NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|269832955|gb|EEZ87063|]
View 

3-hydroxydecanoyl-(acyl-carrier-protein) dehydratase [Vibrio harveyi 1DA3]

Protein Classification

bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase( domain architecture ID 10012262)

bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase catalyzes the dehydration of beta-hydroxyacyl-ACP to trans-2-acyl-ACP and the isomerization of trans-2-acyl-ACP to cis-3-acyl-ACP, possibly in the same active site

EC:  4.2.1.59|5.3.3.14
Gene Ontology:  GO:0019171|GO:0006633|GO:0034017
PubMed:  15307895
SCOP:  4001117

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK05174 PRK05174
bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase;
1-171 3.16e-128

bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase;


:

Pssm-ID: 179953  Cd Length: 172  Bit Score: 356.44  E-value: 3.16e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269832955   1 MQNKRDSYNRDDLLASSQGELW-PQGPQLPAPNMLMMDRITKMSETEGDFGKGLILAELDITPDLWFFDCHFPGDPVMPG 79
Cdd:PRK05174   1 MMTKQSSYTKEDLLACGRGELFgPGNAQLPAPPMLMMDRITEISETGGEFGKGYIVAELDINPDLWFFGCHFIGDPVMPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269832955  80 CLGLDAMWQLVGFFLGWVGGKGKGRALGVGEVKFTGQILPTAKKVTYEIHMKRVVNRKLVMGLADGRVCVDGKEIYVAKD 159
Cdd:PRK05174  81 CLGLDAMWQLVGFYLGWLGGPGKGRALGVGEVKFTGQVLPTAKKVTYEIDIKRVINRKLVMGIADGRVLVDGEEIYTAKD 160

                        170
                 ....*....|..
gi 269832955 160 LKVGLFQDTSSF 171
Cdd:PRK05174 161 LKVGLFKDTSAF 172
 
Name Accession Description Interval E-value
PRK05174 PRK05174
bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase;
1-171 3.16e-128

bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase;


Pssm-ID: 179953  Cd Length: 172  Bit Score: 356.44  E-value: 3.16e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269832955   1 MQNKRDSYNRDDLLASSQGELW-PQGPQLPAPNMLMMDRITKMSETEGDFGKGLILAELDITPDLWFFDCHFPGDPVMPG 79
Cdd:PRK05174   1 MMTKQSSYTKEDLLACGRGELFgPGNAQLPAPPMLMMDRITEISETGGEFGKGYIVAELDINPDLWFFGCHFIGDPVMPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269832955  80 CLGLDAMWQLVGFFLGWVGGKGKGRALGVGEVKFTGQILPTAKKVTYEIHMKRVVNRKLVMGLADGRVCVDGKEIYVAKD 159
Cdd:PRK05174  81 CLGLDAMWQLVGFYLGWLGGPGKGRALGVGEVKFTGQVLPTAKKVTYEIDIKRVINRKLVMGIADGRVLVDGEEIYTAKD 160

                        170
                 ....*....|..
gi 269832955 160 LKVGLFQDTSSF 171
Cdd:PRK05174 161 LKVGLFKDTSAF 172
fabA TIGR01749
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabA; This enzyme, FabA, shows overlapping ...
 4-171 1.87e-108

beta-hydroxyacyl-[acyl carrier protein] dehydratase FabA; This enzyme, FabA, shows overlapping substrate specificity with FabZ with regard to chain length in fatty acid biosynthesis. It is commonly designated 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.60) as if it were specific for that chain length, but its specificity is broader; it is active even in the initiation of fatty acid biosynthesis. This enzyme can also isomerize trans-2-decenoyl-ACP to cis-3-decenoyl-ACP to bypass reduction by FabI and instead allow biosynthesis of unsaturated fatty acids. FabA cannot elongate unsaturated fatty acids. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 130810  Cd Length: 169  Bit Score: 306.34  E-value: 1.87e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269832955    4 KRDSYNRDDLLASSQGELW-PQGPQLPAPNMLMMDRITKMSETEGDFGKGLILAELDITPDLWFFDCHFPGDPVMPGCLG 82
Cdd:TIGR01749   1 KQNAYTREDLLACGRGELFgPGNAQLPAPPMLMIDRIVEISETGGKFGKGYVEAELDIRPDLWFFGCHFIGDPVMPGCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269832955   83 LDAMWQLVGFFLGWVGGKGKGRALGVGEVKFTGQILPTAKKVTYEIHMKRVVNRKLVMGLADGRVCVDGKEIYVAKDLKV 162
Cdd:TIGR01749  81 LDAMWQLVGFFLGWLGGPGRGRALGVGEVKFTGQVLPTAKKVTYRIHFKRVINRRLVMGIADGEVLVDGRLIYTASDLRV 160


