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Conserved domains on  [gi|520785063|ref|WP_020289472|]
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MULTISPECIES: 3-hydroxyacyl-ACP dehydratase FabZ [Pseudomonas]

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

CATH:  3.10.129.10
EC:  4.2.1.59
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 3.13e-94

3-hydroxyacyl-ACP dehydratase FabZ;


:

Pssm-ID: 234568  Cd Length: 147  Bit Score: 268.52  E-value: 3.13e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520785063   1 MMDINEIREYLPHRYPFLLVDRVVELDvESKSIRAYKNVSINEPFFNGHFPAHPIMPGVLIIEAMAQAAGILGFKMLdvk 80
Cdd:PRK00006   6 MLDIEEILKLLPHRYPFLLVDRVLELE-PGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSE--- 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520785063  81 PADGTLYYFVGSDKLRFRQPVLPGDQLILEAKFISCKRQIWKFECQASVDGKPVCSAEIICAERK 145
Cdd:PRK00006  82 ENKGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRD 146
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
1-145 3.13e-94

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 268.52  E-value: 3.13e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520785063   1 MMDINEIREYLPHRYPFLLVDRVVELDvESKSIRAYKNVSINEPFFNGHFPAHPIMPGVLIIEAMAQAAGILGFKMLdvk 80
Cdd:PRK00006   6 MLDIEEILKLLPHRYPFLLVDRVLELE-PGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSE--- 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520785063  81 PADGTLYYFVGSDKLRFRQPVLPGDQLILEAKFISCKRQIWKFECQASVDGKPVCSAEIICAERK 145
Cdd:PRK00006  82 ENKGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRD 146
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
3-143 8.98e-82

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: 236.83  E-value: 8.98e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520785063    3 DINEIREYLPHRYPFLLVDRVVELDvESKSIRAYKNVSINEPFFNGHFPAHPIMPGVLIIEAMAQAAGILGFKMLDVKPA 82
Cdd:TIGR01750   1 DIQDIMELLPHRYPFLLVDRILELE-PGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILSLGGEKG 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520785063   83 DGTLYYFVGSDKLRFRQPVLPGDQLILEAKFISCKRQIWKFECQASVDGKPVCSAEIICAE 143
Cdd:TIGR01750  80 KGKLVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIMFAI 140
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
11-142 4.56e-76

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: 222.03  E-value: 4.56e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520785063  11 LPHRYPFLLVDRVVELDVEsKSIRAYKNVSINEPFFNGHFPAHPIMPGVLIIEAMAQAAGILGFKMLDvkPADGTLYYFV 90
Cdd:cd01288    1 LPHRYPFLLVDRVLELEPG-KSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLE--DFEGKLVYFA 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 520785063  91 GSDKLRFRQPVLPGDQLILEAKFISCKRQIWKFECQASVDGKPVCSAEIICA 142
Cdd:cd01288   78 GIDKARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELMFA 129
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
4-145 2.13e-75

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: 220.84  E-value: 2.13e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520785063   4 INEIREYLPHRYPFLLVDRVVELDvESKSIRAYKNVSINEPFFNGHFPAHPIMPGVLIIEAMAQAAGILGFKMLDvKPAD 83
Cdd:COG0764    1 IEEILALLPHRYPFLLVDRVLEID-PGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEG-LEGK 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520785063  84 GTLYYFVGSDKLRFRQPVLPGDQLILEAKFISCKRQIWKFECQASVDGKPVCSAEIICAERK 145
Cdd:COG0764   79 GRLVYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFALVE 140
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
11-138 3.47e-42

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 136.25  E-value: 3.47e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520785063   11 LPHRYpFLLVDRVVELDVESKS-----IRAYKNVSINEPFFNGHFPAHPIMPGVLIIEAMAQAAGI-LGFKMLDVKPADG 84
Cdd:pfam07977   1 LPHRY-FLMLDRVTEIDPDGGKfgkgyIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFyAIWSGGGEGRGRA 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 520785063   85 tlyyfVGSDKLRFRQPVLPGD-QLILEAKF---ISCKRQIWKFECQASVDGKPVCSAE 138
Cdd:pfam07977  80 -----RGVDEVKFRGQVTPGDkQLRYEVEIkkiIEGRRGIGIADGRALVDGKVVYEAK 132
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
1-145 3.13e-94

