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Conserved domains on  [gi|84621500|gb|ABC59583|]
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ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit, partial (chloroplast) [Pilgerina madagascariensis]

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
1-467 0e+00

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


:

Pssm-ID: 176981  Cd Length: 475  Bit Score: 1095.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500    1 ASVGFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTSVWTDGLTSLDRYKGRCYHIE 80
Cdd:CHL00040   9 ASVGFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYRIE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500   81 PVAGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRVPPAYSKTFQGPPHGIQVERDKLNKYGRP 160
Cdd:CHL00040  89 PVPGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYLKTFQGPPHGIQVERDKLNKYGRP 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  161 LLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCE 240
Cdd:CHL00040 169 LLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCE 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  241 EMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHA 320
Cdd:CHL00040 249 EMYKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHA 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  321 GTVVGKLEGERDITLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLG 400
Cdd:CHL00040 329 GTVVGKLEGEREMTLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLG 408
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84621500  401 HPWGNAPGAVANRVALEACVQARNEGRDLARQGNEIIREASKWSPELAAACEVWKEIKFEFQAMDTL 467
Cdd:CHL00040 409 HPWGNAPGAVANRVALEACVQARNEGRDLAREGNEIIREAAKWSPELAAACEVWKEIKFEFETTDTL 475
 
Name Accession Description Interval E-value
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
1-467 0e+00

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


Pssm-ID: 176981  Cd Length: 475  Bit Score: 1095.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500    1 ASVGFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTSVWTDGLTSLDRYKGRCYHIE 80
Cdd:CHL00040   9 ASVGFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYRIE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500   81 PVAGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRVPPAYSKTFQGPPHGIQVERDKLNKYGRP 160
Cdd:CHL00040  89 PVPGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYLKTFQGPPHGIQVERDKLNKYGRP 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  161 LLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCE 240
Cdd:CHL00040 169 LLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCE 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  241 EMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHA 320
Cdd:CHL00040 249 EMYKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHA 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  321 GTVVGKLEGERDITLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLG 400
Cdd:CHL00040 329 GTVVGKLEGEREMTLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLG 408
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84621500  401 HPWGNAPGAVANRVALEACVQARNEGRDLARQGNEIIREASKWSPELAAACEVWKEIKFEFQAMDTL 467
Cdd:CHL00040 409 HPWGNAPGAVANRVALEACVQARNEGRDLAREGNEIIREAAKWSPELAAACEVWKEIKFEFETTDTL 475
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
15-465 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: 951.10  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  15 TYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTSVWTDGLTSLDRYKGRCYHIEPVAGEENQYIAYVA 94
Cdd:cd08212   1 GYWTPDYQPKDTDILAAFRITPQPGVDPEEAAAAVAGESSTATWTVVWTDRLTALDRYKGKAYRVEPVPGEENQYFAYIA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  95 YPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRVPPAYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSA 174
Cdd:cd08212  81 YPLDLFEEGSVANLTTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDRLNKYGRPLLGCTIKPKLGLSA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 175 KNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMIKRAVFARELGV 254
Cdd:cd08212 161 KNYGRVVYECLRGGLDFTKDDENINSQPFMRWRDRFLFVAEAVNKAQAETGEVKGHYLNVTAGTMEEMYKRAEFAKELGS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 255 PIVMHDYLTgGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGERDIT 334
Cdd:cd08212 241 PIIMHDLLT-GFTAIQSLAKWCRDNGMLLHLHRAGHATYDRQKNHGIHFRVLAKWLRLSGVDHIHAGTVVGKLEGDPLVT 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 335 LGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRV 414
Cdd:cd08212 320 LGFYDLLRDDYIEKDRSRGIFFTQDWASLPGVMPVASGGIHVGQMHQLIEIFGDDVVLQFGGGTIGHPWGIAAGATANRV 399
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
gi 84621500 415 ALEACVQARNEGRDLARQGNEIIREASKWSPELAAACEVWKEIKFEFQAMD 465
Cdd:cd08212 400 ALEAMVQARNEGRDLAREGPEILREAAKWSPELAAALETWKDIKFEFESTD 450
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
16-459 3.62e-180

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


Pssm-ID: 441455  Cd Length: 417  Bit Score: 510.10  E-value: 3.62e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  16 YYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTSVWTDGLTSLDRYKGRCYHIEPV---AGEENQYIAY 92
Cdd:COG1850   2 YVDPDYIPDDDDILATYRITPETGVDPEEAAAAIAGEQSTGTWTEVPTETDELRERLAARVYSIEELpevGGGYRRALVT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  93 VAYPLDLFEeGSVTNMFTSIVGNVFGFKALRALRLEDLRVPPAYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGL 172
Cdd:COG1850  82 IAYPLENFG-GNLPNLLSTVAGNLFGLKAVSGLRLLDLEFPESFLAAFPGPKFGIEGTRELLGVYDRPLLGTIIKPKVGL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 173 SAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTcEEMIKRAVFAREL 252
Cdd:COG1850 161 SPEETAELVYELALGGVDFIKDDENLADQPFCPFEDRVRAVMEAIDRAEEETGEKKMYAFNITADT-DEMLRRADLAVEL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 253 GVPIVMHDYLTGGFTANTSLAHycRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGERD 332
Cdd:COG1850 240 GANAVMVDVNTVGLSAVQTLRE--EHIGLPIHAHRAGHGAFTRSPLHGISMRVLAKLWRLAGADHLHVGTPVGKMEGDDE 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 333 ITLGFVDLLRddfiekdrsrgiyftQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVAN 412
Cdd:COG1850 318 EVLAIADALL---------------QPWGGLKPVFPVPSGGQHPGQVPELYDALGTDLILQAGGGIHGHPDGPAAGARAL 382
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 84621500 413 RVALEACVQarneGRDLArqgneiirEASKWSPELAAACEVWKEIKF 459
Cdd:COG1850 383 RQAWEAAVA----GIPLE--------EYAKTHPELAAALEKWGKKAP 417
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
147-454 8.80e-170

