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Conserved domains on  [gi|663441502|gb|AIF28161|]
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ribulose-1,5-biphosphate carboxylase/oxygenase, partial (chloroplast) [Klebsormidium sp. W419]

Protein Classification

RuBisCO large subunit( domain architecture ID 315)

large subunit of the ribulose bisphosphate carboxylase is part of the complex that catalyzes the primary event in carbon dioxide fixation, the carboxylation of D-ribulose 1,5-bisphosphate, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process.

EC:  4.1.1.39
Gene Ontology:  GO:0016984
PubMed:  18294858

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RuBisCO_large super family cl08232
Ribulose bisphosphate carboxylase large chain; Ribulose bisphosphate carboxylase (Rubisco) ...
1-222 0e+00

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


The actual alignment was detected with superfamily member CHL00040:

Pssm-ID: 471793  Cd Length: 475  Bit Score: 506.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502   1 FLFVAEATFKAQAETGEIKGHYLNATAGTSEEMLKRAQFARELGAPIVMHDYLTGGFTANTSLSHYCRDNGLLLHIHRAM 80
Cdd:CHL00040 218 FLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMYKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAM 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502  81 HAVIDRQRNHGIHFRVLAKALRLSGGDHIHSGTVVGKLEGEREVTLGFVDLLRDDYIEKDRSRGIYFTQDWVSLPGVLPV 160
Cdd:CHL00040 298 HAVIDRQKNHGIHFRVLAKALRMSGGDHIHAGTVVGKLEGEREMTLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPV 377
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663441502 161 ASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLSR 222
Cdd:CHL00040 378 ASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAR 439
 
Name Accession Description Interval E-value
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
1-222 0e+00

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


Pssm-ID: 176981  Cd Length: 475  Bit Score: 506.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502   1 FLFVAEATFKAQAETGEIKGHYLNATAGTSEEMLKRAQFARELGAPIVMHDYLTGGFTANTSLSHYCRDNGLLLHIHRAM 80
Cdd:CHL00040 218 FLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMYKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAM 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502  81 HAVIDRQRNHGIHFRVLAKALRLSGGDHIHSGTVVGKLEGEREVTLGFVDLLRDDYIEKDRSRGIYFTQDWVSLPGVLPV 160
Cdd:CHL00040 298 HAVIDRQKNHGIHFRVLAKALRMSGGDHIHAGTVVGKLEGEREMTLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPV 377
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663441502 161 ASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLSR 222
Cdd:CHL00040 378 ASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAR 439
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
1-222 2.50e-163

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: 458.43  E-value: 2.50e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502   1 FLFVAEATFKAQAETGEIKGHYLNATAGTSEEMLKRAQFARELGAPIVMHDYLTGgFTANTSLSHYCRDNGLLLHIHRAM 80
Cdd:cd08212  196 FLFVAEAVNKAQAETGEVKGHYLNVTAGTMEEMYKRAEFAKELGSPIIMHDLLTG-FTAIQSLAKWCRDNGMLLHLHRAG 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502  81 HAVIDRQRNHGIHFRVLAKALRLSGGDHIHSGTVVGKLEGEREVTLGFVDLLRDDYIEKDRSRGIYFTQDWVSLPGVLPV 160
Cdd:cd08212  275 HATYDRQKNHGIHFRVLAKWLRLSGVDHIHAGTVVGKLEGDPLVTLGFYDLLRDDYIEKDRSRGIFFTQDWASLPGVMPV 354
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663441502 161 ASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLSR 222
Cdd:cd08212  355 ASGGIHVGQMHQLIEIFGDDVVLQFGGGTIGHPWGIAAGATANRVALEAMVQARNEGRDLAR 416
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
1-220 1.71e-109

