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Conserved domains on  [gi|221078579|gb|ACL99364|]
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ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit, partial (plastid) [Diospyros toposia]

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
1-464 0e+00

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


:

Pssm-ID: 176981  Cd Length: 475  Bit Score: 1056.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579   1 GFKAGVKDYKLNYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTAVWTDGLTSLDRYKGRCYHIEPVA 80
Cdd:CHL00040  12 GFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYRIEPVP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  81 GEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTSYVKTFQGPPHGIQVERDKLNKYGRPLLG 160
Cdd:CHL00040  92 GEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYLKTFQGPPHGIQVERDKLNKYGRPLLG 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 161 CTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFCFCAEAIYKAQAETGEIKGHYLNATAGTCEEMM 240
Cdd:CHL00040 172 CTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMY 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 241 KRAIFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHVHAGTV 320
Cdd:CHL00040 252 KRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHAGTV 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 321 VGKLEGEREITLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPW 400
Cdd:CHL00040 332 VGKLEGEREMTLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPW 411
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221078579 401 GNAPGAVANRVSLEACVQARNEGRDLAREGNEIIREASKWSPELAAACEVWKEIKFEFEAMDTL 464
Cdd:CHL00040 412 GNAPGAVANRVALEACVQARNEGRDLAREGNEIIREAAKWSPELAAACEVWKEIKFEFETTDTL 475
 
Name Accession Description Interval E-value
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
1-464 0e+00

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


Pssm-ID: 176981  Cd Length: 475  Bit Score: 1056.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579   1 GFKAGVKDYKLNYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTAVWTDGLTSLDRYKGRCYHIEPVA 80
Cdd:CHL00040  12 GFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYRIEPVP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  81 GEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTSYVKTFQGPPHGIQVERDKLNKYGRPLLG 160
Cdd:CHL00040  92 GEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYLKTFQGPPHGIQVERDKLNKYGRPLLG 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 161 CTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFCFCAEAIYKAQAETGEIKGHYLNATAGTCEEMM 240
Cdd:CHL00040 172 CTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMY 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 241 KRAIFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHVHAGTV 320
Cdd:CHL00040 252 KRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHAGTV 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 321 VGKLEGEREITLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPW 400
Cdd:CHL00040 332 VGKLEGEREMTLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPW 411
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221078579 401 GNAPGAVANRVSLEACVQARNEGRDLAREGNEIIREASKWSPELAAACEVWKEIKFEFEAMDTL 464
Cdd:CHL00040 412 GNAPGAVANRVALEACVQARNEGRDLAREGNEIIREAAKWSPELAAACEVWKEIKFEFETTDTL 475
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
13-462 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: 942.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  13 YYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTAVWTDGLTSLDRYKGRCYHIEPVAGEENQYIAYVAY 92
Cdd:cd08212    2 YWTPDYQPKDTDILAAFRITPQPGVDPEEAAAAVAGESSTATWTVVWTDRLTALDRYKGKAYRVEPVPGEENQYFAYIAY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  93 PLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTSYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAK 172
Cdd:cd08212   82 PLDLFEEGSVANLTTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDRLNKYGRPLLGCTIKPKLGLSAK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 173 NYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFCFCAEAIYKAQAETGEIKGHYLNATAGTCEEMMKRAIFARELGVP 252
Cdd:cd08212  162 NYGRVVYECLRGGLDFTKDDENINSQPFMRWRDRFLFVAEAVNKAQAETGEVKGHYLNVTAGTMEEMYKRAEFAKELGSP 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 253 IVMHDYLTgGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHVHAGTVVGKLEGEREITL 332
Cdd:cd08212  242 IIMHDLLT-GFTAIQSLAKWCRDNGMLLHLHRAGHATYDRQKNHGIHFRVLAKWLRLSGVDHIHAGTVVGKLEGDPLVTL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 333 GFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVS 412
Cdd:cd08212  321 GFYDLLRDDYIEKDRSRGIFFTQDWASLPGVMPVASGGIHVGQMHQLIEIFGDDVVLQFGGGTIGHPWGIAAGATANRVA 400
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 221078579 413 LEACVQARNEGRDLAREGNEIIREASKWSPELAAACEVWKEIKFEFEAMD 462
Cdd:cd08212  401 LEAMVQARNEGRDLAREGPEILREAAKWSPELAAALETWKDIKFEFESTD 450
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
12-456 2.50e-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: 507.78  E-value: 2.50e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  12 NYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTAVWTDGLTSLDRYKGRCYHIEPV---AGEENQYIA 88
Cdd:COG1850    1 DYVDPDYIPDDDDILATYRITPETGVDPEEAAAAIAGEQSTGTWTEVPTETDELRERLAARVYSIEELpevGGGYRRALV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  89 YVAYPLDLFEeGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTSYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLG 168
Cdd:COG1850   81 TIAYPLENFG-GNLPNLLSTVAGNLFGLKAVSGLRLLDLEFPESFLAAFPGPKFGIEGTRELLGVYDRPLLGTIIKPKVG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 169 LSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFCFCAEAIYKAQAETGEIKGHYLNATAGTcEEMMKRAIFARE 248
Cdd:COG1850  160 LSPEETAELVYELALGGVDFIKDDENLADQPFCPFEDRVRAVMEAIDRAEEETGEKKMYAFNITADT-DEMLRRADLAVE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 249 LGVPIVMHDYLTGGFTANTSLAHycRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHVHAGTVVGKLEGER 328
Cdd:COG1850  239 LGANAVMVDVNTVGLSAVQTLRE--EHIGLPIHAHRAGHGAFTRSPLHGISMRVLAKLWRLAGADHLHVGTPVGKMEGDD 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 329 EITLGFVDLLRddfiekdrsrgiyftQDWVSLPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVA 408
Cdd:COG1850  317 EEVLAIADALL---------------QPWGGLKPVFPVPSGGQHPGQVPELYDALGTDLILQAGGGIHGHPDGPAAGARA 381
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 221078579 409 NRVSLEACVQarneGRDLAregneiirEASKWSPELAAACEVWKEIKF 456
Cdd:COG1850  382 LRQAWEAAVA----GIPLE--------EYAKTHPELAAALEKWGKKAP 417
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
144-451 6.85e-167

Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of RuBisCO large chain is the catalytic domain adopting a TIM barrel fold.


