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Conserved domains on  [gi|639237392|ref|WP_024568069|]
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ribulose-phosphate 3-epimerase [Elizabethkingia anophelis]

Protein Classification

ribulose-phosphate 3-epimerase( domain architecture ID 10784968)

ribulose-phosphate 3-epimerase catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate

CATH:  3.20.20.70
Gene Ontology:  GO:0006098|GO:0016857|GO:0004750|GO:0046872|GO:0005975
PubMed:  12206759|11257493
SCOP:  4003059

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 5-216 3.46e-136

Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; Pentose-5-phosphate-3-epimerase is part of the Pathway/BioSystem: Pentose phosphate pathway


:

Pssm-ID: 439806  Cd Length: 218  Bit Score: 380.19  E-value: 3.46e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392   5 LIAPSVLSADFGNLQRDIEMINNSEADWFHVDVMDGRFVPNISFGFPVMKAIKKHAKKFIDVHLMIVEPEKYVEEFVKEG 84
Cdd:COG0036    2 KIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392  85 ADLVTVHYEACTHLHRVIHQIKDLGAKAGVVLNPATPVSVLEDIITDIDLVLLMSVNPGFGGQKFIENTYKKIHQTKALI 164
Cdd:COG0036   82 ADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRELI 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 639237392 165 EKYNSNALIEIDGGVNQHNAAKLFEAGADVLVAGNAVFSAEDPAAMIEELKK 216
Cdd:COG0036  162 DERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALRE 213
 
Name Accession Description Interval E-value
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 5-216 3.46e-136

Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; Pentose-5-phosphate-3-epimerase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 439806  Cd Length: 218  Bit Score: 380.19  E-value: 3.46e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392   5 LIAPSVLSADFGNLQRDIEMINNSEADWFHVDVMDGRFVPNISFGFPVMKAIKKHAKKFIDVHLMIVEPEKYVEEFVKEG 84
Cdd:COG0036    2 KIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392  85 ADLVTVHYEACTHLHRVIHQIKDLGAKAGVVLNPATPVSVLEDIITDIDLVLLMSVNPGFGGQKFIENTYKKIHQTKALI 164
Cdd:COG0036   82 ADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRELI 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 639237392 165 EKYNSNALIEIDGGVNQHNAAKLFEAGADVLVAGNAVFSAEDPAAMIEELKK 216
Cdd:COG0036  162 DERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALRE 213
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
 1-216 8.44e-122

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 344.09  E-value: 8.44e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392   1 MKNKLIAPSVLSADFGNLQRDIEMINNSEADWFHVDVMDGRFVPNISFGFPVMKAIKKHAKKFIDVHLMIVEPEKYVEEF 80
Cdd:PRK05581   1 MKMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392  81 VKEGADLVTVHYEACTHLHRVIHQIKDLGAKAGVVLNPATPVSVLEDIITDIDLVLLMSVNPGFGGQKFIENTYKKIHQT 160
Cdd:PRK05581  81 AKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIREL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 639237392 161 KALIEKYNSNALIEIDGGVNQHNAAKLFEAGADVLVAGNAVFSAEDPAAMIEELKK 216
Cdd:PRK05581 161 RKLIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRA 216
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 5-215 9.82e-121

Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate, as part of the Calvin cycle (reductive pentose phosphate pathway) in chloroplasts and in the oxidative pentose phosphate pathway. In the Calvin cycle Ru5P is phosphorylated by phosphoribulose kinase to ribulose-1,5-bisphosphate, which in turn is used by RubisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) to incorporate CO2 as the central step in carbohydrate synthesis.


