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Conserved domains on  [gi|665767615|gb|AIF76282|]
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ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit, partial (chloroplast) [Galdieria sp. CJH-2014]

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) ...
 1-150 3.58e-103

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: 303.16  E-value: 3.58e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665767615   1 KASASTGEVKGHYLNVTAATMEEMYARANFAKELGSVIIMIDLVI-GYTAIQTMAKWARDNDMILHLHRAGNSTYSRQKN 79
Cdd:CHL00040 227 KAQAETGEIKGHYLNATAGTCEEMYKRAVFARELGVPIVMHDYLTgGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKN 306

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665767615  80 HGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPIITRGFYKTLLLPKLERNLQEGLFFDMEWASLRKVMPV 150
Cdd:CHL00040 307 HGIHFRVLAKALRMSGGDHIHAGTVVGKLEGEREMTLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPV 377
 
Name Accession Description Interval E-value
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
 1-150 3.58e-103

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


Pssm-ID: 176981  Cd Length: 475  Bit Score: 303.16  E-value: 3.58e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665767615   1 KASASTGEVKGHYLNVTAATMEEMYARANFAKELGSVIIMIDLVI-GYTAIQTMAKWARDNDMILHLHRAGNSTYSRQKN 79
Cdd:CHL00040 227 KAQAETGEIKGHYLNATAGTCEEMYKRAVFARELGVPIVMHDYLTgGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKN 306

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665767615  80 HGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPIITRGFYKTLLLPKLERNLQEGLFFDMEWASLRKVMPV 150
Cdd:CHL00040 307 HGIHFRVLAKALRMSGGDHIHAGTVVGKLEGEREMTLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPV 377
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
 1-150 3.88e-103

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: 302.04  E-value: 3.88e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665767615   1 KASASTGEVKGHYLNVTAATMEEMYARANFAKELGSVIIMIDLVIGYTAIQTMAKWARDNDMILHLHRAGNSTYSRQKNH 80
Cdd:cd08212  205 KAQAETGEVKGHYLNVTAGTMEEMYKRAEFAKELGSPIIMHDLLTGFTAIQSLAKWCRDNGMLLHLHRAGHATYDRQKNH 284

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665767615  81 GMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPIITRGFYKTLLLPKLERNLQEGLFFDMEWASLRKVMPV 150
Cdd:cd08212  285 GIHFRVLAKWLRLSGVDHIHAGTVVGKLEGDPLVTLGFYDLLRDDYIEKDRSRGIFFTQDWASLPGVMPV 354
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
 1-150 2.87e-73

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: 221.08  E-value: 2.87e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665767615    1 KASASTGEVKGHYLNVTAATMEEMYARANFAKELGSVIIMID-LVIGYTAIQTMAKWARDNDMILHLHRAGNSTYSRQKN 79
Cdd:pfam00016  73 RAQDETGEAKGHYLNITADDMEEMYRRAEFAKETGGVAVMVDgLVIGPTAITTLRRWFRDNGVILHYHRAGHGAVTRQSK 152

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665767615   80 HGMNFRVICKWMRMAGVDHIHAGTV-VGKLEGDPIITRGFYktlllpKLERNLQEGLFFDMEWASLRKVMPV 150
Cdd:pfam00016 153 HGISFRVLAKMARLAGADHLHTGTMgVGKLEGDPSDTLRAY------MLEEDRARGPFFDQDWGGMPAVMPV 218
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
 1-150 5.68e-48

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


Pssm-ID: 441455  Cd Length: 417  Bit Score: 159.56  E-value: 5.68e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665767615   1 KASASTGEVKGHYLNVTAaTMEEMYARANFAKELGSVIIMID-LVIGYTAIQTMAKwaRDNDMILHLHRAGNSTYSRQKN 79
Cdd:COG1850  207 RAEEETGEKKMYAFNITA-DTDEMLRRADLAVELGANAVMVDvNTVGLSAVQTLRE--EHIGLPIHAHRAGHGAFTRSPL 283

