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Conserved domains on  [gi|194295570|gb|ACF40813|]
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ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit, partial (chloroplast) [Cyanidiales sp. OC1A-12]

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) ...
1-263 0e+00

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: 567.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570   1 PYaKMGYWNPNYVVKDSDMLALFRVTPQPGVDPIEAAAAVAGESSTATWTVVWTDLLTACDVYRAKAYRVDPVPTAPDQY 80
Cdd:CHL00040  19 DY-KLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYRIEPVPGEENQY 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  81 FVYIAYDIDLFEEGSIANLTASIIGNVFGFKAVKALRLEDMRIPFSCLKTFQGPATGVIVERERLNKFGRPFLGCTVKPK 160
Cdd:CHL00040  98 IAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYLKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPK 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570 161 LGLSGKNYGRVVYEGLKGGLDFLKDDENINSQPFMRWRDRFLYVMEGVNRAAAASGEVKGSYLNVTAATMEECYKRAEFA 240
Cdd:CHL00040 178 LGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMYKRAVFA 257
                        250       260
                 ....*....|....*....|....
gi 194295570 241 KEVGSVIIMIDLVI-GYTAIQTMA 263
Cdd:CHL00040 258 RELGVPIVMHDYLTgGFTANTSLA 281
 
Name Accession Description Interval E-value
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
1-263 0e+00

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


Pssm-ID: 176981  Cd Length: 475  Bit Score: 567.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570   1 PYaKMGYWNPNYVVKDSDMLALFRVTPQPGVDPIEAAAAVAGESSTATWTVVWTDLLTACDVYRAKAYRVDPVPTAPDQY 80
Cdd:CHL00040  19 DY-KLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYRIEPVPGEENQY 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  81 FVYIAYDIDLFEEGSIANLTASIIGNVFGFKAVKALRLEDMRIPFSCLKTFQGPATGVIVERERLNKFGRPFLGCTVKPK 160
Cdd:CHL00040  98 IAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYLKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPK 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570 161 LGLSGKNYGRVVYEGLKGGLDFLKDDENINSQPFMRWRDRFLYVMEGVNRAAAASGEVKGSYLNVTAATMEECYKRAEFA 240
Cdd:CHL00040 178 LGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMYKRAVFA 257
                        250       260
                 ....*....|....*....|....
gi 194295570 241 KEVGSVIIMIDLVI-GYTAIQTMA 263
Cdd:CHL00040 258 RELGVPIVMHDYLTgGFTANTSLA 281
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
6-263 0e+00

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: 540.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570   6 GYWNPNYVVKDSDMLALFRVTPQPGVDPIEAAAAVAGESSTATWTVVWTDLLTACDVYRAKAYRVDPVPTAPDQYFVYIA 85
Cdd:cd08212    1 GYWTPDYQPKDTDILAAFRITPQPGVDPEEAAAAVAGESSTATWTVVWTDRLTALDRYKGKAYRVEPVPGEENQYFAYIA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  86 YDIDLFEEGSIANLTASIIGNVFGFKAVKALRLEDMRIPFSCLKTFQGPATGVIVERERLNKFGRPFLGCTVKPKLGLSG 165
Cdd:cd08212   81 YPLDLFEEGSVANLTTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDRLNKYGRPLLGCTIKPKLGLSA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570 166 KNYGRVVYEGLKGGLDFLKDDENINSQPFMRWRDRFLYVMEGVNRAAAASGEVKGSYLNVTAATMEECYKRAEFAKEVGS 245
Cdd:cd08212  161 KNYGRVVYECLRGGLDFTKDDENINSQPFMRWRDRFLFVAEAVNKAQAETGEVKGHYLNVTAGTMEEMYKRAEFAKELGS 240
                        250
                 ....*....|....*...
gi 194295570 246 VIIMIDLVIGYTAIQTMA 263
Cdd:cd08212  241 PIIMHDLLTGFTAIQSLA 258
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
6-263 2.56e-112

