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Conserved domains on  [gi|999847596|gb|AMK98967|]
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3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ [Escherichia coli str. K-12 substr. MG1655]

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

CATH:  3.10.129.10
EC:  4.2.1.59
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;
2-150 1.41e-93

3-hydroxyacyl-ACP dehydratase FabZ;


:

Pssm-ID: 234568  Cd Length: 147  Bit Score: 266.98  E-value: 1.41e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999847596   2 TTNTHTLQIEEILELLPHRFPFLLVDRVLDFEEGRFLRAVKNVSVNEPFFQGHFPGKPIFPGVLILEAMAQATGILAFKS 81
Cdd:PRK00006   1 TTETMMLDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 999847596  82 VGklEPGELYYFAGIDEARFKRPVVPGDQMIMEVTFEKTRRGLTRFKGVALVDGKVVCEATMMCARSRE 150
Cdd:PRK00006  81 EE--NKGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRDK 147
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
2-150 1.41e-93

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 266.98  E-value: 1.41e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999847596   2 TTNTHTLQIEEILELLPHRFPFLLVDRVLDFEEGRFLRAVKNVSVNEPFFQGHFPGKPIFPGVLILEAMAQATGILAFKS 81
Cdd:PRK00006   1 TTETMMLDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 999847596  82 VGklEPGELYYFAGIDEARFKRPVVPGDQMIMEVTFEKTRRGLTRFKGVALVDGKVVCEATMMCARSRE 150
Cdd:PRK00006  81 EE--NKGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRDK 147
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 10-146 3.44e-76

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: 222.96  E-value: 3.44e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999847596   10 IEEILELLPHRFPFLLVDRVLDFEEGRFLRAVKNVSVNEPFFQGHFPGKPIFPGVLILEAMAQATGILAFKSVGKLEP-G 88
Cdd:TIGR01750   2 IQDIMELLPHRYPFLLVDRILELEPGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILSLGGEKGkG 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 999847596   89 ELYYFAGIDEARFKRPVVPGDQMIMEVTFEKTRRGLTRFKGVALVDGKVVCEATMMCA 146
Cdd:TIGR01750  82 KLVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIMFA 139
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 10-147 7.21e-76

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: 221.99  E-value: 7.21e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999847596  10 IEEILELLPHRFPFLLVDRVLDFEEGRFLRAVKNVSVNEPFFQGHFPGKPIFPGVLILEAMAQATGILAFKSVGKLEPGE 89
Cdd:COG0764    1 IEEILALLPHRYPFLLVDRVLEIDPGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEGLEGKGR 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 999847596  90 LYYFAGIDEARFKRPVVPGDQMIMEVTFEKTRRGLTRFKGVALVDGKVVCEATMMCAR 147
Cdd:COG0764   81 LVYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFAL 138
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 17-146 5.94e-75

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: 219.34  E-value: 5.94e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999847596  17 LPHRFPFLLVDRVLDFEEGRFLRAVKNVSVNEPFFQGHFPGKPIFPGVLILEAMAQATGILAFKSVGKLEpGELYYFAGI 96
Cdd:cd01288    1 LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLEDFE-GKLVYFAGI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 999847596  97 DEARFKRPVVPGDQMIMEVTFEKTRRGLTRFKGVALVDGKVVCEATMMCA 146
Cdd:cd01288   80 DKARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELMFA 129
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 17-141 1.31e-45

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 145.11  E-value: 1.31e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999847596   17 LPHRfPFLLVDRVLDFEEG------RFLRAVKNVSVNEPFFQGHFPGKPIFPGVLILEAMAQATGILAFKSVGKLEPGEL 90
Cdd:pfam07977   1 LPHR-YFLMLDRVTEIDPDggkfgkGYIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWSGGGEGRGRA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 999847596   91 yyfAGIDEARFKRPVVPGD-QMIMEVTFEKT---RRGLTRFKGVALVDGKVVCEA 141
Cdd:pfam07977  80 ---RGVDEVKFRGQVTPGDkQLRYEVEIKKIiegRRGIGIADGRALVDGKVVYEA 131
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
2-150 1.41e-93

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 266.98  E-value: 1.41e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999847596   2 TTNTHTLQIEEILELLPHRFPFLLVDRVLDFEEGRFLRAVKNVSVNEPFFQGHFPGKPIFPGVLILEAMAQATGILAFKS 81
Cdd:PRK00006   1 TTETMMLDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKS 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 999847596  82 VGklEPGELYYFAGIDEARFKRPVVPGDQMIMEVTFEKTRRGLTRFKGVALVDGKVVCEATMMCARSRE 150
Cdd:PRK00006  81 EE--NKGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRDK 147
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 10-146 3.44e-76

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: 222.96  E-value: 3.44e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999847596   10 IEEILELLPHRFPFLLVDRVLDFEEGRFLRAVKNVSVNEPFFQGHFPGKPIFPGVLILEAMAQATGILAFKSVGKLEP-G 88
Cdd:TIGR01750   2 IQDIMELLPHRYPFLLVDRILELEPGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILSLGGEKGkG 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 999847596   89 ELYYFAGIDEARFKRPVVPGDQMIMEVTFEKTRRGLTRFKGVALVDGKVVCEATMMCA 146
Cdd:TIGR01750  82 KLVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIMFA 139
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 10-147 7.21e-76

