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Conserved domains on  [gi|489510344|ref|WP_003415201|]
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MULTISPECIES: mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase [Pseudomonas]

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 ...
 1-468 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: 816.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344    1 MIPVILSGGSGSRLWPLSRKQFPKQFLALTGEHTLFQQTLERLVFEGMQEPIVVCNKDHRFIVNEQLAALNLETQAILME 80
Cdd:TIGR01479   1 IIPVILAGGSGTRLWPLSRELYPKQFLALVGDLTMLQQTLKRLAGLPCSSPLVICNEEHRFIVAEQLREIGKLASNIILE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344   81 PFGRNTAPAVALTAMKLV-NEGNDGLMLVLPADHVIEDQKALQRALALATVAAERGEMVLFGVPANKPETGYGYIKSTAd 159
Cdd:TIGR01479  81 PVGRNTAPAIALAALLAArRNGEDPLLLVLAADHVITDEDAFQAAVKLAMPAAAEGKLVTFGIVPTHPETGYGYIRRGA- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344  160 ALLPEGVSRVSQFVEKPDEKRAKEFVEAGGYYWNSGMFLFRASRFLEELKKHDPDIYDTCLLTLERSVQDGDALEIDSST 239
Cdd:TIGR01479 160 PLAGEDVYQVQRFVEKPDLATAQAYLESGDYYWNSGMFLFRASRYLAELKKHAPDIYEACEAAVEASEPDLDFIRLDKEA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344  240 FACCPDNSIDYAVMEKTQRACVVPLSAGWSDVGCWSSLWEVNAKDANGNVTKGDVVIQDSRNCMIHGNGKLVSVIGLDNI 319
Cdd:TIGR01479 240 FEQCPSESIDYAVMEKTADAVVVPMDAGWSDVGSWSALWEISDKDADGNVLKGDVLTHDTKNSYIYSESRLVAVVGVEDL 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344  320 VVVETKDAMMIAHKDKVQGVKQMVATLNEQGRTETQNHLEVYRPWGSYDSVDMGGRFQVKRISVKPGACLSLQMHHHRAE 399
Cdd:TIGR01479 320 VVVETKDAVLVAHKDRVQDVKKIVEQLKADGRTETEQHREVYRPWGKYDSIDQGDRYQVKRITVKPGEKLSLQMHHHRAE 399

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489510344  400 HWIVVSGTAQVTCDENVFLLTENQSTYIPIASVHRLRNPGKIPLEIIEVQSGSYLGEDDIERFEDIYGR 468
Cdd:TIGR01479 400 HWIVVSGTARVTIGDETLLLTENESTYIPLGVIHRLENPGKIPLELIEVQSGSYLGEDDIIRFEDRYGR 468
 
Name Accession Description Interval E-value
GMP_PMI TIGR01479
mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to ...
 1-468 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: 816.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344    1 MIPVILSGGSGSRLWPLSRKQFPKQFLALTGEHTLFQQTLERLVFEGMQEPIVVCNKDHRFIVNEQLAALNLETQAILME 80
Cdd:TIGR01479   1 IIPVILAGGSGTRLWPLSRELYPKQFLALVGDLTMLQQTLKRLAGLPCSSPLVICNEEHRFIVAEQLREIGKLASNIILE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344   81 PFGRNTAPAVALTAMKLV-NEGNDGLMLVLPADHVIEDQKALQRALALATVAAERGEMVLFGVPANKPETGYGYIKSTAd 159
Cdd:TIGR01479  81 PVGRNTAPAIALAALLAArRNGEDPLLLVLAADHVITDEDAFQAAVKLAMPAAAEGKLVTFGIVPTHPETGYGYIRRGA- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344  160 ALLPEGVSRVSQFVEKPDEKRAKEFVEAGGYYWNSGMFLFRASRFLEELKKHDPDIYDTCLLTLERSVQDGDALEIDSST 239
Cdd:TIGR01479 160 PLAGEDVYQVQRFVEKPDLATAQAYLESGDYYWNSGMFLFRASRYLAELKKHAPDIYEACEAAVEASEPDLDFIRLDKEA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344  240 FACCPDNSIDYAVMEKTQRACVVPLSAGWSDVGCWSSLWEVNAKDANGNVTKGDVVIQDSRNCMIHGNGKLVSVIGLDNI 319
Cdd:TIGR01479 240 FEQCPSESIDYAVMEKTADAVVVPMDAGWSDVGSWSALWEISDKDADGNVLKGDVLTHDTKNSYIYSESRLVAVVGVEDL 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344  320 VVVETKDAMMIAHKDKVQGVKQMVATLNEQGRTETQNHLEVYRPWGSYDSVDMGGRFQVKRISVKPGACLSLQMHHHRAE 399
Cdd:TIGR01479 320 VVVETKDAVLVAHKDRVQDVKKIVEQLKADGRTETEQHREVYRPWGKYDSIDQGDRYQVKRITVKPGEKLSLQMHHHRAE 399

