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Conserved domains on  [gi|564813591|gb|AHC03890|]
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ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit, partial (chloroplast) [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) ...
1-171 2.56e-124

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 CHL00040:

Pssm-ID: 471793  Cd Length: 475  Bit Score: 357.86  E-value: 2.56e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591   1 MRWRERFLNCMEGINRASAATGEVKGSYLNVTAATMEEVYKRSEYAKEVGSIIIMIDLVM-GYTAIQSIALWARENDMLL 79
Cdd:CHL00040 212 MRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMYKRAVFARELGVPIVMHDYLTgGFTANTSLAHYCRDNGLLL 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591  80 HLHRAGNSTYARQKNHGINFRVICKWMRMSGVDHIHAGTVVGKLEGDPLMIKGFYDTLRNTTLDVNLPYGLFFEMSWASL 159
Cdd:CHL00040 292 HIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHAGTVVGKLEGEREMTLGFVDLLRDDFIEKDRSRGIYFTQDWVSL 371
                        170
                 ....*....|..
gi 564813591 160 RRCMPVASGGIH 171
Cdd:CHL00040 372 PGVLPVASGGIH 383
 
Name Accession Description Interval E-value
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
1-171 2.56e-124

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


Pssm-ID: 176981  Cd Length: 475  Bit Score: 357.86  E-value: 2.56e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591   1 MRWRERFLNCMEGINRASAATGEVKGSYLNVTAATMEEVYKRSEYAKEVGSIIIMIDLVM-GYTAIQSIALWARENDMLL 79
Cdd:CHL00040 212 MRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMYKRAVFARELGVPIVMHDYLTgGFTANTSLAHYCRDNGLLL 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591  80 HLHRAGNSTYARQKNHGINFRVICKWMRMSGVDHIHAGTVVGKLEGDPLMIKGFYDTLRNTTLDVNLPYGLFFEMSWASL 159
Cdd:CHL00040 292 HIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHAGTVVGKLEGEREMTLGFVDLLRDDFIEKDRSRGIYFTQDWVSL 371
                        170
                 ....*....|..
gi 564813591 160 RRCMPVASGGIH 171
Cdd:CHL00040 372 PGVLPVASGGIH 383
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
1-171 5.79e-117

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: 338.25  E-value: 5.79e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591   1 MRWRERFLNCMEGINRASAATGEVKGSYLNVTAATMEEVYKRSEYAKEVGSIIIMIDLVMGYTAIQSIALWARENDMLLH 80
Cdd:cd08212  190 MRWRDRFLFVAEAVNKAQAETGEVKGHYLNVTAGTMEEMYKRAEFAKELGSPIIMHDLLTGFTAIQSLAKWCRDNGMLLH 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591  81 LHRAGNSTYARQKNHGINFRVICKWMRMSGVDHIHAGTVVGKLEGDPLMIKGFYDTLRNTTLDVNLPYGLFFEMSWASLR 160
Cdd:cd08212  270 LHRAGHATYDRQKNHGIHFRVLAKWLRLSGVDHIHAGTVVGKLEGDPLVTLGFYDLLRDDYIEKDRSRGIFFTQDWASLP 349
                        170
                 ....*....|.
gi 564813591 161 RCMPVASGGIH 171
Cdd:cd08212  350 GVMPVASGGIH 360
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
1-171 3.79e-80

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: 239.19  E-value: 3.79e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591    1 MRWRERFLNCMEGINRASAATGEVKGSYLNVTAATMEEVYKRSEYAKEVGSIIIMID-LVMGYTAIQSIALWARENDMLL 79
Cdd:pfam00016  58 MPWRDRFLFVAEAIDRAQDETGEAKGHYLNITADDMEEMYRRAEFAKETGGVAVMVDgLVIGPTAITTLRRWFRDNGVIL 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591   80 HLHRAGNSTYARQKNHGINFRVICKWMRMSGVDHIHAGTV-VGKLEGDPLmikgfyDTLRNTTLDVNLPYGLFFEMSWAS 158
Cdd:pfam00016 138 HYHRAGHGAVTRQSKHGISFRVLAKMARLAGADHLHTGTMgVGKLEGDPS------DTLRAYMLEEDRARGPFFDQDWGG 211
                         170
                  ....*....|...
gi 564813591  159 LRRCMPVASGGIH 171
Cdd:pfam00016 212 MPAVMPVASGGIH 224
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
1-171 6.91e-52

