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Conserved domains on  [gi|505178706|ref|WP_015365808|]
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mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase [Klebsiella aerogenes]

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 ...
 2-470 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: 795.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706    2 LLPVVMAGGTGSRLWPMSRELYPKQFLRLFGQNSMLQETITRLSGLEIYEPMVICNEEHRFLVAEQLRQLNKLSNNIILE 81
Cdd:TIGR01479   1 IIPVILAGGSGTRLWPLSRELYPKQFLALVGDLTMLQQTLKRLAGLPCSSPLVICNEEHRFIVAEQLREIGKLASNIILE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706   82 PVGRNTAPAIALAALQATR-QGDDPLMLVLAADHIINNQPVFHDAIRVAEQYADAGHLVTFGIVPNAPETGYGYIQRGVA 160
Cdd:TIGR01479  81 PVGRNTAPAIALAALLAARrNGEDPLLLVLAADHVITDEDAFQAAVKLAMPAAAEGKLVTFGIVPTHPETGYGYIRRGAP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  161 LSdsAHTPYQVARFVEKPDRERAEAYLASGEYYWNSGMFMFRAKKYLSELAKFRPDILEACQAAVNAADNGSDFISIPHD 240
Cdd:TIGR01479 161 LA--GEDVYQVQRFVEKPDLATAQAYLESGDYYWNSGMFLFRASRYLAELKKHAPDIYEACEAAVEASEPDLDFIRLDKE 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  241 IFCECPDESVDYAVMEKTADAVVVGLDADWSDVGSWSALWEVSPKDEQGNVLSGDAWVHNSENCYINSDEKLVAAIGVEN 320
Cdd:TIGR01479 239 AFEQCPSESIDYAVMEKTADAVVVPMDAGWSDVGSWSALWEISDKDADGNVLKGDVLTHDTKNSYIYSESRLVAVVGVED 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  321 LVIVSTKDAVLVMNRERSQDVKKAVEFLKQNQRSEYKRHREIYRPWGRCDVVVQTPRFNVNRITVKPGGAFSMQMHHHRA 400
Cdd:TIGR01479 319 LVVVETKDAVLVAHKDRVQDVKKIVEQLKADGRTETEQHREVYRPWGKYDSIDQGDRYQVKRITVKPGEKLSLQMHHHRA 398

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  401 EHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEVLEIQSGSYLGEDDIIRIKDQYGR 470
Cdd:TIGR01479 399 EHWIVVSGTARVTIGDETLLLTENESTYIPLGVIHRLENPGKIPLELIEVQSGSYLGEDDIIRFEDRYGR 468
 
Name Accession Description Interval E-value
GMP_PMI TIGR01479
mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to ...
 2-470 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: 795.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706    2 LLPVVMAGGTGSRLWPMSRELYPKQFLRLFGQNSMLQETITRLSGLEIYEPMVICNEEHRFLVAEQLRQLNKLSNNIILE 81
Cdd:TIGR01479   1 IIPVILAGGSGTRLWPLSRELYPKQFLALVGDLTMLQQTLKRLAGLPCSSPLVICNEEHRFIVAEQLREIGKLASNIILE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706   82 PVGRNTAPAIALAALQATR-QGDDPLMLVLAADHIINNQPVFHDAIRVAEQYADAGHLVTFGIVPNAPETGYGYIQRGVA 160
Cdd:TIGR01479  81 PVGRNTAPAIALAALLAARrNGEDPLLLVLAADHVITDEDAFQAAVKLAMPAAAEGKLVTFGIVPTHPETGYGYIRRGAP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  161 LSdsAHTPYQVARFVEKPDRERAEAYLASGEYYWNSGMFMFRAKKYLSELAKFRPDILEACQAAVNAADNGSDFISIPHD 240
Cdd:TIGR01479 161 LA--GEDVYQVQRFVEKPDLATAQAYLESGDYYWNSGMFLFRASRYLAELKKHAPDIYEACEAAVEASEPDLDFIRLDKE 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  241 IFCECPDESVDYAVMEKTADAVVVGLDADWSDVGSWSALWEVSPKDEQGNVLSGDAWVHNSENCYINSDEKLVAAIGVEN 320
Cdd:TIGR01479 239 AFEQCPSESIDYAVMEKTADAVVVPMDAGWSDVGSWSALWEISDKDADGNVLKGDVLTHDTKNSYIYSESRLVAVVGVED 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  321 LVIVSTKDAVLVMNRERSQDVKKAVEFLKQNQRSEYKRHREIYRPWGRCDVVVQTPRFNVNRITVKPGGAFSMQMHHHRA 400
Cdd:TIGR01479 319 LVVVETKDAVLVAHKDRVQDVKKIVEQLKADGRTETEQHREVYRPWGKYDSIDQGDRYQVKRITVKPGEKLSLQMHHHRA 398

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  401 EHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEVLEIQSGSYLGEDDIIRIKDQYGR 470
Cdd:TIGR01479 399 EHWIVVSGTARVTIGDETLLLTENESTYIPLGVIHRLENPGKIPLELIEVQSGSYLGEDDIIRFEDRYGR 468
cpsB PRK15460
mannose-1-phosphate guanyltransferase; Provisional
 2-470 0e+00

