|
Name |
Accession |
Description |
Interval |
E-value |
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
5-439 |
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: 720.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 5 FFGTDGIRGQANSfPMTPEIAMKVGMAVGYIFRRKGQASRVVIGKDTRRSGYMLENALVAGFTAAGMDVFLLGPIPTPAV 84
Cdd:cd05802 1 LFGTDGIRGVANE-PLTPELALKLGRAAGKVLGKGGGRPKVLIGKDTRISGYMLESALAAGLTSAGVDVLLLGVIPTPAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 85 AMLCRSLRADIGVMISASHNPFYDNGIKLFGPDGFKLSDQIELQIEAMIEGDMTPfLASHGDVGRAKRVDGDIYRYIEFA 164
Cdd:cd05802 80 AYLTRKLRADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVEEEIEALIDKELEL-PPTGEKIGRVYRIDDARGRYIEFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 165 KRTLPRNiSLNGLRVVVDCANGAGYKVAPAALWELGAEVITINNEPNGININEDCGSTHPIGLMKKVHEVRADVGIALDG 244
Cdd:cd05802 159 KSTFPKD-LLSGLKIVLDCANGAAYKVAPEVFRELGAEVIVINNAPDGLNINVNCGSTHPESLQKAVLENGADLGIAFDG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 245 DADRVLLVDENGTVIDGDQLMAVIAESWAASNRLEGGGIVATVMSNLGLERFLADRNLTLARTKVGDRYVVEHMREHGFN 324
Cdd:cd05802 238 DADRVIAVDEKGNIVDGDQILAICARDLKERGRLKGNTVVGTVMSNLGLEKALKELGIKLVRTKVGDRYVLEEMLKHGAN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 325 VGGEQSGHIVLSDFATTGDGLISALQILAVAQEQNKPISDVCRKFQPVPQLLKNVRTTGGKPL-ENKRVKSAIDEAKERL 403
Cdd:cd05802 318 LGGEQSGHIIFLDHSTTGDGLLTALQLLAIMKRSGKSLSELASDMKLYPQVLVNVRVKDKKALlENPRVQAAIAEAEKEL 397
|
410 420 430
....*....|....*....|....*....|....*.
gi 490826587 404 GGQGRLVIRPSGTEPLIRVMAEGDDRGLVEKVVNDI 439
Cdd:cd05802 398 GGEGRVLVRPSGTEPLIRVMVEGEDEELVEKLAEEL 433
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
3-443 |
0e+00 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 684.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 3 RKFFGTDGIRGQANSFPMTPEIAMKVGMAVGYIFRRKGQAsRVVIGKDTRRSGYMLENALVAGFTAAGMDVFLLGPIPTP 82
Cdd:PRK10887 1 RKYFGTDGIRGKVGQAPITPDFVLKLGWAAGKVLARQGRP-KVLIGKDTRISGYMLESALEAGLAAAGVDVLLTGPMPTP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 83 AVAMLCRSLRADIGVMISASHNPFYDNGIKLFGPDGFKLSDQIELQIEAMIEGDMTpfLASHGDVGRAKRVDGDIYRYIE 162
Cdd:PRK10887 80 AVAYLTRTLRAEAGIVISASHNPYYDNGIKFFSADGTKLPDEVELAIEAELDKPLT--CVESAELGKASRINDAAGRYIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 163 FAKRTLPRNISLNGLRVVVDCANGAGYKVAPAALWELGAEVITINNEPNGININEDCGSTHPIGLMKKVHEVRADVGIAL 242
Cdd:PRK10887 158 FCKSTFPNELSLRGLKIVVDCANGATYHIAPNVFRELGAEVIAIGCEPNGLNINDECGATDPEALQAAVLAEKADLGIAF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 243 DGDADRVLLVDENGTVIDGDQLMAVIAESWAASNRLEgGGIVATVMSNLGLERFLADRNLTLARTKVGDRYVVEHMREHG 322
Cdd:PRK10887 238 DGDGDRVIMVDHLGNLVDGDQLLYIIARDRLRRGQLR-GGVVGTLMSNMGLELALKQLGIPFVRAKVGDRYVLEKLQEKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 323 FNVGGEQSGHIVLSDFATTGDGLISALQILAVAQEQNKPISDVCRKFQPVPQLLKNVRTTGGK--PLENKRVKSAIDEAK 400
Cdd:PRK10887 317 WRLGGENSGHILCLDKTTTGDGIVAALQVLAAMVRSGMSLADLCSGMKLFPQVLINVRFKPGAddPLESEAVKAALAEVE 396
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 490826587 401 ERLGGQGRLVIRPSGTEPLIRVMAEGDDRGLVEKVVNDIIDVI 443
Cdd:PRK10887 397 AELGGRGRVLLRKSGTEPLIRVMVEGEDEAQVTALAERIADAV 439
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
6-444 |
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: 652.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 6 FGTDGIRGQANSFPMTPEIAMKVGMAVGYIFRRKG-QASRVVIGKDTRRSGYMLENALVAGFTAAGMDVFLLGPIPTPAV 84
Cdd:TIGR01455 1 FGTDGVRGRAGQEPLTAELALLLGAAAGRVLRQGRdTAPRVVIGKDTRLSGYMLENALAAGLNSAGVDVLLLGPLPTPAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 85 AMLCRSLRADIGVMISASHNPFYDNGIKLFGPDGFKLSDQIELQIEAMIEGDMTPFLASHGDVGRAKRVDGDIYRYIEFA 164
Cdd:TIGR01455 81 AYLTRTLRADAGVMISASHNPYEDNGIKFFGPGGFKLDDATEAAIEALLDEADPLPRPESEGLGRVKRYPDAVGRYIEFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 165 KRTLPRNISLNGLRVVVDCANGAGYKVAPAALWELGAEVITINNEPNGININEDCGSTHPIGLMKKVHEVRADVGIALDG 244
Cdd:TIGR01455 161 KSTLPRGLTLSGLKVVLDCANGAAYKVAPHVFRELGAEVIAIGVEPDGLNINDGCGSTHLDALQKAVREHGADLGIAFDG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 245 DADRVLLVDENGTVIDGDQLMAVIAESWAASNRLEGGGIVATVMSNLGLERFLADRNLTLARTKVGDRYVVEHMREHGFN 324
Cdd:TIGR01455 241 DADRVLAVDANGRIVDGDQILYIIARALKESGELAGNTVVATVMSNLGLERALEKLGLTLIRTAVGDRYVLEEMRESGYN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 325 VGGEQSGHIVLSDFATTGDGLISALQILAVAQEQNKPISDVCRKFQPVPQLLKNVRTTGGK--PLENKRVKSAIDEAKER 402
Cdd:TIGR01455 321 LGGEQSGHIILLDYSTTGDGIVSALQVLTIMKKSGSTLSELAAEFVPYPQTLVNVRVADRKlaAAEAPAVKAAIEDAEAE 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 490826587 403 LGGQGRLVIRPSGTEPLIRVMAEGDDRGLVEKVVNDIIDVIS 444
Cdd:TIGR01455 401 LGGTGRILLRPSGTEPLIRVMVEAADEELVQQLADTLADVVS 442
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
1-446 |
0e+00 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 551.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 1 MT-RKFFGTDGIRGQANSFpMTPEIAMKVGMAVGYIFRRKGQaSRVVIGKDTRRSGYMLENALVAGFTAAGMDVFLLGPI 79
Cdd:COG1109 1 MTyKKLFGTDGIRGIVGEE-LTPEFVLKLGRAFGTYLKEKGG-PKVVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 80 PTPAVAMLCRSLRADIGVMISASHNPFYDNGIKLFGPDGFKLSDQIELQIEAMIEGDMTPFlASHGDVGRAKRVDGDIYR 159
