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Conserved domains on  [gi|74039499|gb|AAZ94822|]
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ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit, partial (plastid) [Gigartina grandifida]

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) ...
9-451 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: 941.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499    9 KETDVLALFRVSPQPGVDPVEASAAVAGESSTATWTVVWTDLLTACDLYRAKAYKVDLVPNTTDQYFAYIAYDIDLFEEG 88
Cdd:CHL00040  32 KDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYRIEPVPGEENQYIAYVAYPLDLFEEG 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   89 SIANLTASIIGNVFGFKAVKALRLEDMRLPVAYLKTFQGPATGIICERERMDKFGRPFLGATVKPKLGLSGKNYGRVVYE 168
Cdd:CHL00040 112 SVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYLKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYE 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  169 GLKGGLDFLKDDENINSQPFMRWKERYLYSMEGVNRSIAASGETKGHYLNVTAATMEEMYERAEFAKQLGSIIIMIDLVI 248
Cdd:CHL00040 192 CLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMYKRAVFARELGVPIVMHDYLT 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  249 -GYTAIQTMAVWSRKNDMILHLHRAGNSTYSRQKIHGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPLMIKGFYNTLLL 327
Cdd:CHL00040 272 gGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHAGTVVGKLEGEREMTLGFVDLLRD 351
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  328 PYLEVNLPQGIFFEQDWASLRKVTPVASGGIHCGQMHQLLDYLGNDVVLQFGGGTIGHPDGIQAGATANRVALESMVIAR 407
Cdd:CHL00040 352 DFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQAR 431
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 74039499  408 NEGRDFVAEGPQILQDAAKTCGPLQTALDLWKDITFNYTSTDTA 451
Cdd:CHL00040 432 NEGRDLAREGNEIIREAAKWSPELAAACEVWKEIKFEFETTDTL 475
 
Name Accession Description Interval E-value
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
9-451 0e+00

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


Pssm-ID: 176981  Cd Length: 475  Bit Score: 941.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499    9 KETDVLALFRVSPQPGVDPVEASAAVAGESSTATWTVVWTDLLTACDLYRAKAYKVDLVPNTTDQYFAYIAYDIDLFEEG 88
Cdd:CHL00040  32 KDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYRIEPVPGEENQYIAYVAYPLDLFEEG 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   89 SIANLTASIIGNVFGFKAVKALRLEDMRLPVAYLKTFQGPATGIICERERMDKFGRPFLGATVKPKLGLSGKNYGRVVYE 168
Cdd:CHL00040 112 SVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYLKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYE 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  169 GLKGGLDFLKDDENINSQPFMRWKERYLYSMEGVNRSIAASGETKGHYLNVTAATMEEMYERAEFAKQLGSIIIMIDLVI 248
Cdd:CHL00040 192 CLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMYKRAVFARELGVPIVMHDYLT 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  249 -GYTAIQTMAVWSRKNDMILHLHRAGNSTYSRQKIHGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPLMIKGFYNTLLL 327
Cdd:CHL00040 272 gGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHAGTVVGKLEGEREMTLGFVDLLRD 351
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  328 PYLEVNLPQGIFFEQDWASLRKVTPVASGGIHCGQMHQLLDYLGNDVVLQFGGGTIGHPDGIQAGATANRVALESMVIAR 407
Cdd:CHL00040 352 DFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQAR 431
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 74039499  408 NEGRDFVAEGPQILQDAAKTCGPLQTALDLWKDITFNYTSTDTA 451
Cdd:CHL00040 432 NEGRDLAREGNEIIREAAKWSPELAAACEVWKEIKFEFETTDTL 475
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
9-449 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: 892.93  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   9 KETDVLALFRVSPQPGVDPVEASAAVAGESSTATWTVVWTDLLTACDLYRAKAYKVDLVPNTTDQYFAYIAYDIDLFEEG 88
Cdd:cd08212  10 KDTDILAAFRITPQPGVDPEEAAAAVAGESSTATWTVVWTDRLTALDRYKGKAYRVEPVPGEENQYFAYIAYPLDLFEEG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  89 SIANLTASIIGNVFGFKAVKALRLEDMRLPVAYLKTFQGPATGIICERERMDKFGRPFLGATVKPKLGLSGKNYGRVVYE 168
Cdd:cd08212  90 SVANLTTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDRLNKYGRPLLGCTIKPKLGLSAKNYGRVVYE 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 169 GLKGGLDFLKDDENINSQPFMRWKERYLYSMEGVNRSIAASGETKGHYLNVTAATMEEMYERAEFAKQLGSIIIMIDLVI 248
Cdd:cd08212 170 CLRGGLDFTKDDENINSQPFMRWRDRFLFVAEAVNKAQAETGEVKGHYLNVTAGTMEEMYKRAEFAKELGSPIIMHDLLT 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 249 GYTAIQTMAVWSRKNDMILHLHRAGNSTYSRQKIHGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPLMIKGFYNTLLLP 328
Cdd:cd08212 250 GFTAIQSLAKWCRDNGMLLHLHRAGHATYDRQKNHGIHFRVLAKWLRLSGVDHIHAGTVVGKLEGDPLVTLGFYDLLRDD 329
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 329 YLEVNLPQGIFFEQDWASLRKVTPVASGGIHCGQMHQLLDYLGNDVVLQFGGGTIGHPDGIQAGATANRVALESMVIARN 408
Cdd:cd08212 330 YIEKDRSRGIFFTQDWASLPGVMPVASGGIHVGQMHQLIEIFGDDVVLQFGGGTIGHPWGIAAGATANRVALEAMVQARN 409
                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 74039499 409 EGRDFVAEGPQILQDAAKTCGPLQTALDLWKDITFNYTSTD 449
Cdd:cd08212 410 EGRDLAREGPEILREAAKWSPELAAALETWKDIKFEFESTD 450
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
9-443 8.67e-179

