NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|74966673|sp|Q23261|]
View 

RecName: Full=Probable 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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
33-232 1.12e-84

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: 251.03  E-value: 1.12e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673    33 FTELMIQFYKLGWMRGSGGAMGC-ISGSELMISPSALQKERIREQDVFVYNMkDKTEVQrpPNKRItvSSCSVLFSLIMK 111
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSArLDEDEILITPSGVDKGRLTPEDFLVVDL-QGKPVS--GGLKP--SAETLLHTQLYR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673   112 ETGSECVIHTHSKCANLITQLIKSN-VFEISHQEYIKGIYDpfsgkALKYSDTLTIPIIDNMPSESQLLEPIRGVLENYP 190
Cdd:TIGR03328  76 LTGAGAVLHTHSVEATVLSRLYPSNgGFELEGYEMLKGLPG-----ITTHEDTLVVPIIENTQDIARLADSVAPALNAYP 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 74966673   191 QAIAVLVRNHGLFVWGPTWESTKIMTECIDYLLELSIEMLKN 232
Cdd:TIGR03328 151 DVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLKL 192
 
Name Accession Description Interval E-value
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
33-232 1.12e-84

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: 251.03  E-value: 1.12e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673    33 FTELMIQFYKLGWMRGSGGAMGC-ISGSELMISPSALQKERIREQDVFVYNMkDKTEVQrpPNKRItvSSCSVLFSLIMK 111
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSArLDEDEILITPSGVDKGRLTPEDFLVVDL-QGKPVS--GGLKP--SAETLLHTQLYR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673   112 ETGSECVIHTHSKCANLITQLIKSN-VFEISHQEYIKGIYDpfsgkALKYSDTLTIPIIDNMPSESQLLEPIRGVLENYP 190
Cdd:TIGR03328  76 LTGAGAVLHTHSVEATVLSRLYPSNgGFELEGYEMLKGLPG-----ITTHEDTLVVPIIENTQDIARLADSVAPALNAYP 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 74966673   191 QAIAVLVRNHGLFVWGPTWESTKIMTECIDYLLELSIEMLKN 232
Cdd:TIGR03328 151 DVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLKL 192
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
35-227 9.96e-29

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: 107.25  E-value: 9.96e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673    35 ELMIQFYKLGWMRGSGGAMGCISGSELM-ISPSALQKERIREQDVFVYNMkDKTEVQRPPNkritVSSCSVLFSLIMKE- 112
Cdd:pfam00596   5 AAGRLLARRGLVEGTGGNISVRLPGDGFlITPSGVDFGELTPEDLVVVDL-DGNVVEGGLK----PSSETPLHLAIYRAr 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673   113 TGSECVIHTHSKCANLITQLIKsnVFEISHQEYIKGIYDpfsgkalkysdtlTIPIIDNMPSESQLL-EPIRGVLENypQ 191
Cdd:pfam00596  80 PDAGAVVHTHSPYATALSLAKE--GLPPITQEAADFLGG-------------DIPIIPYYTPGTEELgERIAEALGG--D 142
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 74966673   192 AIAVLVRNHGLFVWGPTWESTKIMTECIDYLLELSI 227
Cdd:pfam00596 143 RKAVLLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
40-227 3.41e-27

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: 103.49  E-value: 3.41e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673     40 FYKLGWMRGSGGAMGCISGSE--LMISPSALQKERIREQDVFVYNMkDKTEVQRPPNKRitVSSCSVLFSLIMKET-GSE 116
Cdd:smart01007   8 LARRGLVEGTGGNISARVGEEdlFLITPSGVDFGELTASDLVVVDL-DGNVVEGGGGPK--PSSETPLHLAIYRARpDVG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673    117 CVIHTHSKCANLITQLIKSnvFEISHQEYIKGIYdpfsGKALKYsDTLTIPIIDNMPSESQLLEPIRGVLENYPqaiAVL 196
Cdd:smart01007  85 AVVHTHSPYATALAALGKP--LPLLPTEQAAAFL----GGEIPY-APYAGPGTELAEEGAELAEALAEALPDRP---AVL 154
                          170       180       190
                   ....*....|....*....|....*....|.
gi 74966673    197 VRNHGLFVWGPTWESTKIMTECIDYLLELSI 227
Cdd:smart01007 155 LRNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
39-245 3.45e-15

