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Conserved domains on  [gi|664806164|gb|AIF72771|]
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ribulose-1,5-biphosphate carboxylase/oxygenase large subunit, partial (chloroplast) [Panicum aequinerve]

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
1-449 0e+00

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


:

Pssm-ID: 176981  Cd Length: 475  Bit Score: 1032.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164   1 ETKASVGFKAGVKDYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCY 80
Cdd:CHL00040   6 ETKASVGFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  81 HIEPVPGEPDQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKY 160
Cdd:CHL00040  86 RIEPVPGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYLKTFQGPPHGIQVERDKLNKY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 161 GRPLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAG 240
Cdd:CHL00040 166 GRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAG 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 241 TCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDH 320
Cdd:CHL00040 246 TCEEMYKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDH 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 321 IHAGTVVGKLEGEREITLGFVDLLRDDFIEKDRSRGIFFTQDWVSMPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGG 400
Cdd:CHL00040 326 IHAGTVVGKLEGEREMTLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGG 405
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 664806164 401 TLGHPWGNAPGAAANRVALEACVQARNEGRDLAREGNEIIKAACKWSPE 449
Cdd:CHL00040 406 TLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEIIREAAKWSPE 454
 
Name Accession Description Interval E-value
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
1-449 0e+00

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


Pssm-ID: 176981  Cd Length: 475  Bit Score: 1032.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164   1 ETKASVGFKAGVKDYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCY 80
Cdd:CHL00040   6 ETKASVGFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  81 HIEPVPGEPDQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKY 160
Cdd:CHL00040  86 RIEPVPGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYLKTFQGPPHGIQVERDKLNKY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 161 GRPLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAG 240
Cdd:CHL00040 166 GRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAG 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 241 TCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDH 320
Cdd:CHL00040 246 TCEEMYKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDH 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 321 IHAGTVVGKLEGEREITLGFVDLLRDDFIEKDRSRGIFFTQDWVSMPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGG 400
Cdd:CHL00040 326 IHAGTVVGKLEGEREMTLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGG 405
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 664806164 401 TLGHPWGNAPGAAANRVALEACVQARNEGRDLAREGNEIIKAACKWSPE 449
Cdd:CHL00040 406 TLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEIIREAAKWSPE 454
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
18-449 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: 917.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  18 TYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVPGEPDQYICYVA 97
Cdd:cd08212    1 GYWTPDYQPKDTDILAAFRITPQPGVDPEEAAAAVAGESSTATWTVVWTDRLTALDRYKGKAYRVEPVPGEENQYFAYIA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  98 YPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSA 177
Cdd:cd08212   81 YPLDLFEEGSVANLTTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDRLNKYGRPLLGCTIKPKLGLSA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 178 KNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAGTCEEMIKRAVFARELGV 257
Cdd:cd08212  161 KNYGRVVYECLRGGLDFTKDDENINSQPFMRWRDRFLFVAEAVNKAQAETGEVKGHYLNVTAGTMEEMYKRAEFAKELGS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 258 PIVMHDYLTgGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGEREIT 337
Cdd:cd08212  241 PIIMHDLLT-GFTAIQSLAKWCRDNGMLLHLHRAGHATYDRQKNHGIHFRVLAKWLRLSGVDHIHAGTVVGKLEGDPLVT 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 338 LGFVDLLRDDFIEKDRSRGIFFTQDWVSMPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAAANRV 417
Cdd:cd08212  320 LGFYDLLRDDYIEKDRSRGIFFTQDWASLPGVMPVASGGIHVGQMHQLIEIFGDDVVLQFGGGTIGHPWGIAAGATANRV 399
                        410       420       430
                 ....*....|....*....|....*....|..
gi 664806164 418 ALEACVQARNEGRDLAREGNEIIKAACKWSPE 449
Cdd:cd08212  400 ALEAMVQARNEGRDLAREGPEILREAAKWSPE 431
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
19-449 2.51e-172

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


Pssm-ID: 441455  Cd Length: 417  Bit Score: 489.68  E-value: 2.51e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  19 YYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVP---GEPDQYICY 95
Cdd:COG1850    2 YVDPDYIPDDDDILATYRITPETGVDPEEAAAAIAGEQSTGTWTEVPTETDELRERLAARVYSIEELPevgGGYRRALVT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  96 VAYPLDLFEeGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGL 175
Cdd:COG1850   82 IAYPLENFG-GNLPNLLSTVAGNLFGLKAVSGLRLLDLEFPESFLAAFPGPKFGIEGTRELLGVYDRPLLGTIIKPKVGL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 176 SAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAGTcEEMIKRAVFAREL 255
Cdd:COG1850  161 SPEETAELVYELALGGVDFIKDDENLADQPFCPFEDRVRAVMEAIDRAEEETGEKKMYAFNITADT-DEMLRRADLAVEL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 256 GVPIVMHDYLTGGFTANTSLAHycRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGERE 335
Cdd:COG1850  240 GANAVMVDVNTVGLSAVQTLRE--EHIGLPIHAHRAGHGAFTRSPLHGISMRVLAKLWRLAGADHLHVGTPVGKMEGDDE 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 336 ITLGFVDLLRddfiekdrsrgifftQDWVSMPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAAAN 415
Cdd:COG1850  318 EVLAIADALL---------------QPWGGLKPVFPVPSGGQHPGQVPELYDALGTDLILQAGGGIHGHPDGPAAGARAL 382
                        410       420       430
                 ....*....|....*....|....*....|....
gi 664806164 416 RVALEACVQarneGRDLAregneiikAACKWSPE 449
Cdd:COG1850  383 RQAWEAAVA----GIPLE--------EYAKTHPE 404
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
150-449 3.64e-164

