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Conserved domains on  [gi|23505883|gb|AAN28801|]
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At3g04880/T9J14_17 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RpiB COG0698
Ribose 5-phosphate isomerase RpiB [Carbohydrate transport and metabolism]; Ribose 5-phosphate ...
 13-136 4.44e-38

Ribose 5-phosphate isomerase RpiB [Carbohydrate transport and metabolism]; Ribose 5-phosphate isomerase RpiB is part of the Pathway/BioSystem: Pentose phosphate pathway


:

Pssm-ID: 440462  Cd Length: 149  Bit Score: 132.13  E-value: 4.44e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23505883  13 KIITGADDFGASLKDAMVTHLRSLGIDVEDTGVSS-----YYSAGSEVGRRVSASSSSevRGLVCCGTGVGVAMFANKFP 87
Cdd:COG0698   2 KIAIGSDHAGFELKEAIKEYLEEKGHEVVDFGTYSedsvdYPDFAIKVAEAVASGEAD--RGILICGTGIGMSIAANKVP 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 23505883  88 GVYAATCLSVEDAVNARSISNCNVLAFSGIKTSPETALEIFDAWIKTPF 136
Cdd:COG0698  80 GIRAALCHDPYSARLAREHNDANVLCLGARVIGPELAKEIVDAFLATEF 128
cupin_RmlC-like super family cl40423
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 203-290 1.32e-15

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.


The actual alignment was detected with superfamily member cd06989:

Pssm-ID: 477354  Cd Length: 97  Bit Score: 71.02  E-value: 1.32e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23505883 203 MPGGSMKIVRETPTSA---IVRFK--AGSVEPAHHHTFGHDLVVIKGKKSVWNLSK----KERAdLVDGDYLFTPAGDVH 273
Cdd:cd06989   1 PPGAKAAVLEGDPSKPgpfVVRLKfpAGYKIPPHTHPDDERVTVISGTFYLGMGDKfdeaKAKA-LPAGSFFTLPAGTPH 79

                        90
                ....*....|....*...
gi 23505883 274 RVKYH-EDTEFFITWDGH 290
Cdd:cd06989  80 FAWAKdEETVVQVTGEGP 97
 
Name Accession Description Interval E-value
RpiB COG0698
Ribose 5-phosphate isomerase RpiB [Carbohydrate transport and metabolism]; Ribose 5-phosphate ...
 13-136 4.44e-38

Ribose 5-phosphate isomerase RpiB [Carbohydrate transport and metabolism]; Ribose 5-phosphate isomerase RpiB is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 440462  Cd Length: 149  Bit Score: 132.13  E-value: 4.44e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23505883  13 KIITGADDFGASLKDAMVTHLRSLGIDVEDTGVSS-----YYSAGSEVGRRVSASSSSevRGLVCCGTGVGVAMFANKFP 87
Cdd:COG0698   2 KIAIGSDHAGFELKEAIKEYLEEKGHEVVDFGTYSedsvdYPDFAIKVAEAVASGEAD--RGILICGTGIGMSIAANKVP 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 23505883  88 GVYAATCLSVEDAVNARSISNCNVLAFSGIKTSPETALEIFDAWIKTPF 136
Cdd:COG0698  80 GIRAALCHDPYSARLAREHNDANVLCLGARVIGPELAKEIVDAFLATEF 128
LacAB_rpiB pfam02502
Ribose/Galactose Isomerase; This family of proteins contains the sugar isomerase enzymes ...
 14-138 1.67e-34

Ribose/Galactose Isomerase; This family of proteins contains the sugar isomerase enzymes ribose 5-phosphate isomerase B (rpiB), galactose isomerase subunit A (LacA) and galactose isomerase subunit B (LacB).