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: 72.01  E-value: 3.45e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673  39 QFYKLGWMRGSGGAMGCI--SGSELMISPSALQKERIREQDVFVYNMKDKTEVQRPPnkritvSSCSVLFSLIMKETGS- 115
Cdd:cd00398  13 LLDLYGWVTGTGGNVSARdrDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVEGKKP------SSETPLHLALYRARPDi 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673 116 ECVIHTHSKCANLITQLIKSNVfeishqeyikgiydPFSGKALKYSDTLTIPIIDNMPSESQLLEPIRGVLENYPQAIAV 195
Cdd:cd00398  87 GCIVHTHSTHATAVSQLKEGLI--------------PAGHTACAVYFTGDIPCTPYMTPETGEDEIGTQRALGFPNSKAV 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 74966673 196 LVRNHGLFVWGPTWESTKIMTECIDYLLELSIEMLKNN--IPLVNEEAFEKE 245
Cdd:cd00398 153 LLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGgqLPPISLELLNKE 204
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
40-244 1.64e-13

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: 67.55  E-value: 1.64e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673  40 FYKLGWMRGSGGAM-GCISGSELMISPSALQKERIREQDVFVYNMKDKT-EVQRPPnkritvSSCSVLFSLIMKE-TGSE 116
Cdd:COG0235  17 LARRGLVDGTAGNIsVRLDDDRFLITPSGVDFGELTPEDLVVVDLDGNVvEGDLKP------SSETPLHLAIYRArPDVG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673 117 CVIHTHSKCANLITQLIKsnvfEISHQEYIKGIYdpFSGKalkysdtltIPIIDNMPSESQ-LLEPIRGVLENYPqaiAV 195
Cdd:COG0235  91 AVVHTHSPYATALSALGE----PLPPLEQTEAAA--FLGD---------VPVVPYAGPGTEeLAEAIAEALGDRP---AV 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 74966673 196 LVRNHGLFVWGPTWESTKIMTECIDYLLELSIEMLK-NNIPLVNEEAFEK 244
Cdd:COG0235 153 LLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALAlGGPLVLSDEEIDK 202
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
100-230 6.86e-13

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 65.84  E-value: 6.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673  100 SSCSVLFSLIMKETGSECVIHTHSKCANLITQLI-KSNVFEISHQEYIK--GIYdpfsgkalKYSDTLTIPIIDNMPSES 176
Cdd:PRK06754  77 SAETLLHTHIYNNTNAGCVLHVHTVDNNVISELYgDDGAVTFQGQEIIKalGIW--------EENAEIHIPIIENHADIP 148
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 74966673  177 QLLEPIRGVLEnyPQAIAVLVRNHGLFVWGPTWESTKIMTECIDYLLELSIEML 230
Cdd:PRK06754 149 TLAEEFAKHIQ--GDSGAVLIRNHGITVWGRDAFEAKKHLEAYEFLFSYHIKLL 200
 
Name Accession Description Interval E-value
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
33-232 1.12e-84

