|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02307 |
PLN02307 |
phosphoglucomutase |
462-1057 |
0e+00 |
|
phosphoglucomutase
Pssm-ID: 177942 [Multi-domain] Cd Length: 579 Bit Score: 1051.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 462 LTSNAGLGKLKPTSVSTAPIAGQKPGTSGLRKKVAEFKKENYLNNFVQAAFDAIKASgtDISKGSLVIGGDGRYFNPEAI 541
Cdd:PLN02307 1 SSSLAAMASFKVSSVPTKPIEGQKPGTSGLRKKVKVFMQENYLANFVQALFNALPAE--KVKGATLVLGGDGRYFNKEAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 542 QILIQMGVANGVRRFWIGQDGLLSTPAVSAIIREGgpRWQKAFGAFILTASHNPGGPTEDFGIKYNCEHGEPAPERMTDE 621
Cdd:PLN02307 79 QIIIKIAAANGVRRVWVGQNGLLSTPAVSAVIRER--DGSKANGGFILTASHNPGGPEEDFGIKYNYESGQPAPESITDK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 622 IYANTTTIKSYKICKEFPNIDIGAAGHSKIMSDDgsaEVNIEVIDSTEAHVKLLKSIFDFSAIRGLLDRPDFSMVYDAMH 701
Cdd:PLN02307 157 IYGNTLTIKEYKMAEDIPDVDLSAVGVTKFGGPE---DFDVEVIDPVEDYVKLMKSIFDFELIKKLLSRPDFTFCFDAMH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 702 GVNGPYVKKVFCDILGQDLSVTLNCVPKDDFNGGHADPNLTYAKELVAVMGLNRKGEkidmgGRPIPSFGAAADGDGDRN 781
Cdd:PLN02307 234 GVTGAYAKRIFVEELGAPESSLLNCVPKEDFGGGHPDPNLTYAKELVKRMGLGKTSY-----GDEPPEFGAASDGDGDRN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 782 MILGTQFFVSPSDSLAVIVANA-DTIPFFRtqGGLKGVARSMPTSGAVDLVAKDLNYSLFETPTGWKYFGNLMDSKELfd 860
Cdd:PLN02307 309 MILGKRFFVTPSDSVAIIAANAqEAIPYFS--GGLKGVARSMPTSAALDVVAKKLNLPFFEVPTGWKFFGNLMDAGKL-- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 861 gaeytpFICGEESFGTGSDHIREKDGLWAVLAWLSILAHANTNSLS-DTLVTVEDIVKAHWAKYGRNYYSRWDFENMNAT 939
Cdd:PLN02307 385 ------SICGEESFGTGSDHIREKDGIWAVLAWLSILAHKNKDVLPgGKLVTVEDIVREHWATYGRNFYSRYDYENVDSE 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 940 KANAMMDKMRAE-TDANTGKTVGKYSIEKSDDFVYVDPVDGSVAKKQGMRFLMTDGSRIIFRLSGTAGSGATVRMYIEQY 1018
Cdd:PLN02307 459 AANKMMDHLRDLvNKSKKGIKYGVYTLAFADDFEYTDPVDGSVSSKQGIRFLFTDGSRIIFRLSGTGSAGATIRLYIEQY 538
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 219130444 1019 E--PTKIDMVASEALADLIRVALDLSDLKGFLGTEEPTVIT 1057
Cdd:PLN02307 539 EkdPSKHGRDAQEALKPLIDVALKLSKLKEFTGRSKPTVIT 579
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
474-1057 |
0e+00 |
|
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: 904.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 474 TSVSTAPIAGQKPGTSGLRKKVAEFKKENYLNNFVQAAFDAIKASgtDISKGSLVIGGDGRYFNPEAIQILIQMGVANGV 553
Cdd:cd03085 1 QTVPTKPYEGQKPGTSGLRKKVKVFQQPNYLENFVQSIFNALPPE--KLKGATLVVGGDGRYYNKEAIQIIIKIAAANGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 554 RRFWIGQDGLLSTPAVSAIIREGgprwqKAFGAFILTASHNPGGPTEDFGIKYNCEHGEPAPERMTDEIYANTTTIKSYK 633
Cdd:cd03085 79 GKVVVGQNGLLSTPAVSAVIRKR-----KATGGIILTASHNPGGPEGDFGIKYNTSNGGPAPESVTDKIYEITKKITEYK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 634 ICKEfPNIDIGAAGHSKImsDDGSAEVniEVIDSTEAHVKLLKSIFDFSAIRGLLDRPDFSMVYDAMHGVNGPYVKKVFC 713
Cdd:cd03085 154 IADD-PDVDLSKIGVTKF--GGKPFTV--EVIDSVEDYVELMKEIFDFDAIKKLLSRKGFKVRFDAMHGVTGPYAKKIFV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 714 DILGQDLSVTLNCVPKDDFNGGHADPNLTYAKELVAVMglnrkgekidmgGRPIPSFGAAADGDGDRNMILGTQFFVSPS 793
Cdd:cd03085 229 EELGAPESSVVNCTPLPDFGGGHPDPNLTYAKDLVELM------------KSGEPDFGAASDGDGDRNMILGKGFFVTPS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 794 DSLAVIVANADTIPFFRtQGGLKGVARSMPTSGAVDLVAKDLNYSLFETPTGWKYFGNLMDSKELfdgaeytpFICGEES 873
Cdd:cd03085 297 DSVAVIAANAKLIPYFY-KGGLKGVARSMPTSGALDRVAKKLGIPLFETPTGWKFFGNLMDAGKL--------SLCGEES 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 874 FGTGSDHIREKDGLWAVLAWLSILAHANtnslsdtlVTVEDIVKAHWAKYGRNYYSRWDFENMNATKANAMMDKMRA--E 951
Cdd:cd03085 368 FGTGSDHIREKDGLWAVLAWLSILAHRN--------VSVEDIVKEHWQKYGRNFYTRYDYEEVDSEAANKMMDHLRAlvS 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 952 TDANTGKTVGK-YSIEKSDDFVYVDPVDGSVAKKQGMRFLMTDGSRIIFRLSGTAGSGATVRMYIEQYE--PTKIDMVAS 1028
Cdd:cd03085 440 DLPGVGKSGDKgYKVAKADDFSYTDPVDGSVSKKQGLRIIFEDGSRIIFRLSGTGSSGATIRLYIESYEkdPSKYGLDAQ 519
|
570 580
....*....|....*....|....*....
gi 219130444 1029 EALADLIRVALDLSDLKGFLGTEEPTVIT 1057
Cdd:cd03085 520 VALKPLIEIALKLSKLKEFTGREEPTVIT 548
|
|
| UGPase_euk |
cd00897 |
Eukaryotic UGPase catalyses the synthesis of UDP-Glucose; UGPase (UDP-Glucose ... |
65-373 |
2.21e-143 |
|
Eukaryotic UGPase catalyses the synthesis of UDP-Glucose; UGPase (UDP-Glucose Pyrophosphorylase) catalyzes the reversible production of UDP-Glucose and pyrophosphate (PPi) from Glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids, glycoproteins, and proteoglycans. UGPase is found in both prokaryotes and eukaryotes. Interestingly, while the prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity. This family consists of mainly eukaryotic UTP-glucose-1-phosphate uridylyltransferases.
Pssm-ID: 132998 Cd Length: 300 Bit Score: 431.28 E-value: 2.21e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 65 LAETVVLKLNGGLGTGMGLDKAKSLLPVKGDDTFLDLTAKQVIQMRKEYGLNVKFMLMNSFSTSDDTLSFLSsKYPDLAS 144
Cdd:cd00897 1 LNKLVVLKLNGGLGTSMGCTGPKSLIEVRDGKTFLDLTVQQIEHLNKTYGVDVPLVLMNSFNTDEDTKKILK-KYAGVNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 145 EEgLEMMQNKVPKLNAETLEP-ASCESDPENEWCPPGHGDLYAALVGSGRLDALLKEGFKYMFVSNSDNLGASLDLEILT 223
Cdd:cd00897 80 DI-HTFNQSRYPRISKETLLPvPSWADSPDEEWYPPGHGDIFESLYNSGLLDTLLAQGKEYLFVSNIDNLGATVDLRILN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 224 YFAEKNVPFLMECCERTENDKKGGHLAVRksDGQLILRESAMCAEEDEDAFSDISKHRFFNTNNLWVRLDKLKEIIDRNG 303
Cdd:cd00897 159 HMVDNKAEYIMEVTDKTRADVKGGTLIQY--EGKLRLLEIAQVPKEHVDEFKSIKKFKIFNTNNLWVNLKAVKRVVEENA 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 304 gfIPLPMIKNKKTVDPKddssTPVLQLETAMGAAIECFEGASAVVVPRTRFAPVKKCSDLLLLRSDAYLL 373
Cdd:cd00897 237 --LDLEIIVNPKTVDGG----LNVIQLETAVGAAIKNFDNALGVNVPRSRFLPVKTTSDLLLVRSDLYSL 300
|
|
| UDPGP |
pfam01704 |
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ... |
39-427 |
5.62e-143 |
|
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate uridylyltransferases, EC:2.7.7.9. Also known as UDP-glucose pyrophosphorylase (UDPGP) and Glucose-1-phosphate uridylyltransferase. UTP--glucose-1-phosphate uridylyltransferase catalyzes the interconversion of MgUTP + glucose-1-phosphate and UDP-glucose + MgPPi. UDP-glucose is an important intermediate in mammalian carbohydrate interconversion involved in various metabolic roles depending on tissue type. In Dictyostelium (slime mold) mutants in this enzyme abort the development cycle. Also within the family is UDP-N-acetylglucosamine or AGX1 and two hypothetical proteins from Borrelia burgdorferi the lyme disease spirochaete Swiss:O51893 and Swiss:O51036.