Cdd:COG1109 79 PTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKEDFRR-AEAEEIGKVTRIEDVLEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 160 YIEFAKRTLPRNISLNGLRVVVDCANGAGYKVAPAALWELGAEVITINNEPNGININEDCG--STHPIGLMKKVHEVRAD 237
Cdd:COG1109 158 YIEALKSLVDEALRLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFPNHNPNpePENLEDLIEAVKETGAD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 238 VGIALDGDADRVLLVDENGTVIDGDQLMAVIAESWAASNrlEGGGIVATVMSNLGLERFLADRNLTLARTKVGDRYVVEH 317
Cdd:COG1109 238 LGIAFDGDADRLGVVDEKGRFLDGDQLLALLARYLLEKG--PGGTVVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 318 MREHGFNVGGEQSGHIVLSDFATTGDGLISALQILAVAQEQNKPISDVCRKFQPVPQLLKNVRTTGGKPLEN--KRVKSA 395
Cdd:COG1109 316 MRETGAVLGGEESGGIIFPDFVPTDDGILAALLLLELLAKQGKSLSELLAELPRYPQPEINVRVPDEEKIGAvmEKLREA 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 396 ---------IDEAKERLGGQGRLVIRPSGTEPLIRVMAEGDDRGLVEKVVNDIIDVISSE 446
Cdd:COG1109 396 vedkeeldtIDGVKVDLEDGGWVLVRPSGTEPLLRVYAEAKDEEEAEELLAELAELVEEA 455
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
4-443 |
1.96e-113 |
|
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: 340.64 E-value: 1.96e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 4 KFFGTDGIRGQANSfPMTPEIAMKVGMAVGYIFRRKgqasRVVIGKDTRRSGYMLENALVAGFTAAGMDVFLLGPIPTPA 83
Cdd:TIGR03990 2 LLFGTSGIRGIVGE-ELTPELALKVGKAFGTYLRGG----KVVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLGIAPTPT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 84 VAMLCRSLRADIGVMISASHNPFYDNGIKLFGPDGFKLSDQIELQIEAMIEGDmTPFLASHGDVGRAKRVDGDIYRYIEF 163
Cdd:TIGR03990 77 LQYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQEEEIEEIAESG-DFERADWDEIGTVTSDEDAIDDYIEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 164 AKRTLPRN-ISLNGLRVVVDCANGAGYKVAPAALWELGAEVITINNEPNGI-----------NINEdcgsthpigLMKKV 231
Cdd:TIGR03990 156 ILDKVDVEaIRKKGFKVVVDCGNGAGSLTTPYLLRELGCKVITLNCQPDGTfpgrnpeptpeNLKD---------LSALV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 232 HEVRADVGIALDGDADRVLLVDENGTVIDGDQLMAVIAEsWAASNRleGGGIVATVMSNLGLERFLADRNLTLARTKVGD 311
Cdd:TIGR03990 227 KATGADLGIAHDGDADRLVFIDEKGRFIGGDYTLALFAK-YLLEHG--GGKVVTNVSSSRAVEDVAERHGGEVIRTKVGE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 312 RYVVEHMREHGFNVGGEQSGHIVLSDFATTGDGLISALQILAVAQEQNKPISDVCRKFQPVPQLLKNVrttggkPLENKR 391
Cdd:TIGR03990 304 VNVAEKMKEEGAVFGGEGNGGWIFPDHHYCRDGLMAAALFLELLAEEGKPLSELLAELPKYPMSKEKV------ELPDED 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490826587 392 VKSAIDEAKERL--------------GGQGRLVIRPSGTEPLIRVMAEGDDRGLVEKVVNDIIDVI 443
Cdd:TIGR03990 378 KEEVMEAVEEEFadaeidtidgvridFEDGWVLVRPSGTEPIVRIYAEAKTEERAEELLEEGRSLV 443
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
5-439 |
2.25e-107 |
|
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: 324.91 E-value: 2.25e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 5 FFGTDGIRGQANSFpMTPEIAMKVGMAVGYIFrrkgQASRVVIGKDTRRSGYMLENALVAGFTAAGMDVFLLGPIPTPAV 84
Cdd:cd03087 1 LFGTSGIRGVVGEE-LTPELALKVGKALGTYL----GGGTVVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDIGIVPTPAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 85 AMLCRSlRADIGVMISASHNPFYDNGIKLFGPDGFKLSDQIELQIEAMIEGDMTPfLASHGDVGRAKRVDGDIYRYIEFA 164
Cdd:cd03087 76 QYAVRK-LGDAGVMITASHNPPEYNGIKLVNPDGTEFSREQEEEIEEIIFSERFR-RVAWDEVGSVRREDSAIDEYIEAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 165 KRTLPRNISLnGLRVVVDCANGAGYKVAPAALWELGAEVITIN-----------NEPNGININEdcgsthpigLMKKVHE 233
Cdd:cd03087 154 LDKVDIDGGK-GLKVVVDCGNGAGSLTTPYLLRELGCKVITLNanpdgffpgrpPEPTPENLSE---------LMELVRA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 234 VRADVGIALDGDADRVLLVDENGTVIDGDQLMAVIAEsWAASNRleGGGIVATVMSNLGLERFLADRNLTLARTKVGDRY 313
Cdd:cd03087 224 TGADLGIAHDGDADRAVFVDEKGRFIDGDKLLALLAK-YLLEEG--GGKVVTPVDASMLVEDVVEEAGGEVIRTPVGDVH 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 314 VVEHMREHGFNVGGEQSGHIVLSDFATTGDGLISALQILAVAQEqNKPISDVCRKFQPVPQLLKNVRTTGGKPLE-NKRV 392
Cdd:cd03087 301 VAEEMIENGAVFGGEPNGGWIFPDHQLCRDGIMTAALLLELLAE-EKPLSELLDELPKYPLLREKVECPDEKKEEvMEAV 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 393 KSAIDEAKERL---------GGQGRLVIRPSGTEPLIRVMAEGDDR----GLVEKVVNDI 439
Cdd:cd03087 380 EEELSDADEDVdtidgvrieYEDGWVLIRPSGTEPKIRITAEAKTEerakELLEEGRSKV 439
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
11-443 |
2.03e-80 |
|
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: 255.52 E-value: 2.03e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 11 IRGQANSfPMTPEIAMKVGMAVGYIFRRKGQaSRVVIGKDTRRSGYMLENALVAGFTAAGMDVFLLGPIPTPAVAMLCRS 90
Cdd:cd03089 7 IRGIAGE-ELTEEIAYAIGRAFGSWLLEKGA-KKVVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPVLYFATFH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 91 LRADIGVMISASHNPFYDNGIKLFGPDGFKLSDQIElQIEAMIEGDMTPFLASHGDVgraKRVDgDIYRYIEFakrtLPR 170
Cdd:cd03089 85 LDADGGVMITASHNPPEYNGFKIVIGGGPLSGEDIQ-ALRERAEKGDFAAATGRGSV---EKVD-ILPDYIDR----LLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 171 NISLN--GLRVVVDCANGAGYKVAPAALWELGAEVITINNEPNGININEdcgstHP--------IGLMKKVHEVRADVGI 240
