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Conserved domains on  [gi|1913595456|gb|QOH28388|]
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ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit, partial (chloroplast) [Turbinaria tricostata]

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) ...
 1-165 3.29e-118

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: 342.45  E-value: 3.29e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456   1 FRVICKWMRMSGVDHIHAGTVVGKLEGDPLMVRGFYNTLLLTELKINLAEGLFFDMDWASLRKCVPVASGGIHCGQMHQL 80
Cdd:CHL00040  311 FRVLAKALRMSGGDHIHAGTVVGKLEGEREMTLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPAL 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456  81 LYYLGDDVVLQFGGGTIGHPDGIQAGATANRVALEAMVLARNEGRDYVGEGPEILRTAASTCGPLKAALDLWKDITFEYT 160
Cdd:CHL00040  391 TEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEIIREAAKWSPELAAACEVWKEIKFEFE 470


                  ....*
gi 1913595456 161 STDTP 165
Cdd:CHL00040  471 TTDTL 475
 
Name Accession Description Interval E-value
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
 1-165 3.29e-118

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


Pssm-ID: 176981  Cd Length: 475  Bit Score: 342.45  E-value: 3.29e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456   1 FRVICKWMRMSGVDHIHAGTVVGKLEGDPLMVRGFYNTLLLTELKINLAEGLFFDMDWASLRKCVPVASGGIHCGQMHQL 80
Cdd:CHL00040  311 FRVLAKALRMSGGDHIHAGTVVGKLEGEREMTLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPAL 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456  81 LYYLGDDVVLQFGGGTIGHPDGIQAGATANRVALEAMVLARNEGRDYVGEGPEILRTAASTCGPLKAALDLWKDITFEYT 160
Cdd:CHL00040  391 TEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEIIREAAKWSPELAAACEVWKEIKFEFE 470


                  ....*
gi 1913595456 161 STDTP 165
Cdd:CHL00040  471 TTDTL 475
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
 1-163 5.29e-109

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: 318.21  E-value: 5.29e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456   1 FRVICKWMRMSGVDHIHAGTVVGKLEGDPLMVRGFYNTLLLTELKINLAEGLFFDMDWASLRKCVPVASGGIHCGQMHQL 80
Cdd:cd08212   288 FRVLAKWLRLSGVDHIHAGTVVGKLEGDPLVTLGFYDLLRDDYIEKDRSRGIFFTQDWASLPGVMPVASGGIHVGQMHQL 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456  81 LYYLGDDVVLQFGGGTIGHPDGIQAGATANRVALEAMVLARNEGRDYVGEGPEILRTAASTCGPLKAALDLWKDITFEYT 160
Cdd:cd08212   368 IEIFGDDVVLQFGGGTIGHPWGIAAGATANRVALEAMVQARNEGRDLAREGPEILREAAKWSPELAAALETWKDIKFEFE 447


                  ...
gi 1913595456 161 STD 163
Cdd:cd08212   448 STD 450
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
 1-152 8.43e-59

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: 185.26  E-value: 8.43e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456   1 FRVICKWMRMSGVDHIHAGTV-VGKLEGDPLmvrgfyNTLLLTELKINLAEGLFFDMDWASLRKCVPVASGGIHCGQMHQ 79
Cdd:pfam00016 157 FRVLAKMARLAGADHLHTGTMgVGKLEGDPS------DTLRAYMLEEDRARGPFFDQDWGGMPAVMPVASGGIHAGQMPG 230

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1913595456  80 LLYYLGD-DVVLQFGGGTIGHPDGIQAGATANRVALEAMVlarnEGRDYVGEgpeilrtaASTCGPLKAALDLW 152
Cdd:pfam00016 231 LFDNLGDsDVILQFGGGTFGHPDGPAAGAKANRQALEAWV----EGRDLEEY--------AKEHPELARAFESW 292
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
 1-157 9.01e-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: 159.95  E-value: 9.01e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456   1 FRVICKWMRMSGVDHIHAGTVVGKLEGDPLMVRGFYNTLLLtelkinlaeglffdmDWASLRKCVPVASGGIHCGQMHQL 80
Cdd:COG1850   288 MRVLAKLWRLAGADHLHVGTPVGKMEGDDEEVLAIADALLQ---------------PWGGLKPVFPVPSGGQHPGQVPEL 352

