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Conserved domains on  [gi|516270818|ref|WP_017674781|]
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MULTISPECIES: 3-hydroxyacyl-ACP dehydratase FabZ [Pseudomonadaceae]

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;
1-145 1.60e-93

3-hydroxyacyl-ACP dehydratase FabZ;


:

Pssm-ID: 234568  Cd Length: 147  Bit Score: 266.60  E-value: 1.60e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516270818   1 MMDINEIREYLPHRYPFLLVDRVVDLDvEGKQIRAYKNVSINEPFFNGHFPEHPIMPGVLIIEAMAQAAGILGFKMMgvk 80
Cdd:PRK00006   6 MLDIEEILKLLPHRYPFLLVDRVLELE-PGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSE--- 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516270818  81 PADGTLYYFVGSDKLRFRSPVLPGDQLTLEAKYLSDRRSIWKFECRATVDGKEVCAAEIICAERK 145
Cdd:PRK00006  82 ENKGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRD 146
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
1-145 1.60e-93

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 266.60  E-value: 1.60e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516270818   1 MMDINEIREYLPHRYPFLLVDRVVDLDvEGKQIRAYKNVSINEPFFNGHFPEHPIMPGVLIIEAMAQAAGILGFKMMgvk 80
Cdd:PRK00006   6 MLDIEEILKLLPHRYPFLLVDRVLELE-PGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSE--- 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516270818  81 PADGTLYYFVGSDKLRFRSPVLPGDQLTLEAKYLSDRRSIWKFECRATVDGKEVCAAEIICAERK 145
Cdd:PRK00006  82 ENKGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRD 146
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 3-143 2.00e-80

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: 233.36  E-value: 2.00e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516270818    3 DINEIREYLPHRYPFLLVDRVVDLDvEGKQIRAYKNVSINEPFFNGHFPEHPIMPGVLIIEAMAQAAGILGFKMMGVKPA 82
Cdd:TIGR01750   1 DIQDIMELLPHRYPFLLVDRILELE-PGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILSLGGEKG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516270818   83 DGTLYYFVGSDKLRFRSPVLPGDQLTLEAKYLSDRRSIWKFECRATVDGKEVCAAEIICAE 143
Cdd:TIGR01750  80 KGKLVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIMFAI 140
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 4-145 7.20e-76

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: 221.99  E-value: 7.20e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516270818   4 INEIREYLPHRYPFLLVDRVVDLDvEGKQIRAYKNVSINEPFFNGHFPEHPIMPGVLIIEAMAQAAGILGFKMMGvKPAD 83
Cdd:COG0764    1 IEEILALLPHRYPFLLVDRVLEID-PGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEG-LEGK 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516270818  84 GTLYYFVGSDKLRFRSPVLPGDQLTLEAKYLSDRRSIWKFECRATVDGKEVCAAEIICAERK 145
Cdd:COG0764   79 GRLVYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFALVE 140
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 11-142 4.18e-75

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: 219.72  E-value: 4.18e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516270818  11 LPHRYPFLLVDRVVDLDvEGKQIRAYKNVSINEPFFNGHFPEHPIMPGVLIIEAMAQAAGILGFKMMGvkPADGTLYYFV 90
Cdd:cd01288    1 LPHRYPFLLVDRVLELE-PGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLE--DFEGKLVYFA 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 516270818  91 GSDKLRFRSPVLPGDQLTLEAKYLSDRRSIWKFECRATVDGKEVCAAEIICA 142
Cdd:cd01288   78 GIDKARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELMFA 129
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 11-138 1.18e-42

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 137.41  E-value: 1.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516270818   11 LPHRYpFLLVDRVVDLDVEGK-----QIRAYKNVSINEPFFNGHFPEHPIMPGVLIIEAMAQAAGI-LGFKMMGVKPADG 84
Cdd:pfam07977   1 LPHRY-FLMLDRVTEIDPDGGkfgkgYIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFyAIWSGGGEGRGRA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 516270818   85 tlyyfVGSDKLRFRSPVLPGD-QLTLEA---KYLSDRRSIWKFECRATVDGKEVCAAE 138
Cdd:pfam07977  80 -----RGVDEVKFRGQVTPGDkQLRYEVeikKIIEGRRGIGIADGRALVDGKVVYEAK 132
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
1-145 1.60e-93

