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Conserved domains on  [gi|1621529725|ref|WP_136196087|]
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MULTISPECIES: mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase [unclassified Enterobacter]

Protein Classification

mannose-6-phosphate isomerase type 2 family protein( domain architecture ID 11492682)

mannose-6-phosphate isomerase type 2 family protein is involved in nucleotide-sugar biosynthesis, similar to bifunctional mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GMP_PMI TIGR01479
mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to ...
 3-474 0e+00

mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase (EC 5.3.1.8) (PMI) and mannose-1-phosphate guanylyltransferase (EC 2.7.7.22) in Pseudomonas aeruginosa, Xanthomonas campestris, and Gluconacetobacter xylinus. The literature on the enzyme from E. coli attributes mannose-6-phosphate isomerase activity to an adjacent gene, but the present sequence has not been shown to lack the activity. The PMI domain is C-terminal. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


:

Pssm-ID: 273648 [Multi-domain]  Cd Length: 468  Bit Score: 796.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725   3 IIPIIMAGGSGSRLWPLSRLTYPKQFLTLEGEQTMLQQTISRLSKLEVECPVVICNEEHRFIVAEQLRQINALNE-IILE 81
Cdd:TIGR01479   1 IIPVILAGGSGTRLWPLSRELYPKQFLALVGDLTMLQQTLKRLAGLPCSSPLVICNEEHRFIVAEQLREIGKLASnIILE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725  82 PIGRNTAPAVALAAIQCLKDlaDNEDALLLILAADHIIKDNTAFINAIKISTSYAIDGNLVTFGIEPSSPETGFGYIQAG 161
Cdd:TIGR01479  81 PVGRNTAPAIALAALLAARR--NGEDPLLLVLAADHVITDEDAFQAAVKLAMPAAAEGKLVTFGIVPTHPETGYGYIRRG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 162 DEISSGGVsgaFKVNAFVEKPERAVAEGFLSDGGYYWNSGMFMFGARKYLSELHKFCPDIYDSCSKAIQSPDKDLCFIRI 241
Cdd:TIGR01479 159 APLAGEDV---YQVQRFVEKPDLATAQAYLESGDYYWNSGMFLFRASRYLAELKKHAPDIYEACEAAVEASEPDLDFIRL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 242 DYDIFSRCPDLSIDYAVMEHTANAVVVPMSAGWSDVGSWSSLWDISVKDERGNVLIGDVIAHNSSNNYVHAQSGLVTMLG 321
Cdd:TIGR01479 236 DKEAFEQCPSESIDYAVMEKTADAVVVPMDAGWSDVGSWSALWEISDKDADGNVLKGDVLTHDTKNSYIYSESRLVAVVG 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 322 VEDLIVVQTKDAILVTKHNAVQDVKKIVEELKTAGRSEYRIHREVYRPWGRCDSIDAGKRYEVKRIEVNPGEGISLQTHF 401
Cdd:TIGR01479 316 VEDLVVVETKDAVLVAHKDRVQDVKKIVEQLKADGRTETEQHREVYRPWGKYDSIDQGDRYQVKRITVKPGEKLSLQMHH 395

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1621529725 402 HRSEHWVVVAGTAKVTLEDKQFLLGENESVYIPVGAQHCLENPGKIPLEIIEVRSGPYLGDDDIVRIADRYGR 474
Cdd:TIGR01479 396 HRAEHWIVVSGTARVTIGDETLLLTENESTYIPLGVIHRLENPGKIPLELIEVQSGSYLGEDDIIRFEDRYGR 468
 
Name Accession Description Interval E-value
GMP_PMI TIGR01479
mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to ...
 3-474 0e+00

mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase (EC 5.3.1.8) (PMI) and mannose-1-phosphate guanylyltransferase (EC 2.7.7.22) in Pseudomonas aeruginosa, Xanthomonas campestris, and Gluconacetobacter xylinus. The literature on the enzyme from E. coli attributes mannose-6-phosphate isomerase activity to an adjacent gene, but the present sequence has not been shown to lack the activity. The PMI domain is C-terminal. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273648 [Multi-domain]  Cd Length: 468  Bit Score: 796.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725   3 IIPIIMAGGSGSRLWPLSRLTYPKQFLTLEGEQTMLQQTISRLSKLEVECPVVICNEEHRFIVAEQLRQINALNE-IILE 81
Cdd:TIGR01479   1 IIPVILAGGSGTRLWPLSRELYPKQFLALVGDLTMLQQTLKRLAGLPCSSPLVICNEEHRFIVAEQLREIGKLASnIILE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725  82 PIGRNTAPAVALAAIQCLKDlaDNEDALLLILAADHIIKDNTAFINAIKISTSYAIDGNLVTFGIEPSSPETGFGYIQAG 161
Cdd:TIGR01479  81 PVGRNTAPAIALAALLAARR--NGEDPLLLVLAADHVITDEDAFQAAVKLAMPAAAEGKLVTFGIVPTHPETGYGYIRRG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 162 DEISSGGVsgaFKVNAFVEKPERAVAEGFLSDGGYYWNSGMFMFGARKYLSELHKFCPDIYDSCSKAIQSPDKDLCFIRI 241
Cdd:TIGR01479 159 APLAGEDV---YQVQRFVEKPDLATAQAYLESGDYYWNSGMFLFRASRYLAELKKHAPDIYEACEAAVEASEPDLDFIRL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 242 DYDIFSRCPDLSIDYAVMEHTANAVVVPMSAGWSDVGSWSSLWDISVKDERGNVLIGDVIAHNSSNNYVHAQSGLVTMLG 321
Cdd:TIGR01479 236 DKEAFEQCPSESIDYAVMEKTADAVVVPMDAGWSDVGSWSALWEISDKDADGNVLKGDVLTHDTKNSYIYSESRLVAVVG 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 322 VEDLIVVQTKDAILVTKHNAVQDVKKIVEELKTAGRSEYRIHREVYRPWGRCDSIDAGKRYEVKRIEVNPGEGISLQTHF 401
Cdd:TIGR01479 316 VEDLVVVETKDAVLVAHKDRVQDVKKIVEQLKADGRTETEQHREVYRPWGKYDSIDQGDRYQVKRITVKPGEKLSLQMHH 395