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


Pssm-ID: 441455  Cd Length: 417  Bit Score: 329.44  E-value: 2.56e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570   6 GYWNPNYVVKDSDMLALFRVTPQPGVDPIEAAAAVAGESSTATWTVVWTDLLTACDVYRAKAYRVDPVPTAP---DQYFV 82
Cdd:COG1850    1 DYVDPDYIPDDDDILATYRITPETGVDPEEAAAAIAGEQSTGTWTEVPTETDELRERLAARVYSIEELPEVGggyRRALV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  83 YIAYDIDLFEeGSIANLTASIIGNVFGFKAVKALRLEDMRIPFSCLKTFQGPATGVIVERERLNKFGRPFLGCTVKPKLG 162
Cdd:COG1850   81 TIAYPLENFG-GNLPNLLSTVAGNLFGLKAVSGLRLLDLEFPESFLAAFPGPKFGIEGTRELLGVYDRPLLGTIIKPKVG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570 163 LSGKNYGRVVYEGLKGGLDFLKDDENINSQPFMRWRDRFLYVMEGVNRAAAASGEVKGSYLNVTaATMEECYKRAEFAKE 242
Cdd:COG1850  160 LSPEETAELVYELALGGVDFIKDDENLADQPFCPFEDRVRAVMEAIDRAEEETGEKKMYAFNIT-ADTDEMLRRADLAVE 238
                        250       260
                 ....*....|....*....|..
gi 194295570 243 VGSVIIMID-LVIGYTAIQTMA 263
Cdd:COG1850  239 LGANAVMVDvNTVGLSAVQTLR 260
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
138-263 9.41e-72

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: 221.85  E-value: 9.41e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  138 VIVERERLNKFGRPFLGCTVKPKLGLSGKNYGRVVYEGLKGGLDFLKDDENINSQPFMRWRDRFLYVMEGVNRAAAASGE 217
Cdd:pfam00016   1 IAVERRVLNKYGRPILGTIIKPKLGLSPKNYARAVYEFLLGGLDFIKDDENINSQPFMPWRDRFLFVAEAIDRAQDETGE 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 194295570  218 VKGSYLNVTAATMEECYKRAEFAKEVGSVIIMID-LVIGYTAIQTMA 263
Cdd:pfam00016  81 AKGHYLNITADDMEEMYRRAEFAKETGGVAVMVDgLVIGPTAITTLR 127
rubisco_III TIGR03326
ribulose bisphosphate carboxylase, type III; Members of this protein family are the archaeal, ...
7-262 3.24e-69

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: 218.87  E-value: 3.24e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570    7 YWNPNYVVKDSDMLALFRVTPQPGVDPIEAAAAVAGESSTATWTVV--WTDLLTACDVyRAKAYRVDPVPtapDQYFVYI 84
Cdd:TIGR03326   2 FVDLNYEPSDDDLVCTFRITPAEGVSIEDAAGRVASESSIGTWTTLqpWKDPERYKDL-SAKVYDIEEHG---DGSIVRI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570   85 AYDIDLFEEGSIANLTASIIGNVFGFKAVKALRLEDMRIPFSCLKTFQGPATGVIVERERLNKFGRPFLGCTVKPKLGLS 164
Cdd:TIGR03326  78 AYPLGLFEEGNLPQLLSCIAGNIFGMKAVKGLRLLDFEFPAEFLRAFKGPQFGIEGVREILGIKDRPITATVPKPKVGLS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  165 GKNYGRVVYEGLKGGLDFLKDDENINSQPFMRWRDRFLYVMEGVNRAAAASGEVKGSYLNVTAATmEECYKRAEFAKEVG 244
Cdd:TIGR03326 158 TEEHAKVAYELWSGGVDLLKDDENLTSQAFNRFEERVEKSLKVRDKVEAETGEKKSYLINITADV-REMERRAELVADLG 236
                         250
                  ....*....|....*....
gi 194295570  245 SVIIMIDLVI-GYTAIQTM 262
Cdd:TIGR03326 237 GEYVMVDIVVaGWSALQYV 255
 
Name Accession Description Interval E-value
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
1-263 0e+00

