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Conserved domains on  [gi|2510319192|gb|WHU54771|]
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ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit, partial (chloroplast) [Leucopogon virgatus]

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) ...
 1-124 1.16e-90

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: 270.04  E-value: 1.16e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2510319192   1 RVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVPGDENQYIAYVAYPLDLFEEGSVTNMFTSI 80
Cdd:CHL00040   41 RVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYRIEPVPGEENQYIAYVAYPLDLFEEGSVTNMFTSI 120

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2510319192  81 VGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVE*DKLNK 124
Cdd:CHL00040  121 VGNVFGFKALRALRLEDLRIPPAYLKTFQGPPHGIQVERDKLNK 164
 
Name Accession Description Interval E-value
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
 1-124 1.16e-90

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


Pssm-ID: 176981  Cd Length: 475  Bit Score: 270.04  E-value: 1.16e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2510319192   1 RVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVPGDENQYIAYVAYPLDLFEEGSVTNMFTSI 80
Cdd:CHL00040   41 RVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYRIEPVPGEENQYIAYVAYPLDLFEEGSVTNMFTSI 120

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2510319192  81 VGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVE*DKLNK 124
Cdd:CHL00040  121 VGNVFGFKALRALRLEDLRIPPAYLKTFQGPPHGIQVERDKLNK 164
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
 1-124 3.74e-84

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: 252.73  E-value: 3.74e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2510319192   1 RVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVPGDENQYIAYVAYPLDLFEEGSVTNMFTSI 80
Cdd:cd08212    19 RITPQPGVDPEEAAAAVAGESSTATWTVVWTDRLTALDRYKGKAYRVEPVPGEENQYFAYIAYPLDLFEEGSVANLTTSI 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2510319192  81 VGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVE*DKLNK 124
Cdd:cd08212    99 VGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDRLNK 142
RuBisCO_large_N pfam02788
Ribulose bisphosphate carboxylase large chain, N-terminal domain; The N-terminal domain of ...
 1-104 3.23e-47

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: 147.74  E-value: 3.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2510319192   1 RVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVPGDenQYIAYVAYPLDLFEEGSVTNMFTSI 80
Cdd:pfam02788  19 RIEPAAGVSPEEAAAHVAAESSTGTWTEVWTLDDTFTKKLKAKVYEIDEVPGG--SYIVKIAYPLDLFEEGSIPQLLSSI 96

                          90       100
                  ....*....|....*....|....
gi 2510319192  81 VGNVFGFKALRALRLEDLRIPPAY 104
Cdd:pfam02788  97 AGNIFGMKAVKALRLEDIRFPPAY 120
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
 1-124 1.14e-40

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


Pssm-ID: 441455  Cd Length: 417  Bit Score: 139.15  E-value: 1.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2510319192   1 RVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVP---GDENQYIAYVAYPLDLFeEGSVTNMF 77
Cdd:COG1850    19 RITPETGVDPEEAAAAIAGEQSTGTWTEVPTETDELRERLAARVYSIEELPevgGGYRRALVTIAYPLENF-GGNLPNLL 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2510319192  78 TSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVE*DKLNK 124
Cdd:COG1850    98 STVAGNLFGLKAVSGLRLLDLEFPESFLAAFPGPKFGIEGTRELLGV 144
 
Name Accession Description Interval E-value
rbcL CHL00040
ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit
 1-124 1.16e-90

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


Pssm-ID: 176981  Cd Length: 475  Bit Score: 270.04  E-value: 1.16e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2510319192   1 RVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVPGDENQYIAYVAYPLDLFEEGSVTNMFTSI 80
Cdd:CHL00040   41 RVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYRIEPVPGEENQYIAYVAYPLDLFEEGSVTNMFTSI 120

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2510319192  81 VGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVE*DKLNK 124
Cdd:CHL00040  121 VGNVFGFKALRALRLEDLRIPPAYLKTFQGPPHGIQVERDKLNK 164
RuBisCO_large_I cd08212
Ribulose bisphosphate carboxylase large chain, Form I; Ribulose bisphosphate carboxylase ...
 1-124 3.74e-84

