|
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: 910.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 4 RKYFGTDGIRGRVGDAPITPDFVLKLGWAAGKVLARHGSRKIIIGKDTRISGYMLESALEAGLAAAGLSALFTGPMPTPA 83
Cdd:PRK10887 1 RKYFGTDGIRGKVGQAPITPDFVLKLGWAAGKVLARQGRPKVLIGKDTRISGYMLESALEAGLAAAGVDVLLTGPMPTPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 84 VAYLTRTFRAEAGIVISASHNPFYDNGIKFFSIDGTKLPDAVEEAIEAEMEKEISCVDSAELGKASRIVDAAGRYIEFCK 163
Cdd:PRK10887 81 VAYLTRTLRAEAGIVISASHNPYYDNGIKFFSADGTKLPDEVELAIEAELDKPLTCVESAELGKASRINDAAGRYIEFCK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 164 ATFPNELSLSELKIVVDCANGATYHIAPNVLRELGANVIAIGCEPNGVNINAEVGATDVRALQARVLAEKADLGIAFDGD 243
Cdd:PRK10887 161 STFPNELSLRGLKIVVDCANGATYHIAPNVFRELGAEVIAIGCEPNGLNINDECGATDPEALQAAVLAEKADLGIAFDGD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 244 GDRVIMVDHEGNKVDGDQIMYIIAREGLRQGQLRGGAVGTLMSNMGLELALKQLGIPFARAKVGDRYVLEKMQEKGWRIG 323
Cdd:PRK10887 241 GDRVIMVDHLGNLVDGDQLLYIIARDRLRRGQLRGGVVGTLMSNMGLELALKQLGIPFVRAKVGDRYVLEKLQEKGWRLG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 324 AENSGHVILLDKTTTGDGIVAGLQVLAAMARNHMSLHDLCSGMKMFPQILVNVRYTAGSGDPLEHESVKAVTAEVEAALG 403
Cdd:PRK10887 321 GENSGHILCLDKTTTGDGIVAALQVLAAMVRSGMSLADLCSGMKLFPQVLINVRFKPGADDPLESEAVKAALAEVEAELG 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 732683007 404 NRGRVLLRKSGTEPLIRVMVEGEDEAQVTEFAHRIADAVKAV 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: 718.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 6 YFGTDGIRGRVGdAPITPDFVLKLGWAAGKVLARHGSR-KIIIGKDTRISGYMLESALEAGLAAAGLSALFTGPMPTPAV 84
Cdd:cd05802 1 LFGTDGIRGVAN-EPLTPELALKLGRAAGKVLGKGGGRpKVLIGKDTRISGYMLESALAAGLTSAGVDVLLLGVIPTPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 85 AYLTRTFRAEAGIVISASHNPFYDNGIKFFSIDGTKLPDAVEEAIEAEMEKEISCV-DSAELGKASRIVDAAGRYIEFCK 163
Cdd:cd05802 80 AYLTRKLRADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVEEEIEALIDKELELPpTGEKIGRVYRIDDARGRYIEFLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 164 ATFPNELsLSELKIVVDCANGATYHIAPNVLRELGANVIAIGCEPNGVNINAEVGATDVRALQARVLAEKADLGIAFDGD 243
Cdd:cd05802 160 STFPKDL-LSGLKIVLDCANGAAYKVAPEVFRELGAEVIVINNAPDGLNINVNCGSTHPESLQKAVLENGADLGIAFDGD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 244 GDRVIMVDHEGNKVDGDQIMYIIAREGLRQGQLRGGA-VGTLMSNMGLELALKQLGIPFARAKVGDRYVLEKMQEKGWRI 322
Cdd:cd05802 239 ADRVIAVDEKGNIVDGDQILAICARDLKERGRLKGNTvVGTVMSNLGLEKALKELGIKLVRTKVGDRYVLEEMLKHGANL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 323 GAENSGHVILLDKTTTGDGIVAGLQVLAAMARNHMSLHDLCSGMKMFPQILVNVRYTaGSGDPLEHESVKAVTAEVEAAL 402
Cdd:cd05802 319 GGEQSGHIIFLDHSTTGDGLLTALQLLAIMKRSGKSLSELASDMKLYPQVLVNVRVK-DKKALLENPRVQAAIAEAEKEL 397
|
410 420 430
....*....|....*....|....*....|....*..
gi 732683007 403 GNRGRVLLRKSGTEPLIRVMVEGEDEAQVTEFAHRIA 439
Cdd:cd05802 398 GGEGRVLVRPSGTEPLIRVMVEGEDEELVEKLAEELA 434
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
7-444 |
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: 637.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 7 FGTDGIRGRVGDAPITPDFVLKLGWAAGKVLARHGSRK--IIIGKDTRISGYMLESALEAGLAAAGLSALFTGPMPTPAV 84
Cdd:TIGR01455 1 FGTDGVRGRAGQEPLTAELALLLGAAAGRVLRQGRDTAprVVIGKDTRLSGYMLENALAAGLNSAGVDVLLLGPLPTPAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 85 AYLTRTFRAEAGIVISASHNPFYDNGIKFFSIDGTKLPDAVEEAIEAEMEKE--ISCVDSAELGKASRIVDAAGRYIEFC 162
Cdd:TIGR01455 81 AYLTRTLRADAGVMISASHNPYEDNGIKFFGPGGFKLDDATEAAIEALLDEAdpLPRPESEGLGRVKRYPDAVGRYIEFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 163 KATFPNELSLSELKIVVDCANGATYHIAPNVLRELGANVIAIGCEPNGVNINAEVGATDVRALQARVLAEKADLGIAFDG 242
Cdd:TIGR01455 161 KSTLPRGLTLSGLKVVLDCANGAAYKVAPHVFRELGAEVIAIGVEPDGLNINDGCGSTHLDALQKAVREHGADLGIAFDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 243 DGDRVIMVDHEGNKVDGDQIMYIIAREGLRQGQLRGGA-VGTLMSNMGLELALKQLGIPFARAKVGDRYVLEKMQEKGWR 321
Cdd:TIGR01455 241 DADRVLAVDANGRIVDGDQILYIIARALKESGELAGNTvVATVMSNLGLERALEKLGLTLIRTAVGDRYVLEEMRESGYN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 322 IGAENSGHVILLDKTTTGDGIVAGLQVLAAMARNHMSLHDLCSGMKMFPQILVNVRYTAGSGDPLEHESVKAVTAEVEAA 401
Cdd:TIGR01455 321 LGGEQSGHIILLDYSTTGDGIVSALQVLTIMKKSGSTLSELAAEFVPYPQTLVNVRVADRKLAAAEAPAVKAAIEDAEAE 400
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 732683007 402 LGNRGRVLLRKSGTEPLIRVMVEGEDEAQVTEFAHRIADAVKA 444
Cdd:TIGR01455 401 LGGTGRILLRPSGTEPLIRVMVEAADEELVQQLADTLADVVSA 443
|
|
| 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: 519.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 1 MSNRKYFGTDGIRGRVGDApITPDFVLKLGWAAGKVLARHGSRKIIIGKDTRISGYMLESALEAGLAAAGLSALFTGPMP 80
