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Conserved domains on  [gi|1942007|pdb|1RCO|L]
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Chain L, RIBULOSE BISPHOSPHATE CARBOXYLASE/OXYGENASE

Protein Classification

form I ribulose bisphosphate carboxylase large subunit( domain architecture ID 11414014)

form I ribulose bisphosphate carboxylase forms complexes containing 8 large and 8 small subunits; it catalyzes the primary CO2 fixation step in the Calvin reductive pentose phosphate pathway

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
1-475 0e+00

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


:

Pssm-ID: 176981  Cd Length: 475  Bit Score: 1068.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L         1 MSPQTETKASVGFKAGVKDYKLTYYTPEYETLDTDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTNLDRY 80
Cdd:CHL00040   1 MSPQTETKASVGFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        81 KGRCYHIEPVAGEENQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERD 160
Cdd:CHL00040  81 KGRCYRIEPVPGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYLKTFQGPPHGIQVERD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       161 KLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYL 240
Cdd:CHL00040 161 KLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       241 NATAGTCEDMMKRAVFARELGVPIVMHDYLTGGFTANTTLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRL 320
Cdd:CHL00040 241 NATAGTCEEMYKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRM 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       321 SGGDHIHSGTVVGKLEGERDITLGFVDLLRDDYTEKDRSRGIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVL 400
Cdd:CHL00040 321 SGGDHIHAGTVVGKLEGEREMTLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVL 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1RCO_L       401 QFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNTIIREATKWSPELAAACEVWKEIKFEFPAMDTV 475
Cdd:CHL00040 401 QFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEIIREAAKWSPELAAACEVWKEIKFEFETTDTL 475
 
Name Accession Description Interval E-value
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
1-475 0e+00

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


Pssm-ID: 176981  Cd Length: 475  Bit Score: 1068.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L         1 MSPQTETKASVGFKAGVKDYKLTYYTPEYETLDTDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTNLDRY 80
Cdd:CHL00040   1 MSPQTETKASVGFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        81 KGRCYHIEPVAGEENQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERD 160
Cdd:CHL00040  81 KGRCYRIEPVPGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYLKTFQGPPHGIQVERD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       161 KLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYL 240
Cdd:CHL00040 161 KLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       241 NATAGTCEDMMKRAVFARELGVPIVMHDYLTGGFTANTTLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRL 320
Cdd:CHL00040 241 NATAGTCEEMYKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRM 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       321 SGGDHIHSGTVVGKLEGERDITLGFVDLLRDDYTEKDRSRGIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVL 400
Cdd:CHL00040 321 SGGDHIHAGTVVGKLEGEREMTLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVL 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1RCO_L       401 QFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNTIIREATKWSPELAAACEVWKEIKFEFPAMDTV 475
Cdd:CHL00040 401 QFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEIIREAAKWSPELAAACEVWKEIKFEFETTDTL 475
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
23-473 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: 938.77  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       23 TYYTPEYETLDTDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTNLDRYKGRCYHIEPVAGEENQYICYVA 102
Cdd:cd08212   1 GYWTPDYQPKDTDILAAFRITPQPGVDPEEAAAAVAGESSTATWTVVWTDRLTALDRYKGKAYRVEPVPGEENQYFAYIA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      103 YPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSA 182
Cdd:cd08212  81 YPLDLFEEGSVANLTTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDRLNKYGRPLLGCTIKPKLGLSA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      183 KNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEDMMKRAVFARELGV 262
Cdd:cd08212 161 KNYGRVVYECLRGGLDFTKDDENINSQPFMRWRDRFLFVAEAVNKAQAETGEVKGHYLNVTAGTMEEMYKRAEFAKELGS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      263 PIVMHDYLTgGFTANTTLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHSGTVVGKLEGERDIT 342
Cdd:cd08212 241 PIIMHDLLT-GFTAIQSLAKWCRDNGMLLHLHRAGHATYDRQKNHGIHFRVLAKWLRLSGVDHIHAGTVVGKLEGDPLVT 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      343 LGFVDLLRDDYTEKDRSRGIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRV 422
Cdd:cd08212 320 LGFYDLLRDDYIEKDRSRGIFFTQDWASLPGVMPVASGGIHVGQMHQLIEIFGDDVVLQFGGGTIGHPWGIAAGATANRV 399
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
1RCO_L      423 ALEACVQARNEGRDLAREGNTIIREATKWSPELAAACEVWKEIKFEFPAMD 473
Cdd:cd08212 400 ALEAMVQARNEGRDLAREGPEILREAAKWSPELAAALETWKDIKFEFESTD 450
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
14-468 0e+00