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


Pssm-ID: 441455  Cd Length: 417  Bit Score: 170.73  E-value: 6.91e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591   1 MRWRERFLNCMEGINRASAATGEVKGSYLNVTAaTMEEVYKRSEYAKEVGSIIIMID-LVMGYTAIQSIAlwARENDMLL 79
Cdd:COG1850  192 CPFEDRVRAVMEAIDRAEEETGEKKMYAFNITA-DTDEMLRRADLAVELGANAVMVDvNTVGLSAVQTLR--EEHIGLPI 268
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591  80 HLHRAGNSTYARQKNHGINFRVICKWMRMSGVDHIHAGTVVGKLEGDPLMIKGFYDTLRNttldvnlpyglffemSWASL 159
Cdd:COG1850  269 HAHRAGHGAFTRSPLHGISMRVLAKLWRLAGADHLHVGTPVGKMEGDDEEVLAIADALLQ---------------PWGGL 333
                        170
                 ....*....|..
gi 564813591 160 RRCMPVASGGIH 171
Cdd:COG1850  334 KPVFPVPSGGQH 345
rubisco_III TIGR03326
ribulose bisphosphate carboxylase, type III; Members of this protein family are the archaeal, ...
2-171 2.73e-30

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: 113.71  E-value: 2.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591    2 RWRERFLNCMEGINRASAATGEVKGSYLNVTAATMEEVyKRSEYAKEVGSIIIMIDLVM-GYTAIQSIALWARENDMLLH 80
Cdd:TIGR03326 189 RFEERVEKSLKVRDKVEAETGEKKSYLINITADVREME-RRAELVADLGGEYVMVDIVVaGWSALQYVRERTEDLGLAIH 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591   81 LHRAGNSTYARQKNHGINFRVICKWMRMSGVDHIHAGTV-VGKLEGDPLMIKGFYDTLRNttldvnlpyglffemSWASL 159
Cdd:TIGR03326 268 AHRAMHAAFTRNPKHGISMFVLAKLYRLIGVDQLHTGTAgVGKLEGGNEDTKGINDFLRQ---------------DWHHI 332
                         170
                  ....*....|..
gi 564813591  160 RRCMPVASGGIH 171
Cdd:TIGR03326 333 KPVFPVASGGLH 344
 
Name Accession Description Interval E-value
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
1-171 2.56e-124

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


Pssm-ID: 176981  Cd Length: 475  Bit Score: 357.86  E-value: 2.56e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591   1 MRWRERFLNCMEGINRASAATGEVKGSYLNVTAATMEEVYKRSEYAKEVGSIIIMIDLVM-GYTAIQSIALWARENDMLL 79
Cdd:CHL00040 212 MRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMYKRAVFARELGVPIVMHDYLTgGFTANTSLAHYCRDNGLLL 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591  80 HLHRAGNSTYARQKNHGINFRVICKWMRMSGVDHIHAGTVVGKLEGDPLMIKGFYDTLRNTTLDVNLPYGLFFEMSWASL 159
Cdd:CHL00040 292 HIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHAGTVVGKLEGEREMTLGFVDLLRDDFIEKDRSRGIYFTQDWVSL 371
                        170
                 ....*....|..
gi 564813591 160 RRCMPVASGGIH 171
Cdd:CHL00040 372 PGVLPVASGGIH 383
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
1-171 5.79e-117

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: 338.25  E-value: 5.79e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591   1 MRWRERFLNCMEGINRASAATGEVKGSYLNVTAATMEEVYKRSEYAKEVGSIIIMIDLVMGYTAIQSIALWARENDMLLH 80
Cdd:cd08212  190 MRWRDRFLFVAEAVNKAQAETGEVKGHYLNVTAGTMEEMYKRAEFAKELGSPIIMHDLLTGFTAIQSLAKWCRDNGMLLH 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591  81 LHRAGNSTYARQKNHGINFRVICKWMRMSGVDHIHAGTVVGKLEGDPLMIKGFYDTLRNTTLDVNLPYGLFFEMSWASLR 160
Cdd:cd08212  270 LHRAGHATYDRQKNHGIHFRVLAKWLRLSGVDHIHAGTVVGKLEGDPLVTLGFYDLLRDDYIEKDRSRGIFFTQDWASLP 349
                        170
                 ....*....|.
gi 564813591 161 RCMPVASGGIH 171
Cdd:cd08212  350 GVMPVASGGIH 360
rbcL PRK04208
ribulose bisophosphate carboxylase; Reviewed
1-171 5.15e-97