Cdd:COG1109 1 MTYKKLFGTDGIRGIVGEE-LTPEFVLKLGRAFGTYLKEKGGPKVVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 81 TPAVAYLTRTFRAEAGIVISASHNPFYDNGIKFFSIDGTKLPDAVEEAIEAEMEKE-ISCVDSAELGKASRIVDAAGRYI 159
Cdd:COG1109 80 TPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKEdFRRAEAEEIGKVTRIEDVLEAYI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 160 EFCKATFPNELSLSELKIVVDCANGATYHIAPNVLRELGANVIAIGCEPNGVNINAEVG--ATDVRALQARVLAEKADLG 237
Cdd:COG1109 160 EALKSLVDEALRLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFPNHNPNpePENLEDLIEAVKETGADLG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 238 IAFDGDGDRVIMVDHEGNKVDGDQIMYIIAREGLRQGQlRGGAVGTLMSNMGLELALKQLGIPFARAKVGDRYVLEKMQE 317
Cdd:COG1109 240 IAFDGDADRLGVVDEKGRFLDGDQLLALLARYLLEKGP-GGTVVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKMRE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 318 KGWRIGAENSGHVILLDKTTTGDGIVAGLQVLAAMARNHMSLHDLCSGMKMFPQILVNVRYTAGSGDPLEHESVKAV--- 394
Cdd:COG1109 319 TGAVLGGEESGGIIFPDFVPTDDGILAALLLLELLAKQGKSLSELLAELPRYPQPEINVRVPDEEKIGAVMEKLREAved 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 732683007 395 ------TAEVEAALGNRGRVLLRKSGTEPLIRVMVEGEDEAQVTEFAHRIADAVKAV 445
Cdd:COG1109 399 keeldtIDGVKVDLEDGGWVLVRPSGTEPLLRVYAEAKDEEEAEELLAELAELVEEA 455
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
6-439 |
3.07e-132 |
|
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: 385.17 E-value: 3.07e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 6 YFGTDGIRGRVGDApITPDFVLKLGWAAGKvlarhgsrkiiigkdtrisgymlesaleaglaaaglsalftgpmptpava 85
Cdd:cd03084 1 IFGTSGVRGVVGDD-ITPETAVALGQAIGS-------------------------------------------------- 29
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 86 yltrtfraEAGIVISASHNPFYDNGIKFFSIDGTKLPDAVEEAIEAEMEKEISCVDSA-ELGKASRIVDAAGRYIEFCKA 164
Cdd:cd03084 30 --------TGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSAVAyELGGSVKAVDILQRYFEALKK 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 165 TFPNE-LSLSELKIVVDCANGATYHIAPNVLRELGANVIAIGCEPNGV--NINAEVGA-TDVRALQARVLAEKADLGIAF 240
Cdd:cd03084 102 LFDVAaLSNKKFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCEPDGNfgNINPDPGSeTNLKQLLAVVKAEKADFGVAF 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 241 DGDGDRVIMVDHEGNKVDGDQIMYIIAREGLRQGQLRGGAVGTLMSNMGLELALKQLGIPFARAKVGDRYVLEKMQEKGW 320
Cdd:cd03084 182 DGDADRLIVVDENGGFLDGDELLALLAVELFLTFNPRGGVVKTVVSSGALDKVAKKLGIKVIRTKTGFKWVGEAMQEGDV 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 321 RIGAENSGHVILLDKTTTGDGIVAGLQVLAAMARNHMSLHDLCSGMKMFPQILVNVrytagsgdplehesvkavtaevea 400
Cdd:cd03084 262 VLGGEESGGVIFPEFHPGRDGISAALLLLEILANLGKSLSELFSELPRYYYIRLKV------------------------ 317
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 732683007 401 algnRGRVLLRKSGTEPLIRVMVE---GEDEAQVTEFAHRIA 439
Cdd:cd03084 318 ----RGWVLVRASGTEPAIRIYAEadtQEDVEQIKKEARELV 355
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
5-442 |
2.22e-97 |
|
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: 299.04 E-value: 2.22e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 5 KYFGTDGIRGRVGDaPITPDFVLKLGWAAGKVLarhGSRKIIIGKDTRISGYMLESALEAGLAAAGLSALFTGPMPTPAV 84
Cdd:TIGR03990 2 LLFGTSGIRGIVGE-ELTPELALKVGKAFGTYL---RGGKVVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLGIAPTPTL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 85 AYLTRTFRAEAGIVISASHNPFYDNGIKFFSIDGTKLPDAVEEAIEAEMEKE-ISCVDSAELGKASRIVDAAGRYIEFCK 163
Cdd:TIGR03990 78 QYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQEEEIEEIAESGdFERADWDEIGTVTSDEDAIDDYIEAIL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 164 ATFPNE-LSLSELKIVVDCANGATYHIAPNVLRELGANVIAIGCEPNG--VNINAEVGATDVRALQARVLAEKADLGIAF 240
Cdd:TIGR03990 158 DKVDVEaIRKKGFKVVVDCGNGAGSLTTPYLLRELGCKVITLNCQPDGtfPGRNPEPTPENLKDLSALVKATGADLGIAH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 241 DGDGDRVIMVDHEGNKVDGDQIMYIIAREGLRQGqlRGGAVGTLMSNMGLELALKQLGIPFARAKVGDRYVLEKMQEKGW 320
Cdd:TIGR03990 238 DGDADRLVFIDEKGRFIGGDYTLALFAKYLLEHG--GGKVVTNVSSSRAVEDVAERHGGEVIRTKVGEVNVAEKMKEEGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 321 RIGAENSGHVILLDKTTTGDGIVAGLQVLAAMARNHMSLHDLcsgMKMFPQiLVNVRYTAGSGDPLEHESVKAVTAEVEA 400
Cdd:TIGR03990 316 VFGGEGNGGWIFPDHHYCRDGLMAAALFLELLAEEGKPLSEL---LAELPK-YPMSKEKVELPDEDKEEVMEAVEEEFAD 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 732683007 401 ALGNR----------GRVLLRKSGTEPLIRVMVEGEDEAQVTEFAHRIADAV 442
Cdd:TIGR03990 392 AEIDTidgvridfedGWVLVRPSGTEPIVRIYAEAKTEERAEELLEEGRSLV 443
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
6-442 |
1.44e-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: 273.68 E-value: 1.44e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 6 YFGTDGIRGRVGDApITPDFVLKLGWAAGKVLarhGSRKIIIGKDTRISGYMLESALEAGLAAAGLSALFTGPMPTPAVA 85