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: 252.73  E-value: 3.74e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2510319192   1 RVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVPGDENQYIAYVAYPLDLFEEGSVTNMFTSI 80
Cdd:cd08212    19 RITPQPGVDPEEAAAAVAGESSTATWTVVWTDRLTALDRYKGKAYRVEPVPGEENQYFAYIAYPLDLFEEGSVANLTTSI 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2510319192  81 VGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVE*DKLNK 124
Cdd:cd08212    99 VGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVERDRLNK 142
rbcL PRK04208
ribulose bisophosphate carboxylase; Reviewed
 1-124 4.51e-74

ribulose bisophosphate carboxylase; Reviewed


Pssm-ID: 179787  Cd Length: 468  Bit Score: 227.10  E-value: 4.51e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2510319192   1 RVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVPGDENQYIAYVAYPLDLFEEGSVTNMFTSI 80
Cdd:PRK04208   34 RITPQEGVDPEEAAAAVAAESSTGTWTTVWTDLLTDLDKYKAKAYRIEDVPGDDGSYYAFIAYPLDLFEEGSIPNLLASI 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2510319192  81 VGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVE*DKLNK 124
Cdd:PRK04208  114 AGNVFGFKAVKALRLEDIRFPVAYVKTFKGPPFGIQVERERLDK 157
RuBisCO_large_I_II_III cd08206
Ribulose bisphosphate carboxylase large chain, Form I,II,III; Ribulose bisphosphate ...
 1-124 1.09e-65

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: 204.01  E-value: 1.09e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2510319192   1 RVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVPgdENQYIAYVAYPLDLFEEGSVTNMFTSI 80
Cdd:cd08206     8 RMTPAEGVDPEEAAAAVAAESSTGTWTTVWTDRLTATERLKAKVYRIDPVP--DGQYIAKIAYPLDLFEEGSVPNLLTSI 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2510319192  81 VGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVE*DKLNK 124
Cdd:cd08206    86 IGNVFGMKAVKALRLEDFRFPPAYLKTFDGPSFGIQGEREILGK 129
RuBisCO_large_N pfam02788
Ribulose bisphosphate carboxylase large chain, N-terminal domain; The N-terminal domain of ...
 1-104 3.23e-47

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: 147.74  E-value: 3.23e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2510319192   1 RVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVPGDenQYIAYVAYPLDLFEEGSVTNMFTSI 80
Cdd:pfam02788  19 RIEPAAGVSPEEAAAHVAAESSTGTWTEVWTLDDTFTKKLKAKVYEIDEVPGG--SYIVKIAYPLDLFEEGSIPQLLSSI 96

                          90       100
                  ....*....|....*....|....
gi 2510319192  81 VGNVFGFKALRALRLEDLRIPPAY 104
Cdd:pfam02788  97 AGNIFGMKAVKALRLEDIRFPPAY 120
RuBisCO_large cd08148
Ribulose bisphosphate carboxylase large chain; Ribulose bisphosphate carboxylase (Rubisco) ...
 1-124 1.17e-45

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: 151.04  E-value: 1.17e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2510319192   1 RVSPQPgVPPEEAGAAVAAESSTGTWTTVWTdGLTSLDRYKGRCYHIEPVPgdeNQYIAYVAYPLDLFEEGSVTNMFTSI 80
Cdd:cd08148     6 RVHPEA-TPPEKAAEAIAAESSTGTWTEVPT-TQEQLRRVKGRVYSVEELG---KRYIVKIAYPVELFEPGNIPQILTVT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2510319192  81 VGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVE*DKLNK 124
Cdd:cd08148    81 AGNLFGLGALEAVRLEDLEFPEEYKKLFPGPKFGIDGIRKLLGV 124
RbcL COG1850
Ribulose 1,5-bisphosphate carboxylase, large subunit, or a RuBisCO-like protein [Carbohydrate ...
 1-124 1.14e-40

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


Pssm-ID: 441455  Cd Length: 417  Bit Score: 139.15  E-value: 1.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2510319192   1 RVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVP---GDENQYIAYVAYPLDLFeEGSVTNMF 77
Cdd:COG1850    19 RITPETGVDPEEAAAAIAGEQSTGTWTEVPTETDELRERLAARVYSIEELPevgGGYRRALVTIAYPLENF-GGNLPNLL 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2510319192  78 TSIVGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVE*DKLNK 124
Cdd:COG1850    98 STVAGNLFGLKAVSGLRLLDLEFPESFLAAFPGPKFGIEGTRELLGV 144
RuBisCO_large_III cd08213
Ribulose bisphosphate carboxylase large chain, Form III; Ribulose bisphosphate carboxylase ...
 1-122 7.73e-34

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: 121.34  E-value: 7.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2510319192   1 RVSPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEpvpGDENQYIAYVAYPLDLFEEGSVTNMFTSI 80
Cdd:cd08213     8 RIEPAEGISIEEAAGRVASESSIGTWTTLATLYPERAEKLKAKAYYFD---GLGGSYIVKVAYPLELFEEGNMPQLLSSI 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2510319192  81 VGNVFGFKALRALRLEDLRIPPAYVKTFQGPPHGIQVE*DKL 122
Cdd:cd08213    85 AGNIFGMKAVKNLRLEDIYFPESYLREFKGPQFGIEGVREIL 126
RuBisCO_IV_RLP cd08205
Ribulose bisphosphate carboxylase like proteins, Rubisco-Form IV; Ribulose bisphosphate ...
 22-116 2.05e-16