mannose-1-phosphate guanyltransferase; Provisional


Pssm-ID: 185357 [Multi-domain]  Cd Length: 478  Bit Score: 711.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706   2 LLPVVMAGGTGSRLWPMSRELYPKQFLRLFGQNSMLQETITRLSGLEIYEPMVICNEEHRFLVAEQLRQLNKLSNNIILE 81
Cdd:PRK15460   6 LYPVVMAGGSGSRLWPLSRVLYPKQFLCLKGDLTMLQTTICRLNGVECESPVVICNEQHRFIVAEQLRQLNKLTENIILE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  82 PVGRNTAPAIALAALQATRQG--DDPLMLVLAADHIINNQPVFHDAIRVAEQYADAGHLVTFGIVPNAPETGYGYIQRG- 158
Cdd:PRK15460  86 PAGRNTAPAIALAALAAKRHSpeSDPLMLVLAADHVIADEDAFRAAVRNAMPYAEAGKLVTFGIVPDLPETGYGYIRRGe 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 159 VALSDSAHTPYQVARFVEKPDRERAEAYLASGEYYWNSGMFMFRAKKYLSELAKFRPDILEACQAAVNAADNGSDFISIP 238
Cdd:PRK15460 166 VSAGEQDTVAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDPDLDFIRVD 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 239 HDIFCECPDESVDYAVMEKTADAVVVGLDADWSDVGSWSALWEVSPKDEQGNVLSGDAWVHNSENCYINSDEKLVAAIGV 318
Cdd:PRK15460 246 EEAFLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSLWEISAHTAEGNVCHGDVINHKTENSYVYAESGLVTTVGV 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 319 ENLVIVSTKDAVLVMNRERSQDVKKAVEFLKQNQRSEYKRHREIYRPWGRCDVVVQTPRFNVNRITVKPGGAFSMQMHHH 398
Cdd:PRK15460 326 KDLVVVQTKDAVLIADRNAVQDVKKVVEQIKADGRHEHRVHREVYRPWGKYDSIDAGDRYQVKRITVKPGEGLSVQMHHH 405

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505178706 399 RAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEVLEIQSGSYLGEDDIIRIKDQYGR 470
Cdd:PRK15460 406 RAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLIEVRSGSYLEEDDVVRFADRYGR 477
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-350 0e+00

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 603.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706   1 MLLPVVMAGGTGSRLWPMSRELYPKQFLRLFGQNSMLQETITRLSGLEIYE-PMVICNEEHRFLVAEQLRQLNKlsNNII 79
Cdd:COG0836    2 MIYPVILAGGSGTRLWPLSRESYPKQFLPLLGEKSLLQQTVERLAGLVPPEnILVVTNEEHRFLVAEQLPELGP--ANIL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  80 LEPVGRNTAPAIALAALQATRQGDDPLMLVLAADHIINNQPVFHDAIRVAEQYADAGHLVTFGIVPNAPETGYGYIQRGV 159
Cdd:COG0836   80 LEPVGRNTAPAIALAALLIAKRDPDAVLLVLPADHLIEDEEAFREAVRAAVEAAEAGKLVTFGIKPTRPETGYGYIEAGE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 160 ALSDSahTPYQVARFVEKPDRERAEAYLASGEYYWNSGMFMFRAKKYLSELAKFRPDILEACQAAVNAADNGSDFISIPh 239
Cdd:COG0836  160 ALGGA--GAYKVKRFVEKPDLETAEEYLASGNYLWNSGMFVFRASTILEELERHAPEIYAALEAAVAAAGTDLEVRLDA- 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 240 DIFCECPDESVDYAVMEKTADAVVVGLDADWSDVGSWSALWEVSPKDEQGNVLSGDAWVHNSENCYINSDEKLVAAIGVE 319
Cdd:COG0836  237 EAFAALPSISIDYAVMEKADNVAVVPADFGWSDVGSWDALWELLEKDENGNVVLGDVLLIDSSNSLVRSEGRLVAVIGVE 316

                        330       340       350
                 ....*....|....*....|....*....|.
gi 505178706 320 NLVIVSTKDAVLVMNRERSQDVKKAVEFLKQ 350
Cdd:COG0836  317 DLVVVDTPDALLVAPKDRAQEVKKIVEALKE 347
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 4-279 2.98e-146

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: 418.52  E-value: 2.98e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706   4 PVVMAGGTGSRLWPMSRELYPKQFLRLFGQNSMLQETITRLSGLEIYE-PMVICNEEHRFLVAEQLRQLNKlSNNIILEP 82
Cdd:cd02509    3 PVILAGGSGTRLWPLSRESYPKQFLKLFGDKSLLQQTLDRLKGLVPPDrILVVTNEEYRFLVREQLPEGLP-EENIILEP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  83 VGRNTAPAIALAALQATRQGDDPLMLVLAADHIINNQPVFHDAIRVAEQYADAGHLVTFGIVPNAPETGYGYIQRGVALS 162
Cdd:cd02509   82 EGRNTAPAIALAALYLAKRDPDAVLLVLPSDHLIEDVEAFLKAVKKAVEAAEEGYLVTFGIKPTRPETGYGYIEAGEKLG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 163 DSAhtpYQVARFVEKPDRERAEAYLASGEYYWNSGMFMFRAKKYLSELAKFRPDILEACQAAVNAADNGsDFISIPHDIF 242
Cdd:cd02509  162 GGV---YRVKRFVEKPDLETAKEYLESGNYLWNSGIFLFRAKTFLEELKKHAPDIYEALEKALAAAGTD-DFLRLLEEAF 237

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 505178706 243 CECPDESVDYAVMEKTADAVVVGLDADWSDVGSWSAL 279
Cdd:cd02509  238 AKIPSISIDYAVMEKTKKVAVVPADFGWSDLGSWDAL 274
MannoseP_isomer pfam01050
Mannose-6-phosphate isomerase; All of the members of this Pfam entry belong to family 2 of the ...
 316-466 2.04e-81