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: 478.78  E-value: 8.80e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500   147 IQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGE 226
Cdd:pfam00016   1 IAVERRVLNKYGRPILGTIIKPKLGLSPKNYARAVYEFLLGGLDFIKDDENINSQPFMPWRDRFLFVAEAIDRAQDETGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500   227 IKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVL 306
Cdd:pfam00016  81 AKGHYLNITADDMEEMYRRAEFAKETGGVAVMVDGLVIGPTAITTLRRWFRDNGVILHYHRAGHGAVTRQSKHGISFRVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500   307 AKALRMSGGDHIHAGTV-VGKLEGERDitlgfvDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEI 385
Cdd:pfam00016 161 AKMARLAGADHLHTGTMgVGKLEGDPS------DTLRAYMLEEDRARGPFFDQDWGGMPAVMPVASGGIHAGQMPGLFDN 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500   386 FGD-DSVLQFGGGTLGHPWGNAPGAVANRVALEACVqarnEGRDLarqgneiIREAsKWSPELAAACEVW 454
Cdd:pfam00016 235 LGDsDVILQFGGGTFGHPDGPAAGAKANRQALEAWV----EGRDL-------EEYA-KEHPELARAFESW 292
rubisco_III TIGR03326
ribulose bisphosphate carboxylase, type III; Members of this protein family are the archaeal, ...
16-454 1.35e-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: 1.35e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500    16 YYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTSVWTdgLTSLDRYKGRCYHIEPVAGEENQYIAYVAY 95
Cdd:TIGR03326   2 FVDLNYEPSDDDLVCTFRITPAEGVSIEDAAGRVASESSIGTWTTLQP--WKDPERYKDLSAKVYDIEEHGDGSIVRIAY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500    96 PLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRVPPAYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAK 175
Cdd:TIGR03326  80 PLGLFEEGNLPQLLSCIAGNIFGMKAVKGLRLLDFEFPAEFLRAFKGPQFGIEGVREILGIKDRPITATVPKPKVGLSTE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500   176 NYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTcEEMIKRAVFARELGVP 255
Cdd:TIGR03326 160 EHAKVAYELWSGGVDLLKDDENLTSQAFNRFEERVEKSLKVRDKVEAETGEKKSYLINITADV-REMERRAELVADLGGE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500   256 IVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTV-VGKLEGERDIT 334
Cdd:TIGR03326 239 YVMVDIVVAGWSALQYVRERTEDLGLAIHAHRAMHAAFTRNPKHGISMFVLAKLYRLIGVDQLHTGTAgVGKLEGGNEDT 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500   335 LGFVDLLRddfiekdrsrgiyftQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRV 414
Cdd:TIGR03326 319 KGINDFLR---------------QDWHHIKPVFPVASGGLHPGLVPPLIDALGTDLVIQAGGGVHGHPDGTRAGAKALRA 383
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 84621500   415 ALEACVqarnEGRDLarqgneiiREASKWSPELAAACEVW 454
Cdd:TIGR03326 384 AIDAII----EGISL--------EEKAKSVPELKKALEKW 411
 
Name Accession Description Interval E-value
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
1-467 0e+00

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


Pssm-ID: 176981  Cd Length: 475  Bit Score: 1095.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500    1 ASVGFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTSVWTDGLTSLDRYKGRCYHIE 80
Cdd:CHL00040   9 ASVGFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYRIE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500   81 PVAGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRVPPAYSKTFQGPPHGIQVERDKLNKYGRP 160
Cdd:CHL00040  89 PVPGEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPPAYLKTFQGPPHGIQVERDKLNKYGRP 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  161 LLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCE 240
Cdd:CHL00040 169 LLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCE 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  241 EMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHA 320
Cdd:CHL00040 249 EMYKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGIHFRVLAKALRMSGGDHIHA 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  321 GTVVGKLEGERDITLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLG 400
Cdd:CHL00040 329 GTVVGKLEGEREMTLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLG 408
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 84621500  401 HPWGNAPGAVANRVALEACVQARNEGRDLARQGNEIIREASKWSPELAAACEVWKEIKFEFQAMDTL 467
Cdd:CHL00040 409 HPWGNAPGAVANRVALEACVQARNEGRDLAREGNEIIREAAKWSPELAAACEVWKEIKFEFETTDTL 475
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
15-465 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: 951.10  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  15 TYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTSVWTDGLTSLDRYKGRCYHIEPVAGEENQYIAYVA 94
Cdd:cd08212   1 GYWTPDYQPKDTDILAAFRITPQPGVDPEEAAAAVAGESSTATWTVVWTDRLTALDRYKGKAYRVEPVPGEENQYFAYIA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  95 YPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRVPPAYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSA 174
Cdd:cd08212  81 YPLDLFEEGSVANLTTSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDRLNKYGRPLLGCTIKPKLGLSA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 175 KNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMIKRAVFARELGV 254
Cdd:cd08212 161 KNYGRVVYECLRGGLDFTKDDENINSQPFMRWRDRFLFVAEAVNKAQAETGEVKGHYLNVTAGTMEEMYKRAEFAKELGS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 255 PIVMHDYLTgGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGERDIT 334
Cdd:cd08212 241 PIIMHDLLT-GFTAIQSLAKWCRDNGMLLHLHRAGHATYDRQKNHGIHFRVLAKWLRLSGVDHIHAGTVVGKLEGDPLVT 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 335 LGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRV 414
Cdd:cd08212 320 LGFYDLLRDDYIEKDRSRGIFFTQDWASLPGVMPVASGGIHVGQMHQLIEIFGDDVVLQFGGGTIGHPWGIAAGATANRV 399
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
gi 84621500 415 ALEACVQARNEGRDLARQGNEIIREASKWSPELAAACEVWKEIKFEFQAMD 465
Cdd:cd08212 400 ALEAMVQARNEGRDLAREGPEILREAAKWSPELAAALETWKDIKFEFESTD 450
rbcL PRK04208
ribulose bisophosphate carboxylase; Reviewed
4-467 0e+00