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


Pssm-ID: 176981  Cd Length: 475  Bit Score: 567.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570   1 PYaKMGYWNPNYVVKDSDMLALFRVTPQPGVDPIEAAAAVAGESSTATWTVVWTDLLTACDVYRAKAYRVDPVPTAPDQY 80
Cdd:CHL00040  19 DY-KLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYRIEPVPGEENQY 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  81 FVYIAYDIDLFEEGSIANLTASIIGNVFGFKAVKALRLEDMRIPFSCLKTFQGPATGVIVERERLNKFGRPFLGCTVKPK 160
Cdd:CHL00040  98 IAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYLKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPK 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570 161 LGLSGKNYGRVVYEGLKGGLDFLKDDENINSQPFMRWRDRFLYVMEGVNRAAAASGEVKGSYLNVTAATMEECYKRAEFA 240
Cdd:CHL00040 178 LGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMYKRAVFA 257
                        250       260
                 ....*....|....*....|....
gi 194295570 241 KEVGSVIIMIDLVI-GYTAIQTMA 263
Cdd:CHL00040 258 RELGVPIVMHDYLTgGFTANTSLA 281
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
6-263 0e+00

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: 540.47  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570   6 GYWNPNYVVKDSDMLALFRVTPQPGVDPIEAAAAVAGESSTATWTVVWTDLLTACDVYRAKAYRVDPVPTAPDQYFVYIA 85
Cdd:cd08212    1 GYWTPDYQPKDTDILAAFRITPQPGVDPEEAAAAVAGESSTATWTVVWTDRLTALDRYKGKAYRVEPVPGEENQYFAYIA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  86 YDIDLFEEGSIANLTASIIGNVFGFKAVKALRLEDMRIPFSCLKTFQGPATGVIVERERLNKFGRPFLGCTVKPKLGLSG 165
Cdd:cd08212   81 YPLDLFEEGSVANLTTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDRLNKYGRPLLGCTIKPKLGLSA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570 166 KNYGRVVYEGLKGGLDFLKDDENINSQPFMRWRDRFLYVMEGVNRAAAASGEVKGSYLNVTAATMEECYKRAEFAKEVGS 245
Cdd:cd08212  161 KNYGRVVYECLRGGLDFTKDDENINSQPFMRWRDRFLFVAEAVNKAQAETGEVKGHYLNVTAGTMEEMYKRAEFAKELGS 240
                        250
                 ....*....|....*...
gi 194295570 246 VIIMIDLVIGYTAIQTMA 263
Cdd:cd08212  241 PIIMHDLLTGFTAIQSLA 258
rbcL PRK04208
ribulose bisophosphate carboxylase; Reviewed
1-263 1.15e-180

ribulose bisophosphate carboxylase; Reviewed


Pssm-ID: 179787  Cd Length: 468  Bit Score: 504.83  E-value: 1.15e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570   1 PYAKMgYWNPNYVVKDSDMLALFRVTPQPGVDPIEAAAAVAGESSTATWTVVWTDLLTACDVYRAKAYRVDPVPTAPDQY 80
Cdd:PRK04208  12 EYRQM-YWDPDYTPKDTDLLACFRITPQEGVDPEEAAAAVAAESSTGTWTTVWTDLLTDLDKYKAKAYRIEDVPGDDGSY 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  81 FVYIAYDIDLFEEGSIANLTASIIGNVFGFKAVKALRLEDMRIPFSCLKTFQGPATGVIVERERLNKFGRPFLGCTVKPK 160
Cdd:PRK04208  91 YAFIAYPLDLFEEGSIPNLLASIAGNVFGFKAVKALRLEDIRFPVAYVKTFKGPPFGIQVERERLDKYGRPLLGTTPKPK 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570 161 LGLSGKNYGRVVYEGLKGGLDFLKDDENINSQPFMRWRDRFLYVMEGVNRAAAASGEVKGSYLNVTAATMEECYKRAEFA 240
Cdd:PRK04208 171 LGLSAKNYGRVVYEALRGGLDFTKDDENLNSQPFNRWRDRFLFVMEAIDKAEAETGERKGHYLNVTAPTMEEMYKRAEFA 250
                        250       260
                 ....*....|....*....|....
gi 194295570 241 KEVGSVIIMIDLVI-GYTAIQTMA 263
Cdd:PRK04208 251 KELGSPIVMIDVVTaGWTALQSLR 274
RuBisCO_large_I_II_III cd08206
Ribulose bisphosphate carboxylase large chain, Form I,II,III; Ribulose bisphosphate ...
17-263 1.63e-156