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1913595456  81 LYYLGDDVVLQFGGGTIGHPDGIQAGATANRVALEAMVLARNegrdyvgegpeiLRTAASTCGPLKAALDLWKDITF 157
Cdd:COG1850   353 YDALGTDLILQAGGGIHGHPDGPAAGARALRQAWEAAVAGIP------------LEEYAKTHPELAAALEKWGKKAP 417
salvage_mtnW TIGR03332
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Members of this family are the methionine ...
 57-152 5.22e-10

2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Members of this family are the methionine salvage pathway enzyme 2,3-diketo-5-methylthiopentyl-1-phosphate enolase, a homolog of RuBisCO. This protein family seems restricted to Bacillus subtilis and close relatives, where two separate proteins carry the enolase and phosphatase activities that in other species occur in a single protein, MtnC (TIGR01691). [Amino acid biosynthesis, Aspartate family, Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 132375  Cd Length: 407  Bit Score: 57.15  E-value: 5.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456  57 DWASLRKCVPVASGGIHCGQMHQLLYYLGDDVVLQFGGGTIGHPDGIQAGATANRVALEAMVLARNegrdyvgegpeiLR 136
Cdd:TIGR03332 323 DDAPFKKTFAVPSAGIHPGMVPLIMRDFGIDHIINAGGGIHGHPNGAQGGGRAFRAAIDAVLEAKP------------LH 390

                          90
                  ....*....|....*.
gi 1913595456 137 TAASTCGPLKAALDLW 152
Cdd:TIGR03332 391 EKAADDIDLKLALDKW 406
 
Name Accession Description Interval E-value
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
 1-165 3.29e-118

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


Pssm-ID: 176981  Cd Length: 475  Bit Score: 342.45  E-value: 3.29e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456   1 FRVICKWMRMSGVDHIHAGTVVGKLEGDPLMVRGFYNTLLLTELKINLAEGLFFDMDWASLRKCVPVASGGIHCGQMHQL 80
Cdd:CHL00040  311 FRVLAKALRMSGGDHIHAGTVVGKLEGEREMTLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPAL 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456  81 LYYLGDDVVLQFGGGTIGHPDGIQAGATANRVALEAMVLARNEGRDYVGEGPEILRTAASTCGPLKAALDLWKDITFEYT 160
Cdd:CHL00040  391 TEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEIIREAAKWSPELAAACEVWKEIKFEFE 470


                  ....*
gi 1913595456 161 STDTP 165
Cdd:CHL00040  471 TTDTL 475
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
 1-163 5.29e-109

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: 318.21  E-value: 5.29e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456   1 FRVICKWMRMSGVDHIHAGTVVGKLEGDPLMVRGFYNTLLLTELKINLAEGLFFDMDWASLRKCVPVASGGIHCGQMHQL 80
Cdd:cd08212   288 FRVLAKWLRLSGVDHIHAGTVVGKLEGDPLVTLGFYDLLRDDYIEKDRSRGIFFTQDWASLPGVMPVASGGIHVGQMHQL 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456  81 LYYLGDDVVLQFGGGTIGHPDGIQAGATANRVALEAMVLARNEGRDYVGEGPEILRTAASTCGPLKAALDLWKDITFEYT 160
Cdd:cd08212   368 IEIFGDDVVLQFGGGTIGHPWGIAAGATANRVALEAMVQARNEGRDLAREGPEILREAAKWSPELAAALETWKDIKFEFE 447