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1621529725 402 HRSEHWVVVAGTAKVTLEDKQFLLGENESVYIPVGAQHCLENPGKIPLEIIEVRSGPYLGDDDIVRIADRYGR 474
Cdd:TIGR01479 396 HRAEHWIVVSGTARVTIGDETLLLTENESTYIPLGVIHRLENPGKIPLELIEVQSGSYLGEDDIIRFEDRYGR 468
cpsB PRK15460
mannose-1-phosphate guanyltransferase; Provisional
 1-475 0e+00

mannose-1-phosphate guanyltransferase; Provisional


Pssm-ID: 185357 [Multi-domain]  Cd Length: 478  Bit Score: 738.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725   1 MKIIPIIMAGGSGSRLWPLSRLTYPKQFLTLEGEQTMLQQTISRLSKLEVECPVVICNEEHRFIVAEQLRQINALNE-II 79
Cdd:PRK15460    4 SKLYPVVMAGGSGSRLWPLSRVLYPKQFLCLKGDLTMLQTTICRLNGVECESPVVICNEQHRFIVAEQLRQLNKLTEnII 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725  80 LEPIGRNTAPAVALAAIQCLKDLADNeDALLLILAADHIIKDNTAFINAIKISTSYAIDGNLVTFGIEPSSPETGFGYIQ 159
Cdd:PRK15460   84 LEPAGRNTAPAIALAALAAKRHSPES-DPLMLVLAADHVIADEDAFRAAVRNAMPYAEAGKLVTFGIVPDLPETGYGYIR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 160 AGDEISSGGVSGAFKVNAFVEKPERAVAEGFLSDGGYYWNSGMFMFGARKYLSELHKFCPDIYDSCSKAIQSPDKDLCFI 239
Cdd:PRK15460  163 RGEVSAGEQDTVAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDPDLDFI 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 240 RIDYDIFSRCPDLSIDYAVMEHTANAVVVPMSAGWSDVGSWSSLWDISVKDERGNVLIGDVIAHNSSNNYVHAQSGLVTM 319
Cdd:PRK15460  243 RVDEEAFLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSLWEISAHTAEGNVCHGDVINHKTENSYVYAESGLVTT 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 320 LGVEDLIVVQTKDAILVTKHNAVQDVKKIVEELKTAGRSEYRIHREVYRPWGRCDSIDAGKRYEVKRIEVNPGEGISLQT 399
Cdd:PRK15460  323 VGVKDLVVVQTKDAVLIADRNAVQDVKKVVEQIKADGRHEHRVHREVYRPWGKYDSIDAGDRYQVKRITVKPGEGLSVQM 402

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1621529725 400 HFHRSEHWVVVAGTAKVTLEDKQFLLGENESVYIPVGAQHCLENPGKIPLEIIEVRSGPYLGDDDIVRIADRYGRV 475
Cdd:PRK15460  403 HHHRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLIEVRSGSYLEEDDVVRFADRYGRV 478
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-353 0e+00

Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 563.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725   1 MKIIPIIMAGGSGSRLWPLSRLTYPKQFLTLEGEQTMLQQTISRLSKL-EVECPVVICNEEHRFIVAEQLRQINALNeII 79
Cdd:COG0836     1 SMIYPVILAGGSGTRLWPLSRESYPKQFLPLLGEKSLLQQTVERLAGLvPPENILVVTNEEHRFLVAEQLPELGPAN-IL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725  80 LEPIGRNTAPAVALAAIQCLKDladNEDALLLILAADHIIKDNTAFINAIKISTSYAIDGNLVTFGIEPSSPETGFGYIQ 159
Cdd:COG0836    80 LEPVGRNTAPAIALAALLIAKR---DPDAVLLVLPADHLIEDEEAFREAVRAAVEAAEAGKLVTFGIKPTRPETGYGYIE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 160 AGDEISSGGVsgaFKVNAFVEKPERAVAEGFLSDGGYYWNSGMFMFGARKYLSELHKFCPDIYDSCSKAIQSPDKDLcFI 239
Cdd:COG0836   157 AGEALGGAGA---YKVKRFVEKPDLETAEEYLASGNYLWNSGMFVFRASTILEELERHAPEIYAALEAAVAAAGTDL-EV 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 240 RIDYDIFSRCPDLSIDYAVMEHTANAVVVPMSAGWSDVGSWSSLWDISVKDERGNVLIGDVIAHNSSNNYVHAQSGLVTM 319
Cdd:COG0836   233 RLDAEAFAALPSISIDYAVMEKADNVAVVPADFGWSDVGSWDALWELLEKDENGNVVLGDVLLIDSSNSLVRSEGRLVAV 312

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1621529725 320 LGVEDLIVVQTKDAILVTKHNAVQDVKKIVEELK 353
Cdd:COG0836   313 IGVEDLVVVDTPDALLVAPKDRAQEVKKIVEALK 346
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 3-283 8.70e-138

GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 397.33  E-value: 8.70e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725   3 IIPIIMAGGSGSRLWPLSRLTYPKQFLTLEGEQTMLQQTISRLSKL-EVECPVVICNEEHRFIVAEQLRQINALNEIILE 81
Cdd:cd02509     1 IYPVILAGGSGTRLWPLSRESYPKQFLKLFGDKSLLQQTLDRLKGLvPPDRILVVTNEEYRFLVREQLPEGLPEENIILE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725  82 PIGRNTAPAVALAAIQCLKDladNEDALLLILAADHIIKDNTAFINAIKISTSYAIDGNLVTFGIEPSSPETGFGYIQAG 161
Cdd:cd02509    81 PEGRNTAPAIALAALYLAKR---DPDAVLLVLPSDHLIEDVEAFLKAVKKAVEAAEEGYLVTFGIKPTRPETGYGYIEAG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 162 DEISsggvSGAFKVNAFVEKPERAVAEGFLSDGGYYWNSGMFMFGARKYLSELHKFCPDIYDSCSKAIQSPDKDLcFIRI 241
Cdd:cd02509   158 EKLG----GGVYRVKRFVEKPDLETAKEYLESGNYLWNSGIFLFRAKTFLEELKKHAPDIYEALEKALAAAGTDD-FLRL 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1621529725 242 DYDIFSRCPDLSIDYAVMEHTANAVVVPMSAGWSDVGSWSSL 283
Cdd:cd02509   233 LEEAFAKIPSISIDYAVMEKTKKVAVVPADFGWSDLGSWDAL 274
MannoseP_isomer pfam01050
Mannose-6-phosphate isomerase; All of the members of this Pfam entry belong to family 2 of the ...
 320-470 6.16e-87

Mannose-6-phosphate isomerase; All of the members of this Pfam entry belong to family 2 of the mannose-6-phosphate isomerases. The type II phosphomannose isomerases are bifunctional enzymes. This Pfam entry covers the isomerase domain. The guanosine diphospho-D-mannose pyrophosphorylase domain is in another Pfam entry, see pfam00483.


