|
Name |
Accession |
Description |
Interval |
E-value |
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
31-543 |
0e+00 |
|
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: 757.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 31 SYGTAGFRFKSEKLPFIVFRCAYVASLRARQLNSA-IGVMITASHNPSCDNGVKLVDPSGDMLNEQWEIYATEVVNATDA 109
Cdd:cd03086 1 SYGTAGFRTKAELLDSVVFRVGILAALRSKKLGGKtIGVMITASHNPVEDNGVKIVDPDGEMLEESWEPYATQLANASDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 110 ELPAAVRALE--KQISVGKTQLSRVVCGMDTRCSGPCLMNAARAGAALFNVQFDDIGVVSTPMLHYAVKAFN-EPKFAEP 186
Cdd:cd03086 81 ELLVLVLMLIsvKELNIDLSVPANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYLVRAANtEGAYGEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 187 THDGYYSAIADSFKKLYEITEEPKDsrYQPKVIVDCANGVGAPRFRNLLERIPSsLLEVEFRNESEE----LNQGCGADF 262
Cdd:cd03086 161 TEEGYYEKLSKAFNELYNLLQDGGD--EPEKLVVDCANGVGALKLKELLKRLKK-GLSVKIINDGEEgpelLNDGCGADY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 263 VKISQKLPANFSPTAAEPKCASFDGDADRLMYFRAKASensesNDAELFDGDKIAVLIVTYIREQLKDYEnstPMERLRL 342
Cdd:cd03086 238 VKTKQKPPRGFELKPPGVRCCSFDGDADRLVYFYPDSS-----NKFHLLDGDKIATLFAKFIKELLKKAG---EELKLTI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 343 GIVQTAYANGSSTRYIREKLGIEPIIVPTGVKHLHEAASEFDIGIYFEANGHGTVVFSEIFDRIIR----RTPTESLPLR 418
Cdd:cd03086 310 GVVQTAYANGASTKYLEDVLKVPVVCTPTGVKHLHHAAEEFDIGVYFEANGHGTVLFSESALAKIEenssLSDEQEKAAK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 419 RLALFSRVINETVGDAFADLLAVEAVLRHYGWSMDDWAeKLYRDVPNVQIKVPVIDRSIFKTTNAEQTLVKPVGIQKMID 498
Cdd:cd03086 390 TLLAFSRLINQTVGDAISDMLAVELILAALGWSPQDWD-NLYTDLPNRQLKVKVPDRSVIKTTDAERRLVEPKGLQDKID 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 3876103 499 TDVAKYNNSRAFIRPSGTENIVRVYAEADTVENTLQLGKSLEQVV 543
Cdd:cd03086 469 AIVAKYNNGRAFVRPSGTEDVVRVYAEAATQEEADELANEVAELV 513
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
17-547 |
0e+00 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 587.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 17 HSGNVHAIQDDEKFSYGTAGFRFKSEKLPFIVFRCAYVASLRARQLNSAIGVMITASHNPSCDNGVKLVDPSGDMLNEQW 96
Cdd:PLN02895 11 AASSRFPPPQGVRFSYGTAGFRTDASLLESTVFRVGILAALRSLKTGAATGLMITASHNPVSDNGVKIVDPSGGMLPQAW 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 97 EIYATEVVNATDAElpAAVRALEKQI------SVGKTQLSRVVCGMDTRCSGPCLMNAARAGAALFNVQFDDIGVVSTPM 170
Cdd:PLN02895 91 EPFADALANAPDPD--ALVQLIREFVkkenipAVGGNPPAEVLLGRDTRPSGPALLAAALKGVRAIGARAVDMGILTTPQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 171 LHYAVKAFNEPkfAEPTHDGYYSAIADSFKKLYE-ITEEPKDSRYQPKVIVDCANGVGAPRFRNLLERIPSSLLEVefRN 249
Cdd:PLN02895 169 LHWMVRAANKG--MKATESDYFEQLSSSFRALLDlIPNGSGDDRADDKLVVDGANGVGAEKLETLKKALGGLDLEV--RN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 250 ESEE----LNQGCGADFVKISQKLPANFSPTAAEPKCASFDGDADRLMYFrakaSENSESNDAELFDGDKIAVLIVTYIR 325
Cdd:PLN02895 245 SGKEgegvLNEGVGADFVQKEKVPPTGFASKDVGLRCASLDGDADRLVYF----YVSSAGSKIDLLDGDKIASLFALFIK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 326 EQLK---DYENSTPME-RLRLGIVQTAYANGSSTRYIREKLGIEPIIVPTGVKHLHEAASEFDIGIYFEANGHGTVVFSE 401
Cdd:PLN02895 321 EQLRilnGNGNEKPEElLVRLGVVQTAYANGASTAYLKQVLGLEVVCTPTGVKYLHEAAAEFDIGVYFEANGHGTVLFSE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 402 IF-DRIIRRTP--------TESLP-LRRLALFSRVINETVGDAFADLLAVEAVLRHYGWSMDDWAEkLYRDVPNVQIKVP 471
Cdd:PLN02895 401 RFlDWLEAAAAelsskakgSEAHKaARRLLAVSRLINQAVGDALSGLLLVEAILQYRGWSLAEWNA-LYQDLPSRQLKVK 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3876103 472 VIDRSIFKTTNAEQTLVKPVGIQKMIDTDVAKYNNSRAFIRPSGTENIVRVYAEADTVENTLQLGKSLEQVVLNLC 547