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: 464.14  E-value: 3.64e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  150 IQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGE 229
Cdd:pfam00016   1 IAVERRVLNKYGRPILGTIIKPKLGLSPKNYARAVYEFLLGGLDFIKDDENINSQPFMPWRDRFLFVAEAIDRAQDETGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  230 IKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVL 309
Cdd:pfam00016  81 AKGHYLNITADDMEEMYRRAEFAKETGGVAVMVDGLVIGPTAITTLRRWFRDNGVILHYHRAGHGAVTRQSKHGISFRVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  310 AKALRMSGGDHIHAGTV-VGKLEGEREitlgfvDLLRDDFIEKDRSRGIFFTQDWVSMPGVIPVASGGIHVWHMPALTEI 388
Cdd:pfam00016 161 AKMARLAGADHLHTGTMgVGKLEGDPS------DTLRAYMLEEDRARGPFFDQDWGGMPAVMPVASGGIHAGQMPGLFDN 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664806164  389 FGD-DSVLQFGGGTLGHPWGNAPGAAANRVALEACVqarnEGRDLAREGneiikaacKWSPE 449
Cdd:pfam00016 235 LGDsDVILQFGGGTFGHPDGPAAGAKANRQALEAWV----EGRDLEEYA--------KEHPE 284
rubisco_III TIGR03326
ribulose bisphosphate carboxylase, type III; Members of this protein family are the archaeal, ...
24-446 9.02e-116

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: 345.22  E-value: 9.02e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164   24 YETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTdgLTSLDRYKGRCYHIEPVPGEPDQYICYVAYPLDLF 103
Cdd:TIGR03326   7 YEPSDDDLVCTFRITPAEGVSIEDAAGRVASESSIGTWTTLQP--WKDPERYKDLSAKVYDIEEHGDGSIVRIAYPLGLF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  104 EEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRA 183
Cdd:TIGR03326  85 EEGNLPQLLSCIAGNIFGMKAVKGLRLLDFEFPAEFLRAFKGPQFGIEGVREILGIKDRPITATVPKPKVGLSTEEHAKV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  184 CYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAGTcEEMIKRAVFARELGVPIVMHD 263
Cdd:TIGR03326 165 AYELWSGGVDLLKDDENLTSQAFNRFEERVEKSLKVRDKVEAETGEKKSYLINITADV-REMERRAELVADLGGEYVMVD 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  264 YLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTV-VGKLEGEREITLGFVD 342
Cdd:TIGR03326 244 IVVAGWSALQYVRERTEDLGLAIHAHRAMHAAFTRNPKHGISMFVLAKLYRLIGVDQLHTGTAgVGKLEGGNEDTKGIND 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  343 LLRddfiekdrsrgifftQDWVSMPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAAANRVALEAC 422
Cdd:TIGR03326 324 FLR---------------QDWHHIKPVFPVASGGLHPGLVPPLIDALGTDLVIQAGGGVHGHPDGTRAGAKALRAAIDAI 388
                         410       420
                  ....*....|....*....|....*..
gi 664806164  423 VqarnEGRDL---AREGNEIIKAACKW 446
Cdd:TIGR03326 389 I----EGISLeekAKSVPELKKALEKW 411
 
Name Accession Description Interval E-value
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
1-449 0e+00

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


Pssm-ID: 176981  Cd Length: 475  Bit Score: 1032.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164   1 ETKASVGFKAGVKDYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCY 80
Cdd:CHL00040   6 ETKASVGFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  81 HIEPVPGEPDQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKY 160
Cdd:CHL00040  86 RIEPVPGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYLKTFQGPPHGIQVERDKLNKY 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 161 GRPLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAG 240
Cdd:CHL00040 166 GRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAG 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 241 TCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDH 320
Cdd:CHL00040 246 TCEEMYKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDH 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 321 IHAGTVVGKLEGEREITLGFVDLLRDDFIEKDRSRGIFFTQDWVSMPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGG 400
Cdd:CHL00040 326 IHAGTVVGKLEGEREMTLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGG 405
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 664806164 401 TLGHPWGNAPGAAANRVALEACVQARNEGRDLAREGNEIIKAACKWSPE 449
Cdd:CHL00040 406 TLGHPWGNAPGAVANRVALEACVQARNEGRDLAREGNEIIREAAKWSPE 454
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
18-449 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: 917.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  18 TYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVPGEPDQYICYVA 97
Cdd:cd08212    1 GYWTPDYQPKDTDILAAFRITPQPGVDPEEAAAAVAGESSTATWTVVWTDRLTALDRYKGKAYRVEPVPGEENQYFAYIA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  98 YPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSA 177
Cdd:cd08212   81 YPLDLFEEGSVANLTTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDRLNKYGRPLLGCTIKPKLGLSA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 178 KNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAGTCEEMIKRAVFARELGV 257
Cdd:cd08212  161 KNYGRVVYECLRGGLDFTKDDENINSQPFMRWRDRFLFVAEAVNKAQAETGEVKGHYLNVTAGTMEEMYKRAEFAKELGS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 258 PIVMHDYLTgGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGEREIT 337
Cdd:cd08212  241 PIIMHDLLT-GFTAIQSLAKWCRDNGMLLHLHRAGHATYDRQKNHGIHFRVLAKWLRLSGVDHIHAGTVVGKLEGDPLVT 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 338 LGFVDLLRDDFIEKDRSRGIFFTQDWVSMPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAAANRV 417
Cdd:cd08212  320 LGFYDLLRDDYIEKDRSRGIFFTQDWASLPGVMPVASGGIHVGQMHQLIEIFGDDVVLQFGGGTIGHPWGIAAGATANRV 399
                        410       420       430
                 ....*....|....*....|....*....|..
gi 664806164 418 ALEACVQARNEGRDLAREGNEIIKAACKWSPE 449
Cdd:cd08212  400 ALEAMVQARNEGRDLAREGPEILREAAKWSPE 431
rbcL PRK04208
ribulose bisophosphate carboxylase; Reviewed
3-449 0e+00

