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Conserved domains on  [gi|18399910|ref|NP_565528|]
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Thioesterase superfamily protein [Arabidopsis thaliana]

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;
73-213 2.82e-81

3-hydroxyacyl-ACP dehydratase FabZ;


:

Pssm-ID: 234568  Cd Length: 147  Bit Score: 238.86  E-value: 2.82e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399910   73 PTVMDINQIREILPHRFPFLLVDRVIEYTPGVSAVAIKNVTINDNFFPGHFPERPIMPGVLMIEAMAQVGGIVMLQ-PEV 151
Cdd:PRK00006   4 TMMLDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKsEEN 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18399910  152 GGSQdnFFFAGIDKVRFRKPVIAGDTLVMRMTLLKfQKRfGLAKMEGKAYVGGALVCEGEFM 213
Cdd:PRK00006  84 KGKL--VYFAGIDKARFKRPVVPGDQLILEVELLK-QRR-GIWKFKGVATVDGKLVAEAELM 141
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
73-213 2.82e-81

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 238.86  E-value: 2.82e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399910   73 PTVMDINQIREILPHRFPFLLVDRVIEYTPGVSAVAIKNVTINDNFFPGHFPERPIMPGVLMIEAMAQVGGIVMLQ-PEV 151
Cdd:PRK00006   4 TMMLDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKsEEN 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18399910  152 GGSQdnFFFAGIDKVRFRKPVIAGDTLVMRMTLLKfQKRfGLAKMEGKAYVGGALVCEGEFM 213
Cdd:PRK00006  84 KGKL--VYFAGIDKARFKRPVVPGDQLILEVELLK-QRR-GIWKFKGVATVDGKLVAEAELM 141
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 85-217 1.42e-71

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: 213.94  E-value: 1.42e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399910  85 LPHRFPFLLVDRVIEYTPGVSAVAIKNVTINDNFFPGHFPERPIMPGVLMIEAMAQVGGIVMLQPEVGGSQDNFFFAGID 164
Cdd:cd01288   1 LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLEDFEGKLVYFAGID 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 18399910 165 KVRFRKPVIAGDTLVMRMTLLKFQKRFGlaKMEGKAYVGGALVCEGEFMMVSA 217
Cdd:cd01288  81 KARFRKPVVPGDQLILEVELLKLRRGIG--KFKGKAYVDGKLVAEAELMFAIA 131
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 78-215 1.32e-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: 204.27  E-value: 1.32e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399910  78 INQIREILPHRFPFLLVDRVIEYTPGVSAVAIKNVTINDNFFPGHFPERPIMPGVLMIEAMAQVGGIVMLQPEVGGSQDN 157
Cdd:COG0764   1 IEEILALLPHRYPFLLVDRVLEIDPGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEGLEGKGR 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18399910 158 -FFFAGIDKVRFRKPVIAGDTLVMRMTLLKFqkRFGLAKMEGKAYVGGALVCEGEFMMV 215
Cdd:COG0764  81 lVYFLGIDKVKFRGPVVPGDTLTLEVEIKRV--RRGIGKADGKATVDGKLVAEAELTFA 137
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 77-213 6.88e-64

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: 194.84  E-value: 6.88e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399910    77 DINQIREILPHRFPFLLVDRVIEYTPGVSAVAIKNVTINDNFFPGHFPERPIMPGVLMIEAMAQVGGIVMLQ--PEVGGS 154
Cdd:TIGR01750   1 DIQDIMELLPHRYPFLLVDRILELEPGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILslGGEKGK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18399910   155 QDNFFFAGIDKVRFRKPVIAGDTLVMRMTLLKfqKRFGLAKMEGKAYVGGALVCEGEFM 213
Cdd:TIGR01750  81 GKLVYFAGIDKARFRRPVVPGDQLILHVEFLK--KRRGIGKFKGEATVDGKVVAEAEIM 137
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 85-211 6.17e-36

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 123.16  E-value: 6.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399910    85 LPHRfPFLLVDRVIEYTP-GVSA-----VAIKNVTINDNFFPGHFPERPIMPGVLMIEAMAQVGGIVMLQPEVGGSQDNf 158
Cdd:pfam07977   1 LPHR-YFLMLDRVTEIDPdGGKFgkgyiVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWSGGGEGRGR- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18399910   159 fFAGIDKVRFRKPVIAGD-TLVMRMTLLKF-QKRFGLAKMEGKAYVGGALVCEGE 211
Cdd:pfam07977  79 -ARGVDEVKFRGQVTPGDkQLRYEVEIKKIiEGRRGIGIADGRALVDGKVVYEAK 132
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
73-213 2.82e-81

