|
Name |
Accession |
Description |
Interval |
E-value |
| WecB |
COG0381 |
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis]; |
1-357 |
0e+00 |
|
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440150 Cd Length: 366 Bit Score: 556.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 1 MAPLVHALAKDPHFEAKVCVTAQHRE--MLDQVLKLFSI-VPDYDLNImkPGQGLTEITCRILEGLKPVLESFKPDVVLV 77
Cdd:COG0381 17 MAPVIRALKKRPGFEHVLVHTGQHYDyeMSDQFFEELGIpKPDYDLGI--GSGSLAEQTARILEGLEEVLEEEKPDAVLV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 78 HGDTTTTMAASLAAFYQRIPVGHVEAGLRTGDLssPWPEEGNRTLTGHLATYHFAPTETSRQNLLRENIADSRITVTGNT 157
Cdd:COG0381 95 HGDTNSTLAAALAAFKLGIPVAHVEAGLRSFDR--PMPEEINRRLTDHISDLHFAPTELARENLLREGIPPERIFVTGNT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 158 VIDALFWVRDRvlgdeALRETLLQRYPFisHGKKMILVTGHRRESFGL--GFEQICQALAEIAHTHpEVQIVYPVHlnPN 235
Cdd:COG0381 173 VIDALLYVLER-----AEESDILEELGL--EPKKYILVTLHRRENVDDpeRLENILEALRELAERY-DLPVVFPVH--PR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 236 VSEPVNRILGHIDNVMLIEPQDYLPFVWLMDRAWLILTDSGGIQEEAPSLGKPVLVMRDMTERPEAVAAGTVCLVGTDSQ 315
Cdd:COG0381 243 TRKRLEEFLGGHPNIRLIEPLGYLDFLNLMKRAYLVLTDSGGIQEEAPSLGKPCLTLRDTTERPETVEAGTNKLVGTDPE 322
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 893807056 316 RIVAEVTRLLEDDAAYQAMSRAHNPYGDGEACRRILSALKNN 357
Cdd:COG0381 323 RIVAAVERLLDDPAAYERMARAVNPYGDGNASERIVDILLRY 364
|
|
| wecB |
TIGR00236 |
UDP-N-acetylglucosamine 2-epimerase; This cytosolic enzyme converts UDP-N-acetyl-D-glucosamine ... |
1-357 |
0e+00 |
|
UDP-N-acetylglucosamine 2-epimerase; This cytosolic enzyme converts UDP-N-acetyl-D-glucosamine to UDP-N-acetyl-D-mannosamine. In E. coli, this is the first step in the pathway of enterobacterial common antigen biosynthesis.Members of this orthology group have many gene symbols, often reflecting the overall activity of the pathway and/or operon that includes it. Symbols include epsC (exopolysaccharide C) in Burkholderia solanacerum, cap8P (type 8 capsule P) in Staphylococcus aureus, and nfrC in an older designation based on the effects of deletion on phage N4 adsorption. Epimerase activity was also demonstrated in a bifunctional rat enzyme, for which the N-terminal domain appears to be orthologous. The set of proteins found above the suggested cutoff includes E. coli WecB in one of two deeply branched clusters and the rat UDP-N-acetylglucosamine 2-epimerase domain in the other. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 272978 Cd Length: 365 Bit Score: 552.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 1 MAPLVHALAKDPHFEAKVCVTAQHREMLDQVLKLFSIVPDYDLNIMKPGQGLTEITCRILEGLKPVLESFKPDVVLVHGD 80
Cdd:TIGR00236 16 MAPLIRALKKYPEIDSYVIVTAQHREMLDQVLDLFHLPPDYDLNIMSPGQTLGEITSNMLEGLEELLLEEKPDIVLVQGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 81 TTTTMAASLAAFYQRIPVGHVEAGLRTGDLSSPWPEEGNRTLTGHLATYHFAPTETSRQNLLRENIADSRITVTGNTVID 160
Cdd:TIGR00236 96 TTTTLAGALAAFYLQIPVGHVEAGLRTGDRYSPMPEEINRQLTGHIADLHFAPTEQAKDNLLRENVKADSIFVTGNTVID 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 161 ALFWVRDRVLGDEALREtllqrypfISHGKKMILVTGHRRESFGLGFEQICQALAEIAHTHPEVQIVYPVHLNPNVSEPV 240
Cdd:TIGR00236 176 ALLTNVEIAYSSPVLSE--------FGEDKRMILLTLHRRENVGEPLENIFKAIREIVEEFEDVQIVYPVHLNPVVREPL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 241 NRILGHIDNVMLIEPQDYLPFVWLMDRAWLILTDSGGIQEEAPSLGKPVLVMRDMTERPEAVAAGTVCLVGTDSQRIVAE 320
Cdd:TIGR00236 248 HKHLGDSKRVHLIEPLEYLDFLNLAANSHLILTDSGGVQEEAPSLGKPVLVLRDTTERPETVEAGTNKLVGTDKENITKA 327
|
330 340 350
....*....|....*....|....*....|....*..