ribulose bisophosphate carboxylase; Reviewed


Pssm-ID: 179787  Cd Length: 468  Bit Score: 853.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164   3 KASVGFKAGVKDYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHI 82
Cdd:PRK04208   1 MAKERYDAGVKEYRQMYWDPDYTPKDTDLLACFRITPQEGVDPEEAAAAVAAESSTGTWTTVWTDLLTDLDKYKAKAYRI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  83 EPVPGEPDQYICYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKYGR 162
Cdd:PRK04208  81 EDVPGDDGSYYAFIAYPLDLFEEGSIPNLLASIAGNVFGFKAVKALRLEDIRFPVAYVKTFKGPPFGIQVERERLDKYGR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 163 PLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAGTC 242
Cdd:PRK04208 161 PLLGTTPKPKLGLSAKNYGRVVYEALRGGLDFTKDDENLNSQPFNRWRDRFLFVMEAIDKAEAETGERKGHYLNVTAPTM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 243 EEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIH 322
Cdd:PRK04208 241 EEMYKRAEFAKELGSPIVMIDVVTAGWTALQSLREWCRDNGLALHAHRAMHAAFTRNPNHGISFRVLAKLLRLIGVDHLH 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 323 AGTVVGKLEGEREITLGFVDLLRDDFIEKDRSRGIFFTQDWVSMPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTL 402
Cdd:PRK04208 321 TGTVVGKLEGDRAEVLGYYDILREDFVPEDRSRGIFFDQDWGSIKPVFPVASGGIHPGHMPALLDIFGDDVVLQFGGGTH 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 664806164 403 GHPWGNAPGAAANRVALEACVQARNEGRDLAREGNEIIKAACKWSPE 449
Cdd:PRK04208 401 GHPDGTAAGATANRVALEACVEARNEGRDIEKEGPDILEEAAKWSPE 447
RuBisCO_large_I_II_III cd08206
Ribulose bisphosphate carboxylase large chain, Form I,II,III; Ribulose bisphosphate ...
29-449 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: 724.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  29 TDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVPgePDQYICYVAYPLDLFEEGSV 108
Cdd:cd08206    1 TDLLAAFRMTPAEGVDPEEAAAAVAAESSTGTWTTVWTDRLTATERLKAKVYRIDPVP--DGQYIAKIAYPLDLFEEGSV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 109 TNMFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRACYECL 188
Cdd:cd08206   79 PNLLTSIIGNVFGMKAVKALRLEDFRFPPAYLKTFDGPSFGIQGEREILGKYGRPLLGTIVKPKLGLSPKEYARVVYEAL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 189 RGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGG 268
Cdd:cd08206  159 RGGLDFVKDDENQNSQPFMRFEDRILFVAEAMDKAEAETGEAKGHYLNITADTPEEMIKRAEFAKELGSVIVMVDGVTAG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 269 FTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGEREITLGFVDLLRDDF 348
Cdd:cd08206  239 WTAIQSARRWCPDNGLALHAHRAGHAAFTRQKNHGISMRVLAKLARLIGVDHIHTGTVVGKLEGDPSEVKGIADMLREDE 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 349 IEKDRSRgIFFTQDWVSMPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAAANRVALEACVQARne 428
Cdd:cd08206  319 VEGDLSR-IFFNQDWGGMKPVFPVASGGLHPGRMPALIEILGDDVILQFGGGTHGHPDGPAAGAKANRQALEAWVQGR-- 395
                        410       420
                 ....*....|....*....|.
gi 664806164 429 grdlaregneIIKAACKWSPE 449
Cdd:cd08206  396 ----------ILREYAKTHKE 406
RuBisCO_large cd08148
Ribulose bisphosphate carboxylase large chain; Ribulose bisphosphate carboxylase (Rubisco) ...
31-418 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: 537.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  31 ILAAFRVTPQPgVPPEEAGAAVAAESSTGTWTTVWTdGLTSLDRYKGRCYHIEPVPgepDQYICYVAYPLDLFEEGSVTN 110
Cdd:cd08148    1 VLATYRVHPEA-TPPEKAAEAIAAESSTGTWTEVPT-TQEQLRRVKGRVYSVEELG---KRYIVKIAYPVELFEPGNIPQ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 111 MFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRACYECLRG 190
Cdd:cd08148   76 ILTVTAGNLFGLGALEAVRLEDLEFPEEYKKLFPGPKFGIDGIRKLLGVYGRPLVGTIIKPKLGLNPKYTAEAAYAAALG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 191 GLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAGTcEEMIKRAVFARELGVPIVMHDYLTGGFT 270
Cdd:cd08148  156 GLDLIKDDETLTDQPFCPLRDRITEVAAALDRVQEETGEKKLYAVNVTAGT-FEIIERAERALELGANMLMVDVLTAGFS 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 271 ANTSLAHYCRdNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGEREITLGFVDLLRDdfie 350
Cdd:cd08148  235 ALQALAEDFE-IDLPIHVHRAMHGAVTRSKFHGISMLVLAKLLRMAGGDFIHTGTVVGKMALEREEALGIADALTD---- 309
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 664806164 351 kdrsrgifftqDWVSMPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAAANRVA 418
Cdd:cd08148  310 -----------DWAGFKRVFPVASGGIHPGLVPGILRDFGIDVILQAGGGIHGHPDGTVAGARAMRQA 366
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
19-449 2.51e-172