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: 251.03  E-value: 1.12e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673    33 FTELMIQFYKLGWMRGSGGAMGC-ISGSELMISPSALQKERIREQDVFVYNMkDKTEVQrpPNKRItvSSCSVLFSLIMK 111
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSArLDEDEILITPSGVDKGRLTPEDFLVVDL-QGKPVS--GGLKP--SAETLLHTQLYR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673   112 ETGSECVIHTHSKCANLITQLIKSN-VFEISHQEYIKGIYDpfsgkALKYSDTLTIPIIDNMPSESQLLEPIRGVLENYP 190
Cdd:TIGR03328  76 LTGAGAVLHTHSVEATVLSRLYPSNgGFELEGYEMLKGLPG-----ITTHEDTLVVPIIENTQDIARLADSVAPALNAYP 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 74966673   191 QAIAVLVRNHGLFVWGPTWESTKIMTECIDYLLELSIEMLKN 232
Cdd:TIGR03328 151 DVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLKL 192
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
35-227 9.96e-29

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: 107.25  E-value: 9.96e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673    35 ELMIQFYKLGWMRGSGGAMGCISGSELM-ISPSALQKERIREQDVFVYNMkDKTEVQRPPNkritVSSCSVLFSLIMKE- 112
Cdd:pfam00596   5 AAGRLLARRGLVEGTGGNISVRLPGDGFlITPSGVDFGELTPEDLVVVDL-DGNVVEGGLK----PSSETPLHLAIYRAr 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673   113 TGSECVIHTHSKCANLITQLIKsnVFEISHQEYIKGIYDpfsgkalkysdtlTIPIIDNMPSESQLL-EPIRGVLENypQ 191
Cdd:pfam00596  80 PDAGAVVHTHSPYATALSLAKE--GLPPITQEAADFLGG-------------DIPIIPYYTPGTEELgERIAEALGG--D 142
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 74966673   192 AIAVLVRNHGLFVWGPTWESTKIMTECIDYLLELSI 227
Cdd:pfam00596 143 RKAVLLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
40-227 3.41e-27

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: 103.49  E-value: 3.41e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673     40 FYKLGWMRGSGGAMGCISGSE--LMISPSALQKERIREQDVFVYNMkDKTEVQRPPNKRitVSSCSVLFSLIMKET-GSE 116
Cdd:smart01007   8 LARRGLVEGTGGNISARVGEEdlFLITPSGVDFGELTASDLVVVDL-DGNVVEGGGGPK--PSSETPLHLAIYRARpDVG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673    117 CVIHTHSKCANLITQLIKSnvFEISHQEYIKGIYdpfsGKALKYsDTLTIPIIDNMPSESQLLEPIRGVLENYPqaiAVL 196
Cdd:smart01007  85 AVVHTHSPYATALAALGKP--LPLLPTEQAAAFL----GGEIPY-APYAGPGTELAEEGAELAEALAEALPDRP---AVL 154
                          170       180       190
                   ....*....|....*....|....*....|.
gi 74966673    197 VRNHGLFVWGPTWESTKIMTECIDYLLELSI 227
Cdd:smart01007 155 LRNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
39-245 3.45e-15

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: 72.01  E-value: 3.45e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673  39 QFYKLGWMRGSGGAMGCI--SGSELMISPSALQKERIREQDVFVYNMKDKTEVQRPPnkritvSSCSVLFSLIMKETGS- 115
Cdd:cd00398  13 LLDLYGWVTGTGGNVSARdrDRGYFLITPSGVDYEEMTASDLVVVDAQGKVVEGKKP------SSETPLHLALYRARPDi 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673 116 ECVIHTHSKCANLITQLIKSNVfeishqeyikgiydPFSGKALKYSDTLTIPIIDNMPSESQLLEPIRGVLENYPQAIAV 195
Cdd:cd00398  87 GCIVHTHSTHATAVSQLKEGLI--------------PAGHTACAVYFTGDIPCTPYMTPETGEDEIGTQRALGFPNSKAV 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 74966673 196 LVRNHGLFVWGPTWESTKIMTECIDYLLELSIEMLKNN--IPLVNEEAFEKE 245
Cdd:cd00398 153 LLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGgqLPPISLELLNKE 204
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
40-244 1.64e-13