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


Pssm-ID: 441455  Cd Length: 417  Bit Score: 506.24  E-value: 8.67e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   9 KETDVLALFRVSPQPGVDPVEASAAVAGESSTATWTVVWTDLLTACDLYRAKAYKVDLVPNTT---DQYFAYIAYDIDLF 85
Cdd:COG1850  10 DDDDILATYRITPETGVDPEEAAAAIAGEQSTGTWTEVPTETDELRERLAARVYSIEELPEVGggyRRALVTIAYPLENF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  86 EeGSIANLTASIIGNVFGFKAVKALRLEDMRLPVAYLKTFQGPATGIICERERMDKFGRPFLGATVKPKLGLSGKNYGRV 165
Cdd:COG1850  90 G-GNLPNLLSTVAGNLFGLKAVSGLRLLDLEFPESFLAAFPGPKFGIEGTRELLGVYDRPLLGTIIKPKVGLSPEETAEL 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 166 VYEGLKGGLDFLKDDENINSQPFMRWKERYLYSMEGVNRSIAASGETKGHYLNVTaATMEEMYERAEFAKQLGSIIIMID 245
Cdd:COG1850 169 VYELALGGVDFIKDDENLADQPFCPFEDRVRAVMEAIDRAEEETGEKKMYAFNIT-ADTDEMLRRADLAVELGANAVMVD 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 246 -LVIGYTAIQTMAvwSRKNDMILHLHRAGNSTYSRQKIHGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPLMIKGFYNT 324
Cdd:COG1850 248 vNTVGLSAVQTLR--EEHIGLPIHAHRAGHGAFTRSPLHGISMRVLAKLWRLAGADHLHVGTPVGKMEGDDEEVLAIADA 325
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 325 LLlpylevnlpqgiffeQDWASLRKVTPVASGGIHCGQMHQLLDYLGNDVVLQFGGGTIGHPDGIQAGATANRVALESMV 404
Cdd:COG1850 326 LL---------------QPWGGLKPVFPVPSGGQHPGQVPELYDALGTDLILQAGGGIHGHPDGPAAGARALRQAWEAAV 390
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 74039499 405 iarnEGRDfvaegpqiLQDAAKTCGPLQTALDLWKDITF 443
Cdd:COG1850 391 ----AGIP--------LEEYAKTHPELAAALEKWGKKAP 417
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
132-438 1.30e-156

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: 445.27  E-value: 1.30e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   132 IICERERMDKFGRPFLGATVKPKLGLSGKNYGRVVYEGLKGGLDFLKDDENINSQPFMRWKERYLYSMEGVNRSIAASGE 211
Cdd:pfam00016   1 IAVERRVLNKYGRPILGTIIKPKLGLSPKNYARAVYEFLLGGLDFIKDDENINSQPFMPWRDRFLFVAEAIDRAQDETGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   212 TKGHYLNVTAATMEEMYERAEFAKQLGSIIIMID-LVIGYTAIQTMAVWSRKNDMILHLHRAGNSTYSRQKIHGMNFRVI 290
Cdd:pfam00016  81 AKGHYLNITADDMEEMYRRAEFAKETGGVAVMVDgLVIGPTAITTLRRWFRDNGVILHYHRAGHGAVTRQSKHGISFRVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   291 CKWMRMAGVDHIHAGTV-VGKLEGDPLmikgfyNTLLLPYLEVNLPQGIFFEQDWASLRKVTPVASGGIHCGQMHQLLDY 369
Cdd:pfam00016 161 AKMARLAGADHLHTGTMgVGKLEGDPS------DTLRAYMLEEDRARGPFFDQDWGGMPAVMPVASGGIHAGQMPGLFDN 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   370 LGN-DVVLQFGGGTIGHPDGIQAGATANRVALESMViarnEGRDFVAEgpqilqdaAKTCGPLQTALDLW 438
Cdd:pfam00016 235 LGDsDVILQFGGGTFGHPDGPAAGAKANRQALEAWV----EGRDLEEY--------AKEHPELARAFESW 292
rubisco_III TIGR03326
ribulose bisphosphate carboxylase, type III; Members of this protein family are the archaeal, ...
10-438 3.48e-119

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: 354.46  E-value: 3.48e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499    10 ETDVLALFRVSPQPGVDPVEASAAVAGESSTATWTVV--WTDLLTACDLyRAKAYKVDlvpNTTDQYFAYIAYDIDLFEE 87
Cdd:TIGR03326  11 DDDLVCTFRITPAEGVSIEDAAGRVASESSIGTWTTLqpWKDPERYKDL-SAKVYDIE---EHGDGSIVRIAYPLGLFEE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499    88 GSIANLTASIIGNVFGFKAVKALRLEDMRLPVAYLKTFQGPATGIICERERMDKFGRPFLGATVKPKLGLSGKNYGRVVY 167
Cdd:TIGR03326  87 GNLPQLLSCIAGNIFGMKAVKGLRLLDFEFPAEFLRAFKGPQFGIEGVREILGIKDRPITATVPKPKVGLSTEEHAKVAY 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   168 EGLKGGLDFLKDDENINSQPFMRWKERYLYSMEGVNRSIAASGETKGHYLNVTAATmEEMYERAEFAKQLGSIIIMIDLV 247
Cdd:TIGR03326 167 ELWSGGVDLLKDDENLTSQAFNRFEERVEKSLKVRDKVEAETGEKKSYLINITADV-REMERRAELVADLGGEYVMVDIV 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   248 I-GYTAIQTMAVWSRKNDMILHLHRAGNSTYSRQKIHGMNFRVICKWMRMAGVDHIHAGTV-VGKLEGDPLMIKGFYNtl 325
Cdd:TIGR03326 246 VaGWSALQYVRERTEDLGLAIHAHRAMHAAFTRNPKHGISMFVLAKLYRLIGVDQLHTGTAgVGKLEGGNEDTKGIND-- 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   326 llpylevnlpqgiFFEQDWASLRKVTPVASGGIHCGQMHQLLDYLGNDVVLQFGGGTIGHPDGIQAGATANRVALESMVi 405
Cdd:TIGR03326 324 -------------FLRQDWHHIKPVFPVASGGLHPGLVPPLIDALGTDLVIQAGGGVHGHPDGTRAGAKALRAAIDAII- 389
                         410       420       430
                  ....*....|....*....|....*....|...
gi 74039499   406 arnEGRDfvaegpqiLQDAAKTCGPLQTALDLW 438
Cdd:TIGR03326 390 ---EGIS--------LEEKAKSVPELKKALEKW 411
 
Name Accession Description Interval E-value
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
9-451 0e+00

