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Conserved domains on  [gi|15832090|ref|NP_310863|]
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mannose-1-phosphate guanyltransferase [Escherichia coli O157:H7 str. Sakai]

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 ...
 6-480 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: 868.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090     6 IIAVVMAGGTGSRLWPLSRELYPKQFLQLSGDNTLLQTTLLRLSGLSCQKPLVITNEQHRFVVAEQLREINKLNGNIILE 85
Cdd:TIGR01479   1 IIPVILAGGSGTRLWPLSRELYPKQFLALVGDLTMLQQTLKRLAGLPCSSPLVICNEEHRFIVAEQLREIGKLASNIILE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090    86 PCGRNTAPAIAISAFHALKRNpQEDPLLLVLAADHVIAKESVFCDAIKNATPIANQGKIVTFGIIPEYAETGYGYIERGE 165
Cdd:TIGR01479  81 PVGRNTAPAIALAALLAARRN-GEDPLLLVLAADHVITDEDAFQAAVKLAMPAAAEGKLVTFGIVPTHPETGYGYIRRGA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090   166 lsvPLQGhenTGFYYVNKFVEKPNRETAELYMTSGNHYWNSGIFMFKASVYLEELRKFRPDIYNVCEQVASSSYIDLDFI 245
Cdd:TIGR01479 160 ---PLAG---EDVYQVQRFVEKPDLATAQAYLESGDYYWNSGMFLFRASRYLAELKKHAPDIYEACEAAVEASEPDLDFI 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090   246 RLSKEQFQDCPAESIDFAVMEKTEKCVVCPVDIGWSDVGSWQSLWDISLKSKTGDVCKGDILTYDTKNNYIYSESALVAA 325
Cdd:TIGR01479 234 RLDKEAFEQCPSESIDYAVMEKTADAVVVPMDAGWSDVGSWSALWEISDKDADGNVLKGDVLTHDTKNSYIYSESRLVAV 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090   326 IGIEDMVIVQTKDAVLVSKKSDVQHVKKIVEMLKLQQRTEYISHREVFRPWGKFDSIDQGERYKVKKIIVKPGEGLSLRM 405
Cdd:TIGR01479 314 VGVEDLVVVETKDAVLVAHKDRVQDVKKIVEQLKADGRTETEQHREVYRPWGKYDSIDQGDRYQVKRITVKPGEKLSLQM 393

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15832090   406 HHHRSEHWIVLSGTAKVTLGDKTKLVTANESIYIPLGAAYSLENPGIIPLNLIEVSSGDYLGEDDIIRQKERYKH 480
Cdd:TIGR01479 394 HHHRAEHWIVVSGTARVTIGDETLLLTENESTYIPLGVIHRLENPGKIPLELIEVQSGSYLGEDDIIRFEDRYGR 468
 
Name Accession Description Interval E-value
GMP_PMI TIGR01479
mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to ...
 6-480 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: 868.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090     6 IIAVVMAGGTGSRLWPLSRELYPKQFLQLSGDNTLLQTTLLRLSGLSCQKPLVITNEQHRFVVAEQLREINKLNGNIILE 85
Cdd:TIGR01479   1 IIPVILAGGSGTRLWPLSRELYPKQFLALVGDLTMLQQTLKRLAGLPCSSPLVICNEEHRFIVAEQLREIGKLASNIILE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090    86 PCGRNTAPAIAISAFHALKRNpQEDPLLLVLAADHVIAKESVFCDAIKNATPIANQGKIVTFGIIPEYAETGYGYIERGE 165
Cdd:TIGR01479  81 PVGRNTAPAIALAALLAARRN-GEDPLLLVLAADHVITDEDAFQAAVKLAMPAAAEGKLVTFGIVPTHPETGYGYIRRGA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090   166 lsvPLQGhenTGFYYVNKFVEKPNRETAELYMTSGNHYWNSGIFMFKASVYLEELRKFRPDIYNVCEQVASSSYIDLDFI 245
Cdd:TIGR01479 160 ---PLAG---EDVYQVQRFVEKPDLATAQAYLESGDYYWNSGMFLFRASRYLAELKKHAPDIYEACEAAVEASEPDLDFI 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090   246 RLSKEQFQDCPAESIDFAVMEKTEKCVVCPVDIGWSDVGSWQSLWDISLKSKTGDVCKGDILTYDTKNNYIYSESALVAA 325
Cdd:TIGR01479 234 RLDKEAFEQCPSESIDYAVMEKTADAVVVPMDAGWSDVGSWSALWEISDKDADGNVLKGDVLTHDTKNSYIYSESRLVAV 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090   326 IGIEDMVIVQTKDAVLVSKKSDVQHVKKIVEMLKLQQRTEYISHREVFRPWGKFDSIDQGERYKVKKIIVKPGEGLSLRM 405
Cdd:TIGR01479 314 VGVEDLVVVETKDAVLVAHKDRVQDVKKIVEQLKADGRTETEQHREVYRPWGKYDSIDQGDRYQVKRITVKPGEKLSLQM 393

