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Conserved domains on  [gi|294958178|sp|A3LVM9|]
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RecName: Full=Methylthioribulose-1-phosphate dehydratase; Short=MTRu-1-P dehydratase

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 ...
 36-257 3.74e-73

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 TIGR03328:

Pssm-ID: 469663 [Multi-domain]  Cd Length: 192  Bit Score: 221.76  E-value: 3.74e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178   36 ICELCRLFYDNNWVTGTGGGISIRdvdgANPNLVYIAPSGVQKERIQPWEMFLVELpEEKILRTPNdipkeltksykyKP 115
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSAR----LDEDEILITPSGVDKGRLTPEDFLVVDL-QGKPVSGGL------------KP 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178  116 SACTPLFMSCYTMRDAGACIHTHSQHAVMVTLFLEGKKEFEISHIEQIKALPklalnentgkiekiGSMEYYDKLVIPII 195
Cdd:TIGR03328  64 SAETLLHTQLYRLTGAGAVLHTHSVEATVLSRLYPSNGGFELEGYEMLKGLP--------------GITTHEDTLVVPII 129

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 294958178  196 ENTPHEEDLTDSLQEAIKNYPGTSAVLVRRHGIYVWGETVWKAKVYNEAIDYLLELAVKMQQ 257
Cdd:TIGR03328 130 ENTQDIARLADSVAPALNAYPDVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLK 191
 
Name Accession Description Interval E-value
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 36-257 3.74e-73

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: 221.76  E-value: 3.74e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178   36 ICELCRLFYDNNWVTGTGGGISIRdvdgANPNLVYIAPSGVQKERIQPWEMFLVELpEEKILRTPNdipkeltksykyKP 115
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSAR----LDEDEILITPSGVDKGRLTPEDFLVVDL-QGKPVSGGL------------KP 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178  116 SACTPLFMSCYTMRDAGACIHTHSQHAVMVTLFLEGKKEFEISHIEQIKALPklalnentgkiekiGSMEYYDKLVIPII 195
Cdd:TIGR03328  64 SAETLLHTQLYRLTGAGAVLHTHSVEATVLSRLYPSNGGFELEGYEMLKGLP--------------GITTHEDTLVVPII 129

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 294958178  196 ENTPHEEDLTDSLQEAIKNYPGTSAVLVRRHGIYVWGETVWKAKVYNEAIDYLLELAVKMQQ 257
Cdd:TIGR03328 130 ENTQDIARLADSVAPALNAYPDVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLK 191
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 36-253 1.05e-48

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: 159.34  E-value: 1.05e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178    36 ICELCRLFYDNNWVTGTGGGISIRDVDganPNLVYIAPSGVQKERIQPWEMFLVELPEEKILRTPNDipkeltksykyKP 115
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGE---EDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGGP-----------KP 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178   116 SACTPLFMSCYTMR-DAGACIHTHSQHAVMVTLFlegKKEFEISHIEQIKALpklalnentgkiekIGSMEYYDKLVIPI 194
Cdd:smart01007  67 SSETPLHLAIYRARpDVGAVVHTHSPYATALAAL---GKPLPLLPTEQAAAF--------------LGGEIPYAPYAGPG 129

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 294958178   195 IENTPHEEDLTDSLQEAIKNYPgtsAVLVRRHGIYVWGETVWKAKVYNEAIDYLLELAV 253
Cdd:smart01007 130 TELAEEGAELAEALAEALPDRP---AVLLRNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 34-253 1.43e-47

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: 156.17  E-value: 1.43e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178   34 NLICELCRLFYDNNWVTGTGGGISIRDvdgaNPNLVYIAPSGVQKERIQPWEMFLVELpEEKILRTPndipkeltksykY 113
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL----PGDGFLITPSGVDFGELTPEDLVVVDL-DGNVVEGG------------L 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178  114 KPSACTPLFMSCYTMR-DAGACIHTHSQHAVMVTLFLEGkkefeishieqikaLPklALNENtgkiekiGSMEYYDKlvI 192
Cdd:pfam00596  64 KPSSETPLHLAIYRARpDAGAVVHTHSPYATALSLAKEG--------------LP--PITQE-------AADFLGGD--I 118

