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Conserved domains on  [gi|488141826|ref|WP_002213034|]
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MULTISPECIES: 3-hydroxyacyl-ACP dehydratase FabZ family protein [Yersinia pseudotuberculosis complex]

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 ...
 32-168 7.18e-32

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: 111.44  E-value: 7.18e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141826  32 IKKMIPHREPFLMVDNVELINIECRlIKAIRRVDEKDPVFGGHFPNDPIYPGVLQQESMFQTALILMYFLLNetaiPPAE 111
Cdd:COG0764    4 ILALLPHRYPFLLVDRVLEIDPGKS-IVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEG----LEGK 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488141826 112 ENIIHAVGtrVYDVFHLSAVRPGELMTIRCCITEYDTFLATAIVQITVNDQIVTVGK 168
Cdd:COG0764   79 GRLVYFLG--IDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAE 133
 
Name Accession Description Interval E-value
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 32-168 7.18e-32

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: 111.44  E-value: 7.18e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141826  32 IKKMIPHREPFLMVDNVELINIECRlIKAIRRVDEKDPVFGGHFPNDPIYPGVLQQESMFQTALILMYFLLNetaiPPAE 111
Cdd:COG0764    4 ILALLPHRYPFLLVDRVLEIDPGKS-IVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEG----LEGK 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488141826 112 ENIIHAVGtrVYDVFHLSAVRPGELMTIRCCITEYDTFLATAIVQITVNDQIVTVGK 168
Cdd:COG0764   79 GRLVYFLG--IDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAE 133
FabA_FabZ cd00493
FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct ...
 37-168 2.17e-21

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: 84.26  E-value: 2.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141826  37 PHREPFLMVDNVELINiECRLIKAIRRVDEKDPVFGGHFPNDPIYPGVLQQESMFQTALILMYFLLNETAIPPaeeNIIH 116
Cdd:cd00493    1 PHRYPMLLVDRVLEID-PGGRIVAEKNVTPNEPFFQGHFPGDPVMPGVLGIEAMAQAAAALAGLLGLGKGNPP---RLGY 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488141826 117 AVGTRVYDvFHlSAVRPGELMTIRCCITEYDTFLATAIVQITVNDQIVTVGK 168
Cdd:cd00493   77 LAGVRKVK-FR-GPVLPGDTLTLEVELLKVRRGLGKFDGRAYVDGKLVAEAE 126
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
30-99 1.47e-19

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 79.77  E-value: 1.47e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488141826  30 DI--IKKMIPHREPFLMVDNVelinIECRL---IKAIRRVDEKDPVFGGHFPNDPIYPGVLQQESMFQTALILMY 99
Cdd:PRK00006   8 DIeeILKLLPHRYPFLLVDRV----LELEPgksIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLAL 78
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 32-103 7.08e-17

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: 72.73  E-value: 7.08e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488141826   32 IKKMIPHREPFLMVDNVELINIECRLIkAIRRVDEKDPVFGGHFPNDPIYPGVLQQESMFQTALILMYFLLN 103
Cdd:TIGR01750   5 IMELLPHRYPFLLVDRILELEPGKRIV-AIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILSLG 75
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 36-101 4.20e-13

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 62.68  E-value: 4.20e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488141826   36 IPHRePFLMVDNVELINIE-----CRLIKAIRRVDEKDPVFGGHFPNDPIYPGVLQQESMFQTALILMYFL 101
Cdd:pfam07977   1 LPHR-YFLMLDRVTEIDPDggkfgKGYIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWS 70
 
Name Accession Description Interval E-value
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 32-168 7.18e-32

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: 111.44  E-value: 7.18e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141826  32 IKKMIPHREPFLMVDNVELINIECRlIKAIRRVDEKDPVFGGHFPNDPIYPGVLQQESMFQTALILMYFLLNetaiPPAE 111
Cdd:COG0764    4 ILALLPHRYPFLLVDRVLEIDPGKS-IVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEG----LEGK 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488141826 112 ENIIHAVGtrVYDVFHLSAVRPGELMTIRCCITEYDTFLATAIVQITVNDQIVTVGK 168
Cdd:COG0764   79 GRLVYFLG--IDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAE 133
FabA_FabZ cd00493
FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct ...
 37-168 2.17e-21