Pssm-ID: 459631  Cd Length: 292  Bit Score: 471.46  E-value: 6.85e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  144 IQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFCFCAEAIYKAQAETGE 223
Cdd:pfam00016   1 IAVERRVLNKYGRPILGTIIKPKLGLSPKNYARAVYEFLLGGLDFIKDDENINSQPFMPWRDRFLFVAEAIDRAQDETGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  224 IKGHYLNATAGTCEEMMKRAIFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVL 303
Cdd:pfam00016  81 AKGHYLNITADDMEEMYRRAEFAKETGGVAVMVDGLVIGPTAITTLRRWFRDNGVILHYHRAGHGAVTRQSKHGISFRVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  304 AKALRLSGGDHVHAGTV-VGKLEGEREitlgfvDLLRDDFIEKDRSRGIYFTQDWVSLPGVIPVASGGIHVWHMPALTEI 382
Cdd:pfam00016 161 AKMARLAGADHLHTGTMgVGKLEGDPS------DTLRAYMLEEDRARGPFFDQDWGGMPAVMPVASGGIHAGQMPGLFDN 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  383 FGD-DSVLQFGGGTLGHPWGNAPGAVANRVSLEACVqarnEGRDLAREgneiireaSKWSPELAAACEVW 451
Cdd:pfam00016 235 LGDsDVILQFGGGTFGHPDGPAAGAKANRQALEAWV----EGRDLEEY--------AKEHPELARAFESW 292
rubisco_III TIGR03326
ribulose bisphosphate carboxylase, type III; Members of this protein family are the archaeal, ...
18-451 1.55e-117

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: 350.61  E-value: 1.55e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579   18 YETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTAVWTdgLTSLDRYKGRCYHIEPVAGEENQYIAYVAYPLDLF 97
Cdd:TIGR03326   7 YEPSDDDLVCTFRITPAEGVSIEDAAGRVASESSIGTWTTLQP--WKDPERYKDLSAKVYDIEEHGDGSIVRIAYPLGLF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579   98 EEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTSYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRA 177
Cdd:TIGR03326  85 EEGNLPQLLSCIAGNIFGMKAVKGLRLLDFEFPAEFLRAFKGPQFGIEGVREILGIKDRPITATVPKPKVGLSTEEHAKV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  178 VYECLRGGLDFTKDDENVNSQPFMRWRDRFCFCAEAIYKAQAETGEIKGHYLNATAGTcEEMMKRAIFARELGVPIVMHD 257
Cdd:TIGR03326 165 AYELWSGGVDLLKDDENLTSQAFNRFEERVEKSLKVRDKVEAETGEKKSYLINITADV-REMERRAELVADLGGEYVMVD 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  258 YLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHVHAGTV-VGKLEGEREITLGFVD 336
Cdd:TIGR03326 244 IVVAGWSALQYVRERTEDLGLAIHAHRAMHAAFTRNPKHGISMFVLAKLYRLIGVDQLHTGTAgVGKLEGGNEDTKGIND 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  337 LLRddfiekdrsrgiyftQDWVSLPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVSLEAC 416
Cdd:TIGR03326 324 FLR---------------QDWHHIKPVFPVASGGLHPGLVPPLIDALGTDLVIQAGGGVHGHPDGTRAGAKALRAAIDAI 388
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 221078579  417 VqarnEGRDLaregneiiREASKWSPELAAACEVW 451
Cdd:TIGR03326 389 I----EGISL--------EEKAKSVPELKKALEKW 411
 
Name Accession Description Interval E-value
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
1-464 0e+00

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


Pssm-ID: 176981  Cd Length: 475  Bit Score: 1056.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579   1 GFKAGVKDYKLNYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTAVWTDGLTSLDRYKGRCYHIEPVA 80
Cdd:CHL00040  12 GFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYRIEPVP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  81 GEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTSYVKTFQGPPHGIQVERDKLNKYGRPLLG 160
Cdd:CHL00040  92 GEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYLKTFQGPPHGIQVERDKLNKYGRPLLG 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 161 CTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFCFCAEAIYKAQAETGEIKGHYLNATAGTCEEMM 240
Cdd:CHL00040 172 CTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMY 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 241 KRAIFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHVHAGTV 320
Cdd:CHL00040 252 KRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHAGTV 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 321 VGKLEGEREITLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPW 400
Cdd:CHL00040 332 VGKLEGEREMTLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPW 411
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221078579 401 GNAPGAVANRVSLEACVQARNEGRDLAREGNEIIREASKWSPELAAACEVWKEIKFEFEAMDTL 464
Cdd:CHL00040 412 GNAPGAVANRVALEACVQARNEGRDLAREGNEIIREAAKWSPELAAACEVWKEIKFEFETTDTL 475
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
13-462 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: 942.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  13 YYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTAVWTDGLTSLDRYKGRCYHIEPVAGEENQYIAYVAY 92
Cdd:cd08212    2 YWTPDYQPKDTDILAAFRITPQPGVDPEEAAAAVAGESSTATWTVVWTDRLTALDRYKGKAYRVEPVPGEENQYFAYIAY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  93 PLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTSYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAK 172
Cdd:cd08212   82 PLDLFEEGSVANLTTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDRLNKYGRPLLGCTIKPKLGLSAK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 173 NYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFCFCAEAIYKAQAETGEIKGHYLNATAGTCEEMMKRAIFARELGVP 252
Cdd:cd08212  162 NYGRVVYECLRGGLDFTKDDENINSQPFMRWRDRFLFVAEAVNKAQAETGEVKGHYLNVTAGTMEEMYKRAEFAKELGSP 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 253 IVMHDYLTgGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHVHAGTVVGKLEGEREITL 332
Cdd:cd08212  242 IIMHDLLT-GFTAIQSLAKWCRDNGMLLHLHRAGHATYDRQKNHGIHFRVLAKWLRLSGVDHIHAGTVVGKLEGDPLVTL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 333 GFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVS 412
Cdd:cd08212  321 GFYDLLRDDYIEKDRSRGIFFTQDWASLPGVMPVASGGIHVGQMHQLIEIFGDDVVLQFGGGTIGHPWGIAAGATANRVA 400
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 221078579 413 LEACVQARNEGRDLAREGNEIIREASKWSPELAAACEVWKEIKFEFEAMD 462
Cdd:cd08212  401 LEAMVQARNEGRDLAREGPEILREAAKWSPELAAALETWKDIKFEFESTD 450
rbcL PRK04208
ribulose bisophosphate carboxylase; Reviewed
1-464 0e+00

