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Conserved domains on  [gi|613388745|gb|EZZ92631|]
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(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase [Staphylococcus aureus VET0057R]

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;
1-144 2.18e-93

3-hydroxyacyl-ACP dehydratase FabZ;


:

Pssm-ID: 234568  Cd Length: 147  Bit Score: 266.21  E-value: 2.18e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388745   1 METIFDYNQIKQIIPHRQPFLLIDKVVEYEEGQRCVAIKQVSGNEPFFQGHFPEYAVMPGVLITEALAQTGAVAILNSEE 80
Cdd:PRK00006   3 ETMMLDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSEE 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613388745  81 NKGKIALFAGIDKCRFKRQVVPGDTLTLEVEITKIKGPIGKGNAKATVDGQLACSCELTFAIQD 144
Cdd:PRK00006  83 NKGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRD 146
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
1-144 2.18e-93

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 266.21  E-value: 2.18e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388745   1 METIFDYNQIKQIIPHRQPFLLIDKVVEYEEGQRCVAIKQVSGNEPFFQGHFPEYAVMPGVLITEALAQTGAVAILNSEE 80
Cdd:PRK00006   3 ETMMLDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSEE 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613388745  81 NKGKIALFAGIDKCRFKRQVVPGDTLTLEVEITKIKGPIGKGNAKATVDGQLACSCELTFAIQD 144
Cdd:PRK00006  83 NKGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRD 146
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 8-144 8.03e-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: 219.30  E-value: 8.03e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388745   8 NQIKQIIPHRQPFLLIDKVVEYEEGQRCVAIKQVSGNEPFFQGHFPEYAVMPGVLITEALAQTGAVAILNSE--ENKGKI 85
Cdd:COG0764    2 EEILALLPHRYPFLLVDRVLEIDPGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEglEGKGRL 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 613388745  86 ALFAGIDKCRFKRQVVPGDTLTLEVEITKIKGPIGKGNAKATVDGQLACSCELTFAIQD 144
Cdd:COG0764   82 VYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFALVE 140
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 14-143 7.15e-73

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: 213.94  E-value: 7.15e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388745  14 IPHRQPFLLIDKVVEYEEGQRCVAIKQVSGNEPFFQGHFPEYAVMPGVLITEALAQTGAVAILNSEE-NKGKIALFAGID 92
Cdd:cd01288    1 LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLEdFEGKLVYFAGID 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 613388745  93 KCRFKRQVVPGDTLTLEVEITKIKGPIGKGNAKATVDGQLACSCELTFAIQ 143
Cdd:cd01288   81 KARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELMFAIA 131
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 6-142 7.01e-65

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: 194.07  E-value: 7.01e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388745    6 DYNQIKQIIPHRQPFLLIDKVVEYEEGQRCVAIKQVSGNEPFFQGHFPEYAVMPGVLITEALAQTGAV---AILNSEENK 82
Cdd:TIGR01750   1 DIQDIMELLPHRYPFLLVDRILELEPGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVlaiLSLGGEKGK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388745   83 GKIALFAGIDKCRFKRQVVPGDTLTLEVEITKIKGPIGKGNAKATVDGQLACSCELTFAI 142
Cdd:TIGR01750  81 GKLVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIMFAI 140
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 14-137 7.96e-37

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 122.77  E-value: 7.96e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388745   14 IPHRqPFLLIDKVVEYEEGQ------RCVAIKQVSGNEPFFQGHFPEYAVMPGVLITEALAQTGAVAILNSEENKGKiAL 87
Cdd:pfam07977   1 LPHR-YFLMLDRVTEIDPDGgkfgkgYIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWSGGGEGR-GR 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 613388745   88 FAGIDKCRFKRQVVPGD-TLTLEVEITKI---KGPIGKGNAKATVDGQLACSCE 137
Cdd:pfam07977  79 ARGVDEVKFRGQVTPGDkQLRYEVEIKKIiegRRGIGIADGRALVDGKVVYEAK 132
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
1-144 2.18e-93

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 266.21  E-value: 2.18e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388745   1 METIFDYNQIKQIIPHRQPFLLIDKVVEYEEGQRCVAIKQVSGNEPFFQGHFPEYAVMPGVLITEALAQTGAVAILNSEE 80
Cdd:PRK00006   3 ETMMLDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSEE 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 613388745  81 NKGKIALFAGIDKCRFKRQVVPGDTLTLEVEITKIKGPIGKGNAKATVDGQLACSCELTFAIQD 144
Cdd:PRK00006  83 NKGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRD 146
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 8-144 8.03e-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: 219.30  E-value: 8.03e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388745   8 NQIKQIIPHRQPFLLIDKVVEYEEGQRCVAIKQVSGNEPFFQGHFPEYAVMPGVLITEALAQTGAVAILNSE--ENKGKI 85
Cdd:COG0764    2 EEILALLPHRYPFLLVDRVLEIDPGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEglEGKGRL 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 613388745  86 ALFAGIDKCRFKRQVVPGDTLTLEVEITKIKGPIGKGNAKATVDGQLACSCELTFAIQD 144
Cdd:COG0764   82 VYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFALVE 140
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 14-143 7.15e-73

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: 213.94  E-value: 7.15e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388745  14 IPHRQPFLLIDKVVEYEEGQRCVAIKQVSGNEPFFQGHFPEYAVMPGVLITEALAQTGAVAILNSEE-NKGKIALFAGID 92
Cdd:cd01288    1 LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLEdFEGKLVYFAGID 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 613388745  93 KCRFKRQVVPGDTLTLEVEITKIKGPIGKGNAKATVDGQLACSCELTFAIQ 143
Cdd:cd01288   81 KARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELMFAIA 131
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 6-142 7.01e-65

