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Conserved domains on  [gi|511454959|gb|EPC84624|]
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3-hydroxymyristoyl-ACP dehydratase, partial [Lacticaseibacillus paracasei subsp. paracasei Lpp43]

Protein Classification

3-hydroxyacyl-ACP dehydratase FabZ( domain architecture ID 10791549)

3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ catalyzes the dehydration of beta-hydroxyacyl-ACP to trans-2-acyl-ACP

EC:  4.2.1.59
Gene Symbol:  fabZ
Gene Ontology:  GO:0019171|GO:0006633|GO:0009245
PubMed:  15307895
SCOP:  4002539

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
1-144 1.99e-76

3-hydroxyacyl-ACP dehydratase FabZ;


:

Pssm-ID: 234568  Cd Length: 147  Bit Score: 223.45  E-value: 1.99e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511454959   1 RNQETLEAQEIQAILPHRYPMLMVDRVLDLKPGESVVAQKNVSINEQIFQGHFPGNPIFPGVLQIEAMAQAGAIALLSMP 80
Cdd:PRK00006   2 TETMMLDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSE 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511454959  81 DFKGKTAYLGGIKKAKFRHMVRPGDVLRIEVTLEKLIDNAGLGKGKIYVGENMASSADLVFAIG 144
Cdd:PRK00006  82 ENKGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIR 145
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
1-144 1.99e-76

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 223.45  E-value: 1.99e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511454959   1 RNQETLEAQEIQAILPHRYPMLMVDRVLDLKPGESVVAQKNVSINEQIFQGHFPGNPIFPGVLQIEAMAQAGAIALLSMP 80
Cdd:PRK00006   2 TETMMLDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSE 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511454959  81 DFKGKTAYLGGIKKAKFRHMVRPGDVLRIEVTLEKLIDNAGLGKGKIYVGENMASSADLVFAIG 144
Cdd:PRK00006  82 ENKGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIR 145
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 15-144 4.08e-70

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: 207.01  E-value: 4.08e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511454959  15 LPHRYPMLMVDRVLDLKPGESVVAQKNVSINEQIFQGHFPGNPIFPGVLQIEAMAQAGAIALLSMPD-FKGKTAYLGGIK 93
Cdd:cd01288    1 LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLEdFEGKLVYFAGID 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 511454959  94 KAKFRHMVRPGDVLRIEVTLEKLIDNAGLGKGKIYVGENMASSADLVFAIG 144
Cdd:cd01288   81 KARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELMFAIA 131
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 9-143 1.26e-67

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: 200.81  E-value: 1.26e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511454959   9 QEIQAILPHRYPMLMVDRVLDLKPGESVVAQKNVSINEQIFQGHFPGNPIFPGVLQIEAMAQAGAIALLSM--PDFKGKT 86
Cdd:COG0764    2 EEILALLPHRYPFLLVDRVLEIDPGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSegLEGKGRL 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 511454959  87 AYLGGIKKAKFRHMVRPGDVLRIEVTLEKLIDNAGLGKGKIYVGENMASSADLVFAI 143
Cdd:COG0764   82 VYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFAL 138
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 7-143 1.04e-56

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: 173.27  E-value: 1.04e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511454959    7 EAQEIQAILPHRYPMLMVDRVLDLKPGESVVAQKNVSINEQIFQGHFPGNPIFPGVLQIEAMAQA-GAIALLSMPDFKGK 85
Cdd:TIGR01750   1 DIQDIMELLPHRYPFLLVDRILELEPGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAaGVLAILSLGGEKGK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 511454959   86 T--AYLGGIKKAKFRHMVRPGDVLRIEVTLEKLIDNAGLGKGKIYVGENMASSADLVFAI 143
Cdd:TIGR01750  81 GklVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIMFAI 140
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 15-118 2.22e-30

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 106.21  E-value: 2.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511454959   15 LPHRYpMLMVDRVLDLKPGES------VVAQKNVSINEQIFQGHFPGNPIFPGVLQIEAMAQA-GAIALLSMPDFKGKTA 87
Cdd:pfam07977   1 LPHRY-FLMLDRVTEIDPDGGkfgkgyIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLmGFYAIWSGGGEGRGRA 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 511454959   88 ylGGIKKAKFRHMVRPGD-VLRIEVTLEKLID 118
Cdd:pfam07977  80 --RGVDEVKFRGQVTPGDkQLRYEVEIKKIIE 109
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
1-144 1.99e-76

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 223.45  E-value: 1.99e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511454959   1 RNQETLEAQEIQAILPHRYPMLMVDRVLDLKPGESVVAQKNVSINEQIFQGHFPGNPIFPGVLQIEAMAQAGAIALLSMP 80
Cdd:PRK00006   2 TETMMLDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSE 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511454959  81 DFKGKTAYLGGIKKAKFRHMVRPGDVLRIEVTLEKLIDNAGLGKGKIYVGENMASSADLVFAIG 144
Cdd:PRK00006  82 ENKGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIR 145
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 15-144 4.08e-70