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: 315.84  E-value: 1.71e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502    1 FLFVAEATFKAQAETGEIKGHYLNATAGTSEEMLKRAQFARELGAPIVMHDYLTGGFTANTSLSHYCRDNGLLLHIHRAM 80
Cdd:pfam00016  64 FLFVAEAIDRAQDETGEAKGHYLNITADDMEEMYRRAEFAKETGGVAVMVDGLVIGPTAITTLRRWFRDNGVILHYHRAG 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502   81 HAVIDRQRNHGIHFRVLAKALRLSGGDHIHSGTV-VGKLEGEREvtlgfvDLLRDDYIEKDRSRGIYFTQDWVSLPGVLP 159
Cdd:pfam00016 144 HGAVTRQSKHGISFRVLAKMARLAGADHLHTGTMgVGKLEGDPS------DTLRAYMLEEDRARGPFFDQDWGGMPAVMP 217
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663441502  160 VASGGIHVWHMPALTEIFGD-DSVLQFGGGTLGHPWGNAPGAVANRVALEACVqarnEGRDL 220
Cdd:pfam00016 218 VASGGIHAGQMPGLFDNLGDsDVILQFGGGTFGHPDGPAAGAKANRQALEAWV----EGRDL 275
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
1-215 7.69e-78

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


Pssm-ID: 441455  Cd Length: 417  Bit Score: 239.69  E-value: 7.69e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502   1 FLFVAEATFKAQAETGEIKGHYLNATAGTsEEMLKRAQFARELGAPIVMHDYLTGGFTANTSLSHycRDNGLLLHIHRAM 80
Cdd:COG1850  198 VRAVMEAIDRAEEETGEKKMYAFNITADT-DEMLRRADLAVELGANAVMVDVNTVGLSAVQTLRE--EHIGLPIHAHRAG 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502  81 HAVIDRQRNHGIHFRVLAKALRLSGGDHIHSGTVVGKLEGEREVTLGFVDLLRddyiekdrsrgiyftQDWVSLPGVLPV 160
Cdd:COG1850  275 HGAFTRSPLHGISMRVLAKLWRLAGADHLHVGTPVGKMEGDDEEVLAIADALL---------------QPWGGLKPVFPV 339
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 663441502 161 ASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARN 215
Cdd:COG1850  340 PSGGQHPGQVPELYDALGTDLILQAGGGIHGHPDGPAAGARALRQAWEAAVAGIP 394
rubisco_III TIGR03326
ribulose bisphosphate carboxylase, type III; Members of this protein family are the archaeal, ...
10-214 6.07e-56

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: 183.05  E-value: 6.07e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502   10 KAQAETGEIKGHYLNATAGTsEEMLKRAQFARELGAPIVMHDYLTGGFTANTSLSHYCRDNGLLLHIHRAMHAVIDRQRN 89
Cdd:TIGR03326 203 KVEAETGEKKSYLINITADV-REMERRAELVADLGGEYVMVDIVVAGWSALQYVRERTEDLGLAIHAHRAMHAAFTRNPK 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502   90 HGIHFRVLAKALRLSGGDHIHSGTV-VGKLEGEREVTLGFVDLLRddyiekdrsrgiyftQDWVSLPGVLPVASGGIHVW 168
Cdd:TIGR03326 282 HGISMFVLAKLYRLIGVDQLHTGTAgVGKLEGGNEDTKGINDFLR---------------QDWHHIKPVFPVASGGLHPG 346
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 663441502  169 HMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQAR 214
Cdd:TIGR03326 347 LVPPLIDALGTDLVIQAGGGVHGHPDGTRAGAKALRAAIDAIIEGI 392
 
Name Accession Description Interval E-value
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
1-222 0e+00

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


Pssm-ID: 176981  Cd Length: 475  Bit Score: 506.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502   1 FLFVAEATFKAQAETGEIKGHYLNATAGTSEEMLKRAQFARELGAPIVMHDYLTGGFTANTSLSHYCRDNGLLLHIHRAM 80
Cdd:CHL00040 218 FLFCAEAIYKAQAETGEIKGHYLNATAGTCEEMYKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAM 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502  81 HAVIDRQRNHGIHFRVLAKALRLSGGDHIHSGTVVGKLEGEREVTLGFVDLLRDDYIEKDRSRGIYFTQDWVSLPGVLPV 160
Cdd:CHL00040 298 HAVIDRQKNHGIHFRVLAKALRMSGGDHIHAGTVVGKLEGEREMTLGFVDLLRDDFIEKDRSRGIYFTQDWVSLPGVLPV 377
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663441502 161 ASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLSR 222
Cdd:CHL00040 378 ASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLAR 439
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
1-222 2.50e-163