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 238.86  E-value: 2.82e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399910   73 PTVMDINQIREILPHRFPFLLVDRVIEYTPGVSAVAIKNVTINDNFFPGHFPERPIMPGVLMIEAMAQVGGIVMLQ-PEV 151
Cdd:PRK00006   4 TMMLDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKsEEN 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18399910  152 GGSQdnFFFAGIDKVRFRKPVIAGDTLVMRMTLLKfQKRfGLAKMEGKAYVGGALVCEGEFM 213
Cdd:PRK00006  84 KGKL--VYFAGIDKARFKRPVVPGDQLILEVELLK-QRR-GIWKFKGVATVDGKLVAEAELM 141
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 85-217 1.42e-71

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: 213.94  E-value: 1.42e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399910  85 LPHRFPFLLVDRVIEYTPGVSAVAIKNVTINDNFFPGHFPERPIMPGVLMIEAMAQVGGIVMLQPEVGGSQDNFFFAGID 164
Cdd:cd01288   1 LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLEDFEGKLVYFAGID 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 18399910 165 KVRFRKPVIAGDTLVMRMTLLKFQKRFGlaKMEGKAYVGGALVCEGEFMMVSA 217
Cdd:cd01288  81 KARFRKPVVPGDQLILEVELLKLRRGIG--KFKGKAYVDGKLVAEAELMFAIA 131
PRK13188 PRK13188
bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R) ...
 70-213 8.10e-68

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: 215.18  E-value: 8.10e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399910   70 PAFPTVMDINQIREILPHRFPFLLVDRVIEYTPgVSAVAIKNVTINDNFFPGHFPERPIMPGVLMIEAMAQVGGIVMLQ- 148
Cdd:PRK13188 315 PNKEPILDINRIMKILPHRYPFLLVDKIIELGD-TKIVGIKNVTMNEPFFQGHFPGNPVMPGVLQIEAMAQTGGILVLNt 393

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18399910  149 -PEVGGSQDnfFFAGIDKVRFRKPVIAGDTLVMRMTLLKFQKRfGLAKMEGKAYVGGALVCEGEFM 213
Cdd:PRK13188 394 vPDPENYST--YFMKIDKVKFRQKVVPGDTLIFKVELLSPIRR-GICQMQGKAYVNGKLVCEAELM 456
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 78-215 1.32e-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: 204.27  E-value: 1.32e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399910  78 INQIREILPHRFPFLLVDRVIEYTPGVSAVAIKNVTINDNFFPGHFPERPIMPGVLMIEAMAQVGGIVMLQPEVGGSQDN 157
Cdd:COG0764   1 IEEILALLPHRYPFLLVDRVLEIDPGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEGLEGKGR 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18399910 158 -FFFAGIDKVRFRKPVIAGDTLVMRMTLLKFqkRFGLAKMEGKAYVGGALVCEGEFMMV 215
Cdd:COG0764  81 lVYFLGIDKVKFRGPVVPGDTLTLEVEIKRV--RRGIGKADGKATVDGKLVAEAELTFA 137
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 77-213 6.88e-64

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: 194.84  E-value: 6.88e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399910    77 DINQIREILPHRFPFLLVDRVIEYTPGVSAVAIKNVTINDNFFPGHFPERPIMPGVLMIEAMAQVGGIVMLQ--PEVGGS 154
Cdd:TIGR01750   1 DIQDIMELLPHRYPFLLVDRILELEPGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILslGGEKGK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18399910   155 QDNFFFAGIDKVRFRKPVIAGDTLVMRMTLLKfqKRFGLAKMEGKAYVGGALVCEGEFM 213
Cdd:TIGR01750  81 GKLVYFAGIDKARFRRPVVPGDQLILHVEFLK--KRRGIGKFKGEATVDGKVVAEAEIM 137
FabA_FabZ cd00493
FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct ...
 86-213 3.74e-56

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: 174.78  E-value: 3.74e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399910  86 PHRFPFLLVDRVIEYTPGVSAVAIKNVTINDNFFPGHFPERPIMPGVLMIEAMAQVGGIVMLQPEVGGSQDNF--FFAGI 163
Cdd:cd00493   1 PHRYPMLLVDRVLEIDPGGRIVAEKNVTPNEPFFQGHFPGDPVMPGVLGIEAMAQAAAALAGLLGLGKGNPPRlgYLAGV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 18399910 164 DKVRFRKPVIAGDTLVMRMTLLKFqkRFGLAKMEGKAYVGGALVCEGEFM 213
Cdd:cd00493  81 RKVKFRGPVLPGDTLTLEVELLKV--RRGLGKFDGRAYVDGKLVAEAELM 128
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 85-211 6.17e-36