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: 248.49  E-value: 2.04e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  316 IGVENLVIVSTKDAVLVMNRERSQDVKKAVEFLKQNQRSEYKRHREIYRPWGRCDVVVQTPRFNVNRITVKPGGAFSMQM 395
Cdd:pfam01050   1 IGVENLVVVETKDALLVAHKDKVQDVKKVVEELKENGRSEHQTHREVYRPWGSYDVIDEGERYQVKRITVKPGARLSLQM 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505178706  396 HHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEVLEIQSGSYLGEDDIIRIKD 466
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 ...
 2-470 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: 795.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706    2 LLPVVMAGGTGSRLWPMSRELYPKQFLRLFGQNSMLQETITRLSGLEIYEPMVICNEEHRFLVAEQLRQLNKLSNNIILE 81
Cdd:TIGR01479   1 IIPVILAGGSGTRLWPLSRELYPKQFLALVGDLTMLQQTLKRLAGLPCSSPLVICNEEHRFIVAEQLREIGKLASNIILE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706   82 PVGRNTAPAIALAALQATR-QGDDPLMLVLAADHIINNQPVFHDAIRVAEQYADAGHLVTFGIVPNAPETGYGYIQRGVA 160
Cdd:TIGR01479  81 PVGRNTAPAIALAALLAARrNGEDPLLLVLAADHVITDEDAFQAAVKLAMPAAAEGKLVTFGIVPTHPETGYGYIRRGAP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  161 LSdsAHTPYQVARFVEKPDRERAEAYLASGEYYWNSGMFMFRAKKYLSELAKFRPDILEACQAAVNAADNGSDFISIPHD 240
Cdd:TIGR01479 161 LA--GEDVYQVQRFVEKPDLATAQAYLESGDYYWNSGMFLFRASRYLAELKKHAPDIYEACEAAVEASEPDLDFIRLDKE 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  241 IFCECPDESVDYAVMEKTADAVVVGLDADWSDVGSWSALWEVSPKDEQGNVLSGDAWVHNSENCYINSDEKLVAAIGVEN 320
Cdd:TIGR01479 239 AFEQCPSESIDYAVMEKTADAVVVPMDAGWSDVGSWSALWEISDKDADGNVLKGDVLTHDTKNSYIYSESRLVAVVGVED 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  321 LVIVSTKDAVLVMNRERSQDVKKAVEFLKQNQRSEYKRHREIYRPWGRCDVVVQTPRFNVNRITVKPGGAFSMQMHHHRA 400
Cdd:TIGR01479 319 LVVVETKDAVLVAHKDRVQDVKKIVEQLKADGRTETEQHREVYRPWGKYDSIDQGDRYQVKRITVKPGEKLSLQMHHHRA 398

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  401 EHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEVLEIQSGSYLGEDDIIRIKDQYGR 470
Cdd:TIGR01479 399 EHWIVVSGTARVTIGDETLLLTENESTYIPLGVIHRLENPGKIPLELIEVQSGSYLGEDDIIRFEDRYGR 468
cpsB PRK15460
mannose-1-phosphate guanyltransferase; Provisional
 2-470 0e+00

mannose-1-phosphate guanyltransferase; Provisional


Pssm-ID: 185357 [Multi-domain]  Cd Length: 478  Bit Score: 711.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706   2 LLPVVMAGGTGSRLWPMSRELYPKQFLRLFGQNSMLQETITRLSGLEIYEPMVICNEEHRFLVAEQLRQLNKLSNNIILE 81
Cdd:PRK15460   6 LYPVVMAGGSGSRLWPLSRVLYPKQFLCLKGDLTMLQTTICRLNGVECESPVVICNEQHRFIVAEQLRQLNKLTENIILE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  82 PVGRNTAPAIALAALQATRQG--DDPLMLVLAADHIINNQPVFHDAIRVAEQYADAGHLVTFGIVPNAPETGYGYIQRG- 158
Cdd:PRK15460  86 PAGRNTAPAIALAALAAKRHSpeSDPLMLVLAADHVIADEDAFRAAVRNAMPYAEAGKLVTFGIVPDLPETGYGYIRRGe 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 159 VALSDSAHTPYQVARFVEKPDRERAEAYLASGEYYWNSGMFMFRAKKYLSELAKFRPDILEACQAAVNAADNGSDFISIP 238
Cdd:PRK15460 166 VSAGEQDTVAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDPDLDFIRVD 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 239 HDIFCECPDESVDYAVMEKTADAVVVGLDADWSDVGSWSALWEVSPKDEQGNVLSGDAWVHNSENCYINSDEKLVAAIGV 318
Cdd:PRK15460 246 EEAFLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSLWEISAHTAEGNVCHGDVINHKTENSYVYAESGLVTTVGV 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 319 ENLVIVSTKDAVLVMNRERSQDVKKAVEFLKQNQRSEYKRHREIYRPWGRCDVVVQTPRFNVNRITVKPGGAFSMQMHHH 398
Cdd:PRK15460 326 KDLVVVQTKDAVLIADRNAVQDVKKVVEQIKADGRHEHRVHREVYRPWGKYDSIDAGDRYQVKRITVKPGEGLSVQMHHH 405

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505178706 399 RAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEVLEIQSGSYLGEDDIIRIKDQYGR 470
Cdd:PRK15460 406 RAEHWVVVAGTAKVTIDGDIKLLGENESIYIPLGATHCLENPGKIPLDLIEVRSGSYLEEDDVVRFADRYGR 477
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-350 0e+00

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 603.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706   1 MLLPVVMAGGTGSRLWPMSRELYPKQFLRLFGQNSMLQETITRLSGLEIYE-PMVICNEEHRFLVAEQLRQLNKlsNNII 79
Cdd:COG0836    2 MIYPVILAGGSGTRLWPLSRESYPKQFLPLLGEKSLLQQTVERLAGLVPPEnILVVTNEEHRFLVAEQLPELGP--ANIL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  80 LEPVGRNTAPAIALAALQATRQGDDPLMLVLAADHIINNQPVFHDAIRVAEQYADAGHLVTFGIVPNAPETGYGYIQRGV 159
Cdd:COG0836   80 LEPVGRNTAPAIALAALLIAKRDPDAVLLVLPADHLIEDEEAFREAVRAAVEAAEAGKLVTFGIKPTRPETGYGYIEAGE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 160 ALSDSahTPYQVARFVEKPDRERAEAYLASGEYYWNSGMFMFRAKKYLSELAKFRPDILEACQAAVNAADNGSDFISIPh 239
Cdd:COG0836  160 ALGGA--GAYKVKRFVEKPDLETAEEYLASGNYLWNSGMFVFRASTILEELERHAPEIYAALEAAVAAAGTDLEVRLDA- 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 240 DIFCECPDESVDYAVMEKTADAVVVGLDADWSDVGSWSALWEVSPKDEQGNVLSGDAWVHNSENCYINSDEKLVAAIGVE 319
Cdd:COG0836  237 EAFAALPSISIDYAVMEKADNVAVVPADFGWSDVGSWDALWELLEKDENGNVVLGDVLLIDSSNSLVRSEGRLVAVIGVE 316

