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Conserved domains on  [gi|2105327365|ref|WP_225207983|]
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MULTISPECIES: mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase, partial [Klebsiella]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 1-439 0e+00

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


The actual alignment was detected with superfamily member TIGR01479:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 468  Bit Score: 732.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365   1 GQNSMLQETITRLSGLEIHEPMVICNEEHRFLVAEQLRQLNKLSNNIILEPVGRNTAPAIALAALQATRH-GDDPLMLVL 79
Cdd:TIGR01479  31 GDLTMLQQTLKRLAGLPCSSPLVICNEEHRFIVAEQLREIGKLASNIILEPVGRNTAPAIALAALLAARRnGEDPLLLVL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365  80 AADHIINNQPVFHDAIRVAEQYADEGHLVTFGIVPNAPETGYGYIQRGVALtdSAHTPYQVARFVEKPDRERAEAYLASG 159
Cdd:TIGR01479 111 AADHVITDEDAFQAAVKLAMPAAAEGKLVTFGIVPTHPETGYGYIRRGAPL--AGEDVYQVQRFVEKPDLATAQAYLESG 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 160 EYYWNSGMFMFRAKKYLSELAKFRPDILEACQAAVNAADNGSDFISIPHDIFCECPDESVDYAVMEKTADAVVVGLDADW 239
Cdd:TIGR01479 189 DYYWNSGMFLFRASRYLAELKKHAPDIYEACEAAVEASEPDLDFIRLDKEAFEQCPSESIDYAVMEKTADAVVVPMDAGW 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 240 SDVGSWSALWEVSPKDEQGNVLSGDAWVHNSENCYINSDEKLVAAIGVENLVIVSTKDAVLVMNRERSQDVKKAVEFLKQ 319
Cdd:TIGR01479 269 SDVGSWSALWEISDKDADGNVLKGDVLTHDTKNSYIYSESRLVAVVGVEDLVVVETKDAVLVAHKDRVQDVKKIVEQLKA 348

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 320 NQRSEYKRHREIYRPWGRCDVVVQTPRFNVNRITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIP 399
Cdd:TIGR01479 349 DGRTETEQHREVYRPWGKYDSIDQGDRYQVKRITVKPGEKLSLQMHHHRAEHWIVVSGTARVTIGDETLLLTENESTYIP 428

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 2105327365 400 IGAEHSLENPGRIPLEVLEIQSGSYLGEDDIIRIKDQYGR 439
Cdd:TIGR01479 429 LGVIHRLENPGKIPLELIEVQSGSYLGEDDIIRFEDRYGR 468
 
Name Accession Description Interval E-value
GMP_PMI TIGR01479
mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to ...
 1-439 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: 732.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365   1 GQNSMLQETITRLSGLEIHEPMVICNEEHRFLVAEQLRQLNKLSNNIILEPVGRNTAPAIALAALQATRH-GDDPLMLVL 79
Cdd:TIGR01479  31 GDLTMLQQTLKRLAGLPCSSPLVICNEEHRFIVAEQLREIGKLASNIILEPVGRNTAPAIALAALLAARRnGEDPLLLVL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365  80 AADHIINNQPVFHDAIRVAEQYADEGHLVTFGIVPNAPETGYGYIQRGVALtdSAHTPYQVARFVEKPDRERAEAYLASG 159
Cdd:TIGR01479 111 AADHVITDEDAFQAAVKLAMPAAAEGKLVTFGIVPTHPETGYGYIRRGAPL--AGEDVYQVQRFVEKPDLATAQAYLESG 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 160 EYYWNSGMFMFRAKKYLSELAKFRPDILEACQAAVNAADNGSDFISIPHDIFCECPDESVDYAVMEKTADAVVVGLDADW 239
Cdd:TIGR01479 189 DYYWNSGMFLFRASRYLAELKKHAPDIYEACEAAVEASEPDLDFIRLDKEAFEQCPSESIDYAVMEKTADAVVVPMDAGW 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 240 SDVGSWSALWEVSPKDEQGNVLSGDAWVHNSENCYINSDEKLVAAIGVENLVIVSTKDAVLVMNRERSQDVKKAVEFLKQ 319
Cdd:TIGR01479 269 SDVGSWSALWEISDKDADGNVLKGDVLTHDTKNSYIYSESRLVAVVGVEDLVVVETKDAVLVAHKDRVQDVKKIVEQLKA 348

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 320 NQRSEYKRHREIYRPWGRCDVVVQTPRFNVNRITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIP 399
Cdd:TIGR01479 349 DGRTETEQHREVYRPWGKYDSIDQGDRYQVKRITVKPGEKLSLQMHHHRAEHWIVVSGTARVTIGDETLLLTENESTYIP 428