ribulose bisophosphate carboxylase; Reviewed


Pssm-ID: 179787  Cd Length: 468  Bit Score: 885.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579   1 GFKAGVKDYKLNYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTAVWTDGLTSLDRYKGRCYHIEPVA 80
Cdd:PRK04208   5 RYDAGVKEYRQMYWDPDYTPKDTDLLACFRITPQEGVDPEEAAAAVAAESSTGTWTTVWTDLLTDLDKYKAKAYRIEDVP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  81 GEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTSYVKTFQGPPHGIQVERDKLNKYGRPLLG 160
Cdd:PRK04208  85 GDDGSYYAFIAYPLDLFEEGSIPNLLASIAGNVFGFKAVKALRLEDIRFPVAYVKTFKGPPFGIQVERERLDKYGRPLLG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 161 CTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFCFCAEAIYKAQAETGEIKGHYLNATAGTCEEMM 240
Cdd:PRK04208 165 TTPKPKLGLSAKNYGRVVYEALRGGLDFTKDDENLNSQPFNRWRDRFLFVMEAIDKAEAETGERKGHYLNVTAPTMEEMY 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 241 KRAIFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHVHAGTV 320
Cdd:PRK04208 245 KRAEFAKELGSPIVMIDVVTAGWTALQSLREWCRDNGLALHAHRAMHAAFTRNPNHGISFRVLAKLLRLIGVDHLHTGTV 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 321 VGKLEGEREITLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPW 400
Cdd:PRK04208 325 VGKLEGDRAEVLGYYDILREDFVPEDRSRGIFFDQDWGSIKPVFPVASGGIHPGHMPALLDIFGDDVVLQFGGGTHGHPD 404
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221078579 401 GNAPGAVANRVSLEACVQARNEGRDLAREGNEIIREASKWSPELAAACEVWKEIKFEFEAMDTL 464
Cdd:PRK04208 405 GTAAGATANRVALEACVEARNEGRDIEKEGPDILEEAAKWSPELAAALEKWGEIKFEFDTVDTL 468
RuBisCO_large_I_II_III cd08206
Ribulose bisphosphate carboxylase large chain, Form I,II,III; Ribulose bisphosphate ...
23-451 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: 730.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  23 TDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTAVWTDGLTSLDRYKGRCYHIEPVAgeENQYIAYVAYPLDLFEEGSV 102
Cdd:cd08206    1 TDLLAAFRMTPAEGVDPEEAAAAVAAESSTGTWTTVWTDRLTATERLKAKVYRIDPVP--DGQYIAKIAYPLDLFEEGSV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 103 TNMFTSIVGNVFGFKALRALRLEDLRIPTSYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECL 182
Cdd:cd08206   79 PNLLTSIIGNVFGMKAVKALRLEDFRFPPAYLKTFDGPSFGIQGEREILGKYGRPLLGTIVKPKLGLSPKEYARVVYEAL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 183 RGGLDFTKDDENVNSQPFMRWRDRFCFCAEAIYKAQAETGEIKGHYLNATAGTCEEMMKRAIFARELGVPIVMHDYLTGG 262
Cdd:cd08206  159 RGGLDFVKDDENQNSQPFMRFEDRILFVAEAMDKAEAETGEAKGHYLNITADTPEEMIKRAEFAKELGSVIVMVDGVTAG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 263 FTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHVHAGTVVGKLEGEREITLGFVDLLRDDF 342
Cdd:cd08206  239 WTAIQSARRWCPDNGLALHAHRAGHAAFTRQKNHGISMRVLAKLARLIGVDHIHTGTVVGKLEGDPSEVKGIADMLREDE 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 343 IEKDRSRgIYFTQDWVSLPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVSLEACVQARne 422
Cdd:cd08206  319 VEGDLSR-IFFNQDWGGMKPVFPVASGGLHPGRMPALIEILGDDVILQFGGGTHGHPDGPAAGAKANRQALEAWVQGR-- 395
                        410       420
                 ....*....|....*....|....*....
gi 221078579 423 grdlaregneIIREASKWSPELAAACEVW 451
Cdd:cd08206  396 ----------ILREYAKTHKELAAALEKW 414
RuBisCO_large cd08148
Ribulose bisphosphate carboxylase large chain; Ribulose bisphosphate carboxylase (Rubisco) ...
25-412 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: 529.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  25 ILAAFRVTPQPgVPPEEAGAAVAAESSTGTWTAVWTdGLTSLDRYKGRCYHIEPVAgeeNQYIAYVAYPLDLFEEGSVTN 104
Cdd:cd08148    1 VLATYRVHPEA-TPPEKAAEAIAAESSTGTWTEVPT-TQEQLRRVKGRVYSVEELG---KRYIVKIAYPVELFEPGNIPQ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 105 MFTSIVGNVFGFKALRALRLEDLRIPTSYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRG 184
Cdd:cd08148   76 ILTVTAGNLFGLGALEAVRLEDLEFPEEYKKLFPGPKFGIDGIRKLLGVYGRPLVGTIIKPKLGLNPKYTAEAAYAAALG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 185 GLDFTKDDENVNSQPFMRWRDRFCFCAEAIYKAQAETGEIKGHYLNATAGTcEEMMKRAIFARELGVPIVMHDYLTGGFT 264
Cdd:cd08148  156 GLDLIKDDETLTDQPFCPLRDRITEVAAALDRVQEETGEKKLYAVNVTAGT-FEIIERAERALELGANMLMVDVLTAGFS 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 265 ANTSLAHYCRdNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHVHAGTVVGKLEGEREITLGFVDLLRDdfie 344
Cdd:cd08148  235 ALQALAEDFE-IDLPIHVHRAMHGAVTRSKFHGISMLVLAKLLRMAGGDFIHTGTVVGKMALEREEALGIADALTD---- 309
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221078579 345 kdrsrgiyftqDWVSLPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVS 412
Cdd:cd08148  310 -----------DWAGFKRVFPVASGGIHPGLVPGILRDFGIDVILQAGGGIHGHPDGTVAGARAMRQA 366
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
12-456 2.50e-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: 507.78  E-value: 2.50e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  12 NYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTAVWTDGLTSLDRYKGRCYHIEPV---AGEENQYIA 88
Cdd:COG1850    1 DYVDPDYIPDDDDILATYRITPETGVDPEEAAAAIAGEQSTGTWTEVPTETDELRERLAARVYSIEELpevGGGYRRALV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  89 YVAYPLDLFEeGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTSYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLG 168
Cdd:COG1850   81 TIAYPLENFG-GNLPNLLSTVAGNLFGLKAVSGLRLLDLEFPESFLAAFPGPKFGIEGTRELLGVYDRPLLGTIIKPKVG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 169 LSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFCFCAEAIYKAQAETGEIKGHYLNATAGTcEEMMKRAIFARE 248
Cdd:COG1850  160 LSPEETAELVYELALGGVDFIKDDENLADQPFCPFEDRVRAVMEAIDRAEEETGEKKMYAFNITADT-DEMLRRADLAVE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 249 LGVPIVMHDYLTGGFTANTSLAHycRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHVHAGTVVGKLEGER 328
Cdd:COG1850  239 LGANAVMVDVNTVGLSAVQTLRE--EHIGLPIHAHRAGHGAFTRSPLHGISMRVLAKLWRLAGADHLHVGTPVGKMEGDD 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 329 EITLGFVDLLRddfiekdrsrgiyftQDWVSLPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVA 408
Cdd:COG1850  317 EEVLAIADALL---------------QPWGGLKPVFPVPSGGQHPGQVPELYDALGTDLILQAGGGIHGHPDGPAAGARA 381
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 221078579 409 NRVSLEACVQarneGRDLAregneiirEASKWSPELAAACEVWKEIKF 456
Cdd:COG1850  382 LRQAWEAAVA----GIPLE--------EYAKTHPELAAALEKWGKKAP 417
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
144-451 6.85e-167

Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of RuBisCO large chain is the catalytic domain adopting a TIM barrel fold.


Pssm-ID: 459631  Cd Length: 292  Bit Score: 471.46  E-value: 6.85e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  144 IQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFCFCAEAIYKAQAETGE 223
Cdd:pfam00016   1 IAVERRVLNKYGRPILGTIIKPKLGLSPKNYARAVYEFLLGGLDFIKDDENINSQPFMPWRDRFLFVAEAIDRAQDETGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  224 IKGHYLNATAGTCEEMMKRAIFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVL 303
Cdd:pfam00016  81 AKGHYLNITADDMEEMYRRAEFAKETGGVAVMVDGLVIGPTAITTLRRWFRDNGVILHYHRAGHGAVTRQSKHGISFRVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  304 AKALRLSGGDHVHAGTV-VGKLEGEREitlgfvDLLRDDFIEKDRSRGIYFTQDWVSLPGVIPVASGGIHVWHMPALTEI 382
Cdd:pfam00016 161 AKMARLAGADHLHTGTMgVGKLEGDPS------DTLRAYMLEEDRARGPFFDQDWGGMPAVMPVASGGIHAGQMPGLFDN 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  383 FGD-DSVLQFGGGTLGHPWGNAPGAVANRVSLEACVqarnEGRDLAREgneiireaSKWSPELAAACEVW 451
Cdd:pfam00016 235 LGDsDVILQFGGGTFGHPDGPAAGAKANRQALEAWV----EGRDLEEY--------AKEHPELARAFESW 292
RuBisCO_large_III cd08213
Ribulose bisphosphate carboxylase large chain, Form III; Ribulose bisphosphate carboxylase ...
23-451 5.69e-142

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: 412.94  E-value: 5.69e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  23 TDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTAVWTDGLTSLDRYKGRCYHIEPVAGeenQYIAYVAYPLDLFEEGSV 102
Cdd:cd08213    1 DDLIAVFRIEPAEGISIEEAAGRVASESSIGTWTTLATLYPERAEKLKAKAYYFDGLGG---SYIVKVAYPLELFEEGNM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 103 TNMFTSIVGNVFGFKALRALRLEDLRIPTSYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECL 182
Cdd:cd08213   78 PQLLSSIAGNIFGMKAVKNLRLEDIYFPESYLREFKGPQFGIEGVREILGIKDRPLLGTVPKPKVGLSPEEHAEVAYEAL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 183 RGGLDFTKDDENVNSQPFMRWRDRFCFCAEAIYKAQAETGEIKGHYLNATAgTCEEMMKRAIFARELGVPIVMHDYLTGG 262
Cdd:cd08213  158 VGGVDLVKDDENLTSQPFNRFEERAKESLKARDKAEAETGERKAYLANITA-PVREMERRAELVADLGGKYVMIDVVVAG 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 263 FTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHVHAGTVVGKLEGEREITLGFVDLLRDDF 342
Cdd:cd08213  237 WSALQYLRDLAEDYGLAIHAHRAMHAAFTRNPRHGISMLVLAKLYRLIGVDQLHIGTAVGKMEGDKEEVLRIADILREQK 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 343 IEKDrSRGIYFTQDWVSLPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVSLEACVqarnE 422
Cdd:cd08213  317 YKPD-EEDFHLAQDWGGIKPVFPVASGGLHPGLVPDVIDILGKDIVIQVGGGVHGHPDGTRAGAKAVRQAIEAAL----E 391
                        410       420
                 ....*....|....*....|....*....
gi 221078579 423 GRDLaregneiiREASKWSPELAAACEVW 451
Cdd:cd08213  392 GISL--------DEYAKDHKELARALEKW 412
rubisco_III TIGR03326
ribulose bisphosphate carboxylase, type III; Members of this protein family are the archaeal, ...
18-451 1.55e-117