Pssm-ID: 460573  Cd Length: 134  Bit Score: 122.11  E-value: 1.67e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23505883    14 IITGADDFGASLKDAMVTHLRSLGIDVEDTGVSS-----YYSAGSEVGRRVSASSSSevRGLVCCGTGVGVAMFANKFPG 88
Cdd:pfam02502   1 IAIGSDHAGFELKEEIKEYLEEKGHEVIDFGTYSeesvdYPDYAHKVAEAVASGEAD--RGILICGTGIGMSIAANKVPG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 23505883    89 VYAATCLSVEDAVNARSISNCNVLAFSGIKTSPETALEIFDAWIKTPFKS 138
Cdd:pfam02502  79 IRAALCHDPYSAKLAREHNDANVLCLGARVIGPELAKEIVDAFLNTEFEG 128
PRK05571 PRK05571
ribose-5-phosphate isomerase B; Provisional
 13-136 4.33e-29

ribose-5-phosphate isomerase B; Provisional


Pssm-ID: 235509  Cd Length: 148  Bit Score: 108.71  E-value: 4.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23505883   13 KIITGADDFGASLKDAMVTHLRSLGIDVEDTGVSSY-----YSA-GSEVGRRVSASSSSevRGLVCCGTGVGVAMFANKF 86
Cdd:PRK05571   2 KIAIGSDHAGFELKEEIIEHLEELGHEVIDLGPDSYdasvdYPDyAKKVAEAVVAGEAD--RGILICGTGIGMSIAANKV 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 23505883   87 PGVYAATCLSVEDAVNARSISNCNVLAFSGIKTSPETALEIFDAWIKTPF 136
Cdd:PRK05571  80 KGIRAALCHDTYSAHLAREHNNANVLALGARVIGPELAKDIVDAFLATEF 129
rpiB_lacA_lacB TIGR00689
sugar-phosphate isomerase, RpiB/LacA/LacB family; Proteins of known function in this family ...
 14-136 3.36e-22

sugar-phosphate isomerase, RpiB/LacA/LacB family; Proteins of known function in this family act as sugar (pentose and/or hexose)-phosphate isomerases, including the LacA and LacB subunits of galactose-6-phosphate isomerases from Gram-positive bacteria and RpiB. RpiB is the second ribose phosphate isomerase of E. coli. It lacks homology to RpiA, its inducer is unknown (but is not ribose), and it can be replaced by the homologous galactose-6-phosphate isomerase of Streptococcus mutans, all of which suggests that the ribose phosphate isomerase activity of RpiB is a secondary function. On the other hand, there appear to be a significant number of species which contain rpiB, lack rpiA and seem to require rpi activity in order to complete the pentose phosphate pathway.


Pssm-ID: 129772  Cd Length: 144  Bit Score: 90.13  E-value: 3.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23505883    14 IITGADDFGASLKDAMVTHLRSLGIDVEDTGVSS-----YYSAGSEVGRRVSASSSSevRGLVCCGTGVGVAMFANKFPG 88
Cdd:TIGR00689   1 IAIGSDHAGLELKSEIIEHLKQKGHEVIDCGTLYdervdYPDYAKLVADKVVAGEVS--LGILICGTGIGMSIAANKFKG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 23505883    89 VYAATCLSVEDAVNARSISNCNVLAFSGIKTSPETALEIFDAWIKTPF 136
Cdd:TIGR00689  79 IRAALCVDEYTAALARQHNDANVLCLGSRVVGVELALSIVDAFLTTQF 126
cupin_DRT102 cd06989
Arabidopsis thaliana DRT102 and related proteins, cupin domain; This family includes bacterial ...
 203-290 1.32e-15

Arabidopsis thaliana DRT102 and related proteins, cupin domain; This family includes bacterial and eukaryotic proteins homologous to DNA-damage-repair/toleration protein DRT102 found in Arabidopsis thaliana. DRT102 may be involved in DNA repair from UV damage. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380394  Cd Length: 97  Bit Score: 71.02  E-value: 1.32e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23505883 203 MPGGSMKIVRETPTSA---IVRFK--AGSVEPAHHHTFGHDLVVIKGKKSVWNLSK----KERAdLVDGDYLFTPAGDVH 273
Cdd:cd06989   1 PPGAKAAVLEGDPSKPgpfVVRLKfpAGYKIPPHTHPDDERVTVISGTFYLGMGDKfdeaKAKA-LPAGSFFTLPAGTPH 79

                        90
                ....*....|....*...
gi 23505883 274 RVKYH-EDTEFFITWDGH 290
Cdd:cd06989  80 FAWAKdEETVVQVTGEGP 97
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
204-285 2.69e-06