Pssm-ID: 426015 [Multi-domain]  Cd Length: 151  Bit Score: 262.74  E-value: 6.16e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 320 LGVEDLIVVQTKDAILVTKHNAVQDVKKIVEELKTAGRSEYRIHREVYRPWGRCDSIDAGKRYEVKRIEVNPGEGISLQT 399
Cdd:pfam01050   1 IGVENLVVVETKDALLVAHKDKVQDVKKVVEELKENGRSEHQTHREVYRPWGSYDVIDEGERYQVKRITVKPGARLSLQM 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621529725 400 HFHRSEHWVVVAGTAKVTLEDKQFLLGENESVYIPVGAQHCLENPGKIPLEIIEVRSGPYLGDDDIVRIAD 470
Cdd:pfam01050  81 HHHRAEHWIVVSGTARVTKGGETFLLTENESTYIPLGTIHRLENPGKIPLELIEVQSGSYLGEDDIVRFED 151
 
Name Accession Description Interval E-value
GMP_PMI TIGR01479
mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to ...
 3-474 0e+00

mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase (EC 5.3.1.8) (PMI) and mannose-1-phosphate guanylyltransferase (EC 2.7.7.22) in Pseudomonas aeruginosa, Xanthomonas campestris, and Gluconacetobacter xylinus. The literature on the enzyme from E. coli attributes mannose-6-phosphate isomerase activity to an adjacent gene, but the present sequence has not been shown to lack the activity. The PMI domain is C-terminal. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273648 [Multi-domain]  Cd Length: 468  Bit Score: 796.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725   3 IIPIIMAGGSGSRLWPLSRLTYPKQFLTLEGEQTMLQQTISRLSKLEVECPVVICNEEHRFIVAEQLRQINALNE-IILE 81
Cdd:TIGR01479   1 IIPVILAGGSGTRLWPLSRELYPKQFLALVGDLTMLQQTLKRLAGLPCSSPLVICNEEHRFIVAEQLREIGKLASnIILE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725  82 PIGRNTAPAVALAAIQCLKDlaDNEDALLLILAADHIIKDNTAFINAIKISTSYAIDGNLVTFGIEPSSPETGFGYIQAG 161
Cdd:TIGR01479  81 PVGRNTAPAIALAALLAARR--NGEDPLLLVLAADHVITDEDAFQAAVKLAMPAAAEGKLVTFGIVPTHPETGYGYIRRG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 162 DEISSGGVsgaFKVNAFVEKPERAVAEGFLSDGGYYWNSGMFMFGARKYLSELHKFCPDIYDSCSKAIQSPDKDLCFIRI 241
Cdd:TIGR01479 159 APLAGEDV---YQVQRFVEKPDLATAQAYLESGDYYWNSGMFLFRASRYLAELKKHAPDIYEACEAAVEASEPDLDFIRL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 242 DYDIFSRCPDLSIDYAVMEHTANAVVVPMSAGWSDVGSWSSLWDISVKDERGNVLIGDVIAHNSSNNYVHAQSGLVTMLG 321
Cdd:TIGR01479 236 DKEAFEQCPSESIDYAVMEKTADAVVVPMDAGWSDVGSWSALWEISDKDADGNVLKGDVLTHDTKNSYIYSESRLVAVVG 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 322 VEDLIVVQTKDAILVTKHNAVQDVKKIVEELKTAGRSEYRIHREVYRPWGRCDSIDAGKRYEVKRIEVNPGEGISLQTHF 401
Cdd:TIGR01479 316 VEDLVVVETKDAVLVAHKDRVQDVKKIVEQLKADGRTETEQHREVYRPWGKYDSIDQGDRYQVKRITVKPGEKLSLQMHH 395

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1621529725 402 HRSEHWVVVAGTAKVTLEDKQFLLGENESVYIPVGAQHCLENPGKIPLEIIEVRSGPYLGDDDIVRIADRYGR 474
Cdd:TIGR01479 396 HRAEHWIVVSGTARVTIGDETLLLTENESTYIPLGVIHRLENPGKIPLELIEVQSGSYLGEDDIIRFEDRYGR 468
cpsB PRK15460
mannose-1-phosphate guanyltransferase; Provisional
 1-475 0e+00

mannose-1-phosphate guanyltransferase; Provisional


Pssm-ID: 185357 [Multi-domain]  Cd Length: 478  Bit Score: 738.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725   1 MKIIPIIMAGGSGSRLWPLSRLTYPKQFLTLEGEQTMLQQTISRLSKLEVECPVVICNEEHRFIVAEQLRQINALNE-II 79
Cdd:PRK15460    4 SKLYPVVMAGGSGSRLWPLSRVLYPKQFLCLKGDLTMLQTTICRLNGVECESPVVICNEQHRFIVAEQLRQLNKLTEnII 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725  80 LEPIGRNTAPAVALAAIQCLKDLADNeDALLLILAADHIIKDNTAFINAIKISTSYAIDGNLVTFGIEPSSPETGFGYIQ 159
Cdd:PRK15460   84 LEPAGRNTAPAIALAALAAKRHSPES-DPLMLVLAADHVIADEDAFRAAVRNAMPYAEAGKLVTFGIVPDLPETGYGYIR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 160 AGDEISSGGVSGAFKVNAFVEKPERAVAEGFLSDGGYYWNSGMFMFGARKYLSELHKFCPDIYDSCSKAIQSPDKDLCFI 239
Cdd:PRK15460  163 RGEVSAGEQDTVAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDPDLDFI 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 240 RIDYDIFSRCPDLSIDYAVMEHTANAVVVPMSAGWSDVGSWSSLWDISVKDERGNVLIGDVIAHNSSNNYVHAQSGLVTM 319
Cdd:PRK15460  243 RVDEEAFLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSLWEISAHTAEGNVCHGDVINHKTENSYVYAESGLVTT 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 320 LGVEDLIVVQTKDAILVTKHNAVQDVKKIVEELKTAGRSEYRIHREVYRPWGRCDSIDAGKRYEVKRIEVNPGEGISLQT 399
Cdd:PRK15460  323 VGVKDLVVVQTKDAVLIADRNAVQDVKKVVEQIKADGRHEHRVHREVYRPWGKYDSIDAGDRYQVKRITVKPGEGLSVQM 402

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1621529725 400 HFHRSEHWVVVAGTAKVTLEDKQFLLGENESVYIPVGAQHCLENPGKIPLEIIEVRSGPYLGDDDIVRIADRYGRV 475
Cdd:PRK15460  403 HHHRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLIEVRSGSYLEEDDVVRFADRYGRV 478
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-353 0e+00

Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 563.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725   1 MKIIPIIMAGGSGSRLWPLSRLTYPKQFLTLEGEQTMLQQTISRLSKL-EVECPVVICNEEHRFIVAEQLRQINALNeII 79
Cdd:COG0836     1 SMIYPVILAGGSGTRLWPLSRESYPKQFLPLLGEKSLLQQTVERLAGLvPPENILVVTNEEHRFLVAEQLPELGPAN-IL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725  80 LEPIGRNTAPAVALAAIQCLKDladNEDALLLILAADHIIKDNTAFINAIKISTSYAIDGNLVTFGIEPSSPETGFGYIQ 159
Cdd:COG0836    80 LEPVGRNTAPAIALAALLIAKR---DPDAVLLVLPADHLIEDEEAFREAVRAAVEAAEAGKLVTFGIKPTRPETGYGYIE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 160 AGDEISSGGVsgaFKVNAFVEKPERAVAEGFLSDGGYYWNSGMFMFGARKYLSELHKFCPDIYDSCSKAIQSPDKDLcFI 239
Cdd:COG0836   157 AGEALGGAGA---YKVKRFVEKPDLETAEEYLASGNYLWNSGMFVFRASTILEELERHAPEIYAALEAAVAAAGTDL-EV 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 240 RIDYDIFSRCPDLSIDYAVMEHTANAVVVPMSAGWSDVGSWSSLWDISVKDERGNVLIGDVIAHNSSNNYVHAQSGLVTM 319
Cdd:COG0836   233 RLDAEAFAALPSISIDYAVMEKADNVAVVPADFGWSDVGSWDALWELLEKDENGNVVLGDVLLIDSSNSLVRSEGRLVAV 312

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1621529725 320 LGVEDLIVVQTKDAILVTKHNAVQDVKKIVEELK 353
Cdd:COG0836   313 IGVEDLVVVDTPDALLVAPKDRAQEVKKIVEALK 346
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 3-283 8.70e-138

GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 397.33  E-value: 8.70e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725   3 IIPIIMAGGSGSRLWPLSRLTYPKQFLTLEGEQTMLQQTISRLSKL-EVECPVVICNEEHRFIVAEQLRQINALNEIILE 81
Cdd:cd02509     1 IYPVILAGGSGTRLWPLSRESYPKQFLKLFGDKSLLQQTLDRLKGLvPPDRILVVTNEEYRFLVREQLPEGLPEENIILE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725  82 PIGRNTAPAVALAAIQCLKDladNEDALLLILAADHIIKDNTAFINAIKISTSYAIDGNLVTFGIEPSSPETGFGYIQAG 161
Cdd:cd02509    81 PEGRNTAPAIALAALYLAKR---DPDAVLLVLPSDHLIEDVEAFLKAVKKAVEAAEEGYLVTFGIKPTRPETGYGYIEAG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 162 DEISsggvSGAFKVNAFVEKPERAVAEGFLSDGGYYWNSGMFMFGARKYLSELHKFCPDIYDSCSKAIQSPDKDLcFIRI 241
Cdd:cd02509   158 EKLG----GGVYRVKRFVEKPDLETAKEYLESGNYLWNSGIFLFRAKTFLEELKKHAPDIYEALEKALAAAGTDD-FLRL 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1621529725 242 DYDIFSRCPDLSIDYAVMEHTANAVVVPMSAGWSDVGSWSSL 283
Cdd:cd02509   233 LEEAFAKIPSISIDYAVMEKTKKVAVVPADFGWSDLGSWDAL 274
MannoseP_isomer pfam01050
Mannose-6-phosphate isomerase; All of the members of this Pfam entry belong to family 2 of the ...
 320-470 6.16e-87

Mannose-6-phosphate isomerase; All of the members of this Pfam entry belong to family 2 of the mannose-6-phosphate isomerases. The type II phosphomannose isomerases are bifunctional enzymes. This Pfam entry covers the isomerase domain. The guanosine diphospho-D-mannose pyrophosphorylase domain is in another Pfam entry, see pfam00483.


Pssm-ID: 426015 [Multi-domain]  Cd Length: 151  Bit Score: 262.74  E-value: 6.16e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 320 LGVEDLIVVQTKDAILVTKHNAVQDVKKIVEELKTAGRSEYRIHREVYRPWGRCDSIDAGKRYEVKRIEVNPGEGISLQT 399
Cdd:pfam01050   1 IGVENLVVVETKDALLVAHKDKVQDVKKVVEELKENGRSEHQTHREVYRPWGSYDVIDEGERYQVKRITVKPGARLSLQM 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621529725 400 HFHRSEHWVVVAGTAKVTLEDKQFLLGENESVYIPVGAQHCLENPGKIPLEIIEVRSGPYLGDDDIVRIAD 470
Cdd:pfam01050  81 HHHRAEHWIVVSGTARVTKGGETFLLTENESTYIPLGTIHRLENPGKIPLELIEVQSGSYLGEDDIVRFED 151
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 4-291 8.49e-77

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 240.23  E-value: 8.49e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725   4 IPIIMAGGSGSRLWPLSRLTYPKQFLTLEGEqTMLQQTISRLSKLEVECPVVICNEEHRFIVAEQLRQINALN---EIIL 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKY-PLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGvqiTYAL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725  81 EPIGRNTAPAVALAAiqclkDLADNEDALLLILAADHIIKDntAFINAIKISTSYAiDGNLVTFGIEPSSPETGFGYIQA 160
Cdd:pfam00483  80 QPEGKGTAPAVALAA-----DFLGDEKSDVLVLGGDHIYRM--DLEQAVKFHIEKA-ADATVTFGIVPVEPPTGYGVVEF 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 161 GDEissggvsgaFKVNAFVEKPERAVAEGFLSDGGYYWNSGMFMFgARKYLSELHKFCPDIYDSCSKAIQSPDKDLCFIR 240
Cdd:pfam00483 152 DDN---------GRVIRFVEKPKLPKASNYASMGIYIFNSGVLDF-LAKYLEELKRGEDEITDILPKALEDGKLAYAFIF 221

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1621529725 241 IDYdifsrcpdlsidyavmehtanavvvpmsaGWSDVGSWSSLWDISVKDE 291
Cdd:pfam00483 222 KGY-----------------------------AWLDVGTWDSLWEANLFLL 243
cupin_PMI_typeII_C cd02213
Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal ...
 342-468 6.75e-68

Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal cupin domain of mannose-6-phosphate isomerases (MPIs) which have been classified broadly into two groups, type I and type II, based on domain organization. This family contains type II phosphomannose isomerase (also known as PMI-GDP, phosphomannose isomerase/GDP-D-mannose pyrophosphorylase), a bifunctional enzyme with two domains that catalyze the first and third steps in the GDP-mannose pathway in which fructose 6-phosphate is converted to GDP-D-mannose. The N-terminal domain catalyzes the first and rate-limiting step, the isomerization from D-fructose-6-phosphate to D-mannose-6-phosphate, while the C-terminal cupin domain (represented in this alignment model) converts mannose 1-phosphate to GDP-D-mannose in the final step of the reaction. Although these two domains occur together in one protein in most organisms, they occur as separate proteins in certain cyanobacterial organisms. Also, although type I and type II MPIs have no overall sequence similarity, they share a conserved catalytic motif.


