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Conserved domains on  [gi|1491781658|gb|RLL89343|]
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hydroxymyristoyl-ACP dehydratase [Petrotoga sp. HKA.pet.4.5]

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;
1-138 3.83e-81

3-hydroxyacyl-ACP dehydratase FabZ;


:

Pssm-ID: 234568  Cd Length: 147  Bit Score: 235.01  E-value: 3.83e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491781658   1 MNIEEIMKILPHRYPFLLVDGVLELNEEK-IKAFKNVSINEPFFQGHFPNYPIMPGVLIVEGMAQTAGLLLLKDTD-ENV 78
Cdd:PRK00006    7 LDIEEILKLLPHRYPFLLVDRVLELEPGKsIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSEEnKGK 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491781658  79 IPLFTGIDKARFKKEVRPGDKLIYDLEILQRKANMFKLKGIATVEEQVCAQAEIMVGIKK 138
Cdd:PRK00006   87 LVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRD 146
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
1-138 3.83e-81

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 235.01  E-value: 3.83e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491781658   1 MNIEEIMKILPHRYPFLLVDGVLELNEEK-IKAFKNVSINEPFFQGHFPNYPIMPGVLIVEGMAQTAGLLLLKDTD-ENV 78
Cdd:PRK00006    7 LDIEEILKLLPHRYPFLLVDRVLELEPGKsIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSEEnKGK 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491781658  79 IPLFTGIDKARFKKEVRPGDKLIYDLEILQRKANMFKLKGIATVEEQVCAQAEIMVGIKK 138
Cdd:PRK00006   87 LVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRD 146
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
3-139 3.21e-69

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: 204.66  E-value: 3.21e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491781658   3 IEEIMKILPHRYPFLLVDGVLELNEEK-IKAFKNVSINEPFFQGHFPNYPIMPGVLIVEGMAQTAGLLLLK---DTDENV 78
Cdd:COG0764     1 IEEILALLPHRYPFLLVDRVLEIDPGKsIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKsegLEGKGR 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491781658  79 IPLFTGIDKARFKKEVRPGDKLIYDLEILQRKANMFKLKGIATVEEQVCAQAEIMVGIKKS 139
Cdd:COG0764    81 LVYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFALVEK 141
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
10-133 1.90e-64

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: 192.37  E-value: 1.90e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491781658  10 LPHRYPFLLVDGVLELNEEK-IKAFKNVSINEPFFQGHFPNYPIMPGVLIVEGMAQTAGLLLLK--DTDENVIPLFTGID 86
Cdd:cd01288     1 LPHRYPFLLVDRVLELEPGKsIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKslEDFEGKLVYFAGID 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1491781658  87 KARFKKEVRPGDKLIYDLEILQRKANMFKLKGIATVEEQVCAQAEIM 133
Cdd:cd01288    81 KARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELM 127
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
3-133 1.37e-60

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: 182.90  E-value: 1.37e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491781658   3 IEEIMKILPHRYPFLLVDGVLELNEEK-IKAFKNVSINEPFFQGHFPNYPIMPGVLIVEGMAQTAGLLLLK----DTDEN 77
Cdd:TIGR01750   2 IQDIMELLPHRYPFLLVDRILELEPGKrIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILslggEKGKG 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1491781658  78 VIPLFTGIDKARFKKEVRPGDKLIYDLEILQRKANMFKLKGIATVEEQVCAQAEIM 133
Cdd:TIGR01750  82 KLVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIM 137
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
10-131 6.24e-36

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 120.07  E-value: 6.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491781658  10 LPHRYpFLLVDGVLELNEE-------KIKAFKNVSINEPFFQGHFPNYPIMPGVLIVEGMAQTAGLLLLKDTDENVIPLF 82
Cdd:pfam07977   1 LPHRY-FLMLDRVTEIDPDggkfgkgYIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWSGGGEGRGRA 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1491781658  83 TGIDKARFKKEVRPGDK-LIYDLEIL---QRKANMFKLKGIATVEEQVCAQAE 131
Cdd:pfam07977  80 RGVDEVKFRGQVTPGDKqLRYEVEIKkiiEGRRGIGIADGRALVDGKVVYEAK 132
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
1-138 3.83e-81