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15832090   406 HHHRSEHWIVLSGTAKVTLGDKTKLVTANESIYIPLGAAYSLENPGIIPLNLIEVSSGDYLGEDDIIRQKERYKH 480
Cdd:TIGR01479 394 HHHRAEHWIVVSGTARVTIGDETLLLTENESTYIPLGVIHRLENPGKIPLELIEVQSGSYLGEDDIIRFEDRYGR 468
cpsB PRK15460
mannose-1-phosphate guanyltransferase; Provisional
 1-478 0e+00

mannose-1-phosphate guanyltransferase; Provisional


Pssm-ID: 185357 [Multi-domain]  Cd Length: 478  Bit Score: 698.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090    1 MSDAPIIAVVMAGGTGSRLWPLSRELYPKQFLQLSGDNTLLQTTLLRLSGLSCQKPLVITNEQHRFVVAEQLREINKLNG 80
Cdd:PRK15460   1 MAQSKLYPVVMAGGSGSRLWPLSRVLYPKQFLCLKGDLTMLQTTICRLNGVECESPVVICNEQHRFIVAEQLRQLNKLTE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090   81 NIILEPCGRNTAPAIAISAFHALKRNPQEDPLLLVLAADHVIAKESVFCDAIKNATPIANQGKIVTFGIIPEYAETGYGY 160
Cdd:PRK15460  81 NIILEPAGRNTAPAIALAALAAKRHSPESDPLMLVLAADHVIADEDAFRAAVRNAMPYAEAGKLVTFGIVPDLPETGYGY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090  161 IERGELSVplqGHENTGFYYVNKFVEKPNRETAELYMTSGNHYWNSGIFMFKASVYLEELRKFRPDIYNVCEQVASSSYI 240
Cdd:PRK15460 161 IRRGEVSA---GEQDTVAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDP 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090  241 DLDFIRLSKEQFQDCPAESIDFAVMEKTEKCVVCPVDIGWSDVGSWQSLWDISLKSKTGDVCKGDILTYDTKNNYIYSES 320
Cdd:PRK15460 238 DLDFIRVDEEAFLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSLWEISAHTAEGNVCHGDVINHKTENSYVYAES 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090  321 ALVAAIGIEDMVIVQTKDAVLVSKKSDVQHVKKIVEMLKLQQRTEYISHREVFRPWGKFDSIDQGERYKVKKIIVKPGEG 400
Cdd:PRK15460 318 GLVTTVGVKDLVVVQTKDAVLIADRNAVQDVKKVVEQIKADGRHEHRVHREVYRPWGKYDSIDAGDRYQVKRITVKPGEG 397

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832090  401 LSLRMHHHRSEHWIVLSGTAKVTLGDKTKLVTANESIYIPLGAAYSLENPGIIPLNLIEVSSGDYLGEDDIIRQKERY 478
Cdd:PRK15460 398 LSVQMHHHRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLIEVRSGSYLEEDDVVRFADRY 475
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
6-359 0e+00

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 523.09  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090   6 IIAVVMAGGTGSRLWPLSRELYPKQFLQLSGDNtllqttllrlS----------GLSC-QKPLVITNEQHRFVVAEQLRE 74
Cdd:COG0836   3 IYPVILAGGSGTRLWPLSRESYPKQFLPLLGEK----------SllqqtverlaGLVPpENILVVTNEEHRFLVAEQLPE 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090  75 INKlnGNIILEPCGRNTAPAIAISAFHALKRNPqeDPLLLVLAADHVIAKESVFCDAIKNATPIANQGKIVTFGIIPEYA 154
Cdd:COG0836  73 LGP--ANILLEPVGRNTAPAIALAALLIAKRDP--DAVLLVLPADHLIEDEEAFREAVRAAVEAAEAGKLVTFGIKPTRP 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090 155 ETGYGYIERGELSvplqghENTGFYYVNKFVEKPNRETAELYMTSGNHYWNSGIFMFKASVYLEELRKFRPDIYNVCEQV 234
Cdd:COG0836 149 ETGYGYIEAGEAL------GGAGAYKVKRFVEKPDLETAEEYLASGNYLWNSGMFVFRASTILEELERHAPEIYAALEAA 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090 235 ASSSYIDLDfIRLSKEQFQDCPAESIDFAVMEKTEKCVVCPVDIGWSDVGSWQSLWDISLKSKTGDVCKGDILTYDTKNN 314
Cdd:COG0836 223 VAAAGTDLE-VRLDAEAFAALPSISIDYAVMEKADNVAVVPADFGWSDVGSWDALWELLEKDENGNVVLGDVLLIDSSNS 301

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 15832090 315 YIYSESALVAAIGIEDMVIVQTKDAVLVSKKSDVQHVKKIVEMLK 359
Cdd:COG0836 302 LVRSEGRLVAVIGVEDLVVVDTPDALLVAPKDRAQEVKKIVEALK 346
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 6-289 5.57e-129