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


Pssm-ID: 176981  Cd Length: 475  Bit Score: 941.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499    9 KETDVLALFRVSPQPGVDPVEASAAVAGESSTATWTVVWTDLLTACDLYRAKAYKVDLVPNTTDQYFAYIAYDIDLFEEG 88
Cdd:CHL00040  32 KDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYRIEPVPGEENQYIAYVAYPLDLFEEG 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   89 SIANLTASIIGNVFGFKAVKALRLEDMRLPVAYLKTFQGPATGIICERERMDKFGRPFLGATVKPKLGLSGKNYGRVVYE 168
Cdd:CHL00040 112 SVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYLKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYE 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  169 GLKGGLDFLKDDENINSQPFMRWKERYLYSMEGVNRSIAASGETKGHYLNVTAATMEEMYERAEFAKQLGSIIIMIDLVI 248
Cdd:CHL00040 192 CLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMYKRAVFARELGVPIVMHDYLT 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  249 -GYTAIQTMAVWSRKNDMILHLHRAGNSTYSRQKIHGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPLMIKGFYNTLLL 327
Cdd:CHL00040 272 gGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHAGTVVGKLEGEREMTLGFVDLLRD 351
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  328 PYLEVNLPQGIFFEQDWASLRKVTPVASGGIHCGQMHQLLDYLGNDVVLQFGGGTIGHPDGIQAGATANRVALESMVIAR 407
Cdd:CHL00040 352 DFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQAR 431
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 74039499  408 NEGRDFVAEGPQILQDAAKTCGPLQTALDLWKDITFNYTSTDTA 451
Cdd:CHL00040 432 NEGRDLAREGNEIIREAAKWSPELAAACEVWKEIKFEFETTDTL 475
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
9-449 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: 892.93  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   9 KETDVLALFRVSPQPGVDPVEASAAVAGESSTATWTVVWTDLLTACDLYRAKAYKVDLVPNTTDQYFAYIAYDIDLFEEG 88
Cdd:cd08212  10 KDTDILAAFRITPQPGVDPEEAAAAVAGESSTATWTVVWTDRLTALDRYKGKAYRVEPVPGEENQYFAYIAYPLDLFEEG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  89 SIANLTASIIGNVFGFKAVKALRLEDMRLPVAYLKTFQGPATGIICERERMDKFGRPFLGATVKPKLGLSGKNYGRVVYE 168
Cdd:cd08212  90 SVANLTTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDRLNKYGRPLLGCTIKPKLGLSAKNYGRVVYE 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 169 GLKGGLDFLKDDENINSQPFMRWKERYLYSMEGVNRSIAASGETKGHYLNVTAATMEEMYERAEFAKQLGSIIIMIDLVI 248
Cdd:cd08212 170 CLRGGLDFTKDDENINSQPFMRWRDRFLFVAEAVNKAQAETGEVKGHYLNVTAGTMEEMYKRAEFAKELGSPIIMHDLLT 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 249 GYTAIQTMAVWSRKNDMILHLHRAGNSTYSRQKIHGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPLMIKGFYNTLLLP 328
Cdd:cd08212 250 GFTAIQSLAKWCRDNGMLLHLHRAGHATYDRQKNHGIHFRVLAKWLRLSGVDHIHAGTVVGKLEGDPLVTLGFYDLLRDD 329
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 329 YLEVNLPQGIFFEQDWASLRKVTPVASGGIHCGQMHQLLDYLGNDVVLQFGGGTIGHPDGIQAGATANRVALESMVIARN 408
Cdd:cd08212 330 YIEKDRSRGIFFTQDWASLPGVMPVASGGIHVGQMHQLIEIFGDDVVLQFGGGTIGHPWGIAAGATANRVALEAMVQARN 409
                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 74039499 409 EGRDFVAEGPQILQDAAKTCGPLQTALDLWKDITFNYTSTD 449
Cdd:cd08212 410 EGRDLAREGPEILREAAKWSPELAAALETWKDIKFEFESTD 450
rbcL PRK04208
ribulose bisophosphate carboxylase; Reviewed
9-450 0e+00

ribulose bisophosphate carboxylase; Reviewed


Pssm-ID: 179787  Cd Length: 468  Bit Score: 816.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499    9 KETDVLALFRVSPQPGVDPVEASAAVAGESSTATWTVVWTDLLTACDLYRAKAYKVDLVPNTTDQYFAYIAYDIDLFEEG 88
Cdd:PRK04208  25 KDTDLLACFRITPQEGVDPEEAAAAVAAESSTGTWTTVWTDLLTDLDKYKAKAYRIEDVPGDDGSYYAFIAYPLDLFEEG 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   89 SIANLTASIIGNVFGFKAVKALRLEDMRLPVAYLKTFQGPATGIICERERMDKFGRPFLGATVKPKLGLSGKNYGRVVYE 168
Cdd:PRK04208 105 SIPNLLASIAGNVFGFKAVKALRLEDIRFPVAYVKTFKGPPFGIQVERERLDKYGRPLLGTTPKPKLGLSAKNYGRVVYE 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  169 GLKGGLDFLKDDENINSQPFMRWKERYLYSMEGVNRSIAASGETKGHYLNVTAATMEEMYERAEFAKQLGSIIIMIDLVI 248
Cdd:PRK04208 185 ALRGGLDFTKDDENLNSQPFNRWRDRFLFVMEAIDKAEAETGERKGHYLNVTAPTMEEMYKRAEFAKELGSPIVMIDVVT 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  249 -GYTAIQTMAVWSRKNDMILHLHRAGNSTYSRQKIHGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPLMIKGFYNTLLL 327
Cdd:PRK04208 265 aGWTALQSLREWCRDNGLALHAHRAMHAAFTRNPNHGISFRVLAKLLRLIGVDHLHTGTVVGKLEGDRAEVLGYYDILRE 344
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  328 PYLEVNLPQGIFFEQDWASLRKVTPVASGGIHCGQMHQLLDYLGNDVVLQFGGGTIGHPDGIQAGATANRVALESMVIAR 407
Cdd:PRK04208 345 DFVPEDRSRGIFFDQDWGSIKPVFPVASGGIHPGHMPALLDIFGDDVVLQFGGGTHGHPDGTAAGATANRVALEACVEAR 424
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 74039499  408 NEGRDFVAEGPQILQDAAKTCGPLQTALDLWKDITFNYTSTDT 450
Cdd:PRK04208 425 NEGRDIEKEGPDILEEAAKWSPELAAALEKWGEIKFEFDTVDT 467
RuBisCO_large_I_II_III cd08206
Ribulose bisphosphate carboxylase large chain, Form I,II,III; Ribulose bisphosphate ...
11-438 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: 709.77  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  11 TDVLALFRVSPQPGVDPVEASAAVAGESSTATWTVVWTDLLTACDLYRAKAYKVDLVPntTDQYFAYIAYDIDLFEEGSI 90
Cdd:cd08206   1 TDLLAAFRMTPAEGVDPEEAAAAVAAESSTGTWTTVWTDRLTATERLKAKVYRIDPVP--DGQYIAKIAYPLDLFEEGSV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  91 ANLTASIIGNVFGFKAVKALRLEDMRLPVAYLKTFQGPATGIICERERMDKFGRPFLGATVKPKLGLSGKNYGRVVYEGL 170
Cdd:cd08206  79 PNLLTSIIGNVFGMKAVKALRLEDFRFPPAYLKTFDGPSFGIQGEREILGKYGRPLLGTIVKPKLGLSPKEYARVVYEAL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 171 KGGLDFLKDDENINSQPFMRWKERYLYSMEGVNRSIAASGETKGHYLNVTAATMEEMYERAEFAKQLGSIIIMIDLVI-G 249
Cdd:cd08206 159 RGGLDFVKDDENQNSQPFMRFEDRILFVAEAMDKAEAETGEAKGHYLNITADTPEEMIKRAEFAKELGSVIVMVDGVTaG 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 250 YTAIQTMAVWSRKNDMILHLHRAGNSTYSRQKIHGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPLMIKGFYNTLLLPY 329
Cdd:cd08206 239 WTAIQSARRWCPDNGLALHAHRAGHAAFTRQKNHGISMRVLAKLARLIGVDHIHTGTVVGKLEGDPSEVKGIADMLREDE 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 330 LEVNLPQgIFFEQDWASLRKVTPVASGGIHCGQMHQLLDYLGNDVVLQFGGGTIGHPDGIQAGATANRVALESMVIARne 409
Cdd:cd08206 319 VEGDLSR-IFFNQDWGGMKPVFPVASGGLHPGRMPALIEILGDDVILQFGGGTHGHPDGPAAGAKANRQALEAWVQGR-- 395
                       410       420
                ....*....|....*....|....*....
gi 74039499 410 grdfvaegpqILQDAAKTCGPLQTALDLW 438
Cdd:cd08206 396 ----------ILREYAKTHKELAAALEKW 414
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
9-443 8.67e-179

