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Conserved domains on  [gi|322511694|gb|ADX05616|]
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ribulose-1,5-bisphosphate carboxylase/oxygenase form II, partial [gamma proteobacterium SCGC AAA001-E15]

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) ...
 1-108 2.75e-82

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 PRK13475:

Pssm-ID: 471793  Cd Length: 443  Bit Score: 246.94  E-value: 2.75e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322511694   1 FWLGGDFIKNDEPQGNQVYARIKDVTPLVADSMRRAQDETGEAKLFSANITADDHHEMCARADYILETFAENAHHVAFLV 80
Cdd:PRK13475 183 FWLGGDFIKNDEPQGNQVFAPLKKTVPLVADAMKRAQDETGEAKLFSANITADDHYEMIARGEYILETFGENADHVAFLV 262

                         90       100
                 ....*....|....*....|....*...
gi 322511694  81 DGYVGGPGMVTTARRNYPNQYLHYHRAG 108
Cdd:PRK13475 263 DGYVAGPGAVTTARRQYPDQYLHYHRAG 290
 
Name Accession Description Interval E-value
PRK13475 PRK13475
ribulose-bisphosphate carboxylase;
1-108 2.75e-82

ribulose-bisphosphate carboxylase;


Pssm-ID: 184072  Cd Length: 443  Bit Score: 246.94  E-value: 2.75e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322511694   1 FWLGGDFIKNDEPQGNQVYARIKDVTPLVADSMRRAQDETGEAKLFSANITADDHHEMCARADYILETFAENAHHVAFLV 80
Cdd:PRK13475 183 FWLGGDFIKNDEPQGNQVFAPLKKTVPLVADAMKRAQDETGEAKLFSANITADDHYEMIARGEYILETFGENADHVAFLV 262

                         90       100
                 ....*....|....*....|....*...
gi 322511694  81 DGYVGGPGMVTTARRNYPNQYLHYHRAG 108
Cdd:PRK13475 263 DGYVAGPGAVTTARRQYPDQYLHYHRAG 290
RuBisCO_large_II cd08211
Ribulose bisphosphate carboxylase large chain, Form II; Ribulose bisphosphate carboxylase ...
 1-108 1.90e-68

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: 211.21  E-value: 1.90e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322511694   1 FWLGGDFIKNDEPQGNQVYARIKDVTPLVADSMRRAQDETGEAKLFSANITADDHHEMCARADYILETFAENAHHVAFLV 80
Cdd:cd08211  182 FWLGGDFIKNDEPQANQPFCPLKKVIPLVADAMRRAQDETGEAKLFSANITADDPDEMIARGEYILEAFGPNAGHVAFLV 261

                         90       100
                 ....*....|....*....|....*...
gi 322511694  81 DGYVGGPGMVTTARRNYPNQYLHYHRAG 108
Cdd:cd08211  262 DGYVAGPAAVTTARRRFPDQFLHYHRAG 289
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
 1-108 4.97e-49

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: 157.14  E-value: 4.97e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322511694    1 FWLGG-DFIKNDEPQGNQVYARIKDVTPLVADSMRRAQDETGEAKLFSANITADDHHEMCARADYILETFAEnahhvAFL 79
Cdd:pfam00016  38 FLLGGlDFIKDDENINSQPFMPWRDRFLFVAEAIDRAQDETGEAKGHYLNITADDMEEMYRRAEFAKETGGV-----AVM 112

                          90       100       110
                  ....*....|....*....|....*....|.
gi 322511694   80 VDGYVGGPGMVTTARRNYPNQ--YLHYHRAG 108
Cdd:pfam00016 113 VDGLVIGPTAITTLRRWFRDNgvILHYHRAG 143
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
 1-108 4.37e-37