Cdd:cd03089 156 DIKLGkrPLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCEPDGTFPNH-----HPdptdpenlEDLIAAVKENGADLGI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 241 ALDGDADRVLLVDENGTVIDGDQLMAVIAEswAASNRLEGGGIVATVMSNLGLERFLADRNLTLARTKVGDRYVVEHMRE 320
Cdd:cd03089 231 AFDGDGDRLGVVDEKGEIIWGDRLLALFAR--DILKRNPGATIVYDVKCSRNLYDFIEEAGGKPIMWKTGHSFIKAKMKE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 321 HGFNVGGEQSGHIVLSD-FATTGDGLISALQILAVAQEQNKPISDVCRKFQPVPQLLK-NVRTTGGKPLEN-KRVKSAID 397
Cdd:cd03089 309 TGALLAGEMSGHIFFKDrWYGFDDGIYAALRLLELLSKSGKTLSELLADLPKYFSTPEiRIPVTEEDKFAViERLKEHFE 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 490826587 398 EAKERL---------GGQGRLVIRPSGTEPLIRVMAEGDDRGLVEKVVNDIIDVI 443
Cdd:cd03089 389 FPGAEIididgvrvdFEDGWGLVRASNTEPVLVLRFEADTEEGLEEIKAELRKLL 443
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
6-440 |
8.55e-79 |
|
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: 248.43 E-value: 8.55e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 6 FGTDGIRGQANSFpMTPEIAMKVGMAVGyifrRKGqasrvvigkdtrrsgymlenalvagftaagmdvfllgpiptpava 85
Cdd:cd03084 2 FGTSGVRGVVGDD-ITPETAVALGQAIG----STG--------------------------------------------- 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 86 mlcrslradiGVMISASHNPFYDNGIKLFGPDGFKLSDQIELQIEAMIEGDMTPFLASHGDVGRAKRVDGdIYRYIEFAK 165
Cdd:cd03084 32 ----------GIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSAVAYELGGSVKAVDI-LQRYFEALK 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 166 RTLP-RNISLNGLRVVVDCANGAGYKVAPAALWELGAEVITINNEPNG--ININEDCGS-THPIGLMKKVHEVRADVGIA 241
Cdd:cd03084 101 KLFDvAALSNKKFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCEPDGnfGNINPDPGSeTNLKQLLAVVKAEKADFGVA 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 242 LDGDADRVLLVDENGTVIDGDQLMAVIAeSWAASNRLEGGGIVATVMSNLGLERFLADRNLTLARTKVGDRYVVEHMREH 321
Cdd:cd03084 181 FDGDADRLIVVDENGGFLDGDELLALLA-VELFLTFNPRGGVVKTVVSSGALDKVAKKLGIKVIRTKTGFKWVGEAMQEG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 322 GFNVGGEQSGHIVLSDFATTGDGLISALQILAVAQEQNKPISDVCRKFQPVPQLLKNVRttggkplenkrvksaideake 401
Cdd:cd03084 260 DVVLGGEESGGVIFPEFHPGRDGISAALLLLEILANLGKSLSELFSELPRYYYIRLKVR--------------------- 318
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 490826587 402 rlggqGRLVIRPSGTEPLIRVMAEGD---DRGLVEKVVNDII 440
Cdd:cd03084 319 -----GWVLVRASGTEPAIRIYAEADtqeDVEQIKKEARELV 355
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
6-437 |
6.64e-66 |
|
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily and is found in both archaea and bacteria. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four structural domains (subdomains) with a centrally located active site formed by four loops, one from each subdomain. All four subdomains are included in this alignment model.
Pssm-ID: 100093 Cd Length: 461 Bit Score: 218.19 E-value: 6.64e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 6 FGTDGIRGQ-ANSFpmTPEIAMKVGMAVG-YIFRRKGQASRVVIGKDTRrsgYMLEN--ALVAG-FTAAGMDVFLL-GPI 79
Cdd:cd05800 3 FGTDGWRGIiAEDF--TFENVRRVAQAIAdYLKEEGGGGRGVVVGYDTR---FLSEEfaRAVAEvLAANGIDVYLSdRPV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 80 PTPAVAMLCRSLRADIGVMISASHNPFYDNGIKLFGPDGFKLSDQIELQIEAMIEgdmtpflaSHGDVGRAKRVDGDIYR 159
Cdd:cd05800 78 PTPAVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARLA--------SGEPPGLEARAEGLIET 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 160 ------YIEFAKRTL-PRNISLNGLRVVVDCANGAGYKVAPAALWELGAEVITINNEPN----GININedcgsthPIG-- 226
Cdd:cd05800 150 idpkpdYLEALRSLVdLEAIREAGLKVVVDPMYGAGAGYLEELLRGAGVDVEEIRAERDplfgGIPPE-------PIEkn 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 227 ---LMKKVHEVRADVGIALDGDADRVLLVDENGTVIDGDQLMAVIAeSWAASNRLEGGGIVATV-MSNLgLERFLADRNL 302
Cdd:cd05800 223 lgeLAEAVKEGGADLGLATDGDADRIGAVDEKGNFLDPNQILALLL-DYLLENKGLRGPVVKTVsTTHL-IDRIAEKHGL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 303 TLARTKVGDRYVVEHMREHGFNVGGEQSGHIVLSDFATTGDGLISALQILAVAQEQNKPISDVCRKFQ------------ 370
Cdd:cd05800 301 PVYETPVGFKYIAEKMLEEDVLIGGEESGGLGIRGHIPERDGILAGLLLLEAVAKTGKPLSELVAELEeeygpsyydrid 380
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490826587 371 -PVP-----QLLKNVRTTGGKPLENKRVK--SAIDEAKERLGGQGRLVIRPSGTEPLIRVMAEGDDRGLVEKVVN 437
Cdd:cd05800 381 lRLTpaqkeAILEKLKNEPPLSIAGGKVDevNTIDGVKLVLEDGSWLLIRPSGTEPLLRIYAEAPSPEKVEALLD 455
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
10-429 |
3.29e-60 |
|
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate guanyltransferase domain in a protein of unknown function that is found in both prokaryotes and eukaryotes. This domain belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100096 Cd Length: 445 Bit Score: 202.92 E-value: 3.29e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 10 GIRGQANSfPMTPEIAMKVGMAVGYIFRRKGQASRVVIGKDTRRSGYMLENALVAGFTAAGMDVFLLGPIPTPAVAMLCR 89
Cdd:cd05803 6 GIRGIVGE-GLTPEVITRYVAAFATWQPERTKGGKIVVGRDGRPSGPMLEKIVIGALLACGCDVIDLGIAPTPTVQVLVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 90 SLRADIGVMISASHNPFYDNGIKLFGPDGFKLS-DQIELQIEAMIEGDMTPflASHGDVGRAKRVDGDIYRYIEFAKRTL 168