gi 893807056 321 VTRLLEDDAAYQAMSRAHNPYGDGEACRRILSALKNN 357
Cdd:TIGR00236 328 AKRLLTDPDEYKKMSNASNPYGDGEASERIVEELLNH 364
|
|
| GTB_UDP-GlcNAc_2-Epimerase |
cd03786 |
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the ... |
1-355 |
2.31e-163 |
|
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the UDP-N-Acetylglucosamine (GlcNAc) 2-Epimerase family (EC 5.1.3.14) are known to catalyze the reversible interconversion of UDP-GlcNAc and UDP-N-acetylmannosamine (UDP-ManNAc). The enzyme serves to produce an activated form of ManNAc residues (UDP-ManNAc) for use in the biosynthesis of a variety of cell surface polysaccharides; The mammalian enzyme is bifunctional, catalyzing both the inversion of stereochemistry at C-2 and the hydrolysis of the UDP-sugar linkage to generate free ManNAc. It also catalyzes the phosphorylation of ManNAc to generate ManNAc 6-phosphate, a precursor to salic acids. In mammals, sialic acids are found at the termini of oligosaccharides in a large variety of cell surface glycoconjugates and are key mediators of cell-cell recognition events. Mutations in human members of this family have been associated with Sialuria, a rare disease caused by the disorders of sialic acid metabolism. This family belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340819 [Multi-domain] Cd Length: 365 Bit Score: 461.29 E-value: 2.31e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 1 MAPLVHALAKDPHFEAKVCVTAQHREMLDQVLK---LFSIVPDYDLNIMKPGQGLTEITCRILEGLKPVLESFKPDVVLV 77
Cdd:cd03786 15 LAPVLRALKKDPGLELVLVVTGQHLDMLLGVLFffiLFLIKPDYDLDLMGDNQTLGAKTGGLLIGLEEVLFEEKPDAVLV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 78 HGDTTTTMAASLAAFYQRIPVGHVEAGLRTGDLSSPWPEEGNRTLtgHLATYHFAPTETSRQNLLRENIADSRITVTGNT 157
Cdd:cd03786 95 LGDTNTTLAGALAAFKLGIPVAHVEAGLRSFDLGMPEEENRHRID--KLSDLHFAPTEEARENLLQEGEPPERIFVTGNT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 158 VIDALFWVRDRVLGDEALRETLLQrypfishGKKMILVTGHRRESFGLG--FEQICQALAEIAHTHpEVQIVYPVHLN-- 233
Cdd:cd03786 173 VIDALLSAALRIRDELVLSKLGLL-------EKKYILVTLHRRENVDSGerLEELLEALEELAEKY-DLIVVYPNHPRtr 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 234 PNVSEPVNRILGHIDNVMLIEPQDYLPFVWLMDRAWLILTDSGGIQEEAPSLGKPVLVMRDMTERPEAVAAGTVCLVGTD 313
Cdd:cd03786 245 PRIREVGLKFLGGLPNIRLIDPLGYLDLVLLKKRAKLVLTDSGGIQEEASFLGKPVLVLRDRTERPERVEAGTNVLVGTD 324
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 893807056 314 SQRIVAEVTRLLEDDAAYQAMSrAHNPYGDGEACRRILSALK 355
Cdd:cd03786 325 PEAILEAIEKLLSDEFEYSRMS-AINPYGDGNASERIVDILE 365
|
|
| Epimerase_2 |
pfam02350 |
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine ... |
6-355 |
3.61e-163 |
|
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine 2-epimerases EC:5.1.3.14 this enzyme catalyzes the production of UDP-ManNAc from UDP-GlcNAc. Note that some of the enzymes is this family are bifunctional such as Swiss:O35826 and Swiss:Q9Z0P6 in this instance Pfam matches only the N-terminal half of the protein suggesting that the additional C-terminal part (when compared to mono-functional members of this family) is responsible for the UPD-N-acetylmannosamine kinase activity of these enzymes. This hypothesis is further supported by the assumption that the C-terminal part of Swiss:O35826 is the kinase domain.