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: 374.99  E-value: 5.57e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090   6 IIAVVMAGGTGSRLWPLSRELYPKQFLQLSGDNTLLQTTLLRLSGLS-CQKPLVITNEQHRFVVAEQLREINKlNGNIIL 84
Cdd:cd02509   1 IYPVILAGGSGTRLWPLSRESYPKQFLKLFGDKSLLQQTLDRLKGLVpPDRILVVTNEEYRFLVREQLPEGLP-EENIIL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090  85 EPCGRNTAPAIAISAFHALKRNPqeDPLLLVLAADHVIAKESVFCDAIKNATPIANQGKIVTFGIIPEYAETGYGYIERG 164
Cdd:cd02509  80 EPEGRNTAPAIALAALYLAKRDP--DAVLLVLPSDHLIEDVEAFLKAVKKAVEAAEEGYLVTFGIKPTRPETGYGYIEAG 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090 165 ELsvplqghENTGFYYVNKFVEKPNRETAELYMTSGNHYWNSGIFMFKASVYLEELRKFRPDIYNVCEQvASSSYIDLDF 244
Cdd:cd02509 158 EK-------LGGGVYRVKRFVEKPDLETAKEYLESGNYLWNSGIFLFRAKTFLEELKKHAPDIYEALEK-ALAAAGTDDF 229

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 15832090 245 IRLSKEQFQDCPAESIDFAVMEKTEKCVVCPVDIGWSDVGSWQSL 289
Cdd:cd02509 230 LRLLEEAFAKIPSISIDYAVMEKTKKVAVVPADFGWSDLGSWDAL 274
MannoseP_isomer pfam01050
Mannose-6-phosphate isomerase; All of the members of this Pfam entry belong to family 2 of the ...
 326-473 9.88e-82

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: 249.64  E-value: 9.88e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090   326 IGIEDMVIVQTKDAVLVSKKSDVQHVKKIVEMLKLQQRTEYISHREVFRPWGKFDSIDQGERYKVKKIIVKPGEGLSLRM 405
Cdd:pfam01050   1 IGVENLVVVETKDALLVAHKDKVQDVKKVVEELKENGRSEHQTHREVYRPWGSYDVIDEGERYQVKRITVKPGARLSLQM 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832090   406 HHHRSEHWIVLSGTAKVTLGDKTKLVTANESIYIPLGAAYSLENPGIIPLNLIEVSSGDYLGEDDIIR 473
Cdd:pfam01050  81 HHHRAEHWIVVSGTARVTKGGETFLLTENESTYIPLGTIHRLENPGKIPLELIEVQSGSYLGEDDIVR 148
 
Name Accession Description Interval E-value
GMP_PMI TIGR01479
mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to ...
 6-480 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: 868.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090     6 IIAVVMAGGTGSRLWPLSRELYPKQFLQLSGDNTLLQTTLLRLSGLSCQKPLVITNEQHRFVVAEQLREINKLNGNIILE 85
Cdd:TIGR01479   1 IIPVILAGGSGTRLWPLSRELYPKQFLALVGDLTMLQQTLKRLAGLPCSSPLVICNEEHRFIVAEQLREIGKLASNIILE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090    86 PCGRNTAPAIAISAFHALKRNpQEDPLLLVLAADHVIAKESVFCDAIKNATPIANQGKIVTFGIIPEYAETGYGYIERGE 165
Cdd:TIGR01479  81 PVGRNTAPAIALAALLAARRN-GEDPLLLVLAADHVITDEDAFQAAVKLAMPAAAEGKLVTFGIVPTHPETGYGYIRRGA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090   166 lsvPLQGhenTGFYYVNKFVEKPNRETAELYMTSGNHYWNSGIFMFKASVYLEELRKFRPDIYNVCEQVASSSYIDLDFI 245
Cdd:TIGR01479 160 ---PLAG---EDVYQVQRFVEKPDLATAQAYLESGDYYWNSGMFLFRASRYLAELKKHAPDIYEACEAAVEASEPDLDFI 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090   246 RLSKEQFQDCPAESIDFAVMEKTEKCVVCPVDIGWSDVGSWQSLWDISLKSKTGDVCKGDILTYDTKNNYIYSESALVAA 325
Cdd:TIGR01479 234 RLDKEAFEQCPSESIDYAVMEKTADAVVVPMDAGWSDVGSWSALWEISDKDADGNVLKGDVLTHDTKNSYIYSESRLVAV 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090   326 IGIEDMVIVQTKDAVLVSKKSDVQHVKKIVEMLKLQQRTEYISHREVFRPWGKFDSIDQGERYKVKKIIVKPGEGLSLRM 405
Cdd:TIGR01479 314 VGVEDLVVVETKDAVLVAHKDRVQDVKKIVEQLKADGRTETEQHREVYRPWGKYDSIDQGDRYQVKRITVKPGEKLSLQM 393

