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Conserved domains on  [gi|347546312|gb|AEP03278|]
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ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit, partial (plastid) [uncultured marine phototrophic eukaryote]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RuBisCO_large super family cl08232
Ribulose bisphosphate carboxylase large chain; Ribulose bisphosphate carboxylase (Rubisco) ...
 1-137 4.87e-95

Ribulose bisphosphate carboxylase large chain; Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV, which differ in their taxonomic distribution and subunit composition. Form I-III have Rubisco activity, while Form IV, also called Rubisco-like proteins (RLP), are missing critical active site residues and therefore do not catalyze CO2 fixation. They are believed to utilize a related enzymatic mechanism, but have divergent functions.


The actual alignment was detected with superfamily member PRK04208:

Pssm-ID: 471793  Cd Length: 468  Bit Score: 281.41  E-value: 4.87e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347546312   1 MMRRAEYAKEIGVPIIMHDYITGGWAANTQLAQWCQNNGMLLHIHRAMHAVLDRNPHHGIHFRVLTKILRLSGGDHLHSG 80
Cdd:PRK04208 243 MYKRAEFAKELGSPIVMIDVVTAGWTALQSLREWCRDNGLALHAHRAMHAAFTRNPNHGISFRVLAKLLRLIGVDHLHTG 322

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 347546312  81 TVVGKLEGDRDATLGWIDIMRDSYIKEDRSRGIFFDQDWGSMPGVLPVASGGIHVWH 137
Cdd:PRK04208 323 TVVGKLEGDRAEVLGYYDILREDFVPEDRSRGIFFDQDWGSIKPVFPVASGGIHPGH 379
 
Name Accession Description Interval E-value
rbcL PRK04208
ribulose bisophosphate carboxylase; Reviewed
 1-137 4.87e-95

ribulose bisophosphate carboxylase; Reviewed


Pssm-ID: 179787  Cd Length: 468  Bit Score: 281.41  E-value: 4.87e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347546312   1 MMRRAEYAKEIGVPIIMHDYITGGWAANTQLAQWCQNNGMLLHIHRAMHAVLDRNPHHGIHFRVLTKILRLSGGDHLHSG 80
Cdd:PRK04208 243 MYKRAEFAKELGSPIVMIDVVTAGWTALQSLREWCRDNGLALHAHRAMHAAFTRNPNHGISFRVLAKLLRLIGVDHLHTG 322

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 347546312  81 TVVGKLEGDRDATLGWIDIMRDSYIKEDRSRGIFFDQDWGSMPGVLPVASGGIHVWH 137
Cdd:PRK04208 323 TVVGKLEGDRAEVLGYYDILREDFVPEDRSRGIFFDQDWGSIKPVFPVASGGIHPGH 379
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
 1-137 3.66e-87

Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV , which differ in their taxonomic distribution and subunit composition. Form I is the most abundant class, present in plants, algae, and bacteria, and forms large complexes composed of 8 large and 8 small subunits.


Pssm-ID: 173977  Cd Length: 450  Bit Score: 260.82  E-value: 3.66e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347546312   1 MMRRAEYAKEIGVPIIMHDYITGgWAANTQLAQWCQNNGMLLHIHRAMHAVLDRNPHHGIHFRVLTKILRLSGGDHLHSG 80
Cdd:cd08212  228 MYKRAEFAKELGSPIIMHDLLTG-FTAIQSLAKWCRDNGMLLHLHRAGHATYDRQKNHGIHFRVLAKWLRLSGVDHIHAG 306

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 347546312  81 TVVGKLEGDRDATLGWIDIMRDSYIKEDRSRGIFFDQDWGSMPGVLPVASGGIHVWH 137
Cdd:cd08212  307 TVVGKLEGDPLVTLGFYDLLRDDYIEKDRSRGIFFTQDWASLPGVMPVASGGIHVGQ 363
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
 1-137 1.32e-64

Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of RuBisCO large chain is the catalytic domain adopting a TIM barrel fold.