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 268.52  E-value: 3.13e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520785063   1 MMDINEIREYLPHRYPFLLVDRVVELDvESKSIRAYKNVSINEPFFNGHFPAHPIMPGVLIIEAMAQAAGILGFKMLdvk 80
Cdd:PRK00006   6 MLDIEEILKLLPHRYPFLLVDRVLELE-PGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSE--- 81
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520785063  81 PADGTLYYFVGSDKLRFRQPVLPGDQLILEAKFISCKRQIWKFECQASVDGKPVCSAEIICAERK 145
Cdd:PRK00006  82 ENKGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRD 146
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
3-143 8.98e-82

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: 236.83  E-value: 8.98e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520785063    3 DINEIREYLPHRYPFLLVDRVVELDvESKSIRAYKNVSINEPFFNGHFPAHPIMPGVLIIEAMAQAAGILGFKMLDVKPA 82
Cdd:TIGR01750   1 DIQDIMELLPHRYPFLLVDRILELE-PGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILSLGGEKG 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520785063   83 DGTLYYFVGSDKLRFRQPVLPGDQLILEAKFISCKRQIWKFECQASVDGKPVCSAEIICAE 143
Cdd:TIGR01750  80 KGKLVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIMFAI 140
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
11-142 4.56e-76

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: 222.03  E-value: 4.56e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520785063  11 LPHRYPFLLVDRVVELDVEsKSIRAYKNVSINEPFFNGHFPAHPIMPGVLIIEAMAQAAGILGFKMLDvkPADGTLYYFV 90
Cdd:cd01288    1 LPHRYPFLLVDRVLELEPG-KSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLE--DFEGKLVYFA 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 520785063  91 GSDKLRFRQPVLPGDQLILEAKFISCKRQIWKFECQASVDGKPVCSAEIICA 142
Cdd:cd01288   78 GIDKARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELMFA 129
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
4-145 2.13e-75

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: 220.84  E-value: 2.13e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520785063   4 INEIREYLPHRYPFLLVDRVVELDvESKSIRAYKNVSINEPFFNGHFPAHPIMPGVLIIEAMAQAAGILGFKMLDvKPAD 83
Cdd:COG0764    1 IEEILALLPHRYPFLLVDRVLEID-PGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEG-LEGK 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520785063  84 GTLYYFVGSDKLRFRQPVLPGDQLILEAKFISCKRQIWKFECQASVDGKPVCSAEIICAERK 145
Cdd:COG0764   79 GRLVYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFALVE 140
FabA_FabZ cd00493
FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct ...
12-142 4.96e-65

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: 194.04  E-value: 4.96e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520785063  12 PHRYPFLLVDRVVELDvESKSIRAYKNVSINEPFFNGHFPAHPIMPGVLIIEAMAQAAGILGFKMLDVKPADGTLYYFVG 91
Cdd:cd00493    1 PHRYPMLLVDRVLEID-PGGRIVAEKNVTPNEPFFQGHFPGDPVMPGVLGIEAMAQAAAALAGLLGLGKGNPPRLGYLAG 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 520785063  92 SDKLRFRQPVLPGDQLILEAKFISCKRQIWKFECQASVDGKPVCSAEIICA 142
Cdd:cd00493   80 VRKVKFRGPVLPGDTLTLEVELLKVRRGLGKFDGRAYVDGKLVAEAELMAA 130
PRK13188 PRK13188
bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R) ...
2-138 9.24e-61

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: 193.61  E-value: 9.24e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520785063   2 MDINEIREYLPHRYPFLLVDRVVELdvESKSIRAYKNVSINEPFFNGHFPAHPIMPGVLIIEAMAQAAGILgfkMLDVKP 81
Cdd:PRK13188 321 LDINRIMKILPHRYPFLLVDKIIEL--GDTKIVGIKNVTMNEPFFQGHFPGNPVMPGVLQIEAMAQTGGIL---VLNTVP 395
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 520785063  82 -ADGTLYYFVGSDKLRFRQPVLPGDQLILEAKFIS-CKRQIWKFECQASVDGKPVCSAE 138
Cdd:PRK13188 396 dPENYSTYFMKIDKVKFRQKVVPGDTLIFKVELLSpIRRGICQMQGKAYVNGKLVCEAE 454
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
11-138 3.47e-42