                        330       340       350
                 ....*....|....*....|....*....|.
gi 505178706 320 NLVIVSTKDAVLVMNRERSQDVKKAVEFLKQ 350
Cdd:COG0836  317 DLVVVDTPDALLVAPKDRAQEVKKIVEALKE 347
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 4-279 2.98e-146

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: 418.52  E-value: 2.98e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706   4 PVVMAGGTGSRLWPMSRELYPKQFLRLFGQNSMLQETITRLSGLEIYE-PMVICNEEHRFLVAEQLRQLNKlSNNIILEP 82
Cdd:cd02509    3 PVILAGGSGTRLWPLSRESYPKQFLKLFGDKSLLQQTLDRLKGLVPPDrILVVTNEEYRFLVREQLPEGLP-EENIILEP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  83 VGRNTAPAIALAALQATRQGDDPLMLVLAADHIINNQPVFHDAIRVAEQYADAGHLVTFGIVPNAPETGYGYIQRGVALS 162
Cdd:cd02509   82 EGRNTAPAIALAALYLAKRDPDAVLLVLPSDHLIEDVEAFLKAVKKAVEAAEEGYLVTFGIKPTRPETGYGYIEAGEKLG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 163 DSAhtpYQVARFVEKPDRERAEAYLASGEYYWNSGMFMFRAKKYLSELAKFRPDILEACQAAVNAADNGsDFISIPHDIF 242
Cdd:cd02509  162 GGV---YRVKRFVEKPDLETAKEYLESGNYLWNSGIFLFRAKTFLEELKKHAPDIYEALEKALAAAGTD-DFLRLLEEAF 237

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 505178706 243 CECPDESVDYAVMEKTADAVVVGLDADWSDVGSWSAL 279
Cdd:cd02509  238 AKIPSISIDYAVMEKTKKVAVVPADFGWSDLGSWDAL 274
MannoseP_isomer pfam01050
Mannose-6-phosphate isomerase; All of the members of this Pfam entry belong to family 2 of the ...
 316-466 2.04e-81

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: 248.49  E-value: 2.04e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  316 IGVENLVIVSTKDAVLVMNRERSQDVKKAVEFLKQNQRSEYKRHREIYRPWGRCDVVVQTPRFNVNRITVKPGGAFSMQM 395
Cdd:pfam01050   1 IGVENLVVVETKDALLVAHKDKVQDVKKVVEELKENGRSEHQTHREVYRPWGSYDVIDEGERYQVKRITVKPGARLSLQM 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505178706  396 HHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEVLEIQSGSYLGEDDIIRIKD 466
Cdd:pfam01050  81 HHHRAEHWIVVSGTARVTKGGETFLLTENESTYIPLGTIHRLENPGKIPLELIEVQSGSYLGEDDIVRFED 151
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 3-287 8.92e-81

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: 250.25  E-value: 8.92e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706    3 LPVVMAGGTGSRLWPMSRELYPKQFLRLFGQnSMLQETITRLSGLEIYEPMVICNEEHRFLVAEQLRQLNKLSNNI--IL 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKY-PLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQItyAL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706   81 EPVGRNTAPAIALAALQATRQGDDplMLVLAADHIInnQPVFHDAIRVAEQYAdAGHLVTFGIVPNAPETGYGYIQRGVA 160
Cdd:pfam00483  80 QPEGKGTAPAVALAADFLGDEKSD--VLVLGGDHIY--RMDLEQAVKFHIEKA-ADATVTFGIVPVEPPTGYGVVEFDDN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  161 lsdsahtpYQVARFVEKPDRERAEAYLASGEYYWNSGMFMFRAKkYLSELAKFRPDILEACQAAVNAADngsdfisiphd 240
Cdd:pfam00483 155 --------GRVIRFVEKPKLPKASNYASMGIYIFNSGVLDFLAK-YLEELKRGEDEITDILPKALEDGK----------- 214

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 505178706  241 ifcecpdesVDYAVMEKtadavvvglDADWSDVGSWSALWEVSPKDE 287
Cdd:pfam00483 215 ---------LAYAFIFK---------GYAWLDVGTWDSLWEANLFLL 243
cupin_PMI_typeII_C cd02213
Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal ...
 337-464 4.21e-67

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: 210.88  E-value: 4.21e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 337 RSQDVKKAVEFLKQNQRSEykRHREIYRPWGRCDVVVQTPRFNVNRITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNG 416
Cdd:cd02213    1 KSQRVKEIVEELKKRGRSE--EHRTVYRPWGSYEVLDEGEGYKVKRLTVNPGKRLSLQRHHHRSEHWVVVSGTAEVTLDG 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 505178706 417 KQFLLTENQSTFIPIGAEHSLENPGRIPLEVLEIQSGSYLGEDDIIRI 464
Cdd:cd02213   79 KEKLLKEGESIYIPKGTKHRLENPGKIPLEIIEVQTGEYLGEDDIVRL 126
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
364-463 5.17e-36

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 129.11  E-value: 5.17e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 364 RPWGRCDVVVQ-TPRFNVNRITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGR 442
Cdd:COG0662   12 IGWGSYEVLGEgGERLSVKRITVPPGAELSLHVHPHRDEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAGVPHRLRNPGD 91

                         90       100
                 ....*....|....*....|.
gi 505178706 443 IPLEVLEIQSGSYLGEDDIIR 463
Cdd:COG0662   92 EPLELLEVQAPAYLGEDDIVR 112
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
 360-459 1.76e-12

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


Pssm-ID: 380344 [Multi-domain]  Cd Length: 100  Bit Score: 63.31  E-value: 1.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 360 REIYRPwgrcdVVVQTPRFNVNRITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLEN 439
Cdd:cd02214    6 RELLHP-----DNDGDPRYSLAHARVPPGESTLPHRLKGSEEVYYILEGEGTMEIDGEPREVGPGDAVLIPPGAVQRIEN 80

                         90       100
                 ....*....|....*....|
gi 505178706 440 PGRIPLEVLEIQSGSYLGED 459
Cdd:cd02214   81 TGEEDLVFLCICSPAWSPED 100
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 382-450 8.71e-12