Cdd:cd03087 1 LFGTSGIRGVVGEE-LTPELALKVGKALGTYL---GGGTVVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDIGIVPTPALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 86 YLTRTfRAEAGIVISASHNPFYDNGIKFFSIDGTKLPDAVEEAIEAEMEKEI-SCVDSAELGKASRIVDAAGRYIEFCKA 164
Cdd:cd03087 77 YAVRK-LGDAGVMITASHNPPEYNGIKLVNPDGTEFSREQEEEIEEIIFSERfRRVAWDEVGSVRREDSAIDEYIEAILD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 165 TFPNELSlSELKIVVDCANGATYHIAPNVLRELGANVIAIGCEPNG--VNINAEVGATDVRALQARVLAEKADLGIAFDG 242
Cdd:cd03087 156 KVDIDGG-KGLKVVVDCGNGAGSLTTPYLLRELGCKVITLNANPDGffPGRPPEPTPENLSELMELVRATGADLGIAHDG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 243 DGDRVIMVDHEGNKVDGDQIMYIIAREGLRQGqlrGGAVGT-LMSNMGLELALKQLGIPFARAKVGDRYVLEKMQEKGWR 321
Cdd:cd03087 235 DADRAVFVDEKGRFIDGDKLLALLAKYLLEEG---GGKVVTpVDASMLVEDVVEEAGGEVIRTPVGDVHVAEEMIENGAV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 322 IGAENSGHVILLDKTTTGDGIVAGLqVLAAMARNHMSLHDLCSGMKMFPQILVNVRYtagsGDPLEHESVKAVTAEVEAA 401
Cdd:cd03087 312 FGGEPNGGWIFPDHQLCRDGIMTAA-LLLELLAEEKPLSELLDELPKYPLLREKVEC----PDEKKEEVMEAVEEELSDA 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 732683007 402 LGNR------------GRVLLRKSGTEPLIRVMVEGEDEAQVTEFAHRIADAV 442
Cdd:cd03087 387 DEDVdtidgvrieyedGWVLIRPSGTEPKIRITAEAKTEERAKELLEEGRSKV 439
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
12-444 |
5.69e-71 |
|
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: 230.86 E-value: 5.69e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 12 IRGRVGDApITPDFVLKLGWAAGKVLARHGSRKIIIGKDTRISGYMLESALEAGLAAAGLSALFTGPMPTPAVAYLTRTF 91
Cdd:cd03089 7 IRGIAGEE-LTEEIAYAIGRAFGSWLLEKGAKKVVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPVLYFATFHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 92 RAEAGIVISASHNPFYDNGIKFF----SIDGTKLpdaveEAIEAEMEKEIScVDSAELGKASRiVDAAGRYIEFCKATFp 167
Cdd:cd03089 86 DADGGVMITASHNPPEYNGFKIVigggPLSGEDI-----QALRERAEKGDF-AAATGRGSVEK-VDILPDYIDRLLSDI- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 168 nELSLSELKIVVDCANGATYHIAPNVLRELGANVIAIGCEPNGV----NINAEVGATdVRALQARVLAEKADLGIAFDGD 243
Cdd:cd03089 158 -KLGKRPLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCEPDGTfpnhHPDPTDPEN-LEDLIAAVKENGADLGIAFDGD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 244 GDRVIMVDHEGNKVDGDQIMYIIAREGLRQgqlRGGA--VGTLMSNMGL-ELALKQLGIPFaRAKVGDRYVLEKMQEKGW 320
Cdd:cd03089 236 GDRLGVVDEKGEIIWGDRLLALFARDILKR---NPGAtiVYDVKCSRNLyDFIEEAGGKPI-MWKTGHSFIKAKMKETGA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 321 RIGAENSGHVIL------LDktttgDGIVAGLQVLAAMARNHMSLHDLCSGMKMFPQilvnvrytagSGD---PLEHESV 391
Cdd:cd03089 312 LLAGEMSGHIFFkdrwygFD-----DGIYAALRLLELLSKSGKTLSELLADLPKYFS----------TPEiriPVTEEDK 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 732683007 392 KAVTAEVEAALGNR----------------GRVLLRKSGTEPLIRVMVEGEDEaqvtEFAHRIADAVKA 444
Cdd:cd03089 377 FAVIERLKEHFEFPgaeiididgvrvdfedGWGLVRASNTEPVLVLRFEADTE----EGLEEIKAELRK 441
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
7-433 |
2.90e-61 |
|
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: 205.86 E-value: 2.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 7 FGTDGIRGRVGDApITPDFVLKLGWAAGKVLARH--GSRKIIIGKDTR------------------ISGYMLESaleagl 66
Cdd:cd05800 3 FGTDGWRGIIAED-FTFENVRRVAQAIADYLKEEggGGRGVVVGYDTRflseefaravaevlaangIDVYLSDR------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 67 aaaglsalftgPMPTPAVAYLTRTFRAEAGIVISASHNPFYDNGIKFFSIDGTKLPDAVEEAIEAEMEKEISCVDSAELG 146
Cdd:cd05800 76 -----------PVPTPAVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARLASGEPPGLEARAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 147 KASRIVDAAGRYIEFCKATF-PNELSLSELKIVVDCANGATYHIAPNVLRELGANVIAIGCEPN----GvnINAEVGATD 221
Cdd:cd05800 145 GLIETIDPKPDYLEALRSLVdLEAIREAGLKVVVDPMYGAGAGYLEELLRGAGVDVEEIRAERDplfgG--IPPEPIEKN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 222 VRALQARVLAEKADLGIAFDGDGDRVIMVDHEGNKVDGDQIMYIIAREGLRQGQLRGGAVGTL-MSNMGLELALKqLGIP 300
Cdd:cd05800 223 LGELAEAVKEGGADLGLATDGDADRIGAVDEKGNFLDPNQILALLLDYLLENKGLRGPVVKTVsTTHLIDRIAEK-HGLP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 301 FARAKVGDRYVLEKMQEKGWRIGAENSGHVILLDKTTTGDGIVAGLQVLAAMARNHMSLHDLcsgmkmFPQIL--VNVRY 378
Cdd:cd05800 302 VYETPVGFKYIAEKMLEEDVLIGGEESGGLGIRGHIPERDGILAGLLLLEAVAKTGKPLSEL------VAELEeeYGPSY 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732683007 379 TAGSGDPLEHESVKAVTAEVEAA----------------------LGNRGRVLLRKSGTEPLIRVMVEGEDEAQVTE 433
Cdd:cd05800 376 YDRIDLRLTPAQKEAILEKLKNEpplsiaggkvdevntidgvklvLEDGSWLLIRPSGTEPLLRIYAEAPSPEKVEA 452