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: 350.61  E-value: 1.55e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579   18 YETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTAVWTdgLTSLDRYKGRCYHIEPVAGEENQYIAYVAYPLDLF 97
Cdd:TIGR03326   7 YEPSDDDLVCTFRITPAEGVSIEDAAGRVASESSIGTWTTLQP--WKDPERYKDLSAKVYDIEEHGDGSIVRIAYPLGLF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579   98 EEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTSYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRA 177
Cdd:TIGR03326  85 EEGNLPQLLSCIAGNIFGMKAVKGLRLLDFEFPAEFLRAFKGPQFGIEGVREILGIKDRPITATVPKPKVGLSTEEHAKV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  178 VYECLRGGLDFTKDDENVNSQPFMRWRDRFCFCAEAIYKAQAETGEIKGHYLNATAGTcEEMMKRAIFARELGVPIVMHD 257
Cdd:TIGR03326 165 AYELWSGGVDLLKDDENLTSQAFNRFEERVEKSLKVRDKVEAETGEKKSYLINITADV-REMERRAELVADLGGEYVMVD 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  258 YLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHVHAGTV-VGKLEGEREITLGFVD 336
Cdd:TIGR03326 244 IVVAGWSALQYVRERTEDLGLAIHAHRAMHAAFTRNPKHGISMFVLAKLYRLIGVDQLHTGTAgVGKLEGGNEDTKGIND 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  337 LLRddfiekdrsrgiyftQDWVSLPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVSLEAC 416
Cdd:TIGR03326 324 FLR---------------QDWHHIKPVFPVASGGLHPGLVPPLIDALGTDLVIQAGGGVHGHPDGTRAGAKALRAAIDAI 388
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 221078579  417 VqarnEGRDLaregneiiREASKWSPELAAACEVW 451
Cdd:TIGR03326 389 I----EGISL--------EEKAKSVPELKKALEKW 411
RuBisCO_IV_RLP cd08205
Ribulose bisphosphate carboxylase like proteins, Rubisco-Form IV; Ribulose bisphosphate ...
51-410 4.25e-65

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: 213.93  E-value: 4.25e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  51 STGTWTAVWTDGLTSLDRYKGRCYHIEPV---AGEENQYIAYVAYPLDLFEeGSVTNMFTSIVGNVFGfkaLRALRLEDL 127
Cdd:cd08205   26 TVGTWTELPGETEEIRERHVGRVESIEELeesEGKYGRARVTISYPLDNFG-GDLPQLLNTLFGNLSL---LPGIKLVDL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 128 RIPTSYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRF 207
Cdd:cd08205  102 ELPDSLLAAFPGPRFGIEGLRRLLGVHDRPLLGTIIKPSIGLSPEELAELAYELALGGIDLIKDDELLADQPYAPFEERV 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 208 CFCAEAIYKAQAETGEIKGHYLNATAGTcEEMMKRAIFARELGVPIVMHDYLTGGFTANTSLAhycRDNGLLLHIHRAMH 287
Cdd:cd08205  182 RACMEAVRRANEETGRKTLYAPNITGDP-DELRRRADRAVEAGANALLINPNLVGLDALRALA---EDPDLPIMAHPAFA 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 288 AVIDRQKNHGMHFRVLAKALRLSGGDHVHAGTVVGKLEGEREITLGFVDLLRddfiekdrsrgiyftQDWVSLPGVIPVA 367
Cdd:cd08205  258 GALSRSPDYGSHFLLLGKLMRLAGADAVIFPGPGGRFPFSREECLAIARACR---------------RPLGGIKPALPVP 322
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 221078579 368 SGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANR 410
Cdd:cd08205  323 SGGMHPGRVPELYRDYGPDVILLAGGGILGHPDGAAAGVRAFR 365
PRK13475 PRK13475
ribulose-bisphosphate carboxylase;
25-435 1.90e-61

ribulose-bisphosphate carboxylase;


Pssm-ID: 184072  Cd Length: 443  Bit Score: 206.50  E-value: 1.90e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  25 ILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTAVWT-DGLTsldryKG---RCYHIEPVAGeenqyIAYVAYPLDLFE-- 98
Cdd:PRK13475  24 ILCAYKMKPKAGHGYLEAAAHFAAESSTGTNVEVSTtDDFT-----RGvdaLVYEIDEARE-----LMKIAYPVELFDrn 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  99 ----EGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTSYVKTFQGPPHGIqverDKLNKY-GRP------LLGCTIKPKL 167
Cdd:PRK13475  94 iidgRAMIVSFLTLTIGNNQGMGDVEYAKMHDFYVPPRYLELFDGPSTDI----SDLWRVlGRPvkdggyIAGTIIKPKL 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 168 GLSAKNYGRAVYECLRGGlDFTKDDENVNSQPFMRWRDRFCFCAEAIYKAQAETGEIKGHYLNATAGTCEEMMKRAIFAR 247
Cdd:PRK13475 170 GLRPEPFAEACYDFWLGG-DFIKNDEPQGNQVFAPLKKTVPLVADAMKRAQDETGEAKLFSANITADDHYEMIARGEYIL 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 248 ELGVPIVMH-DYLTGGFTANTSLAHYCRDN--GLLLHIHRAMHAVIDRQKN-HGMHFRVLAKALRLSGGDHVHAGTV-VG 322
Cdd:PRK13475 249 ETFGENADHvAFLVDGYVAGPGAVTTARRQypDQYLHYHRAGHGAVTSPSSkRGYTAFVLSKMARLQGASGIHTGTMgYG 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 323 KLEGEREitlgfvDLLRDDFIEKDRSRGIYFTQDWVSLPGVIPVASGGIHVWHMPALTEIFGDDSVLQ-FGGGTLGHPWG 401
Cdd:PRK13475 329 KMEGEAD------DRVIAYMIERDSAQGPFYHQEWYGMKPTTPIISGGMNALRLPGFFDNLGHGNVINtAGGGAFGHIDG 402
                        410       420       430
                 ....*....|....*....|....*....|....
gi 221078579 402 NAPGAVANRVSLEaCVQARNEGRDLAREGNEIIR 435
Cdd:PRK13475 403 PAAGAKSLRQAYD-CWKAGADPIEYAKEHKEFAR 435
RuBisCO_large_II cd08211
Ribulose bisphosphate carboxylase large chain, Form II; Ribulose bisphosphate carboxylase ...
25-435 8.14e-60