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: 207.01  E-value: 4.08e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511454959  15 LPHRYPMLMVDRVLDLKPGESVVAQKNVSINEQIFQGHFPGNPIFPGVLQIEAMAQAGAIALLSMPD-FKGKTAYLGGIK 93
Cdd:cd01288    1 LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLEdFEGKLVYFAGID 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 511454959  94 KAKFRHMVRPGDVLRIEVTLEKLIDNAGLGKGKIYVGENMASSADLVFAIG 144
Cdd:cd01288   81 KARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELMFAIA 131
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 9-143 1.26e-67

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: 200.81  E-value: 1.26e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511454959   9 QEIQAILPHRYPMLMVDRVLDLKPGESVVAQKNVSINEQIFQGHFPGNPIFPGVLQIEAMAQAGAIALLSM--PDFKGKT 86
Cdd:COG0764    2 EEILALLPHRYPFLLVDRVLEIDPGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSegLEGKGRL 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 511454959  87 AYLGGIKKAKFRHMVRPGDVLRIEVTLEKLIDNAGLGKGKIYVGENMASSADLVFAI 143
Cdd:COG0764   82 VYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFAL 138
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 7-143 1.04e-56

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: 173.27  E-value: 1.04e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511454959    7 EAQEIQAILPHRYPMLMVDRVLDLKPGESVVAQKNVSINEQIFQGHFPGNPIFPGVLQIEAMAQA-GAIALLSMPDFKGK 85
Cdd:TIGR01750   1 DIQDIMELLPHRYPFLLVDRILELEPGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAaGVLAILSLGGEKGK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 511454959   86 T--AYLGGIKKAKFRHMVRPGDVLRIEVTLEKLIDNAGLGKGKIYVGENMASSADLVFAI 143
Cdd:TIGR01750  81 GklVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIMFAI 140
FabA_FabZ cd00493
FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct ...
 16-143 2.01e-54

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: 167.08  E-value: 2.01e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511454959  16 PHRYPMLMVDRVLDLKPGESVVAQKNVSINEQIFQGHFPGNPIFPGVLQIEAMAQAGAIALLSMPDFKG---KTAYLGGI 92
Cdd:cd00493    1 PHRYPMLLVDRVLEIDPGGRIVAEKNVTPNEPFFQGHFPGDPVMPGVLGIEAMAQAAAALAGLLGLGKGnppRLGYLAGV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 511454959  93 KKAKFRHMVRPGDVLRIEVTLEKLIDNAGLGKGKIYVGENMASSADLVFAI 143
Cdd:cd00493   81 RKVKFRGPVLPGDTLTLEVELLKVRRGLGKFDGRAYVDGKLVAEAELMAAA 131
PRK13188 PRK13188
bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R) ...
 2-143 3.03e-52

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: 171.65  E-value: 3.03e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511454959   2 NQET-LEAQEIQAILPHRYPMLMVDRVLDLKPgESVVAQKNVSINEQIFQGHFPGNPIFPGVLQIEAMAQAGAIALLS-M 79
Cdd:PRK13188 316 NKEPiLDINRIMKILPHRYPFLLVDKIIELGD-TKIVGIKNVTMNEPFFQGHFPGNPVMPGVLQIEAMAQTGGILVLNtV 394

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 511454959  80 PDFKGKTAYLGGIKKAKFRHMVRPGDVLRIEVTLEKLIDNaGLGK--GKIYVGENMASSADLVFAI 143
Cdd:PRK13188 395 PDPENYSTYFMKIDKVKFRQKVVPGDTLIFKVELLSPIRR-GICQmqGKAYVNGKLVCEAELMAQI 459
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 15-118 2.22e-30

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 106.21  E-value: 2.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511454959   15 LPHRYpMLMVDRVLDLKPGES------VVAQKNVSINEQIFQGHFPGNPIFPGVLQIEAMAQA-GAIALLSMPDFKGKTA 87
Cdd:pfam07977   1 LPHRY-FLMLDRVTEIDPDGGkfgkgyIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLmGFYAIWSGGGEGRGRA 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 511454959   88 ylGGIKKAKFRHMVRPGD-VLRIEVTLEKLID 118
Cdd:pfam07977  80 --RGVDEVKFRGQVTPGDkQLRYEVEIKKIIE 109
FabA cd01287
FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the ...
 20-134 1.58e-11

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: 58.04  E-value: 1.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511454959  20 PMLMVDRVLDLKPGES------VVAQKNVSINEQIFQGHFPGNPIFPGVLQIEAMAQAGAIALLSM--------PDFKGK 85
Cdd:cd01287    7 QLLMLDRVTEIDPGGGtfglgyLRAEKDIDPDDWFFPCHFHGDPVMPGSLGLEAMIQLLQFYLIWLglgtgvdnPRFQGA 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 511454959  86 TaylGGIKKAKFRHMVRPGD-VLRIEVTLEKLIDNAGL------------GKgKIYVGENMA 134
Cdd:cd01287   87 P---GGPGEWKYRGQITPHNkKVTYEVHIKEVGRDGPRpyiiadaslwvdGL-RIYEAKDIA 144
COG4706 COG4706
Predicted 3-hydroxylacyl-ACP dehydratase, HotDog domain [Lipid transport and metabolism];
5-139 1.54e-10

