|
Name |
Accession |
Description |
Interval |
E-value |
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
4-445 |
0e+00 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 913.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 4 RKYFGTDGIRGRVGDAPITPEFVLKLGWAAGKVLARHGSRKIIIGKDTRISGYMLESALEAGLAAAGLSASFTGPMPTPA 83
Cdd:PRK10887 1 RKYFGTDGIRGKVGQAPITPDFVLKLGWAAGKVLARQGRPKVLIGKDTRISGYMLESALEAGLAAAGVDVLLTGPMPTPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 84 IAYLTRTFRAEAGIVISASHNPFYDNGIKFFSIEGTKLPDEVEEAIEAEMEKELTCVDSAELGKASRIVDAAGRYIEFCK 163
Cdd:PRK10887 81 VAYLTRTLRAEAGIVISASHNPYYDNGIKFFSADGTKLPDEVELAIEAELDKPLTCVESAELGKASRINDAAGRYIEFCK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 164 GTFPNELSLNSLKVVVDCAHGATYHIAPSVFRELGAQVIAMGCEPDGLNINEEVGATDVRALQARVLEEKADLGIAYDGD 243
Cdd:PRK10887 161 STFPNELSLRGLKIVVDCANGATYHIAPNVFRELGAEVIAIGCEPNGLNINDECGATDPEALQAAVLAEKADLGIAFDGD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 244 GDRVIMVDHEGNKVDGDQILYIIAREGLRQGQLRGGAVGTLMSNMGLELALKQLGIPFVRAKVGDRYVLEKLQEKGWRIG 323
Cdd:PRK10887 241 GDRVIMVDHLGNLVDGDQLLYIIARDRLRRGQLRGGVVGTLMSNMGLELALKQLGIPFVRAKVGDRYVLEKLQEKGWRLG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 324 AENSGHVILLDKTTTGDGIVASLQVVAAMVRNHMSLHDLCSGMKMFPQLLVNVRFTEGSGNPLEHEHVKAVTAEVEAELG 403
Cdd:PRK10887 321 GENSGHILCLDKTTTGDGIVAALQVLAAMVRSGMSLADLCSGMKLFPQVLINVRFKPGADDPLESEAVKAALAEVEAELG 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 490207696 404 NRGRVLLRKSGTEPLIRVMVEGEHEEKVHEFAHRIADAVKSV 445
Cdd:PRK10887 401 GRGRVLLRKSGTEPLIRVMVEGEDEAQVTALAERIADAVKAA 442
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
6-439 |
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: 715.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 6 YFGTDGIRGRVGdAPITPEFVLKLGWAAGKVLARHGSR-KIIIGKDTRISGYMLESALEAGLAAAGLSASFTGPMPTPAI 84
Cdd:cd05802 1 LFGTDGIRGVAN-EPLTPELALKLGRAAGKVLGKGGGRpKVLIGKDTRISGYMLESALAAGLTSAGVDVLLLGVIPTPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 85 AYLTRTFRAEAGIVISASHNPFYDNGIKFFSIEGTKLPDEVEEAIEAEMEKELTCV-DSAELGKASRIVDAAGRYIEFCK 163
Cdd:cd05802 80 AYLTRKLRADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVEEEIEALIDKELELPpTGEKIGRVYRIDDARGRYIEFLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 164 GTFPNELsLNSLKVVVDCAHGATYHIAPSVFRELGAQVIAMGCEPDGLNINEEVGATDVRALQARVLEEKADLGIAYDGD 243
Cdd:cd05802 160 STFPKDL-LSGLKIVLDCANGAAYKVAPEVFRELGAEVIVINNAPDGLNINVNCGSTHPESLQKAVLENGADLGIAFDGD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 244 GDRVIMVDHEGNKVDGDQILYIIAREGLRQGQLRGGA-VGTLMSNMGLELALKQLGIPFVRAKVGDRYVLEKLQEKGWRI 322
Cdd:cd05802 239 ADRVIAVDEKGNIVDGDQILAICARDLKERGRLKGNTvVGTVMSNLGLEKALKELGIKLVRTKVGDRYVLEEMLKHGANL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 323 GAENSGHVILLDKTTTGDGIVASLQVVAAMVRNHMSLHDLCSGMKMFPQLLVNVRfTEGSGNPLEHEHVKAVTAEVEAEL 402
Cdd:cd05802 319 GGEQSGHIIFLDHSTTGDGLLTALQLLAIMKRSGKSLSELASDMKLYPQVLVNVR-VKDKKALLENPRVQAAIAEAEKEL 397
|
410 420 430
....*....|....*....|....*....|....*..
gi 490207696 403 GNRGRVLLRKSGTEPLIRVMVEGEHEEKVHEFAHRIA 439
Cdd:cd05802 398 GGEGRVLVRPSGTEPLIRVMVEGEDEELVEKLAEELA 434
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
7-443 |
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: 644.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 7 FGTDGIRGRVGDAPITPEFVLKLGWAAGKVLARHGSRK--IIIGKDTRISGYMLESALEAGLAAAGLSASFTGPMPTPAI 84
Cdd:TIGR01455 1 FGTDGVRGRAGQEPLTAELALLLGAAAGRVLRQGRDTAprVVIGKDTRLSGYMLENALAAGLNSAGVDVLLLGPLPTPAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 85 AYLTRTFRAEAGIVISASHNPFYDNGIKFFSIEGTKLPDEVEEAIEAEMEKE--LTCVDSAELGKASRIVDAAGRYIEFC 162
Cdd:TIGR01455 81 AYLTRTLRADAGVMISASHNPYEDNGIKFFGPGGFKLDDATEAAIEALLDEAdpLPRPESEGLGRVKRYPDAVGRYIEFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 163 KGTFPNELSLNSLKVVVDCAHGATYHIAPSVFRELGAQVIAMGCEPDGLNINEEVGATDVRALQARVLEEKADLGIAYDG 242
Cdd:TIGR01455 161 KSTLPRGLTLSGLKVVLDCANGAAYKVAPHVFRELGAEVIAIGVEPDGLNINDGCGSTHLDALQKAVREHGADLGIAFDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 243 DGDRVIMVDHEGNKVDGDQILYIIAREGLRQGQLRGGA-VGTLMSNMGLELALKQLGIPFVRAKVGDRYVLEKLQEKGWR 321
Cdd:TIGR01455 241 DADRVLAVDANGRIVDGDQILYIIARALKESGELAGNTvVATVMSNLGLERALEKLGLTLIRTAVGDRYVLEEMRESGYN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 322 IGAENSGHVILLDKTTTGDGIVASLQVVAAMVRNHMSLHDLCSGMKMFPQLLVNVRFTEGSGNPLEHEHVKAVTAEVEAE 401
Cdd:TIGR01455 321 LGGEQSGHIILLDYSTTGDGIVSALQVLTIMKKSGSTLSELAAEFVPYPQTLVNVRVADRKLAAAEAPAVKAAIEDAEAE 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 490207696 402 LGNRGRVLLRKSGTEPLIRVMVEGEHEEKVHEFAHRIADAVK 443