Pssm-ID: 460300 Cd Length: 412 Bit Score: 434.63 E-value: 5.62e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 39 ILEDSIAPVP---QLD-KTAELDIAPNATLLAETVVLKLNGGLGTGMGLDKAKSLLPVKGDDTFLDLTAKQVIQMRKEYG 114
Cdd:pfam01704 21 IDWDKIKPPPeeeIVDyEDLQEPEEEIKELLNKLAVLKLNGGLGTSMGCVGPKSLIEVRDGLTFLDLIVQQIEHLNKKYN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 115 LNVKFMLMNSFSTSDDTLSFLSsKYPDLaSEEGLEMMQNKVPKLNAETLEPA--SCESDPEnEWCPPGHGDLYAALVGSG 192
Cdd:pfam01704 101 VDVPLVLMNSFNTDEDTKKIIR-KYKGH-KVDILTFNQSRYPRIDKDTLLPVpkSADSDEE-EWYPPGHGDLYESLYNSG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 193 RLDALLKEGFKYMFVSNSDNLGASLDLEILTYFAEKNVPFLMECCERTENDKKGGHLAvrKSDGQLILRESAMCAEEDED 272
Cdd:pfam01704 178 LLDKLLAEGKEYLFVSNIDNLGATVDLNILNYMVDNGAEFLMEVTDKTRADVKGGTLI--EYDGKLRLLEIAQVPKEHVD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 273 AFSDISKHRFFNTNNLWVRLDKLKEIIDRNGgfIPLPMIKNKKTVdpkdDSSTPVLQLETAMGAAIECFEGASAVVVPRT 352
Cdd:pfam01704 256 EFKSIKKFKIFNTNNIWINLKALKRVVEEGE--LQLEIIVNKKTL----DNGENVIQLETAVGAAIKNFKNAIGINVPRS 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219130444 353 RFAPVKKCSDLLLLRSDAYLLVDHKPVLNPACNGSAPVINLDSKLYKLVGALEEATQdGIPSLVKCDKLTIKGLV 427
Cdd:pfam01704 330 RFLPVKTTSDLLLVMSDLYVLNHGSLIMNPKRMFGTPPVVLLGDHFKKVDEFLKRFP-SIPDLLELDHLTVSGDV 403
|
|
| QRI1 |
COG4284 |
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism]; |
1-371 |
1.10e-120 |
|
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
Pssm-ID: 443425 Cd Length: 402 Bit Score: 375.76 E-value: 1.10e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 1 MPSFDPIRAKMEAGGCAPSAIAAFESTY--GSLVSGDSGMILEDSIAPVP--QLDKTAELDIAPN------ATLLAE--T 68
Cdd:COG4284 17 WDELSEAQQKMLEAQIEEIDIDVFQHLYrqLVLAEGATGLIPESDIEPAPvtDLPLTDLDEVDRDraeeagEEALRAgkV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 69 VVLKLNGGLGTGMGLDKAKSLLPVKG--DDTFLDLTAKQVIQMRKEYGLNVKFMLMNSFSTSDDTLSFLSsKYPD--LAS 144
Cdd:COG4284 97 AVILLAGGQGTRLGFDGPKGLLPVRPvkGKSLFDLIAEQVLAARRRYGVPLPLYIMTSFRTHEDTLAFLE-EHDYfgLDG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 145 EEGLEMMQNKVPKLNAEtLEPASCESDPENEWCPPGHGDLYAALVGSGRLDALLKEGFKYMFVSNSDN-LGASLDLEILT 223
Cdd:COG4284 176 LPVHFFLQGMEPALDAD-LGPVLLPADPELELCPPGHGGIYTALLASGLLDKLLERGIRYLFVSNVDNpLGAVPDPAFAG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 224 YFAEKNVPFLMECCERTENDKKGGHLAvrKSDGQLILRESAMCAEEDEDAFSDISKHRFFNTNNLWVRLDKLKEIIDRNG 303
Cdd:COG4284 255 WHAASGAPFTAKVVRRTPPDEKVGHLA--RVDGRLILREYSQLPDEEAEAFTGELRHPYGNINNHWFDLDFLKRLLDERG 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 219130444 304 GfiPLPMIKNKKTVDPKDD----SSTPVLQLETAMGAAIECFEGASAVVVPR-TRFAPVKKCSDllllrSDAY 371
Cdd:COG4284 333 L--GLPLHRAEKKVDPLDEsgkpTSPNVIKFETFMFDAIPLFDGAVAIEVDReERFAPVKNTNG-----SDSP 398
|
|
| PLN02474 |
PLN02474 |
UTP--glucose-1-phosphate uridylyltransferase |
42-462 |
3.77e-84 |
|
UTP--glucose-1-phosphate uridylyltransferase
Pssm-ID: 178092 Cd Length: 469 Bit Score: 280.61 E-value: 3.77e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 42 DSIAPVPQldktaelDIAPNATLLAETVVLKLNGGLGTGMGLDKAKSLLPVKGDDTFLDLTAKQVIQMRKEYGLNVKFML 121
Cdd:PLN02474 61 DKLAPVPE-------DPEETKKLLDKLVVLKLNGGLGTTMGCTGPKSVIEVRNGLTFLDLIVIQIENLNKKYGCNVPLLL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 122 MNSFSTSDDTLSFLSsKYPDlASEEGLEMMQNKVPKLNAETLEPASCESDPENE-WCPPGHGDLYAALVGSGRLDALLKE 200
Cdd:PLN02474 134 MNSFNTHDDTQKIVE-KYTN-SNIEIHTFNQSQYPRVVADDFVPWPSKGKTDKDgWYPPGHGDVFPSLMNSGKLDALLSQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 201 GFKYMFVSNSDNLGASLDLEILTYFAEKNVPFLMECCERTENDKKGGHLAvrKSDGQLILRESAMCAEEDEDAFSDISKH 280
Cdd:PLN02474 212 GKEYVFIANSDNLGAIVDLKILNHLIQNKNEYCMEVTPKTLADVKGGTLI--SYEGKVQLLEIAQVPDEHVNEFKSIEKF 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 281 RFFNTNNLWVRLDKLKEIIDRNGgfIPLPMIKNKKTVDpkddsSTPVLQLETAMGAAIECFEGASAVVVPRTRFAPVKKC 360
Cdd:PLN02474 290 KIFNTNNLWVNLKAIKRLVEADA--LKMEIIPNPKEVD-----GVKVLQLETAAGAAIRFFDNAIGINVPRSRFLPVKAT 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 361 SDLLLLRSDAYLLVDHKPVLNPA-CNGSAPVINLDSKLYKLVGALeeATQDGIPSLVKCDKLTIKGLVRMSKKTKFVGDV 439
Cdd:PLN02474 363 SDLLLVQSDLYTLVDGFVIRNKArTNPSNPSIELGPEFKKVANFL--SRFKSIPSIVELDSLKVSGDVWFGSGIVLKGKV 440
|
410 420
....*....|....*....|...
gi 219130444 440 KIVNSSAESKFVPTGEVTGEHDL 462
Cdd:PLN02474 441 TITAKSGVKLEIPDGAVLENKDI 463
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
487-1039 |
3.75e-42 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 160.75 E-value: 3.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 487 GTSGLRKKVAEFkkenyLNNFVqaAFDAIKASGT---DISKGSLVIGGDGRYFNPE----AIQILIQMGVAngVRRFwig 559
Cdd:COG1109 8 GTDGIRGIVGEE-----LTPEF--VLKLGRAFGTylkEKGGPKVVVGRDTRLSSPMlaraLAAGLASAGID--VYDL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 560 qdGLLSTPAVSAIIREggprwQKAFGAFILTASHNPGgptEDFGIKYNCEHGEPAPERMTDEIYAntttiksykickEFP 639
Cdd:COG1109 76 --GLVPTPALAFAVRH-----LGADGGIMITASHNPP---EYNGIKFFDADGGKLSPEEEKEIEA------------LIE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 640 NIDIGAAGHSKImsddGSAEVNIEVIdstEAHVKLLKSIFDfsairGLLDRPDFSMVYDAMHGVNGPYVKKVFcDILGQD 719
Cdd:COG1109 134 KEDFRRAEAEEI----GKVTRIEDVL---EAYIEALKSLVD-----EALRLRGLKVVVDCGNGAAGGVAPRLL-RELGAE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 720 LsVTLNCVPKDDFNGGHADPNLTYAKELVAVMglnrKGEKIDmggrpipsFGAAADGDGDR-NMILGTQFFVSPsDSLAV 798
Cdd:COG1109 201 V-IVLNAEPDGNFPNHNPNPEPENLEDLIEAV----KETGAD--------LGIAFDGDADRlGVVDEKGRFLDG-DQLLA 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 799 IVANAdtipfFRTQGGLKGVARSMPTSGAVDLVAKDLNYSLFETPTGWKYFGNLMdskelfdgAEYTPFICGEESFGTG- 877
Cdd:COG1109 267 LLARY-----LLEKGPGGTVVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKM--------RETGAVLGGEESGGIIf 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 878 SDHIREKDGLWAVLAWLSILAHANTnSLSDTLvtvedivkahwAKYGRNYYSRWDFENMNATKANAMMDKMRaetdantg 957
Cdd:COG1109 334 PDFVPTDDGILAALLLLELLAKQGK-SLSELL-----------AELPRYPQPEINVRVPDEEKIGAVMEKLR-------- 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 958 ktvgkysiEKSDDFVYVDPVDgsvakkqGMRFLMTDGSRIIFRLSGTagsGATVRMYIEQYEPTKIDMVAsEALADLIRV 1037
Cdd:COG1109 394 --------EAVEDKEELDTID-------GVKVDLEDGGWVLVRPSGT---EPLLRVYAEAKDEEEAEELL-AELAELVEE 454
|
..