Cdd:PLN02895 480 VADRTAITTTDAETVVVRPAGLQDAIDAEVAKYPRGRAFVRPSGTEDVVRVYAEASTQEAADSLAREVARLVYDLL 555
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
59-543 |
5.63e-30 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 122.62 E-value: 5.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 59 ARQLNSAIGVMITASHNPSCDNGVKLVDPSGdmlneqweiyatevvnatdAELPaavRALEKQIsvgktqlsrvvcgmdt 138
Cdd:COG1109 87 VRHLGADGGIMITASHNPPEYNGIKFFDADG-------------------GKLS---PEEEKEI---------------- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 139 rcsgpclmnAARAGAALFN-VQFDDIGVVSTpmlhyavkaFNEPKfaepthDGYYSAIADSFkklyeiteePKDSRYQP- 216
Cdd:COG1109 129 ---------EALIEKEDFRrAEAEEIGKVTR---------IEDVL------EAYIEALKSLV---------DEALRLRGl 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 217 KVIVDCANGVGAPRFRNLLERIPSSLLEV------EFRNESEELNQGCGADFVKISQKLPANFsptaaepkCASFDGDAD 290
Cdd:COG1109 176 KVVVDCGNGAAGGVAPRLLRELGAEVIVLnaepdgNFPNHNPNPEPENLEDLIEAVKETGADL--------GIAFDGDAD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 291 RLMYFrakasenseSNDAELFDGDKIAVLIVTYIreqLKDYENSTpmerlrlgIVQTAYANGSSTRYIrEKLGIEPIIVP 370
Cdd:COG1109 248 RLGVV---------DEKGRFLDGDQLLALLARYL---LEKGPGGT--------VVVTVMSSLALEDIA-EKHGGEVVRTK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 371 TGVKHLHEAASEFDIGIYFEANGHgtVVFSEIFdriirrtpteslplrrlalfsrvineTVGDA-FADLLAVEAVLRHyG 449
Cdd:COG1109 307 VGFKYIKEKMRETGAVLGGEESGG--IIFPDFV--------------------------PTDDGiLAALLLLELLAKQ-G 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 450 WSMDDWAEKLyRDVPNVQIKVPVIDRSIFKTTNAEqtLVKPV-GIQKMIDTDVAKY---NNSRAFIRPSGTENIVRVYAE 525
Cdd:COG1109 358 KSLSELLAEL-PRYPQPEINVRVPDEEKIGAVMEK--LREAVeDKEELDTIDGVKVdleDGGWVLVRPSGTEPLLRVYAE 434
|
490
....*....|....*...
gi 3876103 526 ADTVENTLQLGKSLEQVV 543
Cdd:COG1109 435 AKDEEEAEELLAELAELV 452
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
54-543 |
9.17e-25 |
|
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: 107.07 E-value: 9.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 54 VASLrARQLNSAIGVMITASHNPSCDNGVKLVDPSGDMLNEqweiyatevvnATDAELPAAVRalekqisvGKTQLSRVv 133
Cdd:TIGR01455 80 VAYL-TRTLRADAGVMISASHNPYEDNGIKFFGPGGFKLDD-----------ATEAAIEALLD--------EADPLPRP- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 134 cgmdtrcsgpclmNAARAGAAlfnvqfddigvvstpmlhyavkafnepKFAEPTHDGYYSAIADSFkklyeiteePKDSR 213
Cdd:TIGR01455 139 -------------ESEGLGRV---------------------------KRYPDAVGRYIEFLKSTL---------PRGLT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 214 YQP-KVIVDCANGVG---APR-FRNLLERIPSSLLEVEFRNeseeLNQGCGADFVkisQKLPANFSPTAAEPKCAsFDGD 288
Cdd:TIGR01455 170 LSGlKVVLDCANGAAykvAPHvFRELGAEVIAIGVEPDGLN----INDGCGSTHL---DALQKAVREHGADLGIA-FDGD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 289 ADRLMYFRAKasensesndAELFDGDKIAVLIVTYIRE--QLKDYenstpmerlrlGIVQTAYANGSSTRYIrEKLGIEP 366
Cdd:TIGR01455 242 ADRVLAVDAN---------GRIVDGDQILYIIARALKEsgELAGN-----------TVVATVMSNLGLERAL-EKLGLTL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 367 IIVPTGVKHLHEAASEFDIGIYFEANGHgtVVFSEIfdriirrtpteslplrrlalfsrvinETVGDAFADLLAVEAVLR 446
Cdd:TIGR01455 301 IRTAVGDRYVLEEMRESGYNLGGEQSGH--IILLDY--------------------------STTGDGIVSALQVLTIMK 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 447 HYGWSMDDWAEKLyRDVPNVQIKVPVIDRsifKTTNAEQTLVKpvgiQKMIDTDVAKYNNSRAFIRPSGTENIVRVYAEA 526
Cdd:TIGR01455 353 KSGSTLSELAAEF-VPYPQTLVNVRVADR---KLAAAEAPAVK----AAIEDAEAELGGTGRILLRPSGTEPLIRVMVEA 424
|
490
....*....|....*..