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: 60.35  E-value: 8.71e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505178706  382 RITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEVLEI 450
Cdd:pfam07883   2 LVTLPPGESSPPHRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLLDV 70
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
 376-446 1.75e-11

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


Pssm-ID: 380351 [Multi-domain]  Cd Length: 91  Bit Score: 60.16  E-value: 1.75e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505178706 376 PRFNVNRITVKPGGafSMQMHHHRAEHWV-ILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLE 446
Cdd:cd02222   15 PNFAMRYFEIEPGG--HTPLHTHPWEHEVyVLRGKGVVVIGGEEYPVKPGDVVYIPPNEPHQFRNTGDEPLG 84
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
358-452 3.78e-11

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 59.48  E-value: 3.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 358 RHREIYRPWGRCDVVVQTP-RFNVNRITVKPGGafSMQMHHHRA-EHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEH 435
Cdd:COG1917    2 RLAEIALTGVSVRVLADGEdELEVVRVTFEPGA--RTPWHSHPGeELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPH 79

                         90
                 ....*....|....*..
gi 505178706 436 SLENPGRIPLEVLEIQS 452
Cdd:COG1917   80 AFRNLGDEPAVLLVVFS 96
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
377-466 9.67e-11

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 58.88  E-value: 9.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 377 RFNVNRITVKPGGAFSMQMHHHRAEHWV-ILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEVLEIqsGSY 455
Cdd:COG3837   27 RLGVNLITLPPGASSSPYHAHSAEEEFVyVLEGELTLRIGGEEYVLEPGDSVGFPAGVPHRLRNRGDEPARYLVV--GTR 104

                         90
                 ....*....|.
gi 505178706 456 LGEDDIIRIKD 466
Cdd:COG3837  105 APYPDSFDYWD 115
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 5-274 1.08e-10

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


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 61.06  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706   5 VVMAGGTGSRLWPMSrELYPKQFLRLFGQnSMLQETITRLSGLEIYEPMVICNEEHRfLVAEQLRQLNKLSNNI--ILEP 82
Cdd:cd04181    2 VILAAGKGTRLRPLT-DTRPKPLLPIAGK-PILEYIIERLARAGIDEIILVVGYLGE-QIEEYFGDGSKFGVNIeyVVQE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  83 VGRNTAPAIALAalqATRQGDDPLmLVLAADHIINNqpvfhDAIRVAEQYADAGHLVTFGIVPNAPETGYGYIQrgvaLS 162
Cdd:cd04181   79 EPLGTAGAVRNA---EDFLGDDDF-LVVNGDVLTDL-----DLSELLRFHREKGADATIAVKEVEDPSRYGVVE----LD 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 163 DSahtpYQVARFVEKPDREraEAYLASGEYYwnsgmfmfrakkylselaKFRPDILEACQAavnaadNGSDFISIPHDIF 242
Cdd:cd04181  146 DD----GRVTRFVEKPTLP--ESNLANAGIY------------------IFEPEILDYIPE------ILPRGEDELTDAI 195

                        250       260       270
                 ....*....|....*....|....*....|..
gi 505178706 243 cecpdesvDYAVMEKTADAVVVglDADWSDVG 274
Cdd:cd04181  196 --------PLLIEEGKVYGYPV--DGYWLDIG 217
cupin_TM1287-like cd02221
Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial ...
 382-448 4.19e-10

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: 56.32  E-value: 4.19e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505178706 382 RITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEVL 448
Cdd:cd02221   23 RVTLPPGSSIGYHQHEGEFEIYYILSGEGLYTDNGKEYEVKAGDVTFTRDGESHGIENTGDEDLVFI 89
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 380-450 9.57e-09

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: 52.10  E-value: 9.57e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505178706 380 VNRITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVN-GKQFLLTENQSTFIPIGAEHSLENPGRIPLEVLEI 450
Cdd:cd02208    1 ISVVTLPPGTSSPPHWHPEQDEIFYVLSGEGELTLDdGETVELKAGDIVLIPPGVPHSFVNTSDEPAVFLVV 72
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 5-220 2.05e-08

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: 54.77  E-value: 2.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706   5 VVMAGGTGSRLWPMSRELyPKQFLRLFGQnSMLQETITRLSGLEIYEpMVICneeHRFLvAEQLRQ-LNKLSN-----NI 78
Cdd:COG1208    3 VILAGGLGTRLRPLTDTR-PKPLLPVGGK-PLLEHILERLAAAGITE-IVIN---VGYL-AEQIEEyFGDGSRfgvriTY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  79 ILEPVGRNTAPAIALAA--LqatrqGDDPLmLVLAADHIINnqpvfHDAIRVAEQYADAGHLVTFGIVPNAPETGYGYiq 156
Cdd:COG1208   76 VDEGEPLGTGGALKRALplL-----GDEPF-LVLNGDILTD-----LDLAALLAFHREKGADATLALVPVPDPSRYGV-- 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505178706 157 rgVALSDSahtpYQVARFVEKPdrERAEAYLAsgeyywNSGMFMFRAK--KYLSELAKFR-PDILEA 220
Cdd:COG1208  143 --VELDGD----GRVTRFVEKP--EEPPSNLI------NAGIYVLEPEifDYIPEGEPFDlEDLLPR 195
cupin_Bh2720-like cd02223
Bacillus halodurans Bh2720 and related proteins, cupin domain; This family includes bacterial, ...
 384-452 5.67e-08

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


Pssm-ID: 380352 [Multi-domain]  Cd Length: 98  Bit Score: 50.62  E-value: 5.67e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505178706 384 TVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEVLEIQS 452
Cdd:cd02223   17 SIPPGEDIGLEVHDDVDQFLRIEEGEGKAIMGGFESEVKDGDAIIVPAGTWHNVINTGNEPLKLYTIYA 85
cupin_SPO2919-like cd02224
Silicibacter pomeroyi SPO2919 and related proteins, uncharacterized sugar phosphate isomerase ...
 377-450 4.03e-07

Silicibacter pomeroyi SPO2919 and related proteins, uncharacterized sugar phosphate isomerase with a cupin domain; This family includes proteins similar to sugar phosphate isomerase SPO2919 from Silicibacter pomeroyi and Afe_0303 from Acidithiobacillus ferrooxidans, but are as yet uncharacterized. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer.


