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Conserved domains on  [gi|2743553897|ref|WP_349632895|]
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class II aldolase/adducin family protein [Listeria monocytogenes]

Protein Classification

class II aldolase/adducin head domain-containing protein( domain architecture ID 842)

class II aldolase/adducin head domain-containing protein involved in catalyzing central steps of carbohydrate metabolism; it promotes carbon-carbon bond cleavage and stabilizes enolate intermediates using divalent cations

Gene Symbol:  ADD3
PubMed:  10581174

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Aldolase_II super family cl00214
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 1-129 2.73e-78

Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes catalyzing central steps of carbohydrate metabolism. Based on enzymatic mechanisms, this superfamily has been divided into two distinct classes (Class I and II). Class II enzymes are further divided into two sub-classes A and B. This family includes class II A aldolases and adducins which has not been ascribed any enzymatic function. Members of this class are primarily bacterial and eukaryotic in origin and include L-fuculose-1-phosphate, L-rhamnulose-1-phosphate aldolases and L-ribulose-5-phosphate 4-epimerases. They all share the ability to promote carbon-carbon bond cleavage and stabilize enolate intermediates using divalent cations.


The actual alignment was detected with superfamily member PRK06357:

Pssm-ID: 469663 [Multi-domain]  Cd Length: 216  Bit Score: 230.82  E-value: 2.73e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743553897   1 MLYQKEREDLAKIVKTMFDRFETNAAGGNVSVRM----NSEHIIMTPTLMSQAKLCDLSPYEILVVD-NNNEVVEGDGRV 75
Cdd:PRK06357    1 MLFQKEREDLAKVVKTMFDRKETNAAGGNISVRMtaekNKEYIIMTPTLMSEAKLCDLSPYQILVVDlNTGEVIEGVGRV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2743553897  76 TREINLHRACYVENPKIGCVLHAHPKESMLFATLGMELPNLTEATQKLAKFQHL 129
Cdd:PRK06357   81 TREINMHEAAYVANPKIKCVYHSHAKESMFWATLGLEMPNLTEATQKLGKIPTL 134
 
Name Accession Description Interval E-value
PRK06357 PRK06357
hypothetical protein; Provisional
 1-129 2.73e-78

hypothetical protein; Provisional


Pssm-ID: 180541 [Multi-domain]  Cd Length: 216  Bit Score: 230.82  E-value: 2.73e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743553897   1 MLYQKEREDLAKIVKTMFDRFETNAAGGNVSVRM----NSEHIIMTPTLMSQAKLCDLSPYEILVVD-NNNEVVEGDGRV 75
Cdd:PRK06357    1 MLFQKEREDLAKVVKTMFDRKETNAAGGNISVRMtaekNKEYIIMTPTLMSEAKLCDLSPYQILVVDlNTGEVIEGVGRV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2743553897  76 TREINLHRACYVENPKIGCVLHAHPKESMLFATLGMELPNLTEATQKLAKFQHL 129
Cdd:PRK06357   81 TREINMHEAAYVANPKIKCVYHSHAKESMFWATLGLEMPNLTEATQKLGKIPTL 134
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 1-117 3.96e-32

5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) [Amino acid transport and metabolism, Carbohydrate transport and metabolism]; 5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440005 [Multi-domain]  Cd Length: 208  Bit Score: 113.00  E-value: 3.96e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743553897   1 MLYQKEREDLAKIVKTMFDRFETNAAGGNVSVRMNSEHIIMTPTLMSqakLCDLSPYEILVVDNNNEVVEGDGRVTREIN 80
Cdd:COG0235     1 MEEEELREELAAAGRRLARRGLVDGTAGNISVRLDDDRFLITPSGVD---FGELTPEDLVVVDLDGNVVEGDLKPSSETP 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2743553897  81 LHRACYVENPKIGCVLHAHPKESMLFATLGMELPNLT 117
Cdd:COG0235    78 LHLAIYRARPDVGAVVHTHSPYATALSALGEPLPPLE 114
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 8-118 1.87e-26