Pssm-ID: 459631  Cd Length: 292  Bit Score: 198.35  E-value: 1.32e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347546312    1 MMRRAEYAKEIGVPIIMHDYITGGWAANTQLAQWCQNNGMLLHIHRAMHAVLDRNPHHGIHFRVLTKILRLSGGDHLHSG 80
Cdd:pfam00016  96 MYRRAEFAKETGGVAVMVDGLVIGPTAITTLRRWFRDNGVILHYHRAGHGAVTRQSKHGISFRVLAKMARLAGADHLHTG 175

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 347546312   81 TV-VGKLEGDRDatlgwiDIMRDSYIKEDRSRGIFFDQDWGSMPGVLPVASGGIHVWH 137
Cdd:pfam00016 176 TMgVGKLEGDPS------DTLRAYMLEEDRARGPFFDQDWGGMPAVMPVASGGIHAGQ 227
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
 1-137 1.55e-46

Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate transport and metabolism];


Pssm-ID: 441455  Cd Length: 417  Bit Score: 155.33  E-value: 1.55e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347546312   1 MMRRAEYAKEIGVPIIMHDYITGGWAANTQLAQWcqNNGMLLHIHRAMHAVLDRNPHHGIHFRVLTKILRLSGGDHLHSG 80
Cdd:COG1850  229 MLRRADLAVELGANAVMVDVNTVGLSAVQTLREE--HIGLPIHAHRAGHGAFTRSPLHGISMRVLAKLWRLAGADHLHVG 306

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 347546312  81 TVVGKLEGDRDATLGWIDIMRdsyikedrsrgiffdQDWGSMPGVLPVASGGIHVWH 137
Cdd:COG1850  307 TPVGKMEGDDEEVLAIADALL---------------QPWGGLKPVFPVPSGGQHPGQ 348
rubisco_III TIGR03326
ribulose bisphosphate carboxylase, type III; Members of this protein family are the archaeal, ...
 1-134 1.18e-32

ribulose bisphosphate carboxylase, type III; Members of this protein family are the archaeal, single chain, type III form of ribulose bisphosphate carboxylase, or RuBisCO. Members act is a three-step pathway for conversion of the sugar moiety of AMP to two molecules of 3-phosphoglycerate. Many of these species use ADP-dependent sugar kinases, which form AMP, for glycolysis. [Energy metabolism, Sugars]


Pssm-ID: 188307  Cd Length: 411  Bit Score: 118.72  E-value: 1.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347546312    1 MMRRAEYAKEIGVPIIMHDYITGGWAANTQLAQWCQNNGMLLHIHRAMHAVLDRNPHHGIHFRVLTKILRLSGGDHLHSG 80
Cdd:TIGR03326 225 MERRAELVADLGGEYVMVDIVVAGWSALQYVRERTEDLGLAIHAHRAMHAAFTRNPKHGISMFVLAKLYRLIGVDQLHTG 304

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 347546312   81 TV-VGKLEGDRDATLGWIDIMRdsyikedrsrgiffdQDWGSMPGVLPVASGGIH 134
Cdd:TIGR03326 305 TAgVGKLEGGNEDTKGINDFLR---------------QDWHHIKPVFPVASGGLH 344
 
Name Accession Description Interval E-value
rbcL PRK04208
ribulose bisophosphate carboxylase; Reviewed
 1-137 4.87e-95

ribulose bisophosphate carboxylase; Reviewed


Pssm-ID: 179787  Cd Length: 468  Bit Score: 281.41  E-value: 4.87e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347546312   1 MMRRAEYAKEIGVPIIMHDYITGGWAANTQLAQWCQNNGMLLHIHRAMHAVLDRNPHHGIHFRVLTKILRLSGGDHLHSG 80
Cdd:PRK04208 243 MYKRAEFAKELGSPIVMIDVVTAGWTALQSLREWCRDNGLALHAHRAMHAAFTRNPNHGISFRVLAKLLRLIGVDHLHTG 322

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 347546312  81 TVVGKLEGDRDATLGWIDIMRDSYIKEDRSRGIFFDQDWGSMPGVLPVASGGIHVWH 137
Cdd:PRK04208 323 TVVGKLEGDRAEVLGYYDILREDFVPEDRSRGIFFDQDWGSIKPVFPVASGGIHPGH 379
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
 1-137 4.33e-91

ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit


Pssm-ID: 176981  Cd Length: 475  Bit Score: 271.58  E-value: 4.33e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347546312   1 MMRRAEYAKEIGVPIIMHDYITGGWAANTQLAQWCQNNGMLLHIHRAMHAVLDRNPHHGIHFRVLTKILRLSGGDHLHSG 80
Cdd:CHL00040 250 MYKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHAG 329

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 347546312  81 TVVGKLEGDRDATLGWIDIMRDSYIKEDRSRGIFFDQDWGSMPGVLPVASGGIHVWH 137
Cdd:CHL00040 330 TVVGKLEGEREMTLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWH 386
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
 1-137 3.66e-87

Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV , which differ in their taxonomic distribution and subunit composition. Form I is the most abundant class, present in plants, algae, and bacteria, and forms large complexes composed of 8 large and 8 small subunits.