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


Pssm-ID: 224763  Cd Length: 429  Bit Score: 618.99  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       14 KAGVKDYkLTYYTPEYETLDTDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTNLDRYKGRCYHIEPVAGE 93
Cdd:COG1850   1 KAGVQKY-RDYVDPNYRPKDTDLIATFRITPASGVSTEEAAAAIAGESSTGTWTTVPTDKPELADRLKAKVYDVEEVPGE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       94 --ENQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLG 171
Cdd:COG1850  80 dgQKRAIVKIAYPLDLFEEGSLPALLTSVAGNVFGMKALKGLRLEDLRFPKEFLKAFKGPQFGVEGVRDLLGVKGRPLLG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      172 CTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGtCEDMM 251
Cdd:COG1850 160 TIVKPKLGLSPEEYAELAYELLSGGVDFIKDDENLTSPPFNRFEERVAKIMEAIDKAEAETGEKKMYAVNITAP-CEEMM 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      252 KRAVFARELGVPIVMHDYLTGGFTANTTLSHYcRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHSGTV 331
Cdd:COG1850 239 RRAELAAELGANYVMIDIVVTGFTALQYLRED-EDIGLAIHAHRAMHAAFTRSPNHGISFLVLAKLLRLIGVDQLHIGTV 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      332 VGKLEGErditlgfvdllRDDYTEKDRSrgIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPW 411
Cdd:COG1850 318 VGKLEGD-----------REDYVESDKE--FFFEQDWAHIKPVFPVASGGIHPGMMPELVRIFGKDLVIQAGGGVHGHPD 384
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
1RCO_L      412 GNAPGAVANRVALEACVQARNegrdlaregntiIREATKWSPELAAACEVWKEIKFE 468
Cdd:COG1850 385 GPAAGARAVRQAIEAAVEGIP------------LREYAKWHPELAAALEKWGEIKAA 429
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
155-462 6.53e-167

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: 425422  Cd Length: 292  Bit Score: 471.84  E-value: 6.53e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        155 IQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGE 234
Cdd:pfam00016   1 IAVERRVLNKYGRPILGTIIKPKLGLSPKNYARAVYEFLLGGLDFIKDDENINSQPFMPWRDRFLFVAEAIDRAQDETGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        235 IKGHYLNATAGTCEDMMKRAVFARELGVPIVMHDYLTGGFTANTTLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVL 314
Cdd:pfam00016  81 AKGHYLNITADDMEEMYRRAEFAKETGGVAVMVDGLVIGPTAITTLRRWFRDNGVILHYHRAGHGAVTRQSKHGISFRVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        315 AKALRLSGGDHIHSGTV-VGKLEGERDitlgfvDLLRDDYTEKDRSRGIYFTQSWVSTPGVLPVASGGIHVWHMPALTEI 393
Cdd:pfam00016 161 AKMARLAGADHLHTGTMgVGKLEGDPS------DTLRAYMLEEDRARGPFFDQDWGGMPAVMPVASGGIHAGQMPGLFDN 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        394 FGD-DSVLQFGGGTLGHPWGNAPGAVANRVALEACVqarnEGRDLAREGntiireatKWSPELAAACEVW 462
Cdd:pfam00016 235 LGDsDVILQFGGGTFGHPDGPAAGAKANRQALEAWV----EGRDLEEYA--------KEHPELARAFESW 292
rubisco_III TIGR03326
ribulose bisphosphate carboxylase, type III; Members of this protein family are the archaeal, ...
29-462 6.62e-115

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: 344.06  E-value: 6.62e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L         29 YETLDTDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTdgLTNLDRYKGRCYHIEPVAGEENQYICYVAYPLDLF 108
Cdd:TIGR03326   7 YEPSDDDLVCTFRITPAEGVSIEDAAGRVASESSIGTWTTLQP--WKDPERYKDLSAKVYDIEEHGDGSIVRIAYPLGLF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        109 EEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRA 188
Cdd:TIGR03326  85 EEGNLPQLLSCIAGNIFGMKAVKGLRLLDFEFPAEFLRAFKGPQFGIEGVREILGIKDRPITATVPKPKVGLSTEEHAKV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        189 VYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEdMMKRAVFARELGVPIVMHD 268
Cdd:TIGR03326 165 AYELWSGGVDLLKDDENLTSQAFNRFEERVEKSLKVRDKVEAETGEKKSYLINITADVRE-MERRAELVADLGGEYVMVD 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        269 YLTGGFTANTTLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHSGTV-VGKLEGERDITLGFVD 347
Cdd:TIGR03326 244 IVVAGWSALQYVRERTEDLGLAIHAHRAMHAAFTRNPKHGISMFVLAKLYRLIGVDQLHTGTAgVGKLEGGNEDTKGIND 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        348 LLRddytekdrsrgiyftQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEAC 427
Cdd:TIGR03326 324 FLR---------------QDWHHIKPVFPVASGGLHPGLVPPLIDALGTDLVIQAGGGVHGHPDGTRAGAKALRAAIDAI 388
                         410       420       430
                  ....*....|....*....|....*....|....*
1RCO_L        428 VqarnEGRDLaregntiiREATKWSPELAAACEVW 462
Cdd:TIGR03326 389 I----EGISL--------EEKAKSVPELKKALEKW 411
 
Name Accession Description Interval E-value
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
1-475 0e+00