Pssm-ID: 380353 [Multi-domain]  Cd Length: 105  Bit Score: 48.25  E-value: 4.03e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505178706 377 RFNVNRITVKPGgAFSMQMHHHRA--EHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAE--HSLENPGRIPLEVLEI 450
Cdd:cd02224   16 QLGVNLERLPPG-ARSSPRHWHSAeeEFVYVLSGEGTLRLDGEEVLPRPGDFVGFPAGTGvaHQLINRSDEPLVYLVV 92
cupin_DddK cd06988
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ...
 383-450 6.20e-07

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


Pssm-ID: 380393 [Multi-domain]  Cd Length: 76  Bit Score: 46.85  E-value: 6.20e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505178706 383 ITVKPGGAfSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEVLEI 450
Cdd:cd06988    7 CVVRPGTT-STPHSHHEYEIFIVISGKGIVVVDGEREPVKAGDVVYIPPGTEHYVKNDGDEDFEFYSI 73
AllE COG3257
Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];
366-451 1.17e-06

Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 442488 [Multi-domain]  Cd Length: 262  Bit Score: 49.82  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 366 WGRCDVVVQ-TP----RFNVNRITVKPGGAFSMQMHHHRAEHWV-ILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLEN 439
Cdd:COG3257   42 WENTRVWILaRPlsgaTFSQYIVEVAPGGGSDRPEPDPGAETFLfVLEGEVTLTLGGETHELTPGGYAYLPPGTPWTLRN 121

                         90
                 ....*....|..
gi 505178706 440 PGRIPLEVLEIQ 451
Cdd:COG3257  122 AGDEPARFHWIR 133
cupin_TcmJ-like cd06991
TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of ...
 383-447 1.75e-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: 46.52  E-value: 1.75e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505178706 383 ITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEV 447
Cdd:cd06991   24 LTLAPGERVSEHYHPYSEEFLYVVRGRLVVRVDGEPVVLEAGEALLVPRGVRHRLENAGDEPARL 88
cupin_OxDC_C cd20305
Oxalate decarboxylase (OxDC), C-terminal cupin domain; This model represents the C-terminal ...
 383-455 6.25e-06

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: 46.04  E-value: 6.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 383 ITVKPGGAfsMQMH-HHRAEHW-VILAGTGQVTVngkqFLLTENQSTF---------IPIGAEHSLENPGRIPLEVLEI- 450
Cdd:cd20305   39 VTLEPGAL--RELHwHPNADEWqYYISGKARMTV----FASGGRARTFdfqagdvgyVPRGYGHYIENTGDEPLEFLEVf 112


                 ....*
gi 505178706 451 QSGSY 455
Cdd:cd20305  113 NSGRY 117
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 383-466 9.33e-06

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: 44.57  E-value: 9.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 383 ITVKPGGAFSMQMHHHRAEHWVILAGTGQVTV---NGKQFL--LTENQSTFIPIGAEHSLENPGRIPLEVLEIQSGSYLG 457
Cdd:COG2140    8 TVLEPGGVREEHWHPNAAEWYYVLSGEARMTVqdpPGRARTvdVGPGDVVYVPPGYGHYIINTGDEPLVFLAVFDDDAGS 87


                 ....*....
gi 505178706 458 EDDIIRIKD 466
Cdd:COG2140   88 DYGTISLSG 96
cupin_XRE_C cd02209
XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; ...
 377-448 1.08e-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: 43.65  E-value: 1.08e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505178706 377 RFNVNRITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEVL 448
Cdd:cd02209   15 KMEPFLVTLPPGGSGGEPYSHEGEEFGYVLEGELELTVGGETYVLEAGDSIYFDSDVPHRYRNPGDEPARVL 86
cupin_XcTcmJ-like cd07006
Xanthomonas campestris XcTcmJ and related proteins, cupin domain; This family includes ...
 370-450 1.44e-05

Xanthomonas campestris XcTcmJ and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to plant pathogen Xanthomonas campestris tetracenomycin polyketide synthesis protein XcTcmJ, a protein encoded by the tcmJ gene. XcTcmJ is annotated as being involved in tetracenomycin polyketide biosynthesis. Also included is Xc5357 from a different strain of X. campestris. Structure studies show that binding of zinc induces conformational changes and serves a functional role in this cupin protein. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380409 [Multi-domain]  Cd Length: 89  Bit Score: 43.51  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 370 DVVVQTPRFNVNRITVKPGGAF-SMQMHHHRAEHWV-ILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEV 447
Cdd:cd07006    2 RVLAGTERSQAATMVLAPGDTEgGPDNRHRGSDQWLyVVSGSGEAIVEGERVALKPGSLLLIEAGETHEIRNTGDEPLKT 81


                 ...
gi 505178706 448 LEI 450
Cdd:cd07006   82 LNF 84
cupin_MAE_RS03005 cd06987
Microcystis aeruginosa MAE_RS03005 and related proteins, cupin domain; This family includes ...
 386-441 1.69e-05

Microcystis aeruginosa MAE_RS03005 and related proteins, cupin domain; This family includes bacterial and some eukaryotic proteins homologous to MAE_RS03005, a Microcystis aeruginosa 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: 380392 [Multi-domain]  Cd Length: 122  Bit Score: 44.18  E-value: 1.69e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 505178706 386 KPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPG 441
Cdd:cd06987   36 DPGGRTPPNTHPAAHEMFFVLAGEGRAYCDGQRVPLRPGDALVVPPGSEHVIENTG 91
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 5-127 2.86e-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: 45.12  E-value: 2.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706   5 VVMAGGTGSRlwpMSRELyPKQFLRLFGQnSMLQETITRLSGL-EIYEPMVICNEEHRFLVAEQLRQLNKLSNNIILEpv 83
Cdd:COG1211    1 IIPAAGSGSR---MGAGI-PKQFLPLGGK-PVLEHTLEAFLAHpRIDEIVVVVPPDDIEYFEELLAKYGIDKPVRVVA-- 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 505178706  84 GRNTAPAIALAALQATRQGDDplmLVLaadhiinnqpvFHDAIR 127
Cdd:COG1211   74 GGATRQDSVRNGLEALPDDDD---WVL-----------VHDAAR 103
cupin_TTHA0104 cd06122
Thermus thermophilus TTHA0104 and related proteins, cupin domain; This family contains ...
 374-448 3.34e-05