ribulose bisophosphate carboxylase; Reviewed


Pssm-ID: 179787  Cd Length: 468  Bit Score: 287.96  E-value: 5.15e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591   1 MRWRERFLNCMEGINRASAATGEVKGSYLNVTAATMEEVYKRSEYAKEVGSIIIMIDLVM-GYTAIQSIALWARENDMLL 79
Cdd:PRK04208 205 NRWRDRFLFVMEAIDKAEAETGERKGHYLNVTAPTMEEMYKRAEFAKELGSPIVMIDVVTaGWTALQSLREWCRDNGLAL 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591  80 HLHRAGNSTYARQKNHGINFRVICKWMRMSGVDHIHAGTVVGKLEGDPLMIKGFYDTLRNTTLDVNLPYGLFFEMSWASL 159
Cdd:PRK04208 285 HAHRAMHAAFTRNPNHGISFRVLAKLLRLIGVDHLHTGTVVGKLEGDRAEVLGYYDILREDFVPEDRSRGIFFDQDWGSI 364
                        170
                 ....*....|..
gi 564813591 160 RRCMPVASGGIH 171
Cdd:PRK04208 365 KPVFPVASGGIH 376
RuBisCO_large_I_II_III cd08206
Ribulose bisphosphate carboxylase large chain, Form I,II,III; Ribulose bisphosphate ...
1-171 4.29e-92

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: 273.73  E-value: 4.29e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591   1 MRWRERFLNCMEGINRASAATGEVKGSYLNVTAATMEEVYKRSEYAKEVGSIIIMIDLV-MGYTAIQSIALWARENDMLL 79
Cdd:cd08206  177 MRFEDRILFVAEAMDKAEAETGEAKGHYLNITADTPEEMIKRAEFAKELGSVIVMVDGVtAGWTAIQSARRWCPDNGLAL 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591  80 HLHRAGNSTYARQKNHGINFRVICKWMRMSGVDHIHAGTVVGKLEGDPLMIKGFYDTLRNTTLDVNLPYgLFFEMSWASL 159
Cdd:cd08206  257 HAHRAGHAAFTRQKNHGISMRVLAKLARLIGVDHIHTGTVVGKLEGDPSEVKGIADMLREDEVEGDLSR-IFFNQDWGGM 335
                        170
                 ....*....|..
gi 564813591 160 RRCMPVASGGIH 171
Cdd:cd08206  336 KPVFPVASGGLH 347
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
1-171 3.79e-80

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: 239.19  E-value: 3.79e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591    1 MRWRERFLNCMEGINRASAATGEVKGSYLNVTAATMEEVYKRSEYAKEVGSIIIMID-LVMGYTAIQSIALWARENDMLL 79
Cdd:pfam00016  58 MPWRDRFLFVAEAIDRAQDETGEAKGHYLNITADDMEEMYRRAEFAKETGGVAVMVDgLVIGPTAITTLRRWFRDNGVIL 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591   80 HLHRAGNSTYARQKNHGINFRVICKWMRMSGVDHIHAGTV-VGKLEGDPLmikgfyDTLRNTTLDVNLPYGLFFEMSWAS 158
Cdd:pfam00016 138 HYHRAGHGAVTRQSKHGISFRVLAKMARLAGADHLHTGTMgVGKLEGDPS------DTLRAYMLEEDRARGPFFDQDWGG 211
                         170
                  ....*....|...
gi 564813591  159 LRRCMPVASGGIH 171
Cdd:pfam00016 212 MPAVMPVASGGIH 224
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
1-171 6.91e-52