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15832090   406 HHHRSEHWIVLSGTAKVTLGDKTKLVTANESIYIPLGAAYSLENPGIIPLNLIEVSSGDYLGEDDIIRQKERYKH 480
Cdd:TIGR01479 394 HHHRAEHWIVVSGTARVTIGDETLLLTENESTYIPLGVIHRLENPGKIPLELIEVQSGSYLGEDDIIRFEDRYGR 468
cpsB PRK15460
mannose-1-phosphate guanyltransferase; Provisional
 1-478 0e+00

mannose-1-phosphate guanyltransferase; Provisional


Pssm-ID: 185357 [Multi-domain]  Cd Length: 478  Bit Score: 698.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090    1 MSDAPIIAVVMAGGTGSRLWPLSRELYPKQFLQLSGDNTLLQTTLLRLSGLSCQKPLVITNEQHRFVVAEQLREINKLNG 80
Cdd:PRK15460   1 MAQSKLYPVVMAGGSGSRLWPLSRVLYPKQFLCLKGDLTMLQTTICRLNGVECESPVVICNEQHRFIVAEQLRQLNKLTE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090   81 NIILEPCGRNTAPAIAISAFHALKRNPQEDPLLLVLAADHVIAKESVFCDAIKNATPIANQGKIVTFGIIPEYAETGYGY 160
Cdd:PRK15460  81 NIILEPAGRNTAPAIALAALAAKRHSPESDPLMLVLAADHVIADEDAFRAAVRNAMPYAEAGKLVTFGIVPDLPETGYGY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090  161 IERGELSVplqGHENTGFYYVNKFVEKPNRETAELYMTSGNHYWNSGIFMFKASVYLEELRKFRPDIYNVCEQVASSSYI 240
Cdd:PRK15460 161 IRRGEVSA---GEQDTVAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDP 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090  241 DLDFIRLSKEQFQDCPAESIDFAVMEKTEKCVVCPVDIGWSDVGSWQSLWDISLKSKTGDVCKGDILTYDTKNNYIYSES 320
Cdd:PRK15460 238 DLDFIRVDEEAFLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSLWEISAHTAEGNVCHGDVINHKTENSYVYAES 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090  321 ALVAAIGIEDMVIVQTKDAVLVSKKSDVQHVKKIVEMLKLQQRTEYISHREVFRPWGKFDSIDQGERYKVKKIIVKPGEG 400
Cdd:PRK15460 318 GLVTTVGVKDLVVVQTKDAVLIADRNAVQDVKKVVEQIKADGRHEHRVHREVYRPWGKYDSIDAGDRYQVKRITVKPGEG 397

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832090  401 LSLRMHHHRSEHWIVLSGTAKVTLGDKTKLVTANESIYIPLGAAYSLENPGIIPLNLIEVSSGDYLGEDDIIRQKERY 478
Cdd:PRK15460 398 LSVQMHHHRAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLIEVRSGSYLEEDDVVRFADRY 475
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
6-359 0e+00

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 523.09  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090   6 IIAVVMAGGTGSRLWPLSRELYPKQFLQLSGDNtllqttllrlS----------GLSC-QKPLVITNEQHRFVVAEQLRE 74
Cdd:COG0836   3 IYPVILAGGSGTRLWPLSRESYPKQFLPLLGEK----------SllqqtverlaGLVPpENILVVTNEEHRFLVAEQLPE 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090  75 INKlnGNIILEPCGRNTAPAIAISAFHALKRNPqeDPLLLVLAADHVIAKESVFCDAIKNATPIANQGKIVTFGIIPEYA 154
Cdd:COG0836  73 LGP--ANILLEPVGRNTAPAIALAALLIAKRDP--DAVLLVLPADHLIEDEEAFREAVRAAVEAAEAGKLVTFGIKPTRP 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090 155 ETGYGYIERGELSvplqghENTGFYYVNKFVEKPNRETAELYMTSGNHYWNSGIFMFKASVYLEELRKFRPDIYNVCEQV 234
Cdd:COG0836 149 ETGYGYIEAGEAL------GGAGAYKVKRFVEKPDLETAEEYLASGNYLWNSGMFVFRASTILEELERHAPEIYAALEAA 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090 235 ASSSYIDLDfIRLSKEQFQDCPAESIDFAVMEKTEKCVVCPVDIGWSDVGSWQSLWDISLKSKTGDVCKGDILTYDTKNN 314
Cdd:COG0836 223 VAAAGTDLE-VRLDAEAFAALPSISIDYAVMEKADNVAVVPADFGWSDVGSWDALWELLEKDENGNVVLGDVLLIDSSNS 301

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 15832090 315 YIYSESALVAAIGIEDMVIVQTKDAVLVSKKSDVQHVKKIVEMLK 359
Cdd:COG0836 302 LVRSEGRLVAVIGVEDLVVVDTPDALLVAPKDRAQEVKKIVEALK 346
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 6-289 5.57e-129