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


Pssm-ID: 441455  Cd Length: 417  Bit Score: 506.24  E-value: 8.67e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   9 KETDVLALFRVSPQPGVDPVEASAAVAGESSTATWTVVWTDLLTACDLYRAKAYKVDLVPNTT---DQYFAYIAYDIDLF 85
Cdd:COG1850  10 DDDDILATYRITPETGVDPEEAAAAIAGEQSTGTWTEVPTETDELRERLAARVYSIEELPEVGggyRRALVTIAYPLENF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  86 EeGSIANLTASIIGNVFGFKAVKALRLEDMRLPVAYLKTFQGPATGIICERERMDKFGRPFLGATVKPKLGLSGKNYGRV 165
Cdd:COG1850  90 G-GNLPNLLSTVAGNLFGLKAVSGLRLLDLEFPESFLAAFPGPKFGIEGTRELLGVYDRPLLGTIIKPKVGLSPEETAEL 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 166 VYEGLKGGLDFLKDDENINSQPFMRWKERYLYSMEGVNRSIAASGETKGHYLNVTaATMEEMYERAEFAKQLGSIIIMID 245
Cdd:COG1850 169 VYELALGGVDFIKDDENLADQPFCPFEDRVRAVMEAIDRAEEETGEKKMYAFNIT-ADTDEMLRRADLAVELGANAVMVD 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 246 -LVIGYTAIQTMAvwSRKNDMILHLHRAGNSTYSRQKIHGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPLMIKGFYNT 324
Cdd:COG1850 248 vNTVGLSAVQTLR--EEHIGLPIHAHRAGHGAFTRSPLHGISMRVLAKLWRLAGADHLHVGTPVGKMEGDDEEVLAIADA 325
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 325 LLlpylevnlpqgiffeQDWASLRKVTPVASGGIHCGQMHQLLDYLGNDVVLQFGGGTIGHPDGIQAGATANRVALESMV 404
Cdd:COG1850 326 LL---------------QPWGGLKPVFPVPSGGQHPGQVPELYDALGTDLILQAGGGIHGHPDGPAAGARALRQAWEAAV 390
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 74039499 405 iarnEGRDfvaegpqiLQDAAKTCGPLQTALDLWKDITF 443
Cdd:COG1850 391 ----AGIP--------LEEYAKTHPELAAALEKWGKKAP 417
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
132-438 1.30e-156

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: 445.27  E-value: 1.30e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   132 IICERERMDKFGRPFLGATVKPKLGLSGKNYGRVVYEGLKGGLDFLKDDENINSQPFMRWKERYLYSMEGVNRSIAASGE 211
Cdd:pfam00016   1 IAVERRVLNKYGRPILGTIIKPKLGLSPKNYARAVYEFLLGGLDFIKDDENINSQPFMPWRDRFLFVAEAIDRAQDETGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   212 TKGHYLNVTAATMEEMYERAEFAKQLGSIIIMID-LVIGYTAIQTMAVWSRKNDMILHLHRAGNSTYSRQKIHGMNFRVI 290
Cdd:pfam00016  81 AKGHYLNITADDMEEMYRRAEFAKETGGVAVMVDgLVIGPTAITTLRRWFRDNGVILHYHRAGHGAVTRQSKHGISFRVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   291 CKWMRMAGVDHIHAGTV-VGKLEGDPLmikgfyNTLLLPYLEVNLPQGIFFEQDWASLRKVTPVASGGIHCGQMHQLLDY 369
Cdd:pfam00016 161 AKMARLAGADHLHTGTMgVGKLEGDPS------DTLRAYMLEEDRARGPFFDQDWGGMPAVMPVASGGIHAGQMPGLFDN 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   370 LGN-DVVLQFGGGTIGHPDGIQAGATANRVALESMViarnEGRDFVAEgpqilqdaAKTCGPLQTALDLW 438
Cdd:pfam00016 235 LGDsDVILQFGGGTFGHPDGPAAGAKANRQALEAWV----EGRDLEEY--------AKEHPELARAFESW 292
RuBisCO_large_III cd08213
Ribulose bisphosphate carboxylase large chain, Form III; Ribulose bisphosphate carboxylase ...
11-438 7.91e-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: 407.16  E-value: 7.91e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  11 TDVLALFRVSPQPGVDPVEASAAVAGESSTATWTVVWTDLLTACDLYRAKAYKVDLVPNTtdqYFAYIAYDIDLFEEGSI 90
Cdd:cd08213   1 DDLIAVFRIEPAEGISIEEAAGRVASESSIGTWTTLATLYPERAEKLKAKAYYFDGLGGS---YIVKVAYPLELFEEGNM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  91 ANLTASIIGNVFGFKAVKALRLEDMRLPVAYLKTFQGPATGIICERERMDKFGRPFLGATVKPKLGLSGKNYGRVVYEGL 170
Cdd:cd08213  78 PQLLSSIAGNIFGMKAVKNLRLEDIYFPESYLREFKGPQFGIEGVREILGIKDRPLLGTVPKPKVGLSPEEHAEVAYEAL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 171 KGGLDFLKDDENINSQPFMRWKERYLYSMEGVNRSIAASGETKGHYLNVTAATmEEMYERAEFAKQLGSIIIMIDLVI-G 249
Cdd:cd08213 158 VGGVDLVKDDENLTSQPFNRFEERAKESLKARDKAEAETGERKAYLANITAPV-REMERRAELVADLGGKYVMIDVVVaG 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 250 YTAIQTMAVWSRKNDMILHLHRAGNSTYSRQKIHGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPLMIKGFYNTLLLPY 329
Cdd:cd08213 237 WSALQYLRDLAEDYGLAIHAHRAMHAAFTRNPRHGISMLVLAKLYRLIGVDQLHIGTAVGKMEGDKEEVLRIADILREQK 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 330 LEVNlPQGIFFEQDWASLRKVTPVASGGIHCGQMHQLLDYLGNDVVLQFGGGTIGHPDGIQAGATANRVALEsmviARNE 409
Cdd:cd08213 317 YKPD-EEDFHLAQDWGGIKPVFPVASGGLHPGLVPDVIDILGKDIVIQVGGGVHGHPDGTRAGAKAVRQAIE----AALE 391
                       410       420
                ....*....|....*....|....*....
gi 74039499 410 GRDfvaegpqiLQDAAKTCGPLQTALDLW 438
Cdd:cd08213 392 GIS--------LDEYAKDHKELARALEKW 412
RuBisCO_large cd08148
Ribulose bisphosphate carboxylase large chain; Ribulose bisphosphate carboxylase (Rubisco) ...
13-399 1.05e-129