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


Pssm-ID: 441455  Cd Length: 417  Bit Score: 129.13  E-value: 4.37e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322511694   1 FWLGG-DFIKNDEPQGNQVYARIKDVTPLVADSMRRAQDETGEAKLFSANITaDDHHEMCARADYILETFAEnahhvAFL 79
Cdd:COG1850  172 LALGGvDFIKDDENLADQPFCPFEDRVRAVMEAIDRAEEETGEKKMYAFNIT-ADTDEMLRRADLAVELGAN-----AVM 245

                         90       100
                 ....*....|....*....|....*....
gi 322511694  80 VDGYVGGPGMVTTARRNYPNQYLHYHRAG 108
Cdd:COG1850  246 VDVNTVGLSAVQTLREEHIGLPIHAHRAG 274
 
Name Accession Description Interval E-value
PRK13475 PRK13475
ribulose-bisphosphate carboxylase;
1-108 2.75e-82

ribulose-bisphosphate carboxylase;


Pssm-ID: 184072  Cd Length: 443  Bit Score: 246.94  E-value: 2.75e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322511694   1 FWLGGDFIKNDEPQGNQVYARIKDVTPLVADSMRRAQDETGEAKLFSANITADDHHEMCARADYILETFAENAHHVAFLV 80
Cdd:PRK13475 183 FWLGGDFIKNDEPQGNQVFAPLKKTVPLVADAMKRAQDETGEAKLFSANITADDHYEMIARGEYILETFGENADHVAFLV 262

                         90       100
                 ....*....|....*....|....*...
gi 322511694  81 DGYVGGPGMVTTARRNYPNQYLHYHRAG 108
Cdd:PRK13475 263 DGYVAGPGAVTTARRQYPDQYLHYHRAG 290
RuBisCO_large_II cd08211
Ribulose bisphosphate carboxylase large chain, Form II; Ribulose bisphosphate carboxylase ...
 1-108 1.90e-68

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: 211.21  E-value: 1.90e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322511694   1 FWLGGDFIKNDEPQGNQVYARIKDVTPLVADSMRRAQDETGEAKLFSANITADDHHEMCARADYILETFAENAHHVAFLV 80
Cdd:cd08211  182 FWLGGDFIKNDEPQANQPFCPLKKVIPLVADAMRRAQDETGEAKLFSANITADDPDEMIARGEYILEAFGPNAGHVAFLV 261

                         90       100
                 ....*....|....*....|....*...
gi 322511694  81 DGYVGGPGMVTTARRNYPNQYLHYHRAG 108
Cdd:cd08211  262 DGYVAGPAAVTTARRRFPDQFLHYHRAG 289
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
 1-108 4.97e-49

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: 157.14  E-value: 4.97e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322511694    1 FWLGG-DFIKNDEPQGNQVYARIKDVTPLVADSMRRAQDETGEAKLFSANITADDHHEMCARADYILETFAEnahhvAFL 79
Cdd:pfam00016  38 FLLGGlDFIKDDENINSQPFMPWRDRFLFVAEAIDRAQDETGEAKGHYLNITADDMEEMYRRAEFAKETGGV-----AVM 112

                          90       100       110
                  ....*....|....*....|....*....|.
gi 322511694   80 VDGYVGGPGMVTTARRNYPNQ--YLHYHRAG 108
Cdd:pfam00016 113 VDGLVIGPTAITTLRRWFRDNgvILHYHRAG 143
RuBisCO_large_I_II_III cd08206
Ribulose bisphosphate carboxylase large chain, Form I,II,III; Ribulose bisphosphate ...
 1-108 1.24e-46

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: 153.93  E-value: 1.24e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322511694   1 FWLGG-DFIKNDEPQGNQVYARIKDVTPLVADSMRRAQDETGEAKLFSANITADDHHEMCARADYILETFaenahHVAFL 79
Cdd:cd08206  157 ALRGGlDFVKDDENQNSQPFMRFEDRILFVAEAMDKAEAETGEAKGHYLNITADTPEEMIKRAEFAKELG-----SVIVM 231