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: 374.99  E-value: 5.57e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090   6 IIAVVMAGGTGSRLWPLSRELYPKQFLQLSGDNTLLQTTLLRLSGLS-CQKPLVITNEQHRFVVAEQLREINKlNGNIIL 84
Cdd:cd02509   1 IYPVILAGGSGTRLWPLSRESYPKQFLKLFGDKSLLQQTLDRLKGLVpPDRILVVTNEEYRFLVREQLPEGLP-EENIIL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090  85 EPCGRNTAPAIAISAFHALKRNPqeDPLLLVLAADHVIAKESVFCDAIKNATPIANQGKIVTFGIIPEYAETGYGYIERG 164
Cdd:cd02509  80 EPEGRNTAPAIALAALYLAKRDP--DAVLLVLPSDHLIEDVEAFLKAVKKAVEAAEEGYLVTFGIKPTRPETGYGYIEAG 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090 165 ELsvplqghENTGFYYVNKFVEKPNRETAELYMTSGNHYWNSGIFMFKASVYLEELRKFRPDIYNVCEQvASSSYIDLDF 244
Cdd:cd02509 158 EK-------LGGGVYRVKRFVEKPDLETAKEYLESGNYLWNSGIFLFRAKTFLEELKKHAPDIYEALEK-ALAAAGTDDF 229

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 15832090 245 IRLSKEQFQDCPAESIDFAVMEKTEKCVVCPVDIGWSDVGSWQSL 289
Cdd:cd02509 230 LRLLEEAFAKIPSISIDYAVMEKTKKVAVVPADFGWSDLGSWDAL 274
MannoseP_isomer pfam01050
Mannose-6-phosphate isomerase; All of the members of this Pfam entry belong to family 2 of the ...
 326-473 9.88e-82

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: 249.64  E-value: 9.88e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090   326 IGIEDMVIVQTKDAVLVSKKSDVQHVKKIVEMLKLQQRTEYISHREVFRPWGKFDSIDQGERYKVKKIIVKPGEGLSLRM 405
Cdd:pfam01050   1 IGVENLVVVETKDALLVAHKDKVQDVKKVVEELKENGRSEHQTHREVYRPWGSYDVIDEGERYQVKRITVKPGARLSLQM 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832090   406 HHHRSEHWIVLSGTAKVTLGDKTKLVTANESIYIPLGAAYSLENPGIIPLNLIEVSSGDYLGEDDIIR 473
Cdd:pfam01050  81 HHHRAEHWIVVSGTARVTKGGETFLLTENESTYIPLGTIHRLENPGKIPLELIEVQSGSYLGEDDIVR 148
cupin_PMI_typeII_C cd02213
Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal ...
 348-473 2.64e-65

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: 206.64  E-value: 2.64e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090 348 VQHVKKIVEMLKLQQRTEYisHREVFRPWGKFDSIDQGERYKVKKIIVKPGEGLSLRMHHHRSEHWIVLSGTAKVTLGDK 427
Cdd:cd02213   2 SQRVKEIVEELKKRGRSEE--HRTVYRPWGSYEVLDEGEGYKVKRLTVNPGKRLSLQRHHHRSEHWVVVSGTAEVTLDGK 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15832090 428 TKLVTANESIYIPLGAAYSLENPGIIPLNLIEVSSGDYLGEDDIIR 473
Cdd:cd02213  80 EKLLKEGESIYIPKGTKHRLENPGKIPLEIIEVQTGEYLGEDDIVR 125
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 7-295 2.78e-60

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: 197.86  E-value: 2.78e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090     7 IAVVMAGGTGSRLWPLSRELYPKQFLQLSGDnTLLQTTLLRLSGLSCQKPLVITNEQHRFVVAEQLREINKLNGNI--IL 84
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKY-PLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQItyAL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090    85 EPCGRNTAPAIAISAFHAlkrnPQEDPLLLVLAADHVIAKEsvFCDAIKNATPiANQGKIVTFGIIPEYAETGYGYIERG 164
Cdd:pfam00483  80 QPEGKGTAPAVALAADFL----GDEKSDVLVLGGDHIYRMD--LEQAVKFHIE-KAADATVTFGIVPVEPPTGYGVVEFD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090   165 ElsvplQGHentgfyyVNKFVEKPNRETAELYMTSGNHYWNSGIFMFKASvYLEELRKFRPDIYNVCEQVASSSYIDLDF 244
Cdd:pfam00483 153 D-----NGR-------VIRFVEKPKLPKASNYASMGIYIFNSGVLDFLAK-YLEELKRGEDEITDILPKALEDGKLAYAF 219

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15832090   245 IRlskeqfqdcpaesIDFAvmektekcvvcpvdigWSDVGSWQSLWDISLK 295
Cdd:pfam00483 220 IF-------------KGYA----------------WLDVGTWDSLWEANLF 241
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
374-474 4.01e-35