                  ...
gi 1913595456 161 STD 163
Cdd:cd08212   448 STD 450
rbcL PRK04208
ribulose bisophosphate carboxylase; Reviewed
 1-165 4.84e-95

ribulose bisophosphate carboxylase; Reviewed


Pssm-ID: 179787  Cd Length: 468  Bit Score: 283.34  E-value: 4.84e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456   1 FRVICKWMRMSGVDHIHAGTVVGKLEGDPLMVRGFYNTLLLTELKINLAEGLFFDMDWASLRKCVPVASGGIHCGQMHQL 80
Cdd:PRK04208  304 FRVLAKLLRLIGVDHLHTGTVVGKLEGDRAEVLGYYDILREDFVPEDRSRGIFFDQDWGSIKPVFPVASGGIHPGHMPAL 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456  81 LYYLGDDVVLQFGGGTIGHPDGIQAGATANRVALEAMVLARNEGRDYVGEGPEILRTAASTCGPLKAALDLWKDITFEYT 160
Cdd:PRK04208  384 LDIFGDDVVLQFGGGTHGHPDGTAAGATANRVALEACVEARNEGRDIEKEGPDILEEAAKWSPELAAALEKWGEIKFEFD 463


                  ....*
gi 1913595456 161 STDTP 165
Cdd:PRK04208  464 TVDTL 468
RuBisCO_large_I_II_III cd08206
Ribulose bisphosphate carboxylase large chain, Form I,II,III; Ribulose bisphosphate ...
 1-152 2.18e-70

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: 218.26  E-value: 2.18e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456   1 FRVICKWMRMSGVDHIHAGTVVGKLEGDPLMVRGFYNTLLLTELKINLaEGLFFDMDWASLRKCVPVASGGIHCGQMHQL 80
Cdd:cd08206   276 MRVLAKLARLIGVDHIHTGTVVGKLEGDPSEVKGIADMLREDEVEGDL-SRIFFNQDWGGMKPVFPVASGGLHPGRMPAL 354

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1913595456  81 LYYLGDDVVLQFGGGTIGHPDGIQAGATANRVALEAMVLARnegrdyvgegpeILRTAASTCGPLKAALDLW 152
Cdd:cd08206   355 IEILGDDVILQFGGGTHGHPDGPAAGAKANRQALEAWVQGR------------ILREYAKTHKELAAALEKW 414
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
 1-152 8.43e-59

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: 185.26  E-value: 8.43e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456   1 FRVICKWMRMSGVDHIHAGTV-VGKLEGDPLmvrgfyNTLLLTELKINLAEGLFFDMDWASLRKCVPVASGGIHCGQMHQ 79
Cdd:pfam00016 157 FRVLAKMARLAGADHLHTGTMgVGKLEGDPS------DTLRAYMLEEDRARGPFFDQDWGGMPAVMPVASGGIHAGQMPG 230

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1913595456  80 LLYYLGD-DVVLQFGGGTIGHPDGIQAGATANRVALEAMVlarnEGRDYVGEgpeilrtaASTCGPLKAALDLW 152
Cdd:pfam00016 231 LFDNLGDsDVILQFGGGTFGHPDGPAAGAKANRQALEAWV----EGRDLEEY--------AKEHPELARAFESW 292
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
 1-157 9.01e-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: 159.95  E-value: 9.01e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456   1 FRVICKWMRMSGVDHIHAGTVVGKLEGDPLMVRGFYNTLLLtelkinlaeglffdmDWASLRKCVPVASGGIHCGQMHQL 80
Cdd:COG1850   288 MRVLAKLWRLAGADHLHVGTPVGKMEGDDEEVLAIADALLQ---------------PWGGLKPVFPVPSGGQHPGQVPEL 352

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1913595456  81 LYYLGDDVVLQFGGGTIGHPDGIQAGATANRVALEAMVLARNegrdyvgegpeiLRTAASTCGPLKAALDLWKDITF 157
Cdd:COG1850   353 YDALGTDLILQAGGGIHGHPDGPAAGARALRQAWEAAVAGIP------------LEEYAKTHPELAAALEKWGKKAP 417
RuBisCO_large_III cd08213
Ribulose bisphosphate carboxylase large chain, Form III; Ribulose bisphosphate carboxylase ...
 2-152 1.07e-31

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: 117.49  E-value: 1.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456   2 RVICKWMRMSGVDHIHAGTVVGKLEGDPLMVRGFYNTLLLTELKINlAEGLFFDMDWASLRKCVPVASGGIHCGQMHQLL 81
Cdd:cd08213   275 LVLAKLYRLIGVDQLHIGTAVGKMEGDKEEVLRIADILREQKYKPD-EEDFHLAQDWGGIKPVFPVASGGLHPGLVPDVI 353