ribulose bisophosphate carboxylase; Reviewed


Pssm-ID: 179787  Cd Length: 468  Bit Score: 891.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500    4 GFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTSVWTDGLTSLDRYKGRCYHIEPVA 83
Cdd:PRK04208   5 RYDAGVKEYRQMYWDPDYTPKDTDLLACFRITPQEGVDPEEAAAAVAAESSTGTWTTVWTDLLTDLDKYKAKAYRIEDVP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500   84 GEENQYIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRVPPAYSKTFQGPPHGIQVERDKLNKYGRPLLG 163
Cdd:PRK04208  85 GDDGSYYAFIAYPLDLFEEGSIPNLLASIAGNVFGFKAVKALRLEDIRFPVAYVKTFKGPPFGIQVERERLDKYGRPLLG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  164 CTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMI 243
Cdd:PRK04208 165 TTPKPKLGLSAKNYGRVVYEALRGGLDFTKDDENLNSQPFNRWRDRFLFVMEAIDKAEAETGERKGHYLNVTAPTMEEMY 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  244 KRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTV 323
Cdd:PRK04208 245 KRAEFAKELGSPIVMIDVVTAGWTALQSLREWCRDNGLALHAHRAMHAAFTRNPNHGISFRVLAKLLRLIGVDHLHTGTV 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  324 VGKLEGERDITLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPW 403
Cdd:PRK04208 325 VGKLEGDRAEVLGYYDILREDFVPEDRSRGIFFDQDWGSIKPVFPVASGGIHPGHMPALLDIFGDDVVLQFGGGTHGHPD 404
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 84621500  404 GNAPGAVANRVALEACVQARNEGRDLARQGNEIIREASKWSPELAAACEVWKEIKFEFQAMDTL 467
Cdd:PRK04208 405 GTAAGATANRVALEACVEARNEGRDIEKEGPDILEEAAKWSPELAAALEKWGEIKFEFDTVDTL 468
RuBisCO_large_I_II_III cd08206
Ribulose bisphosphate carboxylase large chain, Form I,II,III; Ribulose bisphosphate ...
26-454 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: 740.20  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  26 TDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTSVWTDGLTSLDRYKGRCYHIEPVAgeENQYIAYVAYPLDLFEEGSV 105
Cdd:cd08206   1 TDLLAAFRMTPAEGVDPEEAAAAVAAESSTGTWTTVWTDRLTATERLKAKVYRIDPVP--DGQYIAKIAYPLDLFEEGSV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 106 TNMFTSIVGNVFGFKALRALRLEDLRVPPAYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECL 185
Cdd:cd08206  79 PNLLTSIIGNVFGMKAVKALRLEDFRFPPAYLKTFDGPSFGIQGEREILGKYGRPLLGTIVKPKLGLSPKEYARVVYEAL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 186 RGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGG 265
Cdd:cd08206 159 RGGLDFVKDDENQNSQPFMRFEDRILFVAEAMDKAEAETGEAKGHYLNITADTPEEMIKRAEFAKELGSVIVMVDGVTAG 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 266 FTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGERDITLGFVDLLRDDF 345
Cdd:cd08206 239 WTAIQSARRWCPDNGLALHAHRAGHAAFTRQKNHGISMRVLAKLARLIGVDHIHTGTVVGKLEGDPSEVKGIADMLREDE 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 346 IEKDRSRgIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARne 425
Cdd:cd08206 319 VEGDLSR-IFFNQDWGGMKPVFPVASGGLHPGRMPALIEILGDDVILQFGGGTHGHPDGPAAGAKANRQALEAWVQGR-- 395
                       410       420
                ....*....|....*....|....*....
gi 84621500 426 grdlarqgneIIREASKWSPELAAACEVW 454
Cdd:cd08206 396 ----------ILREYAKTHKELAAALEKW 414
RuBisCO_large cd08148
Ribulose bisphosphate carboxylase large chain; Ribulose bisphosphate carboxylase (Rubisco) ...
28-415 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: 538.94  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  28 ILAAFRVTPQPgVPPEEAGAAVAAESSTGTWTSVWTdGLTSLDRYKGRCYHIEPVAgeeNQYIAYVAYPLDLFEEGSVTN 107
Cdd:cd08148   1 VLATYRVHPEA-TPPEKAAEAIAAESSTGTWTEVPT-TQEQLRRVKGRVYSVEELG---KRYIVKIAYPVELFEPGNIPQ 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 108 MFTSIVGNVFGFKALRALRLEDLRVPPAYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRG 187
Cdd:cd08148  76 ILTVTAGNLFGLGALEAVRLEDLEFPEEYKKLFPGPKFGIDGIRKLLGVYGRPLVGTIIKPKLGLNPKYTAEAAYAAALG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 188 GLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTcEEMIKRAVFARELGVPIVMHDYLTGGFT 267
Cdd:cd08148 156 GLDLIKDDETLTDQPFCPLRDRITEVAAALDRVQEETGEKKLYAVNVTAGT-FEIIERAERALELGANMLMVDVLTAGFS 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 268 ANTSLAHYCRdNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGERDITLGFVDLLRDdfie 347
Cdd:cd08148 235 ALQALAEDFE-IDLPIHVHRAMHGAVTRSKFHGISMLVLAKLLRMAGGDFIHTGTVVGKMALEREEALGIADALTD---- 309
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 84621500 348 kdrsrgiyftqDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVA 415
Cdd:cd08148 310 -----------DWAGFKRVFPVASGGIHPGLVPGILRDFGIDVILQAGGGIHGHPDGTVAGARAMRQA 366
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
16-459 3.62e-180