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: 458.43  E-value: 2.50e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502   1 FLFVAEATFKAQAETGEIKGHYLNATAGTSEEMLKRAQFARELGAPIVMHDYLTGgFTANTSLSHYCRDNGLLLHIHRAM 80
Cdd:cd08212  196 FLFVAEAVNKAQAETGEVKGHYLNVTAGTMEEMYKRAEFAKELGSPIIMHDLLTG-FTAIQSLAKWCRDNGMLLHLHRAG 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502  81 HAVIDRQRNHGIHFRVLAKALRLSGGDHIHSGTVVGKLEGEREVTLGFVDLLRDDYIEKDRSRGIYFTQDWVSLPGVLPV 160
Cdd:cd08212  275 HATYDRQKNHGIHFRVLAKWLRLSGVDHIHAGTVVGKLEGDPLVTLGFYDLLRDDYIEKDRSRGIFFTQDWASLPGVMPV 354
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663441502 161 ASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLSR 222
Cdd:cd08212  355 ASGGIHVGQMHQLIEIFGDDVVLQFGGGTIGHPWGIAAGATANRVALEAMVQARNEGRDLAR 416
rbcL PRK04208
ribulose bisophosphate carboxylase; Reviewed
1-222 6.03e-153

ribulose bisophosphate carboxylase; Reviewed


Pssm-ID: 179787  Cd Length: 468  Bit Score: 432.79  E-value: 6.03e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502   1 FLFVAEATFKAQAETGEIKGHYLNATAGTSEEMLKRAQFARELGAPIVMHDYLTGGFTANTSLSHYCRDNGLLLHIHRAM 80
Cdd:PRK04208 211 FLFVMEAIDKAEAETGERKGHYLNVTAPTMEEMYKRAEFAKELGSPIVMIDVVTAGWTALQSLREWCRDNGLALHAHRAM 290
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502  81 HAVIDRQRNHGIHFRVLAKALRLSGGDHIHSGTVVGKLEGEREVTLGFVDLLRDDYIEKDRSRGIYFTQDWVSLPGVLPV 160
Cdd:PRK04208 291 HAAFTRNPNHGISFRVLAKLLRLIGVDHLHTGTVVGKLEGDRAEVLGYYDILREDFVPEDRSRGIFFDQDWGSIKPVFPV 370
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663441502 161 ASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLSR 222
Cdd:PRK04208 371 ASGGIHPGHMPALLDIFGDDVVLQFGGGTHGHPDGTAAGATANRVALEACVEARNEGRDIEK 432
RuBisCO_large_I_II_III cd08206
Ribulose bisphosphate carboxylase large chain, Form I,II,III; Ribulose bisphosphate ...
1-214 1.12e-130

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: 374.26  E-value: 1.12e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502   1 FLFVAEATFKAQAETGEIKGHYLNATAGTSEEMLKRAQFARELGAPIVMHDYLTGGFTANTSLSHYCRDNGLLLHIHRAM 80
Cdd:cd08206  183 ILFVAEAMDKAEAETGEAKGHYLNITADTPEEMIKRAEFAKELGSVIVMVDGVTAGWTAIQSARRWCPDNGLALHAHRAG 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502  81 HAVIDRQRNHGIHFRVLAKALRLSGGDHIHSGTVVGKLEGEREVTLGFVDLLRDDYIEKDRSRgIYFTQDWVSLPGVLPV 160
Cdd:cd08206  263 HAAFTRQKNHGISMRVLAKLARLIGVDHIHTGTVVGKLEGDPSEVKGIADMLREDEVEGDLSR-IFFNQDWGGMKPVFPV 341
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 663441502 161 ASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQAR 214
Cdd:cd08206  342 ASGGLHPGRMPALIEILGDDVILQFGGGTHGHPDGPAAGAKANRQALEAWVQGR 395
RuBisCO_large pfam00016
Ribulose bisphosphate carboxylase large chain, catalytic domain; The C-terminal domain of ...
1-220 1.71e-109