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: 441.29  E-value: 1.63e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  17 SDMLALFRVTPQPGVDPIEAAAAVAGESSTATWTVVWTDLLTACDVYRAKAYRVDPVPTapDQYFVYIAYDIDLFEEGSI 96
Cdd:cd08206    1 TDLLAAFRMTPAEGVDPEEAAAAVAAESSTGTWTTVWTDRLTATERLKAKVYRIDPVPD--GQYIAKIAYPLDLFEEGSV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  97 ANLTASIIGNVFGFKAVKALRLEDMRIPFSCLKTFQGPATGVIVERERLNKFGRPFLGCTVKPKLGLSGKNYGRVVYEGL 176
Cdd:cd08206   79 PNLLTSIIGNVFGMKAVKALRLEDFRFPPAYLKTFDGPSFGIQGEREILGKYGRPLLGTIVKPKLGLSPKEYARVVYEAL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570 177 KGGLDFLKDDENINSQPFMRWRDRFLYVMEGVNRAAAASGEVKGSYLNVTAATMEECYKRAEFAKEVGSVIIMIDLVI-G 255
Cdd:cd08206  159 RGGLDFVKDDENQNSQPFMRFEDRILFVAEAMDKAEAETGEAKGHYLNITADTPEEMIKRAEFAKELGSVIVMVDGVTaG 238

                 ....*...
gi 194295570 256 YTAIQTMA 263
Cdd:cd08206  239 WTAIQSAR 246
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
6-263 2.56e-112

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


Pssm-ID: 441455  Cd Length: 417  Bit Score: 329.44  E-value: 2.56e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570   6 GYWNPNYVVKDSDMLALFRVTPQPGVDPIEAAAAVAGESSTATWTVVWTDLLTACDVYRAKAYRVDPVPTAP---DQYFV 82
Cdd:COG1850    1 DYVDPDYIPDDDDILATYRITPETGVDPEEAAAAIAGEQSTGTWTEVPTETDELRERLAARVYSIEELPEVGggyRRALV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  83 YIAYDIDLFEeGSIANLTASIIGNVFGFKAVKALRLEDMRIPFSCLKTFQGPATGVIVERERLNKFGRPFLGCTVKPKLG 162
Cdd:COG1850   81 TIAYPLENFG-GNLPNLLSTVAGNLFGLKAVSGLRLLDLEFPESFLAAFPGPKFGIEGTRELLGVYDRPLLGTIIKPKVG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570 163 LSGKNYGRVVYEGLKGGLDFLKDDENINSQPFMRWRDRFLYVMEGVNRAAAASGEVKGSYLNVTaATMEECYKRAEFAKE 242
Cdd:COG1850  160 LSPEETAELVYELALGGVDFIKDDENLADQPFCPFEDRVRAVMEAIDRAEEETGEKKMYAFNIT-ADTDEMLRRADLAVE 238
                        250       260
                 ....*....|....*....|..
gi 194295570 243 VGSVIIMID-LVIGYTAIQTMA 263
Cdd:COG1850  239 LGANAVMVDvNTVGLSAVQTLR 260
RuBisCO_large cd08148
Ribulose bisphosphate carboxylase large chain; Ribulose bisphosphate carboxylase (Rubisco) ...
20-263 1.12e-83

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: 254.66  E-value: 1.12e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  20 LALFRVTPQPgVDPIEAAAAVAGESSTATWTVVWTdLLTACDVYRAKAYRVDPVPtapDQYFVYIAYDIDLFEEGSIANL 99
Cdd:cd08148    2 LATYRVHPEA-TPPEKAAEAIAAESSTGTWTEVPT-TQEQLRRVKGRVYSVEELG---KRYIVKIAYPVELFEPGNIPQI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570 100 TASIIGNVFGFKAVKALRLEDMRIPFSCLKTFQGPATGVIVERERLNKFGRPFLGCTVKPKLGLSGKNYGRVVYEGLKGG 179
Cdd:cd08148   77 LTVTAGNLFGLGALEAVRLEDLEFPEEYKKLFPGPKFGIDGIRKLLGVYGRPLVGTIIKPKLGLNPKYTAEAAYAAALGG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570 180 LDFLKDDENINSQPFMRWRDRFLYVMEGVNRAAAASGEVKGSYLNVTAATmEECYKRAEFAKEVGSVIIMID-LVIGYTA 258
Cdd:cd08148  157 LDLIKDDETLTDQPFCPLRDRITEVAAALDRVQEETGEKKLYAVNVTAGT-FEIIERAERALELGANMLMVDvLTAGFSA 235