Cdd:cd05803 85 QSQASGGIIITASHNPPQWNGLKFIGPDGEFLTpDEGEEVLSCAEAGSAQK--AGYDQLGEVTFSEDAIAEHIDKVLALV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 169 PRNISLNG---LRVVVDCANGAGYKVAPAALWELGAEVITINNEPNGI--NINEdcgsthPI-----GLMKKVHEVRADV 238
Cdd:cd05803 163 DVDVIKIRernFKVAVDSVNGAGGLLIPRLLEKLGCEVIVLNCEPTGLfpHTPE------PLpenltQLCAAVKESGADV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 239 GIALDGDADRVLLVDENGTVIDGDQLMAVIAESWaasnrLEGGGIVATVMSNLGLERFLAD----RNLTLARTKVGDRYV 314
Cdd:cd05803 237 GFAVDPDADRLALVDEDGRPIGEEYTLALAVDYV-----LKYGGRKGPVVVNLSTSRALEDiarkHGVPVFRSAVGEANV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 315 VEHMREHGFNVGGEQSGHIVLSDFATTGDGLISALQILAVAQEQNKPISDVCRKFQPVPQLLKNVRTTGGKP--LENKRV 392
Cdd:cd05803 312 VEKMKEVDAVIGGEGNGGVILPDVHYGRDSLVGIALVLQLLAASGKPLSEIVDELPQYYISKTKVTIAGEALerLLKKLE 391
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 490826587 393 KSAIDEAKERLGG------QGRLVIRPSGTEPLIRVMAEGDDR 429
Cdd:cd05803 392 AYFKDAEASTLDGlrldseDSWVHVRPSNTEPIVRIIAEAPTQ 434
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
3-134 |
6.27e-52 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 171.25 E-value: 6.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 3 RKFFGTDGIRGQANSFPMTPEIAMKVGMAVGYIFRRKGQASRVVIGKDTRRSGYMLENALVAGFTAAGMDVFLLGPIPTP 82
Cdd:pfam02878 1 RQLFGTSGIRGKVGVGELTPEFALKLGQAIASYLRAQGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTP 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 490826587 83 AVAMLCRSLRADIGVMISASHNPFYDNGIKLFGPDGFKLSDQIELQIEAMIE 134
Cdd:pfam02878 81 AVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIE 132
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
23-443 |
2.23e-45 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 163.61 E-value: 2.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 23 EIAMKVGMAVGYIFRRKGqASRVVIGKDTRRSGYMLENALVAGFTAAGMDVFLLGPIPTPAVAMLCRSLRADiGVMISAS 102
Cdd:PRK09542 17 DLVRDVGAAFARLMRAEG-ATTVVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIGLASTDQLYFASGLLDCP-GAMFTAS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 103 HNPFYDNGIKLFGPDGFKLSDQIEL-QIEAMIEGDMTPFLASHGDVGRaKRVDGDIYRYIefakRTLPRNISLNGLRVVV 181
Cdd:PRK09542 95 HNPAAYNGIKLCRAGAKPVGQDTGLaAIRDDLIAGVPAYDGPPGTVTE-RDVLADYAAFL----RSLVDLSGIRPLKVAV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 182 DCANGAGYKVAPAALWELGAEVITINNEPNGININEDCGSTHP---IGLMKKVHEVRADVGIALDGDADRVLLVDENGTV 258
Cdd:PRK09542 170 DAGNGMGGHTVPAVLGGLPITLLPLYFELDGTFPNHEANPLDPanlVDLQAFVRETGADIGLAFDGDADRCFVVDERGQP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 259 IDGDQLMAVIAESWAAsnRLEGGGIVATVMSNLGLERFLADRNLTLARTKVGDRYVVEHMREHGFNVGGEQSGHIVLSDF 338
Cdd:PRK09542 250 VSPSAVTALVAARELA--REPGATIIHNLITSRAVPELVAERGGTPVRTRVGHSFIKALMAETGAIFGGEHSAHYYFRDF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 339 ATTGDGLISALQILAVAQEQNKPISDVCRKFQPVPQLLKNVRTTGGKPLENKRVKSA----IDEAKE------RLGGQGR 408
Cdd:PRK09542 328 WGADSGMLAALHVLAALGEQDRPLSELMADYQRYAASGEINSTVADAPARMEAVLKAfadrIVSVDHldgvtvDLGDGSW 407
|
410 420 430
....*....|....*....|....*....|....*
gi 490826587 409 LVIRPSGTEPLIRVMAEGDDRGLVEKVVNDIIDVI 443
Cdd:PRK09542 408 FNLRASNTEPLLRLNVEARTEEEVDALVDEVLAII 442
|
|
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
5-443 |
2.18e-44 |
|
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: 160.88 E-value: 2.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 5 FFGTDGIRGQANsFPMTPEIAMKVGMAVGYIFRRKgqaSRVVIGKDTRRSGYMLENALVAGFTAAGMDVFLLGPIPTPAV 84
Cdd:cd05805 1 LFGGRGVSGLIN-VDITPEFATRLGAAYGSTLPPG---STVTVSRDASRASRMLKRALISGLLSTGVNVRDLGALPLPVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 85 AMLCRSLRADIGVMISASHnpfYDNG---IKLFGPDGFKLSDQIELQIE-AMIEGDMtpflashgdvgraKRVDGD---- 156
Cdd:cd05805 77 RYAIRFLGASGGIHVRTSP---DDPDkveIEFFDSRGLNISRAMERKIEnAFFREDF-------------RRAHVDeigd 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 157 ---IYRYIEFAKRTLPRNISL-----NGLRVVVDCANGAGYKVAPAALWELGAEVITIN---NEPNGININEDCGSTHPI 225
Cdd:cd05805 141 itePPDFVEYYIRGLLRALDTsglkkSGLKVVIDYAYGVAGIVLPGLLSRLGCDVVILNarlDEDAPRTDTERQRSLDRL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 226 GlmKKVHEVRADVGIALDGDADRVLLVDENGTVIDGDQLMAVIAESWAASNrlEGGGIVATVMSNLGLERFLADRNLTLA 305
Cdd:cd05805 221 G--RIVKALGADFGVIIDPNGERLILVDEAGRVISDDLLTALVSLLVLKSE--PGGTVVVPVTAPSVIEQLAERYGGRVI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 306 RTKVGDRYVVEHMREHGFNVGGEQSGHIVLSdFATTGDGLISALQILAVAQEQNKPISD---------VCRKFQPVPQLL 376
Cdd:cd05805 297 RTKTSPQALMEAALENVVLAGDGDGGFIFPE-FHPGFDAIAALVKILEMLARTNISLSQivdelprfyVLHKEVPCPWEA 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490826587 377 KN------VRTTGGKPLENkrvksaIDEAKERLGGQGRLVIrPSGTEPLIRVMAEGDDRGLVEKVVNDIIDVI 443
Cdd:cd05805 376 KGrvmrrlIEEAPDKSIEL------IDGVKIYEDDGWVLVL-PDADEPLCHIYAEGSDQERAEELTEFYVEKV 441
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
260-367 |
1.35e-43 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 148.75 E-value: 1.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 260 DGDQLMAVIAESWAASNRLEGG-GIVATVMSNLGLERFLADRNLTLARTKVGDRYVVEHMREHGFNVGGEQSGHIVLSDF 338
Cdd:pfam02880 1 DGDQILALLAKYLLEQGKLPPGaGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLDH 80
|
90 100
....*....|....*....|....*....