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


Pssm-ID: 176981  Cd Length: 475  Bit Score: 1068.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L         1 MSPQTETKASVGFKAGVKDYKLTYYTPEYETLDTDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTNLDRY 80
Cdd:CHL00040   1 MSPQTETKASVGFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        81 KGRCYHIEPVAGEENQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERD 160
Cdd:CHL00040  81 KGRCYRIEPVPGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYLKTFQGPPHGIQVERD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       161 KLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYL 240
Cdd:CHL00040 161 KLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       241 NATAGTCEDMMKRAVFARELGVPIVMHDYLTGGFTANTTLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRL 320
Cdd:CHL00040 241 NATAGTCEEMYKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRM 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       321 SGGDHIHSGTVVGKLEGERDITLGFVDLLRDDYTEKDRSRGIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVL 400
Cdd:CHL00040 321 SGGDHIHAGTVVGKLEGEREMTLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVL 400
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1RCO_L       401 QFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNTIIREATKWSPELAAACEVWKEIKFEFPAMDTV 475
Cdd:CHL00040 401 QFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEIIREAAKWSPELAAACEVWKEIKFEFETTDTL 475
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
23-473 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: 938.77  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       23 TYYTPEYETLDTDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTNLDRYKGRCYHIEPVAGEENQYICYVA 102
Cdd:cd08212   1 GYWTPDYQPKDTDILAAFRITPQPGVDPEEAAAAVAGESSTATWTVVWTDRLTALDRYKGKAYRVEPVPGEENQYFAYIA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      103 YPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSA 182
Cdd:cd08212  81 YPLDLFEEGSVANLTTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDRLNKYGRPLLGCTIKPKLGLSA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      183 KNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEDMMKRAVFARELGV 262
Cdd:cd08212 161 KNYGRVVYECLRGGLDFTKDDENINSQPFMRWRDRFLFVAEAVNKAQAETGEVKGHYLNVTAGTMEEMYKRAEFAKELGS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      263 PIVMHDYLTgGFTANTTLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHSGTVVGKLEGERDIT 342
Cdd:cd08212 241 PIIMHDLLT-GFTAIQSLAKWCRDNGMLLHLHRAGHATYDRQKNHGIHFRVLAKWLRLSGVDHIHAGTVVGKLEGDPLVT 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      343 LGFVDLLRDDYTEKDRSRGIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRV 422
Cdd:cd08212 320 LGFYDLLRDDYIEKDRSRGIFFTQDWASLPGVMPVASGGIHVGQMHQLIEIFGDDVVLQFGGGTIGHPWGIAAGATANRV 399
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
1RCO_L      423 ALEACVQARNEGRDLAREGNTIIREATKWSPELAAACEVWKEIKFEFPAMD 473
Cdd:cd08212 400 ALEAMVQARNEGRDLAREGPEILREAAKWSPELAAALETWKDIKFEFESTD 450
rbcL PRK04208
ribulose bisophosphate carboxylase; Reviewed
8-475 0e+00

ribulose bisophosphate carboxylase; Reviewed


Pssm-ID: 179787  Cd Length: 468  Bit Score: 882.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L         8 KASVGFKAGVKDYKLTYYTPEYETLDTDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTNLDRYKGRCYHI 87
Cdd:PRK04208   1 MAKERYDAGVKEYRQMYWDPDYTPKDTDLLACFRITPQEGVDPEEAAAAVAAESSTGTWTTVWTDLLTDLDKYKAKAYRI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        88 EPVAGEENQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGR 167
Cdd:PRK04208  81 EDVPGDDGSYYAFIAYPLDLFEEGSIPNLLASIAGNVFGFKAVKALRLEDIRFPVAYVKTFKGPPFGIQVERERLDKYGR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       168 PLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTC 247
Cdd:PRK04208 161 PLLGTTPKPKLGLSAKNYGRVVYEALRGGLDFTKDDENLNSQPFNRWRDRFLFVMEAIDKAEAETGERKGHYLNVTAPTM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       248 EDMMKRAVFARELGVPIVMHDYLTGGFTANTTLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIH 327
Cdd:PRK04208 241 EEMYKRAEFAKELGSPIVMIDVVTAGWTALQSLREWCRDNGLALHAHRAMHAAFTRNPNHGISFRVLAKLLRLIGVDHLH 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       328 SGTVVGKLEGERDITLGFVDLLRDDYTEKDRSRGIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTL 407
Cdd:PRK04208 321 TGTVVGKLEGDRAEVLGYYDILREDFVPEDRSRGIFFDQDWGSIKPVFPVASGGIHPGHMPALLDIFGDDVVLQFGGGTH 400
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1RCO_L       408 GHPWGNAPGAVANRVALEACVQARNEGRDLAREGNTIIREATKWSPELAAACEVWKEIKFEFPAMDTV 475
Cdd:PRK04208 401 GHPDGTAAGATANRVALEACVEARNEGRDIEKEGPDILEEAAKWSPELAAALEKWGEIKFEFDTVDTL 468
RuBisCO_large_I_II_III cd08206
Ribulose bisphosphate carboxylase large chain, Form I,II,III; Ribulose bisphosphate ...
34-462 0e+00

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: 731.34  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       34 TDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTNLDRYKGRCYHIEPVAgeENQYICYVAYPLDLFEEGSV 113
Cdd:cd08206   1 TDLLAAFRMTPAEGVDPEEAAAAVAAESSTGTWTTVWTDRLTATERLKAKVYRIDPVP--DGQYIAKIAYPLDLFEEGSV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      114 TNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECL 193
Cdd:cd08206  79 PNLLTSIIGNVFGMKAVKALRLEDFRFPPAYLKTFDGPSFGIQGEREILGKYGRPLLGTIVKPKLGLSPKEYARVVYEAL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      194 RGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEDMMKRAVFARELGVPIVMHDYLTGG 273
Cdd:cd08206 159 RGGLDFVKDDENQNSQPFMRFEDRILFVAEAMDKAEAETGEAKGHYLNITADTPEEMIKRAEFAKELGSVIVMVDGVTAG 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      274 FTANTTLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDY 353
Cdd:cd08206 239 WTAIQSARRWCPDNGLALHAHRAGHAAFTRQKNHGISMRVLAKLARLIGVDHIHTGTVVGKLEGDPSEVKGIADMLREDE 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      354 TEKDRSRgIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARne 433
Cdd:cd08206 319 VEGDLSR-IFFNQDWGGMKPVFPVASGGLHPGRMPALIEILGDDVILQFGGGTHGHPDGPAAGAKANRQALEAWVQGR-- 395
                       410       420
                ....*....|....*....|....*....
1RCO_L      434 grdlaregntIIREATKWSPELAAACEVW 462
Cdd:cd08206 396 ----------ILREYAKTHKELAAALEKW 414
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
14-468 0e+00