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489510344  400 HWIVVSGTAQVTCDENVFLLTENQSTYIPIASVHRLRNPGKIPLEIIEVQSGSYLGEDDIERFEDIYGR 468
Cdd:TIGR01479 400 HWIVVSGTARVTIGDETLLLTENESTYIPLGVIHRLENPGKIPLELIEVQSGSYLGEDDIIRFEDRYGR 468
cpsB PRK15460
mannose-1-phosphate guanyltransferase; Provisional
 1-468 0e+00

mannose-1-phosphate guanyltransferase; Provisional


Pssm-ID: 185357 [Multi-domain]  Cd Length: 478  Bit Score: 600.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344   1 MIPVILSGGSGSRLWPLSRKQFPKQFLALTGEHTLFQQTLERLVFEGMQEPIVVCNKDHRFIVNEQLAALNLETQAILME 80
Cdd:PRK15460   6 LYPVVMAGGSGSRLWPLSRVLYPKQFLCLKGDLTMLQTTICRLNGVECESPVVICNEQHRFIVAEQLRQLNKLTENIILE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344  81 PFGRNTAPAVALTAMKLVNEG--NDGLMLVLPADHVIEDQKALQRALALATVAAERGEMVLFGVPANKPETGYGYIKStA 158
Cdd:PRK15460  86 PAGRNTAPAIALAALAAKRHSpeSDPLMLVLAADHVIADEDAFRAAVRNAMPYAEAGKLVTFGIVPDLPETGYGYIRR-G 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344 159 DALLPEGVS---RVSQFVEKPDEKRAKEFVEAGGYYWNSGMFLFRASRFLEELKKHDPDIYDTCLLTLERSVQDGDALEI 235
Cdd:PRK15460 165 EVSAGEQDTvafEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDPDLDFIRV 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344 236 DSSTFACCPDNSIDYAVMEKTQRACVVPLSAGWSDVGCWSSLWEVNAKDANGNVTKGDVVIQDSRNCMIHGNGKLVSVIG 315
Cdd:PRK15460 245 DEEAFLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSLWEISAHTAEGNVCHGDVINHKTENSYVYAESGLVTTVG 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344 316 LDNIVVVETKDAMMIAHKDKVQGVKQMVATLNEQGRTETQNHLEVYRPWGSYDSVDMGGRFQVKRISVKPGACLSLQMHH 395
Cdd:PRK15460 325 VKDLVVVQTKDAVLIADRNAVQDVKKVVEQIKADGRHEHRVHREVYRPWGKYDSIDAGDRYQVKRITVKPGEGLSVQMHH 404

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489510344 396 HRAEHWIVVSGTAQVTCDENVFLLTENQSTYIPIASVHRLRNPGKIPLEIIEVQSGSYLGEDDIERFEDIYGR 468
Cdd:PRK15460 405 HRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLIEVRSGSYLEEDDVVRFADRYGR 477
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-348 0e+00

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 558.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344   1 MIPVILSGGSGSRLWPLSRKQFPKQFLALTGEHTLFQQTLERLV-FEGMQEPIVVCNKDHRFIVNEQLAALNLEtqAILM 79
Cdd:COG0836    3 IYPVILAGGSGTRLWPLSRESYPKQFLPLLGEKSLLQQTVERLAgLVPPENILVVTNEEHRFLVAEQLPELGPA--NILL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344  80 EPFGRNTAPAVALTAMKLVNEGNDGLMLVLPADHVIEDQKALQRALALATVAAERGEMVLFGVPANKPETGYGYIKsTAD 159
Cdd:COG0836   81 EPVGRNTAPAIALAALLIAKRDPDAVLLVLPADHLIEDEEAFREAVRAAVEAAEAGKLVTFGIKPTRPETGYGYIE-AGE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344 160 ALLPEGVSRVSQFVEKPDEKRAKEFVEAGGYYWNSGMFLFRASRFLEELKKHDPDIYDTCLLTLERSVQDGDaLEIDSST 239
Cdd:COG0836  160 ALGGAGAYKVKRFVEKPDLETAEEYLASGNYLWNSGMFVFRASTILEELERHAPEIYAALEAAVAAAGTDLE-VRLDAEA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344 240 FACCPDNSIDYAVMEKTQRACVVPLSAGWSDVGCWSSLWEVNAKDANGNVTKGDVVIQDSRNCMIHGNGKLVSVIGLDNI 319
Cdd:COG0836  239 FAALPSISIDYAVMEKADNVAVVPADFGWSDVGSWDALWELLEKDENGNVVLGDVLLIDSSNSLVRSEGRLVAVIGVEDL 318