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: 202.35  E-value: 8.14e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  25 ILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTAV-WTDGLT-SLDrykGRCYHIEpvagEENQyIAYVAYPLDLFE---- 98
Cdd:cd08211   23 VLVAYIMKPKAGYGYLATAAHFAAESSTGTNVEVsTTDDFTrGVD---ALVYEID----EARE-LMKIAYPVELFDrnlt 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  99 --EGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTSYVKTFQGPPHGIQVERDKLNKY---GRPLLGCTIKPKLGLSAKN 173
Cdd:cd08211   95 dgRAMVASFLTLIIGNNQGMGDVEYLKMHDFYVPESMLELFDGPSVNISDMWKVLGRPevdGGYIAGTIIKPKLGLRPKP 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 174 YGRAVYECLRGGlDFTKDDENVNSQPFMRWRDRFCFCAEAIYKAQAETGEIKGHYLNATAGTCEEMMKRAIFARELGVPI 253
Cdd:cd08211  175 FAEACYAFWLGG-DFIKNDEPQANQPFCPLKKVIPLVADAMRRAQDETGEAKLFSANITADDPDEMIARGEYILEAFGPN 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 254 VMH-----DYLTGGFTANTSLAHYCRDNglLLHIHRAMHAVIDRQKNH-GMHFRVLAKALRLSGGDHVHAGTV-VGKLEG 326
Cdd:cd08211  254 AGHvaflvDGYVAGPAAVTTARRRFPDQ--FLHYHRAGHGAVTSPQSKrGYTAFVLSKMARLQGASGIHTGTMgFGKMEG 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 327 EREitlgfvDLLRDDFIEKDRSRGIYFTQDWVSLPGVIPVASGGIHVWHMPALTEIFGDDSVLQ-FGGGTLGHPWGNAPG 405
Cdd:cd08211  332 ESS------DKVIAYMIERDEAQGPLFNQKWYGMKPTTPIISGGMNALRLPGFFENLGNGNVILtAGGGSFGHIDGPAAG 405
                        410       420       430
                 ....*....|....*....|....*....|
gi 221078579 406 AVANRVSLEACVQARNEgRDLAREGNEIIR 435
Cdd:cd08211  406 AKSLRQAYDAWKQGVDV-IEYAKEHKELAR 434
RuBisCO_large_N pfam02788
Ribulose bisphosphate carboxylase large chain, N-terminal domain; The N-terminal domain of ...
12-133 5.34e-51

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: 168.55  E-value: 5.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579   12 NYYTPEYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTAVWTDGLTSLDRYKGRCYHIEPVAGEenQYIAYVA 91
Cdd:pfam02788   1 DYVDLDYEPKDTDLLCAFRIEPAAGVSPEEAAAHVAAESSTGTWTEVWTLDDTFTKKLKAKVYEIDEVPGG--SYIVKIA 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 221078579   92 YPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPTSY 133
Cdd:pfam02788  79 YPLDLFEEGSIPQLLSSIAGNIFGMKAVKALRLEDIRFPPAY 120
RLP_NonPhot cd08207
Ribulose bisphosphate carboxylase like proteins from nonphototrophic bacteria; Ribulose ...
51-447 4.02e-48

Ribulose bisphosphate carboxylase like proteins from nonphototrophic bacteria; Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV, which differ in their taxonomic distribution and subunit composition. Form I-III have Rubisco activity, while Form IV, also called Rubisco-like proteins (RLP), are missing critical active site residues and therefore do not catalyze CO2 fixation. They are believed to utilize a related enzymatic mechanism, but have divergent functions. The specific function of this subgroup is unknown.


Pssm-ID: 173972  Cd Length: 406  Bit Score: 170.18  E-value: 4.02e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  51 STGTWTAV--WTDGLTslDRYKGRCYHIEPVAGEENQYIAY-------------VAYPLDLFEEgSVTNMFTSIVGNVFG 115
Cdd:cd08207   26 SSGTFIALpgETDELK--ERSAARVESIEELETAAQPSLPRrasggpytrarvtISFPLDNIGT-SLPNLLATVAGNLFE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 116 FKALRALRLEDLRIPTSYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENV 195
Cdd:cd08207  103 LRELSGLRLVDLGLPDEFAAAFPGPAFGIAGTRRLTGVEDRPLIGTIIKPSVGLTPEETAALVRQLAAAGIDFIKDDELL 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 196 NSQPFMRWRDRFCFCAEAIYKAQAETGEIKGHYLNATaGTCEEMMKRAIFARELGVPIVMHDYLTGGFTAntsLAHYCRD 275
Cdd:cd08207  183 ANPPYSPLDERVRAVMRVINDHAQRTGRKVMYAFNIT-DDIDEMRRNHDLVVEAGGTCVMVSLNSVGLSG---LAALRRH 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 276 NGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHVHAGTVVGKL-EGEREITLGFVDLLRDDFIEKDRsrgiyft 354
Cdd:cd08207  259 SQLPIHGHRNGWGMLTRSPALGISFQAYQKLWRLAGVDHLHVNGLASKFwESDDSVIESARACLTPLGGPDDA------- 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 355 qdwvslpgVIPVASGGIHVWHMPALTEIFGDDSVLQF-GGGTLGHPWGNAPGAVANRVSLEACVQARNegrdlaregnei 433
Cdd:cd08207  332 --------AMPVFSSGQWGGQAPPTYRRLGSVDLLYLaGGGIMAHPDGPAAGVRSLRQAWEAAVAGVP------------ 391
                        410
                 ....*....|....
gi 221078579 434 IREASKWSPELAAA 447
Cdd:cd08207  392 LEEYAKTHPELARA 405
RLP_DK-MTP-1-P-enolase cd08209
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Ribulose bisphosphate carboxylase like ...
53-451 3.93e-42