Cdd:TIGR01455 401 LGGTGRILLRPSGTEPLIRVMVEAADEELVQQLADTLADVVS 442
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
1-445 |
0e+00 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 519.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 1 MSNRKYFGTDGIRGRVGDApITPEFVLKLGWAAGKVLARHGSRKIIIGKDTRISGYMLESALEAGLAAAGLSASFTGPMP 80
Cdd:COG1109 1 MTYKKLFGTDGIRGIVGEE-LTPEFVLKLGRAFGTYLKEKGGPKVVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 81 TPAIAYLTRTFRAEAGIVISASHNPFYDNGIKFFSIEGTKLPDEVEEAIEAEMEKE-LTCVDSAELGKASRIVDAAGRYI 159
Cdd:COG1109 80 TPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKEdFRRAEAEEIGKVTRIEDVLEAYI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 160 EFCKGTFPNELSLNSLKVVVDCAHGATYHIAPSVFRELGAQVIAMGCEPDGLNINEEVG--ATDVRALQARVLEEKADLG 237
Cdd:COG1109 160 EALKSLVDEALRLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFPNHNPNpePENLEDLIEAVKETGADLG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 238 IAYDGDGDRVIMVDHEGNKVDGDQILYIIAREGLRQGQlRGGAVGTLMSNMGLELALKQLGIPFVRAKVGDRYVLEKLQE 317
Cdd:COG1109 240 IAFDGDADRLGVVDEKGRFLDGDQLLALLARYLLEKGP-GGTVVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKMRE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 318 KGWRIGAENSGHVILLDKTTTGDGIVASLQVVAAMVRNHMSLHDLCSGMKMFPQLLVNVRFTEGSGNPLEHEHVKAV--- 394
Cdd:COG1109 319 TGAVLGGEESGGIIFPDFVPTDDGILAALLLLELLAKQGKSLSELLAELPRYPQPEINVRVPDEEKIGAVMEKLREAved 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 490207696 395 ------TAEVEAELGNRGRVLLRKSGTEPLIRVMVEGEHEEKVHEFAHRIADAVKSV 445
Cdd:COG1109 399 keeldtIDGVKVDLEDGGWVLVRPSGTEPLLRVYAEAKDEEEAEELLAELAELVEEA 455
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
6-439 |
1.24e-123 |
|
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: 363.21 E-value: 1.24e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 6 YFGTDGIRGRVGDApITPEFVLKLGWAAGKvlarhgsrkiiigkdtrisgymlesaleaglaaaglsasftgpmptpaia 85
Cdd:cd03084 1 IFGTSGVRGVVGDD-ITPETAVALGQAIGS-------------------------------------------------- 29
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 86 yltrtfraEAGIVISASHNPFYDNGIKFFSIEGTKLPDEVEEAIEAEMEKELTCVDSA-ELGKASRIVDAAGRYIEFCKG 164
Cdd:cd03084 30 --------TGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSAVAyELGGSVKAVDILQRYFEALKK 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 165 TFPNELSLNS-LKVVVDCAHGATYHIAPSVFRELGAQVIAMGCEPDGLNIN---EEVGATDVRALQARVLEEKADLGIAY 240
Cdd:cd03084 102 LFDVAALSNKkFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCEPDGNFGNinpDPGSETNLKQLLAVVKAEKADFGVAF 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 241 DGDGDRVIMVDHEGNKVDGDQILYIIAREGLRQGQLRGGAVGTLMSNMGLELALKQLGIPFVRAKVGDRYVLEKLQEKGW 320
Cdd:cd03084 182 DGDADRLIVVDENGGFLDGDELLALLAVELFLTFNPRGGVVKTVVSSGALDKVAKKLGIKVIRTKTGFKWVGEAMQEGDV 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 321 RIGAENSGHVILLDKTTTGDGIVASLQVVAAMVRNHMSLHDLCSGMKMFPQLLVNVrftegsgnplehehvkavtaevea 400
Cdd:cd03084 262 VLGGEESGGVIFPEFHPGRDGISAALLLLEILANLGKSLSELFSELPRYYYIRLKV------------------------ 317
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 490207696 401 elgnRGRVLLRKSGTEPLIRVMVE---GEHEEKVHEFAHRIA 439
Cdd:cd03084 318 ----RGWVLVRASGTEPAIRIYAEadtQEDVEQIKKEARELV 355
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
5-442 |
7.41e-94 |
|
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been characterized as the archaeal protein responsible for the second step of UDP-GlcNAc biosynthesis. This GlmM protein catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. The first-characterized bacterial GlmM protein is modeled by TIGR01455. These two families are members of the larger phosphoglucomutase/phosphomannomutase family (characterized by three domains: pfam02878, pfam02879 and pfam02880), but are not nearest neighbors to each other. This model also includes a number of sequences from non-archaea in the Bacteroides, Chlorobi, Chloroflexi, Planctomycetes and Spirochaetes lineages. Evidence supporting their inclusion in this equivalog as having the same activity comes from genomic context and phylogenetic profiling. A large number of these organisms are known to produce exo-polysaccharide and yet only appeared to contain the GlmS enzyme of the GlmSMU pathway for UDP-GlcNAc biosynthesis (GenProp0750). In some organisms including Leptospira, this archaeal GlmM is found adjacent to the GlmS as well as a putative GlmU non-orthologous homolog. Phylogenetic profiling of the GlmS-only pattern using PPP identifies members of this archaeal GlmM family as the highest-scoring result. [Central intermediary metabolism, Amino sugars]