                         90       100       110
                 ....*....|....*....|....*....|.
gi 322511694  80 VDGYVGGPGMVTTARRNYPN--QYLHYHRAG 108
Cdd:cd08206  232 VDGVTAGWTAIQSARRWCPDngLALHAHRAG 262
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
 1-108 4.37e-37

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


Pssm-ID: 441455  Cd Length: 417  Bit Score: 129.13  E-value: 4.37e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322511694   1 FWLGG-DFIKNDEPQGNQVYARIKDVTPLVADSMRRAQDETGEAKLFSANITaDDHHEMCARADYILETFAEnahhvAFL 79
Cdd:COG1850  172 LALGGvDFIKDDENLADQPFCPFEDRVRAVMEAIDRAEEETGEKKMYAFNIT-ADTDEMLRRADLAVELGAN-----AVM 245

                         90       100
                 ....*....|....*....|....*....
gi 322511694  80 VDGYVGGPGMVTTARRNYPNQYLHYHRAG 108
Cdd:COG1850  246 VDVNTVGLSAVQTLREEHIGLPIHAHRAG 274
RuBisCO_large cd08148
Ribulose bisphosphate carboxylase large chain; Ribulose bisphosphate carboxylase (Rubisco) ...
 1-108 1.74e-27

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: 102.89  E-value: 1.74e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322511694   1 FWLGG-DFIKNDEPQGNQVYARIKDVTPLVADSMRRAQDETGEAKLFSANITADDhHEMCARADYILETFaenahHVAFL 79
Cdd:cd08148  152 AALGGlDLIKDDETLTDQPFCPLRDRITEVAAALDRVQEETGEKKLYAVNVTAGT-FEIIERAERALELG-----ANMLM 225

                         90       100       110
                 ....*....|....*....|....*....|
gi 322511694  80 VDGYVGGPGMVTTARRNYPNQ-YLHYHRAG 108
Cdd:cd08148  226 VDVLTAGFSALQALAEDFEIDlPIHVHRAM 255
RuBisCO_IV_RLP cd08205
Ribulose bisphosphate carboxylase like proteins, Rubisco-Form IV; Ribulose bisphosphate ...
 1-108 2.67e-12

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: 61.01  E-value: 2.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322511694   1 FWLGG-DFIKNDEPQGNQVYARIKDVTPLVADSMRRAQDETGEAKLFSANITADDhHEMCARADYILETFAEnahhvAFL 79
Cdd:cd08205  155 LALGGiDLIKDDELLADQPYAPFEERVRACMEAVRRANEETGRKTLYAPNITGDP-DELRRRADRAVEAGAN-----ALL 228

                         90       100
                 ....*....|....*....|....*....
gi 322511694  80 VDGYVGGPGMVTTARRNyPNQYLHYHRAG 108
Cdd:cd08205  229 INPNLVGLDALRALAED-PDLPIMAHPAF 256
rbcL PRK04208
ribulose bisophosphate carboxylase; Reviewed
 2-108 4.46e-12

ribulose bisophosphate carboxylase; Reviewed


Pssm-ID: 179787  Cd Length: 468  Bit Score: 60.69  E-value: 4.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322511694   2 WLGG-DFIKNDEPQGNQVYARIKDVTPLVADSMRRAQDETGEAKLFSANITADDHHEMCARADYILETFAENAHHvAFLV 80
Cdd:PRK04208 186 LRGGlDFTKDDENLNSQPFNRWRDRFLFVMEAIDKAEAETGERKGHYLNVTAPTMEEMYKRAEFAKELGSPIVMI-DVVT 264

                         90       100
                 ....*....|....*....|....*...
gi 322511694  81 DGYVGGPGMVTTARRNypNQYLHYHRAG 108
Cdd:PRK04208 265 AGWTALQSLREWCRDN--GLALHAHRAM 290
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
 4-108 9.03e-11

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


Pssm-ID: 176981  Cd Length: 475  Bit Score: 57.02  E-value: 9.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322511694   4 GGDFIKNDEPQGNQVYARIKDVTPLVADSMRRAQDETGEAKLFSANITADDHHEMCARADYILETFAENAHHvAFLVDGY 83
Cdd:CHL00040 196 GLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMYKRAVFARELGVPIVMH-DYLTGGF 274