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1913595456  82 YYLGDDVVLQFGGGTIGHPDGIQAGATANRVALEAMVlarnEGRDyvgegpeiLRTAASTCGPLKAALDLW 152
Cdd:cd08213   354 DILGKDIVIQVGGGVHGHPDGTRAGAKAVRQAIEAAL----EGIS--------LDEYAKDHKELARALEKW 412
RuBisCO_large cd08148
Ribulose bisphosphate carboxylase large chain; Ribulose bisphosphate carboxylase (Rubisco) ...
 1-113 8.89e-31

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: 114.45  E-value: 8.89e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456   1 FRVICKWMRMSGVDHIHAGTVVGKLEGDPLMVRGFYNtlLLTElkinlaeglffdmDWASLRKCVPVASGGIHCGQMHQL 80
Cdd:cd08148   269 MLVLAKLLRMAGGDFIHTGTVVGKMALEREEALGIAD--ALTD-------------DWAGFKRVFPVASGGIHPGLVPGI 333

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1913595456  81 LYYLGDDVVLQFGGGTIGHPDGIQAGATANRVA 113
Cdd:cd08148   334 LRDFGIDVILQAGGGIHGHPDGTVAGARAMRQA 366
PRK13475 PRK13475
ribulose-bisphosphate carboxylase;
3-116 1.80e-15

ribulose-bisphosphate carboxylase;


Pssm-ID: 184072  Cd Length: 443  Bit Score: 72.83  E-value: 1.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456   3 VICKWMRMSGVDHIHAGTV-VGKLEGDPLMVRGFYntlLLTELKinlAEGLFFDMDWASLRKCVPVASGGIHCGQMHQLL 81
Cdd:PRK13475  307 VLSKMARLQGASGIHTGTMgYGKMEGEADDRVIAY---MIERDS---AQGPFYHQEWYGMKPTTPIISGGMNALRLPGFF 380

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1913595456  82 YYLGD-DVVLQFGGGTIGHPDGIQAGATANRVALEA 116
Cdd:PRK13475  381 DNLGHgNVINTAGGGAFGHIDGPAAGAKSLRQAYDC 416
RLP_DK-MTP-1-P-enolase cd08209
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Ribulose bisphosphate carboxylase like ...
 61-152 2.11e-15

2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Ribulose bisphosphate carboxylase like proteins (RLPs) similar to B. subtilis YkrW protein, have been identified as 2,3-diketo-5-methylthiopentyl-1-phosphate enolases. They catalyze the tautomerization of 2,3-diketo-5-methylthiopentane 1-phosphate (DK-MTP 1-P). This is an important step in the methionine salvage pathway in which 5-methylthio-D-ribose (MTR) derived from 5'-methylthioadenosine is converted to methionine.


Pssm-ID: 173974  Cd Length: 391  Bit Score: 72.35  E-value: 2.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456  61 LRKCVPVASGGIHCGQMHQLLYYLGDDVVLQFGGGTIGHPDGIQAGATANRVALEAMvlarnegrdyvgEGPEILRTAAS 140
Cdd:cd08209   311 FKGVFPVPSAGIHPGLVPQLLRDFGTDVILNAGGGIHGHPDGAAAGVRAFREAIDAV------------LAGESLEPAAI 378

                          90
                  ....*....|..
gi 1913595456 141 TCGPLKAALDLW 152
Cdd:cd08209   379 PDGPLKSALDKW 390
RuBisCO_large_II cd08211
Ribulose bisphosphate carboxylase large chain, Form II; Ribulose bisphosphate carboxylase ...
 3-116 1.39e-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: 70.22  E-value: 1.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456   3 VICKWMRMSGVDHIHAGTV-VGKLEGDPlmvrgfYNTLLLTELKINLAEGLFFDMDWASLRKCVPVASGGIHCGQMHQLL 81
Cdd:cd08211   306 VLSKMARLQGASGIHTGTMgFGKMEGES------SDKVIAYMIERDEAQGPLFNQKWYGMKPTTPIISGGMNALRLPGFF 379