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


Pssm-ID: 441455  Cd Length: 417  Bit Score: 489.68  E-value: 2.51e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  19 YYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVP---GEPDQYICY 95
Cdd:COG1850    2 YVDPDYIPDDDDILATYRITPETGVDPEEAAAAIAGEQSTGTWTEVPTETDELRERLAARVYSIEELPevgGGYRRALVT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  96 VAYPLDLFEeGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGL 175
Cdd:COG1850   82 IAYPLENFG-GNLPNLLSTVAGNLFGLKAVSGLRLLDLEFPESFLAAFPGPKFGIEGTRELLGVYDRPLLGTIIKPKVGL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 176 SAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAGTcEEMIKRAVFAREL 255
Cdd:COG1850  161 SPEETAELVYELALGGVDFIKDDENLADQPFCPFEDRVRAVMEAIDRAEEETGEKKMYAFNITADT-DEMLRRADLAVEL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 256 GVPIVMHDYLTGGFTANTSLAHycRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGERE 335
Cdd:COG1850  240 GANAVMVDVNTVGLSAVQTLRE--EHIGLPIHAHRAGHGAFTRSPLHGISMRVLAKLWRLAGADHLHVGTPVGKMEGDDE 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 336 ITLGFVDLLRddfiekdrsrgifftQDWVSMPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAAAN 415
Cdd:COG1850  318 EVLAIADALL---------------QPWGGLKPVFPVPSGGQHPGQVPELYDALGTDLILQAGGGIHGHPDGPAAGARAL 382
                        410       420       430
                 ....*....|....*....|....*....|....
gi 664806164 416 RVALEACVQarneGRDLAregneiikAACKWSPE 449
Cdd:COG1850  383 RQAWEAAVA----GIPLE--------EYAKTHPE 404
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
150-449 3.64e-164

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: 464.14  E-value: 3.64e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  150 IQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGE 229
Cdd:pfam00016   1 IAVERRVLNKYGRPILGTIIKPKLGLSPKNYARAVYEFLLGGLDFIKDDENINSQPFMPWRDRFLFVAEAIDRAQDETGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  230 IKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVL 309
Cdd:pfam00016  81 AKGHYLNITADDMEEMYRRAEFAKETGGVAVMVDGLVIGPTAITTLRRWFRDNGVILHYHRAGHGAVTRQSKHGISFRVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  310 AKALRMSGGDHIHAGTV-VGKLEGEREitlgfvDLLRDDFIEKDRSRGIFFTQDWVSMPGVIPVASGGIHVWHMPALTEI 388
Cdd:pfam00016 161 AKMARLAGADHLHTGTMgVGKLEGDPS------DTLRAYMLEEDRARGPFFDQDWGGMPAVMPVASGGIHAGQMPGLFDN 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 664806164  389 FGD-DSVLQFGGGTLGHPWGNAPGAAANRVALEACVqarnEGRDLAREGneiikaacKWSPE 449
Cdd:pfam00016 235 LGDsDVILQFGGGTFGHPDGPAAGAKANRQALEAWV----EGRDLEEYA--------KEHPE 284
RuBisCO_large_III cd08213
Ribulose bisphosphate carboxylase large chain, Form III; Ribulose bisphosphate carboxylase ...
29-446 3.12e-143