                        330       340
                 ....*....|....*....|....*....
gi 489510344 320 VVVETKDAMMIAHKDKVQGVKQMVATLNE 348
Cdd:COG0836  319 VVVDTPDALLVAPKDRAQEVKKIVEALKE 347
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-277 5.00e-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: 398.10  E-value: 5.00e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344   1 MIPVILSGGSGSRLWPLSRKQFPKQFLALTGEHTLFQQTLERLV-FEGMQEPIVVCNKDHRFIVNEQLAALNLETQaILM 79
Cdd:cd02509    1 IYPVILAGGSGTRLWPLSRESYPKQFLKLFGDKSLLQQTLDRLKgLVPPDRILVVTNEEYRFLVREQLPEGLPEEN-IIL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344  80 EPFGRNTAPAVALTAMKLVNEGNDGLMLVLPADHVIEDQKALQRALALATVAAERGEMVLFGVPANKPETGYGYIKstAD 159
Cdd:cd02509   80 EPEGRNTAPAIALAALYLAKRDPDAVLLVLPSDHLIEDVEAFLKAVKKAVEAAEEGYLVTFGIKPTRPETGYGYIE--AG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344 160 ALLPEGVSRVSQFVEKPDEKRAKEFVEAGGYYWNSGMFLFRASRFLEELKKHDPDIYDTCLLTLeRSVQDGDALEIDSST 239
Cdd:cd02509  158 EKLGGGVYRVKRFVEKPDLETAKEYLESGNYLWNSGIFLFRAKTFLEELKKHAPDIYEALEKAL-AAAGTDDFLRLLEEA 236

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 489510344 240 FACCPDNSIDYAVMEKTQRACVVPLSAGWSDVGCWSSL 277
Cdd:cd02509  237 FAKIPSISIDYAVMEKTKKVAVVPADFGWSDLGSWDAL 274
MannoseP_isomer pfam01050
Mannose-6-phosphate isomerase; All of the members of this Pfam entry belong to family 2 of the ...
 314-464 8.24e-101

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: 298.56  E-value: 8.24e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344  314 IGLDNIVVVETKDAMMIAHKDKVQGVKQMVATLNEQGRTETQNHLEVYRPWGSYDSVDMGGRFQVKRISVKPGACLSLQM 393
Cdd:pfam01050   1 IGVENLVVVETKDALLVAHKDKVQDVKKVVEELKENGRSEHQTHREVYRPWGSYDVIDEGERYQVKRITVKPGARLSLQM 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489510344  394 HHHRAEHWIVVSGTAQVTCDENVFLLTENQSTYIPIASVHRLRNPGKIPLEIIEVQSGSYLGEDDIERFED 464
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 ...
 1-468 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: 816.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344    1 MIPVILSGGSGSRLWPLSRKQFPKQFLALTGEHTLFQQTLERLVFEGMQEPIVVCNKDHRFIVNEQLAALNLETQAILME 80
Cdd:TIGR01479   1 IIPVILAGGSGTRLWPLSRELYPKQFLALVGDLTMLQQTLKRLAGLPCSSPLVICNEEHRFIVAEQLREIGKLASNIILE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344   81 PFGRNTAPAVALTAMKLV-NEGNDGLMLVLPADHVIEDQKALQRALALATVAAERGEMVLFGVPANKPETGYGYIKSTAd 159
Cdd:TIGR01479  81 PVGRNTAPAIALAALLAArRNGEDPLLLVLAADHVITDEDAFQAAVKLAMPAAAEGKLVTFGIVPTHPETGYGYIRRGA- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344  160 ALLPEGVSRVSQFVEKPDEKRAKEFVEAGGYYWNSGMFLFRASRFLEELKKHDPDIYDTCLLTLERSVQDGDALEIDSST 239
Cdd:TIGR01479 160 PLAGEDVYQVQRFVEKPDLATAQAYLESGDYYWNSGMFLFRASRYLAELKKHAPDIYEACEAAVEASEPDLDFIRLDKEA 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344  240 FACCPDNSIDYAVMEKTQRACVVPLSAGWSDVGCWSSLWEVNAKDANGNVTKGDVVIQDSRNCMIHGNGKLVSVIGLDNI 319
Cdd:TIGR01479 240 FEQCPSESIDYAVMEKTADAVVVPMDAGWSDVGSWSALWEISDKDADGNVLKGDVLTHDTKNSYIYSESRLVAVVGVEDL 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344  320 VVVETKDAMMIAHKDKVQGVKQMVATLNEQGRTETQNHLEVYRPWGSYDSVDMGGRFQVKRISVKPGACLSLQMHHHRAE 399
Cdd:TIGR01479 320 VVVETKDAVLVAHKDRVQDVKKIVEQLKADGRTETEQHREVYRPWGKYDSIDQGDRYQVKRITVKPGEKLSLQMHHHRAE 399