Pssm-ID: 426733 [Multi-domain] Cd Length: 336 Bit Score: 459.69 E-value: 3.61e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 6 HALAKDPhFEAKVCVTAQH--REMLDQVLKLFSI-VPDYDLNImkPGQGLTEITCRILEGLKPVLESFKPDVVLVHGDTT 82
Cdd:pfam02350 1 KALKADP-LELQLIVTGQHlsREMGDTFFEGFGIpKPDYLLNS--DSQSLAKSTGLILIGLEDVLAEEKPDLVLVLGDTN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 83 TTMAASLAAFYQRIPVGHVEAGLRTGDLSSPWPEEGNRTLTGHLATYHFAPTETSRQNLLRENIADSRITVTGNTVIDAL 162
Cdd:pfam02350 78 ETLAGALAAFYLRIPVAHVEAGLRSFDLTEPMPEEINRHAIDKLSDLHFAPTEEARENLLQEGEPPERIFVTGNTVIDAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 163 FWVRDRVLGDEALRETLLQRYpfishgkkmILVTGHRRESFGLG--FEQICQALAEIAHtHPEVQIVYPVHLNPNVSEPV 240
Cdd:pfam02350 158 LLSREEIEERSGILAKLGKRY---------VLVTFHRRENEDDPeaLRNILEALRALAE-RPDVPVVFPVHNNPRTRRRL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 241 NRILGHIDNVMLIEPQDYLPFVWLMDRAWLILTDSGGIQEEAPSLGKPVLVMRDMTERPEAVAAGTVCLVGTDSQRIVAE 320
Cdd:pfam02350 228 NERLEGYPRVRLIEPLGYLDFLSLLKRADLVITDSGGIQEEAPSLGVPVVNLRDTTERPEGREAGTNVLVGTDPERIVAA 307
|
330 340 350
....*....|....*....|....*....|....*
gi 893807056 321 VTRLLEDDAAYqamsraHNPYGDGEACRRILSALK 355
Cdd:pfam02350 308 LERLLEDPASY------KNPYGDGNASERIVDILE 336
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| WecB |
COG0381 |
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis]; |
1-357 |
0e+00 |
|
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440150 Cd Length: 366 Bit Score: 556.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 1 MAPLVHALAKDPHFEAKVCVTAQHRE--MLDQVLKLFSI-VPDYDLNImkPGQGLTEITCRILEGLKPVLESFKPDVVLV 77
Cdd:COG0381 17 MAPVIRALKKRPGFEHVLVHTGQHYDyeMSDQFFEELGIpKPDYDLGI--GSGSLAEQTARILEGLEEVLEEEKPDAVLV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 78 HGDTTTTMAASLAAFYQRIPVGHVEAGLRTGDLssPWPEEGNRTLTGHLATYHFAPTETSRQNLLRENIADSRITVTGNT 157
Cdd:COG0381 95 HGDTNSTLAAALAAFKLGIPVAHVEAGLRSFDR--PMPEEINRRLTDHISDLHFAPTELARENLLREGIPPERIFVTGNT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 158 VIDALFWVRDRvlgdeALRETLLQRYPFisHGKKMILVTGHRRESFGL--GFEQICQALAEIAHTHpEVQIVYPVHlnPN 235
Cdd:COG0381 173 VIDALLYVLER-----AEESDILEELGL--EPKKYILVTLHRRENVDDpeRLENILEALRELAERY-DLPVVFPVH--PR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 236 VSEPVNRILGHIDNVMLIEPQDYLPFVWLMDRAWLILTDSGGIQEEAPSLGKPVLVMRDMTERPEAVAAGTVCLVGTDSQ 315
Cdd:COG0381 243 TRKRLEEFLGGHPNIRLIEPLGYLDFLNLMKRAYLVLTDSGGIQEEAPSLGKPCLTLRDTTERPETVEAGTNKLVGTDPE 322