gi 490826587 339 ATTGDGLISALQILAVAQEQNKPISDVCR 367
Cdd:pfam02880 81 ATTKDGILAALLVLEILARTGKSLSELLE 109
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
6-441 |
1.38e-35 |
|
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: 137.25 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 6 FGTDGIRGqansfpmtpeiAMKVG-----------MAVG---YIFRRKGQAS--RVVIGKDTRRSGYmlENALVAG--FT 67
Cdd:cd05799 4 FGTAGLRG-----------KMGAGtnrmndytvrqATQGlanYLKKKGPDAKnrGVVIGYDSRHNSR--EFAELTAavLA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 68 AAGMDVFLL-GPIPTPAVAMLCRSLRADIGVMISASHNPFYDNGIKLFGPDGFKLSDQIELQIEAMIE--GDMTPFLASH 144
Cdd:cd05799 71 ANGIKVYLFdDLRPTPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIPPHDAEIAEEIEavLEPLDIKFEE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 145 G-DVGRAKRVDGDIYR-YIEFAKRTLPRNISLNG--LRVVVDCANGAGYKVAPAALWELGAEVITI---NNEPNG----- 212
Cdd:cd05799 151 AlDSGLIKYIGEEIDDaYLEAVKKLLVNPELNEGkdLKIVYTPLHGVGGKFVPRALKEAGFTNVIVveeQAEPDPdfptv 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 213 --ININEDCGSTHPIGLMKKVHevrADVGIALDGDADR----VLLVDENGTVIDGDQLMAVIAEsWAASNRLEGGG---- 282
Cdd:cd05799 231 kfPNPEEPGALDLAIELAKKVG---ADLILATDPDADRlgvaVKDKDGEWRLLTGNEIGALLAD-YLLEQRKEKGKlpkn 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 283 --IVATVMSNLGLERFLADRNLTLARTKVGDRYVVEHMRE-----HGFNVGGEQS-GHIVlSDFATTGDGLISALQILAV 354
Cdd:cd05799 307 pvIVKTIVSSELLRKIAKKYGVKVEETLTGFKWIGNKIEElesggKKFLFGFEESiGYLV-GPFVRDKDGISAAALLAEM 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 355 AQE---QNKPISDVCRkfqpvpQL----------LKNVRTTGGKPLEnkRVKSAIDEAKE-------RLGGQGRLVIRPS 414
Cdd:cd05799 386 AAYlkaQGKTLLDRLD------ELyekygyykekTISITFEGKEGPE--KIKAIMDRLRNnpnvltfYLEDGSRVTVRPS 457
|
490 500 510
....*....|....*....|....*....|
gi 490826587 415 GTEPLIRVMAE---GDDRGLVEKVVNDIID 441
Cdd:cd05799 458 GTEPKIKFYIEvvgKKTLEEAEKKLDALKK 487
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
6-428 |
2.26e-33 |
|
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: 130.78 E-value: 2.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 6 FGTDGIRGQANSfpMTPEIAMKVGMAVGYIFRRKGQASRVVIGKDTRRSGYMLENALVAGFTAAGMDVFLLGPIPTPAVA 85
Cdd:cd03088 2 FGTSGLRGLVTD--LTDEVCYAYTRAFLQHLESKFPGDTVAVGRDLRPSSPRIAAACAAALRDAGFRVVDCGAVPTPALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 86 mlCRSLRADIG-VMISASHNPFYDNGIKLFGPDGFKLSDQielqiEAMI---EGDMTPFLASHGDVGRAKRVDG-DIY-- 158
Cdd:cd03088 80 --LYAMKRGAPaIMVTGSHIPADRNGLKFYRPDGEITKAD-----EAAIlaaLVELPEALFDPAGALLPPDTDAaDAYia 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 159 RYIEFakrtLPRNiSLNGLRVVVDCANGAGYKVAPAALWELGAEVITINNEPNGININEDCGSTHPIGLMKK-VHEVRAD 237
Cdd:cd03088 153 RYTDF----FGAG-ALKGLRIGVYQHSSVGRDLLVRILEALGAEVVPLGRSDTFIPVDTEAVRPEDRALAAAwAAEHGLD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 238 VGIALDGDADRVLLVDENGTVIDGDQLMAVIAeswaasnRLEGGGIVAT-VMSNLGLErfLADRNLTLARTKVGDRYVVE 316
Cdd:cd03088 228 AIVSTDGDGDRPLVADETGEWLRGDILGLLTA-------RFLGADTVVTpVSSNSAIE--LSGFFKRVVRTRIGSPYVIA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 317 HMREH---GFN--VGGEQSGHIVL-SDFAT---------TGDGLISALQILAVAQEQNKPISDVCRKfQPVP----QLLK 377
Cdd:cd03088 299 AMAEAaaaGAGrvVGYEANGGFLLgSDIERngrtlkalpTRDAVLPILAVLAAAKEAGIPLSELVAS-LPARftasDRLQ 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 378 NVRTTGGKPLENKRVKSAIDEAKERLGGQGRLV-------------------IRPSGTEPLIRVMAEGDD 428
Cdd:cd03088 378 NFPTEKSQALIARLSADPEARAAFFFALGGEVAsidttdglrmtfangdivhLRPSGNAPELRCYVEADS 447
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
11-445 |
8.54e-29 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 117.74 E-value: 8.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 11 IRGQANSfPMTPEIAMKVGMAVGYIFRRKgqasRVVIGKDTRRSGYMLENALVAGFTAAGMDVFLLGPIPTPAVAMLCRS 90
Cdd:PRK15414 12 IRGKLGE-ELNEDIAWRIGRAYGEFLKPK----TIVLGGDVRLTSETLKLALAKGLQDAGVDVLDIGMSGTEEIYFATFH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 91 LRADIGVMISASHNPFYDNGIKLFGPDGFKLSDQIELQ-IEAMIE-GDMTPflASHGDVGRAKRVD------GDIYRYIE 162
Cdd:PRK15414 87 LGVDGGIEVTASHNPMDYNGMKLVREGARPISGDTGLRdVQRLAEaNDFPP--VDETKRGRYQQINlrdayvDHLFGYIN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 163 FAKrtlprnisLNGLRVVVDCANGAGYKVA---PAALWELGA--EVITINNEPNGININedcGSTHPI------GLMKKV 231
Cdd:PRK15414 165 VKN--------LTPLKLVINSGNGAAGPVVdaiEARFKALGApvELIKVHNTPDGNFPN---GIPNPLlpecrdDTRNAV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 232 HEVRADVGIALDGDADRVLLVDENGTVIDGDQLMAVIAESWAASNrlEGGGIVATVMSNLGLERFLADRNLTLARTKVGD 311
Cdd:PRK15414 234 IKHGADMGIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKN--PGAKIIHDPRLSWNTVDVVTAAGGTPVMSKTGH 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 312 RYVVEHMREHGFNVGGEQSGHIVLSDFATTGDGLISALQILAVaqeqnkpisdVCRKFQPVPQLLKN----------VRT 381