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


Pssm-ID: 441455  Cd Length: 417  Bit Score: 510.10  E-value: 3.62e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  16 YYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTSVWTDGLTSLDRYKGRCYHIEPV---AGEENQYIAY 92
Cdd:COG1850   2 YVDPDYIPDDDDILATYRITPETGVDPEEAAAAIAGEQSTGTWTEVPTETDELRERLAARVYSIEELpevGGGYRRALVT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  93 VAYPLDLFEeGSVTNMFTSIVGNVFGFKALRALRLEDLRVPPAYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGL 172
Cdd:COG1850  82 IAYPLENFG-GNLPNLLSTVAGNLFGLKAVSGLRLLDLEFPESFLAAFPGPKFGIEGTRELLGVYDRPLLGTIIKPKVGL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 173 SAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTcEEMIKRAVFAREL 252
Cdd:COG1850 161 SPEETAELVYELALGGVDFIKDDENLADQPFCPFEDRVRAVMEAIDRAEEETGEKKMYAFNITADT-DEMLRRADLAVEL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 253 GVPIVMHDYLTGGFTANTSLAHycRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGERD 332
Cdd:COG1850 240 GANAVMVDVNTVGLSAVQTLRE--EHIGLPIHAHRAGHGAFTRSPLHGISMRVLAKLWRLAGADHLHVGTPVGKMEGDDE 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 333 ITLGFVDLLRddfiekdrsrgiyftQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVAN 412
Cdd:COG1850 318 EVLAIADALL---------------QPWGGLKPVFPVPSGGQHPGQVPELYDALGTDLILQAGGGIHGHPDGPAAGARAL 382
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 84621500 413 RVALEACVQarneGRDLArqgneiirEASKWSPELAAACEVWKEIKF 459
Cdd:COG1850 383 RQAWEAAVA----GIPLE--------EYAKTHPELAAALEKWGKKAP 417
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
147-454 8.80e-170

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: 478.78  E-value: 8.80e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500   147 IQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGE 226
Cdd:pfam00016   1 IAVERRVLNKYGRPILGTIIKPKLGLSPKNYARAVYEFLLGGLDFIKDDENINSQPFMPWRDRFLFVAEAIDRAQDETGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500   227 IKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVL 306
Cdd:pfam00016  81 AKGHYLNITADDMEEMYRRAEFAKETGGVAVMVDGLVIGPTAITTLRRWFRDNGVILHYHRAGHGAVTRQSKHGISFRVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500   307 AKALRMSGGDHIHAGTV-VGKLEGERDitlgfvDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEI 385
Cdd:pfam00016 161 AKMARLAGADHLHTGTMgVGKLEGDPS------DTLRAYMLEEDRARGPFFDQDWGGMPAVMPVASGGIHAGQMPGLFDN 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500   386 FGD-DSVLQFGGGTLGHPWGNAPGAVANRVALEACVqarnEGRDLarqgneiIREAsKWSPELAAACEVW 454
Cdd:pfam00016 235 LGDsDVILQFGGGTFGHPDGPAAGAKANRQALEAWV----EGRDL-------EEYA-KEHPELARAFESW 292
RuBisCO_large_III cd08213
Ribulose bisphosphate carboxylase large chain, Form III; Ribulose bisphosphate carboxylase ...
26-454 4.93e-144