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 126.79  E-value: 4.01e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090 374 RPWGKFDSIDQ-GERYKVKKIIVKPGEGLSLRMHHHRSEHWIVLSGTAKVTLGDKTKLVTANESIYIPLGAAYSLENPGI 452
Cdd:COG0662  12 IGWGSYEVLGEgGERLSVKRITVPPGAELSLHVHPHRDEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAGVPHRLRNPGD 91

                        90       100
                ....*....|....*....|..
gi 15832090 453 IPLNLIEVSSGDYLGEDDIIRQ 474
Cdd:COG0662  92 EPLELLEVQAPAYLGEDDIVRE 113
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
 370-455 1.07e-11

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: 60.99  E-value: 1.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090 370 REVFRPwgkfdSIDQGERYKVKKIIVKPGEGLSLRMHHHRSEHWIVLSGTAKVTLGDKTKLVTANESIYIPLGAAYSLEN 449
Cdd:cd02214   6 RELLHP-----DNDGDPRYSLAHARVPPGESTLPHRLKGSEEVYYILEGEGTMEIDGEPREVGPGDAVLIPPGAVQRIEN 80


                ....*.
gi 15832090 450 PGIIPL 455
Cdd:cd02214  81 TGEEDL 86
cupin_DddK cd06988
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ...
 393-460 5.72e-10

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: 55.32  E-value: 5.72e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832090 393 IIVKPGEGlSLRMHHHRSEHWIVLSGTAKVTLGDKTKLVTANESIYIPLGAAYSLENPGIIPLNLIEV 460
Cdd:cd06988   7 CVVRPGTT-STPHSHHEYEIFIVISGKGIVVVDGEREPVKAGDVVYIPPGTEHYVKNDGDEDFEFYSI 73
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
393-462 8.81e-09

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 53.48  E-value: 8.81e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15832090 393 IIVKPGEGLSLRMHHHRSEHWI-VLSGTAKVTLGDKTKLVTANESIYIPLGAAYSLENPGIIPLNLIEVSS 462
Cdd:COG3837  33 ITLPPGASSSPYHAHSAEEEFVyVLEGELTLRIGGEEYVLEPGDSVGFPAGVPHRLRNRGDEPARYLVVGT 103
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 393-460 1.08e-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: 51.88  E-value: 1.08e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832090   393 IIVKPGEGLSLRMHHHRSEHWIVLSGTAKVTLGDKTKLVTANESIYIPLGAAYSLENPGIIPLNLIEV 460
Cdd:pfam07883   3 VTLPPGESSPPHRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLLDV 70
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
367-462 2.10e-08

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 51.77  E-value: 2.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090 367 ISHREVFRPWGKFDSIDQGE-RYKVKKIIVKPGEglSLRMH-HHRSEHWIVLSGTAKVTLGDKTKLVTANESIYIPLGAA 444
Cdd:COG1917   1 MRLAEIALTGVSVRVLADGEdELEVVRVTFEPGA--RTPWHsHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVP 78

                        90
                ....*....|....*...
gi 15832090 445 YSLENPGIIPLNLIEVSS 462
Cdd:COG1917  79 HAFRNLGDEPAVLLVVFS 96
cupin_TM1287-like cd02221
Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial ...
 392-458 5.07e-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: 47.46  E-value: 5.07e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15832090 392 KIIVKPGEGLSLRMHHHRSEHWIVLSGTAKVTLGDKTKLVTANESIYIPLGAAYSLENPGIIPLNLI 458
Cdd:cd02221  23 RVTLPPGSSIGYHQHEGEFEIYYILSGEGLYTDNGKEYEVKAGDVTFTRDGESHGIENTGDEDLVFI 89
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
 383-455 2.14e-06

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: 45.90  E-value: 2.14e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15832090 383 DQGERYKVKKIIVKPGeGLSlRMHHHRSEHWI-VLSGTAKVTLGDKTKLVTANESIYIPLGAAYSLENPGIIPL 455
Cdd:cd02222  12 DGAPNFAMRYFEIEPG-GHT-PLHTHPWEHEVyVLRGKGVVVIGGEEYPVKPGDVVYIPPNEPHQFRNTGDEPL 83
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 393-461 2.43e-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: 45.17  E-value: 2.43e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090 393 IIVKPGEGLSLRMHHHRSEHWIVLSGTAKVTLGD-KTKLVTANESIYIPLGAAYSLENPGIIPLNLIEVS 461
Cdd:cd02208   4 VTLPPGTSSPPHWHPEQDEIFYVLSGEGELTLDDgETVELKAGDIVLIPPGVPHSFVNTSDEPAVFLVVS 73
cupin_Bh2720-like cd02223
Bacillus halodurans Bh2720 and related proteins, cupin domain; This family includes bacterial, ...
 395-457 5.51e-06

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: 44.84  E-value: 5.51e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15832090 395 VKPGEGLSLRMHHHRSEHWIVLSGTAKVTLGDKTKLVTANESIYIPLGAAYSLENPGIIPLNL 457
Cdd:cd02223  18 IPPGEDIGLEVHDDVDQFLRIEEGEGKAIMGGFESEVKDGDAIIVPAGTWHNVINTGNEPLKL 80
cupin_XRE_C cd02209
XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; ...
 393-451 1.51e-05