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


Pssm-ID: 224763  Cd Length: 429  Bit Score: 618.99  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       14 KAGVKDYkLTYYTPEYETLDTDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTNLDRYKGRCYHIEPVAGE 93
Cdd:COG1850   1 KAGVQKY-RDYVDPNYRPKDTDLIATFRITPASGVSTEEAAAAIAGESSTGTWTTVPTDKPELADRLKAKVYDVEEVPGE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       94 --ENQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLG 171
Cdd:COG1850  80 dgQKRAIVKIAYPLDLFEEGSLPALLTSVAGNVFGMKALKGLRLEDLRFPKEFLKAFKGPQFGVEGVRDLLGVKGRPLLG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      172 CTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGtCEDMM 251
Cdd:COG1850 160 TIVKPKLGLSPEEYAELAYELLSGGVDFIKDDENLTSPPFNRFEERVAKIMEAIDKAEAETGEKKMYAVNITAP-CEEMM 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      252 KRAVFARELGVPIVMHDYLTGGFTANTTLSHYcRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHSGTV 331
Cdd:COG1850 239 RRAELAAELGANYVMIDIVVTGFTALQYLRED-EDIGLAIHAHRAMHAAFTRSPNHGISFLVLAKLLRLIGVDQLHIGTV 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      332 VGKLEGErditlgfvdllRDDYTEKDRSrgIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPW 411
Cdd:COG1850 318 VGKLEGD-----------REDYVESDKE--FFFEQDWAHIKPVFPVASGGIHPGMMPELVRIFGKDLVIQAGGGVHGHPD 384
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
1RCO_L      412 GNAPGAVANRVALEACVQARNegrdlaregntiIREATKWSPELAAACEVWKEIKFE 468
Cdd:COG1850 385 GPAAGARAVRQAIEAAVEGIP------------LREYAKWHPELAAALEKWGEIKAA 429
RuBisCO_large cd08148
Ribulose bisphosphate carboxylase large chain; Ribulose bisphosphate carboxylase (Rubisco) ...
36-423 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.


Pssm-ID: 173969  Cd Length: 366  Bit Score: 531.62  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       36 ILAAFRVSPQPgVPPEEAGAAVAAESSTGTWTTVWTdGLTNLDRYKGRCYHIEPVAgeeNQYICYVAYPLDLFEEGSVTN 115
Cdd:cd08148   1 VLATYRVHPEA-TPPEKAAEAIAAESSTGTWTEVPT-TQEQLRRVKGRVYSVEELG---KRYIVKIAYPVELFEPGNIPQ 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      116 MFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRG 195
Cdd:cd08148  76 ILTVTAGNLFGLGALEAVRLEDLEFPEEYKKLFPGPKFGIDGIRKLLGVYGRPLVGTIIKPKLGLNPKYTAEAAYAAALG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      196 GLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTcEDMMKRAVFARELGVPIVMHDYLTGGFT 275
Cdd:cd08148 156 GLDLIKDDETLTDQPFCPLRDRITEVAAALDRVQEETGEKKLYAVNVTAGT-FEIIERAERALELGANMLMVDVLTAGFS 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      276 ANTTLSHYCRdNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDyte 355
Cdd:cd08148 235 ALQALAEDFE-IDLPIHVHRAMHGAVTRSKFHGISMLVLAKLLRMAGGDFIHTGTVVGKMALEREEALGIADALTDD--- 310
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1RCO_L      356 kdrsrgiyftqsWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVA 423
Cdd:cd08148 311 ------------WAGFKRVFPVASGGIHPGLVPGILRDFGIDVILQAGGGIHGHPDGTVAGARAMRQA 366
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
155-462 6.53e-167

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: 425422  Cd Length: 292  Bit Score: 471.84  E-value: 6.53e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        155 IQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGE 234
Cdd:pfam00016   1 IAVERRVLNKYGRPILGTIIKPKLGLSPKNYARAVYEFLLGGLDFIKDDENINSQPFMPWRDRFLFVAEAIDRAQDETGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        235 IKGHYLNATAGTCEDMMKRAVFARELGVPIVMHDYLTGGFTANTTLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVL 314
Cdd:pfam00016  81 AKGHYLNITADDMEEMYRRAEFAKETGGVAVMVDGLVIGPTAITTLRRWFRDNGVILHYHRAGHGAVTRQSKHGISFRVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        315 AKALRLSGGDHIHSGTV-VGKLEGERDitlgfvDLLRDDYTEKDRSRGIYFTQSWVSTPGVLPVASGGIHVWHMPALTEI 393
Cdd:pfam00016 161 AKMARLAGADHLHTGTMgVGKLEGDPS------DTLRAYMLEEDRARGPFFDQDWGGMPAVMPVASGGIHAGQMPGLFDN 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        394 FGD-DSVLQFGGGTLGHPWGNAPGAVANRVALEACVqarnEGRDLAREGntiireatKWSPELAAACEVW 462
Cdd:pfam00016 235 LGDsDVILQFGGGTFGHPDGPAAGAKANRQALEAWV----EGRDLEEYA--------KEHPELARAFESW 292
RuBisCO_large_III cd08213
Ribulose bisphosphate carboxylase large chain, Form III; Ribulose bisphosphate carboxylase ...
34-462 5.06e-140

