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Conserved domains on  [gi|499470936|ref|WP_011157576|]
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3-hydroxyacyl-ACP dehydratase FabZ family protein [Rhodopseudomonas palustris]

Protein Classification

3-hydroxyacyl-ACP dehydratase FabZ family protein( domain architecture ID 10002379)

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

EC:  4.2.1.-
Gene Ontology:  GO:0016836|GO:0006633
PubMed:  15307895
SCOP:  4002539

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 6-127 1.03e-30

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: 107.97  E-value: 1.03e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470936   6 FHLIDRIAELRlADRSITVEARVPETSTIFEGHFPGYPLMPGVLLIETMAQSSGWLLIALMQFQ---RMPFLAAVKEAKM 82
Cdd:COG0764   14 FLLVDRVLEID-PGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEGLEgkgRLVYFLGIDKVKF 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 499470936  83 RTFVTPGETLSIDVSVVHEGSGFTVTEAKIKSGGKLACNATLTFR 127
Cdd:COG0764   93 RGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFA 137
 
Name Accession Description Interval E-value
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 6-127 1.03e-30

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: 107.97  E-value: 1.03e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470936   6 FHLIDRIAELRlADRSITVEARVPETSTIFEGHFPGYPLMPGVLLIETMAQSSGWLLIALMQFQ---RMPFLAAVKEAKM 82
Cdd:COG0764   14 FLLVDRVLEID-PGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEGLEgkgRLVYFLGIDKVKF 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 499470936  83 RTFVTPGETLSIDVSVVHEGSGFTVTEAKIKSGGKLACNATLTFR 127
Cdd:COG0764   93 RGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFA 137
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 6-126 1.50e-29

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: 104.55  E-value: 1.50e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470936   6 FHLIDRIAELRlADRSITVEARVPETSTIFEGHFPGYPLMPGVLLIETMAQSSGWLLIALMQ--FQRMPFLAAVKEAKMR 83
Cdd:cd01288    7 FLLVDRVLELE-PGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLEdfEGKLVYFAGIDKARFR 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 499470936  84 TFVTPGETLSIDVSVVHEGSGFTVTEAKIKSGGKLACNATLTF 126
Cdd:cd01288   86 KPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELMF 128
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
6-126 2.32e-26

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 96.72  E-value: 2.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470936   6 FHLIDRIAELRlADRSITVEARVpetsTI----FEGHFPGYPLMPGVLLIETMAQSSGWLLIALMQFQ-RMPFLAAVKEA 80
Cdd:PRK00006  22 FLLVDRVLELE-PGKSIVAIKNV----TInepfFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSEENKgKLVYFAGIDKA 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 499470936  81 KMRTFVTPGETLSIDVSVVHEGSGFTVTEAKIKSGGKLACNATLTF 126
Cdd:PRK00006  97 RFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMF 142
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 6-126 3.85e-22

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: 85.83  E-value: 3.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470936    6 FHLIDRIAELRLADRSITVEArVPETSTIFEGHFPGYPLMPGVLLIETMAQSSGWLLIALMQFQR----MPFLAAVKEAK 81
Cdd:TIGR01750  15 FLLVDRILELEPGKRIVAIKN-VTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILSLGGEKgkgkLVYFAGIDKAR 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 499470936   82 MRTFVTPGETLSIDVSVVHEGSGFTVTEAKIKSGGKLACNATLTF 126
Cdd:TIGR01750  94 FRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIMF 138
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 4-122 1.17e-11

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 58.44  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470936    4 EYFHLIDRIAELRLADRS-----ITVEARVPETSTIFEGHFPGYPLMPGVLLIETMAQSSGWLLIALMQFQRMPFLAAVK 78
Cdd:pfam07977   4 RYFLMLDRVTEIDPDGGKfgkgyIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWSGGGEGRGRARGVD 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 499470936   79 EAKMRTFVTPG-ETLSIDVSVV---HEGSGFTVTEAKIKSGGKLACNA 122
Cdd:pfam07977  84 EVKFRGQVTPGdKQLRYEVEIKkiiEGRRGIGIADGRALVDGKVVYEA 131
 
Name Accession Description Interval E-value
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 6-127 1.03e-30

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: 107.97  E-value: 1.03e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470936   6 FHLIDRIAELRlADRSITVEARVPETSTIFEGHFPGYPLMPGVLLIETMAQSSGWLLIALMQFQ---RMPFLAAVKEAKM 82
Cdd:COG0764   14 FLLVDRVLEID-PGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEGLEgkgRLVYFLGIDKVKF 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 499470936  83 RTFVTPGETLSIDVSVVHEGSGFTVTEAKIKSGGKLACNATLTFR 127
Cdd:COG0764   93 RGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFA 137
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 6-126 1.50e-29

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: 104.55  E-value: 1.50e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470936   6 FHLIDRIAELRlADRSITVEARVPETSTIFEGHFPGYPLMPGVLLIETMAQSSGWLLIALMQ--FQRMPFLAAVKEAKMR 83
Cdd:cd01288    7 FLLVDRVLELE-PGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLEdfEGKLVYFAGIDKARFR 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 499470936  84 TFVTPGETLSIDVSVVHEGSGFTVTEAKIKSGGKLACNATLTF 126
Cdd:cd01288   86 KPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELMF 128
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
6-126 2.32e-26