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 893807056 316 RIVAEVTRLLEDDAAYQAMSRAHNPYGDGEACRRILSALKNN 357
Cdd:COG0381 323 RIVAAVERLLDDPAAYERMARAVNPYGDGNASERIVDILLRY 364
|
|
| wecB |
TIGR00236 |
UDP-N-acetylglucosamine 2-epimerase; This cytosolic enzyme converts UDP-N-acetyl-D-glucosamine ... |
1-357 |
0e+00 |
|
UDP-N-acetylglucosamine 2-epimerase; This cytosolic enzyme converts UDP-N-acetyl-D-glucosamine to UDP-N-acetyl-D-mannosamine. In E. coli, this is the first step in the pathway of enterobacterial common antigen biosynthesis.Members of this orthology group have many gene symbols, often reflecting the overall activity of the pathway and/or operon that includes it. Symbols include epsC (exopolysaccharide C) in Burkholderia solanacerum, cap8P (type 8 capsule P) in Staphylococcus aureus, and nfrC in an older designation based on the effects of deletion on phage N4 adsorption. Epimerase activity was also demonstrated in a bifunctional rat enzyme, for which the N-terminal domain appears to be orthologous. The set of proteins found above the suggested cutoff includes E. coli WecB in one of two deeply branched clusters and the rat UDP-N-acetylglucosamine 2-epimerase domain in the other. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 272978 Cd Length: 365 Bit Score: 552.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 1 MAPLVHALAKDPHFEAKVCVTAQHREMLDQVLKLFSIVPDYDLNIMKPGQGLTEITCRILEGLKPVLESFKPDVVLVHGD 80
Cdd:TIGR00236 16 MAPLIRALKKYPEIDSYVIVTAQHREMLDQVLDLFHLPPDYDLNIMSPGQTLGEITSNMLEGLEELLLEEKPDIVLVQGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 81 TTTTMAASLAAFYQRIPVGHVEAGLRTGDLSSPWPEEGNRTLTGHLATYHFAPTETSRQNLLRENIADSRITVTGNTVID 160
Cdd:TIGR00236 96 TTTTLAGALAAFYLQIPVGHVEAGLRTGDRYSPMPEEINRQLTGHIADLHFAPTEQAKDNLLRENVKADSIFVTGNTVID 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 161 ALFWVRDRVLGDEALREtllqrypfISHGKKMILVTGHRRESFGLGFEQICQALAEIAHTHPEVQIVYPVHLNPNVSEPV 240
Cdd:TIGR00236 176 ALLTNVEIAYSSPVLSE--------FGEDKRMILLTLHRRENVGEPLENIFKAIREIVEEFEDVQIVYPVHLNPVVREPL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 241 NRILGHIDNVMLIEPQDYLPFVWLMDRAWLILTDSGGIQEEAPSLGKPVLVMRDMTERPEAVAAGTVCLVGTDSQRIVAE 320
Cdd:TIGR00236 248 HKHLGDSKRVHLIEPLEYLDFLNLAANSHLILTDSGGVQEEAPSLGKPVLVLRDTTERPETVEAGTNKLVGTDKENITKA 327
|
330 340 350
....*....|....*....|....*....|....*..