Cdd:PRK15414 312 AFIKERMRKEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAEL----------VCLKGKTLGELVRDrmaafpasgeINS 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490826587 382 TGGKPLEN-KRVKSAIDE---AKERLGG------QGRLVIRPSGTEPLIRVMAEG-DDRGLVEKVVNDIIDVISS 445
Cdd:PRK15414 382 KLAQPVEAiNRVEQHFSRealAVDRTDGismtfaDWRFNLRSSNTEPVVRLNVESrGDVPLMEARTRTLLTLLNE 456
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
8-332 |
1.42e-28 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 118.24 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 8 TDGIRGQAnsFPMTPEIAMKVGMAVGYIFRRKGQAS-----RVVIGKDTRRSGYMLENALVAGFTAAGMDVFLLGPIPTP 82
Cdd:PLN02371 78 VEGVEGEP--VTLTPPAVEAIGAAFAEWLLEKKKADgsgelRVSVGRDPRISGPRLADAVFAGLASAGLDVVDMGLATTP 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 83 AVAMLCRSLR--ADIGVMISASHNPFYDNGIKLFGPDGFKLSDQIE--LQIEAMIEGDMTPFL---ASHGDVGRAKRVDg 155
Cdd:PLN02371 156 AMFMSTLTERedYDAPIMITASHLPYNRNGLKFFTKDGGLGKPDIKdiLERAARIYKEWSDEGllkSSSGASSVVCRVD- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 156 diyrYIEFAKRTL----------PRNIS--LNGLRVVVDCANGAGYKVAPAALWELGAEVI-TINNEPNGININEDCGST 222
Cdd:PLN02371 235 ----FMSTYAKHLrdaikegvghPTNYEtpLEGFKIVVDAGNGAGGFFAEKVLEPLGADTSgSLFLEPDGMFPNHIPNPE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 223 HPIGL---MKKVHEVRADVGIALDGDADRVLLVDENGTVIDGDQLMAVIAeswAASNRLEGGGIVAT--VMSNlGLERFL 297
Cdd:PLN02371 311 DKAAMsatTQAVLANKADLGIIFDTDVDRSAVVDSSGREINRNRLIALMS---AIVLEEHPGTTIVTdsVTSD-GLTTFI 386
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 490826587 298 ADRNLTLARTKVGDRYVVEHMREhgFNVGGEQ-------SGH 332
Cdd:PLN02371 387 EKKGGKHHRFKRGYKNVIDKGVR--LNSDGEEthlmietSGH 426
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
95-443 |
1.39e-24 |
|
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: 106.14 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 95 IGVMISASHNPFYDNGIKLFGPDGFKL--------------SDQIELQIEAMIEG------------------------- 135
Cdd:cd03086 37 IGVMITASHNPVEDNGVKIVDPDGEMLeeswepyatqlanaSDDELLVLVLMLISvkelnidlsvpanvfvgrdtrpsgp 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 136 ------------------DM----TPFL----ASHGDVGRAKRVDGDIYrYIEFAK-----RTLPRNISLNGLRVVVDCA 184
Cdd:cd03086 117 allqalldglkalggnviDYglvtTPQLhylvRAANTEGAYGEPTEEGY-YEKLSKafnelYNLLQDGGDEPEKLVVDCA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 185 NG-AGYKVAP-AALWELGAEVITIN-NEPNGININEDCGSTH-------PIGLMKKVHEVRAdvgIALDGDADRVL--LV 252
Cdd:cd03086 196 NGvGALKLKElLKRLKKGLSVKIINdGEEGPELLNDGCGADYvktkqkpPRGFELKPPGVRC---CSFDGDADRLVyfYP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 253 DENGTV--IDGDQLMAVIA-------ESWAASNRLeGGGIVATVMSNLGLERFLADR-NLTLARTKVGDRYVveHMREHG 322
Cdd:cd03086 273 DSSNKFhlLDGDKIATLFAkfikellKKAGEELKL-TIGVVQTAYANGASTKYLEDVlKVPVVCTPTGVKHL--HHAAEE 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 323 FNVG--GEQSGH--IVLSDFA------------------------------TTGDGLISALQILAVAQEQNKPISDVCRK 368
Cdd:cd03086 350 FDIGvyFEANGHgtVLFSESAlakieensslsdeqekaaktllafsrlinqTVGDAISDMLAVELILAALGWSPQDWDNL 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 369 FQPVPQLLKNVR--------TTggkPLENKRVK-----SAIDEAKERLGGqGRLVIRPSGTEPLIRVMAEGDDRGLVEKV 435
Cdd:cd03086 430 YTDLPNRQLKVKvpdrsvikTT---DAERRLVEpkglqDKIDAIVAKYNN-GRAFVRPSGTEDVVRVYAEAATQEEADEL 505
|
....*...
gi 490826587 436 VNDIIDVI 443
Cdd:cd03086 506 ANEVAELV 513
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
95-443 |
4.11e-21 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 95.88 E-value: 4.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 95 IGVMISASHNPFYDNGIKLFGPDGFKLSDQIELQIEAM--------IEGDMTPFLASHGD-------------------- 146
Cdd:PTZ00302 77 VGVMITASHNPIQDNGVKIIDPDGGMLEESWEKICTDFanartgedLVSVLMDCLTEHGIklsnlkldlnksncskakvh 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 147 VGRAKRVDGD-----IYRYIEFAKRTLPRNI------------------------------------SLNGL-------- 177
Cdd:PTZ00302 157 VGRDTRPSSPelvsaLLRGLKLLIGSNVRNFgivttpqlhflvafanglgvdvvessdelyyayllaAFKELyrtlqegg 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 178 ----------RVVVDCANG-AGYKVAP--AALWELGAEVITINNEPNGINI-NEDCGSTH-------PIGlMKKVHEVRA 236
Cdd:PTZ00302 237 pvdltqnnskILVVDCANGvGGYKIKRffEALKQLGIEIIPININCDEEELlNDKCGADYvqktrkpPRA-MKEWPGDEE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 237 DVGIALDGDADRVL--LVDENG----TVIDGDQLMAVIAES---WAASNRLEGG---GIVATVMSNLGLERFLAD--RNL 302
Cdd:PTZ00302 316 TRVASFDGDADRLVyfFPDKDGddkwVLLDGDRIAILYAMLikkLLGKIQLKKKldiGVVQTAYANGASTNYLNEllGRL 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 303 TLARTKVGDRYVveHMREHGFNVG--GEQSGH--IVLSDFATTG---------DGLISALQILAVAQEQNKPISD----- 364
Cdd:PTZ00302 396 RVYCAPTGVKNL--HPKAHKYDIGiyFEANGHgtVLFNEKALAEwakflakqnALNSACRQLEKFLRLFNQTIGDaisdl 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 365 ------------------------VCRKFQ-PVPQllKNVRTTggKP-----LENKRVKSAIDEAKERLGGQGRLVIRPS 414
Cdd:PTZ00302 474 lavelalaflglsfqdwlnlytdlPSRQDKvTVKD--RTLITN--TEdetrlLEPKGLQDKIDAIVSKYDNAARAFIRPS 549
|
490 500
....*....|....*....|....*....