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: 418.33  E-value: 4.93e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  26 TDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTSVWTDGLTSLDRYKGRCYHIEPVAGeenQYIAYVAYPLDLFEEGSV 105
Cdd:cd08213   1 DDLIAVFRIEPAEGISIEEAAGRVASESSIGTWTTLATLYPERAEKLKAKAYYFDGLGG---SYIVKVAYPLELFEEGNM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 106 TNMFTSIVGNVFGFKALRALRLEDLRVPPAYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECL 185
Cdd:cd08213  78 PQLLSSIAGNIFGMKAVKNLRLEDIYFPESYLREFKGPQFGIEGVREILGIKDRPLLGTVPKPKVGLSPEEHAEVAYEAL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 186 RGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAgTCEEMIKRAVFARELGVPIVMHDYLTGG 265
Cdd:cd08213 158 VGGVDLVKDDENLTSQPFNRFEERAKESLKARDKAEAETGERKAYLANITA-PVREMERRAELVADLGGKYVMIDVVVAG 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 266 FTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGERDITLGFVDLLRDDF 345
Cdd:cd08213 237 WSALQYLRDLAEDYGLAIHAHRAMHAAFTRNPRHGISMLVLAKLYRLIGVDQLHIGTAVGKMEGDKEEVLRIADILREQK 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 346 IEKDrSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVqarnE 425
Cdd:cd08213 317 YKPD-EEDFHLAQDWGGIKPVFPVASGGLHPGLVPDVIDILGKDIVIQVGGGVHGHPDGTRAGAKAVRQAIEAAL----E 391
                       410       420
                ....*....|....*....|....*....
gi 84621500 426 GRDLarqgneiiREASKWSPELAAACEVW 454
Cdd:cd08213 392 GISL--------DEYAKDHKELARALEKW 412
rubisco_III TIGR03326
ribulose bisphosphate carboxylase, type III; Members of this protein family are the archaeal, ...
16-454 1.35e-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: 1.35e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500    16 YYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTSVWTdgLTSLDRYKGRCYHIEPVAGEENQYIAYVAY 95
Cdd:TIGR03326   2 FVDLNYEPSDDDLVCTFRITPAEGVSIEDAAGRVASESSIGTWTTLQP--WKDPERYKDLSAKVYDIEEHGDGSIVRIAY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500    96 PLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRVPPAYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAK 175
Cdd:TIGR03326  80 PLGLFEEGNLPQLLSCIAGNIFGMKAVKGLRLLDFEFPAEFLRAFKGPQFGIEGVREILGIKDRPITATVPKPKVGLSTE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500   176 NYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTcEEMIKRAVFARELGVP 255
Cdd:TIGR03326 160 EHAKVAYELWSGGVDLLKDDENLTSQAFNRFEERVEKSLKVRDKVEAETGEKKSYLINITADV-REMERRAELVADLGGE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500   256 IVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTV-VGKLEGERDIT 334
Cdd:TIGR03326 239 YVMVDIVVAGWSALQYVRERTEDLGLAIHAHRAMHAAFTRNPKHGISMFVLAKLYRLIGVDQLHTGTAgVGKLEGGNEDT 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500   335 LGFVDLLRddfiekdrsrgiyftQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRV 414
Cdd:TIGR03326 319 KGINDFLR---------------QDWHHIKPVFPVASGGLHPGLVPPLIDALGTDLVIQAGGGVHGHPDGTRAGAKALRA 383
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 84621500   415 ALEACVqarnEGRDLarqgneiiREASKWSPELAAACEVW 454
Cdd:TIGR03326 384 AIDAII----EGISL--------EEKAKSVPELKKALEKW 411
RuBisCO_IV_RLP cd08205
Ribulose bisphosphate carboxylase like proteins, Rubisco-Form IV; Ribulose bisphosphate ...
54-415 2.36e-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: 212.01  E-value: 2.36e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  54 STGTWTSVWTDGLTSLDRYKGRCYHIEPV---AGEENQYIAYVAYPLDLFEeGSVTNMFTSIVGNVFGfkaLRALRLEDL 130
Cdd:cd08205  26 TVGTWTELPGETEEIRERHVGRVESIEELeesEGKYGRARVTISYPLDNFG-GDLPQLLNTLFGNLSL---LPGIKLVDL 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 131 RVPPAYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRF 210
Cdd:cd08205 102 ELPDSLLAAFPGPRFGIEGLRRLLGVHDRPLLGTIIKPSIGLSPEELAELAYELALGGIDLIKDDELLADQPYAPFEERV 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 211 LFCAEAIYKAQAETGEIKGHYLNATAGTcEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAhycRDNGLLLHIHRAMH 290
Cdd:cd08205 182 RACMEAVRRANEETGRKTLYAPNITGDP-DELRRRADRAVEAGANALLINPNLVGLDALRALA---EDPDLPIMAHPAFA 257
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 291 AVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLEGERDITLGFVDLLRddfiekdrsrgiyftQDWVSLPGVLPVA 370
Cdd:cd08205 258 GALSRSPDYGSHFLLLGKLMRLAGADAVIFPGPGGRFPFSREECLAIARACR---------------RPLGGIKPALPVP 322
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 84621500 371 SGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVA 415
Cdd:cd08205 323 SGGMHPGRVPELYRDYGPDVILLAGGGILGHPDGAAAGVRAFRQA 367
PRK13475 PRK13475
ribulose-bisphosphate carboxylase;
28-452 1.26e-63

ribulose-bisphosphate carboxylase;