gi 219130444 1038 AL 1039
Cdd:COG1109 455 AL 456
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
483-633 |
1.72e-34 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 128.50 E-value: 1.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 483 GQKPGTSGLRKKV-AEFKKENYLNNFVQAAFDAIKASGTdisKGSLVIGGDGRYFNPEAIQILIQMGVANGVRRFWIGqd 561
Cdd:pfam02878 1 RQLFGTSGIRGKVgVGELTPEFALKLGQAIASYLRAQGG---GGKVVVGRDTRYSSRELARALAAGLASNGVEVILLG-- 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 219130444 562 gLLSTPAVSAIIREGgprwqKAFGAFILTASHNPGGPTedfGIKYNCEHGEPAPERMTDEIYANTTTIKSYK 633
Cdd:pfam02878 76 -LLPTPAVSFATRKL-----KADGGIMITASHNPPEYN---GIKVFDSNGGPIPPEVEKKIEAIIEKEDFYR 138
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
487-1032 |
1.82e-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: 80.25 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 487 GTSGLRKKVAEfkkenYLNnfVQAAFDAIKASGTDISKGSLVIGGDGRYFNPeaiqiLIQMGVANGVRRfwIGQD----G 562
Cdd:TIGR03990 5 GTSGIRGIVGE-----ELT--PELALKVGKAFGTYLRGGKVVVGRDTRTSGP-----MLENAVIAGLLS--TGCDvvdlG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 563 LLSTPAVSAIIReggprWQKAFGAFILTASHNPGgptEDFGIKYNCEHGEPAPERMTDEIYantttiksykickefpniD 642
Cdd:TIGR03990 71 IAPTPTLQYAVR-----ELGADGGIMITASHNPP---EYNGIKLLNSDGTELSREQEEEIE------------------E 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 643 IGAAGHSKIMSDDGSAEVnIEVIDSTEAHVKLLKSIFDFSAIRGlldrPDFSMVYDAMHGVNG---PYV-KKVFCDIlgq 718
Cdd:TIGR03990 125 IAESGDFERADWDEIGTV-TSDEDAIDDYIEAILDKVDVEAIRK----KGFKVVVDCGNGAGSlttPYLlRELGCKV--- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 719 dlsVTLNCVPKDDFNGGHADP---NLTYAKELVavmglnrKGEKIDmggrpipsFGAAADGDGDRNMIL---GTqfFVSP 792
Cdd:TIGR03990 197 ---ITLNCQPDGTFPGRNPEPtpeNLKDLSALV-------KATGAD--------LGIAHDGDADRLVFIdekGR--FIGG 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 793 SDSLAVIVANADtipffRTQGGLkgVARSMPTSGAVDLVAKDLNYSLFETPTGWKYFGNLMdsKELfdGAEYTpficGEE 872
Cdd:TIGR03990 257 DYTLALFAKYLL-----EHGGGK--VVTNVSSSRAVEDVAERHGGEVIRTKVGEVNVAEKM--KEE--GAVFG----GEG 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 873 SfgtGS----DHIREKDGLWAVLAWLSILAHANtNSLSDTLvtvedivkahwAKYGRNYYSRWDFEnMNATKANAMMDKM 948
Cdd:TIGR03990 322 N---GGwifpDHHYCRDGLMAAALFLELLAEEG-KPLSELL-----------AELPKYPMSKEKVE-LPDEDKEEVMEAV 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 949 RAE-TDANtgktvgkysieksddfvyVDPVDgsvakkqGMRFLMTDGsRIIFRLSGTAgsgATVRMYIEQYEPTKIDMVA 1027
Cdd:TIGR03990 386 EEEfADAE------------------IDTID-------GVRIDFEDG-WVLVRPSGTE---PIVRIYAEAKTEERAEELL 436
|
....*
gi 219130444 1028 SEALA 1032
Cdd:TIGR03990 437 EEGRS 441
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02307 |
PLN02307 |
phosphoglucomutase |
462-1057 |
0e+00 |
|
phosphoglucomutase
Pssm-ID: 177942 [Multi-domain] Cd Length: 579 Bit Score: 1051.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 462 LTSNAGLGKLKPTSVSTAPIAGQKPGTSGLRKKVAEFKKENYLNNFVQAAFDAIKASgtDISKGSLVIGGDGRYFNPEAI 541
Cdd:PLN02307 1 SSSLAAMASFKVSSVPTKPIEGQKPGTSGLRKKVKVFMQENYLANFVQALFNALPAE--KVKGATLVLGGDGRYFNKEAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 542 QILIQMGVANGVRRFWIGQDGLLSTPAVSAIIREGgpRWQKAFGAFILTASHNPGGPTEDFGIKYNCEHGEPAPERMTDE 621
Cdd:PLN02307 79 QIIIKIAAANGVRRVWVGQNGLLSTPAVSAVIRER--DGSKANGGFILTASHNPGGPEEDFGIKYNYESGQPAPESITDK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 622 IYANTTTIKSYKICKEFPNIDIGAAGHSKIMSDDgsaEVNIEVIDSTEAHVKLLKSIFDFSAIRGLLDRPDFSMVYDAMH 701
Cdd:PLN02307 157 IYGNTLTIKEYKMAEDIPDVDLSAVGVTKFGGPE---DFDVEVIDPVEDYVKLMKSIFDFELIKKLLSRPDFTFCFDAMH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 702 GVNGPYVKKVFCDILGQDLSVTLNCVPKDDFNGGHADPNLTYAKELVAVMGLNRKGEkidmgGRPIPSFGAAADGDGDRN 781
Cdd:PLN02307 234 GVTGAYAKRIFVEELGAPESSLLNCVPKEDFGGGHPDPNLTYAKELVKRMGLGKTSY-----GDEPPEFGAASDGDGDRN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 782 MILGTQFFVSPSDSLAVIVANA-DTIPFFRtqGGLKGVARSMPTSGAVDLVAKDLNYSLFETPTGWKYFGNLMDSKELfd 860
Cdd:PLN02307 309 MILGKRFFVTPSDSVAIIAANAqEAIPYFS--GGLKGVARSMPTSAALDVVAKKLNLPFFEVPTGWKFFGNLMDAGKL-- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 861 gaeytpFICGEESFGTGSDHIREKDGLWAVLAWLSILAHANTNSLS-DTLVTVEDIVKAHWAKYGRNYYSRWDFENMNAT 939
Cdd:PLN02307 385 ------SICGEESFGTGSDHIREKDGIWAVLAWLSILAHKNKDVLPgGKLVTVEDIVREHWATYGRNFYSRYDYENVDSE 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 940 KANAMMDKMRAE-TDANTGKTVGKYSIEKSDDFVYVDPVDGSVAKKQGMRFLMTDGSRIIFRLSGTAGSGATVRMYIEQY 1018
Cdd:PLN02307 459 AANKMMDHLRDLvNKSKKGIKYGVYTLAFADDFEYTDPVDGSVSSKQGIRFLFTDGSRIIFRLSGTGSAGATIRLYIEQY 538
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 219130444 1019 E--PTKIDMVASEALADLIRVALDLSDLKGFLGTEEPTVIT 1057
Cdd:PLN02307 539 EkdPSKHGRDAQEALKPLIDVALKLSKLKEFTGRSKPTVIT 579
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
474-1057 |
0e+00 |
|
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: 904.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 474 TSVSTAPIAGQKPGTSGLRKKVAEFKKENYLNNFVQAAFDAIKASgtDISKGSLVIGGDGRYFNPEAIQILIQMGVANGV 553
Cdd:cd03085 1 QTVPTKPYEGQKPGTSGLRKKVKVFQQPNYLENFVQSIFNALPPE--KLKGATLVVGGDGRYYNKEAIQIIIKIAAANGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 554 RRFWIGQDGLLSTPAVSAIIREGgprwqKAFGAFILTASHNPGGPTEDFGIKYNCEHGEPAPERMTDEIYANTTTIKSYK 633
Cdd:cd03085 79 GKVVVGQNGLLSTPAVSAVIRKR-----KATGGIILTASHNPGGPEGDFGIKYNTSNGGPAPESVTDKIYEITKKITEYK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 634 ICKEfPNIDIGAAGHSKImsDDGSAEVniEVIDSTEAHVKLLKSIFDFSAIRGLLDRPDFSMVYDAMHGVNGPYVKKVFC 713
Cdd:cd03085 154 IADD-PDVDLSKIGVTKF--GGKPFTV--EVIDSVEDYVELMKEIFDFDAIKKLLSRKGFKVRFDAMHGVTGPYAKKIFV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 714 DILGQDLSVTLNCVPKDDFNGGHADPNLTYAKELVAVMglnrkgekidmgGRPIPSFGAAADGDGDRNMILGTQFFVSPS 793
Cdd:cd03085 229 EELGAPESSVVNCTPLPDFGGGHPDPNLTYAKDLVELM------------KSGEPDFGAASDGDGDRNMILGKGFFVTPS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 794 DSLAVIVANADTIPFFRtQGGLKGVARSMPTSGAVDLVAKDLNYSLFETPTGWKYFGNLMDSKELfdgaeytpFICGEES 873
Cdd:cd03085 297 DSVAVIAANAKLIPYFY-KGGLKGVARSMPTSGALDRVAKKLGIPLFETPTGWKFFGNLMDAGKL--------SLCGEES 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 874 FGTGSDHIREKDGLWAVLAWLSILAHANtnslsdtlVTVEDIVKAHWAKYGRNYYSRWDFENMNATKANAMMDKMRA--E 951
Cdd:cd03085 368 FGTGSDHIREKDGLWAVLAWLSILAHRN--------VSVEDIVKEHWQKYGRNFYTRYDYEEVDSEAANKMMDHLRAlvS 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 952 TDANTGKTVGK-YSIEKSDDFVYVDPVDGSVAKKQGMRFLMTDGSRIIFRLSGTAGSGATVRMYIEQYE--PTKIDMVAS 1028
Cdd:cd03085 440 DLPGVGKSGDKgYKVAKADDFSYTDPVDGSVSKKQGLRIIFEDGSRIIFRLSGTGSSGATIRLYIESYEkdPSKYGLDAQ 519
|
570 580
....*....|....*....|....*....
gi 219130444 1029 EALADLIRVALDLSDLKGFLGTEEPTVIT 1057
Cdd:cd03085 520 VALKPLIEIALKLSKLKEFTGREEPTVIT 548
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
471-1037 |
6.15e-160 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 483.48 E-value: 6.15e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 471 LKPtsVSTAPIAGQKPGTSGLRKKVaefKKENYLNNFVQAAFDAI----KASGTDiskGSLVIGGDGRYFNPEAIQILIQ 546
Cdd:PRK07564 27 LKP--DPTNPFQDVKFGTSGHRGSS---LQPSFNENHILAIFQAIceyrGKQGIT---GPLFVGGDTHALSEPAIQSALE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 547 MGVANGVRRFWIGQDGLLSTPAVSAIIREGGPRWQKAFGAFILTASHNpggPTEDFGIKYNCEHGEPAPERMTDEIYANT 626
Cdd:PRK07564 99 VLAANGVGVVIVGRGGYTPTPAVSHAILKYNGRGGGLADGIVITPSHN---PPEDGGIKYNPPNGGPADTDVTDAIEARA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 627 TTIKSYKIcKEFPNIDIGAAGHSKimsddgsaevNIEVIDSTEAHVKLLKSIFDFSAIRGLldrpDFSMVYDAMHGVNGP 706
Cdd:PRK07564 176 NELLAYGL-KGVKRIPLDRALASM----------TVEVIDPVADYVEDLENVFDFDAIRKA----GLRLGVDPLGGATGP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 707 YVKKVFcDILGQDLSV-------TLNCVPKDDFNGGHADPNLTYAkeLVAVMGLNRKgekidmggrpiPSFGAAADGDGD 779
Cdd:PRK07564 241 YWKAIA-ERYGLDLTVvnapvdpTFNFMPLDDDGKIRMDCSSPYA--MAGLLALKDA-----------FDLAFANDPDGD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 780 RNMILGTQFFVSPSDSLAVIVANADT-IPFFRTQgglKGVARSMPTSGAVDLVAKDLNYSLFETPTGWKYFGNLmdskeL 858
Cdd:PRK07564 307 RHGIVTPGGLMNPNHYLAVAIAYLFHhRPGWRAG---AGVGKTLVSSAMIDRVAAKLGRKLYEVPVGFKWFVNG-----L 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 859 FDGaEYTpfICGEESFGT------GSDHIREKDGLWAVLAWLSILAHantnslsdTLVTVEDIVKAHWAKYGRNYYSRWD 932
Cdd:PRK07564 379 DDG-SLG--FGGEESAGAsflrrdGSVWTTDKDGLIAVLLAAEILAV--------TGKSPSEIYRELWARFGRPYYSRHD 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 933 FENMNATKAnammdKMRAETDANTGKTV--GkysieksddfvyvDPVDGSVAKKQGMRF------LMTDGSRIIFRLSGT 1004
Cdd:PRK07564 448 APATPEQKA-----ALRKLSPELVGATElaG-------------DPIDASLTEAPGNGAaigglkVVTENGWFAARPSGT 509
|
570 580 590
....*....|....*....|....*....|....*..