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 2105327365 400 IGAEHSLENPGRIPLEVLEIQSGSYLGEDDIIRIKDQYGR 439
Cdd:TIGR01479 429 LGVIHRLENPGKIPLELIEVQSGSYLGEDDIIRFEDRYGR 468
cpsB PRK15460
mannose-1-phosphate guanyltransferase; Provisional
 1-439 0e+00

mannose-1-phosphate guanyltransferase; Provisional


Pssm-ID: 185357 [Multi-domain]  Cd Length: 478  Bit Score: 657.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365   1 GQNSMLQETITRLSGLEIHEPMVICNEEHRFLVAEQLRQLNKLSNNIILEPVGRNTAPAIALAALQATRHG--DDPLMLV 78
Cdd:PRK15460   36 GDLTMLQTTICRLNGVECESPVVICNEQHRFIVAEQLRQLNKLTENIILEPAGRNTAPAIALAALAAKRHSpeSDPLMLV 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365  79 LAADHIINNQPVFHDAIRVAEQYADEGHLVTFGIVPNAPETGYGYIQRGVALTDSAHT-PYQVARFVEKPDRERAEAYLA 157
Cdd:PRK15460  116 LAADHVIADEDAFRAAVRNAMPYAEAGKLVTFGIVPDLPETGYGYIRRGEVSAGEQDTvAFEVAQFVEKPNLETAQAYVA 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 158 SGEYYWNSGMFMFRAKKYLSELAKFRPDILEACQAAVNAADNGSDFISIPHDIFCECPDESVDYAVMEKTADAVVVGLDA 237
Cdd:PRK15460  196 SGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDPDLDFIRVDEEAFLACPEESVDYAVMERTADAVVVPMDA 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 238 DWSDVGSWSALWEVSPKDEQGNVLSGDAWVHNSENCYINSDEKLVAAIGVENLVIVSTKDAVLVMNRERSQDVKKAVEFL 317
Cdd:PRK15460  276 GWSDVGSWSSLWEISAHTAEGNVCHGDVINHKTENSYVYAESGLVTTVGVKDLVVVQTKDAVLIADRNAVQDVKKVVEQI 355

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 318 KQNQRSEYKRHREIYRPWGRCDVVVQTPRFNVNRITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTF 397
Cdd:PRK15460  356 KADGRHEHRVHREVYRPWGKYDSIDAGDRYQVKRITVKPGEGLSVQMHHHRAEHWVVVAGTAKVTIDGDIKLLGENESIY 435

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 2105327365 398 IPIGAEHSLENPGRIPLEVLEIQSGSYLGEDDIIRIKDQYGR 439
Cdd:PRK15460  436 IPLGATHCLENPGKIPLDLIEVRSGSYLEEDDVVRFADRYGR 477
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-319 0e+00

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 531.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365   1 GQNSMLQETITRLSGL-EIHEPMVICNEEHRFLVAEQLRQLNKlsNNIILEPVGRNTAPAIALAALQATRHGDDPLMLVL 79
Cdd:COG0836    33 GEKSLLQQTVERLAGLvPPENILVVTNEEHRFLVAEQLPELGP--ANILLEPVGRNTAPAIALAALLIAKRDPDAVLLVL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365  80 AADHIINNQPVFHDAIRVAEQYADEGHLVTFGIVPNAPETGYGYIQRGVALTDSahTPYQVARFVEKPDRERAEAYLASG 159
Cdd:COG0836   111 PADHLIEDEEAFREAVRAAVEAAEAGKLVTFGIKPTRPETGYGYIEAGEALGGA--GAYKVKRFVEKPDLETAEEYLASG 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 160 EYYWNSGMFMFRAKKYLSELAKFRPDILEACQAAVNAADNGSDFISIPhDIFCECPDESVDYAVMEKTADAVVVGLDADW 239
Cdd:COG0836   189 NYLWNSGMFVFRASTILEELERHAPEIYAALEAAVAAAGTDLEVRLDA-EAFAALPSISIDYAVMEKADNVAVVPADFGW 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 240 SDVGSWSALWEVSPKDEQGNVLSGDAWVHNSENCYINSDEKLVAAIGVENLVIVSTKDAVLVMNRERSQDVKKAVEFLKQ 319
Cdd:COG0836   268 SDVGSWDALWELLEKDENGNVVLGDVLLIDSSNSLVRSEGRLVAVIGVEDLVVVDTPDALLVAPKDRAQEVKKIVEALKE 347
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 4-248 5.05e-121

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: 353.42  E-value: 5.05e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365   4 SMLQETITRLSGL-EIHEPMVICNEEHRFLVAEQLRQLNKlSNNIILEPVGRNTAPAIALAALQATRHGDDPLMLVLAAD 82
Cdd:cd02509    34 SLLQQTLDRLKGLvPPDRILVVTNEEYRFLVREQLPEGLP-EENIILEPEGRNTAPAIALAALYLAKRDPDAVLLVLPSD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365  83 HIINNQPVFHDAIRVAEQYADEGHLVTFGIVPNAPETGYGYIQRGVALTDSAhtpYQVARFVEKPDRERAEAYLASGEYY 162
Cdd:cd02509   113 HLIEDVEAFLKAVKKAVEAAEEGYLVTFGIKPTRPETGYGYIEAGEKLGGGV---YRVKRFVEKPDLETAKEYLESGNYL 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 163 WNSGMFMFRAKKYLSELAKFRPDILEACQAAVNAADNGsDFISIPHDIFCECPDESVDYAVMEKTADAVVVGLDADWSDV 242
Cdd:cd02509   190 WNSGIFLFRAKTFLEELKKHAPDIYEALEKALAAAGTD-DFLRLLEEAFAKIPSISIDYAVMEKTKKVAVVPADFGWSDL 268