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: 221.99  E-value: 7.21e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999847596  10 IEEILELLPHRFPFLLVDRVLDFEEGRFLRAVKNVSVNEPFFQGHFPGKPIFPGVLILEAMAQATGILAFKSVGKLEPGE 89
Cdd:COG0764    1 IEEILALLPHRYPFLLVDRVLEIDPGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEGLEGKGR 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 999847596  90 LYYFAGIDEARFKRPVVPGDQMIMEVTFEKTRRGLTRFKGVALVDGKVVCEATMMCAR 147
Cdd:COG0764   81 LVYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFAL 138
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 17-146 5.94e-75

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: 219.34  E-value: 5.94e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999847596  17 LPHRFPFLLVDRVLDFEEGRFLRAVKNVSVNEPFFQGHFPGKPIFPGVLILEAMAQATGILAFKSVGKLEpGELYYFAGI 96
Cdd:cd01288    1 LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLEDFE-GKLVYFAGI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 999847596  97 DEARFKRPVVPGDQMIMEVTFEKTRRGLTRFKGVALVDGKVVCEATMMCA 146
Cdd:cd01288   80 DKARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELMFA 129
PRK13188 PRK13188
bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R) ...
 8-144 2.36e-62

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: 198.23  E-value: 2.36e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999847596   8 LQIEEILELLPHRFPFLLVDRVLDFEEGRfLRAVKNVSVNEPFFQGHFPGKPIFPGVLILEAMAQATGILAFKSVGklEP 87
Cdd:PRK13188 321 LDINRIMKILPHRYPFLLVDKIIELGDTK-IVGIKNVTMNEPFFQGHFPGNPVMPGVLQIEAMAQTGGILVLNTVP--DP 397

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 999847596  88 GE-LYYFAGIDEARFKRPVVPGDQMIMEVTF-EKTRRGLTRFKGVALVDGKVVCEATMM 144
Cdd:PRK13188 398 ENySTYFMKIDKVKFRQKVVPGDTLIFKVELlSPIRRGICQMQGKAYVNGKLVCEAELM 456
FabA_FabZ cd00493
FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct ...
 18-146 6.52e-60

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: 181.33  E-value: 6.52e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999847596  18 PHRFPFLLVDRVLDFEEGRFLRAVKNVSVNEPFFQGHFPGKPIFPGVLILEAMAQATGILAFKS-VGKLEPGELYYFAGI 96
Cdd:cd00493    1 PHRYPMLLVDRVLEIDPGGRIVAEKNVTPNEPFFQGHFPGDPVMPGVLGIEAMAQAAAALAGLLgLGKGNPPRLGYLAGV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 999847596  97 DEARFKRPVVPGDQMIMEVTFEKTRRGLTRFKGVALVDGKVVCEATMMCA 146
Cdd:cd00493   81 RKVKFRGPVLPGDTLTLEVELLKVRRGLGKFDGRAYVDGKLVAEAELMAA 130
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 17-141 1.31e-45

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 145.11  E-value: 1.31e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999847596   17 LPHRfPFLLVDRVLDFEEG------RFLRAVKNVSVNEPFFQGHFPGKPIFPGVLILEAMAQATGILAFKSVGKLEPGEL 90
Cdd:pfam07977   1 LPHR-YFLMLDRVTEIDPDggkfgkGYIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWSGGGEGRGRA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 999847596   91 yyfAGIDEARFKRPVVPGD-QMIMEVTFEKT---RRGLTRFKGVALVDGKVVCEA 141
Cdd:pfam07977  80 ---RGVDEVKFRGQVTPGDkQLRYEVEIKKIiegRRGIGIADGRALVDGKVVYEA 131
COG4706 COG4706
Predicted 3-hydroxylacyl-ACP dehydratase, HotDog domain [Lipid transport and metabolism];
7-143 4.78e-13