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 459862 [Multi-domain]  Cd Length: 178  Bit Score: 97.62  E-value: 1.87e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743553897   8 EDLAKIVKTMFDRFETNAAGGNVSVRMNSEHIIMTPTLMSqakLCDLSPYEILVVDNNNEVVEGDGRVTREINLHRACYV 87
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLPGDGFLITPSGVD---FGELTPEDLVVVDLDGNVVEGGLKPSSETPLHLAIYR 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2743553897  88 ENPKIGCVLHAHPKESMLFATLGMELPNLTE 118
Cdd:pfam00596  78 ARPDAGAVVHTHSPYATALSLAKEGLPPITQ 108
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 10-114 1.45e-19

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 214970 [Multi-domain]  Cd Length: 185  Bit Score: 79.99  E-value: 1.45e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743553897   10 LAKIVKTMFDRFETNAAGGNVSVRMNSE-HIIMTPTLMSQAklcDLSPYEILVVDNNNEVVEGDG--RVTREINLHRACY 86
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEdLFLITPSGVDFG---ELTASDLVVVDLDGNVVEGGGgpKPSSETPLHLAIY 77

                           90       100
                   ....*....|....*....|....*...
gi 2743553897   87 VENPKIGCVLHAHPKESMLFATLGMELP 114
Cdd:smart01007  78 RARPDVGAVVHTHSPYATALAALGKPLP 105
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 25-107 3.79e-11

methylthioribulose-1-phosphate dehydratase; Members of this family are the methylthioribulose-1-phosphate dehydratase of the methionine salvage pathway. This pathway allows methylthioadenosine, left over from polyamine biosynthesis, to be recycled to methionine. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 274521 [Multi-domain]  Cd Length: 192  Bit Score: 58.05  E-value: 3.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743553897  25 AAGGNVSVRMNSEHIIMTPTLMSQAKLcdlSPYEILVVDNNNEVVEGDGRVTREINLHRACYvENPKIGCVLHAHPKE-- 102
Cdd:TIGR03328  16 GTGGNLSARLDEDEILITPSGVDKGRL---TPEDFLVVDLQGKPVSGGLKPSAETLLHTQLY-RLTGAGAVLHTHSVEat 91


                  ....*..
gi 2743553897 103 --SMLFA 107
Cdd:TIGR03328  92 vlSRLYP 98
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 27-110 5.64e-09

Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes catalyzing central steps of carbohydrate metabolism. Based on enzymatic mechanisms, this superfamily has been divided into two distinct classes (Class I and II). Class II enzymes are further divided into two sub-classes A and B. This family includes class II A aldolases and adducins which has not been ascribed any enzymatic function. Members of this class are primarily bacterial and eukaryotic in origin and include L-fuculose-1-phosphate, L-rhamnulose-1-phosphate aldolases and L-ribulose-5-phosphate 4-epimerases. They all share the ability to promote carbon-carbon bond cleavage and stabilize enolate intermediates using divalent cations.


Pssm-ID: 238232 [Multi-domain]  Cd Length: 209  Bit Score: 52.37  E-value: 5.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743553897  27 GGNVSVRM-NSEHIIMTPTLMSQAKLcdlSPYEILVVDNNNEVVEGDgRVTREINLHRACYVENPKIGCVLHAHPKESML 105
Cdd:cd00398    24 GGNVSARDrDRGYFLITPSGVDYEEM---TASDLVVVDAQGKVVEGK-KPSSETPLHLALYRARPDIGCIVHTHSTHATA 99