Pssm-ID: 274906 Cd Length: 443 Bit Score: 290.18 E-value: 7.41e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 5 KYFGTDGIRGRVGDaPITPEFVLKLGWAAGKVLarhGSRKIIIGKDTRISGYMLESALEAGLAAAGLSASFTGPMPTPAI 84
Cdd:TIGR03990 2 LLFGTSGIRGIVGE-ELTPELALKVGKAFGTYL---RGGKVVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLGIAPTPTL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 85 AYLTRTFRAEAGIVISASHNPFYDNGIKFFSIEGTKLPDEVEEAIEAEMEKELTC-VDSAELGKASRIVDAAGRYIEFCK 163
Cdd:TIGR03990 78 QYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQEEEIEEIAESGDFErADWDEIGTVTSDEDAIDDYIEAIL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 164 GTFPNE-LSLNSLKVVVDCAHGATYHIAPSVFRELGAQVIAMGCEPDGL--NINEEVGATDVRALQARVLEEKADLGIAY 240
Cdd:TIGR03990 158 DKVDVEaIRKKGFKVVVDCGNGAGSLTTPYLLRELGCKVITLNCQPDGTfpGRNPEPTPENLKDLSALVKATGADLGIAH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 241 DGDGDRVIMVDHEGNKVDGDQILYIIAREGLRQGqlRGGAVGTLMSNMGLELALKQLGIPFVRAKVGDRYVLEKLQEKGW 320
Cdd:TIGR03990 238 DGDADRLVFIDEKGRFIGGDYTLALFAKYLLEHG--GGKVVTNVSSSRAVEDVAERHGGEVIRTKVGEVNVAEKMKEEGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 321 RIGAENSGHVILLDKTTTGDGIVASLQVVAAMVRNHMSLHDLcsgMKMFPQlLVNVRftegSGNPLEHEHVKAVTAEVEA 400
Cdd:TIGR03990 316 VFGGEGNGGWIFPDHHYCRDGLMAAALFLELLAEEGKPLSEL---LAELPK-YPMSK----EKVELPDEDKEEVMEAVEE 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 490207696 401 EL---------GNR-----GRVLLRKSGTEPLIRVMVEGEHEEKVHEFAHRIADAV 442
Cdd:TIGR03990 388 EFadaeidtidGVRidfedGWVLVRPSGTEPIVRIYAEAKTEERAEELLEEGRSLV 443
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
6-442 |
3.67e-87 |
|
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: 272.91 E-value: 3.67e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 6 YFGTDGIRGRVGDApITPEFVLKLGWAAGKVLarhGSRKIIIGKDTRISGYMLESALEAGLAAAGLSASFTGPMPTPAIA 85
Cdd:cd03087 1 LFGTSGIRGVVGEE-LTPELALKVGKALGTYL---GGGTVVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDIGIVPTPALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 86 YLTRTfRAEAGIVISASHNPFYDNGIKFFSIEGTKLPDEVEEAIEAEMEKELTC-VDSAELGKASRIVDAAGRYIEFCKG 164
Cdd:cd03087 77 YAVRK-LGDAGVMITASHNPPEYNGIKLVNPDGTEFSREQEEEIEEIIFSERFRrVAWDEVGSVRREDSAIDEYIEAILD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 165 TFPNELSLNsLKVVVDCAHGATYHIAPSVFRELGAQVIAMGCEPDGL-----------NINEevgatdvraLQARVLEEK 233
Cdd:cd03087 156 KVDIDGGKG-LKVVVDCGNGAGSLTTPYLLRELGCKVITLNANPDGFfpgrppeptpeNLSE---------LMELVRATG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 234 ADLGIAYDGDGDRVIMVDHEGNKVDGDQILYIIAREGLRQGqlrGGAVGT-LMSNMGLELALKQLGIPFVRAKVGDRYVL 312
Cdd:cd03087 226 ADLGIAHDGDADRAVFVDEKGRFIDGDKLLALLAKYLLEEG---GGKVVTpVDASMLVEDVVEEAGGEVIRTPVGDVHVA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 313 EKLQEKGWRIGAENSGHVILLDKTTTGDGIVASLqVVAAMVRNHMSLHDLCSGMKMFPQLLVNVrftegsgnPLEHEHVK 392
Cdd:cd03087 303 EEMIENGAVFGGEPNGGWIFPDHQLCRDGIMTAA-LLLELLAEEKPLSELLDELPKYPLLREKV--------ECPDEKKE 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490207696 393 AVTAEVEAELGNRGR----------------VLLRKSGTEPLIRVMVEGEHEEKVHEFAHRIADAV 442
Cdd:cd03087 374 EVMEAVEEELSDADEdvdtidgvrieyedgwVLIRPSGTEPKIRITAEAKTEERAKELLEEGRSKV 439
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
12-442 |
9.65e-69 |
|
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: 225.09 E-value: 9.65e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 12 IRGRVGDApITPEFVLKLGWAAGKVLARHGSRKIIIGKDTRISGYMLESALEAGLAAAGLSASFTGPMPTPAIAYLTRTF 91
Cdd:cd03089 7 IRGIAGEE-LTEEIAYAIGRAFGSWLLEKGAKKVVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPVLYFATFHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 92 RAEAGIVISASHNPFYDNGIKFF----SIEGTKLpdeveEAIEAEMEKELTcVDSAELGKASRiVDAAGRYIEFCKGTFp 167
Cdd:cd03089 86 DADGGVMITASHNPPEYNGFKIVigggPLSGEDI-----QALRERAEKGDF-AAATGRGSVEK-VDILPDYIDRLLSDI- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 168 nELSLNSLKVVVDCAHGATYHIAPSVFRELGAQVIAMGCEPDGLNINEEVGATDV---RALQARVLEEKADLGIAYDGDG 244
Cdd:cd03089 158 -KLGKRPLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCEPDGTFPNHHPDPTDPenlEDLIAAVKENGADLGIAFDGDG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 245 DRVIMVDHEGNKVDGDQILYIIAREGLRQgqlRGGA--VGTLMSNMGL-ELALKQLGIPfVRAKVGDRYVLEKLQEKGWR 321
Cdd:cd03089 237 DRLGVVDEKGEIIWGDRLLALFARDILKR---NPGAtiVYDVKCSRNLyDFIEEAGGKP-IMWKTGHSFIKAKMKETGAL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 322 IGAENSGHVIL------LDktttgDGIVASLQVVAAMVRNHMSLHDLCSGMKMFPQLL-VNVRFTEgsgnplehEHVKAV 394
