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Conserved domains on  [gi|119588567|gb|EAW68161|]
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APAF1 interacting protein [Homo sapiens]

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 ...
 28-227 3.30e-101

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: 291.86  E-value: 3.30e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567   28 IPELCKQFYHLGWVTGTGGGISLK-HGDEIYIAPSGVQKERIQPEDMFVCDINEKDISGpspskKLKKSQCTPLFMNAYT 106
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSARlDEDEILITPSGVDKGRLTPEDFLVVDLQGKPVSG-----GLKPSAETLLHTQLYR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567  107 MRGAGAVIHTHSKAAVMATLLFPGRE-FKITHQEMIKGIKkctsgGYYRYDDMLVVPIIENTPEEKDLKDRMAHAMNEYP 185
Cdd:TIGR03328  76 LTGAGAVLHTHSVEATVLSRLYPSNGgFELEGYEMLKGLP-----GITTHEDTLVVPIIENTQDIARLADSVAPALNAYP 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 119588567  186 DSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKV 227
Cdd:TIGR03328 151 DVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLKL 192
 
Name Accession Description Interval E-value
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 28-227 3.30e-101

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: 291.86  E-value: 3.30e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567   28 IPELCKQFYHLGWVTGTGGGISLK-HGDEIYIAPSGVQKERIQPEDMFVCDINEKDISGpspskKLKKSQCTPLFMNAYT 106
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSARlDEDEILITPSGVDKGRLTPEDFLVVDLQGKPVSG-----GLKPSAETLLHTQLYR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567  107 MRGAGAVIHTHSKAAVMATLLFPGRE-FKITHQEMIKGIKkctsgGYYRYDDMLVVPIIENTPEEKDLKDRMAHAMNEYP 185
Cdd:TIGR03328  76 LTGAGAVLHTHSVEATVLSRLYPSNGgFELEGYEMLKGLP-----GITTHEDTLVVPIIENTQDIARLADSVAPALNAYP 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 119588567  186 DSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKV 227
Cdd:TIGR03328 151 DVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLKL 192
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 28-222 3.76e-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: 164.26  E-value: 3.76e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567   28 IPELCKQFYHLGWVTGTGGGISLK-HGDEIYIAPSGVQKERIQPEDMFVCDINEKDISGPspskkLKKSQCTPLFMNAYT 106
Cdd:pfam00596   3 LAAAGRLLARRGLVEGTGGNISVRlPGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGG-----LKPSSETPLHLAIYR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567  107 MR-GAGAVIHTHSKAAVMATLLfpGREFKITHQEMIKgikkctsggyYRYDDmlvVPIIEN-TPEEKDLKDRMAHAMNEy 184
Cdd:pfam00596  78 ARpDAGAVVHTHSPYATALSLA--KEGLPPITQEAAD----------FLGGD---IPIIPYyTPGTEELGERIAEALGG- 141

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 119588567  185 pDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAV 222
Cdd:pfam00596 142 -DRKAVLLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 28-222 4.64e-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: 4.64e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567    28 IPELCKQFYHLGWVTGTGGGISLKHGDE--IYIAPSGVQKERIQPEDMFVCDINEKDISGPSPskkLKKSQCTPLFMNAY 105
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEdlFLITPSGVDFGELTASDLVVVDLDGNVVEGGGG---PKPSSETPLHLAIY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567   106 TMR-GAGAVIHTHSKAAVMATLLfpGREFKITHQEMIKGIkkctSGGYYRYDDmLVVPIIENTPEEKDLKDRMAHAMNEY 184
Cdd:smart01007  78 RARpDVGAVVHTHSPYATALAAL--GKPLPLLPTEQAAAF----LGGEIPYAP-YAGPGTELAEEGAELAEALAEALPDR 150

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 119588567   185 PdscAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAV 222
Cdd:smart01007 151 P---AVLLRNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 30-235 1.93e-33