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: 379.85  E-value: 1.05e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  13 VLALFRVSPQPgVDPVEASAAVAGESSTATWTVVWTdLLTACDLYRAKAYKVDlvpNTTDQYFAYIAYDIDLFEEGSIAN 92
Cdd:cd08148   1 VLATYRVHPEA-TPPEKAAEAIAAESSTGTWTEVPT-TQEQLRRVKGRVYSVE---ELGKRYIVKIAYPVELFEPGNIPQ 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  93 LTASIIGNVFGFKAVKALRLEDMRLPVAYLKTFQGPATGIICERERMDKFGRPFLGATVKPKLGLSGKNYGRVVYEGLKG 172
Cdd:cd08148  76 ILTVTAGNLFGLGALEAVRLEDLEFPEEYKKLFPGPKFGIDGIRKLLGVYGRPLVGTIIKPKLGLNPKYTAEAAYAAALG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 173 GLDFLKDDENINSQPFMRWKERYLYSMEGVNRSIAASGETKGHYLNVTAATmEEMYERAEFAKQLGSIIIMID-LVIGYT 251
Cdd:cd08148 156 GLDLIKDDETLTDQPFCPLRDRITEVAAALDRVQEETGEKKLYAVNVTAGT-FEIIERAERALELGANMLMVDvLTAGFS 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 252 AIQTMAVWSRkNDMILHLHRAGNSTYSRQKIHGMNFRVICKWMRMAGVDHIHAGTVVGKLEGDPLMIKGFYNTLllpyle 331
Cdd:cd08148 235 ALQALAEDFE-IDLPIHVHRAMHGAVTRSKFHGISMLVLAKLLRMAGGDFIHTGTVVGKMALEREEALGIADAL------ 307
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74039499 332 vnlpqgiffEQDWASLRKVTPVASGGIHCGQMHQLLDYLGNDVVLQFGGGTIGHPDGIQAGATANRVA 399
Cdd:cd08148 308 ---------TDDWAGFKRVFPVASGGIHPGLVPGILRDFGIDVILQAGGGIHGHPDGTVAGARAMRQA 366
rubisco_III TIGR03326
ribulose bisphosphate carboxylase, type III; Members of this protein family are the archaeal, ...
10-438 3.48e-119

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: 354.46  E-value: 3.48e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499    10 ETDVLALFRVSPQPGVDPVEASAAVAGESSTATWTVV--WTDLLTACDLyRAKAYKVDlvpNTTDQYFAYIAYDIDLFEE 87
Cdd:TIGR03326  11 DDDLVCTFRITPAEGVSIEDAAGRVASESSIGTWTTLqpWKDPERYKDL-SAKVYDIE---EHGDGSIVRIAYPLGLFEE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499    88 GSIANLTASIIGNVFGFKAVKALRLEDMRLPVAYLKTFQGPATGIICERERMDKFGRPFLGATVKPKLGLSGKNYGRVVY 167
Cdd:TIGR03326  87 GNLPQLLSCIAGNIFGMKAVKGLRLLDFEFPAEFLRAFKGPQFGIEGVREILGIKDRPITATVPKPKVGLSTEEHAKVAY 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   168 EGLKGGLDFLKDDENINSQPFMRWKERYLYSMEGVNRSIAASGETKGHYLNVTAATmEEMYERAEFAKQLGSIIIMIDLV 247
Cdd:TIGR03326 167 ELWSGGVDLLKDDENLTSQAFNRFEERVEKSLKVRDKVEAETGEKKSYLINITADV-REMERRAELVADLGGEYVMVDIV 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   248 I-GYTAIQTMAVWSRKNDMILHLHRAGNSTYSRQKIHGMNFRVICKWMRMAGVDHIHAGTV-VGKLEGDPLMIKGFYNtl 325
Cdd:TIGR03326 246 VaGWSALQYVRERTEDLGLAIHAHRAMHAAFTRNPKHGISMFVLAKLYRLIGVDQLHTGTAgVGKLEGGNEDTKGIND-- 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   326 llpylevnlpqgiFFEQDWASLRKVTPVASGGIHCGQMHQLLDYLGNDVVLQFGGGTIGHPDGIQAGATANRVALESMVi 405
Cdd:TIGR03326 324 -------------FLRQDWHHIKPVFPVASGGLHPGLVPPLIDALGTDLVIQAGGGVHGHPDGTRAGAKALRAAIDAII- 389
                         410       420       430
                  ....*....|....*....|....*....|...
gi 74039499   406 arnEGRDfvaegpqiLQDAAKTCGPLQTALDLW 438
Cdd:TIGR03326 390 ---EGIS--------LEEKAKSVPELKKALEKW 411
PRK13475 PRK13475
ribulose-bisphosphate carboxylase;
13-401 8.04e-65

ribulose-bisphosphate carboxylase;