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489510344  400 HWIVVSGTAQVTCDENVFLLTENQSTYIPIASVHRLRNPGKIPLEIIEVQSGSYLGEDDIERFEDIYGR 468
Cdd:TIGR01479 400 HWIVVSGTARVTIGDETLLLTENESTYIPLGVIHRLENPGKIPLELIEVQSGSYLGEDDIIRFEDRYGR 468
cpsB PRK15460
mannose-1-phosphate guanyltransferase; Provisional
 1-468 0e+00

mannose-1-phosphate guanyltransferase; Provisional


Pssm-ID: 185357 [Multi-domain]  Cd Length: 478  Bit Score: 600.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344   1 MIPVILSGGSGSRLWPLSRKQFPKQFLALTGEHTLFQQTLERLVFEGMQEPIVVCNKDHRFIVNEQLAALNLETQAILME 80
Cdd:PRK15460   6 LYPVVMAGGSGSRLWPLSRVLYPKQFLCLKGDLTMLQTTICRLNGVECESPVVICNEQHRFIVAEQLRQLNKLTENIILE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344  81 PFGRNTAPAVALTAMKLVNEG--NDGLMLVLPADHVIEDQKALQRALALATVAAERGEMVLFGVPANKPETGYGYIKStA 158
Cdd:PRK15460  86 PAGRNTAPAIALAALAAKRHSpeSDPLMLVLAADHVIADEDAFRAAVRNAMPYAEAGKLVTFGIVPDLPETGYGYIRR-G 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344 159 DALLPEGVS---RVSQFVEKPDEKRAKEFVEAGGYYWNSGMFLFRASRFLEELKKHDPDIYDTCLLTLERSVQDGDALEI 235
Cdd:PRK15460 165 EVSAGEQDTvafEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDPDLDFIRV 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344 236 DSSTFACCPDNSIDYAVMEKTQRACVVPLSAGWSDVGCWSSLWEVNAKDANGNVTKGDVVIQDSRNCMIHGNGKLVSVIG 315
Cdd:PRK15460 245 DEEAFLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSLWEISAHTAEGNVCHGDVINHKTENSYVYAESGLVTTVG 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344 316 LDNIVVVETKDAMMIAHKDKVQGVKQMVATLNEQGRTETQNHLEVYRPWGSYDSVDMGGRFQVKRISVKPGACLSLQMHH 395
Cdd:PRK15460 325 VKDLVVVQTKDAVLIADRNAVQDVKKVVEQIKADGRHEHRVHREVYRPWGKYDSIDAGDRYQVKRITVKPGEGLSVQMHH 404

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489510344 396 HRAEHWIVVSGTAQVTCDENVFLLTENQSTYIPIASVHRLRNPGKIPLEIIEVQSGSYLGEDDIERFEDIYGR 468
Cdd:PRK15460 405 HRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLIEVRSGSYLEEDDVVRFADRYGR 477
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-348 0e+00

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 558.53  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344   1 MIPVILSGGSGSRLWPLSRKQFPKQFLALTGEHTLFQQTLERLV-FEGMQEPIVVCNKDHRFIVNEQLAALNLEtqAILM 79
Cdd:COG0836    3 IYPVILAGGSGTRLWPLSRESYPKQFLPLLGEKSLLQQTVERLAgLVPPENILVVTNEEHRFLVAEQLPELGPA--NILL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344  80 EPFGRNTAPAVALTAMKLVNEGNDGLMLVLPADHVIEDQKALQRALALATVAAERGEMVLFGVPANKPETGYGYIKsTAD 159
Cdd:COG0836   81 EPVGRNTAPAIALAALLIAKRDPDAVLLVLPADHLIEDEEAFREAVRAAVEAAEAGKLVTFGIKPTRPETGYGYIE-AGE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344 160 ALLPEGVSRVSQFVEKPDEKRAKEFVEAGGYYWNSGMFLFRASRFLEELKKHDPDIYDTCLLTLERSVQDGDaLEIDSST 239
Cdd:COG0836  160 ALGGAGAYKVKRFVEKPDLETAEEYLASGNYLWNSGMFVFRASTILEELERHAPEIYAALEAAVAAAGTDLE-VRLDAEA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344 240 FACCPDNSIDYAVMEKTQRACVVPLSAGWSDVGCWSSLWEVNAKDANGNVTKGDVVIQDSRNCMIHGNGKLVSVIGLDNI 319
Cdd:COG0836  239 FAALPSISIDYAVMEKADNVAVVPADFGWSDVGSWDALWELLEKDENGNVVLGDVLLIDSSNSLVRSEGRLVAVIGVEDL 318