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


Pssm-ID: 380377 [Multi-domain]  Cd Length: 102  Bit Score: 42.54  E-value: 3.34e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505178706 374 QTPRFNVNRITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEVL 448
Cdd:cd06122   23 ESERLFCDLYCLEPGQSQKVHAHAGSDKVYFVLEGEGRFTVGDEERELGAGEAVLAPAGVPHGVRNTGAERLVLL 97
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 5-127 3.43e-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: 44.82  E-value: 3.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706   5 VVMAGGTGSRlwpMSRElYPKQFLRLFGQnSMLQETITRLSGL-EIYEPMVICNEEHRFLVaeqlRQLNKLSNNIILEPV 83
Cdd:cd02516    4 IILAAGSGSR---MGAD-IPKQFLELGGK-PVLEHTLEAFLAHpAIDEIVVVVPPDDIDLA----KELAKYGLSKVVKIV 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 505178706  84 --GRNTAPAIaLAALQATRQGDDPLMLVlaadhiinnqpvfHDAIR 127
Cdd:cd02516   75 egGATRQDSV-LNGLKALPDADPDIVLI-------------HDAAR 106
cupin_UGlyAH_N cd02211
(S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain; This family ...
 366-450 1.55e-04

(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: 41.35  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 366 WGRCDVVVQ-TP----RFNVNRITVKPGGAFSMQMHHHRAEHWV-ILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLEN 439
Cdd:cd02211    8 WENTRASVLaSPklgaTFVQYLVEVEPGGGSTAPEGGEGIERFLyVLEGEVELTVGGETHTLTAGGYAYLPPGTKHSLRN 87

                         90
                 ....*....|.
gi 505178706 440 PGRIPLEVLEI 450
Cdd:cd02211   88 AGDEPARLLWY 98
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
5-178 1.75e-04

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 43.54  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706   5 VVMAGGTGSRLWPMSRElYPKQFLRLFGQnSMLQETITRLSGLEIYEPMVICNEEHRFLVAEQLRQLNKLSNNI--ILEP 82
Cdd:COG1209    4 IILAGGSGTRLRPLTLT-VSKQLLPVYDK-PMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKIsyAVQP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  83 VGRNTAPAIALAA--LqatrqGDDPLMLVLaADHIINNQpVFHDAIRVAEQYADAGHLvtFGI-VPNaPEtgygyiqR-G 158
Cdd:COG1209   82 EPLGLAHAFIIAEdfI-----GGDPVALVL-GDNIFYGD-GLSELLREAAARESGATI--FGYkVED-PE-------RyG 144

                        170       180
                 ....*....|....*....|
gi 505178706 159 VALSDSAHtpyQVARFVEKP 178
Cdd:COG1209  145 VVEFDEDG---RVVSLEEKP 161
cupin_yp_001338853-like cd07008
Klebsiella pneumoniae yp_001338853.1 and related proteins, cupin domain; This family includes ...
 337-445 5.14e-04

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: 39.16  E-value: 5.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 337 RSQDVKKAVEFlkqnqrSEYKRHREiyrpwgrcdVVVQTPRFNVNRITVKPGGAFSMQMHHHRAEHWVILAGTGQ-VTVN 415
Cdd:cd07008    1 RIFDVAEFVQF------SDEEPIRS---------VITETDDSAIVVWHVKPGQEIAAHIHPHGQDTWIVLSGEGEyLLGD 65

                         90       100       110
                 ....*....|....*....|....*....|
gi 505178706 416 GKQFLLTENQSTFIPIGAEHSLENPGRIPL 445
Cdd:cd07008   66 GQTVPIKAGDIVIAPAGQVHGARNTGDEPL 95
cupin_CENP-C_C cd06993
centromere-binding protein CENP-C, C-terminal cupin domain; This family includes centromeric ...
 383-441 7.05e-04

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: 38.29  E-value: 7.05e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 505178706 383 ITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPG 441
Cdd:cd06993    8 LELPPGGEKPLKNSKDNTYVFYVIQGAVEVTLHETTFVVTKGCSFQVPRGNYYSIKNIG 66
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 391-446 9.71e-04

AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization domain of the bacterial gene regulatory protein AraC. The domain is found in conjunction with the helix-turn-helix (HTH) DNA-binding motif pfam00165. This domain is distantly related to the Cupin domain pfam00190.


Pssm-ID: 396749 [Multi-domain]  Cd Length: 134  Bit Score: 39.34  E-value: 9.71e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 505178706  391 FSMQMHHHRAEHW-VILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLE 446
Cdd:pfam02311  14 HSFPPHVHDFYVIgYIERGVGRFRLNGRTYHLGPGDLFLLPPGEPHDYEPESEDGWR 70
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 5-114 1.09e-03

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: 39.49  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706    5 VVMAGGTGSRlwpMSRelyPKQFLRLFGQnSMLQETITRLSGL--EIYepmVICNEEhrflvaEQLRQLNKLSNNIILEP 82
Cdd:pfam12804   2 VILAGGRSSR---MGG---DKALLPLGGK-PLLERVLERLRPAgdEVV---VVANDE------EVLAALAGLGVPVVPDP 65

                          90       100       110
                  ....*....|....*....|....*....|...
gi 505178706   83 V-GRNTAPAIAlAALQATRQGDdpLMLVLAADH 114
Cdd:pfam12804  66 DpGQGPLAGLL-AALRAAPGAD--AVLVLACDM 95
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 5-215 1.38e-03