Pssm-ID: 238244  Cd Length: 211  Bit Score: 341.00  E-value: 9.82e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392   5 LIAPSVLSADFGNLQRDIEMINNSEADWFHVDVMDGRFVPNISFGFPVMKAIKKHAKKFIDVHLMIVEPEKYVEEFVKEG 84
Cdd:cd00429    1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392  85 ADLVTVHYEACTHLHRVIHQIKDLGAKAGVVLNPATPVSVLEDIITDIDLVLLMSVNPGFGGQKFIENTYKKIHQTKALI 164
Cdd:cd00429   81 ADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 639237392 165 EKYNSNALIEIDGGVNQHNAAKLFEAGADVLVAGNAVFSAEDPAAMIEELK 215
Cdd:cd00429  161 PENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 6-215 5.77e-107

ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also known as pentose-5-phosphate 3-epimerase (PPE). PPE converts D-ribulose 5-phosphate into D-xylulose 5-phosphate in Calvin's reductive pentose phosphate cycle. It has been found in a wide range of bacteria, archebacteria, fungi and plants. [Energy metabolism, Pentose phosphate pathway]


Pssm-ID: 273475  Cd Length: 210  Bit Score: 306.12  E-value: 5.77e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392    6 IAPSVLSADFGNLQRDIEMINNSEADWFHVDVMDGRFVPNISFGFPVMKAIKKHAKKFIDVHLMIVEPEKYVEEFVKEGA 85
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392   86 DLVTVHYEACTHLHRVIHQIKDLGAKAGVVLNPATPVSVLEDIITDIDLVLLMSVNPGFGGQKFIENTYKKIHQTKALIE 165
Cdd:TIGR01163  81 DIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMID 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 639237392  166 KYNSNALIEIDGGVNQHNAAKLFEAGADVLVAGNAVFSAEDPAAMIEELK 215
Cdd:TIGR01163 161 ELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 6-202 2.22e-92

Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose 5-phosphate into D-xylulose 5-phosphate.


Pssm-ID: 395672  Cd Length: 198  Bit Score: 268.82  E-value: 2.22e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392    6 IAPSVLSADFGNLQRDIEMINNSEADWFHVDVMDGRFVPNISFGFPVMKAIKKHAKKFIDVHLMIVEPEKYVEEFVKEGA 85
Cdd:pfam00834   2 IAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392   86 DLVTVHYEACTHLHRVIHQIKDLGAKAGVVLNPATPVSVLEDIITDIDLVLLMSVNPGFGGQKFIENTYKKIHQTKALIE 165
Cdd:pfam00834  82 DIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMID 161

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 639237392  166 KYNSNALIEIDGGVNQHNAAKLFEAGADVLVAGNAVF 202
Cdd:pfam00834 162 ERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
 
Name Accession Description Interval E-value
Rpe COG0036
Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; ...
 5-216 3.46e-136

Pentose-5-phosphate-3-epimerase [Carbohydrate transport and metabolism]; Pentose-5-phosphate-3-epimerase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 439806  Cd Length: 218  Bit Score: 380.19  E-value: 3.46e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392   5 LIAPSVLSADFGNLQRDIEMINNSEADWFHVDVMDGRFVPNISFGFPVMKAIKKHAKKFIDVHLMIVEPEKYVEEFVKEG 84
Cdd:COG0036    2 KIAPSILSADFANLGEEVKRVEAAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMIENPDRYIEAFAEAG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392  85 ADLVTVHYEACTHLHRVIHQIKDLGAKAGVVLNPATPVSVLEDIITDIDLVLLMSVNPGFGGQKFIENTYKKIHQTKALI 164
Cdd:COG0036   82 ADIITVHAEATPHLHRTLQLIKELGAKAGVALNPATPLEALEYVLDDVDLVLVMSVNPGFGGQKFIPSVLEKIRRLRELI 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 639237392 165 EKYNSNALIEIDGGVNQHNAAKLFEAGADVLVAGNAVFSAEDPAAMIEELKK 216
Cdd:COG0036  162 DERGLDILIEVDGGINAETIPELAEAGADVLVAGSAVFGAEDYAAAIAALRE 213
PRK05581 PRK05581
ribulose-phosphate 3-epimerase; Validated
 1-216 8.44e-122