gi 490826587 415 GTEPLIRVMAEGDDRGLVEKVVNDIIDVI 443
Cdd:PTZ00302 550 GTEPVVRVYAEAPTLEQADELANEVKGLV 578
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
160-256 |
1.22e-17 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 78.10 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 160 YIEFAKRTLPRN-ISLNGLRVVVDCANGAGYKVAPAALWELGAEVITINNEPNGININedcGSTHPIG------LMKKVH 232
Cdd:pfam02879 2 YIDHLLELVDSEaLKKRGLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDPDFPT---RAPNPEEpealalLIELVK 78
|
90 100
....*....|....*....|....
gi 490826587 233 EVRADVGIALDGDADRVLLVDENG 256
Cdd:pfam02879 79 SVGADLGIATDGDADRLGVVDERG 102
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
2-441 |
2.05e-16 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 81.65 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 2 TRKFFGTDGIRG--QANSFPMTPEIAMKV--GMAVGYI--FRRKGQASRVVIGKDTRRSGYMLENALVAGFTAAGMDVFL 75
Cdd:PTZ00150 43 KRMEFGTAGLRGkmGAGFNCMNDLTVQQTaqGLCAYVIetFGQALKSRGVVIGYDGRYHSRRFAEITASVFLSKGFKVYL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 76 LGPI-PTPAVAMLCRSLRADIGVMISASHNPFYDNGIKLFGPDGFKLSDQIELQIEAMIEGDMTPFLASHGDVGRAKRVD 154
Cdd:PTZ00150 123 FGQTvPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVYWSNGAQIIPPHDKNISAKILSNLEPWSSSWEYLTETLVED 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 155 --GDIY-RYIEFAKRTLPRN-ISLNGLRVVVDCANGAGYKVAPAALWELG-AEVITI--NNEPNG-------ININEDCG 220
Cdd:PTZ00150 203 plAEVSdAYFATLKSEYNPAcCDRSKVKIVYTAMHGVGTRFVQKALHTVGlPNLLSVaqQAEPDPefptvtfPNPEEGKG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 221 SthpIGL-MKKVHEVRADVGIALDGDADRvLLVDE--NGT--VIDGDQLMAVIAesWAASNRLEGGGI-------VATVM 288
Cdd:PTZ00150 283 A---LKLsMETAEAHGSTVVLANDPDADR-LAVAEklNNGwkIFTGNELGALLA--WWAMKRYRRQGIdkskcffICTVV 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 289 SNLGLERFLADRNLTLARTKVGDRYV----VEHMREHGFNV--GGEQS-GHiVLSDFATTGDGLISALQILAVA---QEQ 358
Cdd:PTZ00150 357 SSRMLKKMAEKEGFQYDETLTGFKWIgnkaIELNAENGLTTlfAYEEAiGF-MLGTRVRDKDGVTAAAVVAEMAlylYER 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 359 NKPISD-------------------VCRKFQPVPQLLKNVRTTG-------GKPLENKR-----VKSAIDEAKERLG--- 404
Cdd:PTZ00150 436 GKTLVEhleslykqygyhftnnsyyICYDPSRIVSIFNDIRNNGsyptklgGYPVTRIRdlttgYDTATPDGKPLLPvsa 515
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 490826587 405 ----------GQGRLVIRPSGTEPLIRVMAE--GDDRGLVEKVVNDIID 441
Cdd:PTZ00150 516 stqmitfyfeNGAIITIRGSGTEPKLKWYAElsGTKDEAVEKELAALVD 564
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
64-425 |
7.43e-14 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 73.52 E-value: 7.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 64 AGF--TAAGMD--VFLLGpiptpAVAMLcRSLR--ADIGVMISASHNPFYDNGIKLFGPDGFKLSDQIE----------- 126
Cdd:PLN02895 29 AGFrtDASLLEstVFRVG-----ILAAL-RSLKtgAATGLMITASHNPVSDNGVKIVDPSGGMLPQAWEpfadalanapd 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 127 ----LQ-IEAMIEGDMTPFLA--------------SHG-------------------DVG-----------RAKRV---- 153
Cdd:PLN02895 103 pdalVQlIREFVKKENIPAVGgnppaevllgrdtrPSGpallaaalkgvraigaravDMGilttpqlhwmvRAANKgmka 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 154 -DGDIYRYIEFAKRTL----PRNISLN--GLRVVVDCANGAGY-KVAP--AALWELGAEVITINNEPNGInINEDCGS-- 221
Cdd:PLN02895 183 tESDYFEQLSSSFRALldliPNGSGDDraDDKLVVDGANGVGAeKLETlkKALGGLDLEVRNSGKEGEGV-LNEGVGAdf 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 222 -----THPIGLMKKvhevraDVGI---ALDGDADRVLLVDENGT-----VIDGDQLMAVIA-------------ESWAAS 275
Cdd:PLN02895 262 vqkekVPPTGFASK------DVGLrcaSLDGDADRLVYFYVSSAgskidLLDGDKIASLFAlfikeqlrilngnGNEKPE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 276 NRLEGGGIVATVMSNLGLERFLADR-NLTLARTKVGDRYVveHMREHGFNVG--GEQSGH--IVLSD------------F 338
Cdd:PLN02895 336 ELLVRLGVVQTAYANGASTAYLKQVlGLEVVCTPTGVKYL--HEAAAEFDIGvyFEANGHgtVLFSErfldwleaaaaeL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 339 ATTGDG---LISALQILAVAQEQNKPISDV---------------------CRKFQPVP--QLLKNVR------TTggkp 386
Cdd:PLN02895 414 SSKAKGseaHKAARRLLAVSRLINQAVGDAlsglllveailqyrgwslaewNALYQDLPsrQLKVKVAdrtaitTT---- 489
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 490826587 387 lENKRV-------KSAIDEAKERLgGQGRLVIRPSGTEPLIRVMAE 425
Cdd:PLN02895 490 -DAETVvvrpaglQDAIDAEVAKY-PRGRAFVRPSGTEDVVRVYAE 533
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
376-443 |
1.07e-13 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 65.75 E-value: 1.07e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 376 LKNVRTTGG-KPLENKRVKSAIDEAKERLGGQGR-LVIRPSGTEPLIRVMAEGDDRGLVEKVVNDIIDVI 443
Cdd:pfam00408 1 LINVRVAEKkKLAALAAILKVFADAEKILGEDGRrLDVRPSGTEPVLRVMVEGDSDEELARLADEIADLL 70