                        330       340
                 ....*....|....*....|....*....
gi 489510344 320 VVVETKDAMMIAHKDKVQGVKQMVATLNE 348
Cdd:COG0836  319 VVVDTPDALLVAPKDRAQEVKKIVEALKE 347
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-277 5.00e-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: 398.10  E-value: 5.00e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344   1 MIPVILSGGSGSRLWPLSRKQFPKQFLALTGEHTLFQQTLERLV-FEGMQEPIVVCNKDHRFIVNEQLAALNLETQaILM 79
Cdd:cd02509    1 IYPVILAGGSGTRLWPLSRESYPKQFLKLFGDKSLLQQTLDRLKgLVPPDRILVVTNEEYRFLVREQLPEGLPEEN-IIL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344  80 EPFGRNTAPAVALTAMKLVNEGNDGLMLVLPADHVIEDQKALQRALALATVAAERGEMVLFGVPANKPETGYGYIKstAD 159
Cdd:cd02509   80 EPEGRNTAPAIALAALYLAKRDPDAVLLVLPSDHLIEDVEAFLKAVKKAVEAAEEGYLVTFGIKPTRPETGYGYIE--AG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344 160 ALLPEGVSRVSQFVEKPDEKRAKEFVEAGGYYWNSGMFLFRASRFLEELKKHDPDIYDTCLLTLeRSVQDGDALEIDSST 239
Cdd:cd02509  158 EKLGGGVYRVKRFVEKPDLETAKEYLESGNYLWNSGIFLFRAKTFLEELKKHAPDIYEALEKAL-AAAGTDDFLRLLEEA 236

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 489510344 240 FACCPDNSIDYAVMEKTQRACVVPLSAGWSDVGCWSSL 277
Cdd:cd02509  237 FAKIPSISIDYAVMEKTKKVAVVPADFGWSDLGSWDAL 274
MannoseP_isomer pfam01050
Mannose-6-phosphate isomerase; All of the members of this Pfam entry belong to family 2 of the ...
 314-464 8.24e-101

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: 298.56  E-value: 8.24e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344  314 IGLDNIVVVETKDAMMIAHKDKVQGVKQMVATLNEQGRTETQNHLEVYRPWGSYDSVDMGGRFQVKRISVKPGACLSLQM 393
Cdd:pfam01050   1 IGVENLVVVETKDALLVAHKDKVQDVKKVVEELKENGRSEHQTHREVYRPWGSYDVIDEGERYQVKRITVKPGARLSLQM 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489510344  394 HHHRAEHWIVVSGTAQVTCDENVFLLTENQSTYIPIASVHRLRNPGKIPLEIIEVQSGSYLGEDDIERFED 464
Cdd:pfam01050  81 HHHRAEHWIVVSGTARVTKGGETFLLTENESTYIPLGTIHRLENPGKIPLELIEVQSGSYLGEDDIVRFED 151
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-285 5.43e-76

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: 238.31  E-value: 5.43e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344    2 IPVILSGGSGSRLWPLSRKQFPKQFLALTGeHTLFQQTLERLVFEGMQEPIVVCNKDHRFIVNEQLAALNL--ETQAILM 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGK-YPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKfgVQITYAL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344   80 EPFGRNTAPAVALTAMKLVNEGNDglMLVLPADHVIEDqkALQRALALAtVAAERGEMVLFGVPANKPETGYGYIKstad 159
Cdd:pfam00483  80 QPEGKGTAPAVALAADFLGDEKSD--VLVLGGDHIYRM--DLEQAVKFH-IEKAADATVTFGIVPVEPPTGYGVVE---- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344  160 allPEGVSRVSQFVEKPDEKRAKEFVEAGGYYWNSGMFLFRAsRFLEELKKHDPDIYDTClltlERSVQDGDAleidsst 239
Cdd:pfam00483 151 ---FDDNGRVIRFVEKPKLPKASNYASMGIYIFNSGVLDFLA-KYLEELKRGEDEITDIL----PKALEDGKL------- 215

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 489510344  240 faccpdnsiDYAVMEKtqracvvplSAGWSDVGCWSSLWEVNAKDA 285
Cdd:pfam00483 216 ---------AYAFIFK---------GYAWLDVGTWDSLWEANLFLL 243
cupin_PMI_typeII_C cd02213
Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal ...
 335-462 1.36e-71