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: 43.26  E-value: 1.51e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15832090 393 IIVKPGEGLSLRMHHHRSEHWIVLSGTAKVTLGDKTKLVTANESIYIPLGAAYSLENPG 451
Cdd:cd02209  21 VTLPPGGSGGEPYSHEGEEFGYVLEGELELTVGGETYVLEAGDSIYFDSDVPHRYRNPG 79
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 8-227 2.46e-05

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: 45.26  E-value: 2.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090   8 AVVMAGGTGSRLWPLSrELYPKQFLQLSGdntllqttllrlsglscqKPL-----------------VITNEQHRfVVAE 70
Cdd:cd04181   1 AVILAAGKGTRLRPLT-DTRPKPLLPIAG------------------KPIleyiierlaragideiiLVVGYLGE-QIEE 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090  71 QLREINKLNGNI--ILEPCGRNTApaiaisafHALKRNP---QEDPlLLVLAADHVIakesvFCDAIKNATPIANQGKIV 145
Cdd:cd04181  61 YFGDGSKFGVNIeyVVQEEPLGTA--------GAVRNAEdflGDDD-FLVVNGDVLT-----DLDLSELLRFHREKGADA 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090 146 TFGIIPEYAETGYGYIERGelsvplqghentGFYYVNKFVEKPNRETAELymtsgnhyWNSGIFMFKASV--YLEELRKF 223
Cdd:cd04181 127 TIAVKEVEDPSRYGVVELD------------DDGRVTRFVEKPTLPESNL--------ANAGIYIFEPEIldYIPEILPR 186


                ....
gi 15832090 224 RPDI 227
Cdd:cd04181 187 GEDE 190
cupin_TcmJ-like cd06991
TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of ...
 393-458 5.26e-05

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: 42.28  E-value: 5.26e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15832090 393 IIVKPGEGLSLRMHHHRSEHWIVLSGTAKVTLGDKTKLVTANESIYIPLGAAYSLENPGIIPLNLI 458
Cdd:cd06991  24 LTLAPGERVSEHYHPYSEEFLYVVRGRLVVRVDGEPVVLEAGEALLVPRGVRHRLENAGDEPARLV 89
AllE COG3257
Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];
395-451 1.32e-04

Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 442488 [Multi-domain]  Cd Length: 262  Bit Score: 43.66  E-value: 1.32e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15832090 395 VKPGEGLSLRMHHHRSEHWI-VLSGTAKVTLGDKTKLVTANESIYIPLGAAYSLENPG 451
Cdd:COG3257  66 VAPGGGSDRPEPDPGAETFLfVLEGEVTLTLGGETHELTPGGYAYLPPGTPWTLRNAG 123
cupin_KdgF cd02238
pectin degradation protein KdgF and related proteins, cupin domain; This family includes ...
 405-440 2.13e-04

pectin degradation protein KdgF and related proteins, cupin domain; This family includes bacterial and archaeal pectin degradation protein KdgF that catalyzes the linearization of unsaturated uronates from both pectin and alginate, which are polysaccharides found in the cell walls of plants and brown algae, respectively, and represent an important source of carbon. These polysaccharides, mostly consisting of chains of uronates, can be metabolized by bacteria through a pathway of enzymatic steps to the key metabolite 2-keto-3-deoxygluconate (KDG). Pectin degradation is used by many plant-pathogenic bacteria during infection, and also, pectin and alginate can both represent abundant sources of carbohydrate for the production of biofuels. These proteins belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380366 [Multi-domain]  Cd Length: 104  Bit Score: 40.53  E-value: 2.13e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 15832090 405 MHHHRSEHW-IVLSGTAKVTLGDKTKLVTANESIYIP 440
Cdd:cd02238  42 LHSHPHEQIgYVLSGRFEFTIGGETRILKPGDSYYIP 78
cupin_HP0902-like cd02230
Helicobacter pylori HP0902 and related proteins, cupin domain; This family includes ...
 397-448 8.36e-04

Helicobacter pylori HP0902 and related proteins, cupin domain; This family includes prokaryotic and archaeal proteins homologous to HP0902, a functionally uncharacterized protein from Helicobacter pylori and Spy1581, a protein of unknown function from Streptococcus pyogenes. These proteins demonstrate all-beta cupin folds that cannot bind metal ions due to the absence of a metal-binding histidine that is conserved in many metallo-cupins. HP0902 is able to bind bacterial endotoxin lipopolysaccharides (LPS) through its surface-exposed loops, where metal-binding sites are usually found in other metallo-cupins, and thus may have a putative role in H. pylori pathogenicity.