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: 119.93  E-value: 1.93e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567  30 ELCKQFYHLGWVTGTGGGISLKHGDE-IYIAPSGVQKERIQPEDMFVCDINEKDISGPS-PSKklkksqCTPLFMNAYTM 107
Cdd:COG0235   12 AAGRRLARRGLVDGTAGNISVRLDDDrFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLkPSS------ETPLHLAIYRA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567 108 R-GAGAVIHTHSKAAVMATLLfpGREFKITHQEMikgikkctsgGYYRYDDmlvVPIIE-NTPEEKDLKDRMAHAMNEYP 185
Cdd:COG0235   86 RpDVGAVVHTHSPYATALSAL--GEPLPPLEQTE----------AAAFLGD---VPVVPyAGPGTEELAEAIAEALGDRP 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 119588567 186 dscAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKVGlDPSQLP 235
Cdd:COG0235  151 ---AVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALG-GPLVLS 196
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 22-229 1.47e-32

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: 117.47  E-value: 1.47e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567  22 EHPRYLIPELCKQFYHLGWVTGTGGGISLKHGDEIY--IAPSGVQKERIQPEDMFVCDINEKDISGPSPSkklkksQCTP 99
Cdd:cd00398    1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYflITPSGVDYEEMTASDLVVVDAQGKVVEGKKPS------SETP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567 100 LFMNAYTMR-GAGAVIHTHSKAAVMATLLFpGREFKITHQEMikgikkctsgGYYRYDDmlvVPIIENTPEEKDLKDRMA 178
Cdd:cd00398   75 LHLALYRARpDIGCIVHTHSTHATAVSQLK-EGLIPAGHTAC----------AVYFTGD---IPCTPYMTPETGEDEIGT 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119588567 179 HAMNEYPDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKVGL 229
Cdd:cd00398  141 QRALGFPNSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGG 191
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
30-218 9.71e-28

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 105.13  E-value: 9.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567  30 ELCKQFYHLGWVTGTGGGISLKHGDE---IYIAPSGVQKERIQPEDMFVCDINEKdisgPSPSKKLKKSQCTPLFMNAYT 106
Cdd:PRK06754  13 EIKKELAARDWFPATSGNLSIKVSDDpltFLVTASGKDKRKTTPEDFLLVDHDGK----PVEETELKPSAETLLHTHIYN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567 107 MRGAGAVIHTHSKAA-VMATLLFPGREFKITHQEMIKGIkkctsgGYYRYDDMLVVPIIENTPEEKDLKDRMAHAMNeyP 185
Cdd:PRK06754  89 NTNAGCVLHVHTVDNnVISELYGDDGAVTFQGQEIIKAL------GIWEENAEIHIPIIENHADIPTLAEEFAKHIQ--G 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 119588567 186 DSCAVLVRRHGVYVWGETWEKAKTMCECYDYLF 218
Cdd:PRK06754 161 DSGAVLIRNHGITVWGRDAFEAKKHLEAYEFLF 193
 
Name Accession Description Interval E-value
salvage_mtnB TIGR03328
methylthioribulose-1-phosphate dehydratase; Members of this family are the ...
 28-227 3.30e-101

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: 291.86  E-value: 3.30e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567   28 IPELCKQFYHLGWVTGTGGGISLK-HGDEIYIAPSGVQKERIQPEDMFVCDINEKDISGpspskKLKKSQCTPLFMNAYT 106
Cdd:TIGR03328   1 LIEAGRDLYKRGWVPGTGGNLSARlDEDEILITPSGVDKGRLTPEDFLVVDLQGKPVSG-----GLKPSAETLLHTQLYR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567  107 MRGAGAVIHTHSKAAVMATLLFPGRE-FKITHQEMIKGIKkctsgGYYRYDDMLVVPIIENTPEEKDLKDRMAHAMNEYP 185
Cdd:TIGR03328  76 LTGAGAVLHTHSVEATVLSRLYPSNGgFELEGYEMLKGLP-----GITTHEDTLVVPIIENTQDIARLADSVAPALNAYP 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 119588567  186 DSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKV 227
Cdd:TIGR03328 151 DVPGVLIRGHGLYAWGRDWEEAKRHLEALEFLFECELEMLKL 192
Aldolase_II pfam00596
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 28-222 3.76e-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: 164.26  E-value: 3.76e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567   28 IPELCKQFYHLGWVTGTGGGISLK-HGDEIYIAPSGVQKERIQPEDMFVCDINEKDISGPspskkLKKSQCTPLFMNAYT 106
Cdd:pfam00596   3 LAAAGRLLARRGLVEGTGGNISVRlPGDGFLITPSGVDFGELTPEDLVVVDLDGNVVEGG-----LKPSSETPLHLAIYR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567  107 MR-GAGAVIHTHSKAAVMATLLfpGREFKITHQEMIKgikkctsggyYRYDDmlvVPIIEN-TPEEKDLKDRMAHAMNEy 184
Cdd:pfam00596  78 ARpDAGAVVHTHSPYATALSLA--KEGLPPITQEAAD----------FLGGD---IPIIPYyTPGTEELGERIAEALGG- 141