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 96.72  E-value: 2.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470936   6 FHLIDRIAELRlADRSITVEARVpetsTI----FEGHFPGYPLMPGVLLIETMAQSSGWLLIALMQFQ-RMPFLAAVKEA 80
Cdd:PRK00006  22 FLLVDRVLELE-PGKSIVAIKNV----TInepfFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSEENKgKLVYFAGIDKA 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 499470936  81 KMRTFVTPGETLSIDVSVVHEGSGFTVTEAKIKSGGKLACNATLTF 126
Cdd:PRK00006  97 RFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMF 142
FabA_FabZ cd00493
FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct ...
 8-127 1.70e-25

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: 94.27  E-value: 1.70e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470936   8 LIDRIAELRlADRSITVEARVPETSTIFEGHFPGYPLMPGVLLIETMAQSSGWLLIALMQFQ----RMPFLAAVKEAKMR 83
Cdd:cd00493    8 LVDRVLEID-PGGRIVAEKNVTPNEPFFQGHFPGDPVMPGVLGIEAMAQAAAALAGLLGLGKgnppRLGYLAGVRKVKFR 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499470936  84 TFVTPGETLSIDVSVVHEGSGFTVTEAKIKSGGKLACNATLTFR 127
Cdd:cd00493   87 GPVLPGDTLTLEVELLKVRRGLGKFDGRAYVDGKLVAEAELMAA 130
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 6-126 3.85e-22

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: 85.83  E-value: 3.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470936    6 FHLIDRIAELRLADRSITVEArVPETSTIFEGHFPGYPLMPGVLLIETMAQSSGWLLIALMQFQR----MPFLAAVKEAK 81
Cdd:TIGR01750  15 FLLVDRILELEPGKRIVAIKN-VTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILSLGGEKgkgkLVYFAGIDKAR 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 499470936   82 MRTFVTPGETLSIDVSVVHEGSGFTVTEAKIKSGGKLACNATLTF 126
Cdd:TIGR01750  94 FRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIMF 138
PRK13188 PRK13188
bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R) ...
 6-126 9.71e-16

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: 73.04  E-value: 9.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470936   6 FHLIDRIAELRlaDRSITVEARVPETSTIFEGHFPGYPLMPGVLLIETMAQSSGWLLIA-LMQFQRM-PFLAAVKEAKMR 83
Cdd:PRK13188 336 FLLVDKIIELG--DTKIVGIKNVTMNEPFFQGHFPGNPVMPGVLQIEAMAQTGGILVLNtVPDPENYsTYFMKIDKVKFR 413

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499470936  84 TFVTPGETLSIDVSVVHE-GSGFTVTEAKIKSGGKLACNATLTF 126
Cdd:PRK13188 414 QKVVPGDTLIFKVELLSPiRRGICQMQGKAYVNGKLVCEAELMA 457
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 4-122 1.17e-11

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 58.44  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470936    4 EYFHLIDRIAELRLADRS-----ITVEARVPETSTIFEGHFPGYPLMPGVLLIETMAQSSGWLLIALMQFQRMPFLAAVK 78
Cdd:pfam07977   4 RYFLMLDRVTEIDPDGGKfgkgyIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWSGGGEGRGRARGVD 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 499470936   79 EAKMRTFVTPG-ETLSIDVSVV---HEGSGFTVTEAKIKSGGKLACNA 122
Cdd:pfam07977  84 EVKFRGQVTPGdKQLRYEVEIKkiiEGRRGIGIADGRALVDGKVVYEA 131
COG4706 COG4706
Predicted 3-hydroxylacyl-ACP dehydratase, HotDog domain [Lipid transport and metabolism];
8-125 3.68e-09

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


Pssm-ID: 443741  Cd Length: 149  Bit Score: 52.18  E-value: 3.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470936   8 LIDRIaeLRLADRSITVEARVPETSTIFEGHFpgyplMPGVLLIETMAQS----SGWLLIALMQFQRMPFLAAVKeaKMR 83
Cdd:COG4706   22 LLDRV--LAWDEESAVAEVTIRPDNPFRDDGG-----LPAWVGIEYMAQAvaahGGLLARAAGEPPRLGFLLGVR--KVE 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 499470936  84 TFVTP---GETLSIDVSVVHEGSGFTVTEAKIKSGGKLACNATLT 125
Cdd:COG4706   93 LHVPRfpvGETLRIEAERLLQDEGLGLFECRIRAGGELLASGRLN 137
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 33-126 1.74e-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: 41.31  E-value: 1.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499470936  33 TIFEGHFPGYPLMPGVLLIETMAQSSGWLLIALMQFQRMPFLAAVkEAKMRTFVTPGETLSIDVSVVHEGSGFTVTEAKI 112
Cdd:cd03440    6 TVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSL-DVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEV 84

                         90
                 ....*....|....*
gi 499470936 113 KSG-GKLACNATLTF 126
Cdd:cd03440   85 RNEdGKLVATATATF 99
 
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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