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 123.16  E-value: 6.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399910    85 LPHRfPFLLVDRVIEYTP-GVSA-----VAIKNVTINDNFFPGHFPERPIMPGVLMIEAMAQVGGIVMLQPEVGGSQDNf 158
Cdd:pfam07977   1 LPHR-YFLMLDRVTEIDPdGGKFgkgyiVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWSGGGEGRGR- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18399910   159 fFAGIDKVRFRKPVIAGD-TLVMRMTLLKF-QKRFGLAKMEGKAYVGGALVCEGE 211
Cdd:pfam07977  79 -ARGVDEVKFRGQVTPGDkQLRYEVEIKKIiEGRRGIGIADGRALVDGKVVYEAK 132
FabA cd01287
FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the ...
 90-184 2.21e-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: 59.58  E-value: 2.21e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399910  90 PFLLVDRVIEYTPGVS------AVAIKNVTINDNFFPGHFPERPIMPGVLMIEAMAQVGGIVMLQPEVGGSQDNFFFAGI 163
Cdd:cd01287   7 QLLMLDRVTEIDPGGGtfglgyLRAEKDIDPDDWFFPCHFHGDPVMPGSLGLEAMIQLLQFYLIWLGLGTGVDNPRFQGA 86

                        90       100
                ....*....|....*....|....*.
gi 18399910 164 D----KVRFRKPVIAGD-TLVMRMTL 184
Cdd:cd01287  87 PggpgEWKYRGQITPHNkKVTYEVHI 112
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 106-215 3.17e-10

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: 55.17  E-value: 3.17e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399910 106 AVAIKNVTINDNFFPGHfperpiMPGVLMIEAMAQVGGIVMLqpEVGGSQDNFFFAGIDkVRFRKPVIAGDTLVMRMTLL 185
Cdd:cd03440   1 FVLRLTVTPEDIDGGGI------VHGGLLLALADEAAGAAAA--RLGGRGLGAVTLSLD-VRFLRPVRPGDTLTVEAEVV 71

                        90       100       110
                ....*....|....*....|....*....|.
gi 18399910 186 KFQKRFglAKMEGKAYVG-GALVCEGEFMMV 215
Cdd:cd03440  72 RVGRSS--VTVEVEVRNEdGKLVATATATFV 100
COG4706 COG4706
Predicted 3-hydroxylacyl-ACP dehydratase, HotDog domain [Lipid transport and metabolism];
73-211 3.06e-08

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


Pssm-ID: 443741  Cd Length: 149  Bit Score: 51.02  E-value: 3.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399910  73 PTVMDINQIREILPHRFPFLLVDRVIEYTPGvSAVAIknVTINDN--FFPGHFperpiMPGVLMIEAMAQ-VGGIVMLQ- 148
Cdd:COG4706   2 NPTLDRPPIAALIPHRGPMCLLDRVLAWDEE-SAVAE--VTIRPDnpFRDDGG-----LPAWVGIEYMAQaVAAHGGLLa 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399910 149 ------PEVGgsqdnfFFAGIDKVRFRKPVIA-GDTLVMRMTLLkfQKRFGLAKMEGKAYVGGALVCEGE 211
Cdd:COG4706  74 raagepPRLG------FLLGVRKVELHVPRFPvGETLRIEAERL--LQDEGLGLFECRIRAGGELLASGR 135
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
117-215 1.57e-06

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 46.03  E-value: 1.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399910 117 NFFPGHFPE---------RPIMPGVLmieAMAQVGGivMLQPEVGGSQdnFFFAGIDKVRFRKPVIAGDTLVMRMTLL-- 185
Cdd:COG2030  32 DPNPIHLDEeaaaatgfgGRIAHGML---TLSLASG--LLVDDLPGTA--VANLGLQEVRFLRPVRVGDTLRARVEVLek 104

                        90       100       110
                ....*....|....*....|....*....|.
gi 18399910 186 KFQKRFGLAKMEGKAY-VGGALVCEGEFMMV 215
Cdd:COG2030 105 RESKSRGIVTLRTTVTnQDGEVVLTGEATVL 135
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 117-211 7.27e-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: 41.10  E-value: 7.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399910 117 NFFPGHF---------PERPIMPGVLmieAMAQVGGIVmLQPEVGGSQDNFffaGIDKVRFRKPVIAGDTLVMRMTLLKF 187
Cdd:cd03441  24 DPNPIHVdpeyakaagFGGRIAHGML---TLSLASGLL-VQWLPGTDGANL---GSQSVRFLAPVFPGDTLRVEVEVLGK 96