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 235515  Cd Length: 220  Bit Score: 344.09  E-value: 8.44e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392   1 MKNKLIAPSVLSADFGNLQRDIEMINNSEADWFHVDVMDGRFVPNISFGFPVMKAIKKHAKKFIDVHLMIVEPEKYVEEF 80
Cdd:PRK05581   1 MKMVLIAPSILSADFARLGEEVKAVEAAGADWIHVDVMDGHFVPNLTIGPPVVEAIRKVTKLPLDVHLMVENPDRYVPDF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392  81 VKEGADLVTVHYEACTHLHRVIHQIKDLGAKAGVVLNPATPVSVLEDIITDIDLVLLMSVNPGFGGQKFIENTYKKIHQT 160
Cdd:PRK05581  81 AKAGADIITFHVEASEHIHRLLQLIKSAGIKAGLVLNPATPLEPLEDVLDLLDLVLLMSVNPGFGGQKFIPEVLEKIREL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 639237392 161 KALIEKYNSNALIEIDGGVNQHNAAKLFEAGADVLVAGNAVFSAEDPAAMIEELKK 216
Cdd:PRK05581 161 RKLIDERGLDILIEVDGGINADNIKECAEAGADVFVAGSAVFGAPDYKEAIDSLRA 216
RPE cd00429
Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of ...
 5-215 9.82e-121

Ribulose-5-phosphate 3-epimerase (RPE). This enzyme catalyses the interconversion of D-ribulose 5-phosphate (Ru5P) into D-xylulose 5-phosphate, as part of the Calvin cycle (reductive pentose phosphate pathway) in chloroplasts and in the oxidative pentose phosphate pathway. In the Calvin cycle Ru5P is phosphorylated by phosphoribulose kinase to ribulose-1,5-bisphosphate, which in turn is used by RubisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) to incorporate CO2 as the central step in carbohydrate synthesis.


Pssm-ID: 238244  Cd Length: 211  Bit Score: 341.00  E-value: 9.82e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392   5 LIAPSVLSADFGNLQRDIEMINNSEADWFHVDVMDGRFVPNISFGFPVMKAIKKHAKKFIDVHLMIVEPEKYVEEFVKEG 84
Cdd:cd00429    1 KIAPSILSADFANLGEELKRLEEAGADWIHIDVMDGHFVPNLTFGPPVVKALRKHTDLPLDVHLMVENPERYIEAFAKAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392  85 ADLVTVHYEACTHLHRVIHQIKDLGAKAGVVLNPATPVSVLEDIITDIDLVLLMSVNPGFGGQKFIENTYKKIHQTKALI 164
Cdd:cd00429   81 ADIITFHAEATDHLHRTIQLIKELGMKAGVALNPGTPVEVLEPYLDEVDLVLVMSVNPGFGGQKFIPEVLEKIRKLRELI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 639237392 165 EKYNSNALIEIDGGVNQHNAAKLFEAGADVLVAGNAVFSAEDPAAMIEELK 215
Cdd:cd00429  161 PENNLNLLIEVDGGINLETIPLLAEAGADVLVAGSALFGSDDYAEAIKELR 211
rpe TIGR01163
ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also ...
 6-215 5.77e-107

ribulose-phosphate 3-epimerase; This family consists of Ribulose-phosphate 3-epimerase, also known as pentose-5-phosphate 3-epimerase (PPE). PPE converts D-ribulose 5-phosphate into D-xylulose 5-phosphate in Calvin's reductive pentose phosphate cycle. It has been found in a wide range of bacteria, archebacteria, fungi and plants. [Energy metabolism, Pentose phosphate pathway]