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: 315.84  E-value: 1.71e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502    1 FLFVAEATFKAQAETGEIKGHYLNATAGTSEEMLKRAQFARELGAPIVMHDYLTGGFTANTSLSHYCRDNGLLLHIHRAM 80
Cdd:pfam00016  64 FLFVAEAIDRAQDETGEAKGHYLNITADDMEEMYRRAEFAKETGGVAVMVDGLVIGPTAITTLRRWFRDNGVILHYHRAG 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502   81 HAVIDRQRNHGIHFRVLAKALRLSGGDHIHSGTV-VGKLEGEREvtlgfvDLLRDDYIEKDRSRGIYFTQDWVSLPGVLP 159
Cdd:pfam00016 144 HGAVTRQSKHGISFRVLAKMARLAGADHLHTGTMgVGKLEGDPS------DTLRAYMLEEDRARGPFFDQDWGGMPAVMP 217
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663441502  160 VASGGIHVWHMPALTEIFGD-DSVLQFGGGTLGHPWGNAPGAVANRVALEACVqarnEGRDL 220
Cdd:pfam00016 218 VASGGIHAGQMPGLFDNLGDsDVILQFGGGTFGHPDGPAAGAKANRQALEAWV----EGRDL 275
RuBisCO_large cd08148
Ribulose bisphosphate carboxylase large chain; Ribulose bisphosphate carboxylase (Rubisco) ...
1-206 2.44e-93

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: 277.77  E-value: 2.44e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502   1 FLFVAEATFKAQAETGEIKGHYLNATAGTsEEMLKRAQFARELGAPIVMHDYLTGGFTANTSLSHYCRdNGLLLHIHRAM 80
Cdd:cd08148  178 ITEVAAALDRVQEETGEKKLYAVNVTAGT-FEIIERAERALELGANMLMVDVLTAGFSALQALAEDFE-IDLPIHVHRAM 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502  81 HAVIDRQRNHGIHFRVLAKALRLSGGDHIHSGTVVGKLEGEREVTLGFVDLLRDDyiekdrsrgiyftqdWVSLPGVLPV 160
Cdd:cd08148  256 HGAVTRSKFHGISMLVLAKLLRMAGGDFIHTGTVVGKMALEREEALGIADALTDD---------------WAGFKRVFPV 320
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 663441502 161 ASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVA 206
Cdd:cd08148  321 ASGGIHPGLVPGILRDFGIDVILQAGGGIHGHPDGTVAGARAMRQA 366
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
1-215 7.69e-78

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


Pssm-ID: 441455  Cd Length: 417  Bit Score: 239.69  E-value: 7.69e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502   1 FLFVAEATFKAQAETGEIKGHYLNATAGTsEEMLKRAQFARELGAPIVMHDYLTGGFTANTSLSHycRDNGLLLHIHRAM 80
Cdd:COG1850  198 VRAVMEAIDRAEEETGEKKMYAFNITADT-DEMLRRADLAVELGANAVMVDVNTVGLSAVQTLRE--EHIGLPIHAHRAG 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502  81 HAVIDRQRNHGIHFRVLAKALRLSGGDHIHSGTVVGKLEGEREVTLGFVDLLRddyiekdrsrgiyftQDWVSLPGVLPV 160
Cdd:COG1850  275 HGAFTRSPLHGISMRVLAKLWRLAGADHLHVGTPVGKMEGDDEEVLAIADALL---------------QPWGGLKPVFPV 339
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 663441502 161 ASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARN 215
Cdd:COG1850  340 PSGGQHPGQVPELYDALGTDLILQAGGGIHGHPDGPAAGARALRQAWEAAVAGIP 394
RuBisCO_large_III cd08213
Ribulose bisphosphate carboxylase large chain, Form III; Ribulose bisphosphate carboxylase ...
4-213 1.80e-68