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: 84.26  E-value: 2.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141826  37 PHREPFLMVDNVELINiECRLIKAIRRVDEKDPVFGGHFPNDPIYPGVLQQESMFQTALILMYFLLNETAIPPaeeNIIH 116
Cdd:cd00493    1 PHRYPMLLVDRVLEID-PGGRIVAEKNVTPNEPFFQGHFPGDPVMPGVLGIEAMAQAAAALAGLLGLGKGNPP---RLGY 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488141826 117 AVGTRVYDvFHlSAVRPGELMTIRCCITEYDTFLATAIVQITVNDQIVTVGK 168
Cdd:cd00493   77 LAGVRKVK-FR-GPVLPGDTLTLEVELLKVRRGLGKFDGRAYVDGKLVAEAE 126
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 36-168 5.53e-21

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: 83.36  E-value: 5.53e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141826  36 IPHREPFLMVDNVELINIECRlIKAIRRVDEKDPVFGGHFPNDPIYPGVLQQESMFQTALILMYFLLNEtaippAEENII 115
Cdd:cd01288    1 LPHRYPFLLVDRVLELEPGKS-IVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLED-----FEGKLV 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488141826 116 HAVGTRvyDVFHLSAVRPGELMTIRCCITEYDTFLATAIVQITVNDQIVTVGK 168
Cdd:cd01288   75 YFAGID--KARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAE 125
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
30-99 1.47e-19

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 79.77  E-value: 1.47e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488141826  30 DI--IKKMIPHREPFLMVDNVelinIECRL---IKAIRRVDEKDPVFGGHFPNDPIYPGVLQQESMFQTALILMY 99
Cdd:PRK00006   8 DIeeILKLLPHRYPFLLVDRV----LELEPgksIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLAL 78
PRK13188 PRK13188
bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R) ...
 30-145 2.47e-17

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: 78.05  E-value: 2.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488141826  30 DI--IKKMIPHREPFLMVDNVelINIECRLIKAIRRVDEKDPVFGGHFPNDPIYPGVLQQESMFQTALILMyflLNETAI 107
Cdd:PRK13188 322 DInrIMKILPHRYPFLLVDKI--IELGDTKIVGIKNVTMNEPFFQGHFPGNPVMPGVLQIEAMAQTGGILV---LNTVPD 396

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 488141826 108 PpaeENiihavgtrvYDVFHLSA--------VRPGELMTIRCCITE 145
Cdd:PRK13188 397 P---EN---------YSTYFMKIdkvkfrqkVVPGDTLIFKVELLS 430
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 32-103 7.08e-17

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: 72.73  E-value: 7.08e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488141826   32 IKKMIPHREPFLMVDNVELINIECRLIkAIRRVDEKDPVFGGHFPNDPIYPGVLQQESMFQTALILMYFLLN 103
Cdd:TIGR01750   5 IMELLPHRYPFLLVDRILELEPGKRIV-AIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILSLG 75
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 36-101 4.20e-13

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 62.68  E-value: 4.20e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488141826   36 IPHRePFLMVDNVELINIE-----CRLIKAIRRVDEKDPVFGGHFPNDPIYPGVLQQESMFQTALILMYFL 101
Cdd:pfam07977   1 LPHR-YFLMLDRVTEIDPDggkfgKGYIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWS 70
FabA cd01287
FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the ...
 41-104 1.01e-05

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: 1.01e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488141826  41 PFLMVDNVELINIE-----CRLIKAIRRVDEKDPVFGGHFPNDPIYPGVLQQESMFQTaliLMYFLLNE 104
Cdd:cd01287    7 QLLMLDRVTEIDPGggtfgLGYLRAEKDIDPDDWFFPCHFHGDPVMPGSLGLEAMIQL---LQFYLIWL 72
 
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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