Cdd:cd03089 313 LAGEMSGHIFFkdrwygFD-----DGIYAALRLLELLSKSGKTLSELLADLPKYFSTPeIRIPVTE--------EDKFAV 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490207696 395 TAEVEAELGNR----------------GRVLLRKSGTEPLIRVMVEGEHEEKVHEFAHRIADAV 442
Cdd:cd03089 380 IERLKEHFEFPgaeiididgvrvdfedGWGLVRASNTEPVLVLRFEADTEEGLEEIKAELRKLL 443
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
7-433 |
6.20e-60 |
|
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: 202.40 E-value: 6.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 7 FGTDGIRGRVGDApITPEFVLKLGWAAGKVLARH--GSRKIIIGKDTR------------------ISGYMLESaleagl 66
Cdd:cd05800 3 FGTDGWRGIIAED-FTFENVRRVAQAIADYLKEEggGGRGVVVGYDTRflseefaravaevlaangIDVYLSDR------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 67 aaaglsasftgPMPTPAIAYLTRTFRAEAGIVISASHNPFYDNGIKFFSIEGTKLPDEVEEAIEAEMEKELTCVDSAELG 146
Cdd:cd05800 76 -----------PVPTPAVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARLASGEPPGLEARAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 147 KASRIVDAAGRYIEFCKGTF-PNELSLNSLKVVVDCAHGATYHIAPSVFRELGAQVIAMGCEPDGL--NINEEVGATDVR 223
Cdd:cd05800 145 GLIETIDPKPDYLEALRSLVdLEAIREAGLKVVVDPMYGAGAGYLEELLRGAGVDVEEIRAERDPLfgGIPPEPIEKNLG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 224 ALQARVLEEKADLGIAYDGDGDRVIMVDHEGNKVDGDQILYIIAREGLRQGQLRGGAVGTL-MSNMGLELALKqLGIPFV 302
Cdd:cd05800 225 ELAEAVKEGGADLGLATDGDADRIGAVDEKGNFLDPNQILALLLDYLLENKGLRGPVVKTVsTTHLIDRIAEK-HGLPVY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 303 RAKVGDRYVLEKLQEKGWRIGAENSGHVILLDKTTTGDGIVASLQVVAAMVRNHMSLHDLcsgmkmFPQLL--VNVRFTE 380
Cdd:cd05800 304 ETPVGFKYIAEKMLEEDVLIGGEESGGLGIRGHIPERDGILAGLLLLEAVAKTGKPLSEL------VAELEeeYGPSYYD 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490207696 381 GSGNPLEHEHVKAVTAEVEAE----------------------LGNRGRVLLRKSGTEPLIRVMVEGEHEEKVHE 433
Cdd:cd05800 378 RIDLRLTPAQKEAILEKLKNEpplsiaggkvdevntidgvklvLEDGSWLLIRPSGTEPLLRIYAEAPSPEKVEA 452
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
11-437 |
8.73e-54 |
|
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: 185.97 E-value: 8.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 11 GIRGRVGDApITPEFVLKLGWAAGKVLARHGSRK-IIIGKDTRISGYMLESALEAGLAAAGLSASFTGPMPTPAIAYLTR 89
Cdd:cd05803 6 GIRGIVGEG-LTPEVITRYVAAFATWQPERTKGGkIVVGRDGRPSGPMLEKIVIGALLACGCDVIDLGIAPTPTVQVLVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 90 TFRAEAGIVISASHNPFYDNGIKFFSIEGTKL-PDEVEEAIEAEMEKELTCVDSAELGKASRIVDAAGRYIEFCKGTFPN 168
Cdd:cd05803 85 QSQASGGIIITASHNPPQWNGLKFIGPDGEFLtPDEGEEVLSCAEAGSAQKAGYDQLGEVTFSEDAIAEHIDKVLALVDV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 169 ELSLNS---LKVVVDCAHGATYHIAPSVFRELGAQVIAMGCEPDGL-NINEEVGATDVRALQARVLEEKADLGIAYDGDG 244
Cdd:cd05803 165 DVIKIRernFKVAVDSVNGAGGLLIPRLLEKLGCEVIVLNCEPTGLfPHTPEPLPENLTQLCAAVKESGADVGFAVDPDA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 245 DRVIMVDHEGNKVDGDQILYIIAREGLRQGQLRGGAVGTLMSNMGLELALKQLGIPFVRAKVGDRYVLEKLQEKGWRIGA 324
Cdd:cd05803 245 DRLALVDEDGRPIGEEYTLALAVDYVLKYGGRKGPVVVNLSTSRALEDIARKHGVPVFRSAVGEANVVEKMKEVDAVIGG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 325 ENSGHVILLDKTTTGDGIVASLQVVAAMVRNHMSLHDLCSGmkmFPQL-LVNVRFtegsgnPLEHEHVKAVTAEVEAELG 403
Cdd:cd05803 325 EGNGGVILPDVHYGRDSLVGIALVLQLLAASGKPLSEIVDE---LPQYyISKTKV------TIAGEALERLLKKLEAYFK 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 490207696 404 N--------------RGRVLLRKSGTEPLIRVMVEGEHEEKVHEFAHR 437
Cdd:cd05803 396 DaeastldglrldseDSWVHVRPSNTEPIVRIIAEAPTQDEAEALADR 443
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
4-136 |
1.07e-45 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 155.07 E-value: 1.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 4 RKYFGTDGIRGRVGDAPITPEFVLKLGWAAGKVL-ARHGSRKIIIGKDTRISGYMLESALEAGLAAAGLSASFTGPMPTP 82
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGELTPEFALKLGQAIASYLrAQGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 490207696 83 AIAYLTRTFRAEAGIVISASHNPFYDNGIKFFSIEGTKLPDEVEEAIEAEMEKE 136
Cdd:pfam02878 81 AVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKE 134
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
258-363 |
1.90e-40 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 140.28 E-value: 1.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 258 DGDQILYIIAREGLRQGQLRGGA--VGTLMSNMGLELALKQLGIPFVRAKVGDRYVLEKLQEKGWRIGAENSGHVILLDK 335
Cdd:pfam02880 1 DGDQILALLAKYLLEQGKLPPGAgvVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLDH 80
|
90 100
....*....|....*....|....*...