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 266.60  E-value: 1.60e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516270818   1 MMDINEIREYLPHRYPFLLVDRVVDLDvEGKQIRAYKNVSINEPFFNGHFPEHPIMPGVLIIEAMAQAAGILGFKMMgvk 80
Cdd:PRK00006   6 MLDIEEILKLLPHRYPFLLVDRVLELE-PGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSE--- 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516270818  81 PADGTLYYFVGSDKLRFRSPVLPGDQLTLEAKYLSDRRSIWKFECRATVDGKEVCAAEIICAERK 145
Cdd:PRK00006  82 ENKGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRD 146
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 3-143 2.00e-80

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: 233.36  E-value: 2.00e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516270818    3 DINEIREYLPHRYPFLLVDRVVDLDvEGKQIRAYKNVSINEPFFNGHFPEHPIMPGVLIIEAMAQAAGILGFKMMGVKPA 82
Cdd:TIGR01750   1 DIQDIMELLPHRYPFLLVDRILELE-PGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILSLGGEKG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516270818   83 DGTLYYFVGSDKLRFRSPVLPGDQLTLEAKYLSDRRSIWKFECRATVDGKEVCAAEIICAE 143
Cdd:TIGR01750  80 KGKLVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIMFAI 140
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 4-145 7.20e-76

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: 221.99  E-value: 7.20e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516270818   4 INEIREYLPHRYPFLLVDRVVDLDvEGKQIRAYKNVSINEPFFNGHFPEHPIMPGVLIIEAMAQAAGILGFKMMGvKPAD 83
Cdd:COG0764    1 IEEILALLPHRYPFLLVDRVLEID-PGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEG-LEGK 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516270818  84 GTLYYFVGSDKLRFRSPVLPGDQLTLEAKYLSDRRSIWKFECRATVDGKEVCAAEIICAERK 145
Cdd:COG0764   79 GRLVYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFALVE 140
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 11-142 4.18e-75

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: 219.72  E-value: 4.18e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516270818  11 LPHRYPFLLVDRVVDLDvEGKQIRAYKNVSINEPFFNGHFPEHPIMPGVLIIEAMAQAAGILGFKMMGvkPADGTLYYFV 90
Cdd:cd01288    1 LPHRYPFLLVDRVLELE-PGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLE--DFEGKLVYFA 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 516270818  91 GSDKLRFRSPVLPGDQLTLEAKYLSDRRSIWKFECRATVDGKEVCAAEIICA 142
Cdd:cd01288   78 GIDKARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELMFA 129
FabA_FabZ cd00493
FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct ...
 12-142 1.81e-64

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: 192.88  E-value: 1.81e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516270818  12 PHRYPFLLVDRVVDLDvEGKQIRAYKNVSINEPFFNGHFPEHPIMPGVLIIEAMAQAAGILGFKMMGVKPADGTLYYFVG 91
Cdd:cd00493    1 PHRYPMLLVDRVLEID-PGGRIVAEKNVTPNEPFFQGHFPGDPVMPGVLGIEAMAQAAAALAGLLGLGKGNPPRLGYLAG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 516270818  92 SDKLRFRSPVLPGDQLTLEAKYLSDRRSIWKFECRATVDGKEVCAAEIICA 142
Cdd:cd00493   80 VRKVKFRGPVLPGDTLTLEVELLKVRRGLGKFDGRAYVDGKLVAEAELMAA 130
PRK13188 PRK13188
bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R) ...
 2-138 7.72e-59

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: 188.60  E-value: 7.72e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516270818   2 MDINEIREYLPHRYPFLLVDRVVDLdvEGKQIRAYKNVSINEPFFNGHFPEHPIMPGVLIIEAMAQAAGILgfkMM-GVK 80
Cdd:PRK13188 321 LDINRIMKILPHRYPFLLVDKIIEL--GDTKIVGIKNVTMNEPFFQGHFPGNPVMPGVLQIEAMAQTGGIL---VLnTVP 395

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 516270818  81 PADGTLYYFVGSDKLRFRSPVLPGDQLTLEAKYLSD-RRSIWKFECRATVDGKEVCAAE 138
Cdd:PRK13188 396 DPENYSTYFMKIDKVKFRQKVVPGDTLIFKVELLSPiRRGICQMQGKAYVNGKLVCEAE 454
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 11-138 1.18e-42

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 137.41  E-value: 1.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516270818   11 LPHRYpFLLVDRVVDLDVEGK-----QIRAYKNVSINEPFFNGHFPEHPIMPGVLIIEAMAQAAGI-LGFKMMGVKPADG 84
Cdd:pfam07977   1 LPHRY-FLMLDRVTEIDPDGGkfgkgYIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFyAIWSGGGEGRGRA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 516270818   85 tlyyfVGSDKLRFRSPVLPGD-QLTLEA---KYLSDRRSIWKFECRATVDGKEVCAAE 138
Cdd:pfam07977  80 -----RGVDEVKFRGQVTPGDkQLRYEVeikKIIEGRRGIGIADGRALVDGKVVYEAK 132
COG4706 COG4706
Predicted 3-hydroxylacyl-ACP dehydratase, HotDog domain [Lipid transport and metabolism];
1-139 1.55e-16