gi 893807056 321 VTRLLEDDAAYQAMSRAHNPYGDGEACRRILSALKNN 357
Cdd:TIGR00236 328 AKRLLTDPDEYKKMSNASNPYGDGEASERIVEELLNH 364
|
|
| GTB_UDP-GlcNAc_2-Epimerase |
cd03786 |
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the ... |
1-355 |
2.31e-163 |
|
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the UDP-N-Acetylglucosamine (GlcNAc) 2-Epimerase family (EC 5.1.3.14) are known to catalyze the reversible interconversion of UDP-GlcNAc and UDP-N-acetylmannosamine (UDP-ManNAc). The enzyme serves to produce an activated form of ManNAc residues (UDP-ManNAc) for use in the biosynthesis of a variety of cell surface polysaccharides; The mammalian enzyme is bifunctional, catalyzing both the inversion of stereochemistry at C-2 and the hydrolysis of the UDP-sugar linkage to generate free ManNAc. It also catalyzes the phosphorylation of ManNAc to generate ManNAc 6-phosphate, a precursor to salic acids. In mammals, sialic acids are found at the termini of oligosaccharides in a large variety of cell surface glycoconjugates and are key mediators of cell-cell recognition events. Mutations in human members of this family have been associated with Sialuria, a rare disease caused by the disorders of sialic acid metabolism. This family belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340819 [Multi-domain] Cd Length: 365 Bit Score: 461.29 E-value: 2.31e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 1 MAPLVHALAKDPHFEAKVCVTAQHREMLDQVLK---LFSIVPDYDLNIMKPGQGLTEITCRILEGLKPVLESFKPDVVLV 77
Cdd:cd03786 15 LAPVLRALKKDPGLELVLVVTGQHLDMLLGVLFffiLFLIKPDYDLDLMGDNQTLGAKTGGLLIGLEEVLFEEKPDAVLV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 78 HGDTTTTMAASLAAFYQRIPVGHVEAGLRTGDLSSPWPEEGNRTLtgHLATYHFAPTETSRQNLLRENIADSRITVTGNT 157
Cdd:cd03786 95 LGDTNTTLAGALAAFKLGIPVAHVEAGLRSFDLGMPEEENRHRID--KLSDLHFAPTEEARENLLQEGEPPERIFVTGNT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 158 VIDALFWVRDRVLGDEALRETLLQrypfishGKKMILVTGHRRESFGLG--FEQICQALAEIAHTHpEVQIVYPVHLN-- 233
Cdd:cd03786 173 VIDALLSAALRIRDELVLSKLGLL-------EKKYILVTLHRRENVDSGerLEELLEALEELAEKY-DLIVVYPNHPRtr 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 234 PNVSEPVNRILGHIDNVMLIEPQDYLPFVWLMDRAWLILTDSGGIQEEAPSLGKPVLVMRDMTERPEAVAAGTVCLVGTD 313
Cdd:cd03786 245 PRIREVGLKFLGGLPNIRLIDPLGYLDLVLLKKRAKLVLTDSGGIQEEASFLGKPVLVLRDRTERPERVEAGTNVLVGTD 324
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 893807056 314 SQRIVAEVTRLLEDDAAYQAMSrAHNPYGDGEACRRILSALK 355
Cdd:cd03786 325 PEAILEAIEKLLSDEFEYSRMS-AINPYGDGNASERIVDILE 365
|
|
| Epimerase_2 |
pfam02350 |
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine ... |
6-355 |
3.61e-163 |
|
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine 2-epimerases EC:5.1.3.14 this enzyme catalyzes the production of UDP-ManNAc from UDP-GlcNAc. Note that some of the enzymes is this family are bifunctional such as Swiss:O35826 and Swiss:Q9Z0P6 in this instance Pfam matches only the N-terminal half of the protein suggesting that the additional C-terminal part (when compared to mono-functional members of this family) is responsible for the UPD-N-acetylmannosamine kinase activity of these enzymes. This hypothesis is further supported by the assumption that the C-terminal part of Swiss:O35826 is the kinase domain.