Pssm-ID: 380343 [Multi-domain]  Cd Length: 126  Bit Score: 213.19  E-value: 6.75e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 342 VQDVKKIVEELKTAGRSEYriHREVYRPWGRCDSIDAGKRYEVKRIEVNPGEGISLQTHFHRSEHWVVVAGTAKVTLEDK 421
Cdd:cd02213     2 SQRVKEIVEELKKRGRSEE--HRTVYRPWGSYEVLDEGEGYKVKRLTVNPGKRLSLQRHHHRSEHWVVVSGTAEVTLDGK 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1621529725 422 QFLLGENESVYIPVGAQHCLENPGKIPLEIIEVRSGPYLGDDDIVRI 468
Cdd:cd02213    80 EKLLKEGESIYIPKGTKHRLENPGKIPLEIIEVQTGEYLGEDDIVRL 126
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
368-467 1.34e-36

Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 130.65  E-value: 1.34e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 368 RPWGRCDSI-DAGKRYEVKRIEVNPGEGISLQTHFHRSEHWVVVAGTAKVTLEDKQFLLGENESVYIPVGAQHCLENPGK 446
Cdd:COG0662    12 IGWGSYEVLgEGGERLSVKRITVPPGAELSLHVHPHRDEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAGVPHRLRNPGD 91

                          90       100
                  ....*....|....*....|.
gi 1621529725 447 IPLEIIEVRSGPYLGDDDIVR 467
Cdd:COG0662    92 EPLELLEVQAPAYLGEDDIVR 112
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
 364-463 2.28e-12

Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to MJ1618, a Methanocaldococcus jannaschii protein of unknown function with a cupin beta barrel domain. The active site of members of the cupin superfamily is generally located at the center of a conserved barrel and usually includes a metal ion.


Pssm-ID: 380344 [Multi-domain]  Cd Length: 100  Bit Score: 62.92  E-value: 2.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 364 REVYRPwgrcdSIDAGKRYEVKRIEVNPGEGISLQTHFHRSEHWVVVAGTAKVTLEDKQFLLGENESVYIPVGAQHCLEN 443
Cdd:cd02214     6 RELLHP-----DNDGDPRYSLAHARVPPGESTLPHRLKGSEEVYYILEGEGTMEIDGEPREVGPGDAVLIPPGAVQRIEN 80

                          90       100
                  ....*....|....*....|
gi 1621529725 444 PGKIPLEIIEVRSGPYLGDD 463
Cdd:cd02214    81 TGEEDLVFLCICSPAWSPED 100
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
 377-452 1.02e-11

Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to Thermotoga maritima TM1459, a manganese-containing cupin that has been shown to cleave C=C bonds in the presence of alkylperoxide as oxidant in vitro. Its biological function is still unknown. This family also includes Halorhodospira halophila Hhal_0468. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer.


Pssm-ID: 380351 [Multi-domain]  Cd Length: 91  Bit Score: 60.93  E-value: 1.02e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1621529725 377 DAGKRYEVKRIEVNPGEGISLqtHFHRSEHWV-VVAGTAKVTLEDKQFLLGENESVYIPVGAQHCLENPGKIPLEII 452
Cdd:cd02222    12 DGAPNFAMRYFEIEPGGHTPL--HTHPWEHEVyVLRGKGVVVIGGEEYPVKPGDVVYIPPNEPHQFRNTGDEPLGFL 86
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 6-205 1.03e-10

NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 61.44  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725   6 IIMAGGSGSRLWPLSrLTYPKQFLTLEGeQTMLQQTISRLSKLEVECPVVICNEEHRFIVA--EQLRQINALNEIILEPI 83
Cdd:cd04181     2 VILAAGKGTRLRPLT-DTRPKPLLPIAG-KPILEYIIERLARAGIDEIILVVGYLGEQIEEyfGDGSKFGVNIEYVVQEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725  84 GRNTApavalAAIQCLKDLADNEDalLLILAADHIIKDN-TAFINAIKIStsyaidGNLVTFGIEPSSPETGFGYIQAGD 162
Cdd:cd04181    80 PLGTA-----GAVRNAEDFLGDDD--FLVVNGDVLTDLDlSELLRFHREK------GADATIAVKEVEDPSRYGVVELDD 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1621529725 163 EissggvsgaFKVNAFVEKPERAVaegflsdgGYYWNSGMFMF 205
Cdd:cd04181   147 D---------GRVTRFVEKPTLPE--------SNLANAGIYIF 172
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 386-454 1.36e-10

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 57.27  E-value: 1.36e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1621529725 386 RIEVNPGEGISLQTHFHRSEHWVVVAGTAKVTLEDKQFLLGENESVYIPVGAQHCLENPGKIPLEIIEV 454
Cdd:pfam07883   2 LVTLPPGESSPPHRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLLDV 70
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
379-454 2.53e-10

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 57.72  E-value: 2.53e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1621529725 379 GKRYEVKRIEVNPGEGISLqTHFHRS--EHWVVVAGTAKVTLEDKQFLLGENESVYIPVGAQHCLENPGKIPLEIIEV 454
Cdd:COG3837    25 LTRLGVNLITLPPGASSSP-YHAHSAeeEFVYVLEGELTLRIGGEEYVLEPGDSVGFPAGVPHRLRNRGDEPARYLVV 101
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
376-454 6.76e-10

Cupin domain protein related to quercetin dioxygenase [General function prediction only];


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 56.01  E-value: 6.76e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1621529725 376 IDAGKRYEVKRIEVNPGEGISLQTHfHRSEHWVVVAGTAKVTLEDKQFLLGENESVYIPVGAQHCLENPGKIPLEIIEV 454
Cdd:COG1917    17 ADGEDELEVVRVTFEPGARTPWHSH-PGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAFRNLGDEPAVLLVV 94
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 386-455 1.82e-08

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.