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 45.22  E-value: 2.69e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23505883 204 PGGSMKIVRETPTS---AIVRFKAGSVEPAHHHTFGHDLVVIKGKksVWNLSKKERADLVDGDYLFTPAGDVHRVKYHED 280
Cdd:COG1917   9 TGVSVRVLADGEDElevVRVTFEPGARTPWHSHPGEELIYVLEGE--GEVEVGGEEYELKPGDVVFIPPGVPHAFRNLGD 86


                ....*
gi 23505883 281 TEFFI 285
Cdd:COG1917  87 EPAVL 91
Cupin_7 pfam12973
ChrR Cupin-like domain; Members of this family are part of the cupin superfamily. This family ...
 215-286 1.07e-04

ChrR Cupin-like domain; Members of this family are part of the cupin superfamily. This family includes the transcriptional activator ChrR.


Pssm-ID: 463764 [Multi-domain]  Cd Length: 91  Bit Score: 40.31  E-value: 1.07e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23505883   215 PTSAIVRFKAGSVEPAHHHTFGHDLVVIKGkksVWnlsKKERADLVDGDYLFTPAGDVHRVKYHEDTEFFIT 286
Cdd:pfam12973  24 RATSLVRYAPGSRFPAHRHPGGEEILVLEG---VF---SDEHGDYPAGTYLRNPPGSSHAPFSEEGCTIFVK 89
 
Name Accession Description Interval E-value
RpiB COG0698
Ribose 5-phosphate isomerase RpiB [Carbohydrate transport and metabolism]; Ribose 5-phosphate ...
 13-136 4.44e-38

Ribose 5-phosphate isomerase RpiB [Carbohydrate transport and metabolism]; Ribose 5-phosphate isomerase RpiB is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 440462  Cd Length: 149  Bit Score: 132.13  E-value: 4.44e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23505883  13 KIITGADDFGASLKDAMVTHLRSLGIDVEDTGVSS-----YYSAGSEVGRRVSASSSSevRGLVCCGTGVGVAMFANKFP 87
Cdd:COG0698   2 KIAIGSDHAGFELKEAIKEYLEEKGHEVVDFGTYSedsvdYPDFAIKVAEAVASGEAD--RGILICGTGIGMSIAANKVP 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 23505883  88 GVYAATCLSVEDAVNARSISNCNVLAFSGIKTSPETALEIFDAWIKTPF 136
Cdd:COG0698  80 GIRAALCHDPYSARLAREHNDANVLCLGARVIGPELAKEIVDAFLATEF 128
LacAB_rpiB pfam02502
Ribose/Galactose Isomerase; This family of proteins contains the sugar isomerase enzymes ...
 14-138 1.67e-34

Ribose/Galactose Isomerase; This family of proteins contains the sugar isomerase enzymes ribose 5-phosphate isomerase B (rpiB), galactose isomerase subunit A (LacA) and galactose isomerase subunit B (LacB).


Pssm-ID: 460573  Cd Length: 134  Bit Score: 122.11  E-value: 1.67e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23505883    14 IITGADDFGASLKDAMVTHLRSLGIDVEDTGVSS-----YYSAGSEVGRRVSASSSSevRGLVCCGTGVGVAMFANKFPG 88
Cdd:pfam02502   1 IAIGSDHAGFELKEEIKEYLEEKGHEVIDFGTYSeesvdYPDYAHKVAEAVASGEAD--RGILICGTGIGMSIAANKVPG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 23505883    89 VYAATCLSVEDAVNARSISNCNVLAFSGIKTSPETALEIFDAWIKTPFKS 138
Cdd:pfam02502  79 IRAALCHDPYSAKLAREHNDANVLCLGARVIGPELAKEIVDAFLNTEFEG 128
PRK05571 PRK05571
ribose-5-phosphate isomerase B; Provisional
 13-136 4.33e-29