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: 215.33  E-value: 1.80e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502   4 VAEATFKAQAETGEIKGHYLNATAGTsEEMLKRAQFARELGAPIVMHDYLTGGFTANTSLSHYCRDNGLLLHIHRAMHAV 83
Cdd:cd08213  185 SLKARDKAEAETGERKAYLANITAPV-REMERRAELVADLGGKYVMIDVVVAGWSALQYLRDLAEDYGLAIHAHRAMHAA 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502  84 IDRQRNHGIHFRVLAKALRLSGGDHIHSGTVVGKLEGEREVTLGFVDLLRDDYIEKDrSRGIYFTQDWVSLPGVLPVASG 163
Cdd:cd08213  264 FTRNPRHGISMLVLAKLYRLIGVDQLHIGTAVGKMEGDKEEVLRIADILREQKYKPD-EEDFHLAQDWGGIKPVFPVASG 342
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 663441502 164 GIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQA 213
Cdd:cd08213  343 GLHPGLVPDVIDILGKDIVIQVGGGVHGHPDGTRAGAKAVRQAIEAALEG 392
rubisco_III TIGR03326
ribulose bisphosphate carboxylase, type III; Members of this protein family are the archaeal, ...
10-214 6.07e-56

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: 183.05  E-value: 6.07e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502   10 KAQAETGEIKGHYLNATAGTsEEMLKRAQFARELGAPIVMHDYLTGGFTANTSLSHYCRDNGLLLHIHRAMHAVIDRQRN 89
Cdd:TIGR03326 203 KVEAETGEKKSYLINITADV-REMERRAELVADLGGEYVMVDIVVAGWSALQYVRERTEDLGLAIHAHRAMHAAFTRNPK 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502   90 HGIHFRVLAKALRLSGGDHIHSGTV-VGKLEGEREVTLGFVDLLRddyiekdrsrgiyftQDWVSLPGVLPVASGGIHVW 168
Cdd:TIGR03326 282 HGISMFVLAKLYRLIGVDQLHTGTAgVGKLEGGNEDTKGINDFLR---------------QDWHHIKPVFPVASGGLHPG 346
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 663441502  169 HMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQAR 214
Cdd:TIGR03326 347 LVPPLIDALGTDLVIQAGGGVHGHPDGTRAGAKALRAAIDAIIEGI 392
PRK13475 PRK13475
ribulose-bisphosphate carboxylase;
4-209 2.88e-32

ribulose-bisphosphate carboxylase;


Pssm-ID: 184072  Cd Length: 443  Bit Score: 121.37  E-value: 2.88e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502   4 VAEATFKAQAETGEIKGHYLNATAGTSEEMLKRAQFARELGAPIVMH-DYLTGGFTANTSLSHYCRDN--GLLLHIHRAM 80
Cdd:PRK13475 211 VADAMKRAQDETGEAKLFSANITADDHYEMIARGEYILETFGENADHvAFLVDGYVAGPGAVTTARRQypDQYLHYHRAG 290
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502  81 HAVIDRQRN-HGIHFRVLAKALRLSGGDHIHSGTV-VGKLEGEREvtlgfvDLLRDDYIEKDRSRGIYFTQDWVSLPGVL 158
Cdd:PRK13475 291 HGAVTSPSSkRGYTAFVLSKMARLQGASGIHTGTMgYGKMEGEAD------DRVIAYMIERDSAQGPFYHQEWYGMKPTT 364
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 663441502 159 PVASGGIHVWHMPALTEIFGDDSVLQ-FGGGTLGHPWGNAPGAVANRVALEA 209
Cdd:PRK13475 365 PIISGGMNALRLPGFFDNLGHGNVINtAGGGAFGHIDGPAAGAKSLRQAYDC 416
RuBisCO_large_II cd08211
Ribulose bisphosphate carboxylase large chain, Form II; Ribulose bisphosphate carboxylase ...
4-215 2.77e-31