Predicted 3-hydroxylacyl-ACP dehydratase, HotDog domain [Lipid transport and metabolism];


Pssm-ID: 443741  Cd Length: 149  Bit Score: 55.64  E-value: 1.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511454959   5 TLEAQEIQAILPHRYPMLMVDRVLDLKPgESVVAQKNVSineqifqghfPGNP-----IFPGVLQIEAMAQA-GAIALLS 78
Cdd:COG4706    4 TLDRPPIAALIPHRGPMCLLDRVLAWDE-ESAVAEVTIR----------PDNPfrddgGLPAWVGIEYMAQAvAAHGGLL 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 511454959  79 MPDfKGKTA---YLGGIKKAKFRHMV-RPGDVLRIEVTLEKLIDNAGLGKGKIYVGENMASSADL 139
Cdd:COG4706   73 ARA-AGEPPrlgFLLGVRKVELHVPRfPVGETLRIEAERLLQDEGLGLFECRIRAGGELLASGRL 136
PRK05174 PRK05174
bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase;
20-103 5.46e-07

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


Pssm-ID: 179953  Cd Length: 172  Bit Score: 46.36  E-value: 5.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511454959  20 PMLMVDRVLDL--KPGE----SVVAQKNVSINEQIFQGHFPGNPIFPGVLQIEAMAQagaiallsMPDFkgktaYLG--- 90
Cdd:PRK05174  33 PMLMMDRITEIseTGGEfgkgYIVAELDINPDLWFFGCHFIGDPVMPGCLGLDAMWQ--------LVGF-----YLGwlg 99

                         90       100
                 ....*....|....*....|.
gi 511454959  91 --------GIKKAKFRHMVRP 103
Cdd:PRK05174 100 gpgkgralGVGEVKFTGQVLP 120
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 47-131 1.22e-06

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: 44.00  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511454959  47 QIFQGHFPGNPIFPGVLQIEAMAQAGAIALLSMpDFKGKTAYLGGIKkAKFRHMVRPGDVLRIEVTLEKLIDNAGLGKGK 126
Cdd:cd03440    6 TVTPEDIDGGGIVHGGLLLALADEAAGAAAARL-GGRGLGAVTLSLD-VRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVE 83


                 ....*
gi 511454959 127 IYVGE 131
Cdd:cd03440   84 VRNED 88
FabA_like cd01289
Domain of unknown function, appears to be related to a diverse group of beta-hydroxydecanoyl ...
 11-123 7.73e-05

Domain of unknown function, appears to be related to a diverse group of beta-hydroxydecanoyl ACP dehydratases (FabA) and beta-hydroxyacyl ACP dehydratases (FabZ). This group appears to lack the conserved active site histidine of FabA and FabZ.


Pssm-ID: 238616  Cd Length: 138  Bit Score: 39.94  E-value: 7.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511454959  11 IQAILPHRYPMLMVDRVLDLKPgESVVAQknVSINEqifQGHFP--GNPIFPGVLQIEAMAQAGAI--ALLSMPdfKGKT 86
Cdd:cd01289    3 IAALIPHDGPMCLLDRVISWDD-DSIHCR--ATVHP---DPLFPlrAHGRLPAWVGIEYMAQAIAAhgGLLARQ--QGNP 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 511454959  87 A---YLGGIKKAKFRHMVRP-GDVLRIEVTlEKLIDNAGLG 123
Cdd:cd01289   75 PrpgFLLGSRKYEAHVDRFDlGSTLLIVVA-ELLQGDSGLG 114
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 50-123 4.10e-04

(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl CoA to (R)-3-hydroxyacyl-CoA as part of the PHA (polyhydroxyalkanoate) biosynthetic pathway. The structure of the monomer includes a five-strand antiparallel beta-sheet wrapped around a central alpha helix, referred to as a hot dog fold. The active site lies within a substrate-binding tunnel formed by the homodimer. Other enzymes with this fold include MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit.


Pssm-ID: 239525 [Multi-domain]  Cd Length: 127  Bit Score: 38.01  E-value: 4.10e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511454959  50 QGHFPGnPIFPGvlqieaMAQAGAIALLSMPDFKGKTAYLGGIKKAKFRHMVRPGDVLRIEVTLEKLIDNAGLG 123
Cdd:cd03441   37 AAGFGG-RIAHG------MLTLSLASGLLVQWLPGTDGANLGSQSVRFLAPVFPGDTLRVEVEVLGKRPSKGRG 103
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
50-123 2.93e-03

Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 35.63  E-value: 2.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511454959  50 QGHFPGnPIFPGVLqieAMAQAGAialLSMPDFKGKTAYLGGIKKAKFRHMVRPGDVLRIEVTLEKLIDNAGLG 123
Cdd:COG2030   45 ATGFGG-RIAHGML---TLSLASG---LLVDDLPGTAVANLGLQEVRFLRPVRVGDTLRARVEVLEKRESKSRG 111
 
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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