ribose-5-phosphate isomerase B; Provisional


Pssm-ID: 235509  Cd Length: 148  Bit Score: 108.71  E-value: 4.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23505883   13 KIITGADDFGASLKDAMVTHLRSLGIDVEDTGVSSY-----YSA-GSEVGRRVSASSSSevRGLVCCGTGVGVAMFANKF 86
Cdd:PRK05571   2 KIAIGSDHAGFELKEEIIEHLEELGHEVIDLGPDSYdasvdYPDyAKKVAEAVVAGEAD--RGILICGTGIGMSIAANKV 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 23505883   87 PGVYAATCLSVEDAVNARSISNCNVLAFSGIKTSPETALEIFDAWIKTPF 136
Cdd:PRK05571  80 KGIRAALCHDTYSAHLAREHNNANVLALGARVIGPELAKDIVDAFLATEF 129
rpiB_lacA_lacB TIGR00689
sugar-phosphate isomerase, RpiB/LacA/LacB family; Proteins of known function in this family ...
 14-136 3.36e-22

sugar-phosphate isomerase, RpiB/LacA/LacB family; Proteins of known function in this family act as sugar (pentose and/or hexose)-phosphate isomerases, including the LacA and LacB subunits of galactose-6-phosphate isomerases from Gram-positive bacteria and RpiB. RpiB is the second ribose phosphate isomerase of E. coli. It lacks homology to RpiA, its inducer is unknown (but is not ribose), and it can be replaced by the homologous galactose-6-phosphate isomerase of Streptococcus mutans, all of which suggests that the ribose phosphate isomerase activity of RpiB is a secondary function. On the other hand, there appear to be a significant number of species which contain rpiB, lack rpiA and seem to require rpi activity in order to complete the pentose phosphate pathway.


Pssm-ID: 129772  Cd Length: 144  Bit Score: 90.13  E-value: 3.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23505883    14 IITGADDFGASLKDAMVTHLRSLGIDVEDTGVSS-----YYSAGSEVGRRVSASSSSevRGLVCCGTGVGVAMFANKFPG 88
Cdd:TIGR00689   1 IAIGSDHAGLELKSEIIEHLKQKGHEVIDCGTLYdervdYPDYAKLVADKVVAGEVS--LGILICGTGIGMSIAANKFKG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 23505883    89 VYAATCLSVEDAVNARSISNCNVLAFSGIKTSPETALEIFDAWIKTPF 136
Cdd:TIGR00689  79 IRAALCVDEYTAALARQHNDANVLCLGSRVVGVELALSIVDAFLTTQF 126
PTZ00215 PTZ00215
ribose 5-phosphate isomerase; Provisional
 11-137 7.24e-20

ribose 5-phosphate isomerase; Provisional


Pssm-ID: 185516  Cd Length: 151  Bit Score: 84.30  E-value: 7.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23505883   11 PLKIITGADDFGASLKDAMVTHLR--SLGIDVEDTGVSS-----YYSAGSEVGRRVSasSSSEVRGLVCCGTGVGVAMFA 83
Cdd:PTZ00215   2 QKKVAIGSDHAGFDLKNEIIDYIKnkGKEYKIEDMGTYTaesvdYPDFAEKVCEEVL--KGEADTGILVCGSGIGISIAA 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 23505883   84 NKFPGVYAATCLSVEDAVNARSISNCNVLAFSGIKTSPETALEIFDAWIKTPFK 137
Cdd:PTZ00215  80 NKVKGIRCALCHDHYTARMSRQHNNANVLAFGGRTTGIEVAKEIIDTFLSTPFE 133
PRK08622 PRK08622
galactose-6-phosphate isomerase subunit LacB; Reviewed
 12-137 7.58e-19

galactose-6-phosphate isomerase subunit LacB; Reviewed


Pssm-ID: 181506  Cd Length: 171  Bit Score: 82.00  E-value: 7.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23505883   12 LKIITGADDFGASLKDAMVTHLRSLGIDVEDTG----VSSYYSA-GSEVGRRVsASSSSEVrGLVCCGTGVGVAMFANKF 86
Cdd:PRK08622   1 MKIAIGCDHIVTDEKMAVSDYLKSKGHEVIDVGtydfTRTHYPIfGKKVGEAV-ASGEADL-GVCICGTGVGISNAVNKV 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 23505883   87 PGVYAATCLSVEDAVNARSISNCNVLAFSGIKTSPETALEIFDAWIKTPFK 137
Cdd:PRK08622  79 PGIRSALVRDMTSALYAKEELNANVIGFGGKITGELLMCDIIDAFINAEYK 129
rpiB TIGR01120
ribose 5-phosphate isomerase B; Involved in the non-oxidative branch of the pentose phospate ...
 13-137 8.38e-18

ribose 5-phosphate isomerase B; Involved in the non-oxidative branch of the pentose phospate pathway. [Energy metabolism, Pentose phosphate pathway]