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 136.25  E-value: 3.47e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520785063   11 LPHRYpFLLVDRVVELDVESKS-----IRAYKNVSINEPFFNGHFPAHPIMPGVLIIEAMAQAAGI-LGFKMLDVKPADG 84
Cdd:pfam07977   1 LPHRY-FLMLDRVTEIDPDGGKfgkgyIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFyAIWSGGGEGRGRA 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 520785063   85 tlyyfVGSDKLRFRQPVLPGD-QLILEAKF---ISCKRQIWKFECQASVDGKPVCSAE 138
Cdd:pfam07977  80 -----RGVDEVKFRGQVTPGDkQLRYEVEIkkiIEGRRGIGIADGRALVDGKVVYEAK 132
COG4706 COG4706
Predicted 3-hydroxylacyl-ACP dehydratase, HotDog domain [Lipid transport and metabolism];
1-139 4.26e-16

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


Pssm-ID: 443741  Cd Length: 149  Bit Score: 70.28  E-value: 4.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520785063   1 MMDINEIREYLPHRYPFLLVDRVVELDveSKSIRAYKNVSINEPFFNGHFpahpiMPGVLIIEAMAQAAGILG---FKML 77
Cdd:COG4706    4 TLDRPPIAALIPHRGPMCLLDRVLAWD--EESAVAEVTIRPDNPFRDDGG-----LPAWVGIEYMAQAVAAHGgllARAA 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520785063  78 DVKPADGtlyYFVGSDKLRFRQPVLP-GDQLILEAKFISCKRQIWKFECQASVDGKPVCSAEI 139
Cdd:COG4706   77 GEPPRLG---FLLGVRKVELHVPRFPvGETLRIEAERLLQDEGLGLFECRIRAGGELLASGRL 136
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
52-142 6.67e-13

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: 60.57  E-value: 6.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520785063  52 AHPIMPGVLIIEAMAQAAGILGFKMldvkpADGTLYYFVGSDKLRFRQPVLPGDQLILEAKFISCKRQIWKFECQASV-D 130
Cdd:cd03440   14 GGGIVHGGLLLALADEAAGAAAARL-----GGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNeD 88
                         90
                 ....*....|..
gi 520785063 131 GKPVCSAEIICA 142
Cdd:cd03440   89 GKLVATATATFV 100
FabA_like cd01289
Domain of unknown function, appears to be related to a diverse group of beta-hydroxydecanoyl ...
7-137 1.30e-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: 53.04  E-value: 1.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520785063   7 IREYLPHRYPFLLVDRVVELDVEskSIRAYKNVSINEPFFNghfPAHPIMPGVLIIEAMAQA----AGILGFKMLDvKPA 82
Cdd:cd01289    3 IAALIPHDGPMCLLDRVISWDDD--SIHCRATVHPDPLFPL---RAHGRLPAWVGIEYMAQAiaahGGLLARQQGN-PPR 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 520785063  83 DGtlyYFVGSDKLRFRQPVLPGDQ--LILEAKFISCKRQIWKFECQASVDGKPVCSA 137
Cdd:cd01289   77 PG---FLLGSRKYEAHVDRFDLGStlLIVVAELLQGDSGLGVFECTIEDQGGVLASG 130
FabA cd01287
FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the ...
16-108 2.43e-08

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: 49.95  E-value: 2.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520785063  16 PFLLVDRVVELDVESKS-----IRAYKNVSINEPFFNGHFPAHPIMPGVLIIEAMAQAAGI--------LGFKMLDVKPA 82
Cdd:cd01287    7 QLLMLDRVTEIDPGGGTfglgyLRAEKDIDPDDWFFPCHFHGDPVMPGSLGLEAMIQLLQFyliwlglgTGVDNPRFQGA 86
                         90       100
                 ....*....|....*....|....*.
gi 520785063  83 DGtlyyfvGSDKLRFRQPVLPGDQLI 108
Cdd:cd01287   87 PG------GPGEWKYRGQITPHNKKV 106
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
49-140 1.84e-07