Pssm-ID: 273475  Cd Length: 210  Bit Score: 306.12  E-value: 5.77e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392    6 IAPSVLSADFGNLQRDIEMINNSEADWFHVDVMDGRFVPNISFGFPVMKAIKKHAKKFIDVHLMIVEPEKYVEEFVKEGA 85
Cdd:TIGR01163   1 IAPSILSADFARLGEEVKAVEEAGADWIHVDVMDGHFVPNLTFGPPVLEALRKYTDLPIDVHLMVENPDRYIEDFAEAGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392   86 DLVTVHYEACTHLHRVIHQIKDLGAKAGVVLNPATPVSVLEDIITDIDLVLLMSVNPGFGGQKFIENTYKKIHQTKALIE 165
Cdd:TIGR01163  81 DIITVHPEASEHIHRLLQLIKDLGAKAGIVLNPATPLEFLEYVLPDVDLVLLMSVNPGFGGQKFIPDTLEKIREVRKMID 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 639237392  166 KYNSNALIEIDGGVNQHNAAKLFEAGADVLVAGNAVFSAEDPAAMIEELK 215
Cdd:TIGR01163 161 ELGLSILIEVDGGVNDDNARELAEAGADILVAGSAIFGADDYKEVIRSLR 210
PLN02334 PLN02334
ribulose-phosphate 3-epimerase
 1-216 9.11e-94

ribulose-phosphate 3-epimerase


Pssm-ID: 215192  Cd Length: 229  Bit Score: 273.42  E-value: 9.11e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392   1 MKNKLIAPSVLSADFGNLQRDIEMINNSEADWFHVDVMDGRFVPNISFGFPVMKAIKKHAKKFIDVHLMIVEPEKYVEEF 80
Cdd:PLN02334   5 KNDAIIAPSILSADFANLAEEAKRVLDAGADWLHVDVMDGHFVPNLTIGPPVVKALRKHTDAPLDCHLMVTNPEDYVPDF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392  81 VKEGADLVTVHYEACT--HLHRVIHQIKDLGAKAGVVLNPATPVSVLEDII--TDIDLVLLMSVNPGFGGQKFIENTYKK 156
Cdd:PLN02334  85 AKAGASIFTFHIEQAStiHLHRLIQQIKSAGMKAGVVLNPGTPVEAVEPVVekGLVDMVLVMSVEPGFGGQSFIPSMMDK 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392 157 IhqtKALIEKYNSnALIEIDGGVNQHNAAKLFEAGADVLVAGNAVFSAEDPAAMIEELKK 216
Cdd:PLN02334 165 V---RALRKKYPE-LDIEVDGGVGPSTIDKAAEAGANVIVAGSAVFGAPDYAEVISGLRA 220
Ribul_P_3_epim pfam00834
Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose ...
 6-202 2.22e-92

Ribulose-phosphate 3 epimerase family; This enzyme catalyzes the conversion of D-ribulose 5-phosphate into D-xylulose 5-phosphate.


Pssm-ID: 395672  Cd Length: 198  Bit Score: 268.82  E-value: 2.22e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392    6 IAPSVLSADFGNLQRDIEMINNSEADWFHVDVMDGRFVPNISFGFPVMKAIKKHAKKFIDVHLMIVEPEKYVEEFVKEGA 85
Cdd:pfam00834   2 IAPSILSADFARLGEEIKAVENAGADWLHVDVMDGHFVPNLTIGPLVVEALRPLTDLPLDVHLMVEEPDRIIPDFAKAGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392   86 DLVTVHYEACTHLHRVIHQIKDLGAKAGVVLNPATPVSVLEDIITDIDLVLLMSVNPGFGGQKFIENTYKKIHQTKALIE 165
Cdd:pfam00834  82 DIISFHAEATPHPHRTIQLIKEAGAKAGLVLNPATPLDAIEYLLDKLDLVLLMSVNPGFGGQSFIPSVLEKIRKVRKMID 161

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 639237392  166 KYNSNALIEIDGGVNQHNAAKLFEAGADVLVAGNAVF 202
Cdd:pfam00834 162 ERGLDTLIEVDGGIKLDNIPQIAEAGADVIVAGSAVF 198
PTZ00170 PTZ00170
D-ribulose-5-phosphate 3-epimerase; Provisional
 5-216 7.92e-76