                  ....*....
gi 269832955  163 GLFQDTSSF 171
Cdd:TIGR01749 161 GLFTSTSAF 169
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 28-158 2.87e-70

FabA-like domain; This enzyme domain has a HotDog fold.


Pssm-ID: 429766  Cd Length: 132  Bit Score: 208.67  E-value: 2.87e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269832955   28 LPAPNMLMMDRITKMSETEGDFGKGLILAELDITPDLWFFDCHFPGDPVMPGCLGLDAMWQLVGFFLGWVGG-KGKGRAL 106
Cdd:pfam07977   1 LPHRYFLMLDRVTEIDPDGGKFGKGYIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWSGGgEGRGRAR 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 269832955  107 GVGEVKFTGQILPTAKKVTYEIHMKRVVNRKLVMGLADGRVCVDGKEIYVAK 158
Cdd:pfam07977  81 GVDEVKFRGQVTPGDKQLRYEVEIKKIIEGRRGIGIADGRALVDGKVVYEAK 132
FabA cd01287
FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the ...
 26-167 2.95e-65

FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the type II, fatty acid synthase system that binds ACP and catalyzes both dehydration and isomerization reactions, apparently in the same active site. The FabA structure is a homodimer with two independent active sites located at the dimer interface. Each active site is tunnel-shaped and completely inaccessible to solvent. No metal ions or cofactors are required for ligand binding or catalysis.


Pssm-ID: 238614  Cd Length: 150  Bit Score: 196.32  E-value: 2.95e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269832955  26 PQLPAPNMLMMDRITKMSETEGDFGKGLILAELDITPDLWFFDCHFPGDPVMPGCLGLDAMWQLVGFFLGWVGG------ 99
Cdd:cd01287    1 PRLPGGQLLMLDRVTEIDPGGGTFGLGYLRAEKDIDPDDWFFPCHFHGDPVMPGSLGLEAMIQLLQFYLIWLGLgtgvdn 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269832955 100 -KGKGRALGVGEVKFTGQILPTAKKVTYEIHMKRVVN-RKLVMGLADGRVCVDGKEIYVAKDLKVGLFQD 167
Cdd:cd01287   81 pRFQGAPGGPGEWKYRGQITPHNKKVTYEVHIKEVGRdGPRPYIIADASLWVDGLRIYEAKDIAVRLVEA 150
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 26-166 2.86e-45

3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and metabolism]; 3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440527  Cd Length: 141  Bit Score: 145.34  E-value: 2.86e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269832955  26 PQLPAPN-MLMMDRITKMSETEGdfgkglILAELDITPDLWFFDCHFPGDPVMPGCLGLDAMWQLVGFFLGW-VGGKGKG 103
Cdd:COG0764    6 ALLPHRYpFLLVDRVLEIDPGKS------IVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKsEGLEGKG 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 269832955 104 R---ALGVGEVKFTGQILPTAkKVTYEIHMKRVVNRklvMGLADGRVCVDGKEIYVAkDLKVGLFQ 166
Cdd:COG0764   80 RlvyFLGIDKVKFRGPVVPGD-TLTLEVEIKRVRRG---IGKADGKATVDGKLVAEA-ELTFALVE 140
 
Name Accession Description Interval E-value
PRK05174 PRK05174
bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase;
1-171 3.16e-128

bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase;