gi 219130444 1005 agsGATVRMYIEQYEPT----KIDMVASEALADLIRV 1037
Cdd:PRK07564 510 ---ETTYKIYAESFEGDehlhQIQKEAQEIVADLIAA 543
|
|
| UGPase_euk |
cd00897 |
Eukaryotic UGPase catalyses the synthesis of UDP-Glucose; UGPase (UDP-Glucose ... |
65-373 |
2.21e-143 |
|
Eukaryotic UGPase catalyses the synthesis of UDP-Glucose; UGPase (UDP-Glucose Pyrophosphorylase) catalyzes the reversible production of UDP-Glucose and pyrophosphate (PPi) from Glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids, glycoproteins, and proteoglycans. UGPase is found in both prokaryotes and eukaryotes. Interestingly, while the prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity. This family consists of mainly eukaryotic UTP-glucose-1-phosphate uridylyltransferases.
Pssm-ID: 132998 Cd Length: 300 Bit Score: 431.28 E-value: 2.21e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 65 LAETVVLKLNGGLGTGMGLDKAKSLLPVKGDDTFLDLTAKQVIQMRKEYGLNVKFMLMNSFSTSDDTLSFLSsKYPDLAS 144
Cdd:cd00897 1 LNKLVVLKLNGGLGTSMGCTGPKSLIEVRDGKTFLDLTVQQIEHLNKTYGVDVPLVLMNSFNTDEDTKKILK-KYAGVNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 145 EEgLEMMQNKVPKLNAETLEP-ASCESDPENEWCPPGHGDLYAALVGSGRLDALLKEGFKYMFVSNSDNLGASLDLEILT 223
Cdd:cd00897 80 DI-HTFNQSRYPRISKETLLPvPSWADSPDEEWYPPGHGDIFESLYNSGLLDTLLAQGKEYLFVSNIDNLGATVDLRILN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 224 YFAEKNVPFLMECCERTENDKKGGHLAVRksDGQLILRESAMCAEEDEDAFSDISKHRFFNTNNLWVRLDKLKEIIDRNG 303
Cdd:cd00897 159 HMVDNKAEYIMEVTDKTRADVKGGTLIQY--EGKLRLLEIAQVPKEHVDEFKSIKKFKIFNTNNLWVNLKAVKRVVEENA 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 304 gfIPLPMIKNKKTVDPKddssTPVLQLETAMGAAIECFEGASAVVVPRTRFAPVKKCSDLLLLRSDAYLL 373
Cdd:cd00897 237 --LDLEIIVNPKTVDGG----LNVIQLETAVGAAIKNFDNALGVNVPRSRFLPVKTTSDLLLVRSDLYSL 300
|
|
| UDPGP |
pfam01704 |
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate ... |
39-427 |
5.62e-143 |
|
UTP--glucose-1-phosphate uridylyltransferase; This family consists of UTP--glucose-1-phosphate uridylyltransferases, EC:2.7.7.9. Also known as UDP-glucose pyrophosphorylase (UDPGP) and Glucose-1-phosphate uridylyltransferase. UTP--glucose-1-phosphate uridylyltransferase catalyzes the interconversion of MgUTP + glucose-1-phosphate and UDP-glucose + MgPPi. UDP-glucose is an important intermediate in mammalian carbohydrate interconversion involved in various metabolic roles depending on tissue type. In Dictyostelium (slime mold) mutants in this enzyme abort the development cycle. Also within the family is UDP-N-acetylglucosamine or AGX1 and two hypothetical proteins from Borrelia burgdorferi the lyme disease spirochaete Swiss:O51893 and Swiss:O51036.
Pssm-ID: 460300 Cd Length: 412 Bit Score: 434.63 E-value: 5.62e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 39 ILEDSIAPVP---QLD-KTAELDIAPNATLLAETVVLKLNGGLGTGMGLDKAKSLLPVKGDDTFLDLTAKQVIQMRKEYG 114
Cdd:pfam01704 21 IDWDKIKPPPeeeIVDyEDLQEPEEEIKELLNKLAVLKLNGGLGTSMGCVGPKSLIEVRDGLTFLDLIVQQIEHLNKKYN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 115 LNVKFMLMNSFSTSDDTLSFLSsKYPDLaSEEGLEMMQNKVPKLNAETLEPA--SCESDPEnEWCPPGHGDLYAALVGSG 192
Cdd:pfam01704 101 VDVPLVLMNSFNTDEDTKKIIR-KYKGH-KVDILTFNQSRYPRIDKDTLLPVpkSADSDEE-EWYPPGHGDLYESLYNSG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 193 RLDALLKEGFKYMFVSNSDNLGASLDLEILTYFAEKNVPFLMECCERTENDKKGGHLAvrKSDGQLILRESAMCAEEDED 272
Cdd:pfam01704 178 LLDKLLAEGKEYLFVSNIDNLGATVDLNILNYMVDNGAEFLMEVTDKTRADVKGGTLI--EYDGKLRLLEIAQVPKEHVD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 273 AFSDISKHRFFNTNNLWVRLDKLKEIIDRNGgfIPLPMIKNKKTVdpkdDSSTPVLQLETAMGAAIECFEGASAVVVPRT 352
Cdd:pfam01704 256 EFKSIKKFKIFNTNNIWINLKALKRVVEEGE--LQLEIIVNKKTL----DNGENVIQLETAVGAAIKNFKNAIGINVPRS 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219130444 353 RFAPVKKCSDLLLLRSDAYLLVDHKPVLNPACNGSAPVINLDSKLYKLVGALEEATQdGIPSLVKCDKLTIKGLV 427
Cdd:pfam01704 330 RFLPVKTTSDLLLVMSDLYVLNHGSLIMNPKRMFGTPPVVLLGDHFKKVDEFLKRFP-SIPDLLELDHLTVSGDV 403
|
|
| QRI1 |
COG4284 |
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism]; |
1-371 |
1.10e-120 |
|
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
Pssm-ID: 443425 Cd Length: 402 Bit Score: 375.76 E-value: 1.10e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 1 MPSFDPIRAKMEAGGCAPSAIAAFESTY--GSLVSGDSGMILEDSIAPVP--QLDKTAELDIAPN------ATLLAE--T 68
Cdd:COG4284 17 WDELSEAQQKMLEAQIEEIDIDVFQHLYrqLVLAEGATGLIPESDIEPAPvtDLPLTDLDEVDRDraeeagEEALRAgkV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 69 VVLKLNGGLGTGMGLDKAKSLLPVKG--DDTFLDLTAKQVIQMRKEYGLNVKFMLMNSFSTSDDTLSFLSsKYPD--LAS 144
Cdd:COG4284 97 AVILLAGGQGTRLGFDGPKGLLPVRPvkGKSLFDLIAEQVLAARRRYGVPLPLYIMTSFRTHEDTLAFLE-EHDYfgLDG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 145 EEGLEMMQNKVPKLNAEtLEPASCESDPENEWCPPGHGDLYAALVGSGRLDALLKEGFKYMFVSNSDN-LGASLDLEILT 223
Cdd:COG4284 176 LPVHFFLQGMEPALDAD-LGPVLLPADPELELCPPGHGGIYTALLASGLLDKLLERGIRYLFVSNVDNpLGAVPDPAFAG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 224 YFAEKNVPFLMECCERTENDKKGGHLAvrKSDGQLILRESAMCAEEDEDAFSDISKHRFFNTNNLWVRLDKLKEIIDRNG 303
Cdd:COG4284 255 WHAASGAPFTAKVVRRTPPDEKVGHLA--RVDGRLILREYSQLPDEEAEAFTGELRHPYGNINNHWFDLDFLKRLLDERG 332
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 219130444 304 GfiPLPMIKNKKTVDPKDD----SSTPVLQLETAMGAAIECFEGASAVVVPR-TRFAPVKKCSDllllrSDAY 371
Cdd:COG4284 333 L--GLPLHRAEKKVDPLDEsgkpTSPNVIKFETFMFDAIPLFDGAVAIEVDReERFAPVKNTNG-----SDSP 398
|
|
| PLN02474 |
PLN02474 |
UTP--glucose-1-phosphate uridylyltransferase |
42-462 |
3.77e-84 |
|
UTP--glucose-1-phosphate uridylyltransferase
Pssm-ID: 178092 Cd Length: 469 Bit Score: 280.61 E-value: 3.77e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 42 DSIAPVPQldktaelDIAPNATLLAETVVLKLNGGLGTGMGLDKAKSLLPVKGDDTFLDLTAKQVIQMRKEYGLNVKFML 121
Cdd:PLN02474 61 DKLAPVPE-------DPEETKKLLDKLVVLKLNGGLGTTMGCTGPKSVIEVRNGLTFLDLIVIQIENLNKKYGCNVPLLL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 122 MNSFSTSDDTLSFLSsKYPDlASEEGLEMMQNKVPKLNAETLEPASCESDPENE-WCPPGHGDLYAALVGSGRLDALLKE 200
Cdd:PLN02474 134 MNSFNTHDDTQKIVE-KYTN-SNIEIHTFNQSQYPRVVADDFVPWPSKGKTDKDgWYPPGHGDVFPSLMNSGKLDALLSQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 201 GFKYMFVSNSDNLGASLDLEILTYFAEKNVPFLMECCERTENDKKGGHLAvrKSDGQLILRESAMCAEEDEDAFSDISKH 280
Cdd:PLN02474 212 GKEYVFIANSDNLGAIVDLKILNHLIQNKNEYCMEVTPKTLADVKGGTLI--SYEGKVQLLEIAQVPDEHVNEFKSIEKF 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 281 RFFNTNNLWVRLDKLKEIIDRNGgfIPLPMIKNKKTVDpkddsSTPVLQLETAMGAAIECFEGASAVVVPRTRFAPVKKC 360
Cdd:PLN02474 290 KIFNTNNLWVNLKAIKRLVEADA--LKMEIIPNPKEVD-----GVKVLQLETAAGAAIRFFDNAIGINVPRSRFLPVKAT 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 361 SDLLLLRSDAYLLVDHKPVLNPA-CNGSAPVINLDSKLYKLVGALeeATQDGIPSLVKCDKLTIKGLVRMSKKTKFVGDV 439
Cdd:PLN02474 363 SDLLLVQSDLYTLVDGFVIRNKArTNPSNPSIELGPEFKKVANFL--SRFKSIPSIVELDSLKVSGDVWFGSGIVLKGKV 440
|
410 420
....*....|....*....|...
