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Conserved domains on  [gi|1951406446|ref|XP_038557442|]
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methylthioribulose-1-phosphate dehydratase [Micropterus salmoides]

Protein Classification

methylthioribulose-1-phosphate dehydratase( domain architecture ID 10022368)

methylthioribulose-1-phosphate dehydratase catalyzes the formation of diketo methylthiopentyl phosphate from methylribulose phosphate in the methionine salvage pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 30-228 3.81e-92

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: 269.14  E-value: 3.81e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446  30 IPELCRLFYQLGWVTGTGGGISLKRGEQ-IYIAPSGVQKERIQPEDMFVCDLEERDIScppawKKLKKSQCTPLFMNAYI 108
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSARLDEDeILITPSGVDKGRLTPEDFLVVDLQGKPVS-----GGLKPSAETLLHTQLYR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 109 LRGAQAVIHTHSKAAVMATLLYPG-KEFRITHQEMIKGIRKGTSgtnyrYDEILVVPIIENTPEEKDLKDRMAWAMEEYP 187
Cdd:TIGR03328  76 LTGAGAVLHTHSVEATVLSRLYPSnGGFELEGYEMLKGLPGITT-----HEDTLVVPIIENTQDIARLADSVAPALNAYP 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1951406446 188 DSCAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAVQMKQ 228
Cdd:TIGR03328 151 DVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLK 191
 
Name Accession Description Interval E-value
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 30-228 3.81e-92

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: 269.14  E-value: 3.81e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446  30 IPELCRLFYQLGWVTGTGGGISLKRGEQ-IYIAPSGVQKERIQPEDMFVCDLEERDIScppawKKLKKSQCTPLFMNAYI 108
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSARLDEDeILITPSGVDKGRLTPEDFLVVDLQGKPVS-----GGLKPSAETLLHTQLYR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 109 LRGAQAVIHTHSKAAVMATLLYPG-KEFRITHQEMIKGIRKGTSgtnyrYDEILVVPIIENTPEEKDLKDRMAWAMEEYP 187
Cdd:TIGR03328  76 LTGAGAVLHTHSVEATVLSRLYPSnGGFELEGYEMLKGLPGITT-----HEDTLVVPIIENTQDIARLADSVAPALNAYP 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1951406446 188 DSCAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAVQMKQ 228
Cdd:TIGR03328 151 DVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLK 191
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 28-224 6.47e-51

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: 163.87  E-value: 6.47e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446  28 ALIPELCRLFYQLGWVTGTGGGISLKR-GEQIYIAPSGVQKERIQPEDMFVCDLEERDISCPPawkklKKSQCTPLFMNA 106
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLpGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGL-----KPSSETPLHLAI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 107 YILR-GAQAVIHTHSKAAVMATLLYPGkeFRITHQEMIKgirkgtsgtnYRYDEIlvvPIIEN-TPEEKDLKDRMAWAME 184
Cdd:pfam00596  76 YRARpDAGAVVHTHSPYATALSLAKEG--LPPITQEAAD----------FLGGDI---PIIPYyTPGTEELGERIAEALG 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1951406446 185 EypDSCAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAV 224
Cdd:pfam00596 141 G--DRKAVLLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 30-224 5.01e-49

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: 5.01e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446   30 IPELCRLFYQLGWVTGTGGGISLKRGEQ--IYIAPSGVQKERIQPEDMFVCDLEERDIscpPAWKKLKKSQCTPLFMNAY 107
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEdlFLITPSGVDFGELTASDLVVVDLDGNVV---EGGGGPKPSSETPLHLAIY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446  108 ILR-GAQAVIHTHSKAAVMATLLypGKEFRITHQEMIKGIRKGTSG-TNYRydeilvVPIIENTPEEKDLKDRMAWAMEE 185
Cdd:smart01007  78 RARpDVGAVVHTHSPYATALAAL--GKPLPLLPTEQAAAFLGGEIPyAPYA------GPGTELAEEGAELAEALAEALPD 149

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1951406446  186 YPdscAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAV 224
Cdd:smart01007 150 RP---AVLLRNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 24-240 2.30e-34