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: 408.32  E-value: 5.06e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       34 TDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTNLDRYKGRCYHIEPVAGeenQYICYVAYPLDLFEEGSV 113
Cdd:cd08213   1 DDLIAVFRIEPAEGISIEEAAGRVASESSIGTWTTLATLYPERAEKLKAKAYYFDGLGG---SYIVKVAYPLELFEEGNM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      114 TNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECL 193
Cdd:cd08213  78 PQLLSSIAGNIFGMKAVKNLRLEDIYFPESYLREFKGPQFGIEGVREILGIKDRPLLGTVPKPKVGLSPEEHAEVAYEAL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      194 RGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAgTCEDMMKRAVFARELGVPIVMHDYLTGG 273
Cdd:cd08213 158 VGGVDLVKDDENLTSQPFNRFEERAKESLKARDKAEAETGERKAYLANITA-PVREMERRAELVADLGGKYVMIDVVVAG 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      274 FTANTTLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDY 353
Cdd:cd08213 237 WSALQYLRDLAEDYGLAIHAHRAMHAAFTRNPRHGISMLVLAKLYRLIGVDQLHIGTAVGKMEGDKEEVLRIADILREQK 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      354 TEKDrSRGIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVqarnE 433
Cdd:cd08213 317 YKPD-EEDFHLAQDWGGIKPVFPVASGGLHPGLVPDVIDILGKDIVIQVGGGVHGHPDGTRAGAKAVRQAIEAAL----E 391
                       410       420
                ....*....|....*....|....*....
1RCO_L      434 GRDLaregntiiREATKWSPELAAACEVW 462
Cdd:cd08213 392 GISL--------DEYAKDHKELARALEKW 412
rubisco_III TIGR03326
ribulose bisphosphate carboxylase, type III; Members of this protein family are the archaeal, ...
29-462 6.62e-115

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: 344.06  E-value: 6.62e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L         29 YETLDTDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTdgLTNLDRYKGRCYHIEPVAGEENQYICYVAYPLDLF 108
Cdd:TIGR03326   7 YEPSDDDLVCTFRITPAEGVSIEDAAGRVASESSIGTWTTLQP--WKDPERYKDLSAKVYDIEEHGDGSIVRIAYPLGLF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        109 EEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRA 188
Cdd:TIGR03326  85 EEGNLPQLLSCIAGNIFGMKAVKGLRLLDFEFPAEFLRAFKGPQFGIEGVREILGIKDRPITATVPKPKVGLSTEEHAKV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        189 VYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEdMMKRAVFARELGVPIVMHD 268
Cdd:TIGR03326 165 AYELWSGGVDLLKDDENLTSQAFNRFEERVEKSLKVRDKVEAETGEKKSYLINITADVRE-MERRAELVADLGGEYVMVD 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        269 YLTGGFTANTTLSHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHSGTV-VGKLEGERDITLGFVD 347
Cdd:TIGR03326 244 IVVAGWSALQYVRERTEDLGLAIHAHRAMHAAFTRNPKHGISMFVLAKLYRLIGVDQLHTGTAgVGKLEGGNEDTKGIND 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        348 LLRddytekdrsrgiyftQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEAC 427
Cdd:TIGR03326 324 FLR---------------QDWHHIKPVFPVASGGLHPGLVPPLIDALGTDLVIQAGGGVHGHPDGTRAGAKALRAAIDAI 388
                         410       420       430
                  ....*....|....*....|....*....|....*
1RCO_L        428 VqarnEGRDLaregntiiREATKWSPELAAACEVW 462
Cdd:TIGR03326 389 I----EGISL--------EEKAKSVPELKKALEKW 411
RuBisCO_IV_RLP cd08205
Ribulose bisphosphate carboxylase like proteins, Rubisco-Form IV; Ribulose bisphosphate ...
62-423 3.29e-63

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: 209.31  E-value: 3.29e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       62 STGTWTTVWTDGLTNLDRYKGRCYHIEPVAGEENQYICY---VAYPLDLFEeGSVTNMFTSIVGNVFGfkaLRALRLEDL 138
Cdd:cd08205  26 TVGTWTELPGETEEIRERHVGRVESIEELEESEGKYGRArvtISYPLDNFG-GDLPQLLNTLFGNLSL---LPGIKLVDL 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      139 RIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRF 218
Cdd:cd08205 102 ELPDSLLAAFPGPRFGIEGLRRLLGVHDRPLLGTIIKPSIGLSPEELAELAYELALGGIDLIKDDELLADQPYAPFEERV 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      219 LFCAEALYKAQAETGEIKGHYLNATAGTcEDMMKRAVFARELGVPIVMHDYLTGGFTANTTLShycRDNGLLLHIHRAMH 298
Cdd:cd08205 182 RACMEAVRRANEETGRKTLYAPNITGDP-DELRRRADRAVEAGANALLINPNLVGLDALRALA---EDPDLPIMAHPAFA 257
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      299 AVIDRQKNHGMHFRVLAKALRLSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDytekdrsrgiyftqsWVSTPGVLPVA 378
Cdd:cd08205 258 GALSRSPDYGSHFLLLGKLMRLAGADAVIFPGPGGRFPFSREECLAIARACRRP---------------LGGIKPALPVP 322
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
1RCO_L      379 SGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVA 423
Cdd:cd08205 323 SGGMHPGRVPELYRDYGPDVILLAGGGILGHPDGAAAGVRAFRQA 367
PRK13475 PRK13475
ribulose-bisphosphate carboxylase;
36-460 2.66e-59

ribulose-bisphosphate carboxylase;