Pssm-ID: 426733 [Multi-domain] Cd Length: 336 Bit Score: 459.69 E-value: 3.61e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 6 HALAKDPhFEAKVCVTAQH--REMLDQVLKLFSI-VPDYDLNImkPGQGLTEITCRILEGLKPVLESFKPDVVLVHGDTT 82
Cdd:pfam02350 1 KALKADP-LELQLIVTGQHlsREMGDTFFEGFGIpKPDYLLNS--DSQSLAKSTGLILIGLEDVLAEEKPDLVLVLGDTN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 83 TTMAASLAAFYQRIPVGHVEAGLRTGDLSSPWPEEGNRTLTGHLATYHFAPTETSRQNLLRENIADSRITVTGNTVIDAL 162
Cdd:pfam02350 78 ETLAGALAAFYLRIPVAHVEAGLRSFDLTEPMPEEINRHAIDKLSDLHFAPTEEARENLLQEGEPPERIFVTGNTVIDAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 163 FWVRDRVLGDEALRETLLQRYpfishgkkmILVTGHRRESFGLG--FEQICQALAEIAHtHPEVQIVYPVHLNPNVSEPV 240
Cdd:pfam02350 158 LLSREEIEERSGILAKLGKRY---------VLVTFHRRENEDDPeaLRNILEALRALAE-RPDVPVVFPVHNNPRTRRRL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 241 NRILGHIDNVMLIEPQDYLPFVWLMDRAWLILTDSGGIQEEAPSLGKPVLVMRDMTERPEAVAAGTVCLVGTDSQRIVAE 320
Cdd:pfam02350 228 NERLEGYPRVRLIEPLGYLDFLSLLKRADLVITDSGGIQEEAPSLGVPVVNLRDTTERPEGREAGTNVLVGTDPERIVAA 307
|
330 340 350
....*....|....*....|....*....|....*
gi 893807056 321 VTRLLEDDAAYqamsraHNPYGDGEACRRILSALK 355
Cdd:pfam02350 308 LERLLEDPASY------KNPYGDGNASERIVDILE 336
|
|
| NeuC_NnaA |
TIGR03568 |
UDP-N-acetyl-D-glucosamine 2-epimerase, UDP-hydrolysing; This family of enzymes catalyzes the ... |
1-354 |
2.52e-30 |
|
UDP-N-acetyl-D-glucosamine 2-epimerase, UDP-hydrolysing; This family of enzymes catalyzes the combined epimerization and UDP-hydrolysis of UDP-N-acetylglucosamine to N-acetylmannosamine. This is in contrast to the related enzyme WecB (TIGR00236) which retains the UDP moiety. NeuC acts in concert with NeuA and NeuB to synthesize CMP-N5-acetyl-neuraminate.
Pssm-ID: 274654 Cd Length: 364 Bit Score: 118.78 E-value: 2.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 1 MAPLVHALAKDPHFEAKVCVTAQH---------REMLDQVLKLFSIVP---DYDlnimkPGQGLTEITCRILEGLKPVLE 68
Cdd:TIGR03568 15 LRPLLKALQDDPDLELQLIVTGMHlspeygntvNEIEKDGFDIDEKIEillDSD-----SNAGMAKSMGLTIIGFSDAFE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 69 SFKPDVVLVHGDTTTTMAASLAAFYQRIPVGHVEAGLRTgdlsspwpeEGN-----RtltgH----LATYHFAPTETSRQ 139
Cdd:TIGR03568 90 RLKPDLVVVLGDRFEMLAAAIAAALLNIPIAHIHGGEVT---------EGAidesiR----HaitkLSHLHFVATEEYRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 140 NLLRENIADSRITVTGNTVIDALfwvrdrVLGDEALRETLLQRYpFISHGKKMILVTGH----RRESFGLGFEQICQALA 215
Cdd:TIGR03568 157 RVIQMGEDPDRVFNVGSPGLDNI------LSLDLLSKEELEEKL-GIDLDKPYALVTFHpvtlEKAEAEEQIKELLKALD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 216 EIAHthpevQIVYpvhLNPNVSEPVNRILGHI-------DNVMLIE---PQDYLPfvwLMDRAWLIL--TDSGGIqeEAP 283
Cdd:TIGR03568 230 ELNK-----NIIF---TYPNADAGSRIINEAIeeyvekhPNFRLFKslgQERYLS---LLKNADAVIgnSSSGII--EAP 296
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 893807056 284 SLGKPVLvmrDMTERPEA-VAAGTVCLVGTDSQRIVAEVTRLLEDDaaYQAM-SRAHNPYGDGEACRRILSAL 354
Cdd:TIGR03568 297 SFGVPTI---NIGTRQKGrLRADSVIDVDPDKEEIVKAIEKALDPA--FKKSlKKVKNPYGDGNSSKRIIEIL 364
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
58-337 |
4.41e-08 |
|
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.
