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Conserved domains on  [gi|513829095|ref|WP_016513445|]
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MULTISPECIES: 3-hydroxyacyl-ACP dehydratase FabZ [Bacillus cereus group]

Protein Classification

hotdog family protein( domain architecture ID 107)

hotdog family protein may have metabolic roles such as thioester hydrolysis in fatty acid metabolism and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hot_dog super family cl00509
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 1-152 1.82e-55

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.


The actual alignment was detected with superfamily member PRK00006:

Pssm-ID: 469797  Cd Length: 147  Bit Score: 171.07  E-value: 1.82e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829095   1 MRPVLNADQIQNILPHKWPFLFLDKVIQLEPGKSGIGIKNVTVSEPFFEGHFPNESIMPGVLIIEALAQMTAVVYVTGEL 80
Cdd:PRK00006   3 ETMMLDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSEE 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 513829095  81 AKidahgacspkidpsSYVGYLVSVRNMKFLKPVVPGDQLELHVQIGRSLGLISQVEITAYVDKKKVATGSI 152
Cdd:PRK00006  83 NK--------------GKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAEL 140
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
1-152 1.82e-55

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 171.07  E-value: 1.82e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829095   1 MRPVLNADQIQNILPHKWPFLFLDKVIQLEPGKSGIGIKNVTVSEPFFEGHFPNESIMPGVLIIEALAQMTAVVYVTGEL 80
Cdd:PRK00006   3 ETMMLDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSEE 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 513829095  81 AKidahgacspkidpsSYVGYLVSVRNMKFLKPVVPGDQLELHVQIGRSLGLISQVEITAYVDKKKVATGSI 152
Cdd:PRK00006  83 NK--------------GKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAEL 140
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 14-152 1.44e-53

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: 165.79  E-value: 1.44e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829095  14 LPHKWPFLFLDKVIQLEPGKSGIGIKNVTVSEPFFEGHFPNESIMPGVLIIEALAQMTAVVYVTGElakidahgacspkI 93
Cdd:cd01288    1 LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSL-------------E 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 513829095  94 DPSSYVGYLVSVRNMKFLKPVVPGDQLELHVQIGRSLGLISQVEITAYVDKKKVATGSI 152
Cdd:cd01288   68 DFEGKLVYFAGIDKARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAEL 126
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 8-152 2.49e-52

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: 163.06  E-value: 2.49e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829095   8 DQIQNILPHKWPFLFLDKVIQLEPGKSGIGIKNVTVSEPFFEGHFPNESIMPGVLIIEALAQMTAVvyvtgelakidaHG 87
Cdd:COG0764    2 EEILALLPHRYPFLLVDRVLEIDPGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGF------------LL 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 513829095  88 ACSPKIDPSSYVGYLVSVRNMKFLKPVVPGDQLELHVQIGRSLGLISQVEITAYVDKKKVATGSI 152
Cdd:COG0764   70 LKSEGLEGKGRLVYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAEL 134
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 9-152 1.81e-46

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: 148.23  E-value: 1.81e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829095    9 QIQNILPHKWPFLFLDKVIQLEPGKSGIGIKNVTVSEPFFEGHFPNESIMPGVLIIEALAQMTAVVYVTGELAKIdahga 88
Cdd:TIGR01750   4 DIMELLPHRYPFLLVDRILELEPGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILSLGGEK----- 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 513829095   89 cspkidPSSYVGYLVSVRNMKFLKPVVPGDQLELHVQIGRSLGLISQVEITAYVDKKKVATGSI 152
Cdd:TIGR01750  79 ------GKGKLVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEI 136
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 14-151 1.85e-25

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 94.27  E-value: 1.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829095   14 LPHKwPFLFLDKVIQLEP--GKSG----IGIKNVTVSEPFFEGHFPNESIMPGVLIIEALAQMTAV-VYVTGELAKIDAH 86
Cdd:pfam07977   1 LPHR-YFLMLDRVTEIDPdgGKFGkgyiVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFyAIWSGGGEGRGRA 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 513829095   87 GacspkidpssyvgylvSVRNMKFLKPVVPGDQ---LELHV-QIGRSLGLISQVEITAYVDKKKVATGS 151
Cdd:pfam07977  80 R----------------GVDEVKFRGQVTPGDKqlrYEVEIkKIIEGRRGIGIADGRALVDGKVVYEAK 132
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
1-152 1.82e-55