gi 490207696 336 TTTGDGIVASLQVVAAMVRNHMSLHDLC 363
Cdd:pfam02880 81 ATTKDGILAALLVLEILARTGKSLSELL 108
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
12-444 |
3.25e-28 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 115.85 E-value: 3.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 12 IRGRVGDApITPEFVLKLGWAAGKVLARHGSRKIIIGKDTRISGYMLESALEAGLAAAGLSASFTGPMPTPAIAYLTRTF 91
Cdd:PRK09542 6 VRGVVGEQ-IDEDLVRDVGAAFARLMRAEGATTVVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIGLASTDQLYFASGLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 92 RAeAGIVISASHNPFYDNGIKFfSIEGTKlP---DEVEEAIEAEMEKELTCVDSAElGKASRIvDAAGRYIEFCKGtFPN 168
Cdd:PRK09542 85 DC-PGAMFTASHNPAAYNGIKL-CRAGAK-PvgqDTGLAAIRDDLIAGVPAYDGPP-GTVTER-DVLADYAAFLRS-LVD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 169 ELSLNSLKVVVDCAHGATYHIAPSVFRELGAQVIAMGCEPDGLNINEEVGATD---VRALQARVLEEKADLGIAYDGDGD 245
Cdd:PRK09542 159 LSGIRPLKVAVDAGNGMGGHTVPAVLGGLPITLLPLYFELDGTFPNHEANPLDpanLVDLQAFVRETGADIGLAFDGDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 246 RVIMVDHEGNKVDGDQILYIIAREGLRQGqlrGGAvgTLMSNMGLELALKQL-----GIPfVRAKVGDRYVLEKLQEKGW 320
Cdd:PRK09542 239 RCFVVDERGQPVSPSAVTALVAARELARE---PGA--TIIHNLITSRAVPELvaergGTP-VRTRVGHSFIKALMAETGA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 321 RIGAENSGHVILLDKTTTGDGIVASLQVVAAMVRNHMSLHDLCSGMKMFpqllvnvrftEGSG--NPLEHEhVKAVTAEV 398
Cdd:PRK09542 313 IFGGEHSAHYYFRDFWGADSGMLAALHVLAALGEQDRPLSELMADYQRY----------AASGeiNSTVAD-APARMEAV 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490207696 399 EAELGNRGRVL-----------------LRKSGTEPLIRVMVEGEHEEKVHEFAHRIADAVKS 444
Cdd:PRK09542 382 LKAFADRIVSVdhldgvtvdlgdgswfnLRASNTEPLLRLNVEARTEEEVDALVDEVLAIIRA 444
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
7-443 |
6.60e-28 |
|
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: 115.68 E-value: 6.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 7 FGTDGIRGRVG-------DAPIT------PEFVLKLGWAAGKvlarhgsRKIIIGKDTR------------------ISG 55
Cdd:cd05799 4 FGTAGLRGKMGagtnrmnDYTVRqatqglANYLKKKGPDAKN-------RGVVIGYDSRhnsrefaeltaavlaangIKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 56 YMlesaleaglaaaglsasFTGPMPTPAIAYLTRTFRAEAGIVISASHNPFYDNGIKFFSIEGTKLPDEVEEAIEAEMEK 135
Cdd:cd05799 77 YL-----------------FDDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 136 --ELTCVDSAELGKASRIVDAA----GRYIEFCKG--TFPNELSLNSLKVVVDCAHGATYHIAPSVFRELGAQVIAMG-- 205
Cdd:cd05799 140 vlEPLDIKFEEALDSGLIKYIGeeidDAYLEAVKKllVNPELNEGKDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVVee 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 206 -CEPDGlniN---------EEVGATDvRAL-QARvlEEKADLGIAYDGDGDRV-IMVDHEGNK---VDGDQILYIIAREG 270
Cdd:cd05799 220 qAEPDP---DfptvkfpnpEEPGALD-LAIeLAK--KVGADLILATDPDADRLgVAVKDKDGEwrlLTGNEIGALLADYL 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 271 LRQGQLRGGAVGTLM-------SNMGLELAlKQLGIPFVRAKVGDRY---VLEKLQEKGWR--------IGAENSGHVil 332
Cdd:cd05799 294 LEQRKEKGKLPKNPVivktivsSELLRKIA-KKYGVKVEETLTGFKWignKIEELESGGKKflfgfeesIGYLVGPFV-- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 333 LDKtttgDGIVASLqVVAAMV----RNHMSLHDlcsgmKM---------FPQLLVNVRFTEGSGNplehEHVKAVTAEVE 399
Cdd:cd05799 371 RDK----DGISAAA-LLAEMAaylkAQGKTLLD-----RLdelyekygyYKEKTISITFEGKEGP----EKIKAIMDRLR 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 490207696 400 AE-------LGNRGRVLLRKSGTEPLIRVMVEGEHEEKVHEfAHRIADAVK 443
Cdd:cd05799 437 NNpnvltfyLEDGSRVTVRPSGTEPKIKFYIEVVGKKTLEE-AEKKLDALK 486
|
|
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
7-442 |
3.07e-26 |
|
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: 110.03 E-value: 3.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 7 FGTDGIRGRVgDAPITPEFVLKLGWAAGKVLARhGSrKIIIGKDTRISGYMLESALEAGLAAAGLSASFTGPMPTPAIAY 86
Cdd:cd05805 2 FGGRGVSGLI-NVDITPEFATRLGAAYGSTLPP-GS-TVTVSRDASRASRMLKRALISGLLSTGVNVRDLGALPLPVARY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 87 LTRTFRAEAGIVISASHnpfYDNG---IKFFSIEGTKLPDEVEEAIEAEMEKE-LTCVDSAELGKASRIVDAAGRYIE-F 161
Cdd:cd05805 79 AIRFLGASGGIHVRTSP---DDPDkveIEFFDSRGLNISRAMERKIENAFFREdFRRAHVDEIGDITEPPDFVEYYIRgL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 162 CKGTFPNELSLNSLKVVVDCAHGATYHIAPSVFRELGAQVIAmgcepdgLNINEEVGA-----TDVRALQ--ARVLEE-K 233
Cdd:cd05805 156 LRALDTSGLKKSGLKVVIDYAYGVAGIVLPGLLSRLGCDVVI-------LNARLDEDAprtdtERQRSLDrlGRIVKAlG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 234 ADLGIAYDGDGDRVIMVDHEGNKVDGDQ----ILYIIAREglRQGqlrggavGTLM----SNMGLELALKQLGIPFVRAK 305
Cdd:cd05805 229 ADFGVIIDPNGERLILVDEAGRVISDDLltalVSLLVLKS--EPG-------GTVVvpvtAPSVIEQLAERYGGRVIRTK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 306 VGDRYVLEKLQEkGWRIGAENSGHVILLDKTTTGDGIVASLQVVAAMVRNHMSLHDLcsgMKMFPQLLVNVR-------- 377
Cdd:cd05805 300 TSPQALMEAALE-NVVLAGDGDGGFIFPEFHPGFDAIAALVKILEMLARTNISLSQI---VDELPRFYVLHKevpcpwea 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490207696 378 --------FTEGSGNPLEH-EHVKAVtaeveaelGNRGRVLLRKSGTEPLIRVMVEGEHEEKVHEFAHRIADAV 442
Cdd:cd05805 376 kgrvmrrlIEEAPDKSIELiDGVKIY--------EDDGWVLVLPDADEPLCHIYAEGSDQERAEELTEFYVEKV 441
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
9-444 |
1.58e-23 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 103.21 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 9 TDGIRGRVgdAPITPEFVLKLG-----WAAGKVLARHGSR-KIIIGKDTRISGYMLESALEAGLAAAGLSASFTGPMPTP 82
Cdd:PLN02371 78 VEGVEGEP--VTLTPPAVEAIGaafaeWLLEKKKADGSGElRVSVGRDPRISGPRLADAVFAGLASAGLDVVDMGLATTP 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 83 AIAYLTRT--FRAEAGIVISASHNPFYDNGIKFFSIEG------------------TKLPDEVEEAIEAEMEKELTCVD- 141
Cdd:PLN02371 156 AMFMSTLTerEDYDAPIMITASHLPYNRNGLKFFTKDGglgkpdikdileraariyKEWSDEGLLKSSSGASSVVCRVDf 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 142 ----SAELGKAsrIVDAAGRyiefckgTFPNELSLNSLKVVVDCAHGATYHIAPSVFRELGAQVI-AMGCEPDGLNIN-- 214
Cdd:PLN02371 236 mstyAKHLRDA--IKEGVGH-------PTNYETPLEGFKIVVDAGNGAGGFFAEKVLEPLGADTSgSLFLEPDGMFPNhi 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 215 ---EEvgATDVRALQARVLEEKADLGIAYDGDGDRVIMVDHEGNKVDGDQILYIIAREGLRQGQlrGGAVGT-LMSNMGL 290
Cdd:PLN02371 307 pnpED--KAAMSATTQAVLANKADLGIIFDTDVDRSAVVDSSGREINRNRLIALMSAIVLEEHP--GTTIVTdSVTSDGL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 291 ELALKQLGIPFVRAKVGDRYVLEK---LQEKG--WRIGAENSGHVIL-----LDktttgDGIVASLQVVAAMVRNHMS-- 358
Cdd:PLN02371 383 TTFIEKKGGKHHRFKRGYKNVIDKgvrLNSDGeeTHLMIETSGHGALkenhfLD-----DGAYLAVKIIIELVRMRAAga 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 359 ---LHDLCSGMKMfPQLLVNVR---------FTEGSGNPLEH--EHVKAVT----AEVEAE--------LGNRGRVLLRK 412
Cdd:PLN02371 458 gggLGDLIEDLEE-PLEAVELRlkildegkdFKAYGEEVLEHlrNSIESDGklegAPVNYEgvrvsdegEGFGGWFLLRQ 536
|
490 500 510
....*....|....*....|....*....|..