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: 415.63  E-value: 3.12e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  29 TDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEpvpGEPDQYICYVAYPLDLFEEGSV 108
Cdd:cd08213    1 DDLIAVFRIEPAEGISIEEAAGRVASESSIGTWTTLATLYPERAEKLKAKAYYFD---GLGGSYIVKVAYPLELFEEGNM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 109 TNMFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRACYECL 188
Cdd:cd08213   78 PQLLSSIAGNIFGMKAVKNLRLEDIYFPESYLREFKGPQFGIEGVREILGIKDRPLLGTVPKPKVGLSPEEHAEVAYEAL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 189 RGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAgTCEEMIKRAVFARELGVPIVMHDYLTGG 268
Cdd:cd08213  158 VGGVDLVKDDENLTSQPFNRFEERAKESLKARDKAEAETGERKAYLANITA-PVREMERRAELVADLGGKYVMIDVVVAG 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 269 FTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGEREITLGFVDLLRDDF 348
Cdd:cd08213  237 WSALQYLRDLAEDYGLAIHAHRAMHAAFTRNPRHGISMLVLAKLYRLIGVDQLHIGTAVGKMEGDKEEVLRIADILREQK 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 349 IEKDrSRGIFFTQDWVSMPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAAANRVALEACVqarnE 428
Cdd:cd08213  317 YKPD-EEDFHLAQDWGGIKPVFPVASGGLHPGLVPDVIDILGKDIVIQVGGGVHGHPDGTRAGAKAVRQAIEAAL----E 391
                        410       420
                 ....*....|....*....|.
gi 664806164 429 GRDL---AREGNEIIKAACKW 446
Cdd:cd08213  392 GISLdeyAKDHKELARALEKW 412
rubisco_III TIGR03326
ribulose bisphosphate carboxylase, type III; Members of this protein family are the archaeal, ...
24-446 9.02e-116

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: 345.22  E-value: 9.02e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164   24 YETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTdgLTSLDRYKGRCYHIEPVPGEPDQYICYVAYPLDLF 103
Cdd:TIGR03326   7 YEPSDDDLVCTFRITPAEGVSIEDAAGRVASESSIGTWTTLQP--WKDPERYKDLSAKVYDIEEHGDGSIVRIAYPLGLF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  104 EEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRA 183
Cdd:TIGR03326  85 EEGNLPQLLSCIAGNIFGMKAVKGLRLLDFEFPAEFLRAFKGPQFGIEGVREILGIKDRPITATVPKPKVGLSTEEHAKV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  184 CYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAGTcEEMIKRAVFARELGVPIVMHD 263
Cdd:TIGR03326 165 AYELWSGGVDLLKDDENLTSQAFNRFEERVEKSLKVRDKVEAETGEKKSYLINITADV-REMERRAELVADLGGEYVMVD 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  264 YLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTV-VGKLEGEREITLGFVD 342
Cdd:TIGR03326 244 IVVAGWSALQYVRERTEDLGLAIHAHRAMHAAFTRNPKHGISMFVLAKLYRLIGVDQLHTGTAgVGKLEGGNEDTKGIND 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  343 LLRddfiekdrsrgifftQDWVSMPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAAANRVALEAC 422
Cdd:TIGR03326 324 FLR---------------QDWHHIKPVFPVASGGLHPGLVPPLIDALGTDLVIQAGGGVHGHPDGTRAGAKALRAAIDAI 388
                         410       420
                  ....*....|....*....|....*..
gi 664806164  423 VqarnEGRDL---AREGNEIIKAACKW 446
Cdd:TIGR03326 389 I----EGISLeekAKSVPELKKALEKW 411
PRK13475 PRK13475
ribulose-bisphosphate carboxylase;
31-442 1.53e-64

ribulose-bisphosphate carboxylase;


Pssm-ID: 184072  Cd Length: 443  Bit Score: 214.20  E-value: 1.53e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  31 ILAAFRVTPQPGVPPEEAGAAVAAESSTGT-----WTTVWTDGLTSLdrykgrCYHIEPVPGepdqyICYVAYPLDLFE- 104
Cdd:PRK13475  24 ILCAYKMKPKAGHGYLEAAAHFAAESSTGTnvevsTTDDFTRGVDAL------VYEIDEARE-----LMKIAYPVELFDr 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 105 -----EGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIqverDKLNKY-GRP------LLGCTIKPK 172
Cdd:PRK13475  93 niidgRAMIVSFLTLTIGNNQGMGDVEYAKMHDFYVPPRYLELFDGPSTDI----SDLWRVlGRPvkdggyIAGTIIKPK 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 173 LGLSAKNYGRACYECLRGGlDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAGTCEEMIKRAVFA 252
Cdd:PRK13475 169 LGLRPEPFAEACYDFWLGG-DFIKNDEPQGNQVFAPLKKTVPLVADAMKRAQDETGEAKLFSANITADDHYEMIARGEYI 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 253 RELGVPIVMH-DYLTGGFTANTSLAHYCRDN--GLLLHIHRAMHAVIDRQKN-HGMHFRVLAKALRMSGGDHIHAGTV-V 327
Cdd:PRK13475 248 LETFGENADHvAFLVDGYVAGPGAVTTARRQypDQYLHYHRAGHGAVTSPSSkRGYTAFVLSKMARLQGASGIHTGTMgY 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 328 GKLEGEREitlgfvDLLRDDFIEKDRSRGIFFTQDWVSMPGVIPVASGGIHVWHMPALTEIFGDDSVLQ-FGGGTLGHPW 406
Cdd:PRK13475 328 GKMEGEAD------DRVIAYMIERDSAQGPFYHQEWYGMKPTTPIISGGMNALRLPGFFDNLGHGNVINtAGGGAFGHID 401
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 664806164 407 GNAPGAAANRVALEaCVQARNEGRDLAREGNEIIKA 442
Cdd:PRK13475 402 GPAAGAKSLRQAYD-CWKAGADPIEYAKEHKEFARA 436
RuBisCO_IV_RLP cd08205
Ribulose bisphosphate carboxylase like proteins, Rubisco-Form IV; Ribulose bisphosphate ...
57-418 2.20e-64