Pssm-ID: 173977  Cd Length: 450  Bit Score: 260.82  E-value: 3.66e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347546312   1 MMRRAEYAKEIGVPIIMHDYITGgWAANTQLAQWCQNNGMLLHIHRAMHAVLDRNPHHGIHFRVLTKILRLSGGDHLHSG 80
Cdd:cd08212  228 MYKRAEFAKELGSPIIMHDLLTG-FTAIQSLAKWCRDNGMLLHLHRAGHATYDRQKNHGIHFRVLAKWLRLSGVDHIHAG 306

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 347546312  81 TVVGKLEGDRDATLGWIDIMRDSYIKEDRSRGIFFDQDWGSMPGVLPVASGGIHVWH 137
Cdd:cd08212  307 TVVGKLEGDPLVTLGFYDLLRDDYIEKDRSRGIFFTQDWASLPGVMPVASGGIHVGQ 363
RuBisCO_large_I_II_III cd08206
Ribulose bisphosphate carboxylase large chain, Form I,II,III; Ribulose bisphosphate ...
 1-137 7.95e-75

Ribulose bisphosphate carboxylase large chain, Form I,II,III; Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV, which differ in their taxonomic distribution and subunit composition. Form I-III have Rubisco activity, while Form IV, also called Rubico-like proteins (RLP), are missing critical active site residues.


Pssm-ID: 173971  Cd Length: 414  Bit Score: 228.27  E-value: 7.95e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347546312   1 MMRRAEYAKEIGVPIIMHDYITGGWAANTQLAQWCQNNGMLLHIHRAMHAVLDRNPHHGIHFRVLTKILRLSGGDHLHSG 80
Cdd:cd08206  215 MIKRAEFAKELGSVIVMVDGVTAGWTAIQSARRWCPDNGLALHAHRAGHAAFTRQKNHGISMRVLAKLARLIGVDHIHTG 294

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 347546312  81 TVVGKLEGDRDATLGWIDIMRDSYIKEDRSRgIFFDQDWGSMPGVLPVASGGIHVWH 137
Cdd:cd08206  295 TVVGKLEGDPSEVKGIADMLREDEVEGDLSR-IFFNQDWGGMKPVFPVASGGLHPGR 350
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
 1-137 1.32e-64

Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of RuBisCO large chain is the catalytic domain adopting a TIM barrel fold.


Pssm-ID: 459631  Cd Length: 292  Bit Score: 198.35  E-value: 1.32e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347546312    1 MMRRAEYAKEIGVPIIMHDYITGGWAANTQLAQWCQNNGMLLHIHRAMHAVLDRNPHHGIHFRVLTKILRLSGGDHLHSG 80
Cdd:pfam00016  96 MYRRAEFAKETGGVAVMVDGLVIGPTAITTLRRWFRDNGVILHYHRAGHGAVTRQSKHGISFRVLAKMARLAGADHLHTG 175

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 347546312   81 TV-VGKLEGDRDatlgwiDIMRDSYIKEDRSRGIFFDQDWGSMPGVLPVASGGIHVWH 137
Cdd:pfam00016 176 TMgVGKLEGDPS------DTLRAYMLEEDRARGPFFDQDWGGMPAVMPVASGGIHAGQ 227
RuBisCO_large cd08148
Ribulose bisphosphate carboxylase large chain; Ribulose bisphosphate carboxylase (Rubisco) ...
 1-137 3.02e-48

Ribulose bisphosphate carboxylase large chain; Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV, which differ in their taxonomic distribution and subunit composition. Form I-III have Rubisco activity, while Form IV, also called Rubisco-like proteins (RLP), are missing critical active site residues and therefore do not catalyze CO2 fixation. They are believed to utilize a related enzymatic mechanism, but have divergent functions.