gi 219130444 440 KIVNSSAESKFVPTGEVTGEHDL 462
Cdd:PLN02474 441 TITAKSGVKLEIPDGAVLENKDI 463
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
585-931 |
1.95e-52 |
|
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: 187.95 E-value: 1.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 585 GAFILTASHNPGgptEDFGIKYNCEHGEPAPERMTDEIYANTTTIKSYKickefpNIDIGAAGHSKimsddgsaevnieV 664
Cdd:cd03084 31 GGIMITASHNPP---EDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPS------AVAYELGGSVK-------------A 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 665 IDSTEAHVKLLKSIFDFSAIRGlldrPDFSMVYDAMHGVNGPYVKKVFcDILGQDLsVTLNCVPKDDFNGGHADPN-LTY 743
Cdd:cd03084 89 VDILQRYFEALKKLFDVAALSN----KKFKVVVDSVNGVGGPIAPQLL-EKLGAEV-IPLNCEPDGNFGNINPDPGsETN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 744 AKELVAVmglnRKGEKidmggrpiPSFGAAADGDGDRNMILG-TQFFVSPSDSLAVIVANAdtipfFRTQGGLKGVARSM 822
Cdd:cd03084 163 LKQLLAV----VKAEK--------ADFGVAFDGDADRLIVVDeNGGFLDGDELLALLAVEL-----FLTFNPRGGVVKTV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 823 PTSGAVDLVAKDLNYSLFETPTGWKYFGNLMDskelfdgaEYTPFICGEESFGTGS-DHIREKDGLWAVLAWLSILAHAN 901
Cdd:cd03084 226 VSSGALDKVAKKLGIKVIRTKTGFKWVGEAMQ--------EGDVVLGGEESGGVIFpEFHPGRDGISAALLLLEILANLG 297
|
330 340 350
....*....|....*....|....*....|
gi 219130444 902 tnslsdtlVTVEDIVKAHWAKYGRNYYSRW 931
Cdd:cd03084 298 --------KSLSELFSELPRYYYIRLKVRG 319
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
487-1004 |
1.27e-49 |
|
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: 183.14 E-value: 1.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 487 GTSGLRKKVA-EFKKENyLNNFVQAAFDAIKASGTDisKGSLVIGGDGRYFNPEAIQILIQMGVANGVRRFWIgqDGLLS 565
Cdd:cd05800 4 GTDGWRGIIAeDFTFEN-VRRVAQAIADYLKEEGGG--GRGVVVGYDTRFLSEEFARAVAEVLAANGIDVYLS--DRPVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 566 TPAVSAIIREggprwQKAFGAFILTASHNPGgptEDFGIKYNCEHGEPAPERMTDEIYANTTTIKSYKIckefPNIDIGA 645
Cdd:cd05800 79 TPAVSWAVKK-----LGAAGGVMITASHNPP---EYNGVKVKPAFGGSALPEITAAIEARLASGEPPGL----EARAEGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 646 aghskimsddgsaevnIEVIDSTEAHVKLLKSIFDFSAIRGLldrpDFSMVYDAMHGVNGPYVKKVFcDILGQDLsVTLN 725
Cdd:cd05800 147 ----------------IETIDPKPDYLEALRSLVDLEAIREA----GLKVVVDPMYGAGAGYLEELL-RGAGVDV-EEIR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 726 CVPKDDFNGGHADPNLTYAKELVAVMglnrKGEKIDMggrpipsfGAAADGDGDR-NMILGTQFFVSPSDSLAVIvanad 804
Cdd:cd05800 205 AERDPLFGGIPPEPIEKNLGELAEAV----KEGGADL--------GLATDGDADRiGAVDEKGNFLDPNQILALL----- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 805 tIPFFRTQGGLKG-VARSMPTSGAVDLVAKDLNYSLFETPTGWKYFGNLMDSKELFDGaeytpficGEESFGTG-SDHIR 882
Cdd:cd05800 268 -LDYLLENKGLRGpVVKTVSTTHLIDRIAEKHGLPVYETPVGFKYIAEKMLEEDVLIG--------GEESGGLGiRGHIP 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 883 EKDGLWAVLAWLSILAHANTnSLSDTLVTVEDivkahwaKYGRNYYSRWDFENMNATKANAMMDKMRAETDANTGKTVgk 962
Cdd:cd05800 339 ERDGILAGLLLLEAVAKTGK-PLSELVAELEE-------EYGPSYYDRIDLRLTPAQKEAILEKLKNEPPLSIAGGKV-- 408
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 219130444 963 ysieksDDFVYVDpvdgsvakkqGMRFLMTDGSRIIFRLSGT 1004
Cdd:cd05800 409 ------DEVNTID----------GVKLVLEDGSWLLIRPSGT 434
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
487-1039 |
3.75e-42 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 160.75 E-value: 3.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 487 GTSGLRKKVAEFkkenyLNNFVqaAFDAIKASGT---DISKGSLVIGGDGRYFNPE----AIQILIQMGVAngVRRFwig 559
Cdd:COG1109 8 GTDGIRGIVGEE-----LTPEF--VLKLGRAFGTylkEKGGPKVVVGRDTRLSSPMlaraLAAGLASAGID--VYDL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 560 qdGLLSTPAVSAIIREggprwQKAFGAFILTASHNPGgptEDFGIKYNCEHGEPAPERMTDEIYAntttiksykickEFP 639
Cdd:COG1109 76 --GLVPTPALAFAVRH-----LGADGGIMITASHNPP---EYNGIKFFDADGGKLSPEEEKEIEA------------LIE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 640 NIDIGAAGHSKImsddGSAEVNIEVIdstEAHVKLLKSIFDfsairGLLDRPDFSMVYDAMHGVNGPYVKKVFcDILGQD 719
Cdd:COG1109 134 KEDFRRAEAEEI----GKVTRIEDVL---EAYIEALKSLVD-----EALRLRGLKVVVDCGNGAAGGVAPRLL-RELGAE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 720 LsVTLNCVPKDDFNGGHADPNLTYAKELVAVMglnrKGEKIDmggrpipsFGAAADGDGDR-NMILGTQFFVSPsDSLAV 798
Cdd:COG1109 201 V-IVLNAEPDGNFPNHNPNPEPENLEDLIEAV----KETGAD--------LGIAFDGDADRlGVVDEKGRFLDG-DQLLA 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 799 IVANAdtipfFRTQGGLKGVARSMPTSGAVDLVAKDLNYSLFETPTGWKYFGNLMdskelfdgAEYTPFICGEESFGTG- 877
Cdd:COG1109 267 LLARY-----LLEKGPGGTVVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKM--------RETGAVLGGEESGGIIf 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 878 SDHIREKDGLWAVLAWLSILAHANTnSLSDTLvtvedivkahwAKYGRNYYSRWDFENMNATKANAMMDKMRaetdantg 957
Cdd:COG1109 334 PDFVPTDDGILAALLLLELLAKQGK-SLSELL-----------AELPRYPQPEINVRVPDEEKIGAVMEKLR-------- 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 958 ktvgkysiEKSDDFVYVDPVDgsvakkqGMRFLMTDGSRIIFRLSGTagsGATVRMYIEQYEPTKIDMVAsEALADLIRV 1037
Cdd:COG1109 394 --------EAVEDKEELDTID-------GVKVDLEDGGWVLVRPSGT---EPLLRVYAEAKDEEEAEELL-AELAELVEE 454
|
..
gi 219130444 1038 AL 1039
Cdd:COG1109 455 AL 456
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
483-633 |
1.72e-34 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 128.50 E-value: 1.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 483 GQKPGTSGLRKKV-AEFKKENYLNNFVQAAFDAIKASGTdisKGSLVIGGDGRYFNPEAIQILIQMGVANGVRRFWIGqd 561
Cdd:pfam02878 1 RQLFGTSGIRGKVgVGELTPEFALKLGQAIASYLRAQGG---GGKVVVGRDTRYSSRELARALAAGLASNGVEVILLG-- 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 219130444 562 gLLSTPAVSAIIREGgprwqKAFGAFILTASHNPGGPTedfGIKYNCEHGEPAPERMTDEIYANTTTIKSYK 633
Cdd:pfam02878 76 -LLPTPAVSFATRKL-----KADGGIMITASHNPPEYN---GIKVFDSNGGPIPPEVEKKIEAIIEKEDFYR 138
|
|
| UGPase_euk_like |
cd04180 |
Eukaryotic UGPase-like includes UDPase and UDPGlcNAc pyrophosphorylase enzymes; This family ... |
69-358 |
7.17e-33 |
|
Eukaryotic UGPase-like includes UDPase and UDPGlcNAc pyrophosphorylase enzymes; This family includes UDP-Glucose Pyrophosphorylase (UDPase) and UDPGlcNAc pyrophosphorylase enzymes. The two enzymes share significant sequence and structure similarity. UDP-Glucose Pyrophosphorylase catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from Glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans . UDP-N-acetylglucosamine (UDPGlcNAc) pyrophosphorylase (UAP) (also named GlcNAc1P uridyltransferase), catalyzes the reversible conversion of UTP and GlcNAc1P from PPi and UDPGlcNAc, which is a key precursor of N- and O-linked glycosylations and is essential for the synthesis of chitin (a major component of the fungal cell wall) and of the glycosylphosphatidylinositol (GPI) linker anchoring a variety of cell surface proteins to the plasma membrane. In bacteria, UDPGlcNAc represents an essential precursor for both peptidoglycan and lipopolysaccharide biosynthesis.