                 ....*
gi 194295570 259 IQTMA 263
Cdd:cd08148  236 LQALA 240
RuBisCO_large_III cd08213
Ribulose bisphosphate carboxylase large chain, Form III; Ribulose bisphosphate carboxylase ...
17-262 7.51e-83

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: 253.85  E-value: 7.51e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  17 SDMLALFRVTPQPGVDPIEAAAAVAGESSTATWTVVWTDLLTACDVYRAKAYRVDPVPTApdqYFVYIAYDIDLFEEGSI 96
Cdd:cd08213    1 DDLIAVFRIEPAEGISIEEAAGRVASESSIGTWTTLATLYPERAEKLKAKAYYFDGLGGS---YIVKVAYPLELFEEGNM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  97 ANLTASIIGNVFGFKAVKALRLEDMRIPFSCLKTFQGPATGVIVERERLNKFGRPFLGCTVKPKLGLSGKNYGRVVYEGL 176
Cdd:cd08213   78 PQLLSSIAGNIFGMKAVKNLRLEDIYFPESYLREFKGPQFGIEGVREILGIKDRPLLGTVPKPKVGLSPEEHAEVAYEAL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570 177 KGGLDFLKDDENINSQPFMRWRDRFLYVMEGVNRAAAASGEVKGSYLNVTAATmEECYKRAEFAKEVGSVIIMIDLVI-G 255
Cdd:cd08213  158 VGGVDLVKDDENLTSQPFNRFEERAKESLKARDKAEAETGERKAYLANITAPV-REMERRAELVADLGGKYVMIDVVVaG 236

                 ....*..
gi 194295570 256 YTAIQTM 262
Cdd:cd08213  237 WSALQYL 243
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
138-263 9.41e-72

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: 221.85  E-value: 9.41e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  138 VIVERERLNKFGRPFLGCTVKPKLGLSGKNYGRVVYEGLKGGLDFLKDDENINSQPFMRWRDRFLYVMEGVNRAAAASGE 217
Cdd:pfam00016   1 IAVERRVLNKYGRPILGTIIKPKLGLSPKNYARAVYEFLLGGLDFIKDDENINSQPFMPWRDRFLFVAEAIDRAQDETGE 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 194295570  218 VKGSYLNVTAATMEECYKRAEFAKEVGSVIIMID-LVIGYTAIQTMA 263
Cdd:pfam00016  81 AKGHYLNITADDMEEMYRRAEFAKETGGVAVMVDgLVIGPTAITTLR 127
rubisco_III TIGR03326
ribulose bisphosphate carboxylase, type III; Members of this protein family are the archaeal, ...
7-262 3.24e-69

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: 218.87  E-value: 3.24e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570    7 YWNPNYVVKDSDMLALFRVTPQPGVDPIEAAAAVAGESSTATWTVV--WTDLLTACDVyRAKAYRVDPVPtapDQYFVYI 84
Cdd:TIGR03326   2 FVDLNYEPSDDDLVCTFRITPAEGVSIEDAAGRVASESSIGTWTTLqpWKDPERYKDL-SAKVYDIEEHG---DGSIVRI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570   85 AYDIDLFEEGSIANLTASIIGNVFGFKAVKALRLEDMRIPFSCLKTFQGPATGVIVERERLNKFGRPFLGCTVKPKLGLS 164
Cdd:TIGR03326  78 AYPLGLFEEGNLPQLLSCIAGNIFGMKAVKGLRLLDFEFPAEFLRAFKGPQFGIEGVREILGIKDRPITATVPKPKVGLS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  165 GKNYGRVVYEGLKGGLDFLKDDENINSQPFMRWRDRFLYVMEGVNRAAAASGEVKGSYLNVTAATmEECYKRAEFAKEVG 244
Cdd:TIGR03326 158 TEEHAKVAYELWSGGVDLLKDDENLTSQAFNRFEERVEKSLKVRDKVEAETGEKKSYLINITADV-REMERRAELVADLG 236
                         250
                  ....*....|....*....
gi 194295570  245 SVIIMIDLVI-GYTAIQTM 262
Cdd:TIGR03326 237 GEYVMVDIVVaGWSALQYV 255
RuBisCO_large_N pfam02788
Ribulose bisphosphate carboxylase large chain, N-terminal domain; The N-terminal domain of ...
6-124 3.32e-63

Ribulose bisphosphate carboxylase large chain, N-terminal domain; The N-terminal domain of RuBisCO large chain adopts a ferredoxin-like fold.