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 294958178  193 PIIEN-TPHEEDLTDSLQEAIKNypGTSAVLVRRHGIYVWGETVWKAKVYNEAIDYLLELAV 253
Cdd:pfam00596 119 PIIPYyTPGTEELGERIAEALGG--DRKAVLLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 30-261 2.90e-38

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: 133.26  E-value: 2.90e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178  30 NHPANLICELCRLFYDNNWVTGTGGGISIRDVDganPNLVYIAPSGVQKERIQPWEMFLVELPEEKILrtpndipkeltk 109
Cdd:cd00398    1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRD---RGYFLITPSGVDYEEMTASDLVVVDAQGKVVE------------ 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178 110 syKYKPSACTPLFMSCYTMR-DAGACIHTHSQHAVMVTLFLEGkkefeishieQIKALPKLALNENTGKiekigsmeyyd 188
Cdd:cd00398   66 --GKKPSSETPLHLALYRARpDIGCIVHTHSTHATAVSQLKEG----------LIPAGHTACAVYFTGD----------- 122

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 294958178 189 klvIPIIENT---PHEEDLTDSLQEAIknyPGTSAVLVRRHGIYVWGETVWKAKVYNEAIDYLLELAVKMQQSGIP 261
Cdd:cd00398  123 ---IPCTPYMtpeTGEDEIGTQRALGF---PNSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQ 192
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 36-261 1.87e-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: 118.01  E-value: 1.87e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178  36 ICELCRLFYDNNWVTGTGGGISIRDvdgaNPNLVYIAPSGVQKERIQPWEMFLVELpEEKILRTPndipkeltksykYKP 115
Cdd:COG0235   10 LAAAGRRLARRGLVDGTAGNISVRL----DDDRFLITPSGVDFGELTPEDLVVVDL-DGNVVEGD------------LKP 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178 116 SACTPLFMSCYTMR-DAGACIHTHSQHAVMVTLFLEgkkefEISHIEQIKAlpklalnentgkiekigsMEYYDKlvIPI 194
Cdd:COG0235   73 SSETPLHLAIYRARpDVGAVVHTHSPYATALSALGE-----PLPPLEQTEA------------------AAFLGD--VPV 127

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 294958178 195 IE-NTPHEEDLTDSLQEAIKNYPgtsAVLVRRHGIYVWGETVWKAKVYNEAIDYLLELAVKMQQSGIP 261
Cdd:COG0235  128 VPyAGPGTEELAEAIAEALGDRP---AVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGP 192
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
38-257 1.13e-23

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 95.12  E-value: 1.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178  38 ELCRLFYDNNWVTGTGGGISIRDVDgaNPNLVYIAPSGVQKERIQPWEMFLVELPEEKILRTpndipkeltksyKYKPSA 117
Cdd:PRK06754  13 EIKKELAARDWFPATSGNLSIKVSD--DPLTFLVTASGKDKRKTTPEDFLLVDHDGKPVEET------------ELKPSA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178 118 CTPLFMSCYTMRDAGACIHTHSQHAVMVTLFLEGKKEFEISHIEQIKALpklALNENTGKIEkigsmeyydklvIPIIEN 197
Cdd:PRK06754  79 ETLLHTHIYNNTNAGCVLHVHTVDNNVISELYGDDGAVTFQGQEIIKAL---GIWEENAEIH------------IPIIEN 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178 198 TPHEEDLTDSLQEAIKnyPGTSAVLVRRHGIYVWGETVWKAKVYNEAIDYLLELAVKMQQ 257
Cdd:PRK06754 144 HADIPTLAEEFAKHIQ--GDSGAVLIRNHGITVWGRDAFEAKKHLEAYEFLFSYHIKLLS 201
 
Name Accession Description Interval E-value
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 36-257 3.74e-73

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: 221.76  E-value: 3.74e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178   36 ICELCRLFYDNNWVTGTGGGISIRdvdgANPNLVYIAPSGVQKERIQPWEMFLVELpEEKILRTPNdipkeltksykyKP 115
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSAR----LDEDEILITPSGVDKGRLTPEDFLVVDL-QGKPVSGGL------------KP 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178  116 SACTPLFMSCYTMRDAGACIHTHSQHAVMVTLFLEGKKEFEISHIEQIKALPklalnentgkiekiGSMEYYDKLVIPII 195
Cdd:TIGR03328  64 SAETLLHTQLYRLTGAGAVLHTHSVEATVLSRLYPSNGGFELEGYEMLKGLP--------------GITTHEDTLVVPII 129