Pssm-ID: 380338 [Multi-domain]  Cd Length: 73  Bit Score: 51.33  E-value: 1.82e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621529725 386 RIEVNPGEGISLQTHFHRSEHWVVVAGTAKVTLED-KQFLLGENESVYIPVGAQHCLENPGKIPLEIIEVR 455
Cdd:cd02208     3 VVTLPPGTSSPPHWHPEQDEIFYVLSGEGELTLDDgETVELKAGDIVLIPPGVPHSFVNTSDEPAVFLVVS 73
cupin_Bh2720-like cd02223
Bacillus halodurans Bh2720 and related proteins, cupin domain; This family includes bacterial, ...
 389-451 1.87e-08

Bacillus halodurans Bh2720 and related proteins, cupin domain; This family includes bacterial, archaeal, and eukaryotic proteins similar to Bh2720, a Bacillus halodurans protein of unknown function with a cupin beta-barrel fold.


Pssm-ID: 380352 [Multi-domain]  Cd Length: 98  Bit Score: 51.78  E-value: 1.87e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1621529725 389 VNPGEGISLQTHFHRSEHWVVVAGTAKVTLEDKQFLLGENESVYIPVGAQHCLENPGKIPLEI 451
Cdd:cd02223    18 IPPGEDIGLEVHDDVDQFLRIEEGEGKAIMGGFESEVKDGDAIIVPAGTWHNVINTGNEPLKL 80
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 387-470 6.38e-08

Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate transport and metabolism]; Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 441743 [Multi-domain]  Cd Length: 115  Bit Score: 50.74  E-value: 6.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 387 IEVNPGEGISLQTHFHRSEHWVVVAGTAKVTLEDKQ-----FLLGENESVYIPVGAQHCLENPGKIPLEIIEVRSGPYLG 461
Cdd:COG2140     8 TVLEPGGVREEHWHPNAAEWYYVLSGEARMTVQDPPgrartVDVGPGDVVYVPPGYGHYIINTGDEPLVFLAVFDDDAGS 87


                  ....*....
gi 1621529725 462 DDDIVRIAD 470
Cdd:COG2140    88 DYGTISLSG 96
cupin_TcmJ-like cd06991
TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of ...
 387-452 7.65e-08

TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of the tetracenomycin (TCM) polyketide synthase (PKS) type II complex in Streptomyces glaucescens. TcmJ is a quinone-forming monooxygenase involved in the modification of aromatic polyketides synthesized by polyketide synthases of types II and III. Orthologs of TcmJ include the Streptomyces BenD (benastatin biosynthetic pathway), the Streptomyces olivaceus ElmJ (polyketide antibiotic elloramycin biosynthetic pathway), the Actinomadura hibisca PdmL (pradimicin biosynthetic pathway), the Streptomyces cyaneus CurC (curamycin biosynthetic pathway), the Streptomyces rishiriensis Lct30 (lactonamycin biosynthetic pathway), and the Streptomyces WhiE II (spore pigment polyketide biosynthetic pathway). Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380396 [Multi-domain]  Cd Length: 105  Bit Score: 50.37  E-value: 7.65e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1621529725 387 IEVNPGEGISLQTHFHRSEHWVVVAGTAKVTLEDKQFLLGENESVYIPVGAQHCLENPGKIPLEII 452
Cdd:cd06991    24 LTLAPGERVSEHYHPYSEEFLYVVRGRLVVRVDGEPVVLEAGEALLVPRGVRHRLENAGDEPARLV 89
cupin_XRE_C cd02209
XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; ...
 377-452 1.00e-07

XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; This family contains transcriptional regulators containing an N-terminal XRE (Xenobiotic Response Element) family helix-turn-helix (HTH) DNA-binding domain and a C-terminal cupin domain. Included in this family is Escherichia coli transcription factor SutR (YdcN) that plays a regulatory role in sulfur utilization; it regulates a set of genes involved in the generation of sulfate and its reduction, the synthesis of cysteine, the synthesis of enzymes containing Fe-S as cofactors, and the modification of tRNA with use of sulfur-containing substrates. This family belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380339 [Multi-domain]  Cd Length: 90  Bit Score: 49.43  E-value: 1.00e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1621529725 377 DAGKRYEVKRIEVNPGEGiSLQTHFHRS-EHWVVVAGTAKVTLEDKQFLLGENESVYIPVGAQHCLENPGKIPLEII 452
Cdd:cd02209    11 LPGRKMEPFLVTLPPGGS-GGEPYSHEGeEFGYVLEGELELTVGGETYVLEAGDSIYFDSDVPHRYRNPGDEPARVL 86
cupin_TM1287-like cd02221
Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial ...
 386-452 1.27e-07

Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial proteins homologous to TM1287 decarboxylase, a Thermotoga maritima manganese-containing cupin thought to catalyze the conversion of oxalate to formate and carbon dioxide, due to its similarity to oxalate decarboxylase (OXDC) from Bacillus subtilis. TM1287 shows a cupin fold with a conserved "jelly roll-like" beta-barrel fold and forms a homodimer.


Pssm-ID: 380350 [Multi-domain]  Cd Length: 93  Bit Score: 49.39  E-value: 1.27e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1621529725 386 RIEVNPGEGISLQTHFHRSEHWVVVAGTAKVTLEDKQFLLGENESVYIPVGAQHCLENPGKIPLEII 452
Cdd:cd02221    23 RVTLPPGSSIGYHQHEGEFEIYYILSGEGLYTDNGKEYEVKAGDVTFTRDGESHGIENTGDEDLVFI 89
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 6-112 3.57e-07

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 50.99  E-value: 3.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725   6 IIMAGGSGSRLwplsRLTYPKQFLTLEGeQTMLQQTISRLSKL-EVECPVVICNEEHRFIVAEQLRQINALNEIILEPiG 84
Cdd:cd02516     4 IILAAGSGSRM----GADIPKQFLELGG-KPVLEHTLEAFLAHpAIDEIVVVVPPDDIDLAKELAKYGLSKVVKIVEG-G 77

                          90       100
                  ....*....|....*....|....*...
gi 1621529725  85 RNTAPAVALAaiqcLKDLADNEDALLLI 112
Cdd:cd02516    78 ATRQDSVLNG----LKALPDADPDIVLI 101
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 6-74 7.76e-07

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440824  Cd Length: 224  Bit Score: 49.74  E-value: 7.76e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725   6 IIMAGGSGSRLwplsRLTYPKQFLTLEGeQTMLQQTISRLSKL-EVECPVVICNEEHRFIVAEQLRQINA 74
Cdd:COG1211     1 IIPAAGSGSRM----GAGIPKQFLPLGG-KPVLEHTLEAFLAHpRIDEIVVVVPPDDIEYFEELLAKYGI 65
cupin_DddK cd06988
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ...
 387-454 9.17e-07

Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes mostly bacterial proteins homologous to dimethylsulfoniopropionate lyase DddK from marine bacterium Pelagibacter. DddK cleaves dimethylsulfoniopropionate (DMSP), the organic osmolyte and antioxidant produced in marine environments, and yields acrylate and the climate-active gas dimethyl sulfide (DMS). DddK contains a double-stranded beta-helical motif which utilizes various divalent metal ions as cofactors for catalytic activity; however, nickel, an abundant metal ion in marine environments, confers the highest DMSP lyase activity. Also included in this family is Plu4264, a Photorhabdus luminescens manganese-containing cupin shown to have similar metal binding site to TM1287 decarboxylase, but two very different substrate binding pockets. The Plu4264 binding pocket shows a cavity and substrate entry point more than twice as large as and more hydrophobic than TM1287, suggesting that Plu4264 accepts a substrate that is significantly larger than that of TM1287, a putative oxalate decarboxylase. Thus, the function of Plu4264 could be similar to that of TM1287 but with a larger, less charged substrate. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380393 [Multi-domain]  Cd Length: 76  Bit Score: 46.46  E-value: 9.17e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1621529725 387 IEVNPGEGISLQTHfHRSEHWVVVAGTAKVTLEDKQFLLGENESVYIPVGAQHCLENPGKIPLEIIEV 454
Cdd:cd06988     7 CVVRPGTTSTPHSH-HEYEIFIVISGKGIVVVDGEREPVKAGDVVYIPPGTEHYVKNDGDEDFEFYSI 73
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
 385-459 6.16e-06

Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds and both domains are included in this alignment. Each OxDC cupin domain contains one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380367 [Multi-domain]  Cd Length: 145  Bit Score: 45.93  E-value: 6.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 385 KRIEVNPGeGISlQTHFHRSEH-W-VVVAGTAKVTLEDKQ-----FLLGENESVYIPVGAQHCLENPGKIPLEIIEV-RS 456
Cdd:cd02240    30 ALVRVAPG-AMR-ELHWHPNTAeWqYVISGSARVTVFDEDgrfetFNLGAGDVGYVPSGSGHHIENIGDEDAEFLLIfDD 107


                  ...
gi 1621529725 457 GPY 459
Cdd:cd02240   108 GTF 110
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 6-205 9.81e-06

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 46.68  E-value: 9.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725   6 IIMAGGSGSRLWPLSRLTyPKQFLTLeGEQTMLQQTISRLSKLEVEcpvvicneehRFIV-----AEQLRqiNALN---- 76
Cdd:COG1208     3 VILAGGLGTRLRPLTDTR-PKPLLPV-GGKPLLEHILERLAAAGIT----------EIVInvgylAEQIE--EYFGdgsr 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725  77 -----EIILEPIGRNTAPAVALAAiqclkDLADNEDalLLILAADHIIKDN-TAFINAikistsYAIDGNLVTFGIEPSS 150
Cdd:COG1208    69 fgvriTYVDEGEPLGTGGALKRAL-----PLLGDEP--FLVLNGDILTDLDlAALLAF------HREKGADATLALVPVP 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1621529725 151 PETGFGYIqagdEISSGGvsgafKVNAFVEKPERAVaegflsdgGYYWNSGMFMF 205
Cdd:COG1208   136 DPSRYGVV----ELDGDG-----RVTRFVEKPEEPP--------SNLINAGIYVL 173
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
1-62 9.92e-06

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 46.67  E-value: 9.92e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1621529725   1 MKIIPIIMAGGSGSRLwplsRLTYPKQFLTLEGeQTMLQQTISRLSKL-EVECPVVICNEEHR 62
Cdd:PRK00155    2 MMVYAIIPAAGKGSRM----GADRPKQYLPLGG-KPILEHTLEAFLAHpRIDEIIVVVPPDDR 59
AllE COG3257
Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];
387-455 5.05e-05

Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 442488 [Multi-domain]  Cd Length: 262  Bit Score: 44.81  E-value: 5.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 387 IEVNPGEGISLQTHFHRSEHWV-VVAGTAKVTLEDKQFLLGENESVYIPVGAQHCLENPGKIPLEIIEVR 455
Cdd:COG3257    64 VEVAPGGGSDRPEPDPGAETFLfVLEGEVTLTLGGETHELTPGGYAYLPPGTPWTLRNAGDEPARFHWIR 133
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-120 5.76e-05

dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 44.70  E-value: 5.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725   1 MKIIpiIMAGGSGSRLWPLSrLTYPKQFLTLEGeQTMLQQTISRLSKLEVECPVVICNEEHRFIVAEQLRQINALN---E 77
Cdd:COG1209     1 MKGI--ILAGGSGTRLRPLT-LTVSKQLLPVYD-KPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGikiS 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1621529725  78 IILEPIGRNTAPAVALAaiqclKDLADNEDAlLLILaADHIIK 120
Cdd:COG1209    77 YAVQPEPLGLAHAFIIA-----EDFIGGDPV-ALVL-GDNIFY 112
cupin_TTHA0104 cd06122
Thermus thermophilus TTHA0104 and related proteins, cupin domain; This family contains ...
 391-449 2.76e-04

Thermus thermophilus TTHA0104 and related proteins, cupin domain; This family contains bacterial proteins including TTHA0104 (also called TT1209), a putative antibiotic synthesis protein from Thermus thermophilus. TTHA0104 is a cupin-like protein. The cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin (cupa is the Latin term for small barrel).


Pssm-ID: 380377 [Multi-domain]  Cd Length: 102  Bit Score: 40.23  E-value: 2.76e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1621529725 391 PGEGISLQTHFHRSEHWVVVAGTAKVTLEDKQFLLGENESVYIPVGAQHCLENPGKIPL 449
Cdd:cd06122    36 PGQSQKVHAHAGSDKVYFVLEGEGRFTVGDEERELGAGEAVLAPAGVPHGVRNTGAERL 94
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-114 3.38e-04

CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 41.68  E-value: 3.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725   1 MKIIPIIMAGGSGsrlwplSRLTYPKQFLTLEGEqTMLQQTISRLSKLEVECPVVICNEEHRfIVAEQLRQINAlnEIIl 80
Cdd:COG2068     2 SKVAAIILAAGAS------SRMGRPKLLLPLGGK-PLLERAVEAALAAGLDPVVVVLGADAE-EVAAALAGLGV--RVV- 70

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1621529725  81 epigRNTAPAVALAA-IQC-LKDLADNEDALLLILA 114
Cdd:COG2068    71 ----VNPDWEEGMSSsLRAgLAALPADADAVLVLLG 102
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 6-117 3.43e-04

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 41.03  E-value: 3.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725   6 IIMAGGSGsrlwplSRLTYPKQFLTLEGeQTMLQQTISRLSKLEVECpVVICNEEHrfiVAEQLRQINAlnEIILEPIgR 85
Cdd:pfam12804   2 VILAGGRS------SRMGGDKALLPLGG-KPLLERVLERLRPAGDEV-VVVANDEE---VLAALAGLGV--PVVPDPD-P 67