Pssm-ID: 130190  Cd Length: 143  Bit Score: 78.42  E-value: 8.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23505883    13 KIITGADDFGASLKDAMVTHLRSLGIDVEDTGVSS-----YYSAGSEVGRRVSASSSSevRGLVCCGTGVGVAMFANKFP 87
Cdd:TIGR01120   1 KIAIGSDHAGFILKEEIKAFLVERGVKVIDKGTWSsertdYPHYAKQVALAVAGGEVD--GGILICGTGIGMSIAANKFA 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 23505883    88 GVYAATCLSVEDAVNARSISNCNVLAFSGIKTSPETALEIFDAWIKTPFK 137
Cdd:TIGR01120  79 GIRAALCSEPYMAQMSRLHNDANVLCLGERVVGLELAKSIVDAWLGTQFE 128
cupin_DRT102 cd06989
Arabidopsis thaliana DRT102 and related proteins, cupin domain; This family includes bacterial ...
 203-290 1.32e-15

Arabidopsis thaliana DRT102 and related proteins, cupin domain; This family includes bacterial and eukaryotic proteins homologous to DNA-damage-repair/toleration protein DRT102 found in Arabidopsis thaliana. DRT102 may be involved in DNA repair from UV damage. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380394  Cd Length: 97  Bit Score: 71.02  E-value: 1.32e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23505883 203 MPGGSMKIVRETPTSA---IVRFK--AGSVEPAHHHTFGHDLVVIKGKKSVWNLSK----KERAdLVDGDYLFTPAGDVH 273
Cdd:cd06989   1 PPGAKAAVLEGDPSKPgpfVVRLKfpAGYKIPPHTHPDDERVTVISGTFYLGMGDKfdeaKAKA-LPAGSFFTLPAGTPH 79

                        90
                ....*....|....*...
gi 23505883 274 RVKYH-EDTEFFITWDGH 290
Cdd:cd06989  80 FAWAKdEETVVQVTGEGP 97
RPI_actino TIGR02133
ribose 5-phosphate isomerase; This family is a member of the RpiB/LacA/LacB subfamily ...
 12-136 3.61e-15

ribose 5-phosphate isomerase; This family is a member of the RpiB/LacA/LacB subfamily (TIGR00689) but lies outside the RpiB equivalog (TIGR01120) which is also a member of that subfamily. Ribose 5-phosphate isomerase is an essential enzyme of the pentose phosphate pathway; a pathway that appears to be present in the actinobacteria. The only candidates for ribose 5-phosphate isomerase in the Actinobacteria are members of this family.


Pssm-ID: 273989  Cd Length: 148  Bit Score: 71.33  E-value: 3.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23505883    12 LKIITGADDFGASLKDAMVTHLRSLGIDVEDTGV------SSYYSAGSEVGRRVSASSSSevRGLVCCGTGVGVAMFANK 85
Cdd:TIGR02133   1 MRVVLGHDHAGFEYKEALWLDLAAHEPEVCDVGVydadddDDYPCFCIAAAEAVARDAAD--LGIVIGGSGNGEAIAANK 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 23505883    86 FPGVYAATCLSVEDAVNARSISNCNVLAFSGIKTSPETALEIFDAWIKTPF 136
Cdd:TIGR02133  79 VKGARAALAWDTASAGRARLHNNANVVGAGMRMHGLEEAFRLVFEFLGFEF 129
PRK12615 PRK12615
galactose-6-phosphate isomerase subunit LacB; Reviewed
 12-137 1.19e-11