Pssm-ID: 426983  Cd Length: 120  Bit Score: 193.97  E-value: 3.32e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570    6 GYWNPNYVVKDSDMLALFRVTPQPGVDPIEAAAAVAGESSTATWTVVWTDLLTACDVYRAKAYRVDPVPTapDQYFVYIA 85
Cdd:pfam02788   1 DYVDLDYEPKDTDLLCAFRIEPAAGVSPEEAAAHVAAESSTGTWTEVWTLDDTFTKKLKAKVYEIDEVPG--GSYIVKIA 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 194295570   86 YDIDLFEEGSIANLTASIIGNVFGFKAVKALRLEDMRIP 124
Cdd:pfam02788  79 YPLDLFEEGSIPQLLSSIAGNIFGMKAVKALRLEDIRFP 117
RuBisCO_IV_RLP cd08205
Ribulose bisphosphate carboxylase like proteins, Rubisco-Form IV; Ribulose bisphosphate ...
23-263 1.62e-36

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: 132.66  E-value: 1.62e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  23 FRVT---PQPGVDPIEAAAAVAGESSTATWTVVWT---DLLtacDVYRAKAYRVDPVPTAPDQYFVY---IAYDIDLFEe 93
Cdd:cd08205    1 ITATyriEAPGADAEKKAEAIALEQTVGTWTELPGeteEIR---ERHVGRVESIEELEESEGKYGRArvtISYPLDNFG- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  94 GSIANLTASIIGNVFGfkaVKALRLEDMRIPFSCLKTFQGPATGVIVERERLNKFGRPFLGCTVKPKLGLSGKNYGRVVY 173
Cdd:cd08205   77 GDLPQLLNTLFGNLSL---LPGIKLVDLELPDSLLAAFPGPRFGIEGLRRLLGVHDRPLLGTIIKPSIGLSPEELAELAY 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570 174 EGLKGGLDFLKDDENINSQPFMRWRDRFLYVMEGVNRAAAASGEvKGSYL-NVTAAT--MEEcykRAEFAKEVGSVIIMI 250
Cdd:cd08205  154 ELALGGIDLIKDDELLADQPYAPFEERVRACMEAVRRANEETGR-KTLYApNITGDPdeLRR---RADRAVEAGANALLI 229
                        250
                 ....*....|....
gi 194295570 251 DL-VIGYTAIQTMA 263
Cdd:cd08205  230 NPnLVGLDALRALA 243
PRK13475 PRK13475
ribulose-bisphosphate carboxylase;
19-261 2.44e-34

ribulose-bisphosphate carboxylase;


Pssm-ID: 184072  Cd Length: 443  Bit Score: 128.30  E-value: 2.44e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  19 MLALFRVTPQPGVDPIEAAAAVAGESSTATWTVVWT--DLLTACDvyrAKAYRVDPVptapdQYFVYIAYDIDLFE---- 92
Cdd:PRK13475  24 ILCAYKMKPKAGHGYLEAAAHFAAESSTGTNVEVSTtdDFTRGVD---ALVYEIDEA-----RELMKIAYPVELFDrnii 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  93 --EGSIANLTASIIGNVFGFKAVKALRLEDMRIPFSCLKTFQGPATGVIVERERLnkfGRP------FLGCTVKPKLGLS 164
Cdd:PRK13475  96 dgRAMIVSFLTLTIGNNQGMGDVEYAKMHDFYVPPRYLELFDGPSTDISDLWRVL---GRPvkdggyIAGTIIKPKLGLR 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570 165 GKNYGRVVYEGLKGGlDFLKDDENINSQPFMRWRDRFLYVMEGVNRAAAASGEVKGSYLNVTAATMEECYKRAEFAKEV- 243
Cdd:PRK13475 173 PEPFAEACYDFWLGG-DFIKNDEPQGNQVFAPLKKTVPLVADAMKRAQDETGEAKLFSANITADDHYEMIARGEYILETf 251
                        250       260
                 ....*....|....*....|...
gi 194295570 244 ----GSVIIMID-LVIGYTAIQT 261
Cdd:PRK13475 252 genaDHVAFLVDgYVAGPGAVTT 274
RuBisCO_large_II cd08211
Ribulose bisphosphate carboxylase large chain, Form II; Ribulose bisphosphate carboxylase ...
19-261 2.49e-33