Pssm-ID: 133023 Cd Length: 266 Bit Score: 128.44 E-value: 7.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 69 VVLKLNGGLGTGMGLDKAKSLLPVKGDD--TFLDLTAKQV--IQMRKEYGLNVKFMLMNSFSTSDDTLSFLSSKypDLAS 144
Cdd:cd04180 2 AVVLLAGGLGTRLGKDGPKSSTDVGLPSgqCFLQLIGEKIltLQEIDLYSCKIPEQLMNSKYTHEKTQCYFEKI--NQKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 145 EEGLEMMQNKVPKLNAEtlEPASCESDPENEWCPPGHGDLYAALVGSGRLDALLKEGFKYMFVSNSDNLGA-SLDLEILT 223
Cdd:cd04180 80 SYVITFMQGKLPLKNDD--DARDPHNKTKCHLFPCGHGDVVLALIHSGHLNKLLEKGYRYIHFIGVDNLLVkVADPLFIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 224 YFAEKNVPFLMECCERTENDKKGGHLaVRKSDGQLILRESAMCAEE--------DEDAFSDISKHRFFNTNNLWVRLDKL 295
Cdd:cd04180 158 IAIQNRKAINQKVVPKTRNEESGGYR-IANINGRVQLLEYDQIKKLlkqkmvnnQIPKDIDDAPFFLFNTNNLINFLVEF 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 219130444 296 KEIIDrnggfiplpmiknkktvdpkddsstpvlqletamgAAIECFEGASAVVVPRT-RFAPVK 358
Cdd:cd04180 237 KDRVD-----------------------------------DIIEFTDDIVGVMVHRAeEFAPVK 265
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
487-1004 |
2.01e-28 |
|
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The mammalian PGM2 is thought to be a phosphopentomutase that catalyzes the conversion of the nucleoside breakdown products, ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. PGM2L1 is thought to catalyze the 1,3-bisphosphoglycerate-dependent synthesis of glucose 1,6-bisphosphate and other aldose-bisphosphates that serve as cofactors for several sugar phosphomutases and possibly also as regulators of glycolytic enzymes. PGM2 and PGM2L1 belong to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100092 Cd Length: 487 Bit Score: 120.69 E-value: 2.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 487 GTSGLRKKVAEfkKENYLNNFV--QAAF---DAIKASGTDISKGSLVIGGDGRYFNPE----AIQILIQMGVAngVRRFw 557
Cdd:cd05799 5 GTAGLRGKMGA--GTNRMNDYTvrQATQglaNYLKKKGPDAKNRGVVIGYDSRHNSREfaelTAAVLAANGIK--VYLF- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 558 igqDGLLSTPAVSAIIREggprwQKAFGAFILTASHNpggPTEDFGIK-YNcEHGEPAPERMTDEIYANtttIKSYKICK 636
Cdd:cd05799 80 ---DDLRPTPLLSFAVRH-----LGADAGIMITASHN---PKEYNGYKvYW-EDGAQIIPPHDAEIAEE---IEAVLEPL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 637 EFPNIDIGAAGHSKIMSDdgsaevniEVIDSTEAHVKLLksIFDFSAIRGlldrPDFSMVYDAMHGVNGPYVKKVFCDIL 716
Cdd:cd05799 145 DIKFEEALDSGLIKYIGE--------EIDDAYLEAVKKL--LVNPELNEG----KDLKIVYTPLHGVGGKFVPRALKEAG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 717 GQDL-SVTLNCVPKDDFNGGhADPN------LTYAKELvavmglnrkGEKIDmggrpiPSFGAAADGDGDRnmilgtqff 789
Cdd:cd05799 211 FTNViVVEEQAEPDPDFPTV-KFPNpeepgaLDLAIEL---------AKKVG------ADLILATDPDADR--------- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 790 vspsdsLAVIVANADT--IPF----------------FRTQGGLKG---VARSMPTSGAVDLVAKDLNYSLFETPTGWKY 848
Cdd:cd05799 266 ------LGVAVKDKDGewRLLtgneigalladylleqRKEKGKLPKnpvIVKTIVSSELLRKIAKKYGVKVEETLTGFKW 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 849 FGNLMDSkelFDGAEYTPFICGEESFG-TGSDHIREKDGLWAVLAWLSILAH--ANTNSLSDTLvtvEDIvkahWAKYG- 924
Cdd:cd05799 340 IGNKIEE---LESGGKKFLFGFEESIGyLVGPFVRDKDGISAAALLAEMAAYlkAQGKTLLDRL---DEL----YEKYGy 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 925 ---RNYYSRWDFENmNATKANAMMDKMRAETDAntgktvgkysieksddfvyvdpvdgsvakkqgMRFLMTDGSRIIFRL 1001
Cdd:cd05799 410 ykeKTISITFEGKE-GPEKIKAIMDRLRNNPNV--------------------------------LTFYLEDGSRVTVRP 456
|
...
gi 219130444 1002 SGT 1004
Cdd:cd05799 457 SGT 459
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
792-923 |
4.66e-23 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 95.21 E-value: 4.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 792 PSDSLAVIVANAdtipfFRTQGGLK---GVARSMPTSGAVDLVAKDLNYSLFETPTGWKYFGNLMDSKELfdgaeytpFI 868
Cdd:pfam02880 1 DGDQILALLAKY-----LLEQGKLPpgaGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGA--------LF 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 219130444 869 CGEESfGTGS--DHIREKDGLWAVLAWLSILAHANtnslsdtlVTVEDIVKAHWAKY 923
Cdd:pfam02880 68 GGEES-GHIIflDHATTKDGILAALLVLEILARTG--------KSLSELLEELPEKY 115
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
487-1004 |
7.06e-18 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 88.59 E-value: 7.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 487 GTSGLRKKV-AEFkkeNYLNNF--VQAAFD----AIKASGTDISKGSLVIGGDGRYFNPEAIQILIQMGVANGVRRFWIG 559
Cdd:PTZ00150 48 GTAGLRGKMgAGF---NCMNDLtvQQTAQGlcayVIETFGQALKSRGVVIGYDGRYHSRRFAEITASVFLSKGFKVYLFG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 560 QdgLLSTPAVSAIIReggprWQKAFGAFILTASHNPggpTEDFGIKYNCEHG----EPAPERMTDEIYANTTTIKSykic 635
Cdd:PTZ00150 125 Q--TVPTPFVPYAVR-----KLKCLAGVMVTASHNP---KEDNGYKVYWSNGaqiiPPHDKNISAKILSNLEPWSS---- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 636 kefPNIDIGAAGHSkimsdDGSAEVnievidsTEAHVKLLKSIFDFSAIrgllDRPDFSMVYDAMHGVNGPYVKKVFcDI 715
Cdd:PTZ00150 191 ---SWEYLTETLVE-----DPLAEV-------SDAYFATLKSEYNPACC----DRSKVKIVYTAMHGVGTRFVQKAL-HT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 716 LG--QDLSVTLNCVPKDDFngghadPNLTYAKELVAVMGLNRKGEKIDMGGRPIPsfgAAADGDGDRNMI---LGTQFFV 790
Cdd:PTZ00150 251 VGlpNLLSVAQQAEPDPEF------PTVTFPNPEEGKGALKLSMETAEAHGSTVV---LANDPDADRLAVaekLNNGWKI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 791 SPSDSLAVIVAnADTIPFFRTQGGLKGVA---RSMPTSGAVDLVAKDLNYSLFETPTGWKYFGNLmdSKELFDGAEYTPF 867
Cdd:PTZ00150 322 FTGNELGALLA-WWAMKRYRRQGIDKSKCffiCTVVSSRMLKKMAEKEGFQYDETLTGFKWIGNK--AIELNAENGLTTL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 868 ICGEESFGTG-SDHIREKDGLWAVLAW--LSILAHANTNSLSDTLVTVedivkahWAKYG----RN-YYSRWDfenmnAT 939
Cdd:PTZ00150 399 FAYEEAIGFMlGTRVRDKDGVTAAAVVaeMALYLYERGKTLVEHLESL-------YKQYGyhftNNsYYICYD-----PS 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 219130444 940 KANAMMDKMRaeTDANTGKTVGKYSIEKSDDF-VYVD-------PVDGSVAKKQGMRFLMTDGSRIIFRLSGT 1004
Cdd:PTZ00150 467 RIVSIFNDIR--NNGSYPTKLGGYPVTRIRDLtTGYDtatpdgkPLLPVSASTQMITFYFENGAIITIRGSGT 537
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
487-1032 |
1.82e-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: 80.25 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 487 GTSGLRKKVAEfkkenYLNnfVQAAFDAIKASGTDISKGSLVIGGDGRYFNPeaiqiLIQMGVANGVRRfwIGQD----G 562
Cdd:TIGR03990 5 GTSGIRGIVGE-----ELT--PELALKVGKAFGTYLRGGKVVVGRDTRTSGP-----MLENAVIAGLLS--TGCDvvdlG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 563 LLSTPAVSAIIReggprWQKAFGAFILTASHNPGgptEDFGIKYNCEHGEPAPERMTDEIYantttiksykickefpniD 642
Cdd:TIGR03990 71 IAPTPTLQYAVR-----ELGADGGIMITASHNPP---EYNGIKLLNSDGTELSREQEEEIE------------------E 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 643 IGAAGHSKIMSDDGSAEVnIEVIDSTEAHVKLLKSIFDFSAIRGlldrPDFSMVYDAMHGVNG---PYV-KKVFCDIlgq 718
Cdd:TIGR03990 125 IAESGDFERADWDEIGTV-TSDEDAIDDYIEAILDKVDVEAIRK----KGFKVVVDCGNGAGSlttPYLlRELGCKV--- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 719 dlsVTLNCVPKDDFNGGHADP---NLTYAKELVavmglnrKGEKIDmggrpipsFGAAADGDGDRNMIL---GTqfFVSP 792
Cdd:TIGR03990 197 ---ITLNCQPDGTFPGRNPEPtpeNLKDLSALV-------KATGAD--------LGIAHDGDADRLVFIdekGR--FIGG 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 793 SDSLAVIVANADtipffRTQGGLkgVARSMPTSGAVDLVAKDLNYSLFETPTGWKYFGNLMdsKELfdGAEYTpficGEE 872
Cdd:TIGR03990 257 DYTLALFAKYLL-----EHGGGK--VVTNVSSSRAVEDVAERHGGEVIRTKVGEVNVAEKM--KEE--GAVFG----GEG 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 873 SfgtGS----DHIREKDGLWAVLAWLSILAHANtNSLSDTLvtvedivkahwAKYGRNYYSRWDFEnMNATKANAMMDKM 948
Cdd:TIGR03990 322 N---GGwifpDHHYCRDGLMAAALFLELLAEEG-KPLSELL-----------AELPKYPMSKEKVE-LPDEDKEEVMEAV 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 949 RAE-TDANtgktvgkysieksddfvyVDPVDgsvakkqGMRFLMTDGsRIIFRLSGTAgsgATVRMYIEQYEPTKIDMVA 1027