                  ....*.
gi 2105327365 243 GSWSAL 248
Cdd:cd02509   269 GSWDAL 274
MannoseP_isomer pfam01050
Mannose-6-phosphate isomerase; All of the members of this Pfam entry belong to family 2 of the ...
 285-435 1.60e-80

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: 245.41  E-value: 1.60e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 285 IGVENLVIVSTKDAVLVMNRERSQDVKKAVEFLKQNQRSEYKRHREIYRPWGRCDVVVQTPRFNVNRITVKPGGAFSMQM 364
Cdd:pfam01050   1 IGVENLVVVETKDALLVAHKDKVQDVKKVVEELKENGRSEHQTHREVYRPWGSYDVIDEGERYQVKRITVKPGARLSLQM 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2105327365 365 HHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEVLEIQSGSYLGEDDIIRIKD 435
Cdd:pfam01050  81 HHHRAEHWIVVSGTARVTKGGETFLLTENESTYIPLGTIHRLENPGKIPLELIEVQSGSYLGEDDIVRFED 151
 
Name Accession Description Interval E-value
GMP_PMI TIGR01479
mannose-1-phosphate guanylyltransferase/mannose-6-phosphate isomerase; This enzyme is known to ...
 1-439 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: 732.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365   1 GQNSMLQETITRLSGLEIHEPMVICNEEHRFLVAEQLRQLNKLSNNIILEPVGRNTAPAIALAALQATRH-GDDPLMLVL 79
Cdd:TIGR01479  31 GDLTMLQQTLKRLAGLPCSSPLVICNEEHRFIVAEQLREIGKLASNIILEPVGRNTAPAIALAALLAARRnGEDPLLLVL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365  80 AADHIINNQPVFHDAIRVAEQYADEGHLVTFGIVPNAPETGYGYIQRGVALtdSAHTPYQVARFVEKPDRERAEAYLASG 159
Cdd:TIGR01479 111 AADHVITDEDAFQAAVKLAMPAAAEGKLVTFGIVPTHPETGYGYIRRGAPL--AGEDVYQVQRFVEKPDLATAQAYLESG 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 160 EYYWNSGMFMFRAKKYLSELAKFRPDILEACQAAVNAADNGSDFISIPHDIFCECPDESVDYAVMEKTADAVVVGLDADW 239
Cdd:TIGR01479 189 DYYWNSGMFLFRASRYLAELKKHAPDIYEACEAAVEASEPDLDFIRLDKEAFEQCPSESIDYAVMEKTADAVVVPMDAGW 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 240 SDVGSWSALWEVSPKDEQGNVLSGDAWVHNSENCYINSDEKLVAAIGVENLVIVSTKDAVLVMNRERSQDVKKAVEFLKQ 319
Cdd:TIGR01479 269 SDVGSWSALWEISDKDADGNVLKGDVLTHDTKNSYIYSESRLVAVVGVEDLVVVETKDAVLVAHKDRVQDVKKIVEQLKA 348

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 320 NQRSEYKRHREIYRPWGRCDVVVQTPRFNVNRITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIP 399
Cdd:TIGR01479 349 DGRTETEQHREVYRPWGKYDSIDQGDRYQVKRITVKPGEKLSLQMHHHRAEHWIVVSGTARVTIGDETLLLTENESTYIP 428

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 2105327365 400 IGAEHSLENPGRIPLEVLEIQSGSYLGEDDIIRIKDQYGR 439
Cdd:TIGR01479 429 LGVIHRLENPGKIPLELIEVQSGSYLGEDDIIRFEDRYGR 468
cpsB PRK15460
mannose-1-phosphate guanyltransferase; Provisional
 1-439 0e+00

mannose-1-phosphate guanyltransferase; Provisional


Pssm-ID: 185357 [Multi-domain]  Cd Length: 478  Bit Score: 657.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365   1 GQNSMLQETITRLSGLEIHEPMVICNEEHRFLVAEQLRQLNKLSNNIILEPVGRNTAPAIALAALQATRHG--DDPLMLV 78
Cdd:PRK15460   36 GDLTMLQTTICRLNGVECESPVVICNEQHRFIVAEQLRQLNKLTENIILEPAGRNTAPAIALAALAAKRHSpeSDPLMLV 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365  79 LAADHIINNQPVFHDAIRVAEQYADEGHLVTFGIVPNAPETGYGYIQRGVALTDSAHT-PYQVARFVEKPDRERAEAYLA 157
Cdd:PRK15460  116 LAADHVIADEDAFRAAVRNAMPYAEAGKLVTFGIVPDLPETGYGYIRRGEVSAGEQDTvAFEVAQFVEKPNLETAQAYVA 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 158 SGEYYWNSGMFMFRAKKYLSELAKFRPDILEACQAAVNAADNGSDFISIPHDIFCECPDESVDYAVMEKTADAVVVGLDA 237
Cdd:PRK15460  196 SGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDPDLDFIRVDEEAFLACPEESVDYAVMERTADAVVVPMDA 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 238 DWSDVGSWSALWEVSPKDEQGNVLSGDAWVHNSENCYINSDEKLVAAIGVENLVIVSTKDAVLVMNRERSQDVKKAVEFL 317
Cdd:PRK15460  276 GWSDVGSWSSLWEISAHTAEGNVCHGDVINHKTENSYVYAESGLVTTVGVKDLVVVQTKDAVLIADRNAVQDVKKVVEQI 355