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 294958178  196 ENTPHEEDLTDSLQEAIKNYPGTSAVLVRRHGIYVWGETVWKAKVYNEAIDYLLELAVKMQQ 257
Cdd:TIGR03328 130 ENTQDIARLADSVAPALNAYPDVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLK 191
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 36-253 1.05e-48

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: 159.34  E-value: 1.05e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178    36 ICELCRLFYDNNWVTGTGGGISIRDVDganPNLVYIAPSGVQKERIQPWEMFLVELPEEKILRTPNDipkeltksykyKP 115
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGE---EDLFLITPSGVDFGELTASDLVVVDLDGNVVEGGGGP-----------KP 66

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178   116 SACTPLFMSCYTMR-DAGACIHTHSQHAVMVTLFlegKKEFEISHIEQIKALpklalnentgkiekIGSMEYYDKLVIPI 194
Cdd:smart01007  67 SSETPLHLAIYRARpDVGAVVHTHSPYATALAAL---GKPLPLLPTEQAAAF--------------LGGEIPYAPYAGPG 129

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 294958178   195 IENTPHEEDLTDSLQEAIKNYPgtsAVLVRRHGIYVWGETVWKAKVYNEAIDYLLELAV 253
Cdd:smart01007 130 TELAEEGAELAEALAEALPDRP---AVLLRNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 34-253 1.43e-47

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: 156.17  E-value: 1.43e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178   34 NLICELCRLFYDNNWVTGTGGGISIRDvdgaNPNLVYIAPSGVQKERIQPWEMFLVELpEEKILRTPndipkeltksykY 113
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRL----PGDGFLITPSGVDFGELTPEDLVVVDL-DGNVVEGG------------L 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178  114 KPSACTPLFMSCYTMR-DAGACIHTHSQHAVMVTLFLEGkkefeishieqikaLPklALNENtgkiekiGSMEYYDKlvI 192
Cdd:pfam00596  64 KPSSETPLHLAIYRARpDAGAVVHTHSPYATALSLAKEG--------------LP--PITQE-------AADFLGGD--I 118

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 294958178  193 PIIEN-TPHEEDLTDSLQEAIKNypGTSAVLVRRHGIYVWGETVWKAKVYNEAIDYLLELAV 253
Cdd:pfam00596 119 PIIPYyTPGTEELGERIAEALGG--DRKAVLLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 30-261 2.90e-38

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: 133.26  E-value: 2.90e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178  30 NHPANLICELCRLFYDNNWVTGTGGGISIRDVDganPNLVYIAPSGVQKERIQPWEMFLVELPEEKILrtpndipkeltk 109
Cdd:cd00398    1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRD---RGYFLITPSGVDYEEMTASDLVVVDAQGKVVE------------ 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178 110 syKYKPSACTPLFMSCYTMR-DAGACIHTHSQHAVMVTLFLEGkkefeishieQIKALPKLALNENTGKiekigsmeyyd 188
Cdd:cd00398   66 --GKKPSSETPLHLALYRARpDIGCIVHTHSTHATAVSQLKEG----------LIPAGHTACAVYFTGD----------- 122

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 294958178 189 klvIPIIENT---PHEEDLTDSLQEAIknyPGTSAVLVRRHGIYVWGETVWKAKVYNEAIDYLLELAVKMQQSGIP 261
Cdd:cd00398  123 ---IPCTPYMtpeTGEDEIGTQRALGF---PNSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQ 192
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 36-261 1.87e-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: 118.01  E-value: 1.87e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178  36 ICELCRLFYDNNWVTGTGGGISIRDvdgaNPNLVYIAPSGVQKERIQPWEMFLVELpEEKILRTPndipkeltksykYKP 115
Cdd:COG0235   10 LAAAGRRLARRGLVDGTAGNISVRL----DDDRFLITPSGVDFGELTPEDLVVVDL-DGNVVEGD------------LKP 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178 116 SACTPLFMSCYTMR-DAGACIHTHSQHAVMVTLFLEgkkefEISHIEQIKAlpklalnentgkiekigsMEYYDKlvIPI 194
Cdd:COG0235   73 SSETPLHLAIYRARpDVGAVVHTHSPYATALSALGE-----PLPPLEQTEA------------------AAFLGD--VPV 127