Cdd:TIGR03990 386 EEEfADAE------------------IDTID-------GVRIDFEDG-WVLVRPSGTE---PIVRIYAEAKTEERAEELL 436
|
....*
gi 219130444 1028 SEALA 1032
Cdd:TIGR03990 437 EEGRS 441
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
487-1034 |
1.58e-13 |
|
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: 74.14 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 487 GTSGLRKKV-----AEFkkenylnnfvqaAFDAIKASGTDISKGSLVIGGDGRYFNPEAIQILIQMGVANGVRRFWIGqd 561
Cdd:cd03087 3 GTSGIRGVVgeeltPEL------------ALKVGKALGTYLGGGTVVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDIG-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 562 gLLSTPAVSAIIREGGPrwqkafGAFILTASHNPGgptEDFGIK-YN---CEHGEPAPERMTDEIYANTTTIKSYkicke 637
Cdd:cd03087 69 -IVPTPALQYAVRKLGD------AGVMITASHNPP---EYNGIKlVNpdgTEFSREQEEEIEEIIFSERFRRVAW----- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 638 fpnidigaaghskimSDDGSAEVNIEVIDsteAHVKLLKSIFDFSAIRGlldrpdFSMVYDAMHGVNG---PYV-KKVFC 713
Cdd:cd03087 134 ---------------DEVGSVRREDSAID---EYIEAILDKVDIDGGKG------LKVVVDCGNGAGSlttPYLlRELGC 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 714 DIlgqdlsVTLNCVPKDDFNGGHADP---NLTYAKELVAVMGlnrkgekidmggrpiPSFGAAADGDGDRNMILGTQFFV 790
Cdd:cd03087 190 KV------ITLNANPDGFFPGRPPEPtpeNLSELMELVRATG---------------ADLGIAHDGDADRAVFVDEKGRF 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 791 SPSDSLAVIVANadtipFFRTQGGLKgVARSMPTSGAVDLVAKDLNYSLFETPTGWKYFGNLMDskelfdgaEYTPFICG 870
Cdd:cd03087 249 IDGDKLLALLAK-----YLLEEGGGK-VVTPVDASMLVEDVVEEAGGEVIRTPVGDVHVAEEMI--------ENGAVFGG 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 871 EESfgtGS----DHIREKDGLWAVLAWLSILAHanTNSLSDTLvtvEDIVKAHWAKygRNYYSRWDfenmnatKANAMMD 946
Cdd:cd03087 315 EPN---GGwifpDHQLCRDGIMTAALLLELLAE--EKPLSELL---DELPKYPLLR--EKVECPDE-------KKEEVME 377
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 947 KMRAetdantgktvgkysiEKSDDFVYVDPVDgsvakkqGMRFLMTDGsRIIFRLSGTAgsgATVRMYIEQYEPTKIDMV 1026
Cdd:cd03087 378 AVEE---------------ELSDADEDVDTID-------GVRIEYEDG-WVLIRPSGTE---PKIRITAEAKTEERAKEL 431
|
....*...
gi 219130444 1027 ASEALADL 1034
Cdd:cd03087 432 LEEGRSKV 439
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
540-932 |
3.07e-13 |
|
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: 73.44 E-value: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 540 AIQILIqmgvANGVRRFWIGQDGLLSTPAVS-AII-----REGGprwqKAFGaFILTASHNPggPtEDFGIKYNCEHGEP 613
Cdd:cd05801 79 ALEVLA----ANGVEVIIQQNDGYTPTPVIShAILtynrgRTEG----LADG-IVITPSHNP--P-EDGGFKYNPPHGGP 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 614 APERMTDEI--YANtttiksyKICKEfpnidiGAAGHSKIMSDDGSAEVNIEVIDSTEAHVKLLKSIFDFSAIR--GLld 689
Cdd:cd05801 147 ADTDITRWIekRAN-------ALLAN------GLKGVKRIPLEAALASGYTHRHDFVTPYVADLGNVIDMDAIRksGL-- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 690 rpdfSMVYDAMHGVNGPYVKKVfCDILGQDLSVtLNCVPKDDFNGGHAD--------PNLTYAkelvavM-GLNRKGEKI 760
Cdd:cd05801 212 ----RLGVDPLGGASVPYWQPI-AEKYGLNLTV-VNPKVDPTFRFMTLDhdgkirmdCSSPYA------MaGLLKLKDKF 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 761 DMggrpipSFGaaADGDGDRNMIL-GTQFFVSPSDSLAVIVANadtipFFRTQGGLK---GVARSMPTSGAVDLVAKDLN 836
Cdd:cd05801 280 DL------AFA--NDPDADRHGIVtPSAGLMNPNHYLSVAIDY-----LFTHRPLWNksaGVGKTLVSSSMIDRVAAALG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 837 YSLFETPTGWKYFgnlmdSKELFDGaeyTPFICGEESFGT------GSDHIREKDGLwaVLAWLS--ILAhantnslsdt 908
Cdd:cd05801 347 RKLYEVPVGFKWF-----VDGLLDG---SLGFGGEESAGAsflrrdGTVWTTDKDGI--IMCLLAaeILA---------- 406
|
410 420
....*....|....*....|....*..
gi 219130444 909 lVTVEDIVKAH---WAKYGRNYYSRWD 932
Cdd:cd05801 407 -VTGKDPGQLYqelTERFGEPYYARID 432
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
489-845 |
4.05e-10 |
|
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: 63.48 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 489 SGLRKKVAEFKKENYLNNFVqAAFDAIKASGTdiSKGSLVIGGDGRYFNPEAIQILIQMGVANGVRrfwIGQDGLLSTPA 568
Cdd:cd05803 5 SGIRGIVGEGLTPEVITRYV-AAFATWQPERT--KGGKIVVGRDGRPSGPMLEKIVIGALLACGCD---VIDLGIAPTPT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 569 VSAIIREggprwQKAFGAFILTASHNpggPTEDFGIKYNCEHGEPAPERMTDEIYantttikSYKICKEFPnidigAAGH 648
Cdd:cd05803 79 VQVLVRQ-----SQASGGIIITASHN---PPQWNGLKFIGPDGEFLTPDEGEEVL-------SCAEAGSAQ-----KAGY 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 649 SKIMSDDGSAevnieviDSTEAHV-KLLKSIF-DFSAIRglldRPDFSMVYDAMHGVNGPYVkKVFCDILGQDLsVTLNC 726
Cdd:cd05803 139 DQLGEVTFSE-------DAIAEHIdKVLALVDvDVIKIR----ERNFKVAVDSVNGAGGLLI-PRLLEKLGCEV-IVLNC 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 727 VPKDDFngGH-ADP---NLTyakELVAVMglnrKGEKIDmggrpipsFGAAADGDGDRNMILG-TQFFVSPSDSLAVIVA 801
Cdd:cd05803 206 EPTGLF--PHtPEPlpeNLT---QLCAAV----KESGAD--------VGFAVDPDADRLALVDeDGRPIGEEYTLALAVD 268
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 219130444 802 nadtipFFRTQGGLKG-VARSMPTSGAVDLVAKDLNYSLFETPTG 845
Cdd:cd05803 269 ------YVLKYGGRKGpVVVNLSTSRALEDIARKHGVPVFRSAVG 307
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
524-780 |
4.52e-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: 63.30 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 524 KGSLVIGGDGRYFNPEAIQILIQMGVANGVRRFWIGqdgLLSTPAVS-AIIREGGPrwqkafGAFILTASHNPGgptEDF 602
Cdd:cd03089 36 AKKVVVGRDGRLSSPELAAALIEGLLAAGCDVIDIG---LVPTPVLYfATFHLDAD------GGVMITASHNPP---EYN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 603 GIKYnCEHGEPAPERMTDEIYantttiksykickefpniDIGAAGHSKIMSDDGSaevnIEVIDSTEAHVKLLKSIFDfs 682
Cdd:cd03089 104 GFKI-VIGGGPLSGEDIQALR------------------ERAEKGDFAAATGRGS----VEKVDILPDYIDRLLSDIK-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 683 airgLLDRPdFSMVYDAMHGVNGPYVKKVFcDILGQDLsVTLNCVPKDDFNGGHADP----NLTYAKELVavmglnrKGE 758
Cdd:cd03089 159 ----LGKRP-LKVVVDAGNGAAGPIAPQLL-EALGCEV-IPLFCEPDGTFPNHHPDPtdpeNLEDLIAAV-------KEN 224
|
250 260
....*....|....*....|..
gi 219130444 759 KIDmggrpipsFGAAADGDGDR 780
Cdd:cd03089 225 GAD--------LGIAFDGDGDR 238
|
|
| UGGPase |
cd06424 |
UGGPase catalyzes the synthesis of UDP-Glucose/UDP-Galactose; UGGPase: UDP-Galactose/Glucose ... |
75-325 |
1.98e-09 |
|
UGGPase catalyzes the synthesis of UDP-Glucose/UDP-Galactose; UGGPase: UDP-Galactose/Glucose Pyrophosphorylase catalyzes the reversible production of UDP-Glucose/UDP-Galactose and pyrophosphate (PPi) from Glucose-1-phosphate/Galactose-1-phosphate and UTP. Its dual substrate specificity distinguishes it from the single substrate enzyme UDP-glucose pyrophosphorylase. It may play a key role in the galactose metabolism in raffinose oligosaccharide (RFO) metabolizing plants. RFO raffinose is a major photoassimilate and is a galactosylderivative of sucrose (Suc) containing a galactose (Gal) moiety. Upon arriving at the sink tissue, the Gal moieties of the RFOs are initially removed by alpha-galactosidase and then are phosphorylated to Gal-1-P. Gal-1-P is converted to UDP-Gal. The UDP-Gal is further metabolized to UDP-Glc via an epimerase reaction. The UDP-Glc can be directly utilized in cell wall metabolism or in Suc synthesis. However, for the Suc synthesis UDP-Glc must be further metabolized to Glc-1-P. This can be carried out either by the UGPase in the reverse direction or by the dual substrate PPase itself operating in the reverse direction. According to the latter possibility, the three-step pathway of Gal-1-P to Glc-1-P could be carried out by a single PPase, functioning sequentially in reverse directions separated by the epimerase reaction.