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 235.01  E-value: 3.83e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491781658   1 MNIEEIMKILPHRYPFLLVDGVLELNEEK-IKAFKNVSINEPFFQGHFPNYPIMPGVLIVEGMAQTAGLLLLKDTD-ENV 78
Cdd:PRK00006    7 LDIEEILKLLPHRYPFLLVDRVLELEPGKsIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSEEnKGK 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491781658  79 IPLFTGIDKARFKKEVRPGDKLIYDLEILQRKANMFKLKGIATVEEQVCAQAEIMVGIKK 138
Cdd:PRK00006   87 LVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRD 146
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
3-139 3.21e-69

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: 204.66  E-value: 3.21e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491781658   3 IEEIMKILPHRYPFLLVDGVLELNEEK-IKAFKNVSINEPFFQGHFPNYPIMPGVLIVEGMAQTAGLLLLK---DTDENV 78
Cdd:COG0764     1 IEEILALLPHRYPFLLVDRVLEIDPGKsIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKsegLEGKGR 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491781658  79 IPLFTGIDKARFKKEVRPGDKLIYDLEILQRKANMFKLKGIATVEEQVCAQAEIMVGIKKS 139
Cdd:COG0764    81 LVYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFALVEK 141
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
10-133 1.90e-64

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: 192.37  E-value: 1.90e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491781658  10 LPHRYPFLLVDGVLELNEEK-IKAFKNVSINEPFFQGHFPNYPIMPGVLIVEGMAQTAGLLLLK--DTDENVIPLFTGID 86
Cdd:cd01288     1 LPHRYPFLLVDRVLELEPGKsIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKslEDFEGKLVYFAGID 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1491781658  87 KARFKKEVRPGDKLIYDLEILQRKANMFKLKGIATVEEQVCAQAEIM 133
Cdd:cd01288    81 KARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELM 127
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
3-133 1.37e-60

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: 182.90  E-value: 1.37e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491781658   3 IEEIMKILPHRYPFLLVDGVLELNEEK-IKAFKNVSINEPFFQGHFPNYPIMPGVLIVEGMAQTAGLLLLK----DTDEN 77
Cdd:TIGR01750   2 IQDIMELLPHRYPFLLVDRILELEPGKrIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILslggEKGKG 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1491781658  78 VIPLFTGIDKARFKKEVRPGDKLIYDLEILQRKANMFKLKGIATVEEQVCAQAEIM 133
Cdd:TIGR01750  82 KLVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIM 137
PRK13188 PRK13188
bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R) ...
1-138 3.35e-57

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: 183.98  E-value: 3.35e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491781658   1 MNIEEIMKILPHRYPFLLVDGVLELNEEKIKAFKNVSINEPFFQGHFPNYPIMPGVLIVEGMAQTAGLLLLKDTD--ENV 78
Cdd:PRK13188  321 LDINRIMKILPHRYPFLLVDKIIELGDTKIVGIKNVTMNEPFFQGHFPGNPVMPGVLQIEAMAQTGGILVLNTVPdpENY 400
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491781658  79 IPLFTGIDKARFKKEVRPGDKLIYDLEILQ-RKANMFKLKGIATVEEQVCAQAEIMVGIKK 138
Cdd:PRK13188  401 STYFMKIDKVKFRQKVVPGDTLIFKVELLSpIRRGICQMQGKAYVNGKLVCEAELMAQIVK 461
FabA_FabZ cd00493
FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct ...
11-136 6.86e-53

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: 163.22  E-value: 6.86e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491781658  11 PHRYPFLLVDGVLELNE-EKIKAFKNVSINEPFFQGHFPNYPIMPGVLIVEGMAQTAGLLLLK----DTDENVIPLFTGI 85
Cdd:cd00493     1 PHRYPMLLVDRVLEIDPgGRIVAEKNVTPNEPFFQGHFPGDPVMPGVLGIEAMAQAAAALAGLlglgKGNPPRLGYLAGV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1491781658  86 DKARFKKEVRPGDKLIYDLEILQRKANMFKLKGIATVEEQVCAQAEIMVGI 136
Cdd:cd00493    81 RKVKFRGPVLPGDTLTLEVELLKVRRGLGKFDGRAYVDGKLVAEAELMAAA 131
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
10-131 6.24e-36

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 120.07  E-value: 6.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491781658  10 LPHRYpFLLVDGVLELNEE-------KIKAFKNVSINEPFFQGHFPNYPIMPGVLIVEGMAQTAGLLLLKDTDENVIPLF 82
Cdd:pfam07977   1 LPHRY-FLMLDRVTEIDPDggkfgkgYIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWSGGGEGRGRA 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1491781658  83 TGIDKARFKKEVRPGDK-LIYDLEIL---QRKANMFKLKGIATVEEQVCAQAE 131
Cdd:pfam07977  80 RGVDEVKFRGQVTPGDKqLRYEVEIKkiiEGRRGIGIADGRALVDGKVVYEAK 132
FabA cd01287
FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the ...
15-106 6.82e-12