galactose-6-phosphate isomerase subunit LacB; Reviewed


Pssm-ID: 171610  Cd Length: 171  Bit Score: 62.35  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23505883   12 LKIITGADDFGASLKDAMVTHLRSLGIDVEDTGV-----SSYYSAGSEVGRRVsASSSSEVrGLVCCGTGVGVAMFANKF 86
Cdd:PRK12615   1 MKIAIGCDHIVTNEKMAVSDFLKSKGYDVIDCGTydhtrTHYPIFGKKVGEAV-VNGQADL-GVCICGTGVGINNAVNKV 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 23505883   87 PGVYAATCLSVEDAVNARSISNCNVLAFSGIKTSPETALEIFDAWIKTPFK 137
Cdd:PRK12615  79 PGIRSALVRDMTTALYAKEELNANVIGFGGKITGELLMCDIIDAFIKAEYK 129
cupin_DAD cd20302
2,4'-Dihydroxyacetophenone dioxygenase (DAD), cupin domain; 2,4'-Dihydroxyacetophenone ...
 200-298 4.04e-09

2,4'-Dihydroxyacetophenone dioxygenase (DAD), cupin domain; 2,4'-Dihydroxyacetophenone dioxygenase (DAD) catalyzes the oxidation of 2,4'-dihydroxyacetophenone to 4-hydroxybenzoate and formate as part of the 4-hydroxyacetophenone catabolic pathway. This enzyme is a homo-tetramer containing one iron per molecule of enzyme. This enzyme is an unusual dioxygenase in that it cleaves a C-C bond in a substituent of the aromatic ring rather than within the ring itself. As a bacterial dioxygenase, DAD plays an important environmental role in the aerobic catabolism of aromatic compounds; expression of this enzyme in appropriately engineered microorganisms has the potential to use these aromatic pollutants as a carbon source and thus remove them from the environment. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380436 [Multi-domain]  Cd Length: 123  Bit Score: 53.69  E-value: 4.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23505883 200 VDIMPGGSMKIVRETPTS----AIVRFKAGSVEPAHHHT---FGHdlvVIKGKksvWNLskKERADLVD-GDYLFTPAGD 271
Cdd:cd20302   6 TPLGPGVWFKPLRFDPETgewvVLLRVPPGGSLPRHRHTgpvHAY---TLSGS---WRY--LEHDWVATaGSYVYEPAGS 77

                        90       100
                ....*....|....*....|....*....
gi 23505883 272 VH--RVKYHEDTEFFITWDGHWdIFLDED 298
Cdd:cd20302  78 IHtlVVPEEEETIVLFIVQGAL-IFLDED 105
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 219-283 1.45e-07

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: 47.86  E-value: 1.45e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23505883 219 IVRFKAGSVEPAHHHTFGHDLV-VIKGKkSVWNLSKKERADLVDGDYLFTPAGDVHRVKYHEDTEF 283
Cdd:cd02208   3 VVTLPPGTSSPPHWHPEQDEIFyVLSGE-GELTLDDGETVELKAGDIVLIPPGVPHSFVNTSDEPA 67
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
204-285 2.69e-06

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 45.22  E-value: 2.69e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23505883 204 PGGSMKIVRETPTS---AIVRFKAGSVEPAHHHTFGHDLVVIKGKksVWNLSKKERADLVDGDYLFTPAGDVHRVKYHED 280
Cdd:COG1917   9 TGVSVRVLADGEDElevVRVTFEPGARTPWHSHPGEELIYVLEGE--GEVEVGGEEYELKPGDVVFIPPGVPHAFRNLGD 86


                ....*
gi 23505883 281 TEFFI 285
Cdd:COG1917  87 EPAVL 91
PRK08621 PRK08621
galactose-6-phosphate isomerase subunit LacA; Reviewed
 12-134 3.31e-06

galactose-6-phosphate isomerase subunit LacA; Reviewed


Pssm-ID: 181505  Cd Length: 142  Bit Score: 45.86  E-value: 3.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23505883   12 LKIITGADDFGASLKDAMVTHLRSLG---IDVEDTGVSSYYSAGSEVGRRVSASSSSevRGLVCCGTGVGVAMFANKFPG 88
Cdd:PRK08621   1 MAIIIGADKAGFELKEVVKDYLEDNKyevVDVTEEGAEDFVDSTLAVAKEVNKSEDN--LGIVIDAYGAGSFMVATKIKG 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 23505883   89 VYAAtclSVED---AVNARSISNCNVLAF-SGIkTSPETALEIFDAWIKT 134
Cdd:PRK08621  79 MVAA---EVSDersAYMTRGHNNARMITMgSEI-VGDGLAKNIIKGFVEG 124
Cupin_7 pfam12973
ChrR Cupin-like domain; Members of this family are part of the cupin superfamily. This family ...
 215-286 1.07e-04

ChrR Cupin-like domain; Members of this family are part of the cupin superfamily. This family includes the transcriptional activator ChrR.