Pssm-ID: 133046 Cd Length: 315 Bit Score: 60.16 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 75 GGLGTGMGLDKAKSLLPVK--GDDTFLDLTAKQVI----QMRKEYGLNVKFMLMNSFSTSDDTLSFLS-SKYPDLASEEG 147
Cdd:cd06424 8 GGLGERLGYSGIKIGLPVEltTNTTYLQYYLNYIRafqeASKKGEKMEIPFVIMTSDDTHSKTLKLLEeNNYFGLEKDQV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 148 LEMMQNKVPKL--NAetlepASCESDPENEWC----PPGHGDLYAALVGSGRLDALLKEGFKYMFVSNSDNLGASLDLEI 221
Cdd:cd06424 88 HILKQEKVFCLidND-----AHLALDPDNTYSiltkPHGHGDVHTLLYNSGLLKKWIEAGYKWLVFFQDTNALAFKAIPA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 222 -LTYFAEKNVPFLMECCERTENDKKGGHLAVRKSDG----------QL--ILRESAMcaeeDEDAFSDISKHRFF--NTN 286
Cdd:cd06424 163 vLGVSATKSLDMNSLTVPRKPKEAIGALCKLTKNNGksmtinveynQLdpLLRASGK----DDGDVDDKTGFSPFpgNIN 238
|
250 260 270
....*....|....*....|....*....|....*....
gi 219130444 287 NLWVRLDKLKEIIDRNGGFIPlpmiknkKTVDPKDDSST 325
Cdd:cd06424 239 QLVFSLGPYMDELEKTKGAIP-------EFINPKYKDAT 270
|
|
| UDPGlcNAc_PPase |
cd04193 |
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine ... |
67-266 |
5.68e-09 |
|
UDPGlcNAc pyrophosphorylase catalayzes the synthesis of UDPGlcNAc; UDP-N-acetylglucosamine (UDPGlcNAc) pyrophosphorylase (UAP) (also named GlcNAc1P uridyltransferase), catalyzes the reversible conversion of UTP and GlcNAc1 to PPi and UDPGlcNAc. UDP-N-acetylglucosamine (UDPGlcNAc), the activated form of GlcNAc, is a key precursor of N- and O-linked glycosylations. It is essential for the synthesis of chitin (a major component of the fungal cell wall) and of the glycosylphosphatidylinositol (GPI) linker which anchors a variety of cell surface proteins to the plasma membrane. In bacteria, UDPGlcNAc represents an essential precursor for both peptidoglycan and lipopolysaccharide biosynthesis. Human UAP has two isoforms, resulting from alternative splicing of a single gene and differing by the presence or absence of 17 amino acids. UDPGlcNAc pyrophosphorylase shares significant sequence and structure conservation with UDPglucose pyrophosphorylase.
Pssm-ID: 133036 Cd Length: 323 Bit Score: 58.77 E-value: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 67 ETVVLKLNGGLGTGMGLDKAKSLLPVKG--DDTFLDLTAKQVIQMRKEYGLN------VKFMLMNSFSTSDDTLSFLSS- 137
Cdd:cd04193 15 KVAVLLLAGGQGTRLGFDGPKGMFPVGLpsKKSLFQLQAERILKLQELAGEAsgkkvpIPWYIMTSEATHEETRKFFKEn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 138 KYPDLASEEGLEMMQNKVPKLNAE---TLEPAS--CESdpenewcPPGHGDLYAALVGSGRLDALLKEGFKYMFVSNSDN 212
Cdd:cd04193 95 NYFGLDPEQVHFFQQGMLPCVDFDgkiLLEEKGkiAMA-------PNGNGGLYKALQTAGILEDMKKRGIKYIHVYSVDN 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219130444 213 -LGASLDLEILTYFAEKNVPFLMECCERTENDKK-------GGHLAV-------------RKSDGQLILRESAMC 266
Cdd:cd04193 168 iLVKVADPVFIGFCISKGADVGAKVVRKRYPTEKvgvvvlvDGKPQVveyseisdelaekRDADGELQYNAGNIA 242
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
670-783 |
7.41e-09 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 54.22 E-value: 7.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 670 AHVKLLKSIFDFSAIRGLldrpDFSMVYDAMHGVNGPYVKKVfCDILGQDLsVTLNCVPKDDFNGGHADP----NLTYAK 745
Cdd:pfam02879 1 AYIDHLLELVDSEALKKR----GLKVVYDPLHGVGGGYLPEL-LKRLGCDV-VEENCEPDPDFPTRAPNPeepeALALLI 74
|
90 100 110
....*....|....*....|....*....|....*...
gi 219130444 746 ELVavmglnrKGEKIDmggrpipsFGAAADGDGDRNMI 783
Cdd:pfam02879 75 ELV-------KSVGAD--------LGIATDGDADRLGV 97
|
|
| PTZ00339 |
PTZ00339 |
UDP-N-acetylglucosamine pyrophosphorylase; Provisional |
67-213 |
5.38e-08 |
|
UDP-N-acetylglucosamine pyrophosphorylase; Provisional
Pssm-ID: 240368 Cd Length: 482 Bit Score: 56.67 E-value: 5.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 67 ETVVLKLNGGLGTGMGLDKAKSLL---PVKGdDTFLDLTAKQVIQMrKEY---------GLNVKFMLMNSFSTSDDTLSF 134
Cdd:PTZ00339 106 EVAVLILAGGLGTRLGSDKPKGLLectPVKK-KTLFQFHCEKVRRL-EEMavavsgggdDPTIYILVLTSSFNHDQTRQF 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 135 LSSK-YPDLASEEGLEMMQNKVPklnaetlepasCESDP------ENE----WCPPGHGDLYAALVGSGRLDALLKEGFK 203
Cdd:PTZ00339 184 LEENnFFGLDKEQVIFFKQSSLP-----------CYDENtgrfimSSQgslcTAPGGNGDVFKALAKCSELMDIVRKGIK 252
|
170
....*....|
gi 219130444 204 YMFVSNSDNL 213
Cdd:PTZ00339 253 YVQVISIDNI 262
|
|
| PLN02830 |
PLN02830 |
UDP-sugar pyrophosphorylase |
75-204 |
1.52e-04 |
|
UDP-sugar pyrophosphorylase
Pssm-ID: 215444 Cd Length: 615 Bit Score: 45.83 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 75 GGLGTGMGLDKAKSLLPVK--GDDTFLDLTAKQVIQM-------RKEYGLNVKFMLMNSFSTSDDTLSFLSS-KYPDLAS 144
Cdd:PLN02830 136 GGLGERLGYSGIKVALPTEtaTGTCYLQLYIESILALqerakkrKAKKGRKIPLVIMTSDDTHARTLKLLERnDYFGMDP 215
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 219130444 145 EEGLEMMQNKVPKLNAETlepASCESDPENEWC----PPGHGDLYAALVGSGRLDALLKEGFKY 204
Cdd:PLN02830 216 DQVTLLKQEKVACLMDND---ARLALDPNDPYKiqtkPHGHGDVHALLYSSGLLDKWLSAGKKW 276
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
562-907 |
3.07e-04 |
|
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: 44.40 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 562 GLLSTPAVSAIIREGGprwqKAFGAFIlTASHNPGgptEDFGIKYNCEHGEPAPERMTDEIYAntttiksyKICKEFPNI 641
Cdd:cd05802 72 GVIPTPAVAYLTRKLR----ADAGVVI-SASHNPF---EDNGIKFFSSDGYKLPDEVEEEIEA--------LIDKELELP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 642 DIGAaghskimsDDGSAevnIEVIDSTEAHVKLLKSIFDFSAIRGLldrpdfSMVYDAMHGVNGPYVKKVFcDILGQDLs 721
Cdd:cd05802 136 PTGE--------KIGRV---YRIDDARGRYIEFLKSTFPKDLLSGL------KIVLDCANGAAYKVAPEVF-RELGAEV- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 722 VTLNCVPkDDFNgghadPNL----TYAKELVAVMglnrKGEKIDMGgrpIpsfgaAADGDGDRnMIlgtqfFVspsDSLA 797
Cdd:cd05802 197 IVINNAP-DGLN-----INVncgsTHPESLQKAV----LENGADLG---I-----AFDGDADR-VI-----AV---DEKG 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 798 VIVaNADTIPF-----FRTQGGLKG---VARSMpTSGAVDLVAKDLNYSLFETPTGWKYFGNLMDSKELFDGaeytpfic 869
Cdd:cd05802 250 NIV-DGDQILAicardLKERGRLKGntvVGTVM-SNLGLEKALKELGIKLVRTKVGDRYVLEEMLKHGANLG-------- 319
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 219130444 870 GEESfgtG----SDHIREKDGLWAVLAWLSILAHANTnSLSD 907
Cdd:cd05802 320 GEQS---GhiifLDHSTTGDGLLTALQLLAIMKRSGK-SLSE 357
|
|
| PLN02435 |
PLN02435 |
probable UDP-N-acetylglucosamine pyrophosphorylase |
70-230 |
7.61e-03 |
|
probable UDP-N-acetylglucosamine pyrophosphorylase
Pssm-ID: 215238 Cd Length: 493 Bit Score: 40.24 E-value: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 70 VLKLNGGLGT-----------GMGLDKAKSLLPVKGDDTF-LDLTAKQVIQMRKEYGLNVKFMLMNSFSTSDDTLSFLSS 137
Cdd:PLN02435 119 VVLLSGGQGTrlgssdpkgcfNIGLPSGKSLFQLQAERILcVQRLAAQASSEGPGRPVTIHWYIMTSPFTDEATRKFFES 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219130444 138 -KYPDLASEEGLEMMQNKVPKLNAE---TLE-PASCESDPEnewcppGHGDLYAALVGSGRLDALLKEGFKYMFVSNSDN 212
Cdd:PLN02435 199 hKYFGLEADQVTFFQQGTLPCVSKDgkfIMEtPFKVAKAPD------GNGGVYAALKSSRLLEDMASRGIKYVDCYGVDN 272
|
170
....*....|....*....
gi 219130444 213 -LGASLDLEILTYFAEKNV 230
Cdd:PLN02435 273 aLVRVADPTFLGYFIDKGV 291
|
|
| |