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: 153.63  E-value: 3.93e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  53 GTWTAVWTDGLTSLDRYKGRCYHIEPvaGEENQYIAYVAYPLdlfeeGSVTNMFTSIVGNVFGFKALR-ALRLEDLRIPT 131
Cdd:cd08209   27 GSWTDLPALRQAQLQKHLGEVVSVEE--LEEGRGVITIAYPL-----INVSGDIPALLTTIFGKLSLDgKIKLVDLRLPE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 132 SYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFCFCA 211
Cdd:cd08209  100 EFGRAFPGPKFGIEGIRQRLGVHDRPLLMSIFKGVLGLDLDDLAEQLREQALGGVDLIKDDEILFDNPLAPALERIRACR 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 212 EAIYKAQAETGEIKGHYLNATaGTCEEMMKRAIFARELGVPIVMHDYLTGGFTANTSLAhycRDNGLLLHI--HRAMHAV 289
Cdd:cd08209  180 PVLQEVYEQTGRRTLYAVNLT-GPVFTLKEKARRLVEAGANALLFNVFAYGLDVLEALA---SDPEINVPIfaHPAFAGA 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 290 IDRQKNHGM-HFRVLAKALRLSGGDHVHAGTVVGKLEGEREITLGFVDLLRDDFIEKdrsrgiyftqdwvslpGVIPVAS 368
Cdd:cd08209  256 LYGSPDYGIaASVLLGTLMRLAGADAVLFPSPYGSVALSKEEALAIAEALRRGGAFK----------------GVFPVPS 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 369 GGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVSLEACvqarnegrdlarEGNEIIREASKWSPELAAAC 448
Cdd:cd08209  320 AGIHPGLVPQLLRDFGTDVILNAGGGIHGHPDGAAAGVRAFREAIDAV------------LAGESLEPAAIPDGPLKSAL 387

                 ...
gi 221078579 449 EVW 451
Cdd:cd08209  388 DKW 390
mtnW PRK09549
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Reviewed
59-451 1.01e-36

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


Pssm-ID: 236560  Cd Length: 407  Bit Score: 139.37  E-value: 1.01e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  59 WTDgLTSLDR-----YKGRCYHIEPVAGEEN----QYIAYVAYPldlfeEGSVTNMFTSIVGNVFGFKALRA-LRLEDLR 128
Cdd:PRK09549  33 WTD-LPHLEQeqlkkHKGNVVHVEELEEHERkgvkRGIIKIAYP-----LANFSPDLPAILTTTFGKLSLDGeVKLIDLT 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 129 IPTSYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFC 208
Cdd:PRK09549 107 FSDELKRHFPGPKFGIDGIRNLLGVHDRPLLMSIFKGVIGRDLDYLKEQLRDQALGGVDLVKDDEILFENALTPFEKRIV 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 209 FCAEAIYKAQAETGEIKGHYLNATAGTCE--EMMKRAIfarELGVPIVMHDYLTGGFTANTSLAhycRDNGLLLHI--HR 284
Cdd:PRK09549 187 AGKEVLQEVYETTGHKTLYAVNLTGRTFElkEKAKRAA---EAGADALLFNVFAYGLDVLQSLA---EDPEIPVPImaHP 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 285 AMHAVIDRQKNHGM-HFRVLAKALRLSGGDHVHAGTVVGKLEGEREITLGFVDLLRDDFIEKDRSrgiyftqdwvslpgv 363
Cdd:PRK09549 261 AVSGAYTPSPLYGIsSPLLLGKLLRYAGADFSLFPSPYGSVALEKEEALAIAKELTEDDDPFKRS--------------- 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 364 IPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVSLEACVQARNegrdlaregneiIREASKWSPE 443
Cdd:PRK09549 326 FPVPSAGIHPGLVPLLIRDFGKDVVINAGGGIHGHPNGAQGGGKAFRAAIDAVLQGKP------------LHEAAEDDEN 393

                 ....*...
gi 221078579 444 LAAACEVW 451
Cdd:PRK09549 394 LHSALDIW 401
RLP_RrRLP cd08210
Ribulose bisphosphate carboxylase like proteins (RLPs) similar to R.rubrum RLP; RLP from ...
66-399 3.00e-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: 120.42  E-value: 3.00e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  66 LDRYKGRCYHIEPVagEENQYIAYVAYPLDlfeegSVTNMFTSIVGNVFGFKAL-RALRLEDLRIPTSYVKTFQGPPHGI 144
Cdd:cd08210   42 RDNIVGRVESLEPA--GEGSYRARISYSVD-----TAGGELTQLLNVLFGNSSLqPGIRLVDFELPPSLLRRFPGPRFGI 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 145 QVERDKLNKYGRPLLGCTIKPkLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFCFCAEAIYKAQAETGei 224
Cdd:cd08210  115 AGLRALLGIPERPLLCSALKP-QGLSAAELAELAYAFALGGIDIIKDDHGLADQPFAPFEERVKACQEAVAEANAETG-- 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 225 kGH--YLNATAGTCEEMMKRAIFARELGVPIVMHDYLTGGFTANTSLAhycRDNGLLLHIHRAMHAVIDRQKNHGM-HFR 301
Cdd:cd08210  192 -GRtlYAPNVTGPPTQLLERARFAKEAGAGGVLIAPGLTGLDTFRELA---EDFDFLPILAHPAFAGAFVSSGDGIsHAL 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 302 VLAKALRLSGGDHV---HAGtvvGKLEGEREITLGFVDLLRddfiekdrsrgiyftQDWVSLPGVIPVASGGIHVWHMPA 378
Cdd:cd08210  268 LFGTLFRLAGADAVifpNYG---GRFGFSREECQAIADACR---------------RPMGGLKPILPAPGGGMSVERAPE 329
                        330       340
                 ....*....|....*....|.
gi 221078579 379 LTEIFGDDSVLQFGGGTLGHP 399
Cdd:cd08210  330 MVELYGPDVMLLIGGSLLRAG 350
salvage_mtnW TIGR03332
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Members of this family are the methionine ...
51-451 4.65e-25