Pssm-ID: 340831 [Multi-domain] Cd Length: 366 Bit Score: 54.47 E-value: 4.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 58 RILEGLKPVLESFKPDVVLVHgDTTTTMAASLAAFYQRIPVGHVEAGLRTGDLSSPWPEE----GNRTLTGHLATYHFAP 133
Cdd:cd03801 69 RLLRELRPLLRLRKFDVVHAH-GLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAErrllARAEALLRRADAVIAV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 134 TETSRQNLLRE-NIADSRITVTGNTVIDALFWVRDRvlgdealretllqRYPFISHGKKMILVTGhrRESFGLGFEQICQ 212
Cdd:cd03801 148 SEALRDELRALgGIPPEKIVVIPNGVDLERFSPPLR-------------RKLGIPPDRPVLLFVG--RLSPRKGVDLLLE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 213 ALAEIAHTHPEVQ--IVYPVHlnPNVSEPVNRILGHIDNVMLIEPQDYLPFVWLMDRAWLILTDSggIQE-------EAP 283
Cdd:cd03801 213 ALAKLLRRGPDVRlvIVGGDG--PLRAELEELELGLGDRVRFLGFVPDEELPALYAAADVFVLPS--RYEgfglvvlEAM 288
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 893807056 284 SLGKPVLVmrdmTER---PEAVAAGTVCLV--GTDSQRIVAEVTRLLEDDAAYQAMSRA 337
Cdd:cd03801 289 AAGLPVVA----TDVgglPEVVEDGEGGLVvpPDDVEALADALLRLLADPELRARLGRA 343
|
|
| TagB |
COG1887 |
CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope ... |
128-354 |
2.81e-06 |
|
CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];
Pssm-ID: 441491 Cd Length: 369 Bit Score: 48.83 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 128 TYHFAPTETSRQNLLRE-NIADSRITVTGNTVIDALFWVrdrvlGDEALRETLLQRYPfISHGKKMILV--TGHRRES-- 202
Cdd:COG1887 142 DYLLSSSEESTEIFRRAfGYPEGEVLETGYPRNDVLFDA-----DREELREELRERLG-IPEDKKVILYapTWRDDEDnf 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 203 ---FGLGFEQICQALAE----IAHTHPEVQIVYPVHLNPNV-----SEPVNRILGHIDnvMLIepqdylpfvwlmdrawl 270
Cdd:COG1887 216 ddyLDLDLERLAELLGDdyvlLVRLHPFVKDSLDEKYSDRIidvsdYPDINDLLLASD--VLI----------------- 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 271 ilTDSGGIQEEAPSLGKPVLV----------MRDMTERPEAVAAGTVClvgTDSQRIVAEVTRLLEDD----AAYQAMSR 336
Cdd:COG1887 277 --TDYSSVMFDFALLDRPIIFyaydleeyrdERGFYFDYEEDAPGPVV---TTFEELIDAIEDILENGdeyaEKYKAFRE 351
|
250
....*....|....*...
gi 893807056 337 AHNPYGDGEACRRILSAL 354
Cdd:COG1887 352 RFFPYDDGNASERVVDAI 369
|
|
| Glycosyltransferase_GTB-type |
cd01635 |
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
162-310 |
7.15e-05 |
|
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340816 [Multi-domain] Cd Length: 235 Bit Score: 43.55 E-value: 7.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 162 LFWVRDRVLGDEALRETLLQRYPFISHGKKMILVTGHRREsfGLGFEQICQALAEIAHTHPEVQIVYPVHLNPNVSEPVN 241
Cdd:cd01635 82 VVTVHGPDSLESTRSELLALARLLVSLPLADKVSVGRLVP--EKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEAL 159
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 893807056 242 -RILGHIDNVMLIEPQDYLPFVWLMDR-AWLILTDS-----GGIQEEAPSLGKPVLVMRDMTeRPEAVAAGTVCLV 310
Cdd:cd01635 160 aAALGLLERVVIIGGLVDDEVLELLLAaADVFVLPSrsegfGLVLLEAMAAGKPVIATDVGG-IPEFVVDGENGLL 234
|
|
| GT4_WbuB-like |
cd03794 |
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ... |
5-337 |
3.19e-03 |
|
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.