gi 3876103 527 DTVENTLQLGKSLEQVV 543
Cdd:TIGR01455 425 ADEELVQQLADTLADVV 441
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
54-102 |
2.10e-07 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 50.30 E-value: 2.10e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 3876103 54 VASLRARQLNSAIGVMITASHNPSCDNGVKLVDPSG-----DMLNEQWEIYATE 102
Cdd:pfam02878 81 AVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGgpippEVEKKIEAIIEKE 134
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
31-543 |
0e+00 |
|
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: 757.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 31 SYGTAGFRFKSEKLPFIVFRCAYVASLRARQLNSA-IGVMITASHNPSCDNGVKLVDPSGDMLNEQWEIYATEVVNATDA 109
Cdd:cd03086 1 SYGTAGFRTKAELLDSVVFRVGILAALRSKKLGGKtIGVMITASHNPVEDNGVKIVDPDGEMLEESWEPYATQLANASDD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 110 ELPAAVRALE--KQISVGKTQLSRVVCGMDTRCSGPCLMNAARAGAALFNVQFDDIGVVSTPMLHYAVKAFN-EPKFAEP 186
Cdd:cd03086 81 ELLVLVLMLIsvKELNIDLSVPANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYLVRAANtEGAYGEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 187 THDGYYSAIADSFKKLYEITEEPKDsrYQPKVIVDCANGVGAPRFRNLLERIPSsLLEVEFRNESEE----LNQGCGADF 262
Cdd:cd03086 161 TEEGYYEKLSKAFNELYNLLQDGGD--EPEKLVVDCANGVGALKLKELLKRLKK-GLSVKIINDGEEgpelLNDGCGADY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 263 VKISQKLPANFSPTAAEPKCASFDGDADRLMYFRAKASensesNDAELFDGDKIAVLIVTYIREQLKDYEnstPMERLRL 342
Cdd:cd03086 238 VKTKQKPPRGFELKPPGVRCCSFDGDADRLVYFYPDSS-----NKFHLLDGDKIATLFAKFIKELLKKAG---EELKLTI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 343 GIVQTAYANGSSTRYIREKLGIEPIIVPTGVKHLHEAASEFDIGIYFEANGHGTVVFSEIFDRIIR----RTPTESLPLR 418
Cdd:cd03086 310 GVVQTAYANGASTKYLEDVLKVPVVCTPTGVKHLHHAAEEFDIGVYFEANGHGTVLFSESALAKIEenssLSDEQEKAAK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 419 RLALFSRVINETVGDAFADLLAVEAVLRHYGWSMDDWAeKLYRDVPNVQIKVPVIDRSIFKTTNAEQTLVKPVGIQKMID 498
Cdd:cd03086 390 TLLAFSRLINQTVGDAISDMLAVELILAALGWSPQDWD-NLYTDLPNRQLKVKVPDRSVIKTTDAERRLVEPKGLQDKID 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 3876103 499 TDVAKYNNSRAFIRPSGTENIVRVYAEADTVENTLQLGKSLEQVV 543
Cdd:cd03086 469 AIVAKYNNGRAFVRPSGTEDVVRVYAEAATQEEADELANEVAELV 513
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
17-547 |
0e+00 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 587.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 17 HSGNVHAIQDDEKFSYGTAGFRFKSEKLPFIVFRCAYVASLRARQLNSAIGVMITASHNPSCDNGVKLVDPSGDMLNEQW 96
Cdd:PLN02895 11 AASSRFPPPQGVRFSYGTAGFRTDASLLESTVFRVGILAALRSLKTGAATGLMITASHNPVSDNGVKIVDPSGGMLPQAW 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 97 EIYATEVVNATDAElpAAVRALEKQI------SVGKTQLSRVVCGMDTRCSGPCLMNAARAGAALFNVQFDDIGVVSTPM 170
Cdd:PLN02895 91 EPFADALANAPDPD--ALVQLIREFVkkenipAVGGNPPAEVLLGRDTRPSGPALLAAALKGVRAIGARAVDMGILTTPQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 171 LHYAVKAFNEPkfAEPTHDGYYSAIADSFKKLYE-ITEEPKDSRYQPKVIVDCANGVGAPRFRNLLERIPSSLLEVefRN 249
Cdd:PLN02895 169 LHWMVRAANKG--MKATESDYFEQLSSSFRALLDlIPNGSGDDRADDKLVVDGANGVGAEKLETLKKALGGLDLEV--RN 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 250 ESEE----LNQGCGADFVKISQKLPANFSPTAAEPKCASFDGDADRLMYFrakaSENSESNDAELFDGDKIAVLIVTYIR 325
Cdd:PLN02895 245 SGKEgegvLNEGVGADFVQKEKVPPTGFASKDVGLRCASLDGDADRLVYF----YVSSAGSKIDLLDGDKIASLFALFIK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 326 EQLK---DYENSTPME-RLRLGIVQTAYANGSSTRYIREKLGIEPIIVPTGVKHLHEAASEFDIGIYFEANGHGTVVFSE 401
Cdd:PLN02895 321 EQLRilnGNGNEKPEElLVRLGVVQTAYANGASTAYLKQVLGLEVVCTPTGVKYLHEAAAEFDIGVYFEANGHGTVLFSE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 402 IF-DRIIRRTP--------TESLP-LRRLALFSRVINETVGDAFADLLAVEAVLRHYGWSMDDWAEkLYRDVPNVQIKVP 471
Cdd:PLN02895 401 RFlDWLEAAAAelsskakgSEAHKaARRLLAVSRLINQAVGDALSGLLLVEAILQYRGWSLAEWNA-LYQDLPSRQLKVK 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3876103 472 VIDRSIFKTTNAEQTLVKPVGIQKMIDTDVAKYNNSRAFIRPSGTENIVRVYAEADTVENTLQLGKSLEQVVLNLC 547
Cdd:PLN02895 480 VADRTAITTTDAETVVVRPAGLQDAIDAEVAKYPRGRAFVRPSGTEDVVRVYAEASTQEAADSLAREVARLVYDLL 555
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
27-550 |
3.14e-174 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 504.57 E-value: 3.14e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 27 DEKFSYGTAGFRFKSE--KLPFIVFRCAYVASLRARQLNSA--------IGVMITASHNPSCDNGVKLVDPSGDMLNEQW 96
Cdd:PTZ00302 28 ENPLTYGTAGFRTKAElpPLEPVAYRVGILAALRSFLYGGKrakrgnksVGVMITASHNPIQDNGVKIIDPDGGMLEESW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 97 EIYATEVVNATDAElpAAVRALEK------------QISVGKTQLSR--VVCGMDTRCSGPCLMNAARAG-AALFNVQFD 161
Cdd:PTZ00302 108 EKICTDFANARTGE--DLVSVLMDcltehgiklsnlKLDLNKSNCSKakVHVGRDTRPSSPELVSALLRGlKLLIGSNVR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 162 DIGVVSTPMLHYAVKAFNEPKFA--EPTHDGYYSAIADSFKKLYE-ITEEPKDSRYQ---PKVIVDCANGVGAP---RFR 232
Cdd:PTZ00302 186 NFGIVTTPQLHFLVAFANGLGVDvvESSDELYYAYLLAAFKELYRtLQEGGPVDLTQnnsKILVVDCANGVGGYkikRFF 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 233 NLLERIPSSLLEVEFRNESEE-LNQGCGADFVKISQKLPANF--SPTAAEPKCASFDGDADRLMYFRAKASENSEsndAE 309
Cdd:PTZ00302 266 EALKQLGIEIIPININCDEEElLNDKCGADYVQKTRKPPRAMkeWPGDEETRVASFDGDADRLVYFFPDKDGDDK---WV 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 310 LFDGDKIAVLIVTYIREQLkdyENSTPMERLRLGIVQTAYANGSSTRYIREKLGIEPI-IVPTGVKHLHEAASEFDIGIY 388
Cdd:PTZ00302 343 LLDGDRIAILYAMLIKKLL---GKIQLKKKLDIGVVQTAYANGASTNYLNELLGRLRVyCAPTGVKNLHPKAHKYDIGIY 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 389 FEANGHGTVVFSEifDRIIRRTPTESLP------LRRLALFSRVINETVGDAFADLLAVEAVLRHYGWSMDDWAEkLYRD 462
Cdd:PTZ00302 420 FEANGHGTVLFNE--KALAEWAKFLAKQnalnsaCRQLEKFLRLFNQTIGDAISDLLAVELALAFLGLSFQDWLN-LYTD 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 463 VPNVQIKVPVIDRSIFKTTNAEQTLVKPVGIQKMIDTDVAKYNN-SRAFIRPSGTENIVRVYAEADTVENTLQLGKSLEQ 541
Cdd:PTZ00302 497 LPSRQDKVTVKDRTLITNTEDETRLLEPKGLQDKIDAIVSKYDNaARAFIRPSGTEPVVRVYAEAPTLEQADELANEVKG 576
|
....*....