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1621529725  86 NTAPAVALAAiqCLKDLADNEdaLLLILAADH 117
Cdd:pfam12804  68 GQGPLAGLLA--ALRAAPGAD--AVLVLACDM 95
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 6-72 4.18e-04

MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 41.02  E-value: 4.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1621529725   6 IIMAGGSGsrlwplSRLTYPKQFLTLEGeQTMLQQTISRLSKLEVECpVVICNEEHRFIVAEQLRQI 72
Cdd:cd02503     4 VILAGGKS------RRMGGDKALLELGG-KPLLEHVLERLKPLVDEV-VISANRDQERYALLGVPVI 62
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 372-452 7.69e-04

Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and eukaryotic cupin domains of proteins homologous to oxalate decarboxylase (OxDC; EC 4.1.1.2) such as MSMEG_2254, a putative OxDC from Mycobacterium smegmatis. OxDC is a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds with each domain containing one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues.


Pssm-ID: 380440 [Multi-domain]  Cd Length: 151  Bit Score: 39.88  E-value: 7.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 372 RCDSIDAGKRYEVKRIEVNPGeGIslqthfhRSEHW--------VVVAGTAKVTLED-----KQFLLGENESVYIPVGAQ 438
Cdd:cd20306    24 TADQLPVLKGLSIYRLRLSPG-GI-------REPHWhpnanelgYVISGEARVSILDptgslDTFTVKPGQVVFIPQGWL 95

                          90
                  ....*....|....
gi 1621529725 439 HCLENPGKIPLEII 452
Cdd:cd20306    96 HWIENVGDEEAHLL 109
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-117 1.13e-03

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 39.85  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725   3 IIPIIMAGGSGsrlwplSRLTYPKQFLTLEGeQTMLQQTISRLSKLEVECPVVICNEEhrfivAEQLRQinALNEIILEP 82
Cdd:cd04182     1 IAAIILAAGRS------SRMGGNKLLLPLDG-KPLLRHALDAALAAGLSRVIVVLGAE-----ADAVRA--ALAGLPVVV 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1621529725  83 IgRNTAPA------VAlAAIQCLKDLADNedalLLILAADH 117
Cdd:cd04182    67 V-INPDWEegmsssLA-AGLEALPADADA----VLILLADQ 101
cupin_YP766765-like cd20299
Rhizobium leguminosarum YP_766765.1 and related proteins, cupin domain; This family includes ...
 403-445 1.77e-03

Rhizobium leguminosarum YP_766765.1 and related proteins, cupin domain; This family includes mostly bacterial proteins homologous to Rhizobium leguminosarum YP_766765.1, a protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380433 [Multi-domain]  Cd Length: 90  Bit Score: 37.65  E-value: 1.77e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1621529725 403 RSEHWVVVAGTAKVTLEDKQFLLGENESVYIPVGAQHCLENPG 445
Cdd:cd20299    37 REKVYVVLEGELTVTTDGEEVVLGPGDSCYIPPGETRSIDNRT 79
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-63 2.73e-03

Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 39.02  E-value: 2.73e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1621529725   1 MKIIPIIMAGGSGSRLWplsrltYPKQFLTLEGeQTMLQQTISRLSKL--EVecpVVICNEEHRF 63
Cdd:COG0746     3 MPITGVILAGGRSRRMG------QDKALLPLGG-RPLLERVLERLRPQvdEV---VIVANRPERY 57
cupin_UGlyAH_N cd02211
(S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain; This family ...
 391-455 3.99e-03

(S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain; This family includes the N-terminal cupin domain of (S)-ureidoglycine aminohydrolase (UGlyAH), an enzyme that converts (S)-ureidoglycine into (S)-ureidoglycolate and ammonia, providing the final substrate to the ureide pathway. The ureide pathway has recently been identified as the metabolic route of purine catabolism in plants and some bacteria where, uric acid, which is a major product of the early stage of purine catabolism, is degraded into glyoxylate and ammonia via stepwise reactions by seven different enzymes. Thus, this pathway has a possible physiological role in mobilization of purine ring nitrogen for further assimilation. This enzyme from Arabidopsis thaliana(AtUGlyAH) has been shown to bind a Mn2+ ion, via the C-terminal cupin domain, which acts as a molecular anchor to bind (S)-ureidoglycine, and its binding mode dictates the enantioselectivity of the reaction. The structure of AtUGlyAH shows a bi-cupin fold with a conserved "jelly roll-like" beta-barrel fold and an octameric functional unit. Several structural homologs of UGlyAH, including the Escherichia coli ortholog YlbA (also known as GlxB6), also exhibit similar features.


Pssm-ID: 380341 [Multi-domain]  Cd Length: 117  Bit Score: 37.11  E-value: 3.99e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1621529725 391 PGEGIslqthfhrsEHWV-VVAGTAKVTLEDKQFLLGENESVYIPVGAQHCLENPGKIPLEIIEVR 455
Cdd:cd02211    43 GGEGI---------ERFLyVLEGEVELTVGGETHTLTAGGYAYLPPGTKHSLRNAGDEPARLLWYK 99
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 6-45 6.33e-03

NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133048 [Multi-domain]  Cd Length: 220  Bit Score: 38.26  E-value: 6.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1621529725   6 IIMAGGSGSRLWPLSRLTyPKQFLTLeGEQTMLQQTISRL 45
Cdd:cd06426     2 VIMAGGKGTRLRPLTENT-PKPMLKV-GGKPILETIIDRF 39
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
6-56 7.28e-03

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 37.91  E-value: 7.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1621529725   6 IIMAGGSGSRLWPLSRlTYPKQFLTLEGeQTMLQQTISRLSKLEVEcPVVI 56
Cdd:COG1213     3 VILAAGRGSRLGPLTD-DIPKCLVEIGG-KTLLERQLEALAAAGIK-DIVV 50
PRK11171 PRK11171
(S)-ureidoglycine aminohydrolase;
387-455 8.31e-03

(S)-ureidoglycine aminohydrolase;


Pssm-ID: 183011 [Multi-domain]  Cd Length: 266  Bit Score: 37.96  E-value: 8.31e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621529725 387 IEVNPGEGISLQTHFHRSEHWV-VVAGTAKVTLEDKQFLLGENESVYIPVGAQHCLENPGKIPLEIIEVR 455
Cdd:PRK11171   66 VEVEPGGGSDQPEPDEGAETFLfVVEGEITLTLEGKTHALSEGGYAYLPPGSDWTLRNAGAEDARFHWIR 135
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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