Pssm-ID: 340825 [Multi-domain] Cd Length: 391 Bit Score: 39.25 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 5 VHALAKDPHFEAKVCvTAQHREMLDQV-LKLFSIVPDYDLNIMKPGQGLTEITCRILEGLKpvLESFKPDVVLVHGDT-T 82
Cdd:cd03794 34 VTVLTPSPNYPLGRI-FAGATETKDGIrVIRVKLGPIKKNGLIRRLLNYLSFALAALLKLL--VREERPDVIIAYSPPiT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 83 TTMAASLAAFYQRIPVGHV------EAGLRTGDLSSPWPEEGNRTLTG---HLATYHFAPTETSRQNLLRENIADSRITV 153
Cdd:cd03794 111 LGLAALLLKKLRGAPFILDvrdlwpESLIALGVLKKGSLLKLLKKLERklyRLADAIIVLSPGLKEYLLRKGVPKEKIIV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 154 TGNTVIDALFwvrDRVLGDEALRETLLQrypfishGKKMILVTGhrreSFGL--GFEQICQALAEIAHtHPEVQIVY--P 229
Cdd:cd03794 191 IPNWADLEEF---KPPPKDELRKKLGLD-------DKFVVVYAG----NIGKaqGLETLLEAAERLKR-RPDIRFLFvgD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 230 VHLNPNVSEPVNRILghIDNVMLI---EPQDYLPFVWLMDRAWLILTDSGGIQEEAPS-------LGKPVLVMRDMTERP 299
Cdd:cd03794 256 GDEKERLKELAKARG--LDNVTFLgrvPKEEVPELLSAADVGLVPLKDNPANRGSSPSklfeymaAGKPILASDDGGSDL 333
|
330 340 350
....*....|....*....|....*....|....*....
gi 893807056 300 EAVAAGT-VCLVGTDSQRIVAEVTRLLEDDAAYQAMSRA 337
Cdd:cd03794 334 AVEINGCgLVVEPGDPEALADAILELLDDPELRRAMGEN 372
|
|
| GT28_MurG |
cd03785 |
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ... |
66-351 |
9.54e-03 |
|
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340818 [Multi-domain] Cd Length: 350 Bit Score: 37.58 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 66 VLESFKPDVVLVHGDTTTTmAASLAAFYQRIP-VGH---VEAGLrTGDLSSPWpeeGNRTLTghlatyHFAPTETSRQNl 141
Cdd:cd03785 84 ILRKFKPDVVIGFGGYVSG-PVVLAARLLGIPlIIHeqnAVPGL-ANRLLSRF---ADKVAV------SFPETKKYFPA- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 142 lreniadSRITVTGNTVidalfwvRDRVLGDEALRETLLqrypfISHGKKMILVTGhrresfG-LGFEQICQALAEIAHT 220
Cdd:cd03785 152 -------AKVVVTGNPV-------REEILNLRKELKRFG-----LPPDKPTLLVFG------GsQGARAINRAVPKALPK 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 893807056 221 HPE--VQIVY---PVHLNPnVSEPVNRILGHIDnvmliepqdYLPFVWLMDRAW----LILTDSG-GIQEEAPSLGKPVL 290
Cdd:cd03785 207 LLErgIQVIHqtgKGDYDE-VKKLYEDLGINVK---------VFPFIDDMAAAYaaadLVISRAGaSTIAELTAAGKPAI 276
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 893807056 291 VM-------RDMTERPEAVAA--GTVCLVGTD--SQRIVAEVTRLLEDDAAYQAMSRAHNPYGDGEACRRIL 351
Cdd:cd03785 277 LIpypyaadDHQEANARALEKagAAIVIDQEEltPEVLAEAILDLLNDPERLKKMAEAAKKLAKPDAAERIA 348
|
|
| |