gi 3876103 542 VVLNLCNSN 550
Cdd:PTZ00302 577 LVLRYCSGA 585
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
32-543 |
1.09e-39 |
|
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: 147.89 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 32 YGTAGFRFKSEK--LPFIVFRCAYVASLRArqlnsaiGVMITASHNPSCDNGVKLVDPSGDMLNEQWEIYATEVVNATDA 109
Cdd:cd03084 2 FGTSGVRGVVGDdiTPETAVALGQAIGSTG-------GIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 110 elpaavralekqisvgktqlsrvvcgmdtrcsgpclmnaaragaalfnvqfddiGVVSTPMLHYAVKAfnepkfaEPTHD 189
Cdd:cd03084 75 ------------------------------------------------------PSAVAYELGGSVKA-------VDILQ 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 190 GYYSAIADSFKKlyEITEEPKdsryqPKVIVDCANGVGAPRFRNLLERIPSSLLEV------EFRNESEELNQGCG-ADF 262
Cdd:cd03084 94 RYFEALKKLFDV--AALSNKK-----FKVVVDSVNGVGGPIAPQLLEKLGAEVIPLncepdgNFGNINPDPGSETNlKQL 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 263 VKISQKLPANFSptaaepkcASFDGDADRLMYfrakASENSesndaELFDGDKI-AVLIVTYIREQLKdyenstpmerlR 341
Cdd:cd03084 167 LAVVKAEKADFG--------VAFDGDADRLIV----VDENG-----GFLDGDELlALLAVELFLTFNP-----------R 218
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 342 LGIVQTAYANGSSTRYIrEKLGIEPIIVPTGVKHLHEAASEFDIGIYFEANGHgtVVFSEIFdriirrtpteslplrrla 421
Cdd:cd03084 219 GGVVKTVVSSGALDKVA-KKLGIKVIRTKTGFKWVGEAMQEGDVVLGGEESGG--VIFPEFH------------------ 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 422 lfsrvineTVGDAFADLLAVEAVLRHYGWSMDDWAEKLYRDvPNVQIKVPvidrsifkttnaeqtlvkpvgiqkmidtdv 501
Cdd:cd03084 278 --------PGRDGISAALLLLEILANLGKSLSELFSELPRY-YYIRLKVR------------------------------ 318
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 3876103 502 akynnSRAFIRPSGTENIVRVYAEADTVENTLQLGKSLEQVV 543
Cdd:cd03084 319 -----GWVLVRASGTEPAIRIYAEADTQEDVEQIKKEARELV 355
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
59-543 |
5.63e-30 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 122.62 E-value: 5.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 59 ARQLNSAIGVMITASHNPSCDNGVKLVDPSGdmlneqweiyatevvnatdAELPaavRALEKQIsvgktqlsrvvcgmdt 138
Cdd:COG1109 87 VRHLGADGGIMITASHNPPEYNGIKFFDADG-------------------GKLS---PEEEKEI---------------- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 139 rcsgpclmnAARAGAALFN-VQFDDIGVVSTpmlhyavkaFNEPKfaepthDGYYSAIADSFkklyeiteePKDSRYQP- 216
Cdd:COG1109 129 ---------EALIEKEDFRrAEAEEIGKVTR---------IEDVL------EAYIEALKSLV---------DEALRLRGl 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 217 KVIVDCANGVGAPRFRNLLERIPSSLLEV------EFRNESEELNQGCGADFVKISQKLPANFsptaaepkCASFDGDAD 290
Cdd:COG1109 176 KVVVDCGNGAAGGVAPRLLRELGAEVIVLnaepdgNFPNHNPNPEPENLEDLIEAVKETGADL--------GIAFDGDAD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 291 RLMYFrakasenseSNDAELFDGDKIAVLIVTYIreqLKDYENSTpmerlrlgIVQTAYANGSSTRYIrEKLGIEPIIVP 370
Cdd:COG1109 248 RLGVV---------DEKGRFLDGDQLLALLARYL---LEKGPGGT--------VVVTVMSSLALEDIA-EKHGGEVVRTK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 371 TGVKHLHEAASEFDIGIYFEANGHgtVVFSEIFdriirrtpteslplrrlalfsrvineTVGDA-FADLLAVEAVLRHyG 449
Cdd:COG1109 307 VGFKYIKEKMRETGAVLGGEESGG--IIFPDFV--------------------------PTDDGiLAALLLLELLAKQ-G 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 450 WSMDDWAEKLyRDVPNVQIKVPVIDRSIFKTTNAEqtLVKPV-GIQKMIDTDVAKY---NNSRAFIRPSGTENIVRVYAE 525
Cdd:COG1109 358 KSLSELLAEL-PRYPQPEINVRVPDEEKIGAVMEK--LREAVeDKEELDTIDGVKVdleDGGWVLVRPSGTEPLLRVYAE 434
|
490
....*....|....*...