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 318 KQNQRSEYKRHREIYRPWGRCDVVVQTPRFNVNRITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTF 397
Cdd:PRK15460  356 KADGRHEHRVHREVYRPWGKYDSIDAGDRYQVKRITVKPGEGLSVQMHHHRAEHWVVVAGTAKVTIDGDIKLLGENESIY 435

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 2105327365 398 IPIGAEHSLENPGRIPLEVLEIQSGSYLGEDDIIRIKDQYGR 439
Cdd:PRK15460  436 IPLGATHCLENPGKIPLDLIEVRSGSYLEEDDVVRFADRYGR 477
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-319 0e+00

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 531.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365   1 GQNSMLQETITRLSGL-EIHEPMVICNEEHRFLVAEQLRQLNKlsNNIILEPVGRNTAPAIALAALQATRHGDDPLMLVL 79
Cdd:COG0836    33 GEKSLLQQTVERLAGLvPPENILVVTNEEHRFLVAEQLPELGP--ANILLEPVGRNTAPAIALAALLIAKRDPDAVLLVL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365  80 AADHIINNQPVFHDAIRVAEQYADEGHLVTFGIVPNAPETGYGYIQRGVALTDSahTPYQVARFVEKPDRERAEAYLASG 159
Cdd:COG0836   111 PADHLIEDEEAFREAVRAAVEAAEAGKLVTFGIKPTRPETGYGYIEAGEALGGA--GAYKVKRFVEKPDLETAEEYLASG 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 160 EYYWNSGMFMFRAKKYLSELAKFRPDILEACQAAVNAADNGSDFISIPhDIFCECPDESVDYAVMEKTADAVVVGLDADW 239
Cdd:COG0836   189 NYLWNSGMFVFRASTILEELERHAPEIYAALEAAVAAAGTDLEVRLDA-EAFAALPSISIDYAVMEKADNVAVVPADFGW 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 240 SDVGSWSALWEVSPKDEQGNVLSGDAWVHNSENCYINSDEKLVAAIGVENLVIVSTKDAVLVMNRERSQDVKKAVEFLKQ 319
Cdd:COG0836   268 SDVGSWDALWELLEKDENGNVVLGDVLLIDSSNSLVRSEGRLVAVIGVEDLVVVDTPDALLVAPKDRAQEVKKIVEALKE 347
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 4-248 5.05e-121

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: 353.42  E-value: 5.05e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365   4 SMLQETITRLSGL-EIHEPMVICNEEHRFLVAEQLRQLNKlSNNIILEPVGRNTAPAIALAALQATRHGDDPLMLVLAAD 82
Cdd:cd02509    34 SLLQQTLDRLKGLvPPDRILVVTNEEYRFLVREQLPEGLP-EENIILEPEGRNTAPAIALAALYLAKRDPDAVLLVLPSD 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365  83 HIINNQPVFHDAIRVAEQYADEGHLVTFGIVPNAPETGYGYIQRGVALTDSAhtpYQVARFVEKPDRERAEAYLASGEYY 162
Cdd:cd02509   113 HLIEDVEAFLKAVKKAVEAAEEGYLVTFGIKPTRPETGYGYIEAGEKLGGGV---YRVKRFVEKPDLETAKEYLESGNYL 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 163 WNSGMFMFRAKKYLSELAKFRPDILEACQAAVNAADNGsDFISIPHDIFCECPDESVDYAVMEKTADAVVVGLDADWSDV 242
Cdd:cd02509   190 WNSGIFLFRAKTFLEELKKHAPDIYEALEKALAAAGTD-DFLRLLEEAFAKIPSISIDYAVMEKTKKVAVVPADFGWSDL 268


                  ....*.
gi 2105327365 243 GSWSAL 248
Cdd:cd02509   269 GSWDAL 274
MannoseP_isomer pfam01050
Mannose-6-phosphate isomerase; All of the members of this Pfam entry belong to family 2 of the ...
 285-435 1.60e-80