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: 125.69  E-value: 2.49e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  19 MLALFRVTPQPGVDPIEAAAAVAGESSTAT-WTVVWTDLLTacDVYRAKAYRVDPvptapDQYFVYIAYDIDLFE----- 92
Cdd:cd08211   23 VLVAYIMKPKAGYGYLATAAHFAAESSTGTnVEVSTTDDFT--RGVDALVYEIDE-----ARELMKIAYPVELFDrnltd 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  93 -EGSIANLTASIIGNVFGFKAVKALRLEDMRIPFSCLKTFQGPATGVIVERERLNKF---GRPFLGCTVKPKLGLSGKNY 168
Cdd:cd08211   96 gRAMVASFLTLIIGNNQGMGDVEYLKMHDFYVPESMLELFDGPSVNISDMWKVLGRPevdGGYIAGTIIKPKLGLRPKPF 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570 169 GRVVYEGLKGGlDFLKDDENINSQPFMRWRDRFLYVMEGVNRAAAASGEVKGSYLNVTAATMEECYKRAE-----FAKEV 243
Cdd:cd08211  176 AEACYAFWLGG-DFIKNDEPQANQPFCPLKKVIPLVADAMRRAQDETGEAKLFSANITADDPDEMIARGEyileaFGPNA 254
                        250
                 ....*....|....*....
gi 194295570 244 GSVIIMID-LVIGYTAIQT 261
Cdd:cd08211  255 GHVAFLVDgYVAGPAAVTT 273
RLP_NonPhot cd08207
Ribulose bisphosphate carboxylase like proteins from nonphototrophic bacteria; Ribulose ...
31-262 4.71e-33

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: 124.34  E-value: 4.71e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  31 VDPIEAAAAVAGESSTATWTVV--WTDLLTACdvYRAKAYRVDPVPTAPDQY-------------FVYIAYDIDLFEEgS 95
Cdd:cd08207   12 LDLERAAEVIAGEQSSGTFIALpgETDELKER--SAARVESIEELETAAQPSlprrasggpytraRVTISFPLDNIGT-S 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  96 IANLTASIIGNVFGFKAVKALRLEDMRIPFSCLKTFQGPATGVIVERERLNKFGRPFLGCTVKPKLGLSGKNYGRVVYEG 175
Cdd:cd08207   89 LPNLLATVAGNLFELRELSGLRLVDLGLPDEFAAAFPGPAFGIAGTRRLTGVEDRPLIGTIIKPSVGLTPEETAALVRQL 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570 176 LKGGLDFLKDDENINSQPFMRWRDRFLYVMEGVNRAAAASGEvKGSY-LNVTAATmEECYKRAEFAKEVGSVIIMIDL-V 253
Cdd:cd08207  169 AAAGIDFIKDDELLANPPYSPLDERVRAVMRVINDHAQRTGR-KVMYaFNITDDI-DEMRRNHDLVVEAGGTCVMVSLnS 246

                 ....*....
gi 194295570 254 IGYTAIQTM 262
Cdd:cd08207  247 VGLSGLAAL 255
RLP_RrRLP cd08210
Ribulose bisphosphate carboxylase like proteins (RLPs) similar to R.rubrum RLP; RLP from ...
21-250 3.48e-21