gi 490207696 413 SGTEPLIRVMVEGEHEEKVHEFAHRIADAVKS 444
Cdd:PLN02371 537 SLHDPVIPLNIESSSPGGAQKMALVVLTWLKE 568
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
7-331 |
1.08e-21 |
|
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: 96.89 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 7 FGTDGIRGRVGDapITPEFVLKLGWAAGKVLARHGSRKII-IGKDTRISGYMLESALEAGLAAAGLSASFTGPMPTPAIA 85
Cdd:cd03088 2 FGTSGLRGLVTD--LTDEVCYAYTRAFLQHLESKFPGDTVaVGRDLRPSSPRIAAACAAALRDAGFRVVDCGAVPTPALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 86 YLTRTfRAEAGIVISASHNPFYDNGIKFFSIEG--TKlpdEVEEAIEAEMEKELTCVDSAELGKASRIVDAAGRYIEFCK 163
Cdd:cd03088 80 LYAMK-RGAPAIMVTGSHIPADRNGLKFYRPDGeiTK---ADEAAILAALVELPEALFDPAGALLPPDTDAADAYIARYT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 164 GTFPNElSLNSLKVVVDCAHGATYHIAPSVFRELGAQVIAMGCEPDGLNINEE-VGATDVRALQARVLEEKADLGIAYDG 242
Cdd:cd03088 156 DFFGAG-ALKGLRIGVYQHSSVGRDLLVRILEALGAEVVPLGRSDTFIPVDTEaVRPEDRALAAAWAAEHGLDAIVSTDG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 243 DGDRVIMVDHEGNKVDGDqILYII-AREglrqgqLRGGAVGT-LMSNMGLELALKQLGIpfVRAKVGDRYVLEKLQEkgw 320
Cdd:cd03088 235 DGDRPLVADETGEWLRGD-ILGLLtARF------LGADTVVTpVSSNSAIELSGFFKRV--VRTRIGSPYVIAAMAE--- 302
|
330
....*....|.
gi 490207696 321 rIGAENSGHVI 331
Cdd:cd03088 303 -AAAAGAGRVV 312
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
158-254 |
1.62e-21 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 88.89 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 158 YIEFCKGTFPNELSLNS-LKVVVDCAHGATYHIAPSVFRELGAQVIAMGCEPDGLNIN---EEVGATDVRALQARVLEEK 233
Cdd:pfam02879 2 YIDHLLELVDSEALKKRgLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDPDFPTrapNPEEPEALALLIELVKSVG 81
|
90 100
....*....|....*....|.
gi 490207696 234 ADLGIAYDGDGDRVIMVDHEG 254
Cdd:pfam02879 82 ADLGIATDGDADRLGVVDERG 102
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
1-424 |
1.34e-18 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 87.69 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 1 MSNRKYFGTDGIRGRVGDApITPEFVLKLGWAAGKVLArhgSRKIIIGKDTRISGYMLESALEAGLAAAGLSASFTGPMP 80
Cdd:PRK15414 1 MKKLTCFKAYDIRGKLGEE-LNEDIAWRIGRAYGEFLK---PKTIVLGGDVRLTSETLKLALAKGLQDAGVDVLDIGMSG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 81 TPAIAYLTRTFRAEAGIVISASHNPFYDNGIKFFS-----IEGTKLPDEVEEAIEAemeKELTCVDSAELGKASRIvDAA 155
Cdd:PRK15414 77 TEEIYFATFHLGVDGGIEVTASHNPMDYNGMKLVRegarpISGDTGLRDVQRLAEA---NDFPPVDETKRGRYQQI-NLR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 156 GRYIEFCKGtFPNELSLNSLKVVVDCAHGATYHIAPSV---FRELGAQV--IAMGCEPDGlniNEEVGATDVRALQAR-- 228
Cdd:PRK15414 153 DAYVDHLFG-YINVKNLTPLKLVINSGNGAAGPVVDAIearFKALGAPVelIKVHNTPDG---NFPNGIPNPLLPECRdd 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 229 ----VLEEKADLGIAYDGDGDRVIMVDHEGNKVDGDQILYIIAREGLRQGQLRGGAVGTLMSNMGLELALKQLGIPfVRA 304
Cdd:PRK15414 229 trnaVIKHGADMGIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPGAKIIHDPRLSWNTVDVVTAAGGTP-VMS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 305 KVGDRYVLEKLQEKGWRIGAENSGHVILLDKTTTGDGIVASLQVVAAMVRNHMSLHDLCSG-MKMFPqllvnvrfTEGSG 383
Cdd:PRK15414 308 KTGHAFIKERMRKEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELVCLKGKTLGELVRDrMAAFP--------ASGEI 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 490207696 384 NPLEHEHVKAVtAEVEAELGNRG----------------RVLLRKSGTEPLIRVMVE 424
Cdd:PRK15414 380 NSKLAQPVEAI-NRVEQHFSREAlavdrtdgismtfadwRFNLRSSNTEPVVRLNVE 435
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
95-444 |
2.33e-17 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 84.32 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 95 AGIVISASHNPFYDNGIKFFSIEGTKLPDEVE------------EAIEAEMEKELT------------------------ 138
Cdd:PTZ00302 77 VGVMITASHNPIQDNGVKIIDPDGGMLEESWEkictdfanartgEDLVSVLMDCLTehgiklsnlkldlnksncskakvh 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 139 --------CVD---------SAELGKASR------------IVDAAGR------------YIEFCKGTF------PNELS 171
Cdd:PTZ00302 157 vgrdtrpsSPElvsallrglKLLIGSNVRnfgivttpqlhfLVAFANGlgvdvvessdelYYAYLLAAFkelyrtLQEGG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 172 LNSL------KVVVDCAHG-ATYHIAP--SVFRELGAQVI-AMGCEPDGLNINEEVGATDVRALQA--RVLEEKADLGI- 238
Cdd:PTZ00302 237 PVDLtqnnskILVVDCANGvGGYKIKRffEALKQLGIEIIpININCDEEELLNDKCGADYVQKTRKppRAMKEWPGDEEt 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 239 ---AYDGDGDRVI--MVDHEGNKV----DGDQILYIIA---REGLRQGQLRG----GAVGTLMSNMG----LELALKQLG 298
Cdd:PTZ00302 317 rvaSFDGDADRLVyfFPDKDGDDKwvllDGDRIAILYAmliKKLLGKIQLKKkldiGVVQTAYANGAstnyLNELLGRLR 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 299 IPFvrAKVGDRYvLEKLQEKgWRIGA--ENSGH--VILLDKT------------------------------TTGDGIVA 344
Cdd:PTZ00302 397 VYC--APTGVKN-LHPKAHK-YDIGIyfEANGHgtVLFNEKAlaewakflakqnalnsacrqlekflrlfnqTIGDAISD 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 345 SLQVVAAMVRNHMSLHDlCSGMKM-FPQLLVNVrftegsgnPLEHEHVKAVTA----------------EVEAELGNRGR 407
Cdd:PTZ00302 473 LLAVELALAFLGLSFQD-WLNLYTdLPSRQDKV--------TVKDRTLITNTEdetrllepkglqdkidAIVSKYDNAAR 543
|
490 500 510
....*....|....*....|....*....|....*..