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: 211.62  E-value: 2.20e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  57 STGTWTTVWTDGLTSLDRYKGRCYHIEPVPGEPDQYICY---VAYPLDLFEeGSVTNMFTSIVGNVFGfkaLRALRLEDL 133
Cdd:cd08205   26 TVGTWTELPGETEEIRERHVGRVESIEELEESEGKYGRArvtISYPLDNFG-GDLPQLLNTLFGNLSL---LPGIKLVDL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 134 RIPPTYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRF 213
Cdd:cd08205  102 ELPDSLLAAFPGPRFGIEGLRRLLGVHDRPLLGTIIKPSIGLSPEELAELAYELALGGIDLIKDDELLADQPYAPFEERV 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 214 VFCAEAIYKSQAETGEIKGHYLNATAGTcEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAhycRDNGLLLHIHRAMH 293
Cdd:cd08205  182 RACMEAVRRANEETGRKTLYAPNITGDP-DELRRRADRAVEAGANALLINPNLVGLDALRALA---EDPDLPIMAHPAFA 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 294 AVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGEREITLGFVDLLRddfiekdrsrgifftQDWVSMPGVIPVA 373
Cdd:cd08205  258 GALSRSPDYGSHFLLLGKLMRLAGADAVIFPGPGGRFPFSREECLAIARACR---------------RPLGGIKPALPVP 322
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 664806164 374 SGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAAANRVA 418
Cdd:cd08205  323 SGGMHPGRVPELYRDYGPDVILLAGGGILGHPDGAAAGVRAFRQA 367
RuBisCO_large_II cd08211
Ribulose bisphosphate carboxylase large chain, Form II; Ribulose bisphosphate carboxylase ...
31-442 7.88e-63

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: 209.66  E-value: 7.88e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  31 ILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTV-WTDGLT-SLDrykGRCYHIEPvpgepDQYICYVAYPLDLFE---- 104
Cdd:cd08211   23 VLVAYIMKPKAGYGYLATAAHFAAESSTGTNVEVsTTDDFTrGVD---ALVYEIDE-----ARELMKIAYPVELFDrnlt 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 105 --EGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKY---GRPLLGCTIKPKLGLSAKN 179
Cdd:cd08211   95 dgRAMVASFLTLIIGNNQGMGDVEYLKMHDFYVPESMLELFDGPSVNISDMWKVLGRPevdGGYIAGTIIKPKLGLRPKP 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 180 YGRACYECLRGGlDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPI 259
Cdd:cd08211  175 FAEACYAFWLGG-DFIKNDEPQANQPFCPLKKVIPLVADAMRRAQDETGEAKLFSANITADDPDEMIARGEYILEAFGPN 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 260 VMH-----DYLTGGFTANTSLAHYCRDNglLLHIHRAMHAVIDRQKNH-GMHFRVLAKALRMSGGDHIHAGTV-VGKLEG 332
Cdd:cd08211  254 AGHvaflvDGYVAGPAAVTTARRRFPDQ--FLHYHRAGHGAVTSPQSKrGYTAFVLSKMARLQGASGIHTGTMgFGKMEG 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 333 EREitlgfvDLLRDDFIEKDRSRGIFFTQDWVSMPGVIPVASGGIHVWHMPALTEIFGDDSVLQ-FGGGTLGHPWGNAPG 411
Cdd:cd08211  332 ESS------DKVIAYMIERDEAQGPLFNQKWYGMKPTTPIISGGMNALRLPGFFENLGNGNVILtAGGGSFGHIDGPAAG 405
                        410       420       430
                 ....*....|....*....|....*....|.
gi 664806164 412 AAANRVALEACVQARNEgRDLAREGNEIIKA 442
Cdd:cd08211  406 AKSLRQAYDAWKQGVDV-IEYAKEHKELARA 435
RuBisCO_large_N pfam02788
Ribulose bisphosphate carboxylase large chain, N-terminal domain; The N-terminal domain of ...
18-139 2.78e-52

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: 171.63  E-value: 2.78e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164   18 TYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVPGepDQYICYVA 97
Cdd:pfam02788   1 DYVDLDYEPKDTDLLCAFRIEPAAGVSPEEAAAHVAAESSTGTWTEVWTLDDTFTKKLKAKVYEIDEVPG--GSYIVKIA 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 664806164   98 YPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPTY 139
Cdd:pfam02788  79 YPLDLFEEGSIPQLLSSIAGNIFGMKAVKALRLEDIRFPPAY 120
RLP_NonPhot cd08207
Ribulose bisphosphate carboxylase like proteins from nonphototrophic bacteria; Ribulose ...
57-424 4.00e-44