                  ....*
gi 2743553897 106 FATLG 110
Cdd:cd00398   100 VSQLK 104
 
Name Accession Description Interval E-value
PRK06357 PRK06357
hypothetical protein; Provisional
 1-129 2.73e-78

hypothetical protein; Provisional


Pssm-ID: 180541 [Multi-domain]  Cd Length: 216  Bit Score: 230.82  E-value: 2.73e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743553897   1 MLYQKEREDLAKIVKTMFDRFETNAAGGNVSVRM----NSEHIIMTPTLMSQAKLCDLSPYEILVVD-NNNEVVEGDGRV 75
Cdd:PRK06357    1 MLFQKEREDLAKVVKTMFDRKETNAAGGNISVRMtaekNKEYIIMTPTLMSEAKLCDLSPYQILVVDlNTGEVIEGVGRV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2743553897  76 TREINLHRACYVENPKIGCVLHAHPKESMLFATLGMELPNLTEATQKLAKFQHL 129
Cdd:PRK06357   81 TREINMHEAAYVANPKIKCVYHSHAKESMFWATLGLEMPNLTEATQKLGKIPTL 134
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 1-117 3.96e-32

5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) [Amino acid transport and metabolism, Carbohydrate transport and metabolism]; 5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar degradation) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440005 [Multi-domain]  Cd Length: 208  Bit Score: 113.00  E-value: 3.96e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743553897   1 MLYQKEREDLAKIVKTMFDRFETNAAGGNVSVRMNSEHIIMTPTLMSqakLCDLSPYEILVVDNNNEVVEGDGRVTREIN 80
Cdd:COG0235     1 MEEEELREELAAAGRRLARRGLVDGTAGNISVRLDDDRFLITPSGVD---FGELTPEDLVVVDLDGNVVEGDLKPSSETP 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2743553897  81 LHRACYVENPKIGCVLHAHPKESMLFATLGMELPNLT 117
Cdd:COG0235    78 LHLAIYRARPDVGAVVHTHSPYATALSALGEPLPPLE 114
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 8-118 1.87e-26

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 459862 [Multi-domain]  Cd Length: 178  Bit Score: 97.62  E-value: 1.87e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743553897   8 EDLAKIVKTMFDRFETNAAGGNVSVRMNSEHIIMTPTLMSqakLCDLSPYEILVVDNNNEVVEGDGRVTREINLHRACYV 87
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLPGDGFLITPSGVD---FGELTPEDLVVVDLDGNVVEGGLKPSSETPLHLAIYR 77

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2743553897  88 ENPKIGCVLHAHPKESMLFATLGMELPNLTE 118
Cdd:pfam00596  78 ARPDAGAVVHTHSPYATALSLAKEGLPPITQ 108
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 10-114 1.45e-19

Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and adducins which have not been ascribed any enzymatic function.


Pssm-ID: 214970 [Multi-domain]  Cd Length: 185  Bit Score: 79.99  E-value: 1.45e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743553897   10 LAKIVKTMFDRFETNAAGGNVSVRMNSE-HIIMTPTLMSQAklcDLSPYEILVVDNNNEVVEGDG--RVTREINLHRACY 86
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEdLFLITPSGVDFG---ELTASDLVVVDLDGNVVEGGGgpKPSSETPLHLAIY 77

                           90       100
                   ....*....|....*....|....*...
gi 2743553897   87 VENPKIGCVLHAHPKESMLFATLGMELP 114
Cdd:smart01007  78 RARPDVGAVVHTHSPYATALAALGKPLP 105
PRK08130 PRK08130
putative aldolase; Validated
 4-99 2.84e-16

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 72.21  E-value: 2.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743553897   4 QKEREDLAKIVKTMFDRFETNAAGGNVSVRMNSEHIIMTPTlmsQAKLCDLSPYEILVVDNNNEVVEGDgRVTREINLHR 83
Cdd:PRK08130    4 QALREEIVRLGRSLFQRGYTVGSAGNISARLDDGGWLVTPT---GSCLGRLDPARLSKVDADGNWLSGD-KPSKEVPLHR 79

                          90
                  ....*....|....*.
gi 2743553897  84 ACYVENPKIGCVLHAH 99
Cdd:PRK08130   80 AIYRNNPECGAVVHLH 95
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
1-114 2.14e-15