Pssm-ID: 380358 [Multi-domain]  Cd Length: 83  Bit Score: 38.26  E-value: 8.36e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15832090 397 PGEGLSlrmhHHRSEHWI---VLSGTAKVTLGDKTKLVTANESIYIPLGAAYSLE 448
Cdd:cd02230  20 AGQELS----EHTAPGDAtvqVLEGEAEFTIGGETVTLKAGELIVMPANVPHALK 70
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 8-229 3.06e-03

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: 39.37  E-value: 3.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090   8 AVVMAGGTGSRLWPLSRELyPKQFLQLSGdntllqttllrlsglscqKPL---VITN-EQH---RFVV-----AEQLREI 75
Cdd:COG1208   2 AVILAGGLGTRLRPLTDTR-PKPLLPVGG------------------KPLlehILERlAAAgitEIVInvgylAEQIEEY 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090  76 ----NKLNGNIIL--EPCGRNTAPAIAisafHALKRnPQEDPlLLVLAADHVIAKEsvFCDAIKNAtpiANQGKIVTFGI 149
Cdd:COG1208  63 fgdgSRFGVRITYvdEGEPLGTGGALK----RALPL-LGDEP-FLVLNGDILTDLD--LAALLAFH---REKGADATLAL 131

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090 150 IPEYAETGYGYIErgelsvplqgHENTGfyYVNKFVEKPNRETAelymtsgnHYWNSGIFMFKASV--YLEELRKFR-PD 226
Cdd:COG1208 132 VPVPDPSRYGVVE----------LDGDG--RVTRFVEKPEEPPS--------NLINAGIYVLEPEIfdYIPEGEPFDlED 191


                ...
gi 15832090 227 IYN 229
Cdd:COG1208 192 LLP 194
cupin_YP766765-like cd20299
Rhizobium leguminosarum YP_766765.1 and related proteins, cupin domain; This family includes ...
 409-451 3.22e-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: 36.88  E-value: 3.22e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 15832090 409 RSEHWIVLSGTAKVTLGDKTKLVTANESIYIPLGAAYSLENPG 451
Cdd:cd20299  37 REKVYVVLEGELTVTTDGEEVVLGPGDSCYIPPGETRSIDNRT 79
cupin_UGlyAH_N cd02211
(S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain; This family ...
 415-458 4.30e-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: 4.30e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 15832090 415 VLSGTAKVTLGDKTKLVTANESIYIPLGAAYSLENPGIIPLNLI 458
Cdd:cd02211  53 VLEGEVELTVGGETHTLTAGGYAYLPPGTKHSLRNAGDEPARLL 96
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 393-476 4.31e-03

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: 36.87  E-value: 4.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090 393 IIVKPGeGLSlRMHHHRSEH--WIVLSGTAKVTLGDK-----TKLVTANESIYIPLGAAYSLENPGIIPLNLIEVSSGDY 465
Cdd:COG2140   8 TVLEPG-GVR-EEHWHPNAAewYYVLSGEARMTVQDPpgrarTVDVGPGDVVYVPPGYGHYIINTGDEPLVFLAVFDDDA 85

                        90
                ....*....|.
gi 15832090 466 LGEDDIIRQKE 476
Cdd:COG2140  86 GSDYGTISLSG 96
cupin_yp_001338853-like cd07008
Klebsiella pneumoniae yp_001338853.1 and related proteins, cupin domain; This family includes ...
 393-460 5.00e-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: 36.46  E-value: 5.00e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15832090 393 IIVKPGEGLSLRMHHHRSEHWIVLSGTAKVTLGD-KTKLVTANESIYIPLGAAYSLENPGIIPLNLIEV 460
Cdd:cd07008  32 WHVKPGQEIAAHIHPHGQDTWIVLSGEGEYLLGDgQTVPIKAGDIVIAPAGQVHGARNTGDEPLVFVSV 100
cupin_CENP-C_C cd06993
centromere-binding protein CENP-C, C-terminal cupin domain; This family includes centromeric ...
 392-451 5.85e-03

centromere-binding protein CENP-C, C-terminal cupin domain; This family includes centromeric protein C (CENP-C; known as Mif2 in budding yeast and centromere protein 3 or cnp3 in fission yeast), which is an inner kinetochore centromere (CEN)-binding protein found in fungi and metazoans. CENP-C is a component of the CENP-A nucleosome-associated complex (NAC) that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. CENP-C localizes to the inner kinetochore plates adjacent to the centromeric DNA and is known to have DNA-binding ability. CENP-C, along with CENP-H, provides a platform onto which the mitotic kinetochore is assembled and thus plays a critical role in the structuring of kinethocore chromatin. The cupin domain at the C-terminus forms a homodimer which is part of an enhanceosome-like structure that nucleates kinetochore assembly in budding yeast. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380398 [Multi-domain]  Cd Length: 77  Bit Score: 35.60  E-value: 5.85e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832090 392 KIIVKPGEGLSLRMHHHRSEHWIVLSGTAKVTLGDKTKLVTANESIYIPLGAAYSLENPG 451
Cdd:cd06993   7 MLELPPGGEKPLKNSKDNTYVFYVIQGAVEVTLHETTFVVTKGCSFQVPRGNYYSIKNIG 66
 
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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