D-ribulose-5-phosphate 3-epimerase; Provisional


Pssm-ID: 240303  Cd Length: 228  Bit Score: 227.95  E-value: 7.92e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392   5 LIAPSVLSADFGNLQRDIEMINNSEADWFHVDVMDGRFVPNISFGFPVMKAIKKHAKK-FIDVHLMIVEPEKYVEEFVKE 83
Cdd:PTZ00170   8 IIAPSILAADFSKLADEAQDVLSGGADWLHVDVMDGHFVPNLSFGPPVVKSLRKHLPNtFLDCHLMVSNPEKWVDDFAKA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392  84 GADLVTVHYEACT-HLHRVIHQIKDLGAKAGVVLNPATPVSVLEDIITD--IDLVLLMSVNPGFGGQKFIENTYKKIHQt 160
Cdd:PTZ00170  88 GASQFTFHIEATEdDPKAVARKIREAGMKVGVAIKPKTPVEVLFPLIDTdlVDMVLVMTVEPGFGGQSFMHDMMPKVRE- 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 639237392 161 kaLIEKYnSNALIEIDGGVNQHNAAKLFEAGADVLVAGNAVFSAEDPAAMIEELKK 216
Cdd:PTZ00170 167 --LRKRY-PHLNIQVDGGINLETIDIAADAGANVIVAGSSIFKAKDRKQAIELLRE 219
PRK09722 PRK09722
allulose-6-phosphate 3-epimerase; Provisional
 2-207 2.39e-64

allulose-6-phosphate 3-epimerase; Provisional


Pssm-ID: 236616  Cd Length: 229  Bit Score: 198.68  E-value: 2.39e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392   2 KNKLIAPSVLSADFGNLQRDIEMINnSEADWFHVDVMDGRFVPNISFGFPVMKAIKKHAKKFIDVHLMIVEPEKYVEEFV 81
Cdd:PRK09722   1 MRMKISPSLMCMDLLKFKEQIEFLN-SKADYFHIDIMDGHFVPNLTLSPFFVSQVKKLASKPLDVHLMVTDPQDYIDQLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392  82 KEGADLVTVHYE-ACTHLHRVIHQIKDLGAKAGVVLNPATPVSVLEDIITDIDLVLLMSVNPGFGGQKFIENTYKKIHQT 160
Cdd:PRK09722  80 DAGADFITLHPEtINGQAFRLIDEIRRAGMKVGLVLNPETPVESIKYYIHLLDKITVMTVDPGFAGQPFIPEMLDKIAEL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 639237392 161 KALIEKYNSNALIEIDGGVNQHNAAKLFEAGADVLVAGNA-VFSAEDP 207
Cdd:PRK09722 160 KALRERNGLEYLIEVDGSCNQKTYEKLMEAGADVFIVGTSgLFNLDED 207
PRK08005 PRK08005
ribulose-phosphate 3 epimerase family protein;
5-206 7.47e-31

ribulose-phosphate 3 epimerase family protein;


Pssm-ID: 169179  Cd Length: 210  Bit Score: 112.44  E-value: 7.47e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392   5 LIAPSVLSADFGNLQRDIEMINNSEADWFHVDVMDGRFVPNISFGFPVMKAIKKHAKKFIDVHLMIVEPEKYVEEFVKEG 84
Cdd:PRK08005   2 ILHPSLASADPLRYAEALTALHDAPLGSLHLDIEDTSFINNITFGMKTIQAVAQQTRHPLSFHLMVSSPQRWLPWLAAIR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392  85 ADLVTVHYEACTHLHRVIHQIKDLGAKAGVVLNPATPVSVLEDIITDIDLVLLMSVNPGFGGQKFIENTYKKIHQTKALI 164
Cdd:PRK08005  82 PGWIFIHAESVQNPSEILADIRAIGAKAGLALNPATPLLPYRYLALQLDALMIMTSEPDGRGQQFIAAMCEKVSQSREHF 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 639237392 165 EKYNSNAlieiDGGVNQHNAAKLFEAGADVLVAGNAVFSAED 206
Cdd:PRK08005 162 PAAECWA----DGGITLRAARLLAAAGAQHLVIGRALFTTAN 199
PRK14057 PRK14057
epimerase; Provisional
 10-202 2.69e-24