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 69.78  E-value: 2.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743553897   1 MLYQKEREDLAKIVKTMFDRFETNAAGGNVSVrMNSEHIIM--TPTLMSQAKLcdlSPYEILVVDNNNEVVEGDGRVTRE 78
Cdd:PRK06833    1 MLLQKEREEIVAYGKKLISSGLTKGTGGNISI-FNREQGLMaiTPSGIDYFEI---KPEDIVIMDLDGKVVEGERKPSSE 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2743553897  79 INLHRACYVENPKIGCVLHAHPKESMLFATLGMELP 114
Cdd:PRK06833   77 LDMHLIFYRNREDINAIVHTHSPYATTLACLGWELP 112
PRK05874 PRK05874
L-fuculose-phosphate aldolase; Validated
 15-114 6.60e-12

L-fuculose-phosphate aldolase; Validated


Pssm-ID: 102036 [Multi-domain]  Cd Length: 217  Bit Score: 60.43  E-value: 6.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743553897  15 KTMFDRFETNAAGGNVSVRMNSEHIIMTPTLMSQAklcDLSPYEILVVDNNNEVVEG-DGRV-TREINLHRACYVENPKI 92
Cdd:PRK05874   16 KDMLRRGLVEGTAGNISARRSDGNVVITPSSVDYA---EMLLHDLVLVDAGGAVLHAkDGRSpSTELNLHLACYRAFDDI 92

                          90       100
                  ....*....|....*....|..
gi 2743553897  93 GCVLHAHPKESMLFATLGMELP 114
Cdd:PRK05874   93 GSVIHSHPVWATMFAVAHEPIP 114
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 25-107 3.79e-11

methylthioribulose-1-phosphate dehydratase; Members of this family are the methylthioribulose-1-phosphate dehydratase of the methionine salvage pathway. This pathway allows methylthioadenosine, left over from polyamine biosynthesis, to be recycled to methionine. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 274521 [Multi-domain]  Cd Length: 192  Bit Score: 58.05  E-value: 3.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743553897  25 AAGGNVSVRMNSEHIIMTPTLMSQAKLcdlSPYEILVVDNNNEVVEGDGRVTREINLHRACYvENPKIGCVLHAHPKE-- 102
Cdd:TIGR03328  16 GTGGNLSARLDEDEILITPSGVDKGRL---TPEDFLVVDLQGKPVSGGLKPSAETLLHTQLY-RLTGAGAVLHTHSVEat 91


                  ....*..
gi 2743553897 103 --SMLFA 107
Cdd:TIGR03328  92 vlSRLYP 98
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 27-110 5.64e-09

Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes catalyzing central steps of carbohydrate metabolism. Based on enzymatic mechanisms, this superfamily has been divided into two distinct classes (Class I and II). Class II enzymes are further divided into two sub-classes A and B. This family includes class II A aldolases and adducins which has not been ascribed any enzymatic function. Members of this class are primarily bacterial and eukaryotic in origin and include L-fuculose-1-phosphate, L-rhamnulose-1-phosphate aldolases and L-ribulose-5-phosphate 4-epimerases. They all share the ability to promote carbon-carbon bond cleavage and stabilize enolate intermediates using divalent cations.


Pssm-ID: 238232 [Multi-domain]  Cd Length: 209  Bit Score: 52.37  E-value: 5.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743553897  27 GGNVSVRM-NSEHIIMTPTLMSQAKLcdlSPYEILVVDNNNEVVEGDgRVTREINLHRACYVENPKIGCVLHAHPKESML 105
Cdd:cd00398    24 GGNVSARDrDRGYFLITPSGVDYEEM---TASDLVVVDAQGKVVEGK-KPSSETPLHLALYRARPDIGCIVHTHSTHATA 99


                  ....*
gi 2743553897 106 FATLG 110
Cdd:cd00398   100 VSQLK 104
PRK08333 PRK08333
aldolase;
10-125 7.55e-09