Pssm-ID: 179953  Cd Length: 172  Bit Score: 356.44  E-value: 3.16e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269832955   1 MQNKRDSYNRDDLLASSQGELW-PQGPQLPAPNMLMMDRITKMSETEGDFGKGLILAELDITPDLWFFDCHFPGDPVMPG 79
Cdd:PRK05174   1 MMTKQSSYTKEDLLACGRGELFgPGNAQLPAPPMLMMDRITEISETGGEFGKGYIVAELDINPDLWFFGCHFIGDPVMPG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269832955  80 CLGLDAMWQLVGFFLGWVGGKGKGRALGVGEVKFTGQILPTAKKVTYEIHMKRVVNRKLVMGLADGRVCVDGKEIYVAKD 159
Cdd:PRK05174  81 CLGLDAMWQLVGFYLGWLGGPGKGRALGVGEVKFTGQVLPTAKKVTYEIDIKRVINRKLVMGIADGRVLVDGEEIYTAKD 160

                        170
                 ....*....|..
gi 269832955 160 LKVGLFQDTSSF 171
Cdd:PRK05174 161 LKVGLFKDTSAF 172
fabA TIGR01749
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabA; This enzyme, FabA, shows overlapping ...
 4-171 1.87e-108

beta-hydroxyacyl-[acyl carrier protein] dehydratase FabA; This enzyme, FabA, shows overlapping substrate specificity with FabZ with regard to chain length in fatty acid biosynthesis. It is commonly designated 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.60) as if it were specific for that chain length, but its specificity is broader; it is active even in the initiation of fatty acid biosynthesis. This enzyme can also isomerize trans-2-decenoyl-ACP to cis-3-decenoyl-ACP to bypass reduction by FabI and instead allow biosynthesis of unsaturated fatty acids. FabA cannot elongate unsaturated fatty acids. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 130810  Cd Length: 169  Bit Score: 306.34  E-value: 1.87e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269832955    4 KRDSYNRDDLLASSQGELW-PQGPQLPAPNMLMMDRITKMSETEGDFGKGLILAELDITPDLWFFDCHFPGDPVMPGCLG 82
Cdd:TIGR01749   1 KQNAYTREDLLACGRGELFgPGNAQLPAPPMLMIDRIVEISETGGKFGKGYVEAELDIRPDLWFFGCHFIGDPVMPGCLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269832955   83 LDAMWQLVGFFLGWVGGKGKGRALGVGEVKFTGQILPTAKKVTYEIHMKRVVNRKLVMGLADGRVCVDGKEIYVAKDLKV 162
Cdd:TIGR01749  81 LDAMWQLVGFFLGWLGGPGRGRALGVGEVKFTGQVLPTAKKVTYRIHFKRVINRRLVMGIADGEVLVDGRLIYTASDLRV 160


                  ....*....
gi 269832955  163 GLFQDTSSF 171
Cdd:TIGR01749 161 GLFTSTSAF 169
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 28-158 2.87e-70

FabA-like domain; This enzyme domain has a HotDog fold.


Pssm-ID: 429766  Cd Length: 132  Bit Score: 208.67  E-value: 2.87e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269832955   28 LPAPNMLMMDRITKMSETEGDFGKGLILAELDITPDLWFFDCHFPGDPVMPGCLGLDAMWQLVGFFLGWVGG-KGKGRAL 106
Cdd:pfam07977   1 LPHRYFLMLDRVTEIDPDGGKFGKGYIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWSGGgEGRGRAR 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 269832955  107 GVGEVKFTGQILPTAKKVTYEIHMKRVVNRKLVMGLADGRVCVDGKEIYVAK 158
Cdd:pfam07977  81 GVDEVKFRGQVTPGDKQLRYEVEIKKIIEGRRGIGIADGRALVDGKVVYEAK 132
FabA cd01287
FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the ...
 26-167 2.95e-65

FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the type II, fatty acid synthase system that binds ACP and catalyzes both dehydration and isomerization reactions, apparently in the same active site. The FabA structure is a homodimer with two independent active sites located at the dimer interface. Each active site is tunnel-shaped and completely inaccessible to solvent. No metal ions or cofactors are required for ligand binding or catalysis.