gi 490207696 408 VLLRKSGTEPLIRVMVEGEHEEKVHEFAHRIADAVKS 444
Cdd:PTZ00302 544 AFIRPSGTEPVVRVYAEAPTLEQADELANEVKGLVLR 580
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
373-443 |
8.73e-15 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 68.83 E-value: 8.73e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490207696 373 LVNVRFTEGSgNPLEHEHVKAVTAEVEAELGNRGRVL-LRKSGTEPLIRVMVEGEHEEKVHEFAHRIADAVK 443
Cdd:pfam00408 1 LINVRVAEKK-KLAALAAILKVFADAEKILGEDGRRLdVRPSGTEPVLRVMVEGDSDEELARLADEIADLLE 71
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
96-442 |
8.76e-15 |
|
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: 76.09 E-value: 8.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 96 GIVISASHNPFYDNGIKFFSIEGTKLPDEVEE----------AIEAEMEKELTCVDSAELGKAS---------------R 150
Cdd:cd03086 38 GVMITASHNPVEDNGVKIVDPDGEMLEESWEPyatqlanasdDELLVLVLMLISVKELNIDLSVpanvfvgrdtrpsgpA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 151 IVDAA--------GRYIEFCKGTFP-------------------------------NELS-------LNSLKVVVDCAHG 184
Cdd:cd03086 118 LLQALldglkalgGNVIDYGLVTTPqlhylvraantegaygepteegyyeklskafNELYnllqdggDEPEKLVVDCANG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 185 -ATYHI---APSVFRELGAQVIAMGCEPDGLnINEEVGATDV----RALQARVLEEKADLGIAYDGDGDRVI--MVDHEg 254
Cdd:cd03086 198 vGALKLkelLKRLKKGLSVKIINDGEEGPEL-LNDGCGADYVktkqKPPRGFELKPPGVRCCSFDGDADRLVyfYPDSS- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 255 NKV---DGDQILYIIAreglrqgqlrgGAVGTLMSNMGLELALK-------------------QLGIPFVRAKVGDRYVL 312
Cdd:cd03086 276 NKFhllDGDKIATLFA-----------KFIKELLKKAGEELKLTigvvqtayangastkyledVLKVPVVCTPTGVKHLH 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 313 EKLQEkgWRIGA--ENSGH--------------------------------VILLDKTTTGDGIVASLQVVAAMVRNHMS 358
Cdd:cd03086 345 HAAEE--FDIGVyfEANGHgtvlfsesalakieensslsdeqekaaktllaFSRLINQTVGDAISDMLAVELILAALGWS 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 359 LHDLCSGMKMFPQLLVNV---------------RFTEgsgnPLE-HEHVKAVTAEVeaelgNRGRVLLRKSGTEPLIRVM 422
Cdd:cd03086 423 PQDWDNLYTDLPNRQLKVkvpdrsvikttdaerRLVE----PKGlQDKIDAIVAKY-----NNGRAFVRPSGTEDVVRVY 493
|
490 500
....*....|....*....|
gi 490207696 423 VEGEHEEKVHEFAHRIADAV 442
Cdd:cd03086 494 AEAATQEEADELANEVAELV 513
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
35-246 |
5.61e-12 |
|
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: 67.63 E-value: 5.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 35 KVLARHGSRKIIIGKDtrisgymlesaleaglaaaglsasftGPMPTPAIAYLTRTFRAEAGIVISASHNP---FYDNGI 111
Cdd:cd03085 71 KIAAANGVGKVVVGQN--------------------------GLLSTPAVSAVIRKRKATGGIILTASHNPggpEGDFGI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 112 KFFSIEGTKLPDEVEEAIEAE---MEKELTC----VDSAELGKAS--------RIVDAAGRYIEFCKGTF-----PNELS 171
Cdd:cd03085 125 KYNTSNGGPAPESVTDKIYEItkkITEYKIAddpdVDLSKIGVTKfggkpftvEVIDSVEDYVELMKEIFdfdaiKKLLS 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 172 LNSLKVVVDCAHGATYHIAPSVF-RELGA-QVIAMGCEPdglniNEEVGA-------TDVRALQARVLEEKADLGIAYDG 242
Cdd:cd03085 205 RKGFKVRFDAMHGVTGPYAKKIFvEELGApESSVVNCTP-----LPDFGGghpdpnlTYAKDLVELMKSGEPDFGAASDG 279
|
....