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 119588567  185 pDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAV 222
Cdd:pfam00596 142 -DRKAVLLRNHGLLVWGKTLEEAFYLAEELERAAEIQL 178
Aldolase_II smart01007
Class II Aldolase and Adducin N-terminal domain; This family includes class II aldolases and ...
 28-222 4.64e-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: 4.64e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567    28 IPELCKQFYHLGWVTGTGGGISLKHGDE--IYIAPSGVQKERIQPEDMFVCDINEKDISGPSPskkLKKSQCTPLFMNAY 105
Cdd:smart01007   1 LAAACRLLARRGLVEGTGGNISARVGEEdlFLITPSGVDFGELTASDLVVVDLDGNVVEGGGG---PKPSSETPLHLAIY 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567   106 TMR-GAGAVIHTHSKAAVMATLLfpGREFKITHQEMIKGIkkctSGGYYRYDDmLVVPIIENTPEEKDLKDRMAHAMNEY 184
Cdd:smart01007  78 RARpDVGAVVHTHSPYATALAAL--GKPLPLLPTEQAAAF----LGGEIPYAP-YAGPGTELAEEGAELAEALAEALPDR 150

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 119588567   185 PdscAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAV 222
Cdd:smart01007 151 P---AVLLRNHGLLVWGKTLEEAFDLAEELEEAAEIQL 185
AraD COG0235
5-methylthioribulose/5-deoxyribulose/Fuculose 1-phosphate aldolase (methionine salvage, sugar ...
 30-235 1.93e-33

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: 119.93  E-value: 1.93e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567  30 ELCKQFYHLGWVTGTGGGISLKHGDE-IYIAPSGVQKERIQPEDMFVCDINEKDISGPS-PSKklkksqCTPLFMNAYTM 107
Cdd:COG0235   12 AAGRRLARRGLVDGTAGNISVRLDDDrFLITPSGVDFGELTPEDLVVVDLDGNVVEGDLkPSS------ETPLHLAIYRA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567 108 R-GAGAVIHTHSKAAVMATLLfpGREFKITHQEMikgikkctsgGYYRYDDmlvVPIIE-NTPEEKDLKDRMAHAMNEYP 185
Cdd:COG0235   86 RpDVGAVVHTHSPYATALSAL--GEPLPPLEQTE----------AAAFLGD---VPVVPyAGPGTEELAEAIAEALGDRP 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 119588567 186 dscAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKVGlDPSQLP 235
Cdd:COG0235  151 ---AVLLRNHGVVVWGKDLAEAFDRAEVLEEAARIQLLALALG-GPLVLS 196
Aldolase_II cd00398
Class II Aldolase and Adducin head (N-terminal) domain. Aldolases are ubiquitous enzymes ...
 22-229 1.47e-32