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665767615  80 HGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPIITRGFYKTLLLPklernlqeglffdmeWASLRKVMPV 150
Cdd:COG1850  284 HGISMRVLAKLWRLAGADHLHVGTPVGKMEGDDEEVLAIADALLQP---------------WGGLKPVFPV 339
 
Name Accession Description Interval E-value
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
 1-150 3.58e-103

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


Pssm-ID: 176981  Cd Length: 475  Bit Score: 303.16  E-value: 3.58e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665767615   1 KASASTGEVKGHYLNVTAATMEEMYARANFAKELGSVIIMIDLVI-GYTAIQTMAKWARDNDMILHLHRAGNSTYSRQKN 79
Cdd:CHL00040 227 KAQAETGEIKGHYLNATAGTCEEMYKRAVFARELGVPIVMHDYLTgGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKN 306

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665767615  80 HGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPIITRGFYKTLLLPKLERNLQEGLFFDMEWASLRKVMPV 150
Cdd:CHL00040 307 HGIHFRVLAKALRMSGGDHIHAGTVVGKLEGEREMTLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPV 377
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
 1-150 3.88e-103

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: 302.04  E-value: 3.88e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665767615   1 KASASTGEVKGHYLNVTAATMEEMYARANFAKELGSVIIMIDLVIGYTAIQTMAKWARDNDMILHLHRAGNSTYSRQKNH 80
Cdd:cd08212  205 KAQAETGEVKGHYLNVTAGTMEEMYKRAEFAKELGSPIIMHDLLTGFTAIQSLAKWCRDNGMLLHLHRAGHATYDRQKNH 284

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665767615  81 GMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPIITRGFYKTLLLPKLERNLQEGLFFDMEWASLRKVMPV 150
Cdd:cd08212  285 GIHFRVLAKWLRLSGVDHIHAGTVVGKLEGDPLVTLGFYDLLRDDYIEKDRSRGIFFTQDWASLPGVMPV 354
rbcL PRK04208
ribulose bisophosphate carboxylase; Reviewed
 1-150 1.08e-87

ribulose bisophosphate carboxylase; Reviewed


Pssm-ID: 179787  Cd Length: 468  Bit Score: 263.31  E-value: 1.08e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665767615   1 KASASTGEVKGHYLNVTAATMEEMYARANFAKELGSVIIMIDLVI-GYTAIQTMAKWARDNDMILHLHRAGNSTYSRQKN 79
Cdd:PRK04208 220 KAEAETGERKGHYLNVTAPTMEEMYKRAEFAKELGSPIVMIDVVTaGWTALQSLREWCRDNGLALHAHRAMHAAFTRNPN 299

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665767615  80 HGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPIITRGFYKTLLLPKLERNLQEGLFFDMEWASLRKVMPV 150
Cdd:PRK04208 300 HGISFRVLAKLLRLIGVDHLHTGTVVGKLEGDRAEVLGYYDILREDFVPEDRSRGIFFDQDWGSIKPVFPV 370
RuBisCO_large_I_II_III cd08206
Ribulose bisphosphate carboxylase large chain, Form I,II,III; Ribulose bisphosphate ...
 1-150 9.98e-82

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: 246.38  E-value: 9.98e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665767615   1 KASASTGEVKGHYLNVTAATMEEMYARANFAKELGSVIIMIDLVI-GYTAIQTMAKWARDNDMILHLHRAGNSTYSRQKN 79
Cdd:cd08206  192 KAEAETGEAKGHYLNITADTPEEMIKRAEFAKELGSVIVMVDGVTaGWTAIQSARRWCPDNGLALHAHRAGHAAFTRQKN 271