Pssm-ID: 173969  Cd Length: 366  Bit Score: 158.36  E-value: 3.02e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347546312   1 MMRRAEYAKEIGVPIIMHDYITGGWAANTQLAQWCQNnGMLLHIHRAMHAVLDRNPHHGIHFRVLTKILRLSGGDHLHSG 80
Cdd:cd08148  209 IIERAERALELGANMLMVDVLTAGFSALQALAEDFEI-DLPIHVHRAMHGAVTRSKFHGISMLVLAKLLRMAGGDFIHTG 287

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 347546312  81 TVVGKLEGDRDATLGWIDIMRDsyikedrsrgiffdqDWGSMPGVLPVASGGIHVWH 137
Cdd:cd08148  288 TVVGKMALEREEALGIADALTD---------------DWAGFKRVFPVASGGIHPGL 329
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
 1-137 1.55e-46

Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate transport and metabolism];


Pssm-ID: 441455  Cd Length: 417  Bit Score: 155.33  E-value: 1.55e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347546312   1 MMRRAEYAKEIGVPIIMHDYITGGWAANTQLAQWcqNNGMLLHIHRAMHAVLDRNPHHGIHFRVLTKILRLSGGDHLHSG 80
Cdd:COG1850  229 MLRRADLAVELGANAVMVDVNTVGLSAVQTLREE--HIGLPIHAHRAGHGAFTRSPLHGISMRVLAKLWRLAGADHLHVG 306

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 347546312  81 TVVGKLEGDRDATLGWIDIMRdsyikedrsrgiffdQDWGSMPGVLPVASGGIHVWH 137
Cdd:COG1850  307 TPVGKMEGDDEEVLAIADALL---------------QPWGGLKPVFPVPSGGQHPGQ 348
RuBisCO_large_III cd08213
Ribulose bisphosphate carboxylase large chain, Form III; Ribulose bisphosphate carboxylase ...
 1-134 1.32e-42

Ribulose bisphosphate carboxylase large chain, Form III; Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV , which differ in their taxonomic distribution and subunit composition. Form III is only found in archaea and forms large subunit oligomers (dimers or decamers) that do not include small subunits.


Pssm-ID: 173978  Cd Length: 412  Bit Score: 144.84  E-value: 1.32e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347546312   1 MMRRAEYAKEIGVPIIMHDYITGGWAANTQLAQWCQNNGMLLHIHRAMHAVLDRNPHHGIHFRVLTKILRLSGGDHLHSG 80
Cdd:cd08213  213 MERRAELVADLGGKYVMIDVVVAGWSALQYLRDLAEDYGLAIHAHRAMHAAFTRNPRHGISMLVLAKLYRLIGVDQLHIG 292

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 347546312  81 TVVGKLEGDRDATLGWIDIMRDSYIKEDrSRGIFFDQDWGSMPGVLPVASGGIH 134
Cdd:cd08213  293 TAVGKMEGDKEEVLRIADILREQKYKPD-EEDFHLAQDWGGIKPVFPVASGGLH 345
rubisco_III TIGR03326
ribulose bisphosphate carboxylase, type III; Members of this protein family are the archaeal, ...
 1-134 1.18e-32

ribulose bisphosphate carboxylase, type III; Members of this protein family are the archaeal, single chain, type III form of ribulose bisphosphate carboxylase, or RuBisCO. Members act is a three-step pathway for conversion of the sugar moiety of AMP to two molecules of 3-phosphoglycerate. Many of these species use ADP-dependent sugar kinases, which form AMP, for glycolysis. [Energy metabolism, Sugars]


Pssm-ID: 188307  Cd Length: 411  Bit Score: 118.72  E-value: 1.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347546312    1 MMRRAEYAKEIGVPIIMHDYITGGWAANTQLAQWCQNNGMLLHIHRAMHAVLDRNPHHGIHFRVLTKILRLSGGDHLHSG 80
Cdd:TIGR03326 225 MERRAELVADLGGEYVMVDIVVAGWSALQYVRERTEDLGLAIHAHRAMHAAFTRNPKHGISMFVLAKLYRLIGVDQLHTG 304

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 347546312   81 TV-VGKLEGDRDATLGWIDIMRdsyikedrsrgiffdQDWGSMPGVLPVASGGIH 134
Cdd:TIGR03326 305 TAgVGKLEGGNEDTKGINDFLR---------------QDWHHIKPVFPVASGGLH 344
PRK13475 PRK13475
ribulose-bisphosphate carboxylase;
1-133 3.84e-16

ribulose-bisphosphate carboxylase;


Pssm-ID: 184072  Cd Length: 443  Bit Score: 73.60  E-value: 3.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347546312   1 MMRRAEYAKEIGVPIIMH-----DYITGGWAANTQLAQwcQNNGMLLHIHRAMH-AVLDRNPHHGIHFRVLTKILRLSGG 74
Cdd:PRK13475 240 MIARGEYILETFGENADHvaflvDGYVAGPGAVTTARR--QYPDQYLHYHRAGHgAVTSPSSKRGYTAFVLSKMARLQGA 317

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 347546312  75 DHLHSGTV-VGKLEGDRDatlgwiDIMRDSYIKEDRSRGIFFDQDWGSMPGVLPVASGGI 133
Cdd:PRK13475 318 SGIHTGTMgYGKMEGEAD------DRVIAYMIERDSAQGPFYHQEWYGMKPTTPIISGGM 371
RuBisCO_large_II cd08211
Ribulose bisphosphate carboxylase large chain, Form II; Ribulose bisphosphate carboxylase ...
 1-133 2.90e-14

Ribulose bisphosphate carboxylase large chain, Form II; Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV , which differ in their taxonomic distribution and subunit composition. Form II is mainly found in bacteria, and forms large subunit oligomers (dimers, tetramers, etc.) that do not include small subunits.