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: 245.41  E-value: 1.60e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 285 IGVENLVIVSTKDAVLVMNRERSQDVKKAVEFLKQNQRSEYKRHREIYRPWGRCDVVVQTPRFNVNRITVKPGGAFSMQM 364
Cdd:pfam01050   1 IGVENLVVVETKDALLVAHKDKVQDVKKVVEELKENGRSEHQTHREVYRPWGSYDVIDEGERYQVKRITVKPGARLSLQM 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2105327365 365 HHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEVLEIQSGSYLGEDDIIRIKD 435
Cdd:pfam01050  81 HHHRAEHWIVVSGTARVTKGGETFLLTENESTYIPLGTIHRLENPGKIPLELIEVQSGSYLGEDDIVRFED 151
cupin_PMI_typeII_C cd02213
Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal ...
 306-433 1.93e-66

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: 208.18  E-value: 1.93e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 306 RSQDVKKAVEFLKQNQRSEykRHREIYRPWGRCDVVVQTPRFNVNRITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNG 385
Cdd:cd02213     1 KSQRVKEIVEELKKRGRSE--EHRTVYRPWGSYEVLDEGEGYKVKRLTVNPGKRLSLQRHHHRSEHWVVVSGTAEVTLDG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2105327365 386 KQFLLTENQSTFIPIGAEHSLENPGRIPLEVLEIQSGSYLGEDDIIRI 433
Cdd:cd02213    79 KEKLLKEGESIYIPKGTKHRLENPGKIPLEIIEVQTGEYLGEDDIVRL 126
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 1-256 2.08e-65

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: 209.80  E-value: 2.08e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365   1 GQNSMLQETITRLSGLEIHEPMVICNEEHRFLVAEQLRQLNKLSNNI--ILEPVGRNTAPAIALAALQATRHGDDplMLV 78
Cdd:pfam00483  29 GKYPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQItyALQPEGKGTAPAVALAADFLGDEKSD--VLV 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365  79 LAADHIInnQPVFHDAIRVAEQYAdEGHLVTFGIVPNAPETGYGYIQRGVAltdsahtpYQVARFVEKPDRERAEAYLAS 158
Cdd:pfam00483 107 LGGDHIY--RMDLEQAVKFHIEKA-ADATVTFGIVPVEPPTGYGVVEFDDN--------GRVIRFVEKPKLPKASNYASM 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 159 GEYYWNSGMFMFRAKkYLSELAKFRPDILEACQAAVNAADngsdfisiphdifcecpdesVDYAVMEKtadavvvglDAD 238
Cdd:pfam00483 176 GIYIFNSGVLDFLAK-YLEELKRGEDEITDILPKALEDGK--------------------LAYAFIFK---------GYA 225

                         250
                  ....*....|....*...
gi 2105327365 239 WSDVGSWSALWEVSPKDE 256
Cdd:pfam00483 226 WLDVGTWDSLWEANLFLL 243
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
333-432 1.39e-35

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 127.56  E-value: 1.39e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 333 RPWGRCDVVVQ-TPRFNVNRITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGR 411
Cdd:COG0662    12 IGWGSYEVLGEgGERLSVKRITVPPGAELSLHVHPHRDEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAGVPHRLRNPGD 91

                          90       100
                  ....*....|....*....|.
gi 2105327365 412 IPLEVLEIQSGSYLGEDDIIR 432
Cdd:COG0662    92 EPLELLEVQAPAYLGEDDIVR 112
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
 329-428 2.77e-12

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


Pssm-ID: 380344 [Multi-domain]  Cd Length: 100  Bit Score: 62.53  E-value: 2.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 329 REIYRPwgrcdVVVQTPRFNVNRITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLEN 408
Cdd:cd02214     6 RELLHP-----DNDGDPRYSLAHARVPPGESTLPHRLKGSEEVYYILEGEGTMEIDGEPREVGPGDAVLIPPGAVQRIEN 80

                          90       100
                  ....*....|....*....|
gi 2105327365 409 PGRIPLEVLEIQSGSYLGED 428
Cdd:cd02214    81 TGEEDLVFLCICSPAWSPED 100
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 351-419 1.57e-11

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: 59.58  E-value: 1.57e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105327365 351 RITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEVLEI 419
Cdd:pfam07883   2 LVTLPPGESSPPHRHPGEDEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLLDV 70
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
 345-415 2.85e-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: 59.39  E-value: 2.85e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2105327365 345 PRFNVNRITVKPGGafSMQMHHHRAEHWV-ILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLE 415
Cdd:cd02222    15 PNFAMRYFEIEPGG--HTPLHTHPWEHEVyVLRGKGVVVIGGEEYPVKPGDVVYIPPNEPHQFRNTGDEPLG 84
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
327-421 7.57e-11

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 58.71  E-value: 7.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 327 RHREIYRPWGRCDVVVQTP-RFNVNRITVKPGGafSMQMHHHRA-EHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEH 404
Cdd:COG1917     2 RLAEIALTGVSVRVLADGEdELEVVRVTFEPGA--RTPWHSHPGeELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPH 79

                          90
                  ....*....|....*..
gi 2105327365 405 SLENPGRIPLEVLEIQS 421
Cdd:COG1917    80 AFRNLGDEPAVLLVVFS 96
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
346-435 1.51e-10