Pssm-ID: 184072  Cd Length: 443  Bit Score: 212.27  E-value: 1.26e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500   28 ILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTSVWT-DGLTsldryKG---RCYHIEPVAGeenqyIAYVAYPLDLFE-- 101
Cdd:PRK13475  24 ILCAYKMKPKAGHGYLEAAAHFAAESSTGTNVEVSTtDDFT-----RGvdaLVYEIDEARE-----LMKIAYPVELFDrn 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  102 ----EGSVTNMFTSIVGNVFGFKALRALRLEDLRVPPAYSKTFQGPPHGIqverDKLNKY-GRP------LLGCTIKPKL 170
Cdd:PRK13475  94 iidgRAMIVSFLTLTIGNNQGMGDVEYAKMHDFYVPPRYLELFDGPSTDI----SDLWRVlGRPvkdggyIAGTIIKPKL 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  171 GLSAKNYGRAVYECLRGGlDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMIKRAVFAR 250
Cdd:PRK13475 170 GLRPEPFAEACYDFWLGG-DFIKNDEPQGNQVFAPLKKTVPLVADAMKRAQDETGEAKLFSANITADDHYEMIARGEYIL 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  251 ELGVPIVMH-DYLTGGFTANTSLAHYCRDN--GLLLHIHRAMHAVIDRQKN-HGMHFRVLAKALRMSGGDHIHAGTV-VG 325
Cdd:PRK13475 249 ETFGENADHvAFLVDGYVAGPGAVTTARRQypDQYLHYHRAGHGAVTSPSSkRGYTAFVLSKMARLQGASGIHTGTMgYG 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  326 KLEGERDitlgfvDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQ-FGGGTLGHPWG 404
Cdd:PRK13475 329 KMEGEAD------DRVIAYMIERDSAQGPFYHQEWYGMKPTTPIISGGMNALRLPGFFDNLGHGNVINtAGGGAFGHIDG 402
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 84621500  405 NAPGAVANRVALEACvqarnegrdlaRQGNEIIrEASKWSPELAAACE 452
Cdd:PRK13475 403 PAAGAKSLRQAYDCW-----------KAGADPI-EYAKEHKEFARAFE 438
RuBisCO_large_II cd08211
Ribulose bisphosphate carboxylase large chain, Form II; Ribulose bisphosphate carboxylase ...
28-438 6.33e-61

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: 205.04  E-value: 6.33e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  28 ILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTSV-WTDGLT-SLDrykGRCYHIEpvagEENQyIAYVAYPLDLFE---- 101
Cdd:cd08211  23 VLVAYIMKPKAGYGYLATAAHFAAESSTGTNVEVsTTDDFTrGVD---ALVYEID----EARE-LMKIAYPVELFDrnlt 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 102 --EGSVTNMFTSIVGNVFGFKALRALRLEDLRVPPAYSKTFQGPPHGIQVERDKLNKY---GRPLLGCTIKPKLGLSAKN 176
Cdd:cd08211  95 dgRAMVASFLTLIIGNNQGMGDVEYLKMHDFYVPESMLELFDGPSVNISDMWKVLGRPevdGGYIAGTIIKPKLGLRPKP 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 177 YGRAVYECLRGGlDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPI 256
Cdd:cd08211 175 FAEACYAFWLGG-DFIKNDEPQANQPFCPLKKVIPLVADAMRRAQDETGEAKLFSANITADDPDEMIARGEYILEAFGPN 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 257 VMH-----DYLTGGFTANTSLAHYCRDNglLLHIHRAMHAVIDRQKNH-GMHFRVLAKALRMSGGDHIHAGTV-VGKLEG 329
Cdd:cd08211 254 AGHvaflvDGYVAGPAAVTTARRRFPDQ--FLHYHRAGHGAVTSPQSKrGYTAFVLSKMARLQGASGIHTGTMgFGKMEG 331
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 330 E-RDITLGFVdllrddfIEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQ-FGGGTLGHPWGNAP 407
Cdd:cd08211 332 EsSDKVIAYM-------IERDEAQGPLFNQKWYGMKPTTPIISGGMNALRLPGFFENLGNGNVILtAGGGSFGHIDGPAA 404
                       410       420       430
                ....*....|....*....|....*....|.
gi 84621500 408 GAVANRVALEACVQARNEgRDLARQGNEIIR 438
Cdd:cd08211 405 GAKSLRQAYDAWKQGVDV-IEYAKEHKELAR 434
RuBisCO_large_N pfam02788
Ribulose bisphosphate carboxylase large chain, N-terminal domain; The N-terminal domain of ...
15-136 3.63e-53

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: 174.32  E-value: 3.63e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500    15 TYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTSVWTDGLTSLDRYKGRCYHIEPVAGEenQYIAYVA 94
Cdd:pfam02788   1 DYVDLDYEPKDTDLLCAFRIEPAAGVSPEEAAAHVAAESSTGTWTEVWTLDDTFTKKLKAKVYEIDEVPGG--SYIVKIA 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 84621500    95 YPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRVPPAY 136
Cdd:pfam02788  79 YPLDLFEEGSIPQLLSSIAGNIFGMKAVKALRLEDIRFPPAY 120
RLP_NonPhot cd08207
Ribulose bisphosphate carboxylase like proteins from nonphototrophic bacteria; Ribulose ...
54-450 8.50e-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: 169.41  E-value: 8.50e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  54 STGTWTSV--WTDGLTslDRYKGRCYHIEPVAGEENQYIAY-------------VAYPLDLFEEgSVTNMFTSIVGNVFG 118
Cdd:cd08207  26 SSGTFIALpgETDELK--ERSAARVESIEELETAAQPSLPRrasggpytrarvtISFPLDNIGT-SLPNLLATVAGNLFE 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 119 FKALRALRLEDLRVPPAYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENV 198
Cdd:cd08207 103 LRELSGLRLVDLGLPDEFAAAFPGPAFGIAGTRRLTGVEDRPLIGTIIKPSVGLTPEETAALVRQLAAAGIDFIKDDELL 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 199 NSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATaGTCEEMIKRAVFARELGVPIVMHDYLTGGFTAntsLAHYCRD 278
Cdd:cd08207 183 ANPPYSPLDERVRAVMRVINDHAQRTGRKVMYAFNIT-DDIDEMRRNHDLVVEAGGTCVMVSLNSVGLSG---LAALRRH 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 279 NGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDHIHAGTVVGKLeGERDitlgfvdllrDDFIEKDRSrgiyFTQ 358
Cdd:cd08207 259 SQLPIHGHRNGWGMLTRSPALGISFQAYQKLWRLAGVDHLHVNGLASKF-WESD----------DSVIESARA----CLT 323
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 359 DWVSLP-GVLPVASGGIHVWHMPALTEIFGDDSVLQF-GGGTLGHPWGNAPGAVANRVALEACVQARNegrdlarqgnei 436
Cdd:cd08207 324 PLGGPDdAAMPVFSSGQWGGQAPPTYRRLGSVDLLYLaGGGIMAHPDGPAAGVRSLRQAWEAAVAGVP------------ 391
                       410
                ....*....|....
gi 84621500 437 IREASKWSPELAAA 450
Cdd:cd08207 392 LEEYAKTHPELARA 405
RLP_DK-MTP-1-P-enolase cd08209
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Ribulose bisphosphate carboxylase like ...
56-454 3.20e-41