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 51.75  E-value: 7.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743553897  10 LAKIVKTMFDRFETNAAGGNVSVRMNSEHIIM-TPTLMSqaklcDLSPYEILVVDNNNEVVEgDGRVTREINLHRACYVE 88
Cdd:PRK08333    8 LVKYSKLAHERGLTAAFGGNLSIRVGNLVFIKaTGSVMD-----ELTREQVAVIDLNGNQLS-SVRPSSEYRLHLAVYRN 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2743553897  89 NPKIGCVLHAHPKESMLFAT-LGMELPNLT-EATQKLAK 125
Cdd:PRK08333   82 RPDVRAIAHLHPPYSIVASTlLEEELPIITpEAELYLKK 120
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 28-116 2.39e-06

L-ribulose-5-phosphate 4-epimerase; Reviewed


Pssm-ID: 183460  Cd Length: 228  Bit Score: 45.18  E-value: 2.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743553897  28 GNVS-VRMNSEHIIMTPtlmSQAKLCDLSPYEILVVDNNNEVVEGDGRVTREINLHRACYVENPKIGCVLHAHPKESMLF 106
Cdd:PRK12348   26 GNVSaIDRERGLVVIKP---SGVAYETMKADDMVVVDMSGKVVEGEYRPSSDTATHLELYRRYPSLGGIVHTHSTHATAW 102

                          90
                  ....*....|
gi 2743553897 107 ATLGMELPNL 116
Cdd:PRK12348  103 AQAGLAIPAL 112
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
53-116 3.68e-06

L-ribulose-5-phosphate 4-epimerase AraD;


Pssm-ID: 236181  Cd Length: 231  Bit Score: 44.83  E-value: 3.68e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2743553897  53 DLSPYEILVVDNNNEVVEGDGRVTREINLHRACYVENPKIGCVLHAHPKESMLFATLGMELPNL 116
Cdd:PRK08193   50 KMTAEDMVVVDLEGNVVEGKLKPSSDTPTHLVLYKAFPEIGGIVHTHSRHATAWAQAGRDIPAL 113
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 3-114 4.17e-06

L-ribulose-5-phosphate 4-epimerase; Validated


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 44.61  E-value: 4.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743553897   3 YQKEREDLAKIvKTMFDRFETNA-AGGNVSVRM-NSEHIIMTPTLMSQAklcDLSPYEILVVDNNNEVVEGDGRVTREIN 80
Cdd:PRK06557    8 VEKLREEVCKL-HLELPKYGLVVwTSGNVSARDpGTDLVVIKPSGVSYD---DLTPEDMVVVDLDGNVVEGDLKPSSDTA 83

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2743553897  81 LHRACYVENPKIGCVLHAHPKESMLFATLGMELP 114
Cdd:PRK06557   84 SHLYVYRHMPDVGGVVHTHSTYATAWAARGEPIP 117
araD PRK13145
L-ribulose-5-phosphate 4-epimerase; Provisional
 28-114 6.61e-06

L-ribulose-5-phosphate 4-epimerase; Provisional


Pssm-ID: 183870 [Multi-domain]  Cd Length: 234  Bit Score: 44.05  E-value: 6.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743553897  28 GNVS-VRMNSEHIIMTPTLMSQAKLcdlSPYEILVVDNNNEVVEGDGRVTREINLHRACYVENPKIGCVLHAHPKESMLF 106
Cdd:PRK13145   28 GNVSeVCRELGRIVIKPSGVDYDEL---TPENMVVTDLDGNVVEGDLNPSSDLPTHVELYKAWPEVGGIVHTHSTEAVGW 104


                  ....*...
gi 2743553897 107 ATLGMELP 114
Cdd:PRK13145  105 AQAGRDIP 112
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
25-99 1.73e-05