epimerase; Provisional


Pssm-ID: 172549  Cd Length: 254  Bit Score: 96.29  E-value: 2.69e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392  10 VLSADFGNLQRDIEMINNSEADWFHVDVMDGRFVPNISFGfpvMKAIKKHAKKFI-DVHLMIVEPEKYVEEFVKEGADLV 88
Cdd:PRK14057  26 ILAGQWIALHRYLQQLEALNQPLLHLDLMDGQFCPQFTVG---PWAVGQLPQTFIkDVHLMVADQWTAAQACVKAGAHCI 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392  89 TVHYEACTHLHrviHQIKDLGAKA------------GVVLNPATPVSVLEDIITDIDLVLLMSVNPGFGGQKFIENTYKK 156
Cdd:PRK14057 103 TLQAEGDIHLH---HTLSWLGQQTvpviggempvirGISLCPATPLDVIIPILSDVEVIQLLAVNPGYGSKMRSSDLHER 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 639237392 157 IHQTKALIEKYNSNALIEIDGGVNQHNAAKLFEAGADVLVAGNAVF 202
Cdd:PRK14057 180 VAQLLCLLGDKREGKIIVIDGSLTQDQLPSLIAQGIDRVVSGSALF 225
PRK08091 PRK08091
ribulose-phosphate 3-epimerase; Validated
 1-216 1.98e-23

ribulose-phosphate 3-epimerase; Validated


Pssm-ID: 169215  Cd Length: 228  Bit Score: 93.40  E-value: 1.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392   1 MKNKLIAPSVLSADFGNLQRDIEMINNSEADWFHVDVMDGRFVPNISFGFPVMKAIKKHAKKfiDVHLMIVEPEKYVEEF 80
Cdd:PRK08091  10 LKQQPISVGILASNWLKFNETLTTLSENQLRLLHFDIADGQFSPFFTVGAIAIKQFPTHCFK--DVHLMVRDQFEVAKAC 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392  81 VKEGADLVTVHYEACTHLHRVIHQIKDLGAKA--GVVLNPATPVSVLEDIITDIDLVLLMSVNPGFGGQKFIENTYKKIH 158
Cdd:PRK08091  88 VAAGADIVTLQVEQTHDLALTIEWLAKQKTTVliGLCLCPETPISLLEPYLDQIDLIQILTLDPRTGTKAPSDLILDRVI 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 639237392 159 QTKALIEKYNSNALIEIDGGVNQHNAAKLFEAGADVLVAGNAVFSAEDPAAMIEELKK 216
Cdd:PRK08091 168 QVENRLGNRRVEKLISIDGSMTLELASYLKQHQIDWVVSGSALFSQGELKTTLKEWKS 225
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
 177-216 7.05e-06

Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.


Pssm-ID: 238317 [Multi-domain]  Cd Length: 196  Bit Score: 44.82  E-value: 7.05e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 639237392 177 GGVNQHNAAKLFEAGADVLVAGNAVFSAEDPAAMIEELKK 216
Cdd:cd00564  157 GGITPENAAEVLAAGADGVAVISAITGADDPAAAARELLA 196
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
 177-216 1.02e-05

Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440121 [Multi-domain]  Cd Length: 206  Bit Score: 44.79  E-value: 1.02e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 639237392 177 GGVNQHNAAKLFEAGADVLVAGNAVFSAEDPAAMIEELKK 216
Cdd:COG0352  162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRA 201
thiE PRK00043
thiamine phosphate synthase;
177-216 3.21e-05

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 43.25  E-value: 3.21e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 639237392 177 GGVNQHNAAKLFEAGADVLVAGNAVFSAEDPAAMIEELKK 216
Cdd:PRK00043 167 GGITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLA 206
PRK13307 PRK13307
bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;
116-213 1.19e-04

bifunctional 5,6,7,8-tetrahydromethanopterin hydro-lyase/3-hexulose-6-phosphate synthase;