Pssm-ID: 184072  Cd Length: 443  Bit Score: 215.36  E-value: 8.04e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   13 VLALFRVSPQPGVDPVEASAAVAGESSTATWTVVWT--DLLTACDlyrAKAYKVDLVPNTTdqyfaYIAYDIDLFE---- 86
Cdd:PRK13475  24 ILCAYKMKPKAGHGYLEAAAHFAAESSTGTNVEVSTtdDFTRGVD---ALVYEIDEARELM-----KIAYPVELFDrnii 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   87 --EGSIANLTASIIGNVFGFKAVKALRLEDMRLPVAYLKTFQGPATGI-----ICERERMDkfGRPFLGATVKPKLGLSG 159
Cdd:PRK13475  96 dgRAMIVSFLTLTIGNNQGMGDVEYAKMHDFYVPPRYLELFDGPSTDIsdlwrVLGRPVKD--GGYIAGTIIKPKLGLRP 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  160 KNYGRVVYEGLKGGlDFLKDDENINSQPFMRWKERYLYSMEGVNRSIAASGETKGHYLNVTAATMEEMYERAE-----FA 234
Cdd:PRK13475 174 EPFAEACYDFWLGG-DFIKNDEPQGNQVFAPLKKTVPLVADAMKRAQDETGEAKLFSANITADDHYEMIARGEyiletFG 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  235 KQLGSIIIMIDlviGYTAIQTMAVWSRKN--DMILHLHRAGNSTY-SRQKIHGMNFRVICKWMRMAGVDHIHAGTV-VGK 310
Cdd:PRK13475 253 ENADHVAFLVD---GYVAGPGAVTTARRQypDQYLHYHRAGHGAVtSPSSKRGYTAFVLSKMARLQGASGIHTGTMgYGK 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  311 LEGDPLMIKGFYntlLLPYLEVnlpQGIFFEQDWASLRKVTPVASGGIHCGQMHQLLDYLGN-DVVLQFGGGTIGHPDGI 389
Cdd:PRK13475 330 MEGEADDRVIAY---MIERDSA---QGPFYHQEWYGMKPTTPIISGGMNALRLPGFFDNLGHgNVINTAGGGAFGHIDGP 403
                        410
                 ....*....|..
gi 74039499  390 QAGATANRVALE 401
Cdd:PRK13475 404 AAGAKSLRQAYD 415
RuBisCO_large_II cd08211
Ribulose bisphosphate carboxylase large chain, Form II; Ribulose bisphosphate carboxylase ...
13-401 5.10e-64

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: 213.13  E-value: 5.10e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  13 VLALFRVSPQPGVDPVEASAAVAGESSTAT-WTVVWTDLLTACdlYRAKAYKVDLvpnttDQYFAYIAYDIDLFE----- 86
Cdd:cd08211  23 VLVAYIMKPKAGYGYLATAAHFAAESSTGTnVEVSTTDDFTRG--VDALVYEIDE-----ARELMKIAYPVELFDrnltd 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  87 -EGSIANLTASIIGNVFGFKAVKALRLEDMRLPVAYLKTFQGPATGIICERERMDKF---GRPFLGATVKPKLGLSGKNY 162
Cdd:cd08211  96 gRAMVASFLTLIIGNNQGMGDVEYLKMHDFYVPESMLELFDGPSVNISDMWKVLGRPevdGGYIAGTIIKPKLGLRPKPF 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 163 GRVVYEGLKGGlDFLKDDENINSQPFMRWKERYLYSMEGVNRSIAASGETKGHYLNVTAATMEEMYERAE-----FAKQL 237
Cdd:cd08211 176 AEACYAFWLGG-DFIKNDEPQANQPFCPLKKVIPLVADAMRRAQDETGEAKLFSANITADDPDEMIARGEyileaFGPNA 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 238 GSIIIMID-LVIGYTAIQTmavwSRKN--DMILHLHRAGNSTYSRQKIH-GMNFRVICKWMRMAGVDHIHAGTV-VGKLE 312
Cdd:cd08211 255 GHVAFLVDgYVAGPAAVTT----ARRRfpDQFLHYHRAGHGAVTSPQSKrGYTAFVLSKMARLQGASGIHTGTMgFGKME 330
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 313 GDPLMIKGFYntlLLPYLEVnlpQGIFFEQDWASLRKVTPVASGGIHCGQMHQLLDYLGN-DVVLQFGGGTIGHPDGIQA 391
Cdd:cd08211 331 GESSDKVIAY---MIERDEA---QGPLFNQKWYGMKPTTPIISGGMNALRLPGFFENLGNgNVILTAGGGSFGHIDGPAA 404
                       410
                ....*....|
gi 74039499 392 GATANRVALE 401
Cdd:cd08211 405 GAKSLRQAYD 414
RuBisCO_IV_RLP cd08205
Ribulose bisphosphate carboxylase like proteins, Rubisco-Form IV; Ribulose bisphosphate ...
15-399 3.54e-61

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: 203.53  E-value: 3.54e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  15 ALFRVSPqPGVDPVEASAAVAGESSTATWTVVWTdlLTACDLYRAKA-----YKVDLVPNTTDQYFAYIAYDIDLFEeGS 89
Cdd:cd08205   3 ATYRIEA-PGADAEKKAEAIALEQTVGTWTELPG--ETEEIRERHVGrvesiEELEESEGKYGRARVTISYPLDNFG-GD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  90 IANLTASIIGNVFGfkaVKALRLEDMRLPVAYLKTFQGPATGIICERERMDKFGRPFLGATVKPKLGLSGKNYGRVVYEG 169
Cdd:cd08205  79 LPQLLNTLFGNLSL---LPGIKLVDLELPDSLLAAFPGPRFGIEGLRRLLGVHDRPLLGTIIKPSIGLSPEELAELAYEL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 170 LKGGLDFLKDDENINSQPFMRWKERYLYSMEGVNRSIAASGETKGHYLNVTAATmEEMYERAEFAKQLGSIIIMIDL-VI 248
Cdd:cd08205 156 ALGGIDLIKDDELLADQPYAPFEERVRACMEAVRRANEETGRKTLYAPNITGDP-DELRRRADRAVEAGANALLINPnLV 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 249 GYTAIQTMAvwsRKNDMILHLHRAGNSTYSRQKIHGMNFRVICKWMRMAGVDHIHagtvvgklegdplmIKGFYNTLLLP 328
Cdd:cd08205 235 GLDALRALA---EDPDLPIMAHPAFAGALSRSPDYGSHFLLLGKLMRLAGADAVI--------------FPGPGGRFPFS 297
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74039499 329 YLEVnlpQGIF--FEQDWASLRKVTPVASGGIHCGQMHQLLDYLGNDVVLQFGGGTIGHPDGIQAGATANRVA 399
Cdd:cd08205 298 REEC---LAIAraCRRPLGGIKPALPVPSGGMHPGRVPELYRDYGPDVILLAGGGILGHPDGAAAGVRAFRQA 367
RuBisCO_large_N pfam02788
Ribulose bisphosphate carboxylase large chain, N-terminal domain; The N-terminal domain of ...
9-121 1.45e-56

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: 183.18  E-value: 1.45e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499     9 KETDVLALFRVSPQPGVDPVEASAAVAGESSTATWTVVWTDLLTACDLYRAKAYKVDLVPNttDQYFAYIAYDIDLFEEG 88
Cdd:pfam02788  10 KDTDLLCAFRIEPAAGVSPEEAAAHVAAESSTGTWTEVWTLDDTFTKKLKAKVYEIDEVPG--GSYIVKIAYPLDLFEEG 87
                          90       100       110
                  ....*....|....*....|....*....|...
gi 74039499    89 SIANLTASIIGNVFGFKAVKALRLEDMRLPVAY 121
Cdd:pfam02788  88 SIPQLLSSIAGNIFGMKAVKALRLEDIRFPPAY 120
RLP_NonPhot cd08207
Ribulose bisphosphate carboxylase like proteins from nonphototrophic bacteria; Ribulose ...
25-435 7.95e-55