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 47.19  E-value: 1.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520785063  49 HFPAH-------------PIMPGVLIieaMAQAAGILGFKMLDVKPAdgtlyyFVGSDKLRFRQPVLPGDQLILEAKFIS 115
Cdd:COG2030   33 PNPIHldeeaaaatgfggRIAHGMLT---LSLASGLLVDDLPGTAVA------NLGLQEVRFLRPVRVGDTLRARVEVLE 103
                         90       100       110
                 ....*....|....*....|....*....|
gi 520785063 116 CK----RQIWKFECQAS-VDGKPVCSAEII 140
Cdd:COG2030  104 KResksRGIVTLRTTVTnQDGEVVLTGEAT 133
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
48-139 4.89e-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: 45.72  E-value: 4.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520785063  48 GHFPaHPIMPGVLIieaMAQAAGILGFKMLDvkpADGTLYyfvGSDKLRFRQPVLPGDQLILE----AKFISCKRQIWKF 123
Cdd:cd03441   38 AGFG-GRIAHGMLT---LSLASGLLVQWLPG---TDGANL---GSQSVRFLAPVFPGDTLRVEvevlGKRPSKGRGVVTV 107
                         90
                 ....*....|....*..
gi 520785063 124 ECQASV-DGKPVCSAEI 139
Cdd:cd03441  108 RTEARNqGGEVVLSGEA 124
PRK05174 PRK05174
bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase;
16-74 4.47e-06

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


Pssm-ID: 179953  Cd Length: 172  Bit Score: 44.05  E-value: 4.47e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 520785063  16 PFLLVDRVVELDVE----SK-SIRAYKNVSINEPFFNGHFPAHPIMPGVLIIEAMAQaagILGF 74
Cdd:PRK05174  33 PMLMMDRITEISETggefGKgYIVAELDINPDLWFFGCHFIGDPVMPGCLGLDAMWQ---LVGF 93
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
48-146 5.73e-04

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 38.71  E-value: 5.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520785063  48 GHFPAHPIMPGVLIieamaqaAGILGFKMldvkPADGTLYyfVGSDkLRFRQPVLPGDQLI----LEAKFISCKRQIwkF 123
Cdd:PRK08190  57 HHVVAHGMWGGALI-------SAVLGTRL----PGPGTIY--LGQS-LRFRRPVRIGDTLTvtvtVREKDPEKRIVV--L 120
                         90       100
                 ....*....|....*....|....*.
gi 520785063 124 ECQASV-DGKPVCS--AEIICAERKL 146
Cdd:PRK08190 121 DCRCTNqDGEVVITgtAEVIAPTEKV 146
MaoC_C cd03452
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory ...
43-120 1.08e-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: 36.99  E-value: 1.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 520785063  43 EPFFnGHFPAHpimpGVLIIEAmaqAAGILgfkmldVKPADGTLYYFVGSDKLRFRQPVLPGDQLILEakfISCKRQI 120
Cdd:cd03452   45 ASFF-GKRVAH----GYFVLSA---AAGLF------VDPAPGPVLANYGLENLRFLEPVYPGDTIQVR---LTCKRKI 105
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
69-138 1.91e-03

(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: 35.98  E-value: 1.91e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 520785063  69 AGILGFKMldvkPADGTLYYfvgSDKLRFRQPVLPGDQLILEAK---FISCKRQIwKFECQASV-DGKPVCSAE 138
Cdd:cd03449   58 SAVLGTLL----PGPGTIYL---SQSLRFLRPVFIGDTVTATVTvteKREDKKRV-TLETVCTNqNGEVVIEGE 123
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
87-142 7.62e-03

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 34.53  E-value: 7.62e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 520785063  87 YYFVGSD-KLRFRQPVLPGDQLILEAKFISCKRQIWKFECQASV-DGKPVCSAEIICA 142
Cdd:COG2050   75 RRAVTIElNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDeDGKLVATATGTFA 132
 
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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