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
11-437 |
3.01e-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: 187.13 E-value: 3.01e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 11 GIRGRVGDApITPDFVLKLGWAAGKVLARHGSRK-IIIGKDTRISGYMLESALEAGLAAAGLSALFTGPMPTPAVAYLTR 89
Cdd:cd05803 6 GIRGIVGEG-LTPEVITRYVAAFATWQPERTKGGkIVVGRDGRPSGPMLEKIVIGALLACGCDVIDLGIAPTPTVQVLVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 90 TFRAEAGIVISASHNPFYDNGIKFFSIDGTKL-PDAVEEAIEAEMEKEISCVDSAELGKASRIVDAAGRYIEFCKATFPN 168
Cdd:cd05803 85 QSQASGGIIITASHNPPQWNGLKFIGPDGEFLtPDEGEEVLSCAEAGSAQKAGYDQLGEVTFSEDAIAEHIDKVLALVDV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 169 ELSLSE---LKIVVDCANGATYHIAPNVLRELGANVIAIGCEPNG-VNINAEVGATDVRALQARVLAEKADLGIAFDGDG 244
Cdd:cd05803 165 DVIKIRernFKVAVDSVNGAGGLLIPRLLEKLGCEVIVLNCEPTGlFPHTPEPLPENLTQLCAAVKESGADVGFAVDPDA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 245 DRVIMVDHEGNKVDGDQIMYIIAREGLRQGQLRGGAVGTLMSNMGLELALKQLGIPFARAKVGDRYVLEKMQEKGWRIGA 324
Cdd:cd05803 245 DRLALVDEDGRPIGEEYTLALAVDYVLKYGGRKGPVVVNLSTSRALEDIARKHGVPVFRSAVGEANVVEKMKEVDAVIGG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 325 ENSGHVILLDKTTTGDGIVAGLQVLAAMARNHMSLHDLCSGmkmFPQILvNVRYTAGSGDPLEHESVKAVTAEVEAALGN 404
Cdd:cd05803 325 EGNGGVILPDVHYGRDSLVGIALVLQLLAASGKPLSEIVDE---LPQYY-ISKTKVTIAGEALERLLKKLEAYFKDAEAS 400
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 732683007 405 R----------GRVLLRKSGTEPLIRVMVEGEDEAQVTEFAHR 437
Cdd:cd05803 401 TldglrldsedSWVHVRPSNTEPIVRIIAEAPTQDEAEALADR 443
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
4-136 |
1.45e-45 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 154.69 E-value: 1.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 4 RKYFGTDGIRGRVGDAPITPDFVLKLGWAAGKVL-ARHGSRKIIIGKDTRISGYMLESALEAGLAAAGLSALFTGPMPTP 82
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGELTPEFALKLGQAIASYLrAQGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 732683007 83 AVAYLTRTFRAEAGIVISASHNPFYDNGIKFFSIDGTKLPDAVEEAIEAEMEKE 136
Cdd:pfam02878 81 AVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKE 134
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
258-363 |
1.26e-41 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 143.36 E-value: 1.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 258 DGDQIMYIIAREGLRQGQLRGGA--VGTLMSNMGLELALKQLGIPFARAKVGDRYVLEKMQEKGWRIGAENSGHVILLDK 335
Cdd:pfam02880 1 DGDQILALLAKYLLEQGKLPPGAgvVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLDH 80
|
90 100
....*....|....*....|....*...
gi 732683007 336 TTTGDGIVAGLQVLAAMARNHMSLHDLC 363
Cdd:pfam02880 81 ATTKDGILAALLVLEILARTGKSLSELL 108
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
12-444 |
2.00e-31 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 125.09 E-value: 2.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 12 IRGRVGDApITPDFVLKLGWAAGKVLARHGSRKIIIGKDTRISGYMLESALEAGLAAAGLSALFTGPMPTPAVAYLTRTF 91
Cdd:PRK09542 6 VRGVVGEQ-IDEDLVRDVGAAFARLMRAEGATTVVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIGLASTDQLYFASGLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 92 RAeAGIVISASHNPFYDNGIKFfSIDGTKlPDAVE---EAIEAEMEKEISCVDSAElGKASRIvDAAGRYIEFCKaTFPN 168
Cdd:PRK09542 85 DC-PGAMFTASHNPAAYNGIKL-CRAGAK-PVGQDtglAAIRDDLIAGVPAYDGPP-GTVTER-DVLADYAAFLR-SLVD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 169 ELSLSELKIVVDCANGATYHIAPNVLRELGANVIAIGCEPNGVNINAEVGATD---VRALQARVLAEKADLGIAFDGDGD 245
Cdd:PRK09542 159 LSGIRPLKVAVDAGNGMGGHTVPAVLGGLPITLLPLYFELDGTFPNHEANPLDpanLVDLQAFVRETGADIGLAFDGDAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 246 RVIMVDHEGNKVDGDQIMYIIAREGLRQGqlrGGAvgTLMSNMGLELALKQL-----GIPfARAKVGDRYVLEKMQEKGW 320
Cdd:PRK09542 239 RCFVVDERGQPVSPSAVTALVAARELARE---PGA--TIIHNLITSRAVPELvaergGTP-VRTRVGHSFIKALMAETGA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 321 RIGAENSGHVILLDKTTTGDGIVAGLQVLAAMARNHMSLHDLCSGMKmfpqilvnvRYtAGSGD-PLEHESVKAVTAEVE 399
Cdd:PRK09542 313 IFGGEHSAHYYFRDFWGADSGMLAALHVLAALGEQDRPLSELMADYQ---------RY-AASGEiNSTVADAPARMEAVL 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732683007 400 AALGNRGRVL-----------------LRKSGTEPLIRVMVEGEDEAQVTEFAHRIADAVKA 444
Cdd:PRK09542 383 KAFADRIVSVdhldgvtvdlgdgswfnLRASNTEPLLRLNVEARTEEEVDALVDEVLAIIRA 444
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
7-444 |
8.70e-27 |
|
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: 112.21 E-value: 8.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 7 FGTDGIRGRVG-------DAPIT------PDFVLKLGWAAGKvlarhgsRKIIIGKDTR------------------ISG 55