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 294958178 195 IE-NTPHEEDLTDSLQEAIKNYPgtsAVLVRRHGIYVWGETVWKAKVYNEAIDYLLELAVKMQQSGIP 261
Cdd:COG0235  128 VPyAGPGTEELAEAIAEALGDRP---AVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALGGP 192
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
38-257 1.13e-23

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 95.12  E-value: 1.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178  38 ELCRLFYDNNWVTGTGGGISIRDVDgaNPNLVYIAPSGVQKERIQPWEMFLVELPEEKILRTpndipkeltksyKYKPSA 117
Cdd:PRK06754  13 EIKKELAARDWFPATSGNLSIKVSD--DPLTFLVTASGKDKRKTTPEDFLLVDHDGKPVEET------------ELKPSA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178 118 CTPLFMSCYTMRDAGACIHTHSQHAVMVTLFLEGKKEFEISHIEQIKALpklALNENTGKIEkigsmeyydklvIPIIEN 197
Cdd:PRK06754  79 ETLLHTHIYNNTNAGCVLHVHTVDNNVISELYGDDGAVTFQGQEIIKAL---GIWEENAEIH------------IPIIEN 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178 198 TPHEEDLTDSLQEAIKnyPGTSAVLVRRHGIYVWGETVWKAKVYNEAIDYLLELAVKMQQ 257
Cdd:PRK06754 144 HADIPTLAEEFAKHIQ--GDSGAVLIRNHGITVWGRDAFEAKKHLEAYEFLFSYHIKLLS 201
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
33-257 7.25e-15

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 71.12  E-value: 7.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178  33 ANLICELCRLFYDNNWVTGTGGGISIRDVDGanpnLVYIAPSGVQKERIQPWEMFLVELpEEKILRTPNdipkeltksyk 112
Cdd:PRK09220   7 LQQLIAAGRWIGARGWVPATSGNMSVRLDEQ----HCAITVSGKDKGSLTAEDFLQVDI-AGNAVPSGR----------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178 113 yKPSACTPLFMSCYTMR-DAGACIHTHSQHAVMVTLfLEGKKEFEISHIEQIKALPklalnentgkiekiGSMEYYDKLV 191
Cdd:PRK09220  71 -KPSAETLLHTQLYRLFpEIGAVLHTHSVNATVLSR-VEKSDALVLEGYELQKAFA--------------GQTTHETAVV 134

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 294958178 192 IPIIENTPHEEDLTDSLQEAIKNYPGTSAVLVRRHGIYVWGETVWKAKVYNEAIDYLLELAVKMQQ 257
Cdd:PRK09220 135 VPIFDNDQDIARLAARVAPYLDAQPLRYGYLIRGHGLYCWGRDMAEARRHLEGLEFLFECELERRL 200
PRK06755 PRK06755
hypothetical protein; Validated
 176-255 5.36e-09

hypothetical protein; Validated


Pssm-ID: 102532  Cd Length: 209  Bit Score: 55.04  E-value: 5.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178 176 GKIEKIGSMEYYDKLVIPIIENtphEEDLTDSLQEAIKNYP-GTSAVLVRRHGIYVWGETVWKAKVYNEAIDYLLELAVK 254
Cdd:PRK06755 121 RSVERVFGKEGITEMTIPIVED---EKKFADLLENNVPNFIeGGGVVLVHNYGMIVWGKTPEEAKKWLEGIEYLMNYHVK 197


                 .
gi 294958178 255 M 255
Cdd:PRK06755 198 L 198
PRK08660 PRK08660
aldolase;
41-254 4.46e-07