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665767615  80 HGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPIITRGFYKTLLLPKLERNLQEgLFFDMEWASLRKVMPV 150
Cdd:cd08206  272 HGISMRVLAKLARLIGVDHIHTGTVVGKLEGDPSEVKGIADMLREDEVEGDLSR-IFFNQDWGGMKPVFPV 341
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
 1-150 2.87e-73

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: 221.08  E-value: 2.87e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665767615    1 KASASTGEVKGHYLNVTAATMEEMYARANFAKELGSVIIMID-LVIGYTAIQTMAKWARDNDMILHLHRAGNSTYSRQKN 79
Cdd:pfam00016  73 RAQDETGEAKGHYLNITADDMEEMYRRAEFAKETGGVAVMVDgLVIGPTAITTLRRWFRDNGVILHYHRAGHGAVTRQSK 152

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665767615   80 HGMNFRVICKWMRMAGVDHIHAGTV-VGKLEGDPIITRGFYktlllpKLERNLQEGLFFDMEWASLRKVMPV 150
Cdd:pfam00016 153 HGISFRVLAKMARLAGADHLHTGTMgVGKLEGDPSDTLRAY------MLEEDRARGPFFDQDWGGMPAVMPV 218
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
 1-150 5.68e-48

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


Pssm-ID: 441455  Cd Length: 417  Bit Score: 159.56  E-value: 5.68e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665767615   1 KASASTGEVKGHYLNVTAaTMEEMYARANFAKELGSVIIMID-LVIGYTAIQTMAKwaRDNDMILHLHRAGNSTYSRQKN 79
Cdd:COG1850  207 RAEEETGEKKMYAFNITA-DTDEMLRRADLAVELGANAVMVDvNTVGLSAVQTLRE--EHIGLPIHAHRAGHGAFTRSPL 283

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665767615  80 HGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPIITRGFYKTLLLPklernlqeglffdmeWASLRKVMPV 150
Cdd:COG1850  284 HGISMRVLAKLWRLAGADHLHVGTPVGKMEGDDEEVLAIADALLQP---------------WGGLKPVFPV 339
RuBisCO_large_III cd08213
Ribulose bisphosphate carboxylase large chain, Form III; Ribulose bisphosphate carboxylase ...
 1-150 7.04e-36

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: 127.89  E-value: 7.04e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665767615   1 KASASTGEVKGHYLNVTAATmEEMYARANFAKELGSVIIMIDLVI-GYTAIQTMAKWARDNDMILHLHRAGNSTYSRQKN 79
Cdd:cd08213  191 KAEAETGERKAYLANITAPV-REMERRAELVADLGGKYVMIDVVVaGWSALQYLRDLAEDYGLAIHAHRAMHAAFTRNPR 269

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665767615  80 HGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPIITRGFYKTLLLPKLERNlQEGLFFDMEWASLRKVMPV 150
Cdd:cd08213  270 HGISMLVLAKLYRLIGVDQLHIGTAVGKMEGDKEEVLRIADILREQKYKPD-EEDFHLAQDWGGIKPVFPV 339
RuBisCO_large cd08148
Ribulose bisphosphate carboxylase large chain; Ribulose bisphosphate carboxylase (Rubisco) ...
 1-150 2.01e-35

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: 125.62  E-value: 2.01e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665767615   1 KASASTGEVKGHYLNVTAATmEEMYARANFAKELGSVIIMID-LVIGYTAIQTMAKWARdNDMILHLHRAGNSTYSRQKN 79
Cdd:cd08148  187 RVQEETGEKKLYAVNVTAGT-FEIIERAERALELGANMLMVDvLTAGFSALQALAEDFE-IDLPIHVHRAMHGAVTRSKF 264

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665767615  80 HGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPIITRGFYKTLLLPklernlqeglffdmeWASLRKVMPV 150
Cdd:cd08148  265 HGISMLVLAKLLRMAGGDFIHTGTVVGKMALEREEALGIADALTDD---------------WAGFKRVFPV 320
RuBisCO_large_II cd08211
Ribulose bisphosphate carboxylase large chain, Form II; Ribulose bisphosphate carboxylase ...
 1-150 7.94e-21