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 171.07  E-value: 1.82e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829095   1 MRPVLNADQIQNILPHKWPFLFLDKVIQLEPGKSGIGIKNVTVSEPFFEGHFPNESIMPGVLIIEALAQMTAVVYVTGEL 80
Cdd:PRK00006   3 ETMMLDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSEE 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 513829095  81 AKidahgacspkidpsSYVGYLVSVRNMKFLKPVVPGDQLELHVQIGRSLGLISQVEITAYVDKKKVATGSI 152
Cdd:PRK00006  83 NK--------------GKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAEL 140
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 14-152 1.44e-53

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: 165.79  E-value: 1.44e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829095  14 LPHKWPFLFLDKVIQLEPGKSGIGIKNVTVSEPFFEGHFPNESIMPGVLIIEALAQMTAVVYVTGElakidahgacspkI 93
Cdd:cd01288    1 LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSL-------------E 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 513829095  94 DPSSYVGYLVSVRNMKFLKPVVPGDQLELHVQIGRSLGLISQVEITAYVDKKKVATGSI 152
Cdd:cd01288   68 DFEGKLVYFAGIDKARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAEL 126
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 8-152 2.49e-52

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: 163.06  E-value: 2.49e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829095   8 DQIQNILPHKWPFLFLDKVIQLEPGKSGIGIKNVTVSEPFFEGHFPNESIMPGVLIIEALAQMTAVvyvtgelakidaHG 87
Cdd:COG0764    2 EEILALLPHRYPFLLVDRVLEIDPGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGF------------LL 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 513829095  88 ACSPKIDPSSYVGYLVSVRNMKFLKPVVPGDQLELHVQIGRSLGLISQVEITAYVDKKKVATGSI 152
Cdd:COG0764   70 LKSEGLEGKGRLVYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAEL 134
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 9-152 1.81e-46

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: 148.23  E-value: 1.81e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829095    9 QIQNILPHKWPFLFLDKVIQLEPGKSGIGIKNVTVSEPFFEGHFPNESIMPGVLIIEALAQMTAVVYVTGELAKIdahga 88
Cdd:TIGR01750   4 DIMELLPHRYPFLLVDRILELEPGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILSLGGEK----- 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 513829095   89 cspkidPSSYVGYLVSVRNMKFLKPVVPGDQLELHVQIGRSLGLISQVEITAYVDKKKVATGSI 152
Cdd:TIGR01750  79 ------GKGKLVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEI 136
FabA_FabZ cd00493
FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct ...
 15-152 3.46e-43

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: 139.34  E-value: 3.46e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829095  15 PHKWPFLFLDKVIQLEPGKSGIGIKNVTVSEPFFEGHFPNESIMPGVLIIEALAQMTAVVyvtgeLAKIDAHGACSPKId 94
Cdd:cd00493    1 PHRYPMLLVDRVLEIDPGGRIVAEKNVTPNEPFFQGHFPGDPVMPGVLGIEAMAQAAAAL-----AGLLGLGKGNPPRL- 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 513829095  95 pssyvGYLVSVRNMKFLKPVVPGDQLELHVQIGRSLGLISQVEITAYVDKKKVATGSI 152
Cdd:cd00493   75 -----GYLAGVRKVKFRGPVLPGDTLTLEVELLKVRRGLGKFDGRAYVDGKLVAEAEL 127
PRK13188 PRK13188
bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R) ...
 3-159 1.90e-41

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: 143.92  E-value: 1.90e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829095   3 PVLNADQIQNILPHKWPFLFLDKVIQLEPgKSGIGIKNVTVSEPFFEGHFPNESIMPGVLIIEALAQmTAVVYVtgeLAK 82
Cdd:PRK13188 319 PILDINRIMKILPHRYPFLLVDKIIELGD-TKIVGIKNVTMNEPFFQGHFPGNPVMPGVLQIEAMAQ-TGGILV---LNT 393