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


Pssm-ID: 441455  Cd Length: 417  Bit Score: 170.73  E-value: 6.91e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591   1 MRWRERFLNCMEGINRASAATGEVKGSYLNVTAaTMEEVYKRSEYAKEVGSIIIMID-LVMGYTAIQSIAlwARENDMLL 79
Cdd:COG1850  192 CPFEDRVRAVMEAIDRAEEETGEKKMYAFNITA-DTDEMLRRADLAVELGANAVMVDvNTVGLSAVQTLR--EEHIGLPI 268
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591  80 HLHRAGNSTYARQKNHGINFRVICKWMRMSGVDHIHAGTVVGKLEGDPLMIKGFYDTLRNttldvnlpyglffemSWASL 159
Cdd:COG1850  269 HAHRAGHGAFTRSPLHGISMRVLAKLWRLAGADHLHVGTPVGKMEGDDEEVLAIADALLQ---------------PWGGL 333
                        170
                 ....*....|..
gi 564813591 160 RRCMPVASGGIH 171
Cdd:COG1850  334 KPVFPVPSGGQH 345
RuBisCO_large cd08148
Ribulose bisphosphate carboxylase large chain; Ribulose bisphosphate carboxylase (Rubisco) ...
1-171 1.43e-46

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: 155.66  E-value: 1.43e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591   1 MRWRERFLNCMEGINRASAATGEVKGSYLNVTAATmEEVYKRSEYAKEVGSIIIMID-LVMGYTAIQSIALwARENDMLL 79
Cdd:cd08148  172 CPLRDRITEVAAALDRVQEETGEKKLYAVNVTAGT-FEIIERAERALELGANMLMVDvLTAGFSALQALAE-DFEIDLPI 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591  80 HLHRAGNSTYARQKNHGINFRVICKWMRMSGVDHIHAGTVVGKLEGDPLMIKGFYDTLRNttldvnlpyglffemSWASL 159
Cdd:cd08148  250 HVHRAMHGAVTRSKFHGISMLVLAKLLRMAGGDFIHTGTVVGKMALEREEALGIADALTD---------------DWAGF 314
                        170
                 ....*....|..
gi 564813591 160 RRCMPVASGGIH 171
Cdd:cd08148  315 KRVFPVASGGIH 326
RuBisCO_large_III cd08213
Ribulose bisphosphate carboxylase large chain, Form III; Ribulose bisphosphate carboxylase ...
2-171 1.25e-39

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: 138.29  E-value: 1.25e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591   2 RWRERFLNCMEGINRASAATGEVKGSYLNVTAATmEEVYKRSEYAKEVGSIIIMIDLVM-GYTAIQSIALWARENDMLLH 80
Cdd:cd08213  177 RFEERAKESLKARDKAEAETGERKAYLANITAPV-REMERRAELVADLGGKYVMIDVVVaGWSALQYLRDLAEDYGLAIH 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591  81 LHRAGNSTYARQKNHGINFRVICKWMRMSGVDHIHAGTVVGKLEGDPLMIKGFYDTLRNTTLdVNLPYGLFFEMSWASLR 160
Cdd:cd08213  256 AHRAMHAAFTRNPRHGISMLVLAKLYRLIGVDQLHIGTAVGKMEGDKEEVLRIADILREQKY-KPDEEDFHLAQDWGGIK 334
                        170
                 ....*....|.
gi 564813591 161 RCMPVASGGIH 171
Cdd:cd08213  335 PVFPVASGGLH 345
rubisco_III TIGR03326
ribulose bisphosphate carboxylase, type III; Members of this protein family are the archaeal, ...
2-171 2.73e-30

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: 113.71  E-value: 2.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591    2 RWRERFLNCMEGINRASAATGEVKGSYLNVTAATMEEVyKRSEYAKEVGSIIIMIDLVM-GYTAIQSIALWARENDMLLH 80
Cdd:TIGR03326 189 RFEERVEKSLKVRDKVEAETGEKKSYLINITADVREME-RRAELVADLGGEYVMVDIVVaGWSALQYVRERTEDLGLAIH 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591   81 LHRAGNSTYARQKNHGINFRVICKWMRMSGVDHIHAGTV-VGKLEGDPLMIKGFYDTLRNttldvnlpyglffemSWASL 159
Cdd:TIGR03326 268 AHRAMHAAFTRNPKHGISMFVLAKLYRLIGVDQLHTGTAgVGKLEGGNEDTKGINDFLRQ---------------DWHHI 332
                         170
                  ....*....|..
gi 564813591  160 RRCMPVASGGIH 171
Cdd:TIGR03326 333 KPVFPVASGGLH 344
RuBisCO_large_II cd08211
Ribulose bisphosphate carboxylase large chain, Form II; Ribulose bisphosphate carboxylase ...
12-170 1.89e-18