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: 159.01  E-value: 4.00e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  57 STGTWTTV--WTDGLTslDRYKGRCYHIEPVPGEPDQYI-------CY------VAYPLDLFEEgSVTNMFTSIVGNVFG 121
Cdd:cd08207   26 SSGTFIALpgETDELK--ERSAARVESIEELETAAQPSLprrasggPYtrarvtISFPLDNIGT-SLPNLLATVAGNLFE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 122 FKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENV 201
Cdd:cd08207  103 LRELSGLRLVDLGLPDEFAAAFPGPAFGIAGTRRLTGVEDRPLIGTIIKPSVGLTPEETAALVRQLAAAGIDFIKDDELL 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 202 NSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATaGTCEEMIKRAVFARELGVPIVMHDYLTGGFTAntsLAHYCRD 281
Cdd:cd08207  183 ANPPYSPLDERVRAVMRVINDHAQRTGRKVMYAFNIT-DDIDEMRRNHDLVVEAGGTCVMVSLNSVGLSG---LAALRRH 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 282 NGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKL-EGEREITLGFVDLLRDdfiekdrsrgiFFT 360
Cdd:cd08207  259 SQLPIHGHRNGWGMLTRSPALGISFQAYQKLWRLAGVDHLHVNGLASKFwESDDSVIESARACLTP-----------LGG 327
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 664806164 361 QDWVSMpgviPVASGGIHVWHMPALTEIFGDDSVLQF-GGGTLGHPWGNAPGAAANRVALEACVQ 424
Cdd:cd08207  328 PDDAAM----PVFSSGQWGGQAPPTYRRLGSVDLLYLaGGGIMAHPDGPAAGVRSLRQAWEAAVA 388
RLP_DK-MTP-1-P-enolase cd08209
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Ribulose bisphosphate carboxylase like ...
59-446 9.55e-38

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: 141.69  E-value: 9.55e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  59 GTWTTVWTDGLTSLDRYKGRCYHIEPvpGEPDQYICYVAYPLdlfeeGSVTNMFTSIVGNVFGFKALR-ALRLEDLRIPP 137
Cdd:cd08209   27 GSWTDLPALRQAQLQKHLGEVVSVEE--LEEGRGVITIAYPL-----INVSGDIPALLTTIFGKLSLDgKIKLVDLRLPE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 138 TYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCA 217
Cdd:cd08209  100 EFGRAFPGPKFGIEGIRQRLGVHDRPLLMSIFKGVLGLDLDDLAEQLREQALGGVDLIKDDEILFDNPLAPALERIRACR 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 218 EAIYKSQAETGEIKGHYLNATaGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAhycRDNGLLLHI--HRAMHAV 295
Cdd:cd08209  180 PVLQEVYEQTGRRTLYAVNLT-GPVFTLKEKARRLVEAGANALLFNVFAYGLDVLEALA---SDPEINVPIfaHPAFAGA 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 296 IDRQKNHGM-HFRVLAKALRMSGGDHIHAGTVVGKLEGEREITLGFVDLLRDDfiekDRSRGIFftqdwvsmpgviPVAS 374
Cdd:cd08209  256 LYGSPDYGIaASVLLGTLMRLAGADAVLFPSPYGSVALSKEEALAIAEALRRG----GAFKGVF------------PVPS 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 664806164 375 GGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAAANRVALEACVQarNEGRDLAREGNEIIKAAC-KW 446
Cdd:cd08209  320 AGIHPGLVPQLLRDFGTDVILNAGGGIHGHPDGAAAGVRAFREAIDAVLA--GESLEPAAIPDGPLKSALdKW 390
mtnW PRK09549
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Reviewed
59-446 2.57e-34

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


Pssm-ID: 236560  Cd Length: 407  Bit Score: 132.44  E-value: 2.57e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  59 GTWTTVWTDGLTSLDRYKGRCYHIEPVPGEPD----QYICYVAYPldlfeEGSVTNMFTSIVGNVFGFKALRA-LRLEDL 133
Cdd:PRK09549  31 GSWTDLPHLEQEQLKKHKGNVVHVEELEEHERkgvkRGIIKIAYP-----LANFSPDLPAILTTTFGKLSLDGeVKLIDL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 134 RIPPTYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRF 213
Cdd:PRK09549 106 TFSDELKRHFPGPKFGIDGIRNLLGVHDRPLLMSIFKGVIGRDLDYLKEQLRDQALGGVDLVKDDEILFENALTPFEKRI 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 214 VFCAEAIYKSQAETGEIKGHYLNATAGTCE--EMIKRAVfarELGVPIVMHDYLTGGFTANTSLAhycRDNGLLLHI--H 289
Cdd:PRK09549 186 VAGKEVLQEVYETTGHKTLYAVNLTGRTFElkEKAKRAA---EAGADALLFNVFAYGLDVLQSLA---EDPEIPVPImaH 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 290 RAMHAVIDRQKNHGM-HFRVLAKALRMSGGDHIHAGTVVGKLEGEREITLGFVDLLRDdfiEKDRSRGIFftqdwvsmpg 368
Cdd:PRK09549 260 PAVSGAYTPSPLYGIsSPLLLGKLLRYAGADFSLFPSPYGSVALEKEEALAIAKELTE---DDDPFKRSF---------- 326
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 664806164 369 viPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAAANRVALEACVQARNEgRDLAREGNEIIKAACKW 446
Cdd:PRK09549 327 --PVPSAGIHPGLVPLLIRDFGKDVVINAGGGIHGHPNGAQGGGKAFRAAIDAVLQGKPL-HEAAEDDENLHSALDIW 401
RLP_RrRLP cd08210
Ribulose bisphosphate carboxylase like proteins (RLPs) similar to R.rubrum RLP; RLP from ...
72-405 7.32e-30