gi 490207696 243 DGDR 246
Cdd:cd03085 280 DGDR 283
|
|
| PLN02307 |
PLN02307 |
phosphoglucomutase |
35-246 |
1.08e-10 |
|
phosphoglucomutase
Pssm-ID: 177942 [Multi-domain] Cd Length: 579 Bit Score: 63.52 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 35 KVLARHGSRKIIIGKDtrisgymlesaleaglaaaglsasftGPMPTPAIAYLTR---TFRAEAGIVISASHN---PFYD 108
Cdd:PLN02307 83 KIAAANGVRRVWVGQN--------------------------GLLSTPAVSAVIRerdGSKANGGFILTASHNpggPEED 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 109 NGIKFFSIEGTKLPDEVEEAI--------EAEMEKELTCVDSAELGKAS---------RIVDAAGRYIEFCKGTFPNE-- 169
Cdd:PLN02307 137 FGIKYNYESGQPAPESITDKIygntltikEYKMAEDIPDVDLSAVGVTKfggpedfdvEVIDPVEDYVKLMKSIFDFEli 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 170 ---LSLNSLKVVVDCAHGATYHIAPSVF-RELGAQVIAM----------GCEPD-GLNINEEVGATdVRALQARVLEEKA 234
Cdd:PLN02307 217 kklLSRPDFTFCFDAMHGVTGAYAKRIFvEELGAPESSLlncvpkedfgGGHPDpNLTYAKELVKR-MGLGKTSYGDEPP 295
|
250
....*....|..
gi 490207696 235 DLGIAYDGDGDR 246
Cdd:PLN02307 296 EFGAASDGDGDR 307
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
35-246 |
2.58e-09 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 58.99 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 35 KVLARHGSRKIIIGKDtrisgymlesaleaglaaaglsasftGPMPTPAIAYLTRTFRAEA-----GIVISASHNPFYDN 109
Cdd:PRK07564 98 EVLAANGVGVVIVGRG--------------------------GYTPTPAVSHAILKYNGRGggladGIVITPSHNPPEDG 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 110 GIKFFSIEGTKLPDEVEEAIEAEmEKELTC--------VDSAELGKASRI--VDAAGRYIEfckgtfpnelSLNS----- 174
Cdd:PRK07564 152 GIKYNPPNGGPADTDVTDAIEAR-ANELLAyglkgvkrIPLDRALASMTVevIDPVADYVE----------DLENvfdfd 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 175 ------LKVVVDCAHGATYHIapsvfrelgAQVIAmgcEPDGLNI---NEEVGAT--------------D---VRALQAR 228
Cdd:PRK07564 221 airkagLRLGVDPLGGATGPY---------WKAIA---ERYGLDLtvvNAPVDPTfnfmpldddgkirmDcssPYAMAGL 288
|
250
....*....|....*....
gi 490207696 229 V-LEEKADLGIAYDGDGDR 246
Cdd:PRK07564 289 LaLKDAFDLAFANDPDGDR 307
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
3-267 |
5.69e-09 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 58.16 E-value: 5.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 3 NRKYFGTDGIRGRVGdapitpefvlkLGWAAGKVL----ARHG--------------SRKIIIGKDTRISGYML-ESALE 63
Cdd:PTZ00150 43 KRMEFGTAGLRGKMG-----------AGFNCMNDLtvqqTAQGlcayvietfgqalkSRGVVIGYDGRYHSRRFaEITAS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 64 AGLAAAGLSASFTGPMPTPAIAYLTRTFRAEAGIVISASHNPFYDNGIKFFSIEGTKLPDEVEEAIEAEMEKELTCVDSA 143
Cdd:PTZ00150 112 VFLSKGFKVYLFGQTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVYWSNGAQIIPPHDKNISAKILSNLEPWSSS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 144 -ELGKASRIVDA----AGRYIEFCKGTF-PNELSLNSLKVVVDCAHGATYHIAPSVFRELGAQ---VIAMGCEPDG---- 210
Cdd:PTZ00150 192 wEYLTETLVEDPlaevSDAYFATLKSEYnPACCDRSKVKIVYTAMHGVGTRFVQKALHTVGLPnllSVAQQAEPDPefpt 271
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490207696 211 ---LNINEEVGATDVR-ALQARVleeKADLGIAYDGDGDRVIMVDHEGNK---VDGDQILYIIA 267
Cdd:PTZ00150 272 vtfPNPEEGKGALKLSmETAEAH---GSTVVLANDPDADRLAVAEKLNNGwkiFTGNELGALLA 332
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
93-444 |
2.68e-08 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 55.80 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 93 AEAGIVISASHNPFYDNGIKFFSIEGTKLP----------------DEVEEAIEAEMEKE----LTCVDSAE--LGKASR 150
Cdd:PLN02895 58 AATGLMITASHNPVSDNGVKIVDPSGGMLPqawepfadalanapdpDALVQLIREFVKKEnipaVGGNPPAEvlLGRDTR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 151 -----IVDAAGRYIEFC-----------------------KGTFPNE--------------LSLNS---------LKVVV 179
Cdd:PLN02895 138 psgpaLLAAALKGVRAIgaravdmgilttpqlhwmvraanKGMKATEsdyfeqlsssfralLDLIPngsgddradDKLVV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 180 DCAHGATYHIAPSVFRELGAQVIAM---GCEPDGLnINEEVGATDVRAlQARVLEEKADLG-----IAYDGDGDRVI--- 248
Cdd:PLN02895 218 DGANGVGAEKLETLKKALGGLDLEVrnsGKEGEGV-LNEGVGADFVQK-EKVPPTGFASKDvglrcASLDGDADRLVyfy 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 249 MVDHEGN--KVDGDQILYIIA---REGLRQ-----------GQLRGGAVGTLMSNMGLELALKQ-LGIPFVRAKVGDRYV 311
Cdd:PLN02895 296 VSSAGSKidLLDGDKIASLFAlfiKEQLRIlngngnekpeeLLVRLGVVQTAYANGASTAYLKQvLGLEVVCTPTGVKYL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 312 LEKLQEKGWRIGAENSGH--VILLDKT------------------------------------TTGDGIVASLQVVAAMV 353
Cdd:PLN02895 376 HEAAAEFDIGVYFEANGHgtVLFSERFldwleaaaaelsskakgseahkaarrllavsrlinqAVGDALSGLLLVEAILQ 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490207696 354 RNHMSLHDLCSGMKMFP--QLLVNVR-FTEGSGNPLEHEHV------KAVTAEVEAElgNRGRVLLRKSGTEPLIRVMVE 424
Cdd:PLN02895 456 YRGWSLAEWNALYQDLPsrQLKVKVAdRTAITTTDAETVVVrpaglqDAIDAEVAKY--PRGRAFVRPSGTEDVVRVYAE 533
|
490 500
....*....|....*....|
gi 490207696 425 GEHEEKVHEFAHRIADAVKS 444
Cdd:PLN02895 534 ASTQEAADSLAREVARLVYD 553
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
77-131 |
8.20e-04 |
|
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100094 [Multi-domain] Cd Length: 522 Bit Score: 41.85 E-value: 8.20e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490207696 77 GPMPTPAI--AYLT--RTfRAEA---GIVISASHNPFYDNGIKFFSIEGTKLPDEVEEAIEA 131
Cdd:cd05801 97 GYTPTPVIshAILTynRG-RTEGladGIVITPSHNPPEDGGFKYNPPHGGPADTDITRWIEK 157
|
|
| |
