHNPggpEGDFGIKYNTSNGgpapesvtdkiyeitkkiteYKIADDPDVDLSKIG 166
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 134 DQENPELPRPVgnDIVHysdyfeGAQKYLSYLKSTVD-------VNFEGLKIALDGANGSTSSLAPFLFGD-LEADTET- 204
Cdd:cd03085 167 VTKFGGKPFTV--EVID------SVEDYVELMKEIFDfdaikklLSRKGFKVRFDAMHGVTGPYAKKIFVEeLGAPESSv 238
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170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446443636 205 IGCSPdgyniNEKCGSTHP-------EKLAEKVVETESDFGLAFDGDGDR 247
Cdd:cd03085 239 VNCTP-----LPDFGGGHPdpnltyaKDLVELMKSGEPDFGAASDGDGDR 283
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| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
47-247 |
1.27e-06 |
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phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 50.52 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 47 VGRDTR-VSGEMLESAL---IAGlisiGAEVM---RLGIISTPGV-----AYLTRDMGAELGVMISASHNPVADNGIKFF 114
Cdd:PRK07564 81 VGGDTHaLSEPAIQSALevlAAN----GVGVVivgRGGYTPTPAVshailKYNGRGGGLADGIVITPSHNPPEDGGIKYN 156
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 115 GSDG----FKLSDEQENEIEALLDQENPELPR-----PVGNDIVHYSDYfegAQKYLSYLKSTVDvnFE-----GLKIAL 180
Cdd:PRK07564 157 PPNGgpadTDVTDAIEARANELLAYGLKGVKRipldrALASMTVEVIDP---VADYVEDLENVFD--FDairkaGLRLGV 231
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446443636 181 DGANGST----SSLAPFLFGDLE-----ADTeTIGCSP---DGyNINEKCGSTHpeKLAEKVVETES-DFGLAFDGDGDR 247
Cdd:PRK07564 232 DPLGGATgpywKAIAERYGLDLTvvnapVDP-TFNFMPlddDG-KIRMDCSSPY--AMAGLLALKDAfDLAFANDPDGDR 307
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