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
46-425 |
1.82e-11 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 65.93 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 46 VIGKDTRrsgYMLENALVAG---FTAAGMDVFL---LGPIPTPAV--AMLCRSLRADI---GVMISASHNPFYDNGIKLF 114
Cdd:PRK07564 80 FVGGDTH---ALSEPAIQSAlevLAANGVGVVIvgrGGYTPTPAVshAILKYNGRGGGladGIVITPSHNPPEDGGIKYN 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 115 GPDG----FKLSDQIELQIEAMIEGDM----TPFLASHGDVGRAKRVDGdIYRYIE-------FAKrtlprnISLNGLRV 179
Cdd:PRK07564 157 PPNGgpadTDVTDAIEARANELLAYGLkgvkRIPLDRALASMTVEVIDP-VADYVEdlenvfdFDA------IRKAGLRL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 180 VVDCANGAGYKVAPAALWELGAEvITINNEP-----NGIN------INEDCGSTHPI-GLMKkvHEVRADVGIALDGDAD 247
Cdd:PRK07564 230 GVDPLGGATGPYWKAIAERYGLD-LTVVNAPvdptfNFMPldddgkIRMDCSSPYAMaGLLA--LKDAFDLAFANDPDGD 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 248 RVLLVDENGTVIDGDQLmAVIAE-------SWAAsnrleGGGIVATVMSNLGLERFLADRNLTLARTKVGDRYVVEHMRE 320
Cdd:PRK07564 307 RHGIVTPGGLMNPNHYL-AVAIAylfhhrpGWRA-----GAGVGKTLVSSAMIDRVAAKLGRKLYEVPVGFKWFVNGLDD 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 321 HGFNVGGEQS-GHIVL----SDFATTGDGLISAL---QILAVAQeqnkpisdvcrkfQPVPQLLKNVRTTGGKPLENkRV 392
Cdd:PRK07564 381 GSLGFGGEESaGASFLrrdgSVWTTDKDGLIAVLlaaEILAVTG-------------KSPSEIYRELWARFGRPYYS-RH 446
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490826587 393 KS-AIDEAKERLGGQ--------------------------------------GRLVIRPSGTEPLIRVMAE 425
Cdd:PRK07564 447 DApATPEQKAALRKLspelvgatelagdpidaslteapgngaaigglkvvtenGWFAARPSGTETTYKIYAE 518
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
3-425 |
4.53e-09 |
|
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: 58.41 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 3 RKFFGTDGIRGQA--NSFPMTPEIAmkVGMAVGYIFRRKGQASRVVIGKDTRR-SGYMLENAL-VagFTAAGMDVFL--- 75
Cdd:cd05801 20 RVAFGTSGHRGSSlkGSFNEAHILA--ISQAICDYRKSQGITGPLFLGKDTHAlSEPAFISALeV--LAANGVEVIIqqn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 76 LGPIPTPAV--AMLC-----RSLRADiGVMISASHNPFYDNGIKLFGPDG----FKLSDQIELQIEAMIEGDM----TPF 140
Cdd:cd05801 96 DGYTPTPVIshAILTynrgrTEGLAD-GIVITPSHNPPEDGGFKYNPPHGgpadTDITRWIEKRANALLANGLkgvkRIP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 141 LASHGDVGRAKRVD------GDIYRYIEFAKrtlprnISLNGLRVVVDCANGAGYKVapaalWELGAEV----ITINNEP 210
Cdd:cd05801 175 LEAALASGYTHRHDfvtpyvADLGNVIDMDA------IRKSGLRLGVDPLGGASVPY-----WQPIAEKyglnLTVVNPK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 211 ------------NGiNINEDCGS----THPIGLMKKVhevraDVGIALDGDADRVLLVDENGTVIDGDQLMAViAESWAA 274
Cdd:cd05801 244 vdptfrfmtldhDG-KIRMDCSSpyamAGLLKLKDKF-----DLAFANDPDADRHGIVTPSAGLMNPNHYLSV-AIDYLF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 275 SNRLEGGGIVA---TVMSNLGLERFLADRNLTLARTKVGDRYVVEHMREHGFNVGGEQSGHIVLSDFA----TTG-DGLI 346
Cdd:cd05801 317 THRPLWNKSAGvgkTLVSSSMIDRVAAALGRKLYEVPVGFKWFVDGLLDGSLGFGGEESAGASFLRRDgtvwTTDkDGII 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 347 SAL---QILAVA-QEQNKPISDVCRKF-QPV----------PQLLKNVRTT---------GGKPLENKRVKSAIDEAKer 402
Cdd:cd05801 397 MCLlaaEILAVTgKDPGQLYQELTERFgEPYyaridapatpEQKARLKKLSpeqvtatelAGDPILAKLTRAPGNGAS-- 474
|
490 500
....*....|....*....|....*....
gi 490826587 403 LGG------QGRLVIRPSGTEPLIRVMAE 425
Cdd:cd05801 475 IGGlkvttaNGWFAARPSGTEDVYKIYAE 503
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
81-369 |
6.67e-06 |
|
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: 48.37 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 81 TPAVAMLCRSLRADIGVMISASHNPFYDN---GIKlF-----GPDGFKLSDQIELQIEAMIEGDMTPflASHGDVGRAKR 152
Cdd:cd03085 91 TPAVSAVIRKRKATGGIILTASHNPGGPEgdfGIK-YntsngGPAPESVTDKIYEITKKITEYKIAD--DPDVDLSKIGV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 153 VDGDIYR-----------YIEFAKR-----TLPRNISLNGLRVVVDCANG-AGYKVAPAALWELGA-EVITINNEPNgin 214
Cdd:cd03085 168 TKFGGKPftvevidsvedYVELMKEifdfdAIKKLLSRKGFKVRFDAMHGvTGPYAKKIFVEELGApESSVVNCTPL--- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 215 inEDCGSTHP-------IGLMKKVHEVRADVGIALDGDADRVLLVDENGTVIDGDQLmAVIAESWAASNRLEGGGI--VA 285
Cdd:cd03085 245 --PDFGGGHPdpnltyaKDLVELMKSGEPDFGAASDGDGDRNMILGKGFFVTPSDSV-AVIAANAKLIPYFYKGGLkgVA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490826587 286 TVMSNLG-LERFLADRNLTLARTKVGDRYVVEHMREHGFNVGGEQS---GhivlSDFATTGDGL---ISALQILAVaqeQ 358
Cdd:cd03085 322 RSMPTSGaLDRVAKKLGIPLFETPTGWKFFGNLMDAGKLSLCGEESfgtG----SDHIREKDGLwavLAWLSILAH---R 394
|
330
....*....|.
gi 490826587 359 NKPISDVCRKF 369
Cdd:cd03085 395 NVSVEDIVKEH 405
|
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