G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 40.24  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706   5 VVMAGGTGSRLWPMSrelY--PKQFLRLFGQnSMLQETITRLSGLEIYEPMVICNeEHRFLVAEQLRQLNKLSNNI--IL 80
Cdd:cd04189    4 LILAGGKGTRLRPLT---YtrPKQLIPVAGK-PIIQYAIEDLREAGIEDIGIVVG-PTGEEIKEALGDGSRFGVRItyIL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  81 EPVGRNTAPAIALAALQAtrqGDDPLMLVLaADHIINNqPVFHDAIRVAEQYADAGHLVTfgIVPNaPEtgygyiQRGVA 160
Cdd:cd04189   79 QEEPLGLAHAVLAARDFL---GDEPFVVYL-GDNLIQE-GISPLVRDFLEEDADASILLA--EVED-PR------RFGVA 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 505178706 161 -LSDSahtpyQVARFVEKPDRERAEAYLAsgeyywnsGMFMFRaKKYLSELAKFRP 215
Cdd:cd04189  145 vVDDG-----RIVRLVEKPKEPPSNLALV--------GVYAFT-PAIFDAISRLKP 186
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 382-448 2.54e-03

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


Pssm-ID: 380440 [Multi-domain]  Cd Length: 151  Bit Score: 38.34  E-value: 2.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 382 RITVKPGGAfsmqmhhhRAEHW--------VILAGTGQVTV--NGKQ---FLLTENQSTFIPIGAEHSLENPGRIPLEVL 448
Cdd:cd20306   38 RLRLSPGGI--------REPHWhpnanelgYVISGEARVSIldPTGSldtFTVKPGQVVFIPQGWLHWIENVGDEEAHLL 109
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
 382-450 2.62e-03

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: 38.23  E-value: 2.62e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505178706 382 RITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQ-----FLLTENQSTFIPIGAEHSLENPGRIPLEVLEI 450
Cdd:cd02240   31 LVRVAPGAMRELHWHPNTAEWQYVISGSARVTVFDEDgrfetFNLGAGDVGYVPSGSGHHIENIGDEDAEFLLI 104
PRK09943 PRK09943
HTH-type transcriptional regulator PuuR;
384-440 3.29e-03

HTH-type transcriptional regulator PuuR;


Pssm-ID: 182158 [Multi-domain]  Cd Length: 185  Bit Score: 38.62  E-value: 3.29e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 505178706 384 TVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENP 440
Cdd:PRK09943 113 TYQPGTTTGERIKHQGEEIGTVLEGEIVLTINGQDYHLVAGQSYAINTGIPHSFSNT 169
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 5-178 3.30e-03

N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 39.12  E-value: 3.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706   5 VVMAGGTGSRLWPMSRELyPKQfLRLFGQNSMLQETITRLSGLEIYEPMVICNEEHRFLVAEQLRQLNKLSNNIIL---- 80
Cdd:cd06425    4 LILVGGYGTRLRPLTLTV-PKP-LVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKLGIKITFsiet 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706  81 EPVGrnTAPAIALAalQATRQGDDPLMLVLAADhIINNQPV-----FHDAirvaeqyadAGHLVTfgIVPNAPETGYGYi 155
Cdd:cd06425   82 EPLG--TAGPLALA--RDLLGDDDEPFFVLNSD-VICDFPLaelldFHKK---------HGAEGT--ILVTKVEDPSKY- 144

                        170       180
                 ....*....|....*....|...
gi 505178706 156 qrGVALSDSAHtpYQVARFVEKP 178
Cdd:cd06425  145 --GVVVHDENT--GRIERFVEKP 163
PRK11171 PRK11171
(S)-ureidoglycine aminohydrolase;
366-441 3.45e-03

(S)-ureidoglycine aminohydrolase;


Pssm-ID: 183011 [Multi-domain]  Cd Length: 266  Bit Score: 39.11  E-value: 3.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 366 WGRCDVVVQ-TP----RFNVNRITVKPGGAFSMQMHHHRAEHWV-ILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLEN 439
Cdd:PRK11171  44 WENTRAWVLaRPglgaTFSQYLVEVEPGGGSDQPEPDEGAETFLfVVEGEITLTLEGKTHALSEGGYAYLPPGSDWTLRN 123


                 ..
gi 505178706 440 PG 441
Cdd:PRK11171 124 AG 125
bicupin_oxalic TIGR03404
bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins ...
 383-450 4.94e-03

bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins as they have two copies of the cupin domain (pfam00190). Two different known activities for members of this family are oxalate decarboxylase (EC 4.1.1.2) and oxalate oxidase (EC 1.2.3.4), although the latter activity has more often been found in distantly related monocupin (germin) proteins.


Pssm-ID: 274565 [Multi-domain]  Cd Length: 367  Bit Score: 39.23  E-value: 4.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505178706  383 ITVKPGGAfsMQMH-HHRAEHWV-ILAGTGQVTVngkqFLLTENQSTF---------IPIGAEHSLENPGRIPLEVLEI 450
Cdd:TIGR03404 250 VTVEPGAM--RELHwHPNADEWQyFIQGQARMTV----FAAGGNARTFdyqagdvgyVPRNMGHYVENTGDETLVFLEV 322
cupin_CV2614-like cd02236
Chromobacterium violaceum CV2614 and related proteins, cupin domain; This family includes ...
 375-460 5.24e-03

Chromobacterium violaceum CV2614 and related proteins, cupin domain; This family includes mostly bacterial proteins homologous to CV2614, a Chromobacterium violaceum 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: 380364 [Multi-domain]  Cd Length: 102  Bit Score: 36.32  E-value: 5.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505178706 375 TPRFNVNRITVKPGGAFSmqMHHHRaehwVILAG---TGQVTV---NGKQFLLTENQStFI-PIGAEHSLENPGRIPLEV 447
Cdd:cd02236   19 QPEITVLRITIPPGAELP--WHTHP----VPNAGyvlSGELTVeyeDGKKRTFKAGDA-FVeAVNTWHRGRNGGDEPVEL 91

                         90
                 ....*....|...
gi 505178706 448 LEIqsgsYLGEDD 460
Cdd:cd02236   92 LVF----YAGAKG 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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