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: 222.82  E-value: 1.36e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344 335 KVQGVKQMVATLNEQGRTEtqNHLEVYRPWGSYDSVDMGGRFQVKRISVKPGACLSLQMHHHRAEHWIVVSGTAQVTCDE 414
Cdd:cd02213    1 KSQRVKEIVEELKKRGRSE--EHRTVYRPWGSYEVLDEGEGYKVKRLTVNPGKRLSLQRHHHRSEHWVVVSGTAEVTLDG 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 489510344 415 NVFLLTENQSTYIPIASVHRLRNPGKIPLEIIEVQSGSYLGEDDIERF 462
Cdd:cd02213   79 KEKLLKEGESIYIPKGTKHRLENPGKIPLEIIEVQTGEYLGEDDIVRL 126
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
362-463 1.82e-38

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 135.65  E-value: 1.82e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344 362 RPWGSYDSV-DMGGRFQVKRISVKPGACLSLQMHHHRAEHWIVVSGTAQVTCDENVFLLTENQSTYIPIASVHRLRNPGK 440
Cdd:COG0662   12 IGWGSYEVLgEGGERLSVKRITVPPGAELSLHVHPHRDEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAGVPHRLRNPGD 91

                         90       100
                 ....*....|....*....|...
gi 489510344 441 IPLEIIEVQSGSYLGEDDIERFE 463
Cdd:COG0662   92 EPLELLEVQAPAYLGEDDIVRED 114
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 4-272 1.87e-09

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: 57.59  E-value: 1.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344   4 VILSGGSGSRLWPLSRKQfPKQFLALtGEHTLFQQTLERLVFEGMQEPIVVCNKDHRFIVNEQLAA----LNLETqAILM 79
Cdd:cd04181    2 VILAAGKGTRLRPLTDTR-PKPLLPI-AGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGskfgVNIEY-VVQE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344  80 EPFGrnTAPAVALtAMKLVNEGNdglMLVLPADHVIEDqkALQRALALATvaAERGEMVLFGVPANKPETgYGYIKStad 159
Cdd:cd04181   79 EPLG--TAGAVRN-AEDFLGDDD---FLVVNGDVLTDL--DLSELLRFHR--EKGADATIAVKEVEDPSR-YGVVEL--- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344 160 allpEGVSRVSQFVEKPDekrakefvEAGGYYWNSGMFLFRaSRFLEELKKHDPDIYDtclltlersvQDGDALEIdsst 239
Cdd:cd04181  145 ----DDDGRVTRFVEKPT--------LPESNLANAGIYIFE-PEILDYIPEILPRGED----------ELTDAIPL---- 197

                        250       260       270
                 ....*....|....*....|....*....|...
gi 489510344 240 faccpdnsidyavMEKTQRACVVPLSAGWSDVG 272
Cdd:cd04181  198 -------------LIEEGKVYGYPVDGYWLDIG 217
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
 375-446 4.49e-09

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: 53.22  E-value: 4.49e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489510344 375 RFQVKRISVKPGACLSLqmHHHRAEHWI-VVSGTAQVTCDENVFLLTENQSTYIPIASVHRLRNPGKIPLEII 446
Cdd:cd02222   16 NFAMRYFEIEPGGHTPL--HTHPWEHEVyVLRGKGVVVIGGEEYPVKPGDVVYIPPNEPHQFRNTGDEPLGFL 86
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
 380-457 9.34e-09

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: 52.90  E-value: 9.34e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489510344 380 RISVKPGACLSLQMHHHRAEHWIVVSGTAQVTCDENVFLLTENQSTYIPIASVHRLRNPGKIPLEIIEVQSGSYLGED 457
Cdd:cd02214   23 HARVPPGESTLPHRLKGSEEVYYILEGEGTMEIDGEPREVGPGDAVLIPPGAVQRIENTGEEDLVFLCICSPAWSPED 100
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
374-450 9.84e-09

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 52.93  E-value: 9.84e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489510344 374 GRFQVKRISVKPGAclSLQMHHHRA-EHWIVVSGTAQVTCDENVFLLTENQSTYIPIASVHRLRNPGKIPLEIIEVQS 450
Cdd:COG1917   21 DELEVVRVTFEPGA--RTPWHSHPGeELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAFRNLGDEPAVLLVVFS 96
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 380-448 1.78e-08

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: 51.10  E-value: 1.78e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489510344  380 RISVKPGACLSLQMHHHRAEHWIVVSGTAQVTCDENVFLLTENQSTYIPIASVHRLRNPGKIPLEIIEV 448
Cdd:pfam07883   2 LVTLPPGESSPPHRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLLDV 70
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
373-450 1.77e-07