Pssm-ID: 173976  Cd Length: 439  Bit Score: 67.91  E-value: 2.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347546312   1 MMRRAEYAKEIGVPIIMH-----DYITGGWAANTQLAQWCQNNgmLLHIHRAMH-AVLDRNPHHGIHFRVLTKILRLSGG 74
Cdd:cd08211  239 MIARGEYILEAFGPNAGHvaflvDGYVAGPAAVTTARRRFPDQ--FLHYHRAGHgAVTSPQSKRGYTAFVLSKMARLQGA 316

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 347546312  75 DHLHSGTV-VGKLEGDRDATLgwIDIMrdsyIKEDRSRGIFFDQDWGSMPGVLPVASGGI 133
Cdd:cd08211  317 SGIHTGTMgFGKMEGESSDKV--IAYM----IERDEAQGPLFNQKWYGMKPTTPIISGGM 370
RuBisCO_IV_RLP cd08205
Ribulose bisphosphate carboxylase like proteins, Rubisco-Form IV; Ribulose bisphosphate ...
 1-136 3.88e-14

Ribulose bisphosphate carboxylase like proteins, Rubisco-Form IV; Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV, which differ in their taxonomic distribution and subunit composition. Form I-III have Rubisco activity, while Form IV, also called Rubisco-like proteins (RLP), are missing critical active site residues and therefore do not catalyze CO2 fixation. They are believed to utilize a related enzymatic mechanism, but have divergent functions, like for example 2,3-diketo-5-methylthiopentyl-1-phosphate enolase or 5-methylthio-d-ribulose 1-phosphate isomerase.


Pssm-ID: 173970  Cd Length: 367  Bit Score: 67.56  E-value: 3.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347546312   1 MMRRAEYAKEIGVPIIMHDYITGGWAANTQLAQwcqNNGMLLHIHRAMHAVLDRNPHHGIHFRVLTKILRLSGGDHLHSG 80
Cdd:cd08205  212 LRRRADRAVEAGANALLINPNLVGLDALRALAE---DPDLPIMAHPAFAGALSRSPDYGSHFLLLGKLMRLAGADAVIFP 288

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 347546312  81 TVVGKLEGDRDATLGWIDIMRdsyikedrsrgiffdQDWGSMPGVLPVASGGIHVW 136
Cdd:cd08205  289 GPGGRFPFSREECLAIARACR---------------RPLGGIKPALPVPSGGMHPG 329
RLP_NonPhot cd08207
Ribulose bisphosphate carboxylase like proteins from nonphototrophic bacteria; Ribulose ...
 1-136 6.39e-09

Ribulose bisphosphate carboxylase like proteins from nonphototrophic bacteria; Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV, which differ in their taxonomic distribution and subunit composition. Form I-III have Rubisco activity, while Form IV, also called Rubisco-like proteins (RLP), are missing critical active site residues and therefore do not catalyze CO2 fixation. They are believed to utilize a related enzymatic mechanism, but have divergent functions. The specific function of this subgroup is unknown.


Pssm-ID: 173972  Cd Length: 406  Bit Score: 52.70  E-value: 6.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347546312   1 MMRRAEYAKEIGVPIIMHDYITGGWAANTQLAQWCQnngMLLHIHRAMHAVLDRNPHHGIHFRVLTKILRLSGGDHLHSG 80
Cdd:cd08207  225 MRRNHDLVVEAGGTCVMVSLNSVGLSGLAALRRHSQ---LPIHGHRNGWGMLTRSPALGISFQAYQKLWRLAGVDHLHVN 301

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 347546312  81 TVVGKL-EGDrdatlgwidimrDSYIKEDRSrgiFFDQDWGSMPGVLPVASGGIHVW 136
Cdd:cd08207  302 GLASKFwESD------------DSVIESARA---CLTPLGGPDDAAMPVFSSGQWGG 343
 
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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