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: 117.47  E-value: 1.47e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567  22 EHPRYLIPELCKQFYHLGWVTGTGGGISLKHGDEIY--IAPSGVQKERIQPEDMFVCDINEKDISGPSPSkklkksQCTP 99
Cdd:cd00398    1 EKLKRKIIAACLLLDLYGWVTGTGGNVSARDRDRGYflITPSGVDYEEMTASDLVVVDAQGKVVEGKKPS------SETP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567 100 LFMNAYTMR-GAGAVIHTHSKAAVMATLLFpGREFKITHQEMikgikkctsgGYYRYDDmlvVPIIENTPEEKDLKDRMA 178
Cdd:cd00398   75 LHLALYRARpDIGCIVHTHSTHATAVSQLK-EGLIPAGHTAC----------AVYFTGD---IPCTPYMTPETGEDEIGT 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119588567 179 HAMNEYPDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKVGL 229
Cdd:cd00398  141 QRALGFPNSKAVLLRNHGLFAWGPTLDEAFHLAVVLEVAAEIQLKALSMGG 191
mtnB PRK06754
methylthioribulose 1-phosphate dehydratase;
30-218 9.71e-28

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 180679 [Multi-domain]  Cd Length: 208  Bit Score: 105.13  E-value: 9.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567  30 ELCKQFYHLGWVTGTGGGISLKHGDE---IYIAPSGVQKERIQPEDMFVCDINEKdisgPSPSKKLKKSQCTPLFMNAYT 106
Cdd:PRK06754  13 EIKKELAARDWFPATSGNLSIKVSDDpltFLVTASGKDKRKTTPEDFLLVDHDGK----PVEETELKPSAETLLHTHIYN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567 107 MRGAGAVIHTHSKAA-VMATLLFPGREFKITHQEMIKGIkkctsgGYYRYDDMLVVPIIENTPEEKDLKDRMAHAMNeyP 185
Cdd:PRK06754  89 NTNAGCVLHVHTVDNnVISELYGDDGAVTFQGQEIIKAL------GIWEENAEIHIPIIENHADIPTLAEEFAKHIQ--G 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 119588567 186 DSCAVLVRRHGVYVWGETWEKAKTMCECYDYLF 218
Cdd:PRK06754 161 DSGAVLIRNHGITVWGRDAFEAKKHLEAYEFLF 193
PRK09220 PRK09220
methylthioribulose 1-phosphate dehydratase;
27-227 7.18e-20

methylthioribulose 1-phosphate dehydratase;


Pssm-ID: 236415 [Multi-domain]  Cd Length: 204  Bit Score: 84.22  E-value: 7.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567  27 LIPELCKQFYHLGWVTGTGGGISLKHGD-EIYIAPSGVQKERIQPEDMFVCDINekdiSGPSPSKKlKKSQCTPLFMNAY 105
Cdd:PRK09220   9 QLIAAGRWIGARGWVPATSGNMSVRLDEqHCAITVSGKDKGSLTAEDFLQVDIA----GNAVPSGR-KPSAETLLHTQLY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567 106 TMR-GAGAVIHTHSKAAVMATLLFPGREFKITHQEMIKgikkcTSGGYYRYDDMLVVPIIENTPEEKDLKDRMAHAMNEY 184
Cdd:PRK09220  84 RLFpEIGAVLHTHSVNATVLSRVEKSDALVLEGYELQK-----AFAGQTTHETAVVVPIFDNDQDIARLAARVAPYLDAQ 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 119588567 185 PDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSMKKV 227
Cdd:PRK09220 159 PLRYGYLIRGHGLYCWGRDMAEARRHLEGLEFLFECELERRLL 201
PRK08130 PRK08130
putative aldolase; Validated
 25-207 1.05e-10

putative aldolase; Validated


Pssm-ID: 181241 [Multi-domain]  Cd Length: 213  Bit Score: 59.50  E-value: 1.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567  25 RYLIPELCKQFYHLGWVTGTGGGISLKHGDE-IYIAPSGVQKERIQPEDMFVCDINEKDISGPSPSKKLkksqctPLFMN 103
Cdd:PRK08130   7 REEIVRLGRSLFQRGYTVGSAGNISARLDDGgWLVTPTGSCLGRLDPARLSKVDADGNWLSGDKPSKEV------PLHRA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567 104 AYTMRG-AGAVIHTHSKAAVMATLLfPGrefkITHQEMIKGIKKctsggYY--RYDDMLVVPIIEntPEEKDLKDRMAHA 180
Cdd:PRK08130  81 IYRNNPeCGAVVHLHSTHLTALSCL-GG----LDPTNVLPPFTP-----YYvmRVGHVPLIPYYR--PGDPAIAEALAGL 148