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 48.80  E-value: 4.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178  41 RLFyDNNWVTGTGGGISIRDVDGanpnlVYIAPSGVQkeriqpwemfLVELPEEKILRTPNDIPKELTKsykyKPSACTP 120
Cdd:PRK08660  11 KLF-AHGLVSSHFGNISVRTGDG-----LLITRTGSM----------LDEITEGDVIEVGIDDDGSVDP----LASSETP 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178 121 LFMSCYTMRDAGACIHTHSQHAVMVTLfLEGKkefeishIEQIKALPKLALNEntgkiekigsmeyydklvIPIIENTPH 200
Cdd:PRK08660  71 VHRAIYRRTSAKAIVHAHPPYAVALSL-LEDE-------IVPLDSEGLYFLGT------------------IPVVGGDIG 124

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178 201 EEDLTDSLQEAIKNYPGtsaVLVRRHGIYVWGETVWKAKVYNEAID------YLLELAVK 254
Cdd:PRK08660 125 SGELAENVARALSEHKG---VVVRGHGTFAIGKTLEEAYIYTSQLEhsckvlYLVRTAKK 181
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 49-255 2.57e-06

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


Pssm-ID: 183460  Cd Length: 228  Bit Score: 47.10  E-value: 2.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178  49 VTGTGGGISIRDVDGAnpnLVYIAPSGVQKERIQPWEMFLVELpEEKILRTpndipkeltksyKYKPSACTPLFMSCY-T 127
Cdd:PRK12348  21 VTFTWGNVSAIDRERG---LVVIKPSGVAYETMKADDMVVVDM-SGKVVEG------------EYRPSSDTATHLELYrR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178 128 MRDAGACIHTHSQHAvmvTLFLEGKKE---FEISH-------IEQIKALPKLALNE----NTGKIekigsmeyydklvip 193
Cdd:PRK12348  85 YPSLGGIVHTHSTHA---TAWAQAGLAipaLGTTHadyffgdIPCTRGLSEEEVQGeyelNTGKV--------------- 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 294958178 194 IIENTPHEEDLTdslqeaiknypgTSAVLVRRHGIYVWGETVWKAkVYNEAIdylLELAVKM 255
Cdd:PRK12348 147 IIETLGNAEPLH------------TPGIVVYQHGPFAWGKDAHDA-VHNAVV---MEEVAKM 192
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 35-142 3.27e-06

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


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 46.92  E-value: 3.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178  35 LICELCRLFYDNNWVTGTGGGISIRDVDGanpNLVYIAPSGVQKERIQPWEMFLVELPEEKIlrtpndipkeltkSYKYK 114
Cdd:PRK06557  14 EVCKLHLELPKYGLVVWTSGNVSARDPGT---DLVVIKPSGVSYDDLTPEDMVVVDLDGNVV-------------EGDLK 77

                         90       100
                 ....*....|....*....|....*....
gi 294958178 115 PSACTPLFMSCYT-MRDAGACIHTHSQHA 142
Cdd:PRK06557  78 PSSDTASHLYVYRhMPDVGGVVHTHSTYA 106
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
33-255 9.81e-06

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


Pssm-ID: 236181  Cd Length: 231  Bit Score: 45.60  E-value: 9.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178  33 ANLicELCRLfydnNWVTGTGGGISIRDVDganPNLVYIAPSGVQKERIQPWEMFLVELpEEKILRTpndipkeltksyK 112
Cdd:PRK08193  12 ANL--ALPKH----GLVTFTWGNVSAIDRE---RGLFVIKPSGVDYDKMTAEDMVVVDL-EGNVVEG------------K 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 294958178 113 YKPSACTPLFMSCY-TMRDAGACIHTHSQHAvmvTLFLEGKKE---FEISHIE----QIKALPKLALNE-------NTGK 177
Cdd:PRK08193  70 LKPSSDTPTHLVLYkAFPEIGGIVHTHSRHA---TAWAQAGRDipaLGTTHADyfygDIPCTRKMTDEEingeyewETGK 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 294958178 178 IekigsmeyydklvipIIEnTPHEEDLtdslqeaikNYPGTSAVLVRRHGIYVWGETVWKAkVYNEAIdylLELAVKM 255
Cdd:PRK08193 147 V---------------IVE-TFEKRGI---------DPAAVPGVLVHSHGPFTWGKDAEDA-VHNAVV---LEEVAKM 195
 
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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