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: 91.15  E-value: 3.48e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  21 ALFRVTPQPGVDPIEAAAAVAGESstatwTV-VWTDLLTACDVYRAKAYRVDPV-PTAPDQYFVYIAYDIDlfeegSIAN 98
Cdd:cd08210    4 VTYRLVAASEAEAEARARGIALEQ-----TVeMPLELVPDGYIRDNIVGRVESLePAGEGSYRARISYSVD-----TAGG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  99 LTASIIGNVFGFKAVKA-LRLEDMRIPFSCLKTFQGPATGVIVERERLNKFGRPFLGCTVKPkLGLSGKNYGRVVYEGLK 177
Cdd:cd08210   74 ELTQLLNVLFGNSSLQPgIRLVDFELPPSLLRRFPGPRFGIAGLRALLGIPERPLLCSALKP-QGLSAAELAELAYAFAL 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194295570 178 GGLDFLKDDENINSQPFMRWRDRFLYVMEGVNRAAAASGEvKGSYL-NVTAATMeECYKRAEFAKEVGSVIIMI 250
Cdd:cd08210  153 GGIDIIKDDHGLADQPFAPFEERVKACQEAVAEANAETGG-RTLYApNVTGPPT-QLLERARFAKEAGAGGVLI 224
RLP_Photo cd08208
Ribulose bisphosphate carboxylase like proteins from phototrophic bacteria; Ribulose ...
32-226 1.41e-19

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: 87.26  E-value: 1.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  32 DPIEAAAAVAGESSTATWTVVWTDL------------LTACDVYRAKAYRVDPVPTAP-DQYFVYIAYDIDLFEEgSIAN 98
Cdd:cd08208   29 DPETAAAHFCSEQSTAQWRRVGVDEdfrprfaakvidLEVIEELEQLSYPVKHSETGPvHACRVTIAHPHGNFGP-KIPN 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  99 LTASIIGN-VFGFKAVKALRLEDMRIPFSCLKTFQGPATGVIVERERLNKFGRPFLGCTVKPKLGLSGKNYGRVVYEGLK 177
Cdd:cd08208  108 LLSAVCGEgTFFSPGVPVVKLMDIHFPETYLADFEGPKFGIAGLRERLQAHDRPIFFGVIKPNIGLPPGEFAELGYQSWL 187
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 194295570 178 GGLDFLKDDENINSQPFMRWRDRFLYVMEGVNRAAAASGEVKGSYLNVT 226
Cdd:cd08208  188 GGLDIAKDDEMLADVDWCPLEERAALLGKARRRAEAETGVPKIYLANIT 236
RLP_DK-MTP-1-P-enolase cd08209
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Ribulose bisphosphate carboxylase like ...
28-187 1.34e-08

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: 54.63  E-value: 1.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  28 QPGVDPIEAAAAVAGESSTATWTVVWtdLLTACDVYRAKAyRVDPVPTAPDQYFVY-IAYdidlfEEGSIANLTASIIGN 106
Cdd:cd08209    8 PDGADLEKKAEQIAVGLTVGSWTDLP--ALRQAQLQKHLG-EVVSVEELEEGRGVItIAY-----PLINVSGDIPALLTT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570 107 VFG-FKAVKALRLEDMRIPFSCLKTFQGPATGVIVERERLNKFGRPFLGCTVKPKLGLSGKNYGRVVYEGLKGGLDFLKD 185
Cdd:cd08209   80 IFGkLSLDGKIKLVDLRLPEEFGRAFPGPKFGIEGIRQRLGVHDRPLLMSIFKGVLGLDLDDLAEQLREQALGGVDLIKD 159

                 ..
gi 194295570 186 DE 187
Cdd:cd08209  160 DE 161
mtnW PRK09549
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Reviewed
97-187 2.09e-04

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


Pssm-ID: 236560  Cd Length: 407  Bit Score: 41.92  E-value: 2.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194295570  97 ANLTA---SIIGNVFGFKAVKA-LRLEDMRIPFSCLKTFQGPATGVIVERERLNKFGRPFLGCTVKPKLGLSGKNYGRVV 172
Cdd:PRK09549  77 ANFSPdlpAILTTTFGKLSLDGeVKLIDLTFSDELKRHFPGPKFGIDGIRNLLGVHDRPLLMSIFKGVIGRDLDYLKEQL 156
                         90
                 ....*....|....*
gi 194295570 173 YEGLKGGLDFLKDDE 187
Cdd:PRK09549 157 RDQALGGVDLVKDDE 171
 
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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