gi 3876103 526 ADTVENTLQLGKSLEQVV 543
Cdd:COG1109 435 AKDEEEAEELLAELAELV 452
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
54-543 |
9.17e-25 |
|
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: 107.07 E-value: 9.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 54 VASLrARQLNSAIGVMITASHNPSCDNGVKLVDPSGDMLNEqweiyatevvnATDAELPAAVRalekqisvGKTQLSRVv 133
Cdd:TIGR01455 80 VAYL-TRTLRADAGVMISASHNPYEDNGIKFFGPGGFKLDD-----------ATEAAIEALLD--------EADPLPRP- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 134 cgmdtrcsgpclmNAARAGAAlfnvqfddigvvstpmlhyavkafnepKFAEPTHDGYYSAIADSFkklyeiteePKDSR 213
Cdd:TIGR01455 139 -------------ESEGLGRV---------------------------KRYPDAVGRYIEFLKSTL---------PRGLT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 214 YQP-KVIVDCANGVG---APR-FRNLLERIPSSLLEVEFRNeseeLNQGCGADFVkisQKLPANFSPTAAEPKCAsFDGD 288
Cdd:TIGR01455 170 LSGlKVVLDCANGAAykvAPHvFRELGAEVIAIGVEPDGLN----INDGCGSTHL---DALQKAVREHGADLGIA-FDGD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 289 ADRLMYFRAKasensesndAELFDGDKIAVLIVTYIRE--QLKDYenstpmerlrlGIVQTAYANGSSTRYIrEKLGIEP 366
Cdd:TIGR01455 242 ADRVLAVDAN---------GRIVDGDQILYIIARALKEsgELAGN-----------TVVATVMSNLGLERAL-EKLGLTL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 367 IIVPTGVKHLHEAASEFDIGIYFEANGHgtVVFSEIfdriirrtpteslplrrlalfsrvinETVGDAFADLLAVEAVLR 446
Cdd:TIGR01455 301 IRTAVGDRYVLEEMRESGYNLGGEQSGH--IILLDY--------------------------STTGDGIVSALQVLTIMK 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 447 HYGWSMDDWAEKLyRDVPNVQIKVPVIDRsifKTTNAEQTLVKpvgiQKMIDTDVAKYNNSRAFIRPSGTENIVRVYAEA 526
Cdd:TIGR01455 353 KSGSTLSELAAEF-VPYPQTLVNVRVADR---KLAAAEAPAVK----AAIEDAEAELGGTGRILLRPSGTEPLIRVMVEA 424
|
490
....*....|....*..
gi 3876103 527 DTVENTLQLGKSLEQVV 543
Cdd:TIGR01455 425 ADEELVQQLADTLADVV 441
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
54-539 |
4.65e-20 |
|
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: 92.93 E-value: 4.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 54 VASLrARQLNSAIGVMITASHNPSCDNGVKLVDPSGDMLNEQWEiyatevvnatdaelpaavRALEKQISVGKTQLSrvv 133
Cdd:cd05802 79 VAYL-TRKLRADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVE------------------EEIEALIDKELELPP--- 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 134 cgmdtrcsgpclmnaaragaalfnvQFDDIGVVstpmlHYAVKAFNEpkfaepthdgYYSAIADSFkklyeiteePKDSR 213
Cdd:cd05802 137 -------------------------TGEKIGRV-----YRIDDARGR----------YIEFLKSTF---------PKDLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 214 YQPKVIVDCANGVG---APR-FRNLleripssLLEVEF-------RNeseeLNQGCGAdfvkisqklpanfspTAAEPKC 282
Cdd:cd05802 168 SGLKIVLDCANGAAykvAPEvFREL-------GAEVIVinnapdgLN----INVNCGS---------------THPESLQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 283 A-----------SFDGDADRLMyfrakASEnsesNDAELFDGDKIAVLIVTYIREQLKDYENstpmerlrlGIVQTAYAN 351
Cdd:cd05802 222 KavlengadlgiAFDGDADRVI-----AVD----EKGNIVDGDQILAICARDLKERGRLKGN---------TVVGTVMSN 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 352 GSSTRYIREkLGIEPIIVPTGVKHLHEA--ASEFDIGiyFEANGHgtVVFSEifdriirrtpteslplrrlalfsrviNE 429
Cdd:cd05802 284 LGLEKALKE-LGIKLVRTKVGDRYVLEEmlKHGANLG--GEQSGH--IIFLD--------------------------HS 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 430 TVGDAFADLLAVEAVLRHYGWSMDDWAEKLyRDVPNVQIKVPVIDRSIFKTTNAEQTLVKpvGIQKMIDtdvakyNNSRA 509
Cdd:cd05802 333 TTGDGLLTALQLLAIMKRSGKSLSELASDM-KLYPQVLVNVRVKDKKALLENPRVQAAIA--EAEKELG------GEGRV 403
|
490 500 510
....*....|....*....|....*....|
gi 3876103 510 FIRPSGTENIVRVYAEADTVENTLQLGKSL 539
Cdd:cd05802 404 LVRPSGTEPLIRVMVEGEDEELVEKLAEEL 433
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
130-530 |
5.68e-16 |
|
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: 80.31 E-value: 5.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 130 SRVVCGMDTRCSGPCLMNAARAGAALFNVQFDDIGVVSTPMLHYAVKAFNEP----------------KFAEPthDGY-- 191
Cdd:cd03087 34 GTVVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDIGIVPTPALQYAVRKLGDAgvmitashnppeyngiKLVNP--DGTef 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 192 --------------------------YSAIADSFKKLYE---ITEEPKDSRYQPKVIVDCANGVGA---PRFRNLLERIP 239