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


Pssm-ID: 443741  Cd Length: 149  Bit Score: 62.19  E-value: 4.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999847596   7 TLQIEEILELLPHRFPFLLVDRVLDFEEGRfLRAVKNVSVNEPFFQGHFpgkpiFPGVLILEAMAQA----TGILAFKSV 82
Cdd:COG4706    4 TLDRPPIAALIPHRGPMCLLDRVLAWDEES-AVAEVTIRPDNPFRDDGG-----LPAWVGIEYMAQAvaahGGLLARAAG 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 999847596  83 GKLEPGelyYFAGIDEARFKRPVVPGDQMImEVTFEKTRR--GLTRFKGVALVDGKVVCEATM 143
Cdd:COG4706   78 EPPRLG---FLLGVRKVELHVPRFPVGETL-RIEAERLLQdeGLGLFECRIRAGGELLASGRL 136
FabA cd01287
FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the ...
 22-151 5.64e-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: 56.88  E-value: 5.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999847596  22 PFLLVDRVL--DFEEGRF----LRAVKNVSVNEPFFQGHFPGKPIFPGVLILEAMAQATGILAFKSVGKLEPGELYYFAG 95
Cdd:cd01287    7 QLLMLDRVTeiDPGGGTFglgyLRAEKDIDPDDWFFPCHFHGDPVMPGSLGLEAMIQLLQFYLIWLGLGTGVDNPRFQGA 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 999847596  96 IDEA---RFKRPVVPGD-QMIMEVTFEKTRRGLTRFKGVA----LVDGKVVCEATMMCARSREA 151
Cdd:cd01287   87 PGGPgewKYRGQITPHNkKVTYEVHIKEVGRDGPRPYIIAdaslWVDGLRIYEAKDIAVRLVEA 150
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 57-146 8.46e-09

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: 50.17  E-value: 8.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999847596  57 GKPIFPGVLILEAMAQATGILAFKSVGklePGELYYFAGIDeARFKRPVVPGDQMIMEVTFEKTRRGLTRFKGVALV-DG 135
Cdd:cd03440   14 GGGIVHGGLLLALADEAAGAAAARLGG---RGLGAVTLSLD-VRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNeDG 89

                         90
                 ....*....|.
gi 999847596 136 KVVCEATMMCA 146
Cdd:cd03440   90 KLVATATATFV 100
PRK05174 PRK05174
bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase;
22-142 1.08e-07

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


Pssm-ID: 179953  Cd Length: 172  Bit Score: 48.67  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999847596  22 PFLLVDRVLDFEE--GRF----LRAVKNVSVNEPFFQGHFPGKPIFPGVLILEAMAQATGI-LAFK-SVGK---Lepgel 90
Cdd:PRK05174  33 PMLMMDRITEISEtgGEFgkgyIVAELDINPDLWFFGCHFIGDPVMPGCLGLDAMWQLVGFyLGWLgGPGKgraL----- 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 999847596  91 yyfaGIDEARFKRPVVPGDQMIM-EVTFEKT-RRGLTRfkGVA----LVDGKVVCEAT 142
Cdd:PRK05174 108 ----GVGEVKFTGQVLPTAKKVTyEIDIKRViNRKLVM--GIAdgrvLVDGEEIYTAK 159
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
57-151 3.13e-06

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 44.11  E-value: 3.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999847596  57 GKPIFPGVLileamaqaTGILAFKSVGKLEPGELYYFAGIDEARFKRPVVPGDQMIMEVT----FEKTRRGLTRFKGVAL 132
Cdd:COG2030   49 GGRIAHGML--------TLSLASGLLVDDLPGTAVANLGLQEVRFLRPVRVGDTLRARVEvlekRESKSRGIVTLRTTVT 120

                         90       100
                 ....*....|....*....|
gi 999847596 133 -VDGKVVCEATMMCARSREA 151
Cdd:COG2030  121 nQDGEVVLTGEATVLVPRRP 140
FabA_like cd01289
Domain of unknown function, appears to be related to a diverse group of beta-hydroxydecanoyl ...
 13-90 3.10e-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: 41.10  E-value: 3.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999847596  13 ILELLPHRFPFLLVDRVLDFEEGRfLRAVKNVSVNEPFFQGHFPGKPIFPGVlilEAMAQAT----GILAFKSVGKLEPG 88
Cdd:cd01289    3 IAALIPHDGPMCLLDRVISWDDDS-IHCRATVHPDPLFPLRAHGRLPAWVGI---EYMAQAIaahgGLLARQQGNPPRPG 78


                 ..
gi 999847596  89 EL 90
Cdd:cd01289   79 FL 80
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 56-142 9.16e-05

(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: 39.94  E-value: 9.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999847596  56 PGKPIFPGVLileamaqaTGILAFKSVGKLEPGELYYFAGIDEARFKRPVVPGDQMIMEVT----FEKTRRGLTRFKGVA 131
Cdd:cd03441   40 FGGRIAHGML--------TLSLASGLLVQWLPGTDGANLGSQSVRFLAPVFPGDTLRVEVEvlgkRPSKGRGVVTVRTEA 111

                         90
                 ....*....|..
gi 999847596 132 LV-DGKVVCEAT 142
Cdd:cd03441  112 RNqGGEVVLSGE 123
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 95-140 1.87e-04

YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown function. YdeM has sequence similarity to the hot-dog fold of (R)-specific enoyl-CoA hydratase. Other enzymes with this fold include the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.


Pssm-ID: 239538 [Multi-domain]  Cd Length: 140  Bit Score: 39.09  E-value: 1.87e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 999847596  95 GIDEARFKRPVVPGDQM-----IMEVTFEKTR--RGLTRFKGVALV-DGKVVCE 140
Cdd:cd03454   79 GIDELRWPRPVRPGDTLsveveVLDKRPSRSRpdRGIVTLRSETLNqRGEVVLT 132
 
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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