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 58.11  E-value: 1.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 346 RFNVNRITVKPGGAFSMQMHHHRAEHWV-ILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEVLEIqsGSY 424
Cdd:COG3837    27 RLGVNLITLPPGASSSPYHAHSAEEEFVyVLEGELTLRIGGEEYVLEPGDSVGFPAGVPHRLRNRGDEPARYLVV--GTR 104

                          90
                  ....*....|.
gi 2105327365 425 LGEDDIIRIKD 435
Cdd:COG3837   105 APYPDSFDYWD 115
cupin_TM1287-like cd02221
Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial ...
 351-417 6.27e-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: 55.94  E-value: 6.27e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2105327365 351 RITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEVL 417
Cdd:cd02221    23 RVTLPPGSSIGYHQHEGEFEIYYILSGEGLYTDNGKEYEVKAGDVTFTRDGESHGIENTGDEDLVFI 89
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 349-419 2.21e-08

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


Pssm-ID: 380338 [Multi-domain]  Cd Length: 73  Bit Score: 50.94  E-value: 2.21e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2105327365 349 VNRITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVN-GKQFLLTENQSTFIPIGAEHSLENPGRIPLEVLEI 419
Cdd:cd02208     1 ISVVTLPPGTSSPPHWHPEQDEIFYVLSGEGELTLDdGETVELKAGDIVLIPPGVPHSFVNTSDEPAVFLVV 72
cupin_Bh2720-like cd02223
Bacillus halodurans Bh2720 and related proteins, cupin domain; This family includes bacterial, ...
 353-421 6.91e-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: 50.24  E-value: 6.91e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105327365 353 TVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEVLEIQS 421
Cdd:cd02223    17 SIPPGEDIGLEVHDDVDQFLRIEEGEGKAIMGGFESEVKDGDAIIVPAGTWHNVINTGNEPLKLYTIYA 85
cupin_SPO2919-like cd02224
Silicibacter pomeroyi SPO2919 and related proteins, uncharacterized sugar phosphate isomerase ...
 346-419 5.45e-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: 47.87  E-value: 5.45e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105327365 346 RFNVNRITVKPGgAFSMQMHHHRA--EHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAE--HSLENPGRIPLEVLEI 419
Cdd:cd02224    16 QLGVNLERLPPG-ARSSPRHWHSAeeEFVYVLSGEGTLRLDGEEVLPRPGDFVGFPAGTGvaHQLINRSDEPLVYLVV 92
AllE COG3257
Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];
335-420 9.27e-07

Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 442488 [Multi-domain]  Cd Length: 262  Bit Score: 49.82  E-value: 9.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 335 WGRCDVVVQ-TP----RFNVNRITVKPGGAFSMQMHHHRAEHWV-ILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLEN 408
Cdd:COG3257    42 WENTRVWILaRPlsgaTFSQYIVEVAPGGGSDRPEPDPGAETFLfVLEGEVTLTLGGETHELTPGGYAYLPPGTPWTLRN 121

                          90
                  ....*....|..
gi 2105327365 409 PGRIPLEVLEIQ 420
Cdd:COG3257   122 AGDEPARFHWIR 133
cupin_DddK cd06988
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ...
 352-419 1.05e-06

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: 46.07  E-value: 1.05e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105327365 352 ITVKPGGAfSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEVLEI 419
Cdd:cd06988     7 CVVRPGTT-STPHSHHEYEIFIVISGKGIVVVDGEREPVKAGDVVYIPPGTEHYVKNDGDEDFEFYSI 73
cupin_TcmJ-like cd06991
TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of ...
 352-416 1.67e-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: 1.67e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105327365 352 ITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEV 416
Cdd:cd06991    24 LTLAPGERVSEHYHPYSEEFLYVVRGRLVVRVDGEPVVLEAGEALLVPRGVRHRLENAGDEPARL 88
cupin_OxDC_C cd20305
Oxalate decarboxylase (OxDC), C-terminal cupin domain; This model represents the C-terminal ...
 352-424 5.75e-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: 5.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 352 ITVKPGGAfsMQMH-HHRAEHW-VILAGTGQVTVngkqFLLTENQSTF---------IPIGAEHSLENPGRIPLEVLEI- 419
Cdd:cd20305    39 VTLEPGAL--RELHwHPNADEWqYYISGKARMTV----FASGGRARTFdfqagdvgyVPRGYGHYIENTGDEPLEFLEVf 112


                  ....*
gi 2105327365 420 QSGSY 424
Cdd:cd20305   113 NSGRY 117
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 352-435 1.13e-05

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


Pssm-ID: 441743 [Multi-domain]  Cd Length: 115  Bit Score: 44.19  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 352 ITVKPGGAFSMQMHHHRAEHWVILAGTGQVTV---NGKQFL--LTENQSTFIPIGAEHSLENPGRIPLEVLEIQSGSYLG 426
Cdd:COG2140     8 TVLEPGGVREEHWHPNAAEWYYVLSGEARMTVqdpPGRARTvdVGPGDVVYVPPGYGHYIINTGDEPLVFLAVFDDDAGS 87