Pssm-ID: 463764 [Multi-domain]  Cd Length: 91  Bit Score: 40.31  E-value: 1.07e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23505883   215 PTSAIVRFKAGSVEPAHHHTFGHDLVVIKGkksVWnlsKKERADLVDGDYLFTPAGDVHRVKYHEDTEFFIT 286
Cdd:pfam12973  24 RATSLVRYAPGSRFPAHRHPGGEEILVLEG---VF---SDEHGDYPAGTYLRNPPGSSHAPFSEEGCTIFVK 89
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 218-287 1.21e-04

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: 39.55  E-value: 1.21e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23505883   218 AIVRFKAGSVEPAHHHTfGHD--LVVIKGKKSVWNlsKKERADLVDGDYLFTPAGDVHRVKYHEDTEFFITW 287
Cdd:pfam07883   1 GLVTLPPGESSPPHRHP-GEDefFYVLEGEGELTV--DGEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLLD 69
cupin_QDO_N_C cd02215
quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known ...
 224-297 1.14e-03

quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known as quercetin 2,3-dioxygenase, 2,3QD, QDO and YxaG; EC 1.13.11.24), a mononuclear copper-dependent dioxygenase that catalyzes the cleavage of the flavonol quercetin (5,7,3',4'-tetrahydroxyflavonol) heterocyclic ring to produce 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon monoxide. Bacillus subtilis quercetin 2,3-dioxygenase (QDO) is a homodimer that shows oxygenase activity with several divalent metals such as Mn2+, Co2+, Fe2+, and Cu2+, although the preferred one appears to be Mn2+. The dioxygen binds to the metal ion of the Cu-QDO-quercetin complex, yielding a Cu2+-superoxo quercetin radical intermediate, which then forms a Cu2+-alkylperoxo complex which then evolves into endoperoxide intermediate that decomposes to the product. Quercetinase is a bicupin with two tandem cupin beta-barrel domains, both of which are included in this alignment model. The pirins, which also belong to the cupin domain family, have been shown to catalyze a reaction involving quercetin and may have a function similar to that of quercetinase.


Pssm-ID: 380345 [Multi-domain]  Cd Length: 122  Bit Score: 38.29  E-value: 1.14e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23505883 224 AGSVEPAHHHTFGHD-LVVIKGKKSVWnLSKKERaDLVDGDYLFTPAGDVH--RVKYHeDTEF--FITwDGHWDIFLDE 297
Cdd:cd02215  41 KGDAIPPHYHKRHHEtFYVLEGRLQLW-LDGESR-LLTPGDFASVPPGTIHayRMLSP-DTRFlgVIT-PGGFERFFRA 115
PRK09273 PRK09273
hypothetical protein; Provisional
 73-115 3.56e-03

hypothetical protein; Provisional


Pssm-ID: 181746 [Multi-domain]  Cd Length: 211  Bit Score: 38.02  E-value: 3.56e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 23505883   73 CGTGVGVAMFANKFPGVYAATCLSVEDAVNARSISNCNVLAFS 115
Cdd:PRK09273  71 CGTGQGAMLALNSFPGVVCGYCIDPTDAYLFAQINNGNALSLP 113
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
 229-285 4.30e-03

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: 35.89  E-value: 4.30e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 23505883 229 PAHHHTFGHDLVVIKGKKSVwnLSKKERADLVDGDYLFTPAGDVHRVKYHEDTEF-FI 285
Cdd:cd02222  31 PLHTHPWEHEVYVLRGKGVV--VIGGEEYPVKPGDVVYIPPNEPHQFRNTGDEPLgFL 86
 
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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