Pssm-ID: 184072  Cd Length: 443  Bit Score: 201.10  E-value: 2.66e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        36 ILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWT-DGLTnldryKG---RCYHIEPVAGeenqyICYVAYPLDLFE-- 109
Cdd:PRK13475  24 ILCAYKMKPKAGHGYLEAAAHFAAESSTGTNVEVSTtDDFT-----RGvdaLVYEIDEARE-----LMKIAYPVELFDrn 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       110 ----EGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIqverDKLNKY-GRP------LLGCTIKPKL 178
Cdd:PRK13475  94 iidgRAMIVSFLTLTIGNNQGMGDVEYAKMHDFYVPPRYLELFDGPSTDI----SDLWRVlGRPvkdggyIAGTIIKPKL 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       179 GLSAKNYGRAVYECLRGGlDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEDMMKRAVFAR 258
Cdd:PRK13475 170 GLRPEPFAEACYDFWLGG-DFIKNDEPQGNQVFAPLKKTVPLVADAMKRAQDETGEAKLFSANITADDHYEMIARGEYIL 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       259 ELGVPIVMH-----DYLTGGFTANTTlshyCRDN--GLLLHIHRAMHAVIDRQKN-HGMHFRVLAKALRLSGGDHIHSGT 330
Cdd:PRK13475 249 ETFGENADHvaflvDGYVAGPGAVTT----ARRQypDQYLHYHRAGHGAVTSPSSkRGYTAFVLSKMARLQGASGIHTGT 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       331 V-VGKLEGERDitlgfvDLLRDDYTEKDRSRGIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVLQ-FGGGTLG 408
Cdd:PRK13475 325 MgYGKMEGEAD------DRVIAYMIERDSAQGPFYHQEWYGMKPTTPIISGGMNALRLPGFFDNLGHGNVINtAGGGAFG 398
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
1RCO_L       409 HPWGNAPGAVANRVALEACVQarneGRDlaregntiIREATKWSPELAAACE 460
Cdd:PRK13475 399 HIDGPAAGAKSLRQAYDCWKA----GAD--------PIEYAKEHKEFARAFE 438
RuBisCO_large_II cd08211
Ribulose bisphosphate carboxylase large chain, Form II; Ribulose bisphosphate carboxylase ...
36-432 4.76e-58

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: 197.72  E-value: 4.76e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       36 ILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGltnlDRYKG---RCYHIEpvagEENQyICYVAYPLDLFE--- 109
Cdd:cd08211  23 VLVAYIMKPKAGYGYLATAAHFAAESSTGTNVEVSTTD----DFTRGvdaLVYEID----EARE-LMKIAYPVELFDrnl 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      110 ---EGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKY---GRPLLGCTIKPKLGLSAK 183
Cdd:cd08211  94 tdgRAMVASFLTLIIGNNQGMGDVEYLKMHDFYVPESMLELFDGPSVNISDMWKVLGRPevdGGYIAGTIIKPKLGLRPK 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      184 NYGRAVYECLRGGlDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEDMMKRAVFARELGVP 263
Cdd:cd08211 174 PFAEACYAFWLGG-DFIKNDEPQANQPFCPLKKVIPLVADAMRRAQDETGEAKLFSANITADDPDEMIARGEYILEAFGP 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      264 IVMH-----DYLTGGFTANTTLSHYCRDNglLLHIHRAMHAVIDRQKNH-GMHFRVLAKALRLSGGDHIHSGTV-VGKLE 336
Cdd:cd08211 253 NAGHvaflvDGYVAGPAAVTTARRRFPDQ--FLHYHRAGHGAVTSPQSKrGYTAFVLSKMARLQGASGIHTGTMgFGKME 330
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      337 GE-RDITLGFVdllrddyTEKDRSRGIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGDDSVLQ-FGGGTLGHPWGNA 414
Cdd:cd08211 331 GEsSDKVIAYM-------IERDEAQGPLFNQKWYGMKPTTPIISGGMNALRLPGFFENLGNGNVILtAGGGSFGHIDGPA 403
                       410
                ....*....|....*...
1RCO_L      415 PGAVANRVALEACVQARN 432
Cdd:cd08211 404 AGAKSLRQAYDAWKQGVD 421
RuBisCO_large_N pfam02788
Ribulose bisphosphate carboxylase large chain, N-terminal domain; The N-terminal domain of ...
23-144 1.15e-49

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: 165.46  E-value: 1.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L         23 TYYTPEYETLDTDILAAFRVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTNLDRYKGRCYHIEPVAGEenQYICYVA 102
Cdd:pfam02788   1 DYVDLDYEPKDTDLLCAFRIEPAAGVSPEEAAAHVAAESSTGTWTEVWTLDDTFTKKLKAKVYEIDEVPGG--SYIVKIA 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
1RCO_L        103 YPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPVAY 144
Cdd:pfam02788  79 YPLDLFEEGSIPQLLSSIAGNIFGMKAVKALRLEDIRFPPAY 120
RLP_NonPhot cd08207
Ribulose bisphosphate carboxylase like proteins from nonphototrophic bacteria; Ribulose ...
62-458 3.65e-48