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 49.63  E-value: 1.77e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489510344 373 GGRFQVKRISVKPGACLSLQMHHHRAEHWIVV-SGTAQVTCDENVFLLTENQSTYIPIASVHRLRNPGKIPLEIIEVQS 450
Cdd:COG3837   25 LTRLGVNLITLPPGASSSPYHAHSAEEEFVYVlEGELTLRIGGEEYVLEPGDSVGFPAGVPHRLRNRGDEPARYLVVGT 103
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 380-448 1.63e-06

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: 45.55  E-value: 1.63e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344 380 RISVKPGACLSLQMHHHRAEHWIVVSGTAQVTCD-ENVFLLTENQSTYIPIASVHRLRNPGKIPLEIIEV 448
Cdd:cd02208    3 VVTLPPGTSSPPHWHPEQDEIFYVLSGEGELTLDdGETVELKAGDIVLIPPGVPHSFVNTSDEPAVFLVV 72
cupin_XRE_C cd02209
XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; ...
 371-446 5.94e-06

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: 44.42  E-value: 5.94e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489510344 371 DMGGRFQVKRISVKPGACLSLQMHHHRAEHWIVVSGTAQVTCDENVFLLTENQSTYIPIASVHRLRNPGKIPLEII 446
Cdd:cd02209   11 LPGRKMEPFLVTLPPGGSGGEPYSHEGEEFGYVLEGELELTVGGETYVLEAGDSIYFDSDVPHRYRNPGDEPARVL 86
cupin_TcmJ-like cd06991
TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of ...
 381-446 8.15e-06

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: 44.59  E-value: 8.15e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489510344 381 ISVKPGACLSLQMHHHRAEHWIVVSGTAQVTCDENVFLLTENQSTYIPIASVHRLRNPGKIPLEII 446
Cdd:cd06991   24 LTLAPGERVSEHYHPYSEEFLYVVRGRLVVRVDGEPVVLEAGEALLVPRGVRHRLENAGDEPARLV 89
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 372-448 1.59e-05

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: 44.19  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344 372 MGGRFQVKRIsvKPGACLSLQMHHHRAEHWIVVSGTAQVTCDEN-----VFLLTENQSTYIPIASVHRLRNPGKIPLEII 446
Cdd:COG2140    1 MTLAGGLTVL--EPGGVREEHWHPNAAEWYYVLSGEARMTVQDPpgrarTVDVGPGDVVYVPPGYGHYIINTGDEPLVFL 78


                 ..
gi 489510344 447 EV 448
Cdd:COG2140   79 AV 80
cupin_DddK cd06988
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ...
 394-448 1.68e-05

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: 42.99  E-value: 1.68e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489510344 394 HHHRAEHWIVVSGTAQVTCDENVFLLTENQSTYIPIASVHRLRNPGKIPLEIIEV 448
Cdd:cd06988   19 SHHEYEIFIVISGKGIVVVDGEREPVKAGDVVYIPPGTEHYVKNDGDEDFEFYSI 73
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 4-68 3.12e-05

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: 45.21  E-value: 3.12e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489510344   4 VILSGGSGSRlwpLSRKQfPKQFLALTGEhTLFQQTLERLV-FEGMQEPIVVCNKDHRFIVNEQLA 68
Cdd:cd02516    4 IILAAGSGSR---MGADI-PKQFLELGGK-PVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAK 64
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 4-73 7.70e-05

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: 43.97  E-value: 7.70e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489510344   4 VILSGGSGSRLwplsRKQFPKQFLALTGEhTLFQQTLERLV-FEGMQEPIVVCNKDHRFIVNEQLAALNLE 73
Cdd:COG1211    1 IIPAAGSGSRM----GAGIPKQFLPLGGK-PVLEHTLEAFLaHPRIDEIVVVVPPDDIEYFEELLAKYGID 66
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
 379-468 7.93e-05

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: 42.85  E-value: 7.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344 379 KRISVKPGACLSLQMHHHRAEHWIVVSGTAQVTC-DE----NVFLLTENQSTYIPIASVHRLRNPGKIPLEIIEVQsgsy 453
Cdd:cd02240   30 ALVRVAPGAMRELHWHPNTAEWQYVISGSARVTVfDEdgrfETFNLGAGDVGYVPSGSGHHIENIGDEDAEFLLIF---- 105

                         90
                 ....*....|....*
gi 489510344 454 lgedDIERFEDIYGR 468
Cdd:cd02240  106 ----DDGTFADVSLP 116
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 4-141 8.14e-05