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 42.62  E-value: 1.73e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2743553897  25 AAGGNVSVRMNSEHIIMTptlmsqAKLCD---LSPYEILVVDNNNEVVEGDGRVTREINLHRACYVENPKIGCVLHAH 99
Cdd:PRK09220   25 ATSGNMSVRLDEQHCAIT------VSGKDkgsLTAEDFLQVDIAGNAVPSGRKPSAETLLHTQLYRLFPEIGAVLHTH 96
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
6-114 3.97e-04

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 38.95  E-value: 3.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743553897   6 EREDLA-KIVKTMFdrfETNAAG------GNVSVRMNSEHIImTPTLMSQAKLcdlSPYEILVVDNNNEVVEGDgRVTRE 78
Cdd:PRK08087    2 ERNKLArQIIDTCL---EMTRLGlnqgtaGNVSVRYQDGMLI-TPTGIPYEKL---TESHIVFVDGNGKHEEGK-LPSSE 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2743553897  79 INLHRACYVENPKIGCVLHAHPKESMLFATLGMELP 114
Cdd:PRK08087   74 WRFHMAAYQTRPDANAVVHNHAVHCTAVSILNRPIP 109
sgbE PRK12347
L-ribulose-5-phosphate 4-epimerase; Reviewed
 57-114 4.85e-04

L-ribulose-5-phosphate 4-epimerase; Reviewed


Pssm-ID: 183459  Cd Length: 231  Bit Score: 38.65  E-value: 4.85e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2743553897  57 YEILVVDN-------NNEVVEGDGRVTREINLHRACYVENPKIGCVLHAHPKESMLFATLGMELP 114
Cdd:PRK12347   48 YDVMTADDmvvveiaSGKVVEGSKKPSSDTPTHLALYRRYPEIGGIVHTHSRHATIWSQAGLDLP 112
araD PRK13213
L-ribulose-5-phosphate 4-epimerase; Reviewed
 28-116 2.92e-03

L-ribulose-5-phosphate 4-epimerase; Reviewed


Pssm-ID: 106181  Cd Length: 231  Bit Score: 36.63  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743553897  28 GNVSvRMNSEH--IIMTPtlmSQAKLCDLSPYEILVVD-NNNEVVEGDGRVTREINLHRACYVENPKIGCVLHAHPKESM 104
Cdd:PRK13213   27 GNVS-GIDREHglVVIKP---SGVEYDVMSVNDMVVVDlATGKVVEGDKKPSSDTDTHLVLYRAFAEIGGIVHTHSRHAT 102

                          90
                  ....*....|..
gi 2743553897 105 LFATLGMELPNL 116
Cdd:PRK13213  103 IWAQAGKSLSAL 114
PRK06486 PRK06486
aldolase;
59-127 3.11e-03

aldolase;


Pssm-ID: 235814  Cd Length: 262  Bit Score: 36.61  E-value: 3.11e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2743553897  59 ILVVDNNNEVVEGDGRV-TREINLHRACYVENPKIGCVLHAHpkesMLFAT-LGM-ELPNLTEATQKLAKFQ 127
Cdd:PRK06486   79 LLICDFDGNVLAGRGEPeATAFFIHARIHRAIPRAKAAFHTH----MPYATaLSLtEGRPLTTLGQTALKFY 146
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
1-99 7.77e-03

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 35.03  E-value: 7.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2743553897   1 MLYQKEREDLAKIVKTMFDRFETNAAGGNVSVRMNSEHIIMTPTLMSQAKLcDLSPYEILVVDNNNEVVEG-DGRVTREI 79
Cdd:PRK06754    2 KQLQRRWNELAEIKKELAARDWFPATSGNLSIKVSDDPLTFLVTASGKDKR-KTTPEDFLLVDHDGKPVEEtELKPSAET 80

                          90       100
                  ....*....|....*....|
gi 2743553897  80 NLHRACYvENPKIGCVLHAH 99
Cdd:PRK06754   81 LLHTHIY-NNTNAGCVLHVH 99
 
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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