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: 170.57  E-value: 3.65e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       62 STGTWTTVWTDGLTNLDRYKGRCYHIEPVAGEENQYI-------CY------VAYPLDLFEEgSVTNMFTSIVGNVFGFK 128
Cdd:cd08207  26 SSGTFIALPGETDELKERSAARVESIEELETAAQPSLprrasggPYtrarvtISFPLDNIGT-SLPNLLATVAGNLFELR 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      129 ALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNS 208
Cdd:cd08207 105 ELSGLRLVDLGLPDEFAAAFPGPAFGIAGTRRLTGVEDRPLIGTIIKPSVGLTPEETAALVRQLAAAGIDFIKDDELLAN 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      209 QPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATaGTCEDMMKRAVFARELGVPIVMHDYLTGGFTANTTLShycRDNG 288
Cdd:cd08207 185 PPYSPLDERVRAVMRVINDHAQRTGRKVMYAFNIT-DDIDEMRRNHDLVVEAGGTCVMVSLNSVGLSGLAALR---RHSQ 260
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      289 LLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHsgtvvgklegerditlgfVDLLRDDYTEKDRS--RGIYFTQ 366
Cdd:cd08207 261 LPIHGHRNGWGMLTRSPALGISFQAYQKLWRLAGVDHLH------------------VNGLASKFWESDDSviESARACL 322
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      367 SWVSTPG--VLPVASGGIHVWHMPALTEIFGDDSVLQF-GGGTLGHPWGNAPGAVANRVALEACVQARNegrdlaregnt 443
Cdd:cd08207 323 TPLGGPDdaAMPVFSSGQWGGQAPPTYRRLGSVDLLYLaGGGIMAHPDGPAAGVRSLRQAWEAAVAGVP----------- 391
                       410
                ....*....|....*
1RCO_L      444 iIREATKWSPELAAA 458
Cdd:cd08207 392 -LEEYAKTHPELARA 405
RLP_DK-MTP-1-P-enolase cd08209
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Ribulose bisphosphate carboxylase like ...
64-462 8.03e-40

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: 147.85  E-value: 8.03e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       64 GTWTTVWTDGLTNLDRYKGRCYHIEPvaGEENQYICYVAYPLdlfeeGSVTNMFTSIVGNVFGFKALR-ALRLEDLRIPV 142
Cdd:cd08209  27 GSWTDLPALRQAQLQKHLGEVVSVEE--LEEGRGVITIAYPL-----INVSGDIPALLTTIFGKLSLDgKIKLVDLRLPE 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      143 AYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCA 222
Cdd:cd08209 100 EFGRAFPGPKFGIEGIRQRLGVHDRPLLMSIFKGVLGLDLDDLAEQLREQALGGVDLIKDDEILFDNPLAPALERIRACR 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      223 EALYKAQAETGEIKGHYLNATaGTCEDMMKRAVFARELGVPIVMHDYLTGGFTANTTLShycRDNGLLLHI--HRAMHAV 300
Cdd:cd08209 180 PVLQEVYEQTGRRTLYAVNLT-GPVFTLKEKARRLVEAGANALLFNVFAYGLDVLEALA---SDPEINVPIfaHPAFAGA 255
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      301 IDRQKNHGM-HFRVLAKALRLSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDYTEKdrsrgiyftqswvstpGVLPVAS 379
Cdd:cd08209 256 LYGSPDYGIaASVLLGTLMRLAGADAVLFPSPYGSVALSKEEALAIAEALRRGGAFK----------------GVFPVPS 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      380 GGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNegrdlaregntiIREATKWSPELAAAC 459
Cdd:cd08209 320 AGIHPGLVPQLLRDFGTDVILNAGGGIHGHPDGAAAGVRAFREAIDAVLAGES------------LEPAAIPDGPLKSAL 387

                ...
1RCO_L      460 EVW 462
Cdd:cd08209 388 DKW 390
mtnW PRK09549
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Reviewed
64-462 4.73e-36

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


Pssm-ID: 236560  Cd Length: 407  Bit Score: 137.83  E-value: 4.73e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        64 GTWTTVWTDGLTNLDRYKGRCYHIEPVAGEEN----QYICYVAYPldlfeEGSVTNMFTSIVGNVFGFKALRA-LRLEDL 138
Cdd:PRK09549  31 GSWTDLPHLEQEQLKKHKGNVVHVEELEEHERkgvkRGIIKIAYP-----LANFSPDLPAILTTTFGKLSLDGeVKLIDL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       139 RIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRF 218
Cdd:PRK09549 106 TFSDELKRHFPGPKFGIDGIRNLLGVHDRPLLMSIFKGVIGRDLDYLKEQLRDQALGGVDLVKDDEILFENALTPFEKRI 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       219 LFCAEALYKAQAETGEIKGHYLNATAGTCE--DMMKRAVfarELGVPIVMHDYLTGGFTANTTLShycRDNGLLLHI--H 294
Cdd:PRK09549 186 VAGKEVLQEVYETTGHKTLYAVNLTGRTFElkEKAKRAA---EAGADALLFNVFAYGLDVLQSLA---EDPEIPVPImaH 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       295 RAMHAVIDRQKNHGM-HFRVLAKALRLSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDYTEKDRSrgiyftqswvstpg 373
Cdd:PRK09549 260 PAVSGAYTPSPLYGIsSPLLLGKLLRYAGADFSLFPSPYGSVALEKEEALAIAKELTEDDDPFKRS-------------- 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       374 vLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNegrdlaregntiIREATKWSP 453
Cdd:PRK09549 326 -FPVPSAGIHPGLVPLLIRDFGKDVVINAGGGIHGHPNGAQGGGKAFRAAIDAVLQGKP------------LHEAAEDDE 392

                 ....*....
1RCO_L       454 ELAAACEVW 462
Cdd:PRK09549 393 NLHSALDIW 401
RLP_RrRLP cd08210
Ribulose bisphosphate carboxylase like proteins (RLPs) similar to R.rubrum RLP; RLP from ...
77-410 9.91e-28