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: 119.27  E-value: 7.32e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  72 LDRYKGRCYHIEPVpgEPDQYICYVAYPLDlfeegSVTNMFTSIVGNVFGFKAL-RALRLEDLRIPPTYSKTFQGPPHGI 150
Cdd:cd08210   42 RDNIVGRVESLEPA--GEGSYRARISYSVD-----TAGGELTQLLNVLFGNSSLqPGIRLVDFELPPSLLRRFPGPRFGI 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 151 QVERDKLNKYGRPLLGCTIKPkLGLSAKNYGRACYECLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGei 230
Cdd:cd08210  115 AGLRALLGIPERPLLCSALKP-QGLSAAELAELAYAFALGGIDIIKDDHGLADQPFAPFEERVKACQEAVAEANAETG-- 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 231 kGH--YLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAhycRDNGLLLHIHRAMHAVIDRQKNHGM-HFR 307
Cdd:cd08210  192 -GRtlYAPNVTGPPTQLLERARFAKEAGAGGVLIAPGLTGLDTFRELA---EDFDFLPILAHPAFAGAFVSSGDGIsHAL 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 308 VLAKALRMSGGDHI---HAGtvvGKLEGEREITLGFVDLLRddfiekdrsrgifftQDWVSMPGVIPVASGGIHVWHMPA 384
Cdd:cd08210  268 LFGTLFRLAGADAVifpNYG---GRFGFSREECQAIADACR---------------RPMGGLKPILPAPGGGMSVERAPE 329
                        330       340
                 ....*....|....*....|.
gi 664806164 385 LTEIFGDDSVLQFGGGTLGHP 405
Cdd:cd08210  330 MVELYGPDVMLLIGGSLLRAG 350
RLP_Photo cd08208
Ribulose bisphosphate carboxylase like proteins from phototrophic bacteria; Ribulose ...
108-424 1.15e-22

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: 99.58  E-value: 1.15e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 108 VTNMFTSIVGN-VFGFKALRALRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRACYE 186
Cdd:cd08208  105 IPNLLSAVCGEgTFFSPGVPVVKLMDIHFPETYLADFEGPKFGIAGLRERLQAHDRPIFFGVIKPNIGLPPGEFAELGYQ 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 187 CLRGGLDFTKDDENVNSQPFMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATaGTCEEMIKRAVFARELGVPIVMHDYLT 266
Cdd:cd08208  185 SWLGGLDIAKDDEMLADVDWCPLEERAALLGKARRRAEAETGVPKIYLANIT-DEVDRLMELHDVAVRNGANALLINAMP 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164 267 GGFTANTSLAHYCRdngLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDhihagTVVGKLEGEREITLGfvDLLRD 346
Cdd:cd08208  264 VGLSAVRMLRKHAQ---VPLIAHFPFIASFSRLEKYGIHSRVMTKLQRLAGLD-----VVIMPGFGPRMMTPE--EEVLE 333
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 664806164 347 DFIEKDRSRGifftqdwvSMPGVIPVASGGIHVWHMPALTEIFGD-DSVLQFGGGTLGHPWGNAPGAAANRVALEACVQ 424
Cdd:cd08208  334 CVIACLEPMG--------PIKPCLPVPGGSDSALTLQTVYEKVGNvDFGFVPGRGVFGHPMGPKAGAKSIRQAWEAIEA 404
salvage_mtnW TIGR03332
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Members of this family are the methionine ...
57-446 3.24e-22

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: 97.98  E-value: 3.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164   57 STGTWTTVWTDGLTSLDRYKGRCYHIEPVPG----------EPDQYICYVAYPLDLFeegsvTNMFTSIVGNVFGFKALR 126
Cdd:TIGR03332  28 TIGSWTDLPLLKQEQLKKHKGRVVHVEELAEsehtnsylrkKVKRAIIKIAYPELNF-----SPDLPALLTTTFGKLSLD 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  127 A-LRLEDLRIPPTYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRACYECLRGGLDFTKDDENVNSQP 205
Cdd:TIGR03332 103 GeVKLIDLEFSDEFKRHFPGPKFGIDGIRKLLGVHERPLLMSIFKGMIGRDLGYLKEQLRQQALGGVDLVKDDEILFETG 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  206 FMRWRDRFVFCAEAIYKSQAETGEIKGHYLNATAGTCE--EMIKRAVfarELGVPIVMHDYLTGGFTANTSLAHycrDNG 283
Cdd:TIGR03332 183 LAPFEKRITEGKEVLQEVYEQTGHKTLYAVNLTGRTFDlkDKAKRAA---ELGADVLLFNVFAYGLDVLQSLAE---DDE 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  284 LLLHI--HRAMHAVIDRQKNHGM-HFRVLAKALRMSGGDHIHAGTVVGKLEGEREITLGFVDLLrddfiekdrsrgiffT 360
Cdd:TIGR03332 257 IPVPImaHPAVSGAYTSSPFYGFsHSLLLGKLLRYAGADFSLFPSPYGSVALEREDALAISKEL---------------T 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 664806164  361 QDWVSMPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAAANRVALEACVQARnEGRDLAREGNEII 440
Cdd:TIGR03332 322 EDDAPFKKTFAVPSAGIHPGMVPLIMRDFGIDHIINAGGGIHGHPNGAQGGGRAFRAAIDAVLEAK-PLHEKAADDIDLK 400

                  ....*.
gi 664806164  441 KAACKW 446
Cdd:TIGR03332 401 LALDKW 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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