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829095  83 IDahgacspkiDPSSYVGYLVSVRNMKFLKPVVPGDQLELHVQ----IGRSlglISQVEITAYVDKKKVATGSI--QVSK 156
Cdd:PRK13188 394 VP---------DPENYSTYFMKIDKVKFRQKVVPGDTLIFKVEllspIRRG---ICQMQGKAYVNGKLVCEAELmaQIVK 461


                 ...
gi 513829095 157 RVE 159
Cdd:PRK13188 462 KKE 464
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 14-151 1.85e-25

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 94.27  E-value: 1.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829095   14 LPHKwPFLFLDKVIQLEP--GKSG----IGIKNVTVSEPFFEGHFPNESIMPGVLIIEALAQMTAV-VYVTGELAKIDAH 86
Cdd:pfam07977   1 LPHR-YFLMLDRVTEIDPdgGKFGkgyiVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFyAIWSGGGEGRGRA 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 513829095   87 GacspkidpssyvgylvSVRNMKFLKPVVPGDQ---LELHV-QIGRSLGLISQVEITAYVDKKKVATGS 151
Cdd:pfam07977  80 R----------------GVDEVKFRGQVTPGDKqlrYEVEIkKIIEGRRGIGIADGRALVDGKVVYEAK 132
FabA cd01287
FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the ...
 19-70 7.31e-06

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: 43.40  E-value: 7.31e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 513829095  19 PFLFLDKVIQLEP--GKSG----IGIKNVTVSEPFFEGHFPNESIMPGVLIIEALAQM 70
Cdd:cd01287    7 QLLMLDRVTEIDPggGTFGlgylRAEKDIDPDDWFFPCHFHGDPVMPGSLGLEAMIQL 64
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 57-154 8.17e-05

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: 39.77  E-value: 8.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829095  57 IMPGVLIIEALAQMTavvyvtgelakidahGACSPKIDPSSYVGYLVSVrNMKFLKPVVPGDQLELHVQIGRSLGLISQV 136
Cdd:cd03440   17 IVHGGLLLALADEAA---------------GAAAARLGGRGLGAVTLSL-DVRFLRPVRPGDTLTVEAEVVRVGRSSVTV 80

                         90
                 ....*....|....*...
gi 513829095 137 EITAYVDKKKVATGSIQV 154
Cdd:cd03440   81 EVEVRNEDGKLVATATAT 98
FabA_like cd01289
Domain of unknown function, appears to be related to a diverse group of beta-hydroxydecanoyl ...
 8-154 5.77e-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: 38.01  E-value: 5.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 513829095   8 DQIQNILPHKWPFLFLDKVIQLEPGKsgiGIKNVTVSEpffEGHFPNESI--MPGVLIIEALAQMTAVvyVTGELAKida 85
Cdd:cd01289    1 PWIAALIPHDGPMCLLDRVISWDDDS---IHCRATVHP---DPLFPLRAHgrLPAWVGIEYMAQAIAA--HGGLLAR--- 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 513829095  86 HGACSPKIdpssyvGYLVSVRNMKFLKPVVPGDQlELHVQIGRSL----GLiSQVEITAYVDKKKVATGSIQV 154
Cdd:cd01289   70 QQGNPPRP------GFLLGSRKYEAHVDRFDLGS-TLLIVVAELLqgdsGL-GVFECTIEDQGGVLASGRLNV 134
PRK05174 PRK05174
bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase;
19-71 5.81e-03

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


Pssm-ID: 179953  Cd Length: 172  Bit Score: 35.57  E-value: 5.81e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 513829095  19 PFLFLDKV--IQLEPGKSGIG-IK---NVTVSEPFFEGHFPNESIMPGVLIIEALAQMT 71
Cdd:PRK05174  33 PMLMMDRIteISETGGEFGKGyIVaelDINPDLWFFGCHFIGDPVMPGCLGLDAMWQLV 91
 
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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