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: 151.32  E-value: 3.20e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  56 GTWTSVWTDGLTSLDRYKGRCYHIEPvaGEENQYIAYVAYPLdlfeeGSVTNMFTSIVGNVFGFKALR-ALRLEDLRVPP 134
Cdd:cd08209  27 GSWTDLPALRQAQLQKHLGEVVSVEE--LEEGRGVITIAYPL-----INVSGDIPALLTTIFGKLSLDgKIKLVDLRLPE 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 135 AYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCA 214
Cdd:cd08209 100 EFGRAFPGPKFGIEGIRQRLGVHDRPLLMSIFKGVLGLDLDDLAEQLREQALGGVDLIKDDEILFDNPLAPALERIRACR 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 215 EAIYKAQAETGEIKGHYLNATaGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAhycRDNGLLLHI--HRAMHAV 292
Cdd:cd08209 180 PVLQEVYEQTGRRTLYAVNLT-GPVFTLKEKARRLVEAGANALLFNVFAYGLDVLEALA---SDPEINVPIfaHPAFAGA 255
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 293 IDRQKNHGM-HFRVLAKALRMSGGDHIHAGTVVGKLEGERDITLGFVDLLRDDFIEKdrsrgiyftqdwvslpGVLPVAS 371
Cdd:cd08209 256 LYGSPDYGIaASVLLGTLMRLAGADAVLFPSPYGSVALSKEEALAIAEALRRGGAFK----------------GVFPVPS 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 372 GGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACvqarnegrdlarQGNEIIREASKWSPELAAAC 451
Cdd:cd08209 320 AGIHPGLVPQLLRDFGTDVILNAGGGIHGHPDGAAAGVRAFREAIDAV------------LAGESLEPAAIPDGPLKSAL 387

                ...
gi 84621500 452 EVW 454
Cdd:cd08209 388 DKW 390
mtnW PRK09549
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Reviewed
56-454 1.34e-36

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


Pssm-ID: 236560  Cd Length: 407  Bit Score: 138.99  E-value: 1.34e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500   56 GTWTSVWTDGLTSLDRYKGRCYHIEPVAGEEN----QYIAYVAYPldlfeEGSVTNMFTSIVGNVFGFKALRA-LRLEDL 130
Cdd:PRK09549  31 GSWTDLPHLEQEQLKKHKGNVVHVEELEEHERkgvkRGIIKIAYP-----LANFSPDLPAILTTTFGKLSLDGeVKLIDL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  131 RVPPAYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRF 210
Cdd:PRK09549 106 TFSDELKRHFPGPKFGIDGIRNLLGVHDRPLLMSIFKGVIGRDLDYLKEQLRDQALGGVDLVKDDEILFENALTPFEKRI 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  211 LFCAEAIYKAQAETGEIKGHYLNATAGTCE--EMIKRAVfarELGVPIVMHDYLTGGFTANTSLAhycRDNGLLLHI--H 286
Cdd:PRK09549 186 VAGKEVLQEVYETTGHKTLYAVNLTGRTFElkEKAKRAA---EAGADALLFNVFAYGLDVLQSLA---EDPEIPVPImaH 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  287 RAMHAVIDRQKNHGM-HFRVLAKALRMSGGDHIHAGTVVGKLEGERDITLGFVDLLRDDFIEKDRSrgiyftqdwvslpg 365
Cdd:PRK09549 260 PAVSGAYTPSPLYGIsSPLLLGKLLRYAGADFSLFPSPYGSVALEKEEALAIAKELTEDDDPFKRS-------------- 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  366 vLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNegrdlarqgneiIREASKWSP 445
Cdd:PRK09549 326 -FPVPSAGIHPGLVPLLIRDFGKDVVINAGGGIHGHPNGAQGGGKAFRAAIDAVLQGKP------------LHEAAEDDE 392