Cdd:cd03087 112 sreqeeeieeiifserfrrvawdevgSVRREDSAIDEYIeaiLDKVDIDGGKGLKVVVDCGNGAGSlttPYLLRELGCKV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 240 SSL---LEVEF--RNeSEELNQGCGaDFVKISQKLPANFSptaaepkcASFDGDADRLMYFrakasenseSNDAELFDGD 314
Cdd:cd03087 192 ITLnanPDGFFpgRP-PEPTPENLS-ELMELVRATGADLG--------IAHDGDADRAVFV---------DEKGRFIDGD 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 315 KIAVLIVTYIREQLKdyenstpmerlrlGIVQTAYANGSSTRYIREKLGIEPIIVPTGVKHLHEAASEFDIGIYFEANGh 394
Cdd:cd03087 253 KLLALLAKYLLEEGG-------------GKVVTPVDASMLVEDVVEEAGGEVIRTPVGDVHVAEEMIENGAVFGGEPNG- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 395 gTVVFSEifdriirrtpteslplrrlalFSRVINetvGdAFADLLAVEAVLRHYGWSmddwaeKLYRDVP---NVQIKVP 471
Cdd:cd03087 319 -GWIFPD---------------------HQLCRD---G-IMTAALLLELLAEEKPLS------ELLDELPkypLLREKVE 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3876103 472 VidrsifKTTNAEQTL-----VKPVGIQKMIDTDVAK--YNNSRAFIRPSGTENIVRVYAEADTVE 530
Cdd:cd03087 367 C------PDEKKEEVMeaveeELSDADEDVDTIDGVRieYEDGWVLIRPSGTEPKIRITAEAKTEE 426
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
130-543 |
3.30e-15 |
|
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: 77.94 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 130 SRVVCGMDTRCSGPCLMNAARAGAALFNVQFDDIGVVSTPMLHYAVKAFN------------------------------ 179
Cdd:TIGR03990 36 GKVVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLGIAPTPTLQYAVRELGadggimitashnppeyngikllnsdgtels 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 180 ------------EPKFAEPTHDG------YYSAIADSFKKLYEITEEPKDSRYQPKVIVDCANGVGA---PRfrnLLERI 238
Cdd:TIGR03990 116 reqeeeieeiaeSGDFERADWDEigtvtsDEDAIDDYIEAILDKVDVEAIRKKGFKVVVDCGNGAGSlttPY---LLREL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 239 PSSLLEVEF--------RNeSEELNQGCGaDFVKISQKLPANFSptaaepkcASFDGDADRLMYFrakasenseSNDAEL 310
Cdd:TIGR03990 193 GCKVITLNCqpdgtfpgRN-PEPTPENLK-DLSALVKATGADLG--------IAHDGDADRLVFI---------DEKGRF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 311 FDGDKIAVLIVTYIREQLKDyenstpmerlrlgivqTAYANGSSTRYIRE---KLGIEPIIVPTGVKHLHEAASEFDIGI 387
Cdd:TIGR03990 254 IGGDYTLALFAKYLLEHGGG----------------KVVTNVSSSRAVEDvaeRHGGEVIRTKVGEVNVAEKMKEEGAVF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 388 YFEANGHgtVVFSEIfdriirrtpteslplrrlaLFSRvinetvgDAFADLLAVEAVLRHYGWSMDDwaekLYRDVP--- 464
Cdd:TIGR03990 318 GGEGNGG--WIFPDH-------------------HYCR-------DGLMAAALFLELLAEEGKPLSE----LLAELPkyp 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 465 NVQIKVPVIDRSifkttnaEQTLVKPVGIQ----KMIDTDVAK--YNNSRAFIRPSGTENIVRVYAEADTVENTLQLGKS 538
Cdd:TIGR03990 366 MSKEKVELPDED-------KEEVMEAVEEEfadaEIDTIDGVRidFEDGWVLVRPSGTEPIVRIYAEAKTEERAEELLEE 438
|
....*
gi 3876103 539 LEQVV 543
Cdd:TIGR03990 439 GRSLV 443
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
116-530 |
4.30e-10 |
|
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: 61.76 E-value: 4.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 116 RALEKQIsvGKTQLSRVVCGMDTRCSGPCLMNA-----ARAGAALFnvqfdDIGVVSTPMLHYAVKAF------------ 178
Cdd:cd03089 25 RAFGSWL--LEKGAKKVVVGRDGRLSSPELAAAlieglLAAGCDVI-----DIGLVPTPVLYFATFHLdadggvmitash 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 179 NEP-----KFAepTHDG--YYSAIadsfKKLYEITEEPKD---------------SRYQ------------P-KVIVDCA 223
Cdd:cd03089 98 NPPeyngfKIV--IGGGplSGEDI----QALRERAEKGDFaaatgrgsvekvdilPDYIdrllsdiklgkrPlKVVVDAG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 224 NGVGAPRFRNLLERIpssllevefrneseelnqgcGADFVKISQKLPANFS-----PTaaEPKC---------------- 282
Cdd:cd03089 172 NGAAGPIAPQLLEAL--------------------GCEVIPLFCEPDGTFPnhhpdPT--DPENledliaavkengadlg 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 283 ASFDGDADRLMYFrakasenseSNDAELFDGDKIAVLIVTYIreqLKDYENSTpmerlrlgIVqtayANGSSTRYIRE-- 360
Cdd:cd03089 230 IAFDGDGDRLGVV---------DEKGEIIWGDRLLALFARDI---LKRNPGAT--------IV----YDVKCSRNLYDfi 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 361 -KLGIEPIIVPTGVKHLHEAASEFDIGIYFEANGHgtVVFSEIF----DRIIrrtptesLPLRRLALFSRViNETVGDAF 435
Cdd:cd03089 286 eEAGGKPIMWKTGHSFIKAKMKETGALLAGEMSGH--IFFKDRWygfdDGIY-------AALRLLELLSKS-GKTLSELL 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 436 ADLLAVEAvlrhygwsmddwAEKLYRDVPNvQIKVPVIDRsifkttnAEQTLVKPVGiqKMIDTDVAK--YNNSRAFIRP 513
Cdd:cd03089 356 ADLPKYFS------------TPEIRIPVTE-EDKFAVIER-------LKEHFEFPGA--EIIDIDGVRvdFEDGWGLVRA 413
|
490
....*....|....*..