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: 42.95  E-value: 8.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344    4 VILSGGSGSRLwplsrkQFPKQFLALTGEhTLFQQTLERLvfEGMQEPIVVCNKDHRfiVNEQLAALNLETqaILMEPFG 83
Cdd:pfam12804   2 VILAGGRSSRM------GGDKALLPLGGK-PLLERVLERL--RPAGDEVVVVANDEE--VLAALAGLGVPV--VPDPDPG 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489510344   84 RNTAPAVAlTAMKLVnEGNDGLmLVLPADHVIEDQKALQR----------ALALATVAAERGEMVLFG 141
Cdd:pfam12804  69 QGPLAGLL-AALRAA-PGADAV-LVLACDMPFLTPELLRRllaaaeesgaDIVVPVYDGGRGHPLLYR 133
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
4-55 4.26e-04

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 41.77  E-value: 4.26e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489510344   4 VILSGGSGSRLWPLSRKQfPKQFLALTGEhTLFQQTLERLVFEGMQEPIVVC 55
Cdd:COG1213    3 VILAAGRGSRLGPLTDDI-PKCLVEIGGK-TLLERQLEALAAAGIKDIVVVT 52
AllE COG3257
Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];
372-445 6.27e-04

Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 442488 [Multi-domain]  Cd Length: 262  Bit Score: 41.35  E-value: 6.27e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489510344 372 MGGRFQVKRISVKPGACLSLQMHHHRAEHWI-VVSGTAQVTCDENVFLLTENQSTYIPIASVHRLRNPGKIPLEI 445
Cdd:COG3257   55 SGATFSQYIVEVAPGGGSDRPEPDPGAETFLfVLEGEVTLTLGGETHELTPGGYAYLPPGTPWTLRNAGDEPARF 129
cupin_OxDC_C cd20305
Oxalate decarboxylase (OxDC), C-terminal cupin domain; This model represents the C-terminal ...
 381-465 1.27e-03

Oxalate decarboxylase (OxDC), C-terminal cupin domain; This model represents the C-terminal cupin domain of oxalate decarboxylase (OxDC; EC 4.1.1.2), 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. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380439 [Multi-domain]  Cd Length: 153  Bit Score: 39.49  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344 381 ISVKPGAclsL-QMH-HHRAEHWI-VVSGTAQVTcdenVFLLTENQST---------YIPIASVHRLRNPGKIPLEIIEV 448
Cdd:cd20305   39 VTLEPGA---LrELHwHPNADEWQyYISGKARMT----VFASGGRARTfdfqagdvgYVPRGYGHYIENTGDEPLEFLEV 111

                         90
                 ....*....|....*...
gi 489510344 449 -QSGsylgeddieRFEDI 465
Cdd:cd20305  112 fNSG---------RYQDI 120
cupin_TM1287-like cd02221
Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial ...
 380-446 2.04e-03

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: 37.45  E-value: 2.04e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489510344 380 RISVKPGACLSLQMHHHRAEHWIVVSGTAQVTCDENVFLLTENQSTYIPIASVHRLRNPGKIPLEII 446
Cdd:cd02221   23 RVTLPPGSSIGYHQHEGEFEIYYILSGEGLYTDNGKEYEVKAGDVTFTRDGESHGIENTGDEDLVFI 89
cupin_Bh2720-like cd02223
Bacillus halodurans Bh2720 and related proteins, cupin domain; This family includes bacterial, ...
 376-445 3.00e-03

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: 37.14  E-value: 3.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489510344 376 FQVKRISVKPGACLSLQMHHHRAEHWIVVSGTAQVTCDENVFLLTENQSTYIPIASVHRLRNPGKIPLEI 445
Cdd:cd02223   11 LQLVLMSIPPGEDIGLEVHDDVDQFLRIEEGEGKAIMGGFESEVKDGDAIIVPAGTWHNVINTGNEPLKL 80
cupin_yp_001338853-like cd07008
Klebsiella pneumoniae yp_001338853.1 and related proteins, cupin domain; This family includes ...
 383-448 6.84e-03

Klebsiella pneumoniae yp_001338853.1 and related proteins, cupin domain; This family includes bacterial proteins homologous to Klebsiella pneumoniae yp_001338853.1, an uncharacterized conserved protein with double-stranded beta-helix domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380411 [Multi-domain]  Cd Length: 101  Bit Score: 36.08  E-value: 6.84e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489510344 383 VKPGACLSLQMHHHRAEHWIVVSGTAQ-VTCDENVFLLTENQSTYIPIASVHRLRNPGKIPLEIIEV 448
Cdd:cd07008   34 VKPGQEIAAHIHPHGQDTWIVLSGEGEyLLGDGQTVPIKAGDIVIAPAGQVHGARNTGDEPLVFVSV 100
 
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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