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: 122.25  E-value: 2.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446  24 EHPRALIPELCRLFYQLGWVTGTGGGISLK-RGEQIYIAPSGVQKERIQPEDMFVCDLEERDIscppaWKKLKKSQCTPL 102
Cdd:COG0235     4 EELREELAAAGRRLARRGLVDGTAGNISVRlDDDRFLITPSGVDFGELTPEDLVVVDLDGNVV-----EGDLKPSSETPL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 103 FMNAYILR-GAQAVIHTHSKAAVMATLLypGKEFRITHQEMIKgirkgtsgtnYRYDEILVVPiiENTPEEKDLKDRMAW 181
Cdd:COG0235    79 HLAIYRARpDVGAVVHTHSPYATALSAL--GEPLPPLEQTEAA----------AFLGDVPVVP--YAGPGTEELAEAIAE 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1951406446 182 AMEEYPdscAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAVQMKQCGlDPAALPVEE 240
Cdd:COG0235   145 ALGDRP---AVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALG-GPLVLSDEE 199
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 24-240 5.76e-28

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: 105.91  E-value: 5.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446  24 EHPRALIPELCRLFYQLGWVTGTGGGISLKRGEQIY--IAPSGVQKERIQPEDMFVCDLEERDIscppawKKLKKSQCTP 101
Cdd:cd00398     1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYflITPSGVDYEEMTASDLVVVDAQGKVV------EGKKPSSETP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 102 LFMNAYILR-GAQAVIHTHSKAAVMATLLypgkefritHQEMIKGIrkGTSGTNYRYDEIlvvPIIENTPEEKDLKDRMA 180
Cdd:cd00398    75 LHLALYRARpDIGCIVHTHSTHATAVSQL---------KEGLIPAG--HTACAVYFTGDI---PCTPYMTPETGEDEIGT 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 181 WAMEEYPDSCAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAVQMKQCGLDPAALPVEE 240
Cdd:cd00398   141 QRALGFPNSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLEL 200
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
28-228 3.62e-21

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 87.69  E-value: 3.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446  28 ALIPELCRLFYQLGWVTGTGGGISLKRGEQ-IYIAPSGVQKERIQPEDMFVCDLEERdiSCPPAwkkLKKSQCTPLFMNA 106
Cdd:PRK09220    8 QQLIAAGRWIGARGWVPATSGNMSVRLDEQhCAITVSGKDKGSLTAEDFLQVDIAGN--AVPSG---RKPSAETLLHTQL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 107 YILR-GAQAVIHTHSKAAVMATLLYPGKEFRITHQEMIKGIRKGTSgtnyrYDEILVVPIIENTPEEKDLKDRMAWAMEE 185
Cdd:PRK09220   83 YRLFpEIGAVLHTHSVNATVLSRVEKSDALVLEGYELQKAFAGQTT-----HETAVVVPIFDNDQDIARLAARVAPYLDA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1951406446 186 YPDSCAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAVQMKQ 228
Cdd:PRK09220  158 QPLRYGYLIRGHGLYCWGRDMAEARRHLEGLEFLFECELERRL 200
 
Name Accession Description Interval E-value
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 30-228 3.81e-92

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: 269.14  E-value: 3.81e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446  30 IPELCRLFYQLGWVTGTGGGISLKRGEQ-IYIAPSGVQKERIQPEDMFVCDLEERDIScppawKKLKKSQCTPLFMNAYI 108
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSARLDEDeILITPSGVDKGRLTPEDFLVVDLQGKPVS-----GGLKPSAETLLHTQLYR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 109 LRGAQAVIHTHSKAAVMATLLYPG-KEFRITHQEMIKGIRKGTSgtnyrYDEILVVPIIENTPEEKDLKDRMAWAMEEYP 187
Cdd:TIGR03328  76 LTGAGAVLHTHSVEATVLSRLYPSnGGFELEGYEMLKGLPGITT-----HEDTLVVPIIENTQDIARLADSVAPALNAYP 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1951406446 188 DSCAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAVQMKQ 228
Cdd:TIGR03328 151 DVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLK 191
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 28-224 6.47e-51

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: 163.87  E-value: 6.47e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446  28 ALIPELCRLFYQLGWVTGTGGGISLKR-GEQIYIAPSGVQKERIQPEDMFVCDLEERDISCPPawkklKKSQCTPLFMNA 106
Cdd:pfam00596   1 EELAAAGRLLARRGLVEGTGGNISVRLpGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGGL-----KPSSETPLHLAI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 107 YILR-GAQAVIHTHSKAAVMATLLYPGkeFRITHQEMIKgirkgtsgtnYRYDEIlvvPIIEN-TPEEKDLKDRMAWAME 184
Cdd:pfam00596  76 YRARpDAGAVVHTHSPYATALSLAKEG--LPPITQEAAD----------FLGGDI---PIIPYyTPGTEELGERIAEALG 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1951406446 185 EypDSCAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAV 224
Cdd:pfam00596 141 G--DRKAVLLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 30-224 5.01e-49

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: 5.01e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446   30 IPELCRLFYQLGWVTGTGGGISLKRGEQ--IYIAPSGVQKERIQPEDMFVCDLEERDIscpPAWKKLKKSQCTPLFMNAY 107
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEdlFLITPSGVDFGELTASDLVVVDLDGNVV---EGGGGPKPSSETPLHLAIY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446  108 ILR-GAQAVIHTHSKAAVMATLLypGKEFRITHQEMIKGIRKGTSG-TNYRydeilvVPIIENTPEEKDLKDRMAWAMEE 185
Cdd:smart01007  78 RARpDVGAVVHTHSPYATALAAL--GKPLPLLPTEQAAAFLGGEIPyAPYA------GPGTELAEEGAELAEALAEALPD 149

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1951406446  186 YPdscAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAV 224
Cdd:smart01007 150 RP---AVLLRNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 24-240 2.30e-34

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: 122.25  E-value: 2.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446  24 EHPRALIPELCRLFYQLGWVTGTGGGISLK-RGEQIYIAPSGVQKERIQPEDMFVCDLEERDIscppaWKKLKKSQCTPL 102
Cdd:COG0235     4 EELREELAAAGRRLARRGLVDGTAGNISVRlDDDRFLITPSGVDFGELTPEDLVVVDLDGNVV-----EGDLKPSSETPL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 103 FMNAYILR-GAQAVIHTHSKAAVMATLLypGKEFRITHQEMIKgirkgtsgtnYRYDEILVVPiiENTPEEKDLKDRMAW 181
Cdd:COG0235    79 HLAIYRARpDVGAVVHTHSPYATALSAL--GEPLPPLEQTEAA----------AFLGDVPVVP--YAGPGTEELAEAIAE 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1951406446 182 AMEEYPdscAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAVQMKQCGlDPAALPVEE 240
Cdd:COG0235   145 ALGDRP---AVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALG-GPLVLSDEE 199
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 24-240 5.76e-28

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: 105.91  E-value: 5.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446  24 EHPRALIPELCRLFYQLGWVTGTGGGISLKRGEQIY--IAPSGVQKERIQPEDMFVCDLEERDIscppawKKLKKSQCTP 101
Cdd:cd00398     1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYflITPSGVDYEEMTASDLVVVDAQGKVV------EGKKPSSETP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 102 LFMNAYILR-GAQAVIHTHSKAAVMATLLypgkefritHQEMIKGIrkGTSGTNYRYDEIlvvPIIENTPEEKDLKDRMA 180
Cdd:cd00398    75 LHLALYRARpDIGCIVHTHSTHATAVSQL---------KEGLIPAG--HTACAVYFTGDI---PCTPYMTPETGEDEIGT 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 181 WAMEEYPDSCAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAVQMKQCGLDPAALPVEE 240
Cdd:cd00398   141 QRALGFPNSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGGQLPPISLEL 200
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
28-228 3.62e-21

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 87.69  E-value: 3.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446  28 ALIPELCRLFYQLGWVTGTGGGISLKRGEQ-IYIAPSGVQKERIQPEDMFVCDLEERdiSCPPAwkkLKKSQCTPLFMNA 106
Cdd:PRK09220    8 QQLIAAGRWIGARGWVPATSGNMSVRLDEQhCAITVSGKDKGSLTAEDFLQVDIAGN--AVPSG---RKPSAETLLHTQL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 107 YILR-GAQAVIHTHSKAAVMATLLYPGKEFRITHQEMIKGIRKGTSgtnyrYDEILVVPIIENTPEEKDLKDRMAWAMEE 185
Cdd:PRK09220   83 YRLFpEIGAVLHTHSVNATVLSRVEKSDALVLEGYELQKAFAGQTT-----HETAVVVPIFDNDQDIARLAARVAPYLDA 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1951406446 186 YPDSCAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAVQMKQ 228
Cdd:PRK09220  158 QPLRYGYLIRGHGLYCWGRDMAEARRHLEGLEFLFECELERRL 200
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
32-230 1.45e-19

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 83.56  E-value: 1.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446  32 ELCRLFYQLGWVTGTGGGISLKRGE---QIYIAPSGVQKERIQPEDMFVCDLEERdiscpPAWK-KLKKSQCTPLFMNAY 107
Cdd:PRK06754   13 EIKKELAARDWFPATSGNLSIKVSDdplTFLVTASGKDKRKTTPEDFLLVDHDGK-----PVEEtELKPSAETLLHTHIY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 108 ILRGAQAVIHTHSKAAVMATLLYPG-KEFRITHQEMIK--GIrkgtsgtnYRYDEILVVPIIENTPEEKDLKDRMAWAME 184
Cdd:PRK06754   88 NNTNAGCVLHVHTVDNNVISELYGDdGAVTFQGQEIIKalGI--------WEENAEIHIPIIENHADIPTLAEEFAKHIQ 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1951406446 185 eyPDSCAVLVRRHGVYVWGESWEKAKTMCECYDYLFDIAVQMKQCG 230
Cdd:PRK06754  160 --GDSGAVLIRNHGITVWGRDAFEAKKHLEAYEFLFSYHIKLLSIQ 203
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 32-240 3.63e-08

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


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 52.32  E-value: 3.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446  32 ELCRLFYQL---GWVTGTGGGISLKRGEQ--IYIAPSGVQKERIQPEDMFVCDLEERDIScppawKKLKKSQCTPlfMNA 106
Cdd:PRK06557   14 EVCKLHLELpkyGLVVWTSGNVSARDPGTdlVVIKPSGVSYDDLTPEDMVVVDLDGNVVE-----GDLKPSSDTA--SHL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 107 YILR---GAQAVIHTHSK-AAVMATLLYP------------GKEFRITHQEMIKG--IRKGtsgtnyrydeilVVPIIEN 168
Cdd:PRK06557   87 YVYRhmpDVGGVVHTHSTyATAWAARGEPipcvltamadefGGPIPVGPFALIGDeaIGKG------------IVETLKG 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1951406446 169 tpeekdlkdrmawameeyPDSCAVLVRRHGVYVWGESWE---KAKTMCEcydylfDIAVQM---KQCGlDPAALPVEE 240
Cdd:PRK06557  155 ------------------GRSPAVLMQNHGVFTIGKDAEdavKAAVMVE------EVARTVhiaRQLG-EPIPIPQEE 207
PRK08130 PRK08130
putative aldolase; Validated
 32-209 8.26e-08

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 51.03  E-value: 8.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446  32 ELCRL---FYQLGWVTGTGGGISLKRGEQ-IYIAPSGVQKERIQPEDMFVCDLEERDISCPPAWKKLkksqctPLFMNAY 107
Cdd:PRK08130    9 EIVRLgrsLFQRGYTVGSAGNISARLDDGgWLVTPTGSCLGRLDPARLSKVDADGNWLSGDKPSKEV------PLHRAIY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 108 ILRG-AQAVIHTHSKAAVMATLLyPGkefrITHQEMIKGIrkgtsgTNY---RYDEILVVPIIEntPEEKDLKDRMAwam 183
Cdd:PRK08130   83 RNNPeCGAVVHLHSTHLTALSCL-GG----LDPTNVLPPF------TPYyvmRVGHVPLIPYYR--PGDPAIAEALA--- 146

                         170       180
                  ....*....|....*....|....*.
gi 1951406446 184 EEYPDSCAVLVRRHGVYVWGESWEKA 209
Cdd:PRK08130  147 GLAARYRAVLLANHGPVVWGSSLEAA 172
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
38-209 2.00e-07

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


Pssm-ID: 236181  Cd Length: 231  Bit Score: 50.22  E-value: 2.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446  38 YQLGWVTGTGG---GISLKRGeQIYIAPSGVQKERIQPEDMFVCDLEERDIscppaWKKLKKSQCTP---LFMNAYilRG 111
Cdd:PRK08193   17 PKHGLVTFTWGnvsAIDRERG-LFVIKPSGVDYDKMTAEDMVVVDLEGNVV-----EGKLKPSSDTPthlVLYKAF--PE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 112 AQAVIHTHSKAAV-----------MATllypgkefriTH---------------QEMIKGirkgtsgtNYRYDEILVvpI 165
Cdd:PRK08193   89 IGGIVHTHSRHATawaqagrdipaLGT----------THadyfygdipctrkmtDEEING--------EYEWETGKV--I 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1951406446 166 IEnTPEEKDLkdrmawameEYPDSCAVLVRRHGVYVWGESWEKA 209
Cdd:PRK08193  149 VE-TFEKRGI---------DPAAVPGVLVHSHGPFTWGKDAEDA 182
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
45-240 7.74e-07

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 48.21  E-value: 7.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446  45 GTGGGISLKRGEQIYIA--PSGVQKERIQPEDMFVCDLEERDIScppawKKLKKSQCTPLFMNAYILR-GAQAVIHTHSK 121
Cdd:PRK06833   25 GTGGNISIFNREQGLMAitPSGIDYFEIKPEDIVIMDLDGKVVE-----GERKPSSELDMHLIFYRNReDINAIVHTHSP 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 122 -AAVMATLlypGKEFRITHQeMIkgirkGTSGTNYRYDEIlvvpiieNTPEEKDLKDRMAWAMEeypDSCAVLVRRHGVY 200
Cdd:PRK06833  100 yATTLACL---GWELPAVHY-LI-----AVAGPNVRCAEY-------ATFGTKELAENAFEAME---DRRAVLLANHGLL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1951406446 201 VWGESWEKAKTMCECYDYLFDIAVQMKQCGlDPAALPVEE 240
Cdd:PRK06833  161 AGANNLKNAFNIAEEIEFCAEIYYQTKSIG-EPKLLPEDE 199
PRK08660 PRK08660
aldolase;
35-218 5.47e-06

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 45.33  E-value: 5.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446  35 RLFYQlGWVTGTGGGISLKRGEQIYIAPSGVQKERIQPEDMFVCDLEERDISCPPAwkklkkSQCTPLFMNAYILRGAQA 114
Cdd:PRK08660   11 KLFAH-GLVSSHFGNISVRTGDGLLITRTGSMLDEITEGDVIEVGIDDDGSVDPLA------SSETPVHRAIYRRTSAKA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 115 VIHTHSKAAVMATLLypgkefrithqemIKGIRKGTSGTNYRYDEIlvvPIIENTPEEKDLKDRMAWAMEEYPdscAVLV 194
Cdd:PRK08660   84 IVHAHPPYAVALSLL-------------EDEIVPLDSEGLYFLGTI---PVVGGDIGSGELAENVARALSEHK---GVVV 144

                         170       180
                  ....*....|....*....|....
gi 1951406446 195 RRHGVYVWGeswekaKTMCECYDY 218
Cdd:PRK08660  145 RGHGTFAIG------KTLEEAYIY 162
araD PRK13145
L-ribulose-5-phosphate 4-epimerase; Provisional
 41-209 7.24e-06

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


Pssm-ID: 183870 [Multi-domain]  Cd Length: 234  Bit Score: 45.59  E-value: 7.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446  41 GWVTGTGGGISL--KRGEQIYIAPSGVQKERIQPEDMFVCDLEERDIScppawKKLKKSQCTPLFMNAYILRG-AQAVIH 117
Cdd:PRK13145   21 GLVKFTWGNVSEvcRELGRIVIKPSGVDYDELTPENMVVTDLDGNVVE-----GDLNPSSDLPTHVELYKAWPeVGGIVH 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 118 THSKAAVmaTLLYPGKE---FRITHQEMIKG----IRKGTSG-TNYRYDEILVVPIIENTpEEKDLkDRMAWAmeeypds 189
Cdd:PRK13145   96 THSTEAV--GWAQAGRDipfYGTTHADYFYGpipcARSLTKDeVNGAYEKETGSVIIEEF-EKRGL-DPMAVP------- 164

                         170       180
                  ....*....|....*....|
gi 1951406446 190 cAVLVRRHGVYVWGESWEKA 209
Cdd:PRK13145  165 -GIVVRNHGPFTWGKNPEQA 183
PRK08333 PRK08333
aldolase;
35-209 1.56e-05

aldolase;


Pssm-ID: 181393 [Multi-domain]  Cd Length: 184  Bit Score: 44.04  E-value: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446  35 RLFYQLGWVTGTGGGISLKRGEQIYIAPSGVQKERIQPEDMFVCDLEERDIScppawkKLKKSQCTPLFMNAYILR-GAQ 113
Cdd:PRK08333   13 KLAHERGLTAAFGGNLSIRVGNLVFIKATGSVMDELTREQVAVIDLNGNQLS------SVRPSSEYRLHLAVYRNRpDVR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 114 AVIHTHSKAAVMATLLYPGKEFRITHQEMIKgIRKgtsgtnyrydeilvVPIIENTPE-EKDLKDRMAWAMEEYPdscAV 192
Cdd:PRK08333   87 AIAHLHPPYSIVASTLLEEELPIITPEAELY-LKK--------------IPILPFRPAgSVELAEQVAEAMKEYD---AV 148

                         170
                  ....*....|....*..
gi 1951406446 193 LVRRHGVYVWGESWEKA 209
Cdd:PRK08333  149 IMERHGIVTVGRSLREA 165
PRK06755 PRK06755
hypothetical protein; Validated
 42-226 2.60e-05

hypothetical protein; Validated


Pssm-ID: 102532  Cd Length: 209  Bit Score: 43.87  E-value: 2.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446  42 WVTGTGGGISL---KRGEQIYIAPSGVQKERIQPEDMFVCDleerdISCPPAWKKLKKSQCTPlFMNAYILR--GAQAVI 116
Cdd:PRK06755   23 WFYGTKISLSLctsKEPLTFLVNVEGRDKGLFSEEDFIVVN-----CMCEPVFENEEKPAAES-FMHADIYKksSAECIL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446 117 HTHSKAAVMATLLYpGKEFRITHQEmiKGIRK--GTSGTnyrydEILVVPIIENTPEEKDLKDRMAWAMEEypDSCAVLV 194
Cdd:PRK06755   97 QVQTVDSHLISELY-GEEGEVTFDK--RSVERvfGKEGI-----TEMTIPIVEDEKKFADLLENNVPNFIE--GGGVVLV 166

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1951406446 195 RRHGVYVWGESWEKAKTMCECYDYLFDIAVQM 226
Cdd:PRK06755  167 HNYGMIVWGKTPEEAKKWLEGIEYLMNYHVKL 198
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 41-123 3.10e-04

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


Pssm-ID: 183460  Cd Length: 228  Bit Score: 40.94  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1951406446  41 GWVTGTGGGISLKRGEQ--IYIAPSGVQKERIQPEDMFVCDLEERDIScppawKKLKKSQCTPLFMNAY----ILRGaqa 114
Cdd:PRK12348   19 GLVTFTWGNVSAIDRERglVVIKPSGVAYETMKADDMVVVDMSGKVVE-----GEYRPSSDTATHLELYrrypSLGG--- 90


                  ....*....
gi 1951406446 115 VIHTHSKAA 123
Cdd:PRK12348   91 IVHTHSTHA 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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