Cdd:cd05799 4 FGTAGLRGKMGagtnrmnDYTVRqatqglANYLKKKGPDAKN-------RGVVIGYDSRhnsrefaeltaavlaangIKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 56 YMlesaleaglaaaglsalFTGPMPTPAVAYLTRTFRAEAGIVISASHNPFYDNGIKFFSIDGTKLPDAVEEAIEAEMEK 135
Cdd:cd05799 77 YL-----------------FDDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 136 --EISCVDSAELGKASRIVDAA----GRYIEFCKA--TFPNELSLSELKIVVDCANGATYHIAPNVLRELGANVIAIG-- 205
Cdd:cd05799 140 vlEPLDIKFEEALDSGLIKYIGeeidDAYLEAVKKllVNPELNEGKDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVVee 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 206 -CEPNG-----VNINAEV-GATDvRALQarvLAEK--ADLGIAFDGDGDRV-IMVDHEGNK---VDGDQIMYIIAREGLR 272
Cdd:cd05799 220 qAEPDPdfptvKFPNPEEpGALD-LAIE---LAKKvgADLILATDPDADRLgVAVKDKDGEwrlLTGNEIGALLADYLLE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 273 QGQLRGGAVGTLM-------SNMGLELAlKQLGIPFARAKVGDRY---VLEKMQEKGWR--------IGAENSGHVilLD 334
Cdd:cd05799 296 QRKEKGKLPKNPVivktivsSELLRKIA-KKYGVKVEETLTGFKWignKIEELESGGKKflfgfeesIGYLVGPFV--RD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 335 KtttgDGIVAGLqVLAAMA----RNHMSLHDLCsgMKMFPQI------LVNVRYtAGSGDPlehESVKAVTAEVEAA--- 401
Cdd:cd05799 373 K----DGISAAA-LLAEMAaylkAQGKTLLDRL--DELYEKYgyykekTISITF-EGKEGP---EKIKAIMDRLRNNpnv 441
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 732683007 402 ----LGNRGRVLLRKSGTEPLIR--VMVEGEDEAQVtefAHRIADAVKA 444
Cdd:cd05799 442 ltfyLEDGSRVTVRPSGTEPKIKfyIEVVGKKTLEE---AEKKLDALKK 487
|
|
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
7-442 |
1.27e-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: 111.18 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 7 FGTDGIRGRVgDAPITPDFVLKLGWAAGKVLARhGSrKIIIGKDTRISGYMLESALEAGLAAAGLSALFTGPMPTPAVAY 86
Cdd:cd05805 2 FGGRGVSGLI-NVDITPEFATRLGAAYGSTLPP-GS-TVTVSRDASRASRMLKRALISGLLSTGVNVRDLGALPLPVARY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 87 LTRTFRAEAGIVISASHnpfYDNG---IKFFSIDGTKLPDAVEEAIEAEMEKE-ISCVDSAELGKASRIVDAAGRYIE-F 161
Cdd:cd05805 79 AIRFLGASGGIHVRTSP---DDPDkveIEFFDSRGLNISRAMERKIENAFFREdFRRAHVDEIGDITEPPDFVEYYIRgL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 162 CKATFPNELSLSELKIVVDCANGATYHIAPNVLRELGANVIAigcepngVNINAEVGA-----TDVRALQ--ARVLAE-K 233
Cdd:cd05805 156 LRALDTSGLKKSGLKVVIDYAYGVAGIVLPGLLSRLGCDVVI-------LNARLDEDAprtdtERQRSLDrlGRIVKAlG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 234 ADLGIAFDGDGDRVIMVDHEGNKVDGDQ----IMYIIAREglRQGqlrggavGTLM----SNMGLELALKQLGIPFARAK 305
Cdd:cd05805 229 ADFGVIIDPNGERLILVDEAGRVISDDLltalVSLLVLKS--EPG-------GTVVvpvtAPSVIEQLAERYGGRVIRTK 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 306 VGDRYVLEKMQEkGWRIGAENSGHVILLDKTTTGDGIVAGLQVLAAMARNHMSLHDLcsgMKMFPQILVNvrytagsgdp 385
Cdd:cd05805 300 TSPQALMEAALE-NVVLAGDGDGGFIFPEFHPGFDAIAALVKILEMLARTNISLSQI---VDELPRFYVL---------- 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732683007 386 leHESVKAVTAE--------VEAALGNR-------------GRVLLRKSGTEPLIRVMVEGEDEAQVTEFAHRIADAV 442
Cdd:cd05805 366 --HKEVPCPWEAkgrvmrrlIEEAPDKSielidgvkiyeddGWVLVLPDADEPLCHIYAEGSDQERAEELTEFYVEKV 441
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
9-443 |
1.69e-25 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 108.99 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 9 TDGIRGRVgdAPITPDFVLKLG-----WAAGKVLARHGSR-KIIIGKDTRISGYMLESALEAGLAAAGLSALFTGPMPTP 82
Cdd:PLN02371 78 VEGVEGEP--VTLTPPAVEAIGaafaeWLLEKKKADGSGElRVSVGRDPRISGPRLADAVFAGLASAGLDVVDMGLATTP 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 83 AVAYLTRT--FRAEAGIVISASHNPFYDNGIKFFSIDG------------------TKLPDAVEEAIEAEMEKEISCVD- 141
Cdd:PLN02371 156 AMFMSTLTerEDYDAPIMITASHLPYNRNGLKFFTKDGglgkpdikdileraariyKEWSDEGLLKSSSGASSVVCRVDf 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 142 ----SAELGKAsrIVDAAGRyiefckaTFPNELSLSELKIVVDCANGATYHIAPNVLRELGANVIAI------GCEPNGV 211
Cdd:PLN02371 236 mstyAKHLRDA--IKEGVGH-------PTNYETPLEGFKIVVDAGNGAGGFFAEKVLEPLGADTSGSlflepdGMFPNHI 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 212 NiNAEvGATDVRALQARVLAEKADLGIAFDGDGDRVIMVDHEGNKVDGDQIMYIIAREGLRQGQlrGGAVGT-LMSNMGL 290
Cdd:PLN02371 307 P-NPE-DKAAMSATTQAVLANKADLGIIFDTDVDRSAVVDSSGREINRNRLIALMSAIVLEEHP--GTTIVTdSVTSDGL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 291 ELALKQLGIPFARAKVGDRYVLekmqEKGWRIGA---------ENSGHVILLDKTTTGDGIVAGLQVLAAMARNHMS--- 358
Cdd:PLN02371 383 TTFIEKKGGKHHRFKRGYKNVI----DKGVRLNSdgeethlmiETSGHGALKENHFLDDGAYLAVKIIIELVRMRAAgag 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 359 --LHDLCSGM-----------------KMFPQILVNVRYTAG---------SGDPLEHESVKaVTAEVEaalGNRGRVLL 410
Cdd:PLN02371 459 ggLGDLIEDLeepleavelrlkildegKDFKAYGEEVLEHLRnsiesdgklEGAPVNYEGVR-VSDEGE---GFGGWFLL 534
|
490 500 510
....*....|....*....|....*....|...
gi 732683007 411 RKSGTEPLIRVMVEGEDEAQVTEFAHRIADAVK 443
Cdd:PLN02371 535 RQSLHDPVIPLNIESSSPGGAQKMALVVLTWLK 567
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
7-430 |
1.19e-23 |
|
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: 102.66 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 7 FGTDGIRGRVGDapITPDFVLKLGWAAGKVLARHGSRKII-IGKDTRISGYMLESALEAGLAAAGLSALFTGPMPTPAVA 85
Cdd:cd03088 2 FGTSGLRGLVTD--LTDEVCYAYTRAFLQHLESKFPGDTVaVGRDLRPSSPRIAAACAAALRDAGFRVVDCGAVPTPALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 86 YLTRTfRAEAGIVISASHNPFYDNGIKFFSIDG--TKlpdAVEEAIEAEMEKEISCVDSAELGKASRIVDAAGRYIEFCK 163
Cdd:cd03088 80 LYAMK-RGAPAIMVTGSHIPADRNGLKFYRPDGeiTK---ADEAAILAALVELPEALFDPAGALLPPDTDAADAYIARYT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 164 ATFPNElSLSELKIVVDCANGATYHIAPNVLRELGANVIAIGCEPNGVNINAE-VGATDVRALQARVLAEKADLGIAFDG 242
Cdd:cd03088 156 DFFGAG-ALKGLRIGVYQHSSVGRDLLVRILEALGAEVVPLGRSDTFIPVDTEaVRPEDRALAAAWAAEHGLDAIVSTDG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 243 DGDRVIMVDHEGNKVDGDQIMYIIAREglrqgqLRGGAVGT-LMSNMGLELALKQLGIPfaRAKVGDRYVLEKMQEkgwr 321
Cdd:cd03088 235 DGDRPLVADETGEWLRGDILGLLTARF------LGADTVVTpVSSNSAIELSGFFKRVV--RTRIGSPYVIAAMAE---- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 322 IGAENSGHVI--------LLDKTTTGDG--------------IVAglqVLAAMARNHMSLHDLCSGM----------KMF 369
Cdd:cd03088 303 AAAAGAGRVVgyeanggfLLGSDIERNGrtlkalptrdavlpILA---VLAAAKEAGIPLSELVASLparftasdrlQNF 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732683007 370 PQILVNVRYTAGSGDPLEHESVKAVTAEVEAAL----GNR-----GRVL-LRKSGTEPLIRVMVEGEDEAQ 430
Cdd:cd03088 380 PTEKSQALIARLSADPEARAAFFFALGGEVASIdttdGLRmtfanGDIVhLRPSGNAPELRCYVEADSEER 450
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
158-254 |
8.37e-22 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 89.66 E-value: 8.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 158 YIEFCKATFPNE-LSLSELKIVVDCANGATYHIAPNVLRELGANVIAIGCEPNG----VNINAEvGATDVRALQARVLAE 232
Cdd:pfam02879 2 YIDHLLELVDSEaLKKRGLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDPdfptRAPNPE-EPEALALLIELVKSV 80
|
90 100
....*....|....*....|..
gi 732683007 233 KADLGIAFDGDGDRVIMVDHEG 254
Cdd:pfam02879 81 GADLGIATDGDADRLGVVDERG 102
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
95-444 |
8.39e-22 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 98.19 E-value: 8.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 95 AGIVISASHNPFYDNGIKFFSIDG--------TKLPDAV----EEAIEAEMEKEI------------------------- 137
Cdd:PTZ00302 77 VGVMITASHNPIQDNGVKIIDPDGgmleesweKICTDFAnartGEDLVSVLMDCLtehgiklsnlkldlnksncskakvh 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 138 -------SCVD---------SAELGKASR------------IVDAAGR------------YIEFCKATF------PNELS 171
Cdd:PTZ00302 157 vgrdtrpSSPElvsallrglKLLIGSNVRnfgivttpqlhfLVAFANGlgvdvvessdelYYAYLLAAFkelyrtLQEGG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 172 LSEL------KIVVDCANG-ATYHIAP--NVLRELGANVI-AIGCEPNGVNINAEVGATDVRALQARVLAEKADLGI--- 238
Cdd:PTZ00302 237 PVDLtqnnskILVVDCANGvGGYKIKRffEALKQLGIEIIpININCDEEELLNDKCGADYVQKTRKPPRAMKEWPGDeet 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 239 ---AFDGDGDRVI--MVDHEGNKV----DGDQI-----MYIiaREGLRQGQLRG----GAVGTLMSNMG----LELALKQ 296
Cdd:PTZ00302 317 rvaSFDGDADRLVyfFPDKDGDDKwvllDGDRIailyaMLI--KKLLGKIQLKKkldiGVVQTAYANGAstnyLNELLGR 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 297 LGIPFAraKVGDRYvLEKMQEKgWRIGA--ENSGH--VILLDKT------------------------------TTGDGI 342
Cdd:PTZ00302 395 LRVYCA--PTGVKN-LHPKAHK-YDIGIyfEANGHgtVLFNEKAlaewakflakqnalnsacrqlekflrlfnqTIGDAI 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 343 VAGLQVLAAMARNHMSLHDlCSGMKM-FP--QILVNVRytagsgDPL-----EHESV----KAVTAEVEAAL---GNRGR 407
Cdd:PTZ00302 471 SDLLAVELALAFLGLSFQD-WLNLYTdLPsrQDKVTVK------DRTlitntEDETRllepKGLQDKIDAIVskyDNAAR 543
|
490 500 510
....*....|....*....|....*....|....*..