                         90       100
                 ....*....|....*....|....*
gi 322511694  84 VGGPGMVTTARRNypNQYLHYHRAG 108
Cdd:CHL00040 275 TANTSLAHYCRDN--GLLLHIHRAM 297
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
 4-108 1.01e-10

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: 56.66  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322511694   4 GGDFIKNDEPQGNQVYARIKDVTPLVADSMRRAQDETGEAKLFSANITADDHHEMCARADyiletFAENAHHVAFLVD-- 81
Cdd:cd08212  174 GLDFTKDDENINSQPFMRWRDRFLFVAEAVNKAQAETGEVKGHYLNVTAGTMEEMYKRAE-----FAKELGSPIIMHDll 248

                         90       100
                 ....*....|....*....|....*...
gi 322511694  82 -GYVGGPGMVTTARRNypNQYLHYHRAG 108
Cdd:cd08212  249 tGFTAIQSLAKWCRDN--GMLLHLHRAG 274
RuBisCO_large_III cd08213
Ribulose bisphosphate carboxylase large chain, Form III; Ribulose bisphosphate carboxylase ...
 2-107 2.18e-09

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: 53.16  E-value: 2.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322511694   2 WLGG-DFIKNDEPQGNQVYARIKDVTPLVADSMRRAQDETGEAKLFSANITAdDHHEMCARADYILEtfaENAHHVafLV 80
Cdd:cd08213  157 LVGGvDLVKDDENLTSQPFNRFEERAKESLKARDKAEAETGERKAYLANITA-PVREMERRAELVAD---LGGKYV--MI 230

                         90       100       110
                 ....*....|....*....|....*....|
gi 322511694  81 DGYVGGPGMVTTArRNYPNQY---LHYHRA 107
Cdd:cd08213  231 DVVVAGWSALQYL-RDLAEDYglaIHAHRA 259
RLP_RrRLP cd08210
Ribulose bisphosphate carboxylase like proteins (RLPs) similar to R.rubrum RLP; RLP from ...
 1-98 1.81e-07

Ribulose bisphosphate carboxylase like proteins (RLPs) similar to R.rubrum RLP; RLP from Rhodospirillum rubrum plays a role in an uncharacterized sulfur salvage pathway and has been shown to catalyze a novel isomerization reaction that converts 5-methylthio-d-ribulose 1-phosphate to a 3:1 mixture of 1-methylthioxylulose 5-phosphate and 1-methylthioribulose 5-phosphate.


Pssm-ID: 173975  Cd Length: 364  Bit Score: 47.62  E-value: 1.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 322511694   1 FWLGG-DFIKNDEPQGNQVYARIKDVTPLVADSMRRAQDETGEAKLFSANITAdDHHEMCARADyiletFAENAHHVAFL 79
Cdd:cd08210  150 FALGGiDIIKDDHGLADQPFAPFEERVKACQEAVAEANAETGGRTLYAPNVTG-PPTQLLERAR-----FAKEAGAGGVL 223

                         90
                 ....*....|....*....
gi 322511694  80 VDGYVGGPGMVTTARRNYP 98
Cdd:cd08210  224 IAPGLTGLDTFRELAEDFD 242
RLP_Photo cd08208
Ribulose bisphosphate carboxylase like proteins from phototrophic bacteria; Ribulose ...
 2-51 1.58e-05

Ribulose bisphosphate carboxylase like proteins from phototrophic 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: 173973  Cd Length: 424  Bit Score: 42.19  E-value: 1.58e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 322511694   2 WLGG-DFIKNDEPQGNQVYARIKDVTPLVADSMRRAQDETGEAKLFSANIT 51
Cdd:cd08208  186 WLGGlDIAKDDEMLADVDWCPLEERAALLGKARRRAEAETGVPKIYLANIT 236
 
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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