                  ....*....
gi 2105327365 427 EDDIIRIKD 435
Cdd:COG2140    88 DYGTISLSG 96
cupin_XRE_C cd02209
XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; ...
 346-417 1.16e-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: 1.16e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2105327365 346 RFNVNRITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEVL 417
Cdd:cd02209    15 KMEPFLVTLPPGGSGGEPYSHEGEEFGYVLEGELELTVGGETYVLEAGDSIYFDSDVPHRYRNPGDEPARVL 86
cupin_XcTcmJ-like cd07006
Xanthomonas campestris XcTcmJ and related proteins, cupin domain; This family includes ...
 339-419 1.50e-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: 43.12  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 339 DVVVQTPRFNVNRITVKPGGAF-SMQMHHHRAEHWV-ILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEV 416
Cdd:cd07006     2 RVLAGTERSQAATMVLAPGDTEgGPDNRHRGSDQWLyVVSGSGEAIVEGERVALKPGSLLLIEAGETHEIRNTGDEPLKT 81


                  ...
gi 2105327365 417 LEI 419
Cdd:cd07006    82 LNF 84
cupin_MAE_RS03005 cd06987
Microcystis aeruginosa MAE_RS03005 and related proteins, cupin domain; This family includes ...
 355-410 1.57e-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: 1.57e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2105327365 355 KPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPG 410
Cdd:cd06987    36 DPGGRTPPNTHPAAHEMFFVLAGEGRAYCDGQRVPLRPGDALVVPPGSEHVIENTG 91
cupin_TTHA0104 cd06122
Thermus thermophilus TTHA0104 and related proteins, cupin domain; This family contains ...
 343-417 3.16e-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: 3.16e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105327365 343 QTPRFNVNRITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLEVL 417
Cdd:cd06122    23 ESERLFCDLYCLEPGQSQKVHAHAGSDKVYFVLEGEGRFTVGDEERELGAGEAVLAPAGVPHGVRNTGAERLVLL 97
cupin_UGlyAH_N cd02211
(S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain; This family ...
 335-419 1.43e-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: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 335 WGRCDVVVQ-TP----RFNVNRITVKPGGAFSMQMHHHRAEHWV-ILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLEN 408
Cdd:cd02211     8 WENTRASVLaSPklgaTFVQYLVEVEPGGGSTAPEGGEGIERFLyVLEGEVELTVGGETHTLTAGGYAYLPPGTKHSLRN 87

                          90
                  ....*....|.
gi 2105327365 409 PGRIPLEVLEI 419
Cdd:cd02211    88 AGDEPARLLWY 98
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 5-243 3.32e-04

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: 41.80  E-value: 3.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365   5 MLQETITRLSGLEIHEPMVICNEEHRfLVAEQLRQLNKLSNNI--ILEPVGRNTAPAIALAAlqaTRHGDDPLmLVLAAD 82
Cdd:cd04181    31 ILEYIIERLARAGIDEIILVVGYLGE-QIEEYFGDGSKFGVNIeyVVQEEPLGTAGAVRNAE---DFLGDDDF-LVVNGD 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365  83 HIINNqpvfhDAIRVAEQYADEGHLVTFGIVPNAPETGYGyiqrgVALTDSAhtpYQVARFVEKPDREraEAYLASGEYY 162
Cdd:cd04181   106 VLTDL-----DLSELLRFHREKGADATIAVKEVEDPSRYG-----VVELDDD---GRVTRFVEKPTLP--ESNLANAGIY 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 163 wnsgmfmfrakkylselaKFRPDILEACQAavnaadNGSDFISIPHDIFcecpdesvDYAVMEKTADAVVVglDADWSDV 242
Cdd:cd04181   171 ------------------IFEPEILDYIPE------ILPRGEDELTDAI--------PLLIEEGKVYGYPV--DGYWLDI 216


                  .
gi 2105327365 243 G 243
Cdd:cd04181   217 G 217
cupin_CENP-C_C cd06993
centromere-binding protein CENP-C, C-terminal cupin domain; This family includes centromeric ...
 352-410 6.55e-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: 6.55e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2105327365 352 ITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPG 410
Cdd:cd06993     8 LELPPGGEKPLKNSKDNTYVFYVIQGAVEVTLHETTFVVTKGCSFQVPRGNYYSIKNIG 66
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 4-174 8.63e-04

GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 40.70  E-value: 8.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365   4 SMLQETITRLSGLEIHEPMVICNEEHR--FLVAEQLRQLNKLSNNIILEPVGRNTAPAIALAALQAtrHGDDPLmLVLAA 81
Cdd:cd04183    30 PMIEWVIESLAKIFDSRFIFICRDEHNtkFHLDESLKLLAPNATVVELDGETLGAACTVLLAADLI--DNDDPL-LIFNC 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365  82 DHIINNQpvFHDAIRVAEQYADEGHLVTFgivpNAPETGYGYiqrgVALTDSAHtpyqVARFVEKpdrERAEAYLASGEY 161
Cdd:cd04183   107 DQIVESD--LLAFLAAFRERDLDGGVLTF----FSSHPRWSY----VKLDENGR----VIETAEK---EPISDLATAGLY 169