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: 106.46  E-value: 4.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579   51 STGTWTAVWTDGLTSLDRYKGRCYHIEPVAGEE----------NQYIAYVAYPLDLFeegsvTNMFTSIVGNVFGFKALR 120
Cdd:TIGR03332  28 TIGSWTDLPLLKQEQLKKHKGRVVHVEELAESEhtnsylrkkvKRAIIKIAYPELNF-----SPDLPALLTTTFGKLSLD 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  121 A-LRLEDLRIPTSYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQP 199
Cdd:TIGR03332 103 GeVKLIDLEFSDEFKRHFPGPKFGIDGIRKLLGVHERPLLMSIFKGMIGRDLGYLKEQLRQQALGGVDLVKDDEILFETG 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  200 FMRWRDRFCFCAEAIYKAQAETGEIKGHYLNATAGTCEeMMKRAIFARELGVPIVMHDYLTGGFTANTSLAHycrDNGLL 279
Cdd:TIGR03332 183 LAPFEKRITEGKEVLQEVYEQTGHKTLYAVNLTGRTFD-LKDKAKRAAELGADVLLFNVFAYGLDVLQSLAE---DDEIP 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  280 LHI--HRAMHAVIDRQKNHGM-HFRVLAKALRLSGGDHVHAGTVVGKLEGEREITLGFVDllrddfiekdrsrgiYFTQD 356
Cdd:TIGR03332 259 VPImaHPAVSGAYTSSPFYGFsHSLLLGKLLRYAGADFSLFPSPYGSVALEREDALAISK---------------ELTED 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579  357 WVSLPGVIPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVSLEACVQARNegrdlaregneiIRE 436
Cdd:TIGR03332 324 DAPFKKTFAVPSAGIHPGMVPLIMRDFGIDHIINAGGGIHGHPNGAQGGGRAFRAAIDAVLEAKP------------LHE 391
                         410
                  ....*....|....*
gi 221078579  437 ASKWSPELAAACEVW 451
Cdd:TIGR03332 392 KAADDIDLKLALDKW 406
RLP_Photo cd08208
Ribulose bisphosphate carboxylase like proteins from phototrophic bacteria; Ribulose ...
102-447 7.20e-25

Ribulose bisphosphate carboxylase like proteins from phototrophic bacteria; Ribulose bisphosphate carboxylase (Rubisco) plays an important role in the Calvin reductive pentose phosphate pathway. It catalyzes the primary CO2 fixation step. Rubisco is activated by carbamylation of an active site lysine, stabilized by a divalent cation, which then catalyzes the proton abstraction from the substrate ribulose 1,5 bisphosphate (RuBP) and leads to the formation of two molecules of 3-phosphoglycerate. Members of the Rubisco family can be divided into 4 subgroups, Form I-IV, which differ in their taxonomic distribution and subunit composition. Form I-III have Rubisco activity, while Form IV, also called Rubisco-like proteins (RLP), are missing critical active site residues and therefore do not catalyze CO2 fixation. They are believed to utilize a related enzymatic mechanism, but have divergent functions. The specific function of this subgroup is unknown.


Pssm-ID: 173973  Cd Length: 424  Bit Score: 106.13  E-value: 7.20e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 102 VTNMFTSIVGN-VFGFKALRALRLEDLRIPTSYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYE 180
Cdd:cd08208  105 IPNLLSAVCGEgTFFSPGVPVVKLMDIHFPETYLADFEGPKFGIAGLRERLQAHDRPIFFGVIKPNIGLPPGEFAELGYQ 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 181 CLRGGLDFTKDDENVNSQPFMRWRDRFCFCAEAIYKAQAETGEIKGHYLNATaGTCEEMMKRAIFARELGVPIVMHDYLT 260
Cdd:cd08208  185 SWLGGLDIAKDDEMLADVDWCPLEERAALLGKARRRAEAETGVPKIYLANIT-DEVDRLMELHDVAVRNGANALLINAMP 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 261 GGFTANTSLAHYCRdngLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDhvhagTVVGKLEGEREITLGfvDLLRD 340
Cdd:cd08208  264 VGLSAVRMLRKHAQ---VPLIAHFPFIASFSRLEKYGIHSRVMTKLQRLAGLD-----VVIMPGFGPRMMTPE--EEVLE 333
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221078579 341 DFIEKDRSRGiyftqdwvSLPGVIPVASGGIHVWHMPALTEIFGD-DSVLQFGGGTLGHPWGNAPGAVANRVSLEACVQA 419
Cdd:cd08208  334 CVIACLEPMG--------PIKPCLPVPGGSDSALTLQTVYEKVGNvDFGFVPGRGVFGHPMGPKAGAKSIRQAWEAIEAG 405
                        330       340
                 ....*....|....*....|....*...
gi 221078579 420 rnegrdlaregnEIIREASKWSPELAAA 447
Cdd:cd08208  406 ------------ISIETWAETHPELQAA 421
 
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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