Pssm-ID: 183964 [Multi-domain]  Cd Length: 391  Bit Score: 42.31  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392 116 LNPATPVSVLEDIITDIDLVLL-MSVNpgfggqkfIENTYKKIHQTKAlIEKYNSNALIEIDGGVNQHNAAKLFEAGADV 194
Cdd:PRK13307 284 LNVEDPVKLLESLKVKPDVVELhRGID--------EEGTEHAWGNIKE-IKKAGGKILVAVAGGVRVENVEEALKAGADI 354

                         90
                 ....*....|....*....
gi 639237392 195 LVAGNAVFSAEDPAAMIEE 213
Cdd:PRK13307 355 LVVGRAITKSKDVRRAAED 373
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 28-198 2.10e-04

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 40.65  E-value: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392  28 SEADWFHVDVMDGRFVPNISFGFPVMKAIKKHAKKFIDVHLMIVEPEKYVEEFVK----EGADLVTVHyEACTHLHRVIH 103
Cdd:cd04722   24 AGADAIIVGTRSSDPEEAETDDKEVLKEVAAETDLPLGVQLAINDAAAAVDIAAAaaraAGADGVEIH-GAVGYLAREDL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392 104 QIKDLGAKAG-----VVLNPATPVSVLEDIITD-IDLVLLMSVNPGFGGQKFIENTYKKIHQTKALIEKYnsnalIEIDG 177
Cdd:cd04722  103 ELIRELREAVpdvkvVVKLSPTGELAAAAAEEAgVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSKVP-----VIAGG 177

                        170       180
                 ....*....|....*....|..
gi 639237392 178 GVNQH-NAAKLFEAGADVLVAG 198
Cdd:cd04722  178 GINDPeDAAEALALGADGVIVG 199
KGPDC_HPS cd04726
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ...
 166-214 2.78e-03

3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate synthase (HPS). KGPDC catalyzes the formation of L-xylulose 5-phosphate and carbon dioxide from 3-keto-L-gulonate 6-phosphate as part of the anaerobic pathway for L-ascorbate utilization in some eubacteria. HPS catalyzes the formation of D-arabino-3-hexulose-6-phosphate from D-ribulose 5-phosphate and formaldehyde in microorganisms that can use formaldehyde as a carbon source. Both catalyze reactions that involve the Mg2+-assisted formation and stabilization of 1,2-enediolate reaction intermediates.


Pssm-ID: 240077 [Multi-domain]  Cd Length: 202  Bit Score: 37.56  E-value: 2.78e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 639237392 166 KYNSNALIEIDGGVNQHNAAKLFEAGADVLVAGNAVFSAEDPAAMIEEL 214
Cdd:cd04726  154 KKLLGVKVAVAGGITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
PcrB pfam01884
PcrB family; This family contains proteins that are related to PcrB. The function of these ...
 87-216 8.06e-03

PcrB family; This family contains proteins that are related to PcrB. The function of these proteins is unknown.


Pssm-ID: 396454  Cd Length: 226  Bit Score: 36.35  E-value: 8.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639237392   87 LVTVHYEACTHLHRVIHQIKDLgAKAGVVLNPATPVSVLEDIITDIDLVLLMS---VNPGFGGQKFI----ENTYKKIHQ 159
Cdd:pfam01884  92 IVGMHYLGAQTFTEIIESEEIQ-PEGYLVLNPDSKVAAVTEALCPINKPDIAAyalVGAKLFGLPIFyleySGAYGNVEE 170

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 639237392  160 TKALIEKYNSNALIeIDGGVNQHNAAKLFEAGADVLVAGNAVFsaEDPAAMIEELKK 216
Cdd:pfam01884 171 VIALKKVLDKARLF-YGGGIRSREKAREMARAADVIVVGNVVY--EKGERAIDAILE 224
 
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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