                 ....*....
gi 84621500  446 ELAAACEVW 454
Cdd:PRK09549 393 NLHSALDIW 401
RLP_RrRLP cd08210
Ribulose bisphosphate carboxylase like proteins (RLPs) similar to R.rubrum RLP; RLP from ...
69-402 2.18e-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: 120.81  E-value: 2.18e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500  69 LDRYKGRCYHIEPVagEENQYIAYVAYPLDlfeegSVTNMFTSIVGNVFGFKAL-RALRLEDLRVPPAYSKTFQGPPHGI 147
Cdd:cd08210  42 RDNIVGRVESLEPA--GEGSYRARISYSVD-----TAGGELTQLLNVLFGNSSLqPGIRLVDFELPPSLLRRFPGPRFGI 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 148 QVERDKLNKYGRPLLGCTIKPkLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGei 227
Cdd:cd08210 115 AGLRALLGIPERPLLCSALKP-QGLSAAELAELAYAFALGGIDIIKDDHGLADQPFAPFEERVKACQEAVAEANAETG-- 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 228 kGH--YLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAhycRDNGLLLHIHRAMHAVIDRQKNHGM-HFR 304
Cdd:cd08210 192 -GRtlYAPNVTGPPTQLLERARFAKEAGAGGVLIAPGLTGLDTFRELA---EDFDFLPILAHPAFAGAFVSSGDGIsHAL 267
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 305 VLAKALRMSGGDHI---HAGtvvGKLEGERDITLGFVDLLRddfiekdrsrgiyftQDWVSLPGVLPVASGGIHVWHMPA 381
Cdd:cd08210 268 LFGTLFRLAGADAVifpNYG---GRFGFSREECQAIADACR---------------RPMGGLKPILPAPGGGMSVERAPE 329
                       330       340
                ....*....|....*....|.
gi 84621500 382 LTEIFGDDSVLQFGGGTLGHP 402
Cdd:cd08210 330 MVELYGPDVMLLIGGSLLRAG 350
salvage_mtnW TIGR03332
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Members of this family are the methionine ...
54-454 9.27e-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: 105.69  E-value: 9.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500    54 STGTWTSVWTDGLTSLDRYKGRCYHIEPVAGEE----------NQYIAYVAYPLDLFeegsvTNMFTSIVGNVFGFKALR 123
Cdd:TIGR03332  28 TIGSWTDLPLLKQEQLKKHKGRVVHVEELAESEhtnsylrkkvKRAIIKIAYPELNF-----SPDLPALLTTTFGKLSLD 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500   124 A-LRLEDLRVPPAYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQP 202
Cdd:TIGR03332 103 GeVKLIDLEFSDEFKRHFPGPKFGIDGIRKLLGVHERPLLMSIFKGMIGRDLGYLKEQLRQQALGGVDLVKDDEILFETG 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500   203 FMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATAGTCE--EMIKRAVfarELGVPIVMHDYLTGGFTANTSLAHycrDNG 280
Cdd:TIGR03332 183 LAPFEKRITEGKEVLQEVYEQTGHKTLYAVNLTGRTFDlkDKAKRAA---ELGADVLLFNVFAYGLDVLQSLAE---DDE 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500   281 LLLHI--HRAMHAVIDRQKNHGM-HFRVLAKALRMSGGDHIHAGTVVGKLEGERDITLGFVDllrddfiekdrsrgiYFT 357
Cdd:TIGR03332 257 IPVPImaHPAVSGAYTSSPFYGFsHSLLLGKLLRYAGADFSLFPSPYGSVALEREDALAISK---------------ELT 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500   358 QDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNegrdlarqgneiI 437
Cdd:TIGR03332 322 EDDAPFKKTFAVPSAGIHPGMVPLIMRDFGIDHIINAGGGIHGHPNGAQGGGRAFRAAIDAVLEAKP------------L 389
                         410
                  ....*....|....*..
gi 84621500   438 REASKWSPELAAACEVW 454
Cdd:TIGR03332 390 HEKAADDIDLKLALDKW 406
RLP_Photo cd08208
Ribulose bisphosphate carboxylase like proteins from phototrophic bacteria; Ribulose ...
105-450 1.31e-23

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: 102.67  E-value: 1.31e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 105 VTNMFTSIVGN-VFGFKALRALRLEDLRVPPAYSKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYE 183
Cdd:cd08208 105 IPNLLSAVCGEgTFFSPGVPVVKLMDIHFPETYLADFEGPKFGIAGLRERLQAHDRPIFFGVIKPNIGLPPGEFAELGYQ 184
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 184 CLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEAIYKAQAETGEIKGHYLNATaGTCEEMIKRAVFARELGVPIVMHDYLT 263
Cdd:cd08208 185 SWLGGLDIAKDDEMLADVDWCPLEERAALLGKARRRAEAETGVPKIYLANIT-DEVDRLMELHDVAVRNGANALLINAMP 263
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 264 GGFTANTSLAHYCRdngLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRMSGGDhihagTVVGKLEGERDITLGfvDLLRD 343
Cdd:cd08208 264 VGLSAVRMLRKHAQ---VPLIAHFPFIASFSRLEKYGIHSRVMTKLQRLAGLD-----VVIMPGFGPRMMTPE--EEVLE 333
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 84621500 344 DFIEKDRSRGiyftqdwvSLPGVLPVASGGIHVWHMPALTEIFGD-DSVLQFGGGTLGHPWGNAPGAVANRVALEACVQA 422
Cdd:cd08208 334 CVIACLEPMG--------PIKPCLPVPGGSDSALTLQTVYEKVGNvDFGFVPGRGVFGHPMGPKAGAKSIRQAWEAIEAG 405
                       330       340
                ....*....|....*....|....*...
gi 84621500 423 rnegrdlarqgnEIIREASKWSPELAAA 450
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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