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1913595456  82 YYLGD-DVVLQFGGGTIGHPDGIQAGATANRVALEA 116
Cdd:cd08211   380 ENLGNgNVILTAGGGSFGHIDGPAAGAKSLRQAYDA 415
mtnW PRK09549
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Reviewed
 56-152 1.53e-14

2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Reviewed


Pssm-ID: 236560  Cd Length: 407  Bit Score: 70.04  E-value: 1.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456  56 MDWASLRKCVPVASGGIHCGQMHQLLYYLGDDVVLQFGGGTIGHPDGIQAGATANRVALEAMvlarNEGRDyvgegpeiL 135
Cdd:PRK09549  317 EDDDPFKRSFPVPSAGIHPGLVPLLIRDFGKDVVINAGGGIHGHPNGAQGGGKAFRAAIDAV----LQGKP--------L 384

                          90
                  ....*....|....*..
gi 1913595456 136 RTAASTCGPLKAALDLW 152
Cdd:PRK09549  385 HEAAEDDENLHSALDIW 401
RuBisCO_IV_RLP cd08205
Ribulose bisphosphate carboxylase like proteins, Rubisco-Form IV; Ribulose bisphosphate ...
 1-113 1.28e-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: 64.48  E-value: 1.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456   1 FRVICKWMRMSGVDHIHagtvvgklegdplmVRGFYNTLLLTELK-INLAEGLFfdMDWASLRKCVPVASGGIHCGQMHQ 79
Cdd:cd08205   270 FLLLGKLMRLAGADAVI--------------FPGPGGRFPFSREEcLAIARACR--RPLGGIKPALPVPSGGMHPGRVPE 333

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1913595456  80 LLYYLGDDVVLQFGGGTIGHPDGIQAGATANRVA 113
Cdd:cd08205   334 LYRDYGPDVILLAGGGILGHPDGAAAGVRAFRQA 367
salvage_mtnW TIGR03332
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Members of this family are the methionine ...
 57-152 5.22e-10

2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Members of this family are the methionine salvage pathway enzyme 2,3-diketo-5-methylthiopentyl-1-phosphate enolase, a homolog of RuBisCO. This protein family seems restricted to Bacillus subtilis and close relatives, where two separate proteins carry the enolase and phosphatase activities that in other species occur in a single protein, MtnC (TIGR01691). [Amino acid biosynthesis, Aspartate family, Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 132375  Cd Length: 407  Bit Score: 57.15  E-value: 5.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456  57 DWASLRKCVPVASGGIHCGQMHQLLYYLGDDVVLQFGGGTIGHPDGIQAGATANRVALEAMVLARNegrdyvgegpeiLR 136
Cdd:TIGR03332 323 DDAPFKKTFAVPSAGIHPGMVPLIMRDFGIDHIINAGGGIHGHPNGAQGGGRAFRAAIDAVLEAKP------------LH 390

                          90
                  ....*....|....*.
gi 1913595456 137 TAASTCGPLKAALDLW 152
Cdd:TIGR03332 391 EKAADDIDLKLALDKW 406
RLP_NonPhot cd08207
Ribulose bisphosphate carboxylase like proteins from nonphototrophic bacteria; Ribulose ...
 1-118 2.01e-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: 55.39  E-value: 2.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1913595456   1 FRVICKWMRMSGVDHIHAGTVVGKL-EGDPLMVRGFYNtlLLTELkinlaeglffdmdWASLRKCVPVASGGIHCGQMHQ 79
Cdd:cd08207   283 FQAYQKLWRLAGVDHLHVNGLASKFwESDDSVIESARA--CLTPL-------------GGPDDAAMPVFSSGQWGGQAPP 347

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1913595456  80 LLYYLG-DDVVLQFGGGTIGHPDGIQAGATANRVALEAMV 118
Cdd:cd08207   348 TYRRLGsVDLLYLAGGGIMAHPDGPAAGVRSLRQAWEAAV 387
 
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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