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: 73.34  E-value: 2.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2510319192  22 STGTWTTVWTDGLTSLDRYKGRCYHIEPVP---GDENQYIAYVAYPLDLFEeGSVTNMFTSIVGNVFGfkaLRALRLEDL 98
Cdd:cd08205    26 TVGTWTELPGETEEIRERHVGRVESIEELEeseGKYGRARVTISYPLDNFG-GDLPQLLNTLFGNLSL---LPGIKLVDL 101

                          90
                  ....*....|....*...
gi 2510319192  99 RIPPAYVKTFQGPPHGIQ 116
Cdd:cd08205   102 ELPDSLLAAFPGPRFGIE 119
PRK13475 PRK13475
ribulose-bisphosphate carboxylase;
21-111 2.37e-11

ribulose-bisphosphate carboxylase;


Pssm-ID: 184072  Cd Length: 443  Bit Score: 59.35  E-value: 2.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2510319192  21 SSTGT-----WTTVWTDGLTSLdrykgrCYHIepvpgDENQYIAYVAYPLDLFE------EGSVTNMFTSIVGNVFGFKA 89
Cdd:PRK13475   49 SSTGTnvevsTTDDFTRGVDAL------VYEI-----DEARELMKIAYPVELFDrniidgRAMIVSFLTLTIGNNQGMGD 117

                          90       100
                  ....*....|....*....|..
gi 2510319192  90 LRALRLEDLRIPPAYVKTFQGP 111
Cdd:PRK13475  118 VEYAKMHDFYVPPRYLELFDGP 139
RuBisCO_large_II cd08211
Ribulose bisphosphate carboxylase large chain, Form II; Ribulose bisphosphate carboxylase ...
 21-115 9.03e-10

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: 54.81  E-value: 9.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2510319192  21 SSTGTWTTV-WTDGLT-SLDrykGRCYHIepvpgDENQYIAYVAYPLDLFE------EGSVTNMFTSIVGNVFGFKALRA 92
Cdd:cd08211    48 SSTGTNVEVsTTDDFTrGVD---ALVYEI-----DEARELMKIAYPVELFDrnltdgRAMVASFLTLIIGNNQGMGDVEY 119

                          90       100
                  ....*....|....*....|...
gi 2510319192  93 LRLEDLRIPPAYVKTFQGPPHGI 115
Cdd:cd08211   120 LKMHDFYVPESMLELFDGPSVNI 142
RLP_DK-MTP-1-P-enolase cd08209
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Ribulose bisphosphate carboxylase like ...
 24-116 6.02e-08

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: 49.63  E-value: 6.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2510319192  24 GTWTTVWTDGLTSLDRYKGRCYHIEPvpGDENQYIAYVAYPLdlfeeGSVTNMFTSIVGNVFGFKALR-ALRLEDLRIPP 102
Cdd:cd08209    27 GSWTDLPALRQAQLQKHLGEVVSVEE--LEEGRGVITIAYPL-----INVSGDIPALLTTIFGKLSLDgKIKLVDLRLPE 99

                          90
                  ....*....|....
gi 2510319192 103 AYVKTFQGPPHGIQ 116
Cdd:cd08209   100 EFGRAFPGPKFGIE 113
mtnW PRK09549
2,3-diketo-5-methylthiopentyl-1-phosphate enolase; Reviewed
 24-116 1.06e-05

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


Pssm-ID: 236560  Cd Length: 407  Bit Score: 43.07  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2510319192  24 GTWTTVWTDGLTSLDRYKGRCYHIEPVPGDEN----QYIAYVAYPldlfeEGSVTNMFTSIVGNVFGFKALRA-LRLEDL 98
Cdd:PRK09549   31 GSWTDLPHLEQEQLKKHKGNVVHVEELEEHERkgvkRGIIKIAYP-----LANFSPDLPAILTTTFGKLSLDGeVKLIDL 105

                          90
                  ....*....|....*...
gi 2510319192  99 RIPPAYVKTFQGPPHGIQ 116
Cdd:PRK09549  106 TFSDELKRHFPGPKFGID 123
RLP_RrRLP cd08210
Ribulose bisphosphate carboxylase like proteins (RLPs) similar to R.rubrum RLP; RLP from ...
 37-116 8.31e-04

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: 37.60  E-value: 8.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2510319192  37 LDRYKGRCYHIEPVpgDENQYIAYVAYPLDlfeegSVTNMFTSIVGNVFGFKAL-RALRLEDLRIPPAYVKTFQGPPHGI 115
Cdd:cd08210    42 RDNIVGRVESLEPA--GEGSYRARISYSVD-----TAGGELTQLLNVLFGNSSLqPGIRLVDFELPPSLLRRFPGPRFGI 114


                  .
gi 2510319192 116 Q 116
Cdd:cd08210   115 A 115
 
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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