                        90       100
                ....*....|....*....|....*..
gi 18399910 188 Q--KRFGLAKMEGKAYV-GGALVCEGE 211
Cdd:cd03441  97 RpsKGRGVVTVRTEARNqGGEVVLSGE 123
PRK05174 PRK05174
bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase;
90-142 6.02e-04

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


Pssm-ID: 179953  Cd Length: 172  Bit Score: 39.04  E-value: 6.02e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18399910   90 PFLLVDRVIEYTPGVSA------VAIKNVTINDNFFPGHFPERPIMPGVLMIEAMAQ-VG 142
Cdd:PRK05174  33 PMLMMDRITEISETGGEfgkgyiVAELDINPDLWFFGCHFIGDPVMPGCLGLDAMWQlVG 92
FabA_like cd01289
Domain of unknown function, appears to be related to a diverse group of beta-hydroxydecanoyl ...
 80-140 6.18e-04

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: 38.78  E-value: 6.18e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18399910  80 QIREILPHRFPFLLVDRVIEYTPGvSAVAIKNVTINDNFFPghfPERPIMPGVLMIEAMAQ 140
Cdd:cd01289   2 WIAALIPHDGPMCLLDRVISWDDD-SIHCRATVHPDPLFPL---RAHGRLPAWVGIEYMAQ 58
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 160-212 1.69e-03

MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but without the N-terminal PutA domain. This protein family has a hot-dog fold similar to that of (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.


Pssm-ID: 239530 [Multi-domain]  Cd Length: 140  Bit Score: 37.28  E-value: 1.69e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 18399910 160 FAGIDKVRFRKPVIAGDTLVMRMTLL----KFQKRFGLAKMEGKAY-VGGALVCEGEF 212
Cdd:cd03446  79 FYGIDNLRFLNPVFIGDTIRAEAEVVekeeKDGEDAGVVTRRIEVVnQRGEVVQSGEM 136
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 167-212 2.57e-03

(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. (R)-hydratase contains a hot-dog fold similar to those of thioesterase II, and beta-hydroxydecanoyl-ACP dehydratase, MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit. The active site lies within a substrate-binding tunnel formed by the (R)-hydratase homodimer. A subset of the bacterial (R)-hydratases contain a C-terminal phosphotransacetylase (PTA) domain.


Pssm-ID: 239533 [Multi-domain]  Cd Length: 128  Bit Score: 36.75  E-value: 2.57e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 18399910 167 RFRKPVIAGDTLVMRMTLLKFQKRFGLAKMEGKAYVG-GALVCEGEF 212
Cdd:cd03449  78 RFLRPVFIGDTVTATVTVTEKREDKKRVTLETVCTNQnGEVVIEGEA 124
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 162-211 3.49e-03

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: 36.39  E-value: 3.49e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 18399910 162 GIDKVRFRKPVIAGDTLVMRMTLLKfqKRF-------GLAKMEGKAYV-GGALVCEGE 211
Cdd:cd03454  79 GIDELRWPRPVRPGDTLSVEVEVLD--KRPsrsrpdrGIVTLRSETLNqRGEVVLTFE 134
PRK04424 PRK04424
transcription factor FapR;
162-216 4.89e-03

transcription factor FapR;


Pssm-ID: 179847 [Multi-domain]  Cd Length: 185  Bit Score: 36.72  E-value: 4.89e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 18399910  162 GIDKVRFRKPVIAGDTLVMRMTLLKfqKRFGLAKMEGKAYVGGALVCEGEFMMVS 216
Cdd:PRK04424 129 GVANIRFKRPVKLGERVVAKAEVVR--KKGNKYIVEVKSYVGDELVFRGKFIMYR 181
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 162-214 6.56e-03

FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved family of proteins found in prokaryotes and archaea but not in eukaryotes. FkbR2 has sequence similarity to (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. The function of FkbR2 is unknown.


Pssm-ID: 239535 [Multi-domain]  Cd Length: 146  Bit Score: 35.64  E-value: 6.56e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18399910 162 GIDKVRFRKPVIAGDTLVMRMTLL-----KFQKRFGLAKMEGKAY-VGGALVCEGE--FMM 214
Cdd:cd03451  82 GYDEVRFPAPVFHGDTLYAESEVLskresKSRPDAGIVTVRTVGYnQDGEPVLSFErtALV 142
 
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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