                         170
                  ....*....|...
gi 2105327365 162 YWNSGMFMFRAKK 174
Cdd:cd04183   170 YFKSGSLFVEAAK 182
cupin_yp_001338853-like cd07008
Klebsiella pneumoniae yp_001338853.1 and related proteins, cupin domain; This family includes ...
 306-414 9.24e-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: 38.39  E-value: 9.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 306 RSQDVKKAVEFlkqnqrSEYKRHREiyrpwgrcdVVVQTPRFNVNRITVKPGGAFSMQMHHHRAEHWVILAGTGQ-VTVN 384
Cdd:cd07008     1 RIFDVAEFVQF------SDEEPIRS---------VITETDDSAIVVWHVKPGQEIAAHIHPHGQDTWIVLSGEGEyLLGD 65

                          90       100       110
                  ....*....|....*....|....*....|
gi 2105327365 385 GKQFLLTENQSTFIPIGAEHSLENPGRIPL 414
Cdd:cd07008    66 GQTVPIKAGDIVIAPAGQVHGARNTGDEPL 95
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 360-415 1.08e-03

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: 38.96  E-value: 1.08e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2105327365 360 FSMQMHHHRAEHW-VILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENPGRIPLE 415
Cdd:pfam02311  14 HSFPPHVHDFYVIgYIERGVGRFRLNGRTYHLGPGDLFLLPPGEPHDYEPESEDGWR 70
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
 351-419 2.70e-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: 2.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2105327365 351 RITVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQ-----FLLTENQSTFIPIGAEHSLENPGRIPLEVLEI 419
Cdd:cd02240    31 LVRVAPGAMRELHWHPNTAEWQYVISGSARVTVFDEDgrfetFNLGAGDVGYVPSGSGHHIENIGDEDAEFLLI 104
PRK11171 PRK11171
(S)-ureidoglycine aminohydrolase;
335-410 2.80e-03

(S)-ureidoglycine aminohydrolase;


Pssm-ID: 183011 [Multi-domain]  Cd Length: 266  Bit Score: 39.50  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 335 WGRCDVVVQ-TPRFNVN----RITVKPGGAFSMQMHHHRAEHWV-ILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLEN 408
Cdd:PRK11171   44 WENTRAWVLaRPGLGATfsqyLVEVEPGGGSDQPEPDEGAETFLfVVEGEITLTLEGKTHALSEGGYAYLPPGSDWTLRN 123


                  ..
gi 2105327365 409 PG 410
Cdd:PRK11171  124 AG 125
PRK09943 PRK09943
HTH-type transcriptional regulator PuuR;
353-409 3.01e-03

HTH-type transcriptional regulator PuuR;


Pssm-ID: 182158 [Multi-domain]  Cd Length: 185  Bit Score: 38.62  E-value: 3.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2105327365 353 TVKPGGAFSMQMHHHRAEHWVILAGTGQVTVNGKQFLLTENQSTFIPIGAEHSLENP 409
Cdd:PRK09943  113 TYQPGTTTGERIKHQGEEIGTVLEGEIVLTINGQDYHLVAGQSYAINTGIPHSFSNT 169
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 351-417 3.02e-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: 37.96  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 351 RITVKPGGAfsmqmhhhRAEHW--------VILAGTGQVTV--NGKQ---FLLTENQSTFIPIGAEHSLENPGRIPLEVL 417
Cdd:cd20306    38 RLRLSPGGI--------REPHWhpnanelgYVISGEARVSIldPTGSldtFTVKPGQVVFIPQGWLHWIENVGDEEAHLL 109
bicupin_oxalic TIGR03404
bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins ...
 352-419 4.89e-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: 38.84  E-value: 4.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105327365 352 ITVKPGGAfsMQMH-HHRAEHWV-ILAGTGQVTVngkqFLLTENQSTF---------IPIGAEHSLENPGRIPLEVLEI 419
Cdd:TIGR03404 250 VTVEPGAM--RELHwHPNADEWQyFIQGQARMTV----FAAGGNARTFdyqagdvgyVPRNMGHYVENTGDETLVFLEV 322
cupin_CV2614-like cd02236
Chromobacterium violaceum CV2614 and related proteins, cupin domain; This family includes ...
 344-429 6.01e-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: 6.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105327365 344 TPRFNVNRITVKPGGAFSmqMHHHRaehwVILAG---TGQVTV---NGKQFLLTENQStFI-PIGAEHSLENPGRIPLEV 416
Cdd:cd02236    19 QPEITVLRITIPPGAELP--WHTHP----VPNAGyvlSGELTVeyeDGKKRTFKAGDA-FVeAVNTWHRGRNGGDEPVEL 91

                          90
                  ....*....|...
gi 2105327365 417 LEIqsgsYLGEDD 429
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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