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: 118.76  E-value: 2.77e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502   4 VAEATFKAQAETGEIKGHYLNATAGTSEEMLKRAQFARELGAPIVMH-----DYLTGGFTANTSLSHYCRDNglLLHIHR 78
Cdd:cd08211  210 VADAMRRAQDETGEAKLFSANITADDPDEMIARGEYILEAFGPNAGHvaflvDGYVAGPAAVTTARRRFPDQ--FLHYHR 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502  79 AMHAVIDRQRNH-GIHFRVLAKALRLSGGDHIHSGTV-VGKLEGEREvtlgfvDLLRDDYIEKDRSRGIYFTQDWVSLPG 156
Cdd:cd08211  288 AGHGAVTSPQSKrGYTAFVLSKMARLQGASGIHTGTMgFGKMEGESS------DKVIAYMIERDEAQGPLFNQKWYGMKP 361
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502 157 VLPVASGGIHVWHMPALTEIFGDDSVLQ-FGGGTLGHPWGNAPGAVANRVALEACVQARN 215
Cdd:cd08211  362 TTPIISGGMNALRLPGFFENLGNGNVILtAGGGSFGHIDGPAAGAKSLRQAYDAWKQGVD 421
RuBisCO_IV_RLP cd08205
Ribulose bisphosphate carboxylase like proteins, Rubisco-Form IV; Ribulose bisphosphate ...
4-206 5.15e-23

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: 94.91  E-value: 5.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502   4 VAEATFKAQAETGEIKGHYLNATaGTSEEMLKRAQFARELGAPIVMHDYLTGGFTANTSLShycRDNGLLLHIHRAMHAV 83
Cdd:cd08205  184 CMEAVRRANEETGRKTLYAPNIT-GDPDELRRRADRAVEAGANALLINPNLVGLDALRALA---EDPDLPIMAHPAFAGA 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502  84 IDRQRNHGIHFRVLAKALRLSGGDHIHSGTVVGKLEGEREVTLGFVDLLRddyiekdrsrgiyftQDWVSLPGVLPVASG 163
Cdd:cd08205  260 LSRSPDYGSHFLLLGKLMRLAGADAVIFPGPGGRFPFSREECLAIARACR---------------RPLGGIKPALPVPSG 324
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 663441502 164 GIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVA 206
Cdd:cd08205  325 GMHPGRVPELYRDYGPDVILLAGGGILGHPDGAAAGVRAFRQA 367
mtnW PRK09549
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Reviewed
10-214 4.47e-14

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


Pssm-ID: 236560  Cd Length: 407  Bit Score: 70.04  E-value: 4.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502  10 KAQAETGEIKGHYLNATAGTSEemLK-RAQFARELGAPIVMHDYLTGGFTANTSLShycRDNGLLLHI--HRAMHAVIDR 86
Cdd:PRK09549 194 EVYETTGHKTLYAVNLTGRTFE--LKeKAKRAAEAGADALLFNVFAYGLDVLQSLA---EDPEIPVPImaHPAVSGAYTP 268
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502  87 QRNHGI-HFRVLAKALRLSGGDHIHSGTVVGKLEGEREVTLGFVDLLRDDYIEKDRSrgiyftqdwvslpgvLPVASGGI 165
Cdd:PRK09549 269 SPLYGIsSPLLLGKLLRYAGADFSLFPSPYGSVALEKEEALAIAKELTEDDDPFKRS---------------FPVPSAGI 333
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 663441502 166 HVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQAR 214
Cdd:PRK09549 334 HPGLVPLLIRDFGKDVVINAGGGIHGHPNGAQGGGKAFRAAIDAVLQGK 382
RLP_NonPhot cd08207
Ribulose bisphosphate carboxylase like proteins from nonphototrophic bacteria; Ribulose ...
31-212 6.91e-13