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: 187.90  E-value: 7.95e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  25 VDPVEASAAVAGESSTATWTVV--WTDLLTACdlYRAKAYKVDLVPNTTDQYFAY-------------IAYDIDLFEEgS 89
Cdd:cd08207  12 LDLERAAEVIAGEQSSGTFIALpgETDELKER--SAARVESIEELETAAQPSLPRrasggpytrarvtISFPLDNIGT-S 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  90 IANLTASIIGNVFGFKAVKALRLEDMRLPVAYLKTFQGPATGIICERERMDKFGRPFLGATVKPKLGLSGKNYGRVVYEG 169
Cdd:cd08207  89 LPNLLATVAGNLFELRELSGLRLVDLGLPDEFAAAFPGPAFGIAGTRRLTGVEDRPLIGTIIKPSVGLTPEETAALVRQL 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 170 LKGGLDFLKDDENINSQPFMRWKERYLYSMEGVNRSIAASGETKGHYLNVTAATmEEMYERAEFAKQLGSIIIMIDL-VI 248
Cdd:cd08207 169 AAAGIDFIKDDELLANPPYSPLDERVRAVMRVINDHAQRTGRKVMYAFNITDDI-DEMRRNHDLVVEAGGTCVMVSLnSV 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 249 GYTAIQTMavwSRKNDMILHLHRAGNSTYSRQKIHGMNFRVICKWMRMAGVDHIHAGTVVGKL-EGDPLMIKGFYnTLLL 327
Cdd:cd08207 248 GLSGLAAL---RRHSQLPIHGHRNGWGMLTRSPALGISFQAYQKLWRLAGVDHLHVNGLASKFwESDDSVIESAR-ACLT 323
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 328 PylevnlpqgiFFEQDWASLrkvtPVASGGIHCGQMHQLLDYLGN-DVVLQFGGGTIGHPDGIQAGATANRVALESMVIA 406
Cdd:cd08207 324 P----------LGGPDDAAM----PVFSSGQWGGQAPPTYRRLGSvDLLYLAGGGIMAHPDGPAAGVRSLRQAWEAAVAG 389
                       410       420
                ....*....|....*....|....*....
gi 74039499 407 rnegrdfvaegpQILQDAAKTCGPLQTAL 435
Cdd:cd08207 390 ------------VPLEEYAKTHPELARAL 406
RLP_DK-MTP-1-P-enolase cd08209
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Ribulose bisphosphate carboxylase like ...
13-438 1.24e-28

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: 116.65  E-value: 1.24e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  13 VLALFRVspQPGVDPVEASAAVAGESSTATWTVVWtdLLTACDLYRAKAYKVDLVPNTTDQYFAYIAYdidlfEEGSIAN 92
Cdd:cd08209   1 IVATYRF--PDGADLEKKAEQIAVGLTVGSWTDLP--ALRQAQLQKHLGEVVSVEELEEGRGVITIAY-----PLINVSG 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  93 LTASIIGNVFG-FKAVKALRLEDMRLPVAYLKTFQGPATGIICERERMDKFGRPFLGATVKPKLGLSGKNYGRVVYEGLK 171
Cdd:cd08209  72 DIPALLTTIFGkLSLDGKIKLVDLRLPEEFGRAFPGPKFGIEGIRQRLGVHDRPLLMSIFKGVLGLDLDDLAEQLREQAL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 172 GGLDFLKDDENINSQPFMRWKERYLYSMEGVNRSIAASGETKGHYLNVTAATmEEMYERAEFAKQLGSIIIMID-LVIGY 250
Cdd:cd08209 152 GGVDLIKDDEILFDNPLAPALERIRACRPVLQEVYEQTGRRTLYAVNLTGPV-FTLKEKARRLVEAGANALLFNvFAYGL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 251 TAIQTMAVWSRKNDMILhLHRAGNSTYSRQKIHGMNFRVIC-KWMRMAGVDHIhagtvvgkLEGDPlmikgfYNTLLLPY 329
Cdd:cd08209 231 DVLEALASDPEINVPIF-AHPAFAGALYGSPDYGIAASVLLgTLMRLAGADAV--------LFPSP------YGSVALSK 295
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 330 LEVNLPQGIFFEQDWasLRKVTPVASGGIHCGQMHQLLDYLGNDVVLQFGGGTIGHPDGIQAGATANRVALESmviarne 409
Cdd:cd08209 296 EEALAIAEALRRGGA--FKGVFPVPSAGIHPGLVPQLLRDFGTDVILNAGGGIHGHPDGAAAGVRAFREAIDA------- 366
                       410       420
                ....*....|....*....|....*....
gi 74039499 410 grdfvAEGPQILQDAAKTCGPLQTALDLW 438
Cdd:cd08209 367 -----VLAGESLEPAAIPDGPLKSALDKW 390
RLP_Photo cd08208
Ribulose bisphosphate carboxylase like proteins from phototrophic bacteria; Ribulose ...
26-404 1.50e-28

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: 116.92  E-value: 1.50e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  26 DPVEASAAVAGESSTATWTVVWTDLltacDLYRAKAYKV-DL-VPNTTDQYFAYIAYDID----------LFEEGS---- 89
Cdd:cd08208  29 DPETAAAHFCSEQSTAQWRRVGVDE----DFRPRFAAKViDLeVIEELEQLSYPVKHSETgpvhacrvtiAHPHGNfgpk 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  90 IANLTASIIGN-VFGFKAVKALRLEDMRLPVAYLKTFQGPATGIICERERMDKFGRPFLGATVKPKLGLSGKNYGRVVYE 168
Cdd:cd08208 105 IPNLLSAVCGEgTFFSPGVPVVKLMDIHFPETYLADFEGPKFGIAGLRERLQAHDRPIFFGVIKPNIGLPPGEFAELGYQ 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 169 GLKGGLDFLKDDENINSQPFMRWKERYLYSMEGVNRSIAASGETKGHYLNVTaATMEEMYERAEFAKQLGSIIIMID-LV 247
Cdd:cd08208 185 SWLGGLDIAKDDEMLADVDWCPLEERAALLGKARRRAEAETGVPKIYLANIT-DEVDRLMELHDVAVRNGANALLINaMP 263
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 248 IGYTAIQTMavwSRKNDMILHLHRAGNSTYSRQKIHGMNFRVICKWMRMAGVDHIhagtvvgklegdplMIKGFYNTLLL 327
Cdd:cd08208 264 VGLSAVRML---RKHAQVPLIAHFPFIASFSRLEKYGIHSRVMTKLQRLAGLDVV--------------IMPGFGPRMMT 326
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74039499 328 PYLEVnLPQGIFFEQDWASLRKVTPVASGGIHCGQMHQLLDYLGN-DVVLQFGGGTIGHPDGIQAGATANRVALESMV 404
Cdd:cd08208 327 PEEEV-LECVIACLEPMGPIKPCLPVPGGSDSALTLQTVYEKVGNvDFGFVPGRGVFGHPMGPKAGAKSIRQAWEAIE 403
mtnW PRK09549
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Reviewed
91-438 1.95e-26