gi 3876103 514 SGTENIVRVYAEADTVE 530
Cdd:cd03089 414 SNTEPVLVLRFEADTEE 430
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
54-539 |
3.50e-09 |
|
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: 59.10 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 54 VASLRARQLNSAIGVMITASHNPSCDNGVKLVDPSGDmlneqweiyatevvnatdAELPAAVRALEKQISVGktqlsrvv 133
Cdd:cd05800 81 AVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGG------------------SALPEITAAIEARLASG-------- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 134 cgmdtrcsGPCLMNAARAGAAlfnVQFDdigvvstpmlhyavkafnePKfaepthDGYYSAIAD--SFKKLYEiteepkd 211
Cdd:cd05800 135 --------EPPGLEARAEGLI---ETID-------------------PK------PDYLEALRSlvDLEAIRE------- 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 212 srYQPKVIVDCANGVGaprfRNLLERipssLLEvEFRNESEELNQGCGADFVKIS-QKLPANFSPTAAEPK------CAS 284
Cdd:cd05800 172 --AGLKVVVDPMYGAG----AGYLEE----LLR-GAGVDVEEIRAERDPLFGGIPpEPIEKNLGELAEAVKeggadlGLA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 285 FDGDADRLmyfrAKASEnsesnDAELFDGDKIAVLIVTYIREQLKdyenstpmerLRLGIVQTAyangSSTRYIR---EK 361
Cdd:cd05800 241 TDGDADRI----GAVDE-----KGNFLDPNQILALLLDYLLENKG----------LRGPVVKTV----STTHLIDriaEK 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 362 LGIEPIIVPTGVKHLHEAASEFDI--------GIYFEanGHgtvvfseifdriirrtptesLPLRrlalfsrvinetvgD 433
Cdd:cd05800 298 HGLPVYETPVGFKYIAEKMLEEDVliggeesgGLGIR--GH--------------------IPER--------------D 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 434 A-FADLLAVEAVLRhYGWSMDDWAEKLY----------RDVP-NVQIKVPVIDRsifkTTNAEQTLVKPVGIQKMIDTDV 501
Cdd:cd05800 342 GiLAGLLLLEAVAK-TGKPLSELVAELEeeygpsyydrIDLRlTPAQKEAILEK----LKNEPPLSIAGGKVDEVNTIDG 416
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 3876103 502 AKY---NNSRAFIRPSGTENIVRVYAEA---DTVENTLQLGKSL 539
Cdd:cd05800 417 VKLvleDGSWLLIRPSGTEPLLRIYAEApspEKVEALLDAGKKL 460
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
60-530 |
1.03e-07 |
|
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: 54.24 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 60 RQLNSAIGVMITASHNPSCDNGVKLVDPSGdmlneqweiyatEVVNATDAELpaavralekqisvgktqlsrvvcgmdtr 139
Cdd:cd05803 84 RQSQASGGIIITASHNPPQWNGLKFIGPDG------------EFLTPDEGEE---------------------------- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 140 csgpcLMNAARAGAALFnVQFDDIGVVstpmlhyavkAFNEPKFAEptHdgyysaIADSFKKLYEITEEPKDSRYqpKVI 219
Cdd:cd05803 124 -----VLSCAEAGSAQK-AGYDQLGEV----------TFSEDAIAE--H------IDKVLALVDVDVIKIRERNF--KVA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 220 VDCANGVGAPRFRNLLERipsslLEVEFrnesEELNQGCGADFVKISQKLPANFSPTAA---EPKC-ASF--DGDADRLM 293
Cdd:cd05803 178 VDSVNGAGGLLIPRLLEK-----LGCEV----IVLNCEPTGLFPHTPEPLPENLTQLCAavkESGAdVGFavDPDADRLA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 294 yfrakasensesndaeLFDGDKIA-------VLIVTYIreqLKDYENSTPmerlrlgIVqtayANGSSTR---YIREKLG 363
Cdd:cd05803 249 ----------------LVDEDGRPigeeytlALAVDYV---LKYGGRKGP-------VV----VNLSTSRaleDIARKHG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 364 IEPIIVPTGVKHLHEAASEFDIGIYFEANghGTVVFSEIfdRIIRRTPTES-LPLRRLALFSRVINETVGDAFAdllave 442
Cdd:cd05803 299 VPVFRSAVGEANVVEKMKEVDAVIGGEGN--GGVILPDV--HYGRDSLVGIaLVLQLLAASGKPLSEIVDELPQ------ 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 443 avlrhygWSMddwaeklyrdvpnVQIKVPVIDRS---IFKTTNAEQtlvkpvgIQKMIDT-DVAKYNNSRAFI--RPSGT 516
Cdd:cd05803 369 -------YYI-------------SKTKVTIAGEAlerLLKKLEAYF-------KDAEASTlDGLRLDSEDSWVhvRPSNT 421
|
490
....*....|....
gi 3876103 517 ENIVRVYAEADTVE 530
Cdd:cd05803 422 EPIVRIIAEAPTQD 435
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
54-102 |
2.10e-07 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 50.30 E-value: 2.10e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 3876103 54 VASLRARQLNSAIGVMITASHNPSCDNGVKLVDPSG-----DMLNEQWEIYATE 102
Cdd:pfam02878 81 AVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGgpippEVEKKIEAIIEKE 134
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
60-526 |
3.87e-07 |
|
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: 52.51 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 60 RQLNSAIGVMITASHNPSCDNGVKLVDPSGdmlneqweiyaTEVVNATDAELPAAVRALEKqisvgktqlsrvvcgmdtr 139
Cdd:cd05799 93 RHLGADAGIMITASHNPKEYNGYKVYWEDG-----------AQIIPPHDAEIAEEIEAVLE------------------- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 140 csgpclmnaaragaaLFNVQFDDIgvVSTPMLHYavkafnepkFAEPTHDGYYSAIadsfKKLYEITEEPKDSryQPKVI 219
Cdd:cd05799 143 ---------------PLDIKFEEA--LDSGLIKY---------IGEEIDDAYLEAV----KKLLVNPELNEGK--DLKIV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 220 VDCANGVGAPRFRNLLERipsslleVEFRNeseelnqgcgADFVKiSQKLP-ANFsPTAA----EPKCA---SF------ 285
Cdd:cd05799 191 YTPLHGVGGKFVPRALKE-------AGFTN----------VIVVE-EQAEPdPDF-PTVKfpnpEEPGAldlAIelakkv 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 286 --------DGDADRLMyfrakASENSESNDAELFDGDKIAVLIVTYIREQLKdyENSTPMERLRlgIVQTAYangsSTRY 357
Cdd:cd05799 252 gadlilatDPDADRLG-----VAVKDKDGEWRLLTGNEIGALLADYLLEQRK--EKGKLPKNPV--IVKTIV----SSEL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 358 IR---EKLGIEPIIVPTGVKHLHEAASEFDigiyfeaNGHGTVVFSeiFDriirrtptESLPlrrlALFSRVINETvgDA 434
Cdd:cd05799 319 LRkiaKKYGVKVEETLTGFKWIGNKIEELE-------SGGKKFLFG--FE--------ESIG----YLVGPFVRDK--DG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 435 F-ADLLAVEAVLRHY--GWSMDDWAEKLYRDV-----PNVQIKVPVIDrsifkttNAEQtlvkpvgIQKMIDT-----DV 501
Cdd:cd05799 376 IsAAALLAEMAAYLKaqGKTLLDRLDELYEKYgyykeKTISITFEGKE-------GPEK-------IKAIMDRlrnnpNV 441
|
490 500
....*....|....*....|....*...