Pssm-ID: 238614  Cd Length: 150  Bit Score: 196.32  E-value: 2.95e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269832955  26 PQLPAPNMLMMDRITKMSETEGDFGKGLILAELDITPDLWFFDCHFPGDPVMPGCLGLDAMWQLVGFFLGWVGG------ 99
Cdd:cd01287    1 PRLPGGQLLMLDRVTEIDPGGGTFGLGYLRAEKDIDPDDWFFPCHFHGDPVMPGSLGLEAMIQLLQFYLIWLGLgtgvdn 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269832955 100 -KGKGRALGVGEVKFTGQILPTAKKVTYEIHMKRVVN-RKLVMGLADGRVCVDGKEIYVAKDLKVGLFQD 167
Cdd:cd01287   81 pRFQGAPGGPGEWKYRGQITPHNKKVTYEVHIKEVGRdGPRPYIIADASLWVDGLRIYEAKDIAVRLVEA 150
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 26-166 2.86e-45

3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and metabolism]; 3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440527  Cd Length: 141  Bit Score: 145.34  E-value: 2.86e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269832955  26 PQLPAPN-MLMMDRITKMSETEGdfgkglILAELDITPDLWFFDCHFPGDPVMPGCLGLDAMWQLVGFFLGW-VGGKGKG 103
Cdd:COG0764    6 ALLPHRYpFLLVDRVLEIDPGKS------IVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKsEGLEGKG 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 269832955 104 R---ALGVGEVKFTGQILPTAkKVTYEIHMKRVVNRklvMGLADGRVCVDGKEIYVAkDLKVGLFQ 166
Cdd:COG0764   80 RlvyFLGIDKVKFRGPVVPGD-TLTLEVEIKRVRRG---IGKADGKATVDGKLVAEA-ELTFALVE 140
FabA_FabZ cd00493
FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct ...
 28-158 5.77e-34

FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct enzyme types of the dissociative, type II, fatty acid synthase system (found in bacteria and plants) required to complete successive cycles of fatty acid elongation. The third step of the elongation cycle, the dehydration of beta-hydroxyacyl-ACP to trans-2-acyl-ACP, is catalyzed by FabA or FabZ. FabA is bifunctional and catalyzes an additional isomerization reaction of trans-2-acyl-ACP to cis-3-acyl-ACP, an essential reaction to unsaturated fatty acid synthesis. FabZ is the primary dehydratase that participates in the elongation cycles of saturated as well as unsaturated fatty acid biosynthesis, whereas FabA is more active in the dehydration of beta-hydroxydecanoyl-ACP. The FabA structure is homodimeric with two independent active sites located at the dimer interface.


Pssm-ID: 238275  Cd Length: 131  Bit Score: 116.23  E-value: 5.77e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269832955  28 LPAPNMLMMDRITKMSEtegdfgKGLILAELDITPDLWFFDCHFPGDPVMPGCLGLDAMWQLVGFFLGWVGGKGK----- 102
Cdd:cd00493    1 PHRYPMLLVDRVLEIDP------GGRIVAEKNVTPNEPFFQGHFPGDPVMPGVLGIEAMAQAAAALAGLLGLGKGnpprl 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 269832955 103 GRALGVGEVKFTGQILPTAkKVTYEIHMKRVvnrKLVMGLADGRVCVDGKEIYVAK 158
Cdd:cd00493   75 GYLAGVRKVKFRGPVLPGD-TLTLEVELLKV---RRGLGKFDGRAYVDGKLVAEAE 126
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 33-152 3.98e-13

FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily catalyzes the dehydration of beta-hydroxyacyl-ACP to trans-2-acyl-ACP, the third step in the elongation phase of the bacterial/ plastid, type II, fatty-acid biosynthesis pathway.