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


Pssm-ID: 443741  Cd Length: 149  Bit Score: 71.44  E-value: 1.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516270818   1 MMDINEIREYLPHRYPFLLVDRVVDLDVEgkQIRAYKNVSINEPFFNGHFpehpiMPGVLIIEAMAQAAGILG---FKMM 77
Cdd:COG4706    4 TLDRPPIAALIPHRGPMCLLDRVLAWDEE--SAVAEVTIRPDNPFRDDGG-----LPAWVGIEYMAQAVAAHGgllARAA 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516270818  78 GVKPADGtlyYFVGSDKLRFRSPVLP-GDQLTLEAKYLSDRRSIWKFECRATVDGKEVCAAEI 139
Cdd:COG4706   77 GEPPRLG---FLLGVRKVELHVPRFPvGETLRIEAERLLQDEGLGLFECRIRAGGELLASGRL 136
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 53-136 1.10e-12

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: 60.18  E-value: 1.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516270818  53 HPIMPGVLIIEAMAQAAGILGFKMMGvkpadGTLYYFVGSDKLRFRSPVLPGDQLTLEAKYLSDRRSIWKFECRATVDGK 132
Cdd:cd03440   15 GGIVHGGLLLALADEAAGAAAARLGG-----RGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNEDG 89


                 ....
gi 516270818 133 EVCA 136
Cdd:cd03440   90 KLVA 93
FabA cd01287
FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the ...
 16-110 7.02e-10

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: 53.80  E-value: 7.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516270818  16 PFLLVDRVVDLDVEGK-----QIRAYKNVSINEPFFNGHFPEHPIMPGVLIIEAMAQAAGI-LGFKMMGV-------KPA 82
Cdd:cd01287    7 QLLMLDRVTEIDPGGGtfglgYLRAEKDIDPDDWFFPCHFHGDPVMPGSLGLEAMIQLLQFyLIWLGLGTgvdnprfQGA 86

                         90       100
                 ....*....|....*....|....*....
gi 516270818  83 DGtlyyfvGSDKLRFRSPVLPGD-QLTLE 110
Cdd:cd01287   87 PG------GPGEWKYRGQITPHNkKVTYE 109
FabA_like cd01289
Domain of unknown function, appears to be related to a diverse group of beta-hydroxydecanoyl ...
 7-134 3.62e-09

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: 51.88  E-value: 3.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516270818   7 IREYLPHRYPFLLVDRVVDLDVEgkQIRAYKNVSINEPFFNghfPEHPIMPGVLIIEAMAQA----AGILGfKMMGVKPA 82
Cdd:cd01289    3 IAALIPHDGPMCLLDRVISWDDD--SIHCRATVHPDPLFPL---RAHGRLPAWVGIEYMAQAiaahGGLLA-RQQGNPPR 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 516270818  83 DGtlyYFVGSDKLRFRSPVLPGDQ--LTLEAKYLSDRRSIWKFECRATVDGKEV 134
Cdd:cd01289   77 PG---FLLGSRKYEAHVDRFDLGStlLIVVAELLQGDSGLGVFECTIEDQGGVL 127
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
48-140 1.63e-08

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 49.88  E-value: 1.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516270818  48 GHFPEhPIMPGVLIieaMAQAAGILGFKMMGVKPAdgtlyyFVGSDKLRFRSPVLPGDQLTLEA----KYLSDRRSIWKF 123
Cdd:COG2030   46 TGFGG-RIAHGMLT---LSLASGLLVDDLPGTAVA------NLGLQEVRFLRPVRVGDTLRARVevleKRESKSRGIVTL 115

                         90
                 ....*....|....*...
gi 516270818 124 ECRAT-VDGKEVCAAEII 140
Cdd:COG2030  116 RTTVTnQDGEVVLTGEAT 133
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 48-139 1.56e-07

(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: 47.26  E-value: 1.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516270818  48 GHFPeHPIMPGVLIieaMAQAAGILGFKMMGvkpADGTLYyfvGSDKLRFRSPVLPGDQLTLE----AKYLSDRRSIWKF 123
Cdd:cd03441   38 AGFG-GRIAHGMLT---LSLASGLLVQWLPG---TDGANL---GSQSVRFLAPVFPGDTLRVEvevlGKRPSKGRGVVTV 107