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: 58.81  E-value: 6.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491781658  15 PFLLVDGVLELNEE-------KIKAFKNVSINEPFFQGHFPNYPIMPGVLIVEGMAQTAGLLLLKD--TDENVIPLFTGI 85
Cdd:cd01287     7 QLLMLDRVTEIDPGggtfglgYLRAEKDIDPDDWFFPCHFHGDPVMPGSLGLEAMIQLLQFYLIWLglGTGVDNPRFQGA 86
                          90       100
                  ....*....|....*....|....*.
gi 1491781658  86 D----KARFKKEVRPGDKLI-YDLEI 106
Cdd:cd01287    87 PggpgEWKYRGQITPHNKKVtYEVHI 112
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
50-134 8.93e-10

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: 52.48  E-value: 8.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491781658  50 YPIMPGVLIVEGMAQTAGLLLLKDTDENVIPLFTGIDkARFKKEVRPGDKLIYDLEILQRKANMFKLKGIATVE-EQVCA 128
Cdd:cd03440    15 GGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLD-VRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNEdGKLVA 93

                  ....*.
gi 1491781658 129 QAEIMV 134
Cdd:cd03440    94 TATATF 99
COG4706 COG4706
Predicted 3-hydroxylacyl-ACP dehydratase, HotDog domain [Lipid transport and metabolism];
1-134 3.80e-09

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


Pssm-ID: 443741  Cd Length: 149  Bit Score: 51.79  E-value: 3.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491781658   1 MNIEEIMKILPHRYPFLLVDGVLELNEEKIKAFKNVSINEPFFQGHFpnypiMPGVLIVEGMAQTAGL---LLLKDTDEN 77
Cdd:COG4706     5 LDRPPIAALIPHRGPMCLLDRVLAWDEESAVAEVTIRPDNPFRDDGG-----LPAWVGIEYMAQAVAAhggLLARAAGEP 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1491781658  78 VIPLF-TGIDKARFKKEV-RPGDKLIYDLEILQRKANMFKLKGIATVEEQVCAQAEIMV 134
Cdd:COG4706    80 PRLGFlLGVRKVELHVPRfPVGETLRIEAERLLQDEGLGLFECRIRAGGELLASGRLNV 138
PRK05174 PRK05174
bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase;
15-120 2.42e-06

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


Pssm-ID: 179953  Cd Length: 172  Bit Score: 44.43  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491781658  15 PFLLVDGVLELNEE-------KIKAFKNVSINEPFFQGHFPNYPIMPGVLIVEGMAQTAGLLL-----------Lkdtde 76
Cdd:PRK05174   33 PMLMMDRITEISETggefgkgYIVAELDINPDLWFFGCHFIGDPVMPGCLGLDAMWQLVGFYLgwlggpgkgraL----- 107
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1491781658  77 nviplftGIDKARFKKEVRPGDKLI-YDLEI---LQRKANMfklkGIA 120
Cdd:PRK05174  108 -------GVGEVKFTGQVLPTAKKVtYEIDIkrvINRKLVM----GIA 144
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
57-134 6.77e-05

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 40.25  E-value: 6.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491781658  57 LIVEGMaQTAGLL--LLKDTDENVIPLFTGIDKARFKKEVRPGDKLIYDLEILQRKANmfKLKGIATVE--------EQV 126
Cdd:COG2030    51 RIAHGM-LTLSLAsgLLVDDLPGTAVANLGLQEVRFLRPVRVGDTLRARVEVLEKRES--KSRGIVTLRttvtnqdgEVV 127

                  ....*....
gi 1491781658 127 C-AQAEIMV 134
Cdd:COG2030   128 LtGEATVLV 136
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
53-134 1.56e-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. 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: 36.09  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491781658  53 MPGVLIVEGMaQTAGL---LLLKDTDENVIPLFtGIDKARFKKEVRPGDKLIYDLEILQRKANmfKLKGIATVEEQVCAQ 129
Cdd:cd03441    39 GFGGRIAHGM-LTLSLasgLLVQWLPGTDGANL-GSQSVRFLAPVFPGDTLRVEVEVLGKRPS--KGRGVVTVRTEARNQ 114

                  ....*
gi 1491781658 130 AEIMV 134
Cdd:cd03441   115 GGEVV 119
 
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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