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: 66.56  E-value: 6.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502  31 EEMLKRAQFARELGAPIVMHDYLTGGFTAntsLSHYCRDNGLLLHIHRAMHAVIDRQRNHGIHFRVLAKALRLSGGDHIH 110
Cdd:cd08207  223 DEMRRNHDLVVEAGGTCVMVSLNSVGLSG---LAALRRHSQLPIHGHRNGWGMLTRSPALGISFQAYQKLWRLAGVDHLH 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502 111 SGTVVGKL-EGEREVTLGFVDLLRDDYIEKDRsrgiyftqdwvslpgVLPVASGGIHVWHMPALTEIFGDDSVLQF-GGG 188
Cdd:cd08207  300 VNGLASKFwESDDSVIESARACLTPLGGPDDA---------------AMPVFSSGQWGGQAPPTYRRLGSVDLLYLaGGG 364
                        170       180
                 ....*....|....*....|....
gi 663441502 189 TLGHPWGNAPGAVANRVALEACVQ 212
Cdd:cd08207  365 IMAHPDGPAAGVRSLRQAWEAAVA 388
RLP_DK-MTP-1-P-enolase cd08209
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Ribulose bisphosphate carboxylase like ...
10-214 1.19e-12

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: 66.19  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502  10 KAQAETGEIKGHYLNATaGTSEEMLKRAQFARELGAPIVMHDYLTGGFTANTSLShycRDNGLLLHI--HRAMHAVIDRQ 87
Cdd:cd08209  184 EVYEQTGRRTLYAVNLT-GPVFTLKEKARRLVEAGANALLFNVFAYGLDVLEALA---SDPEINVPIfaHPAFAGALYGS 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502  88 RNHGI-HFRVLAKALRLSGGDHIHSGTVVGKLEGEREVTLGFVDLLRDDYIEKdrsrgiyftqdwvslpGVLPVASGGIH 166
Cdd:cd08209  260 PDYGIaASVLLGTLMRLAGADAVLFPSPYGSVALSKEEALAIAEALRRGGAFK----------------GVFPVPSAGIH 323
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 663441502 167 VWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQAR 214
Cdd:cd08209  324 PGLVPQLLRDFGTDVILNAGGGIHGHPDGAAAGVRAFREAIDAVLAGE 371
salvage_mtnW TIGR03332
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Members of this family are the methionine ...
10-214 6.75e-10

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: 57.92  E-value: 6.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502   10 KAQAETGEIKGH---YLNATAGTSEEMLKRAQFARELGAPIVMHDYLTGGFTANTSLSHycrDNGLLLHI--HRAMHAVI 84
Cdd:TIGR03332 195 EVLQEVYEQTGHktlYAVNLTGRTFDLKDKAKRAAELGADVLLFNVFAYGLDVLQSLAE---DDEIPVPImaHPAVSGAY 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502   85 DRQRNHGI-HFRVLAKALRLSGGDHIHSGTVVGKLEGEREVTLGFVDllrddyiekdrsrgiYFTQDWVSLPGVLPVASG 163
Cdd:TIGR03332 272 TSSPFYGFsHSLLLGKLLRYAGADFSLFPSPYGSVALEREDALAISK---------------ELTEDDAPFKKTFAVPSA 336
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 663441502  164 GIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQAR 214
Cdd:TIGR03332 337 GIHPGMVPLIMRDFGIDHIINAGGGIHGHPNGAQGGGRAFRAAIDAVLEAK 387
RLP_RrRLP cd08210
Ribulose bisphosphate carboxylase like proteins (RLPs) similar to R.rubrum RLP; RLP from ...
4-193 4.76e-06

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: 46.46  E-value: 4.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502   4 VAEATFKAQAETGeikGH--YLNATAGTSEEMLKRAQFARELGAPIVMhdyLTGGFTANTSLSHYCRDNGLLLHIHRAMH 81
Cdd:cd08210  179 CQEAVAEANAETG---GRtlYAPNVTGPPTQLLERARFAKEAGAGGVL---IAPGLTGLDTFRELAEDFDFLPILAHPAF 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663441502  82 AVIDRQRNHGI-HFRVLAKALRLSGGDHIHSGTVVGKLEGEREVTLGFVDLLRddyiekdrsrgiyftQDWVSLPGVLPV 160
Cdd:cd08210  253 AGAFVSSGDGIsHALLFGTLFRLAGADAVIFPNYGGRFGFSREECQAIADACR---------------RPMGGLKPILPA 317
                        170       180       190
                 ....*....|....*....|....*....|...
gi 663441502 161 ASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHP 193
Cdd:cd08210  318 PGGGMSVERAPEMVELYGPDVMLLIGGSLLRAG 350
 
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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