gi 3876103 502 AKY---NNSRAFIRPSGTENIVRVYAEA 526
Cdd:cd05799 442 LTFyleDGSRVTVRPSGTEPKIKFYIEV 469
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
60-547 |
4.10e-07 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 52.45 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 60 RQLNSAIGVMITASHNPSCDNGVKLVDPSGDMLNEQWEiyatEVVNAtdaelpaavrALEKQISV------GKTqlSRVV 133
Cdd:PRK10887 86 RTLRAEAGIVISASHNPYYDNGIKFFSADGTKLPDEVE----LAIEA----------ELDKPLTCvesaelGKA--SRIN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 134 cgmdtrcsgpclmnaaragaalfnvqfDDIGvvstpmlHYAvkafnepKFAEPTHDGYYsaiadSFKKLyeiteepkdsr 213
Cdd:PRK10887 150 ---------------------------DAAG-------RYI-------EFCKSTFPNEL-----SLRGL----------- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 214 yqpKVIVDCANGVG---APR-FRNLLERIpsslleVEFRNESEEL--NQGCGA-DFVKISQKLPANfsptAAEPKCAsFD 286
Cdd:PRK10887 173 ---KIVVDCANGATyhiAPNvFRELGAEV------IAIGCEPNGLniNDECGAtDPEALQAAVLAE----KADLGIA-FD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 287 GDADRLMYFRAKasensesndAELFDGDKIAVLIVtyiREQLKdyenstpMERLRLGIVQTAYANGSSTRYIREkLGIEP 366
Cdd:PRK10887 239 GDGDRVIMVDHL---------GNLVDGDQLLYIIA---RDRLR-------RGQLRGGVVGTLMSNMGLELALKQ-LGIPF 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 367 IIVPTGVKHLHEAASEFDIGIYFEANGHgtVVfseIFDRiirrtpteslplrrlalfsrvinETVGDAFADLLAVEAVLR 446
Cdd:PRK10887 299 VRAKVGDRYVLEKLQEKGWRLGGENSGH--IL---CLDK-----------------------TTTGDGIVAALQVLAAMV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 447 HYGWSMDDWAEKLyRDVPNVQIKVPVIDRSIFKTTNAEqtlVKpvGIQKMIDTDVAkyNNSRAFIRPSGTENIVRVYAEA 526
Cdd:PRK10887 351 RSGMSLADLCSGM-KLFPQVLINVRFKPGADDPLESEA---VK--AALAEVEAELG--GRGRVLLRKSGTEPLIRVMVEG 422
|
490 500
....*....|....*....|.
gi 3876103 527 DTVENTLQLGKSLEQVVLNLC 547
Cdd:PRK10887 423 EDEAQVTALAERIADAVKAAA 443
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
130-179 |
8.09e-07 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 48.37 E-value: 8.09e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 3876103 130 SRVVCGMDTRCSGPCLMNAARAGAALFNVQFDDIGVVSTPMLHYAVKAFN 179
Cdd:pfam02878 41 GKVVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTPAVSFATRKLK 90
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
60-83 |
1.30e-04 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 44.67 E-value: 1.30e-04
10 20
....*....|....*....|....
gi 3876103 60 RQLNSAIGVMITASHNPSCDNGVK 83
Cdd:PTZ00150 137 RKLKCLAGVMVTASHNPKEDNGYK 160
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
312-395 |
7.88e-04 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 39.35 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 312 DGDKIAVLIVTYIREQLKDYENstpmerlrLGIVQTAyangSSTRYIR---EKLGIEPIIVPTGVKHLHEAASEFDIGIY 388
Cdd:pfam02880 1 DGDQILALLAKYLLEQGKLPPG--------AGVVKTV----MSSLGLDrvaKKLGGKLVRTPVGDKYVKEKMREEGALFG 68
|
....*..
gi 3876103 389 FEANGHG 395
Cdd:pfam02880 69 GEESGHI 75
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
217-293 |
9.89e-04 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 38.81 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3876103 217 KVIVDCANGVGAPRFRNLLERIpssllevefrneseelnqgcGADFVKISQKLPANFSPTAAEPK--------------- 281
Cdd:pfam02879 21 KVVYDPLHGVGGGYLPELLKRL--------------------GCDVVEENCEPDPDFPTRAPNPEepealallielvksv 80
|
90
....*....|....*.
gi 3876103 282 ----CASFDGDADRLM 293
Cdd:pfam02879 81 gadlGIATDGDADRLG 96
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
505-530 |
1.18e-03 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 37.63 E-value: 1.18e-03
10 20
....*....|....*....|....*.
gi 3876103 505 NNSRAFIRPSGTENIVRVYAEADTVE 530
Cdd:pfam00408 32 DGRRLDVRPSGTEPVLRVMVEGDSDE 57
|
|
| |