gi 732683007 408 VLLRKSGTEPLIRVMVEGEDEAQVTEFAHRIADAVKA 444
Cdd:PTZ00302 544 AFIRPSGTEPVVRVYAEAPTLEQADELANEVKGLVLR 580
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
1-433 |
1.15e-17 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 85.00 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 1 MSNRKYFGTDGIRGRVGDApITPDFVLKLGWAAGKVLArhgSRKIIIGKDTRISGYMLESALEAGLAAAGLSALFTGPMP 80
Cdd:PRK15414 1 MKKLTCFKAYDIRGKLGEE-LNEDIAWRIGRAYGEFLK---PKTIVLGGDVRLTSETLKLALAKGLQDAGVDVLDIGMSG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 81 TPAVAYLTRTFRAEAGIVISASHNPFYDNGIKFFS-----IDG-TKLPDaVEEAIEAemeKEISCVDSAELGKASRIvDA 154
Cdd:PRK15414 77 TEEIYFATFHLGVDGGIEVTASHNPMDYNGMKLVRegarpISGdTGLRD-VQRLAEA---NDFPPVDETKRGRYQQI-NL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 155 AGRYIEFCKAtFPNELSLSELKIVVDCANGATYHIAPNV---LRELGANVIAI-------GCEPNGV-NINAEVGATDVR 223
Cdd:PRK15414 152 RDAYVDHLFG-YINVKNLTPLKLVINSGNGAAGPVVDAIearFKALGAPVELIkvhntpdGNFPNGIpNPLLPECRDDTR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 224 alqARVLAEKADLGIAFDGDGDRVIMVDHEGNKVDGDQIMYIIAREGLRQGQLRGGAVGTLMSNMGLELALKQLGIPfAR 303
Cdd:PRK15414 231 ---NAVIKHGADMGIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPGAKIIHDPRLSWNTVDVVTAAGGTP-VM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 304 AKVGDRYVLEKMQEKGWRIGAENSGHVILLDKTTTGDGIVAGLQVLAAMARNHMSLHDLCSG-MKMFPqilvnvryTAGS 382
Cdd:PRK15414 307 SKTGHAFIKERMRKEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELVCLKGKTLGELVRDrMAAFP--------ASGE 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 732683007 383 GDPLEHESVKAVtAEVEAALGNRG----------------RVLLRKSGTEPLIRVMVEGEDEAQVTE 433
Cdd:PRK15414 379 INSKLAQPVEAI-NRVEQHFSREAlavdrtdgismtfadwRFNLRSSNTEPVVRLNVESRGDVPLME 444
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
96-442 |
1.65e-17 |
|
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: 84.57 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 96 GIVISASHNPFYDNGIKFFSIDGTKLPDAVEE----------AIEAEMEKEISCVDSAELGKAS---------------R 150
Cdd:cd03086 38 GVMITASHNPVEDNGVKIVDPDGEMLEESWEPyatqlanasdDELLVLVLMLISVKELNIDLSVpanvfvgrdtrpsgpA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 151 IVDAA--------GRYIEFCKATFP-------------------------------NELS-------LSELKIVVDCANG 184
Cdd:cd03086 118 LLQALldglkalgGNVIDYGLVTTPqlhylvraantegaygepteegyyeklskafNELYnllqdggDEPEKLVVDCANG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 185 -ATYHIAP--NVLR-ELGANVIAIGCEPNGVnINAEVGATDV----RALQARVLAEKADLGIAFDGDGDRVI--MVDHEg 254
Cdd:cd03086 198 vGALKLKEllKRLKkGLSVKIINDGEEGPEL-LNDGCGADYVktkqKPPRGFELKPPGVRCCSFDGDADRLVyfYPDSS- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 255 NKV---DGDQI-----MYIIAR-EGLRQGQ-LRGGAVGTLMSNmG-----LElalKQLGIPFARAKVGDRYVLEKMQEkg 319
Cdd:cd03086 276 NKFhllDGDKIatlfaKFIKELlKKAGEELkLTIGVVQTAYAN-GastkyLE---DVLKVPVVCTPTGVKHLHHAAEE-- 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 320 WRIGA--ENSGH--------------------------------VILLDKTTTGDGIVAGLQVLAAMARNHMSLHDLCSG 365
Cdd:cd03086 350 FDIGVyfEANGHgtvlfsesalakieensslsdeqekaaktllaFSRLINQTVGDAISDMLAVELILAALGWSPQDWDNL 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 366 MKMFPQILVNV---RYTAGSGDPLEHESVK------AVTAEVEAAlgNRGRVLLRKSGTEPLIRVMVEGEDEAQVTEFAH 436
Cdd:cd03086 430 YTDLPNRQLKVkvpDRSVIKTTDAERRLVEpkglqdKIDAIVAKY--NNGRAFVRPSGTEDVVRVYAEAATQEEADELAN 507
|
....*.
gi 732683007 437 RIADAV 442
Cdd:cd03086 508 EVAELV 513
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
373-443 |
4.11e-15 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 69.99 E-value: 4.11e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732683007 373 LVNVRYTAGSgDPLEHESVKAVTAEVEAALGNRGRVL-LRKSGTEPLIRVMVEGEDEAQVTEFAHRIADAVK 443
Cdd:pfam00408 1 LINVRVAEKK-KLAALAAILKVFADAEKILGEDGRRLdVRPSGTEPVLRVMVEGDSDEELARLADEIADLLE 71
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
35-246 |
3.97e-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: 68.02 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 35 KVLARHGSRKIIIGKDtrisgymlesaleaglaaaglsalftGPMPTPAVAYLTRTFRAEAGIVISASHNP---FYDNGI 111
Cdd:cd03085 71 KIAAANGVGKVVVGQN--------------------------GLLSTPAVSAVIRKRKATGGIILTASHNPggpEGDFGI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 112 KFFSIDGTKLPDAVEEAIEAEMEK-------EISCVDSAELGKAS--------RIVDAAGRYIEFCKATF-----PNELS 171
Cdd:cd03085 125 KYNTSNGGPAPESVTDKIYEITKKiteykiaDDPDVDLSKIGVTKfggkpftvEVIDSVEDYVELMKEIFdfdaiKKLLS 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 172 LSELKIVVDCANGATyhiapnvlrelGANVIAIGCEPNGVNINAEVGA---------------TDVRALQARVLAEKADL 236
Cdd:cd03085 205 RKGFKVRFDAMHGVT-----------GPYAKKIFVEELGAPESSVVNCtplpdfggghpdpnlTYAKDLVELMKSGEPDF 273
|
250
....*....|
gi 732683007 237 GIAFDGDGDR 246
Cdd:cd03085 274 GAASDGDGDR 283
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
3-442 |
3.34e-11 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 65.09 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 3 NRKYFGTDGIRGRVGdapitpdfvlkLGWAAGKVL----ARHG--------------SRKIIIGKDTRISGYML-ESALE 63
Cdd:PTZ00150 43 KRMEFGTAGLRGKMG-----------AGFNCMNDLtvqqTAQGlcayvietfgqalkSRGVVIGYDGRYHSRRFaEITAS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 64 AGLAAAGLSALFTGPMPTPAVAYLTRTFRAEAGIVISASHNPFYDNGIKFFSIDGTKlpdaveeaIEAEMEKEIS-CVDS 142