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: 87.17  E-value: 7.94e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665767615   1 KASASTGEVKGHYLNVTAATMEEMYARAN-----FAKELGSVIIMID-LVIGYTAIQTmakwARDN--DMILHLHRAGNS 72
Cdd:cd08211  216 RAQDETGEAKLFSANITADDPDEMIARGEyileaFGPNAGHVAFLVDgYVAGPAAVTT----ARRRfpDQFLHYHRAGHG 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665767615  73 TYSRQKNH-GMNFRVICKWMRMAGVDHIHAGTV-VGKLEGDPIITRGFYktlllpKLERNLQEGLFFDMEWASLRKVMPV 150
Cdd:cd08211  292 AVTSPQSKrGYTAFVLSKMARLQGASGIHTGTMgFGKMEGESSDKVIAY------MIERDEAQGPLFNQKWYGMKPTTPI 365
PRK13475 PRK13475
ribulose-bisphosphate carboxylase;
1-150 5.76e-20

ribulose-bisphosphate carboxylase;


Pssm-ID: 184072  Cd Length: 443  Bit Score: 84.77  E-value: 5.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665767615   1 KASASTGEVKGHYLNVTAATMEEMYARAN-----FAKELGSVIIMIDlviGYTAIQTMAKWARDN--DMILHLHRAGNST 73
Cdd:PRK13475 217 RAQDETGEAKLFSANITADDHYEMIARGEyiletFGENADHVAFLVD---GYVAGPGAVTTARRQypDQYLHYHRAGHGA 293

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665767615  74 YSRQKN-HGMNFRVICKWMRMAGVDHIHAGTV-VGKLEGDPIITRGFYktlllpKLERNLQEGLFFDMEWASLRKVMPV 150
Cdd:PRK13475 294 VTSPSSkRGYTAFVLSKMARLQGASGIHTGTMgYGKMEGEADDRVIAY------MIERDSAQGPFYHQEWYGMKPTTPI 366
RuBisCO_IV_RLP cd08205
Ribulose bisphosphate carboxylase like proteins, Rubisco-Form IV; Ribulose bisphosphate ...
 1-108 1.06e-11

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: 1.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665767615   1 KASASTGEVKGHYLNVTAATmEEMYARANFAKELGSVIIMIDL-VIGYTAIQTMAkwaRDNDMILHLHRAGNSTYSRQKN 79
Cdd:cd08205  190 RANEETGRKTLYAPNITGDP-DELRRRADRAVEAGANALLINPnLVGLDALRALA---EDPDLPIMAHPAFAGALSRSPD 265

                         90       100
                 ....*....|....*....|....*....
gi 665767615  80 HGMNFRVICKWMRMAGVDHIHAGTVVGKL 108
Cdd:cd08205  266 YGSHFLLLGKLMRLAGADAVIFPGPGGRF 294
RLP_NonPhot cd08207
Ribulose bisphosphate carboxylase like proteins from nonphototrophic bacteria; Ribulose ...
 15-119 3.43e-11

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: 59.63  E-value: 3.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665767615  15 NVTAATmEEMYARANFAKELGSVIIMIDL-VIGYTAIQTMAKWArdnDMILHLHRAGNSTYSRQKNHGMNFRVICKWMRM 93
Cdd:cd08207  217 NITDDI-DEMRRNHDLVVEAGGTCVMVSLnSVGLSGLAALRRHS---QLPIHGHRNGWGMLTRSPALGISFQAYQKLWRL 292

                         90       100
                 ....*....|....*....|....*..
gi 665767615  94 AGVDHIHAGTVVGKL-EGDPIITRGFY 119
Cdd:cd08207  293 AGVDHLHVNGLASKFwESDDSVIESAR 319
 
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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