Pssm-ID: 238615  Cd Length: 131  Bit Score: 62.56  E-value: 3.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269832955  33 MLMMDRITKMseTEGDFgkglILAELDITPDLWFFDCHFPGDPVMPGCLGLDAMWQLVGFFLGWVGGKGKGRA---LGVG 109
Cdd:cd01288    7 FLLVDRVLEL--EPGKS----IVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLEDFEGKLvyfAGID 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 269832955 110 EVKFTGQILPTAkkvTYEIHMKrVVNRKLVMGLADGRVCVDGK 152
Cdd:cd01288   81 KARFRKPVVPGD---QLILEVE-LLKLRRGIGKFKGKAYVDGK 119
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 33-152 1.36e-10

beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping substrate specificity with FabA with regard to chain length in fatty acid biosynthesis. FabZ works preferentially on shorter chains and is often designated (3R)-hydroxymyristoyl-[acyl carrier protein] dehydratase, although its actual specificity is broader. Unlike FabA, FabZ does not function as an isomerase and cannot initiate unsaturated fatty acid biosynthesis. However, only FabZ can act during the elongation of unsaturated fatty acid chains. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 130811  Cd Length: 140  Bit Score: 56.17  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269832955   33 MLMMDRITKMSETEGdfgkglILAELDITPDLWFFDCHFPGDPVMPGCLGLDAMWQLVGFF----LGWVGGKGK-GRALG 107
Cdd:TIGR01750  15 FLLVDRILELEPGKR------IVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLailsLGGEKGKGKlVYFAG 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 269832955  108 VGEVKFTGQILPTAKkvtYEIHMKrVVNRKLVMGLADGRVCVDGK 152
Cdd:TIGR01750  89 IDKARFRRPVVPGDQ---LILHVE-FLKKRRGIGKFKGEATVDGK 129
PRK13188 PRK13188
bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R) ...
 33-152 1.94e-08

bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase; Reviewed


Pssm-ID: 237296 [Multi-domain]  Cd Length: 464  Bit Score: 52.24  E-value: 1.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269832955  33 MLMMDRITKMSETEgdfgkglILAELDITPDLWFFDCHFPGDPVMPGCLGLDAMWQLVGFF-LGWVGGKGKGRA--LGVG 109
Cdd:PRK13188 336 FLLVDKIIELGDTK-------IVGIKNVTMNEPFFQGHFPGNPVMPGVLQIEAMAQTGGILvLNTVPDPENYSTyfMKID 408

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 269832955 110 EVKFTGQILPTAkkvTYEIHMKRVVNRKLVMGLADGRVCVDGK 152
Cdd:PRK13188 409 KVKFRQKVVPGD---TLIFKVELLSPIRRGICQMQGKAYVNGK 448
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
33-152 2.37e-07

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 47.42  E-value: 2.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269832955  33 MLMMDRITKMseTEGDFGKGLilaeLDITPDLWFFDCHFPGDPVMPGCLGLDAMWQlVGFFLGWVGGKGKGRA---LGVG 109
Cdd:PRK00006  22 FLLVDRVLEL--EPGKSIVAI----KNVTINEPFFQGHFPGYPVMPGVLIIEAMAQ-AAGVLALKSEENKGKLvyfAGID 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 269832955 110 EVKFTGQILPTAkkvTYEIHMKrVVNRKLVMGLADGRVCVDGK 152
Cdd:PRK00006  95 KARFKRPVVPGD---QLILEVE-LLKQRRGIWKFKGVATVDGK 133
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 54-156 8.38e-03

The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase) structure and subsequently in 4HBT (4-hydroxybenzoyl-CoA thioesterase) from Pseudomonas. A number of other seemingly unrelated proteins also share the hotdog fold. These proteins have related, but distinct, catalytic activities that include metabolic roles such as thioester hydrolysis in fatty acid metabolism, and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate. This superfamily also includes the PaaI-like protein FapR, a non-catalytic bacterial homolog involved in transcriptional regulation of fatty acid biosynthesis.


Pssm-ID: 239524 [Multi-domain]  Cd Length: 100  Bit Score: 34.37  E-value: 8.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 269832955  54 ILAELDITPDLWFfdchfpGDPVMPGCLGLDAMWQLVGFFLGWVGGKGKGRALGVGEVKFTGQILPTaKKVTYEIHMKRV 133
Cdd:cd03440    1 FVLRLTVTPEDID------GGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPG-DTLTVEAEVVRV 73

                         90       100
                 ....*....|....*....|....*..
gi 269832955 134 VNRKLVMGL----ADGRVCVDGKEIYV 156
Cdd:cd03440   74 GRSSVTVEVevrnEDGKLVATATATFV 100
 
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