                         90
                 ....*....|....*..
gi 516270818 124 ECRATV-DGKEVCAAEI 139
Cdd:cd03441  108 RTEARNqGGEVVLSGEA 124
PRK05174 PRK05174
bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase;
16-74 5.59e-07

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


Pssm-ID: 179953  Cd Length: 172  Bit Score: 46.36  E-value: 5.59e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516270818  16 PFLLVDRVVDLDVEGK-----QIRAYKNVSINEPFFNGHFPEHPIMPGVLIIEAMAQaagILGF 74
Cdd:PRK05174  33 PMLMMDRITEISETGGefgkgYIVAELDINPDLWFFGCHFIGDPVMPGCLGLDAMWQ---LVGF 93
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 69-138 5.22e-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. (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: 40.22  E-value: 5.22e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516270818  69 AGILGFKMmgvkPADGTLYYfvgSDKLRFRSPVLPGDQLT--LEAKYLSDRRSIWKFECRATV-DGKEVCAAE 138
Cdd:cd03449   58 SAVLGTLL----PGPGTIYL---SQSLRFLRPVFIGDTVTatVTVTEKREDKKRVTLETVCTNqNGEVVIEGE 123
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 33-146 1.18e-04

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 40.63  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516270818  33 IRAYKNVS--INEPFFNGHFPEHPIMPGVlIIEAM---AQAAGILGFKMmgvkPADGTLYyfVGSDkLRFRSPVLPGDQL 107
Cdd:PRK08190  31 IELFAAMSgdVNPAHLDAAYAASDGFHHV-VAHGMwggALISAVLGTRL----PGPGTIY--LGQS-LRFRRPVRIGDTL 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 516270818 108 T--LEAKYLSDRRSIWKFECRATV-DGKEVCA--AEIICAERKL 146
Cdd:PRK08190 103 TvtVTVREKDPEKRIVVLDCRCTNqDGEVVITgtAEVIAPTEKV 146
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 91-119 8.96e-04

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: 37.16  E-value: 8.96e-04
                         10        20
                 ....*....|....*....|....*....
gi 516270818  91 GSDKLRFRSPVLPGDQLTLEAKYLSDRRS 119
Cdd:cd03454   79 GIDELRWPRPVRPGDTLSVEVEVLDKRPS 107
MaoC_C cd03452
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory ...
 48-118 1.39e-03

MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory protein. Orthologs of MaoC include PaaZ [Escherichia coli] and PaaN [Pseudomonas putida], which are putative ring-opening enzymes involved in phenylacetic acid degradation. The C-terminal domain of MaoC has sequence similarity to (R)-specific enoyl-CoA hydratase,Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. MaoC also has an N-terminal PutA domain like that found in the E. coli PutA proline dehydrogenase and other members of the aldehyde dehydrogenase family.


Pssm-ID: 239536 [Multi-domain]  Cd Length: 142  Bit Score: 36.61  E-value: 1.39e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516270818  48 GHFPEHPIMPGVLIIEAmaqAAGILgfkmmgVKPADGTLYYFVGSDKLRFRSPVLPGD--QLTLEAKYLSDRR 118
Cdd:cd03452   45 ASFFGKRVAHGYFVLSA---AAGLF------VDPAPGPVLANYGLENLRFLEPVYPGDtiQVRLTCKRKIPRD 108
HDE_HSD cd03448
HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), ...
 64-134 7.34e-03

HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), and Hydratase-Dehydrogenase-Epimerase (HDE) proteins. Other enzymes with this fold include MaoC dehydratase, and the fatty acid synthase beta subunit.


Pssm-ID: 239532 [Multi-domain]  Cd Length: 122  Bit Score: 34.50  E-value: 7.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516270818  64 AMAQAAG----IL-GFKMMGVKpADGTLYYFVGSD-------KLRFRSPVLPGDQLTLEakylsdrrsIWK------FEC 125
Cdd:cd03448   35 AFAKAAGfprpILhGLCTYGFA-ARAVLEAFADGDparfkaiKVRFSSPVFPGETLRTE---------MWKegnrviFQT 104


                 ....*....
gi 516270818 126 RATVDGKEV 134
Cdd:cd03448  105 KVVERDVVV 113
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 64-136 8.20e-03

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 33.38  E-value: 8.20e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516270818   64 AMAQAAGILGFKMMGVKPADGTlyyfVGSDKLRFRSPVLPGDQLTLEAKYLSDRRSIWKFECRATVDGKEVCA 136
Cdd:pfam03061  11 ALADEAAGAAARRLGGSQQVVV----VVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
 
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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