Cdd:PTZ00150 112 VFLSKGFKVYLFGQTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVYWSNGAQ--------IIPPHDKNISaKILS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 143 A--------ELGKASRIVDA----AGRYIEFCKATF-PNELSLSELKIVVDCANGATYHIAPNVLRELGAN---VIAIGC 206
Cdd:PTZ00150 184 NlepwssswEYLTETLVEDPlaevSDAYFATLKSEYnPACCDRSKVKIVYTAMHGVGTRFVQKALHTVGLPnllSVAQQA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 207 EPNG----VNI-NAEVGATdvrALQ-ARVLAEKADLGI--AFDGDGDRVIMVDHEGNK---VDGDQIMYIIAREGLRQGQ 275
Cdd:PTZ00150 264 EPDPefptVTFpNPEEGKG---ALKlSMETAEAHGSTVvlANDPDADRLAVAEKLNNGwkiFTGNELGALLAWWAMKRYR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 276 LRGGA------VGTLMSNMGLELALKQLGIPFARAKVGDRYV----LEKMQEKGWRI---GAENSGHVI---LLDKtttg 339
Cdd:PTZ00150 341 RQGIDkskcffICTVVSSRMLKKMAEKEGFQYDETLTGFKWIgnkaIELNAENGLTTlfaYEEAIGFMLgtrVRDK---- 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 340 DGIVAgLQVLAAMA----RNHMSLHDLCSGM-----------------------KMFPQILVNVRY-------------- 378
Cdd:PTZ00150 417 DGVTA-AAVVAEMAlylyERGKTLVEHLESLykqygyhftnnsyyicydpsrivSIFNDIRNNGSYptklggypvtrird 495
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 732683007 379 -TAG--SGDPlEHESVKAVTAEVEA---ALGNRGRVLLRKSGTEPLIRVMVE---GEDEAQVTEFAHRIADAV 442
Cdd:PTZ00150 496 lTTGydTATP-DGKPLLPVSASTQMitfYFENGAIITIRGSGTEPKLKWYAElsgTKDEAVEKELAALVDEVV 567
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
35-246 |
1.19e-09 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 60.15 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 35 KVLARHGSRKIIIGKDtrisgymlesaleaglaaaglsalftGPMPTPAVAYLTRTFRAEA-----GIVISASHNPFYDN 109
Cdd:PRK07564 98 EVLAANGVGVVIVGRG--------------------------GYTPTPAVSHAILKYNGRGggladGIVITPSHNPPEDG 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 110 GIKFFSIDG----TKLPDAVEE---AIEAEMEKEISCVDSAELGKASRI--VDAAGRYIEFCKATFPNE-LSLSELKIVV 179
Cdd:PRK07564 152 GIKYNPPNGgpadTDVTDAIEAranELLAYGLKGVKRIPLDRALASMTVevIDPVADYVEDLENVFDFDaIRKAGLRLGV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 180 DCANGATYHIAPNVLRELGANViaigcepnGVnINAEVGAT--------------D---VRALQARVLAEKA-DLGIAFD 241
Cdd:PRK07564 232 DPLGGATGPYWKAIAERYGLDL--------TV-VNAPVDPTfnfmpldddgkirmDcssPYAMAGLLALKDAfDLAFAND 302
|
....*
gi 732683007 242 GDGDR 246
Cdd:PRK07564 303 PDGDR 307
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
93-444 |
4.15e-09 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 58.50 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 93 AEAGIVISASHNPFYDNGIKFFSIDGTKLPDA--------------------VEEAIEAEMEKEISCVDSAE--LGKASR 150
Cdd:PLN02895 58 AATGLMITASHNPVSDNGVKIVDPSGGMLPQAwepfadalanapdpdalvqlIREFVKKENIPAVGGNPPAEvlLGRDTR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 151 -----IVDAAGRYIEFCKA--------TFP---------------NE------LSLS-----------------ELKIVV 179
Cdd:PLN02895 138 psgpaLLAAALKGVRAIGAravdmgilTTPqlhwmvraankgmkaTEsdyfeqLSSSfralldlipngsgddraDDKLVV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 180 DCANGATYHIAPNVLRELGANVIAI---GCEPNGVnINAEVGATDVRalQARVL---AEKADLGI---AFDGDGDRVI-- 248
Cdd:PLN02895 218 DGANGVGAEKLETLKKALGGLDLEVrnsGKEGEGV-LNEGVGADFVQ--KEKVPptgFASKDVGLrcaSLDGDADRLVyf 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 249 -MVDHEGN--KVDGDQIMYIIA---REGLRQ-----------GQLRGGAVGTLMSNMGLELALKQ-LGIPFARAKVGDRY 310
Cdd:PLN02895 295 yVSSAGSKidLLDGDKIASLFAlfiKEQLRIlngngnekpeeLLVRLGVVQTAYANGASTAYLKQvLGLEVVCTPTGVKY 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 311 VLEKMQEKGWRIGAENSGHVILLDKTTTGDGIVAGLQVLAAMARN-----------------HMSLHDLCSGMKMFPQIL 373
Cdd:PLN02895 375 LHEAAAEFDIGVYFEANGHGTVLFSERFLDWLEAAAAELSSKAKGseahkaarrllavsrliNQAVGDALSGLLLVEAIL 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 374 VNVRYTAGSGDPL----------------------EHESV--------KAVTAEVEAAlgNRGRVLLRKSGTEPLIRVMV 423
Cdd:PLN02895 455 QYRGWSLAEWNALyqdlpsrqlkvkvadrtaitttDAETVvvrpaglqDAIDAEVAKY--PRGRAFVRPSGTEDVVRVYA 532
|
490 500
....*....|....*....|.
gi 732683007 424 EGEDEAQVTEFAHRIADAVKA 444
Cdd:PLN02895 533 EASTQEAADSLAREVARLVYD 553
|
|
| PLN02307 |
PLN02307 |
phosphoglucomutase |
35-246 |
4.36e-09 |
|
phosphoglucomutase
Pssm-ID: 177942 [Multi-domain] Cd Length: 579 Bit Score: 58.51 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 35 KVLARHGSRKIIIGKDtrisgymlesaleaglaaaglsalftGPMPTPAVAYLTR---TFRAEAGIVISASHN---PFYD 108
Cdd:PLN02307 83 KIAAANGVRRVWVGQN--------------------------GLLSTPAVSAVIRerdGSKANGGFILTASHNpggPEED 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 109 NGIKFFSIDGTKLPDAVEEAI--------EAEMEKEISCVDSAELGKAS---------RIVDAAGRYIEFCKATFPNE-- 169
Cdd:PLN02307 137 FGIKYNYESGQPAPESITDKIygntltikEYKMAEDIPDVDLSAVGVTKfggpedfdvEVIDPVEDYVKLMKSIFDFEli 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732683007 170 ---LSLSELKIVVDCANGATYHIAPNVL-RELGANVIAI----------GCEPNGvNINAEVGATDVRALQARVLAEKA- 234
Cdd:PLN02307 217 kklLSRPDFTFCFDAMHGVTGAYAKRIFvEELGAPESSLlncvpkedfgGGHPDP-NLTYAKELVKRMGLGKTSYGDEPp 295
|
250
....*....|..
gi 732683007 235 DLGIAFDGDGDR 246
Cdd:PLN02307 296 EFGAASDGDGDR 307
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
77-131 |
1.08e-03 |
|
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: 41.46 E-value: 1.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732683007 77 GPMPTPAVAYLTRTFRAEA------GIVISASHNPFYDNGIKFFSIDGTKLPDAVEEAIEA 131
Cdd:cd05801 97 GYTPTPVISHAILTYNRGRtegladGIVITPSHNPPEDGGFKYNPPHGGPADTDITRWIEK 157
|
|
| |