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


Pssm-ID: 236560  Cd Length: 407  Bit Score: 110.48  E-value: 1.95e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   91 ANLTA---SIIGNVFGFKAVKA-LRLEDMRLPVAYLKTFQGPATGIICERERMDKFGRPFLGATVKPKLGLSGKNYGRVV 166
Cdd:PRK09549  77 ANFSPdlpAILTTTFGKLSLDGeVKLIDLTFSDELKRHFPGPKFGIDGIRNLLGVHDRPLLMSIFKGVIGRDLDYLKEQL 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  167 YEGLKGGLDFLKDDENINSQPFMRWKERYLYSMEGVNRSIAASGETKGHYLNVTAATMEeMYERAEFAKQLGSIIIMID- 245
Cdd:PRK09549 157 RDQALGGVDLVKDDEILFENALTPFEKRIVAGKEVLQEVYETTGHKTLYAVNLTGRTFE-LKEKAKRAAEAGADALLFNv 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  246 LVIGYTAIQTMAVWSRKNDMILHlHRAGNSTYSRQKIHGMNFRVIC-KWMRMAGVDhihagtvvgklegdplmikgfynt 324
Cdd:PRK09549 236 FAYGLDVLQSLAEDPEIPVPIMA-HPAVSGAYTPSPLYGISSPLLLgKLLRYAGAD------------------------ 290
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  325 LLL---PYLEVNLP----QGIFFE--QDWASLRKVTPVASGGIHCGQMHQLLDYLGNDVVLQFGGGTIGHPDGIQAGATA 395
Cdd:PRK09549 291 FSLfpsPYGSVALEkeeaLAIAKEltEDDDPFKRSFPVPSAGIHPGLVPLLIRDFGKDVVINAGGGIHGHPNGAQGGGKA 370
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 74039499  396 NRVALESmviarnegrdfvAEGPQILQDAAKTCGPLQTALDLW 438
Cdd:PRK09549 371 FRAAIDA------------VLQGKPLHEAAEDDENLHSALDIW 401
RLP_RrRLP cd08210
Ribulose bisphosphate carboxylase like proteins (RLPs) similar to R.rubrum RLP; RLP from ...
64-400 3.13e-26

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: 109.25  E-value: 3.13e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499  64 VDLVPNTTDQYFAYIAYDIDlfeegSIANLTASIIGNVFGFKAVKA-LRLEDMRLPVAYLKTFQGPATGIICERERMDKF 142
Cdd:cd08210  50 ESLEPAGEGSYRARISYSVD-----TAGGELTQLLNVLFGNSSLQPgIRLVDFELPPSLLRRFPGPRFGIAGLRALLGIP 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 143 GRPFLGATVKPkLGLSGKNYGRVVYEGLKGGLDFLKDDENINSQPFMRWKERYLYSMEGVNRsiaASGETKGHYL---NV 219
Cdd:cd08210 125 ERPLLCSALKP-QGLSAAELAELAYAFALGGIDIIKDDHGLADQPFAPFEERVKACQEAVAE---ANAETGGRTLyapNV 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 220 TAATMeEMYERAEFAKQLGSIIIMI-DLVIGYTAIQTMAvwSRKNDMILHLHRA--GNSTYSRQKI-HGMNFRVIckwMR 295
Cdd:cd08210 201 TGPPT-QLLERARFAKEAGAGGVLIaPGLTGLDTFRELA--EDFDFLPILAHPAfaGAFVSSGDGIsHALLFGTL---FR 274
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499 296 MAGVDHI---HAGtvvGKLegdplmikGFyntlllpylEVNLPQGI--FFEQDWASLRKVTPVASGGIHCGQMHQLLDYL 370
Cdd:cd08210 275 LAGADAVifpNYG---GRF--------GF---------SREECQAIadACRRPMGGLKPILPAPGGGMSVERAPEMVELY 334
                       330       340       350
                ....*....|....*....|....*....|
gi 74039499 371 GNDVVLQFGGGTIGHPDGIQAGATANRVAL 400
Cdd:cd08210 335 GPDVMLLIGGSLLRAGDDLTENTRAFVEAV 364
salvage_mtnW TIGR03332
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Members of this family are the methionine ...
110-438 2.00e-18

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: 86.81  E-value: 2.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   110 LRLEDMRLPVAYLKTFQGPATGIICERERMDKFGRPFLGATVKpklGLSGKNYGRVVYEGLK---GGLDFLKDDENINSQ 186
Cdd:TIGR03332 105 VKLIDLEFSDEFKRHFPGPKFGIDGIRKLLGVHERPLLMSIFK---GMIGRDLGYLKEQLRQqalGGVDLVKDDEILFET 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   187 PFMRWKERYLYSMEGVNRSIAASGETKGHYLNVTAATMEeMYERAEFAKQLGSIIIMIDL-VIGYTAIQTMAvwsrKNDM 265
Cdd:TIGR03332 182 GLAPFEKRITEGKEVLQEVYEQTGHKTLYAVNLTGRTFD-LKDKAKRAAELGADVLLFNVfAYGLDVLQSLA----EDDE 256
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   266 I---LHLHRAGNSTYSRQKIHGMNFRVIC-KWMRMAGVDhihagtvvgklegdplmikgfYNTLLLPYLEVNLPQ----G 337
Cdd:TIGR03332 257 IpvpIMAHPAVSGAYTSSPFYGFSHSLLLgKLLRYAGAD---------------------FSLFPSPYGSVALERedalA 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74039499   338 IFFE--QDWASLRKVTPVASGGIHCGQMHQLLDYLGNDVVLQFGGGTIGHPDGIQAGATANRVALESMVIARNegrdfva 415
Cdd:TIGR03332 316 ISKEltEDDAPFKKTFAVPSAGIHPGMVPLIMRDFGIDHIINAGGGIHGHPNGAQGGGRAFRAAIDAVLEAKP------- 388
                         330       340
                  ....*....|....*....|...
gi 74039499   416 egpqiLQDAAKTCGPLQTALDLW 438
Cdd:TIGR03332 389 -----LHEKAADDIDLKLALDKW 406
 
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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