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: 81.39  E-value: 1.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591  12 EGINRASAATGEVKGSYLNVTAATMEEVYKRSEY-----AKEVGSIIIMID-LVMGYTAIQSialwAREN--DMLLHLHR 83
Cdd:cd08211  212 DAMRRAQDETGEAKLFSANITADDPDEMIARGEYileafGPNAGHVAFLVDgYVAGPAAVTT----ARRRfpDQFLHYHR 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591  84 AGNSTYARQKNH-GINFRVICKWMRMSGVDHIHAGTV-VGKLEGDplmikgfydtlrntTLDVNLPY--------GLFFE 153
Cdd:cd08211  288 AGHGAVTSPQSKrGYTAFVLSKMARLQGASGIHTGTMgFGKMEGE--------------SSDKVIAYmierdeaqGPLFN 353
                        170
                 ....*....|....*..
gi 564813591 154 MSWASLRRCMPVASGGI 170
Cdd:cd08211  354 QKWYGMKPTTPIISGGM 370
PRK13475 PRK13475
ribulose-bisphosphate carboxylase;
12-170 6.79e-18

ribulose-bisphosphate carboxylase;


Pssm-ID: 184072  Cd Length: 443  Bit Score: 79.77  E-value: 6.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591  12 EGINRASAATGEVKGSYLNVTAATMEEVYKRSEYAKEV-----GSIIIMID-LVMGYTAIQSialwAREN--DMLLHLHR 83
Cdd:PRK13475 213 DAMKRAQDETGEAKLFSANITADDHYEMIARGEYILETfgenaDHVAFLVDgYVAGPGAVTT----ARRQypDQYLHYHR 288
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591  84 AGNSTYARQKN-HGINFRVICKWMRMSGVDHIHAGTV-VGKLEGDPlmikgfydtlrnttLDVNLPYGL--------FFE 153
Cdd:PRK13475 289 AGHGAVTSPSSkRGYTAFVLSKMARLQGASGIHTGTMgYGKMEGEA--------------DDRVIAYMIerdsaqgpFYH 354
                        170
                 ....*....|....*..
gi 564813591 154 MSWASLRRCMPVASGGI 170
Cdd:PRK13475 355 QEWYGMKPTTPIISGGM 371
RuBisCO_IV_RLP cd08205
Ribulose bisphosphate carboxylase like proteins, Rubisco-Form IV; Ribulose bisphosphate ...
4-171 1.03e-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: 70.25  E-value: 1.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591   4 RERFLNCMEGINRASAATGEvKGSYL-NVTAATmEEVYKRSEYAKEVGSIIIMIDL-VMGYTAIQSIAlwaRENDMLLHL 81
Cdd:cd08205  178 EERVRACMEAVRRANEETGR-KTLYApNITGDP-DELRRRADRAVEAGANALLINPnLVGLDALRALA---EDPDLPIMA 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591  82 HRAGNSTYARQKNHGINFRVICKWMRMSGVDHIHAGTVVGKLEGDPLMIKGFYDTLRnttldvnlpyglffeMSWASLRR 161
Cdd:cd08205  253 HPAFAGALSRSPDYGSHFLLLGKLMRLAGADAVIFPGPGGRFPFSREECLAIARACR---------------RPLGGIKP 317
                        170
                 ....*....|
gi 564813591 162 CMPVASGGIH 171
Cdd:cd08205  318 ALPVPSGGMH 327
RLP_NonPhot cd08207
Ribulose bisphosphate carboxylase like proteins from nonphototrophic bacteria; Ribulose ...
4-169 7.04e-12

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: 62.33  E-value: 7.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591   4 RERFLNCMEGINRASAATGEvKGSY-LNVTAATmEEVYKRSEYAKEVGSIIIMIDL-VMGYTAIQSIAlwaRENDMLLHL 81
Cdd:cd08207  191 DERVRAVMRVINDHAQRTGR-KVMYaFNITDDI-DEMRRNHDLVVEAGGTCVMVSLnSVGLSGLAALR---RHSQLPIHG 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564813591  82 HRAGNSTYARQKNHGINFRVICKWMRMSGVDHIHAGTVVGKL-EGDPLMIKGFYDTLRnttldvnlPYglffemsWASLR 160
Cdd:cd08207  266 HRNGWGMLTRSPALGISFQAYQKLWRLAGVDHLHVNGLASKFwESDDSVIESARACLT--------PL-------GGPDD 330

                 ....*....
gi 564813591 161 RCMPVASGG 169
Cdd:cd08207  331 AAMPVFSSG 339
 
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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