                        170       180
                 ....*....|....*....|....*..
gi 119588567 181 MNEYPdscAVLVRRHGVYVWGETWEKA 207
Cdd:PRK08130 149 AARYR---AVLLANHGPVVWGSSLEAA 172
PRK06557 PRK06557
L-ribulose-5-phosphate 4-epimerase; Validated
 39-212 3.30e-09

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


Pssm-ID: 235829 [Multi-domain]  Cd Length: 221  Bit Score: 55.40  E-value: 3.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567  39 GWVTGTGGGIS--LKHGDEIYIAPSGVQKERIQPEDMFVCDINEKDISGpspskKLKKSQCTPLFMNAYT-MRGAGAVIH 115
Cdd:PRK06557  26 GLVVWTSGNVSarDPGTDLVVIKPSGVSYDDLTPEDMVVVDLDGNVVEG-----DLKPSSDTASHLYVYRhMPDVGGVVH 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567 116 THSKAAVMatllFPGREfkithqEMIKGIkkCTS-----GGyyryddmlVVPIienTPEEKDLKDRMAHAMNEY---PDS 187
Cdd:PRK06557 101 THSTYATA----WAARG------EPIPCV--LTAmadefGG--------PIPV---GPFALIGDEAIGKGIVETlkgGRS 157

                        170       180
                 ....*....|....*....|....*...
gi 119588567 188 CAVLVRRHGVYVWGETWE---KAKTMCE 212
Cdd:PRK06557 158 PAVLMQNHGVFTIGKDAEdavKAAVMVE 185
araD PRK13145
L-ribulose-5-phosphate 4-epimerase; Provisional
 27-207 3.40e-08

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


Pssm-ID: 183870 [Multi-domain]  Cd Length: 234  Bit Score: 52.53  E-value: 3.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567  27 LIPELCKQFYHL-------GWVTGTGGGISL--KHGDEIYIAPSGVQKERIQPEDMFVCDINEKDISGpspskKLKKSQC 97
Cdd:PRK13145   2 NLQEMRERVCAAnkslpkhGLVKFTWGNVSEvcRELGRIVIKPSGVDYDELTPENMVVTDLDGNVVEG-----DLNPSSD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567  98 TPLFMNAYTMRG-AGAVIHTHSKAAVmaTLLFPGRE---FKITHQEMIKGIKKCTSG-------GYYRYDDMLVvpIIEN 166
Cdd:PRK13145  77 LPTHVELYKAWPeVGGIVHTHSTEAV--GWAQAGRDipfYGTTHADYFYGPIPCARSltkdevnGAYEKETGSV--IIEE 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 119588567 167 TpEEKDLkDRMAHAmneypdscAVLVRRHGVYVWGETWEKA 207
Cdd:PRK13145 153 F-EKRGL-DPMAVP--------GIVVRNHGPFTWGKNPEQA 183
PRK08660 PRK08660
aldolase;
39-207 5.94e-08

aldolase;


Pssm-ID: 181527 [Multi-domain]  Cd Length: 181  Bit Score: 51.11  E-value: 5.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567  39 GWVTGTGGGISLKHGDEIYIAPSGVQKERIQPEDmfvcdINEKDISGPSPSKKLKKSQcTPLFMNAYTMRGAGAVIHTHS 118
Cdd:PRK08660  16 GLVSSHFGNISVRTGDGLLITRTGSMLDEITEGD-----VIEVGIDDDGSVDPLASSE-TPVHRAIYRRTSAKAIVHAHP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567 119 KAAVMATLLfpgrefkithQEMIKGIkkCTSGGYYryddMLVVPIIENTPEEKDLKDRMAHAMNEYPdscAVLVRRHGVY 198
Cdd:PRK08660  90 PYAVALSLL----------EDEIVPL--DSEGLYF----LGTIPVVGGDIGSGELAENVARALSEHK---GVVVRGHGTF 150