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: 67.55  E-value: 1.64e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673  40 FYKLGWMRGSGGAM-GCISGSELMISPSALQKERIREQDVFVYNMKDKT-EVQRPPnkritvSSCSVLFSLIMKE-TGSE 116
Cdd:COG0235  17 LARRGLVDGTAGNIsVRLDDDRFLITPSGVDFGELTPEDLVVVDLDGNVvEGDLKP------SSETPLHLAIYRArPDVG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673 117 CVIHTHSKCANLITQLIKsnvfEISHQEYIKGIYdpFSGKalkysdtltIPIIDNMPSESQ-LLEPIRGVLENYPqaiAV 195
Cdd:COG0235  91 AVVHTHSPYATALSALGE----PLPPLEQTEAAA--FLGD---------VPVVPYAGPGTEeLAEAIAEALGDRP---AV 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 74966673 196 LVRNHGLFVWGPTWESTKIMTECIDYLLELSIEMLK-NNIPLVNEEAFEK 244
Cdd:COG0235 153 LLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALAlGGPLVLSDEEIDK 202
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
100-230 6.86e-13

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 65.84  E-value: 6.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673  100 SSCSVLFSLIMKETGSECVIHTHSKCANLITQLI-KSNVFEISHQEYIK--GIYdpfsgkalKYSDTLTIPIIDNMPSES 176
Cdd:PRK06754  77 SAETLLHTHIYNNTNAGCVLHVHTVDNNVISELYgDDGAVTFQGQEIIKalGIW--------EENAEIHIPIIENHADIP 148
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 74966673  177 QLLEPIRGVLEnyPQAIAVLVRNHGLFVWGPTWESTKIMTECIDYLLELSIEML 230
Cdd:PRK06754 149 TLAEEFAKHIQ--GDSGAVLIRNHGITVWGRDAFEAKKHLEAYEFLFSYHIKLL 200
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
44-231 1.09e-09

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 56.48  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673   44 GWMRGSGGAMGC-ISGSELMISPSALQKERIREQDVFVYNMkDKTEVqRPPNKRitvSSCSVLFSLIMK---ETGseCVI 119
Cdd:PRK09220  21 GWVPATSGNMSVrLDEQHCAITVSGKDKGSLTAEDFLQVDI-AGNAV-PSGRKP---SAETLLHTQLYRlfpEIG--AVL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673  120 HTHSKCANLITQLIKSNVFEISHQEYIKGiydpFSGKAlKYSDTLTIPIIDN---MPSESQLLEPIrgvLENYPQAIAVL 196
Cdd:PRK09220  94 HTHSVNATVLSRVEKSDALVLEGYELQKA----FAGQT-THETAVVVPIFDNdqdIARLAARVAPY---LDAQPLRYGYL 165
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 74966673  197 VRNHGLFVWGPTWESTKIMTECIDYLLELSIEMLK 231
Cdd:PRK09220 166 IRGHGLYCWGRDMAEARRHLEGLEFLFECELERRL 200
PRK06755 PRK06755
hypothetical protein; Validated
103-230 1.98e-07

hypothetical protein; Validated


Pssm-ID: 102532  Cd Length: 209  Bit Score: 50.42  E-value: 1.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74966673  103 SVLFSLIMKETGSECVIHTHSKCANLITQLIKsnvfEISHQEYIKGIYDPFSGKalKYSDTLTIPIIDNMPSESQLLEpi 182
Cdd:PRK06755  80 SFMHADIYKKSSAECILQVQTVDSHLISELYG----EEGEVTFDKRSVERVFGK--EGITEMTIPIVEDEKKFADLLE-- 151
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 74966673  183 rgvlENYPQ----AIAVLVRNHGLFVWGPTWESTKIMTECIDYLLELSIEML 230
Cdd:PRK06755 152 ----NNVPNfiegGGVVLVHNYGMIVWGKTPEEAKKWLEGIEYLMNYHVKLL 199
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH