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Conserved domains on  [gi|1260148482|gb|PEW91740|]
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beta-hydroxyacyl-ACP dehydratase [Bacillus thuringiensis]

Protein Classification

3-hydroxyacyl-ACP dehydratase FabZ family protein( domain architecture ID 10101294)

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

CATH:  3.10.129.10
Gene Ontology:  GO:0006633
PubMed:  15307895
SCOP:  4002539

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 7-124 4.53e-40

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: 130.36  E-value: 4.53e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1260148482   7 LPHRYPFLMTDKVTNVKQGESVTGYKLITNNEWFIND---NQKHMPHMLIVEALAQLSAF-VHTSD---SEGLGFLSSLD 79
Cdd:cd01288     1 LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGhfpGNPIMPGVLIIEALAQAAGIlGLKSLedfEGKLVYFAGID 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1260148482  80 GVEFQGKAYPGDKLDLHYELTRNRRGFVLGKGIATVNDQPIVTIE 124
Cdd:cd01288    81 KARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAE 125
 
Name Accession Description Interval E-value
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 7-124 4.53e-40

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: 130.36  E-value: 4.53e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1260148482   7 LPHRYPFLMTDKVTNVKQGESVTGYKLITNNEWFIND---NQKHMPHMLIVEALAQLSAF-VHTSD---SEGLGFLSSLD 79
Cdd:cd01288     1 LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGhfpGNPIMPGVLIIEALAQAAGIlGLKSLedfEGKLVYFAGID 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1260148482  80 GVEFQGKAYPGDKLDLHYELTRNRRGFVLGKGIATVNDQPIVTIE 124
Cdd:cd01288    81 KARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAE 125
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 1-124 5.89e-39

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: 128.00  E-value: 5.89e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1260148482   1 MHIKDTLPHRYPFLMTDKVTNVKQGESVTGYKLITNNEWFIND---NQKHMPHMLIVEALAQLSAF-----VHTSDSEGL 72
Cdd:COG0764     2 EEILALLPHRYPFLLVDRVLEIDPGKSIVAEKNVTPNEPFFQGhfpGDPVMPGVLILEAMAQLGGFlllksEGLEGKGRL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1260148482  73 GFLSSLDGVEFQGKAYPGDKLDLHYELTRNRRGFVLGKGIATVNDQPIVTIE 124
Cdd:COG0764    82 VYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAE 133
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
3-118 5.12e-36

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 120.61  E-value: 5.12e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1260148482   3 IKDTLPHRYPFLMTDKVTNVKQGESVTGYKLITNNEWFIndnQKH------MPHMLIVEALAQLSAFVHTSDSE---GLG 73
Cdd:PRK00006   12 ILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFF---QGHfpgypvMPGVLIIEAMAQAAGVLALKSEEnkgKLV 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1260148482  74 FLSSLDGVEFQGKAYPGDKLDLHYELTRNRRGFVLGKGIATVNDQ 118
Cdd:PRK00006   89 YFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGK 133
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 1-124 8.06e-29

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: 102.01  E-value: 8.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1260148482   1 MHIKDTLPHRYPFLMTDKVTNVKQGESVTGYKLITNNEWFIND---NQKHMPHMLIVEALAQLSAFV------HTSDSEG 71
Cdd:TIGR01750   3 QDIMELLPHRYPFLLVDRILELEPGKRIVAIKNVTINEPFFQGhfpEKPIMPGVLIIEAMAQAAGVLailslgGEKGKGK 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1260148482  72 LGFLSSLDGVEFQGKAYPGDKLDLHYELTRNRRGFVLGKGIATVNDQPIVTIE 124
Cdd:TIGR01750  83 LVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAE 135
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 7-124 3.70e-16

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 69.23  E-value: 3.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1260148482   7 LPHRYpFLMTDKVTNV-KQGES-----VTGYKLITNNEWFIndnQKHMPHM------LIVEALAQLSAF--VHTSDSEGL 72
Cdd:pfam07977   1 LPHRY-FLMLDRVTEIdPDGGKfgkgyIVAEKDITPNEWFF---QGHFPGDpvmpgvLGLEAMAQLMGFyaIWSGGGEGR 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1260148482  73 GFLSSLDGVEFQGKAYPGDKLdLHYEL-----TRNRRGFVLGKGIATVNDQPIVTIE 124
Cdd:pfam07977  77 GRARGVDEVKFRGQVTPGDKQ-LRYEVeikkiIEGRRGIGIADGRALVDGKVVYEAK 132
 
Name Accession Description Interval E-value
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 7-124 4.53e-40

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: 130.36  E-value: 4.53e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1260148482   7 LPHRYPFLMTDKVTNVKQGESVTGYKLITNNEWFIND---NQKHMPHMLIVEALAQLSAF-VHTSD---SEGLGFLSSLD 79
Cdd:cd01288     1 LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGhfpGNPIMPGVLIIEALAQAAGIlGLKSLedfEGKLVYFAGID 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1260148482  80 GVEFQGKAYPGDKLDLHYELTRNRRGFVLGKGIATVNDQPIVTIE 124
Cdd:cd01288    81 KARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAE 125
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 1-124 5.89e-39

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: 128.00  E-value: 5.89e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1260148482   1 MHIKDTLPHRYPFLMTDKVTNVKQGESVTGYKLITNNEWFIND---NQKHMPHMLIVEALAQLSAF-----VHTSDSEGL 72
Cdd:COG0764     2 EEILALLPHRYPFLLVDRVLEIDPGKSIVAEKNVTPNEPFFQGhfpGDPVMPGVLILEAMAQLGGFlllksEGLEGKGRL 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1260148482  73 GFLSSLDGVEFQGKAYPGDKLDLHYELTRNRRGFVLGKGIATVNDQPIVTIE 124
Cdd:COG0764    82 VYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAE 133
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
3-118 5.12e-36

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 120.61  E-value: 5.12e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1260148482   3 IKDTLPHRYPFLMTDKVTNVKQGESVTGYKLITNNEWFIndnQKH------MPHMLIVEALAQLSAFVHTSDSE---GLG 73
Cdd:PRK00006   12 ILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFF---QGHfpgypvMPGVLIIEAMAQAAGVLALKSEEnkgKLV 88

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1260148482  74 FLSSLDGVEFQGKAYPGDKLDLHYELTRNRRGFVLGKGIATVNDQ 118
Cdd:PRK00006   89 YFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGK 133
FabA_FabZ cd00493
FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct ...
 8-124 3.99e-33

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: 112.76  E-value: 3.99e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1260148482   8 PHRYPFLMTDKVTNVKQGESVTGYKLITNNEWFINDNQKHMPHM---LIVEALAQLSAF------VHTSDSEGLGFLSSL 78
Cdd:cd00493     1 PHRYPMLLVDRVLEIDPGGRIVAEKNVTPNEPFFQGHFPGDPVMpgvLGIEAMAQAAAAlagllgLGKGNPPRLGYLAGV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1260148482  79 DGVEFQGKAYPGDKLDLHYELTRNRRGFVLGKGIATVNDQPIVTIE 124
Cdd:cd00493    81 RKVKFRGPVLPGDTLTLEVELLKVRRGLGKFDGRAYVDGKLVAEAE 126
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 1-124 8.06e-29

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: 102.01  E-value: 8.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1260148482   1 MHIKDTLPHRYPFLMTDKVTNVKQGESVTGYKLITNNEWFIND---NQKHMPHMLIVEALAQLSAFV------HTSDSEG 71
Cdd:TIGR01750   3 QDIMELLPHRYPFLLVDRILELEPGKRIVAIKNVTINEPFFQGhfpEKPIMPGVLIIEAMAQAAGVLailslgGEKGKGK 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1260148482  72 LGFLSSLDGVEFQGKAYPGDKLDLHYELTRNRRGFVLGKGIATVNDQPIVTIE 124
Cdd:TIGR01750  83 LVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAE 135
PRK13188 PRK13188
bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R) ...
 3-118 6.60e-20

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: 83.83  E-value: 6.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1260148482   3 IKDTLPHRYPFLMTDKVTNVKQgESVTGYKLITNNEWFIndnQKH------MPHMLIVEALAQLSAFV----HTSDSEGL 72
Cdd:PRK13188  326 IMKILPHRYPFLLVDKIIELGD-TKIVGIKNVTMNEPFF---QGHfpgnpvMPGVLQIEAMAQTGGILvlntVPDPENYS 401

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1260148482  73 GFLSSLDGVEFQGKAYPGDKLDLHYELTRN-RRGFVLGKGIATVNDQ 118
Cdd:PRK13188  402 TYFMKIDKVKFRQKVVPGDTLIFKVELLSPiRRGICQMQGKAYVNGK 448
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 7-124 3.70e-16

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 69.23  E-value: 3.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1260148482   7 LPHRYpFLMTDKVTNV-KQGES-----VTGYKLITNNEWFIndnQKHMPHM------LIVEALAQLSAF--VHTSDSEGL 72
Cdd:pfam07977   1 LPHRY-FLMLDRVTEIdPDGGKfgkgyIVAEKDITPNEWFF---QGHFPGDpvmpgvLGLEAMAQLMGFyaIWSGGGEGR 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1260148482  73 GFLSSLDGVEFQGKAYPGDKLdLHYEL-----TRNRRGFVLGKGIATVNDQPIVTIE 124
Cdd:pfam07977  77 GRARGVDEVKFRGQVTPGDKQ-LRYEVeikkiIEGRRGIGIADGRALVDGKVVYEAK 132
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 42-122 1.43e-03

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


Pssm-ID: 239524 [Multi-domain]  Cd Length: 100  Bit Score: 35.53  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1260148482  42 NDNQKHMPHMLIVEALAQL-SAFVHTSDSEGLGFLSSLDGVEFQGKAYPGDKLDLHYELTRNRRGFVLGKGIATVNDQPI 120
Cdd:cd03440    12 IDGGGIVHGGLLLALADEAaGAAAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNEDGKL 91


                  ..
gi 1260148482 121 VT 122
Cdd:cd03440    92 VA 93
 
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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