                 ....*....
gi 119588567 199 VWGETWEKA 207
Cdd:PRK08660 151 AIGKTLEEA 159
sgaE PRK12348
L-ribulose-5-phosphate 4-epimerase; Reviewed
 39-202 2.07e-07

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


Pssm-ID: 183460  Cd Length: 228  Bit Score: 50.18  E-value: 2.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567  39 GWVTGTGGGISL--KHGDEIYIAPSGVQKERIQPEDMFVCDINEKDISGpspskKLKKSQCTPLFMNAY-TMRGAGAVIH 115
Cdd:PRK12348  19 GLVTFTWGNVSAidRERGLVVIKPSGVAYETMKADDMVVVDMSGKVVEG-----EYRPSSDTATHLELYrRYPSLGGIVH 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567 116 THSKAAV---MATLLFPGreFKITHQEMIKGIKKCTSG-------GYYRYDDMLVvpIIENTPEEKDLkdrmahamnEYP 185
Cdd:PRK12348  94 THSTHATawaQAGLAIPA--LGTTHADYFFGDIPCTRGlseeevqGEYELNTGKV--IIETLGNAEPL---------HTP 160

                        170
                 ....*....|....*..
gi 119588567 186 dscAVLVRRHGVYVWGE 202
Cdd:PRK12348 161 ---GIVVYQHGPFAWGK 174
araD PRK08193
L-ribulose-5-phosphate 4-epimerase AraD;
34-207 6.16e-07

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


Pssm-ID: 236181  Cd Length: 231  Bit Score: 48.68  E-value: 6.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567  34 QFYHLGWVTGTGG---GISLKHGdEIYIAPSGVQKERIQPEDMFVCDINEKDISGpspskKLKKSQCTPLFMNAY-TMRG 109
Cdd:PRK08193  15 ALPKHGLVTFTWGnvsAIDRERG-LFVIKPSGVDYDKMTAEDMVVVDLEGNVVEG-----KLKPSSDTPTHLVLYkAFPE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567 110 AGAVIHTHSKAAVM---AtllfpGRE---FKITHQEMIKGIKKCTS-------GGYYRYDDMLVvpIIEnTPEEKDLkdr 176
Cdd:PRK08193  89 IGGIVHTHSRHATAwaqA-----GRDipaLGTTHADYFYGDIPCTRkmtdeeiNGEYEWETGKV--IVE-TFEKRGI--- 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 119588567 177 mahamnEYPDSCAVLVRRHGVYVWGETWEKA 207
Cdd:PRK08193 158 ------DPAAVPGVLVHSHGPFTWGKDAEDA 182
sgbE PRK12347
L-ribulose-5-phosphate 4-epimerase; Reviewed
 36-201 7.87e-07

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


Pssm-ID: 183459  Cd Length: 231  Bit Score: 48.66  E-value: 7.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567  36 YHLgwVTGTGGGISLKHGDE--IYIAPSGVQKERIQPEDMFVCDInekdISGPSPSKKLKKSQCTPLFMNAY-TMRGAGA 112
Cdd:PRK12347  19 HHL--VTFTWGNVSAVDETRqlMVIKPSGVEYDVMTADDMVVVEI----ASGKVVEGSKKPSSDTPTHLALYrRYPEIGG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567 113 VIHTHSKAAVM---ATLLFPgrEFKITHQEMIKGIKKCTS-------GGYYRYDDMLVvpIIEnTPEEKDLKDRmahamn 182
Cdd:PRK12347  93 IVHTHSRHATIwsqAGLDLP--AWGTTHADYFYGAIPCTRlmtaeeiNGEYEYQTGEV--IIE-TFEERGISPA------ 161

                        170
                 ....*....|....*....
gi 119588567 183 eypDSCAVLVRRHGVYVWG 201
Cdd:PRK12347 162 ---QIPAVLVHSHGPFAWG 177
PRK08087 PRK08087
L-fuculose-phosphate aldolase;
28-207 2.99e-06