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: 113.49  E-value: 9.91e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L       77 LDRYKGRCYHIEPVagEENQYICYVAYPLDlfeegSVTNMFTSIVGNVFGFKAL-RALRLEDLRIPVAYVKTFQGPPHGI 155
Cdd:cd08210  42 RDNIVGRVESLEPA--GEGSYRARISYSVD-----TAGGELTQLLNVLFGNSSLqPGIRLVDFELPPSLLRRFPGPRFGI 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      156 QVERDKLNKYGRPLLGCTIKPkLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGei 235
Cdd:cd08210 115 AGLRALLGIPERPLLCSALKP-QGLSAAELAELAYAFALGGIDIIKDDHGLADQPFAPFEERVKACQEAVAEANAETG-- 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      236 kGH--YLNATAGTCEDMMKRAVFARELGVPIVMhdyLTGGFTANTTLSHYCRDNGLLLHIHRAMHAVIDRQKNHGM-HFR 312
Cdd:cd08210 192 -GRtlYAPNVTGPPTQLLERARFAKEAGAGGVL---IAPGLTGLDTFRELAEDFDFLPILAHPAFAGAFVSSGDGIsHAL 267
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      313 VLAKALRLSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDytekdrsrgiyftqsWVSTPGVLPVASGGIHVWHMPALTE 392
Cdd:cd08210 268 LFGTLFRLAGADAVIFPNYGGRFGFSREECQAIADACRRP---------------MGGLKPILPAPGGGMSVERAPEMVE 332
                       330
                ....*....|....*...
1RCO_L      393 IFGDDSVLQFGGGTLGHP 410
Cdd:cd08210 333 LYGPDVMLLIGGSLLRAG 350
RLP_Photo cd08208
Ribulose bisphosphate carboxylase like proteins from phototrophic bacteria; Ribulose ...
113-458 6.30e-25

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: 106.52  E-value: 6.30e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      113 VTNMFTSIVGN-VFGFKALRALRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYE 191
Cdd:cd08208 105 IPNLLSAVCGEgTFFSPGVPVVKLMDIHFPETYLADFEGPKFGIAGLRERLQAHDRPIFFGVIKPNIGLPPGEFAELGYQ 184
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      192 CLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATaGTCEDMMKRAVFARELGVPIVMHDYLT 271
Cdd:cd08208 185 SWLGGLDIAKDDEMLADVDWCPLEERAALLGKARRRAEAETGVPKIYLANIT-DEVDRLMELHDVAVRNGANALLINAMP 263
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      272 GGFTANTTLSHYCRdngLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIhsgtvvgklegerdITLGFVDllRD 351
Cdd:cd08208 264 VGLSAVRMLRKHAQ---VPLIAHFPFIASFSRLEKYGIHSRVMTKLQRLAGLDVV--------------IMPGFGP--RM 324
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L      352 DYTEKD-RSRGIYFTQSWVSTPGVLPVASGGIHVWHMPALTEIFGD-DSVLQFGGGTLGHPWGNAPGAVANRVALEACVQ 429
Cdd:cd08208 325 MTPEEEvLECVIACLEPMGPIKPCLPVPGGSDSALTLQTVYEKVGNvDFGFVPGRGVFGHPMGPKAGAKSIRQAWEAIEA 404
                       330       340
                ....*....|....*....|....*....
1RCO_L      430 ARNegrdlaregntiIREATKWSPELAAA 458
Cdd:cd08208 405 GIS------------IETWAETHPELQAA 421
salvage_mtnW TIGR03332
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Members of this family are the methionine ...
62-462 3.66e-24

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: 104.14  E-value: 3.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L         62 STGTWTTVWTDGLTNLDRYKGRCYHIEPVAGEE----------NQYICYVAYPLDLFeegsvTNMFTSIVGNVFGFKALR 131
Cdd:TIGR03332  28 TIGSWTDLPLLKQEQLKKHKGRVVHVEELAESEhtnsylrkkvKRAIIKIAYPELNF-----SPDLPALLTTTFGKLSLD 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        132 A-LRLEDLRIPVAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQP 210
Cdd:TIGR03332 103 GeVKLIDLEFSDEFKRHFPGPKFGIDGIRKLLGVHERPLLMSIFKGMIGRDLGYLKEQLRQQALGGVDLVKDDEILFETG 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        211 FMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCeDMMKRAVFARELGVPIVMHDYLTGGFTantTLSHYCRDNGLL 290
Cdd:TIGR03332 183 LAPFEKRITEGKEVLQEVYEQTGHKTLYAVNLTGRTF-DLKDKAKRAAELGADVLLFNVFAYGLD---VLQSLAEDDEIP 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        291 LHI--HRAMHAVIDRQKNHGM-HFRVLAKALRLSGGDHIHSGTVVGKLEGERDITLGFVDLLRDDytekdrsrGIYFTQS 367
Cdd:TIGR03332 259 VPImaHPAVSGAYTSSPFYGFsHSLLLGKLLRYAGADFSLFPSPYGSVALEREDALAISKELTED--------DAPFKKT 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1RCO_L        368 WvstpgvlPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNegrdlaregntiIRE 447
Cdd:TIGR03332 331 F-------AVPSAGIHPGMVPLIMRDFGIDHIINAGGGIHGHPNGAQGGGRAFRAAIDAVLEAKP------------LHE 391
                         410
                  ....*....|....*
1RCO_L        448 ATKWSPELAAACEVW 462
Cdd:TIGR03332 392 KAADDIDLKLALDKW 406
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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