L-fuculose-phosphate aldolase;


Pssm-ID: 181226 [Multi-domain]  Cd Length: 215  Bit Score: 46.66  E-value: 2.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567  28 IPELCKQFYHLGWVTGTGGGISLKHGDEIYIAPSGVQKERIQPEDMFVCDINEKDISGPSPSKKLKksqctpLFMNAYTM 107
Cdd:PRK08087  10 IIDTCLEMTRLGLNQGTAGNVSVRYQDGMLITPTGIPYEKLTESHIVFVDGNGKHEEGKLPSSEWR------FHMAAYQT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567 108 R-GAGAVIHTHSKAAVMATLLfpGREFKITHQeMIkgikkCTSGGyyryDDMLVVPIIenTPEEKDLKDRMAHAMNEypd 186
Cdd:PRK08087  84 RpDANAVVHNHAVHCTAVSIL--NRPIPAIHY-MI-----AAAGG----NSIPCAPYA--TFGTRELSEHVALALKN--- 146

                        170       180
                 ....*....|....*....|.
gi 119588567 187 SCAVLVRRHGVYVWGETWEKA 207
Cdd:PRK08087 147 RKATLLQHHGLIACEVNLEKA 167
PRK06833 PRK06833
L-fuculose-phosphate aldolase;
22-126 7.95e-06

L-fuculose-phosphate aldolase;


Pssm-ID: 180717 [Multi-domain]  Cd Length: 214  Bit Score: 45.51  E-value: 7.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567  22 EHPRYLIPELCKQFYHLGWVTGTGGGISLKHGDEIYIA--PSGVQKERIQPEDMFVCDINEKDISG---PSPSKKLKKSQ 96
Cdd:PRK06833   4 QKEREEIVAYGKKLISSGLTKGTGGNISIFNREQGLMAitPSGIDYFEIKPEDIVIMDLDGKVVEGerkPSSELDMHLIF 83

                         90       100       110
                 ....*....|....*....|....*....|..
gi 119588567  97 ctplfmnaYTMR-GAGAVIHTHSK-AAVMATL 126
Cdd:PRK06833  84 --------YRNReDINAIVHTHSPyATTLACL 107
PRK06755 PRK06755
hypothetical protein; Validated
 159-224 1.59e-04

hypothetical protein; Validated


Pssm-ID: 102532  Cd Length: 209  Bit Score: 41.56  E-value: 1.59e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119588567 159 LVVPIIENTPEEKDLKDRMAHAMNEypDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVSM 224
Cdd:PRK06755 135 MTIPIVEDEKKFADLLENNVPNFIE--GGGVVLVHNYGMIVWGKTPEEAKKWLEGIEYLMNYHVKL 198
araD PRK13213
L-ribulose-5-phosphate 4-epimerase; Reviewed
 43-207 3.07e-03

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


Pssm-ID: 106181  Cd Length: 231  Bit Score: 37.78  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567  43 GTGGGISLKHGdEIYIAPSGVQKERIQPEDMFVCDInekdISGPSPSKKLKKSQCTPLFMNAY-TMRGAGAVIHTHSK-A 120
Cdd:PRK13213  27 GNVSGIDREHG-LVVIKPSGVEYDVMSVNDMVVVDL----ATGKVVEGDKKPSSDTDTHLVLYrAFAEIGGIVHTHSRhA 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119588567 121 AVMATLLFPGREFKITHQEMIKGIKKCTS-------GGYYRYDdmlVVPIIENTPEEKDLKDrmahamneyPDSCAVLVR 193
Cdd:PRK13213 102 TIWAQAGKSLSALGTTHADYFYGPIPCTRlmteaeiTGDYEHE---TGKVIVETFAEQGLRA---------ADIPAVLVN 169

                        170
                 ....*....|....
gi 119588567 194 RHGVYVWGETWEKA 207
Cdd:PRK13213 170 GHGPFAWGSNAANA 183
 
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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