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: 194.07  E-value: 7.01e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388745    6 DYNQIKQIIPHRQPFLLIDKVVEYEEGQRCVAIKQVSGNEPFFQGHFPEYAVMPGVLITEALAQTGAV---AILNSEENK 82
Cdd:TIGR01750   1 DIQDIMELLPHRYPFLLVDRILELEPGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVlaiLSLGGEKGK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388745   83 GKIALFAGIDKCRFKRQVVPGDTLTLEVEITKIKGPIGKGNAKATVDGQLACSCELTFAI 142
Cdd:TIGR01750  81 GKLVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIMFAI 140
PRK13188 PRK13188
bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R) ...
 2-146 2.30e-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: 195.15  E-value: 2.30e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388745   2 ETIFDYNQIKQIIPHRQPFLLIDKVVEYEEgQRCVAIKQVSGNEPFFQGHFPEYAVMPGVLITEALAQTGAVAILNSEEN 81
Cdd:PRK13188 318 EPILDINRIMKILPHRYPFLLVDKIIELGD-TKIVGIKNVTMNEPFFQGHFPGNPVMPGVLQIEAMAQTGGILVLNTVPD 396

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613388745  82 -KGKIALFAGIDKCRFKRQVVPGDTLTLEVE-ITKIKGPIGKGNAKATVDGQLACSCELTFAIQDVK 146
Cdd:PRK13188 397 pENYSTYFMKIDKVKFRQKVVPGDTLIFKVElLSPIRRGICQMQGKAYVNGKLVCEAELMAQIVKKK 463
FabA_FabZ cd00493
FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct ...
 15-142 2.80e-58

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: 177.09  E-value: 2.80e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388745  15 PHRQPFLLIDKVVEYEEGQRCVAIKQVSGNEPFFQGHFPEYAVMPGVLITEALAQTGAVAILNSEE---NKGKIALFAGI 91
Cdd:cd00493    1 PHRYPMLLVDRVLEIDPGGRIVAEKNVTPNEPFFQGHFPGDPVMPGVLGIEAMAQAAAALAGLLGLgkgNPPRLGYLAGV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 613388745  92 DKCRFKRQVVPGDTLTLEVEITKIKGPIGKGNAKATVDGQLACSCELTFAI 142
Cdd:cd00493   81 RKVKFRGPVLPGDTLTLEVELLKVRRGLGKFDGRAYVDGKLVAEAELMAAA 131
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 14-137 7.96e-37

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 122.77  E-value: 7.96e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388745   14 IPHRqPFLLIDKVVEYEEGQ------RCVAIKQVSGNEPFFQGHFPEYAVMPGVLITEALAQTGAVAILNSEENKGKiAL 87
Cdd:pfam07977   1 LPHR-YFLMLDRVTEIDPDGgkfgkgYIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWSGGGEGR-GR 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 613388745   88 FAGIDKCRFKRQVVPGD-TLTLEVEITKI---KGPIGKGNAKATVDGQLACSCE 137
Cdd:pfam07977  79 ARGVDEVKFRGQVTPGDkQLRYEVEIKKIiegRRGIGIADGRALVDGKVVYEAK 132
COG4706 COG4706
Predicted 3-hydroxylacyl-ACP dehydratase, HotDog domain [Lipid transport and metabolism];
1-144 3.14e-13

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


Pssm-ID: 443741  Cd Length: 149  Bit Score: 62.58  E-value: 3.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388745   1 METIFDYNQIKQIIPHRQPFLLIDKVVEYEEgQRCVAIKQVSGNEPFF-QGHFPEYavmpgVLItEALAQTGAV--AILN 77
Cdd:COG4706    1 MNPTLDRPPIAALIPHRGPMCLLDRVLAWDE-ESAVAEVTIRPDNPFRdDGGLPAW-----VGI-EYMAQAVAAhgGLLA 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 613388745  78 SEENKG-KIALFAGIDKCRFKRQVVP-GDTLTLEVEITKIKGPIGKGNAKATVDGQLACSCELTFAIQD 144
Cdd:COG4706   74 RAAGEPpRLGFLLGVRKVELHVPRFPvGETLRIEAERLLQDEGLGLFECRIRAGGELLASGRLNVFQPA 142
FabA cd01287
FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the ...
 19-131 4.67e-11

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: 56.88  E-value: 4.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388745  19 PFLLIDKV--VEYEEGQ----RCVAIKQVSGNEPFFQGHFPEYAVMPGVLITEALAQT-GAVAILNSEENKGKIALFAGI 91
Cdd:cd01287    7 QLLMLDRVteIDPGGGTfglgYLRAEKDIDPDDWFFPCHFHGDPVMPGSLGLEAMIQLlQFYLIWLGLGTGVDNPRFQGA 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 613388745  92 D----KCRFKRQVVPGD-TLTLEVEITKI----KGPIGKGNAKATVDGQ 131
Cdd:cd01287   87 PggpgEWKYRGQITPHNkKVTYEVHIKEVgrdgPRPYIIADASLWVDGL 135
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 35-141 5.53e-11

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: 55.56  E-value: 5.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388745  35 CVAIKQVSGNEPFFQGHfpeyavMPGVLITeALAQTGAVAILNSEENKGKIALFAGIDkCRFKRQVVPGDTLTLEVEITK 114
Cdd:cd03440    1 FVLRLTVTPEDIDGGGI------VHGGLLL-ALADEAAGAAAARLGGRGLGAVTLSLD-VRFLRPVRPGDTLTVEAEVVR 72

                         90       100
                 ....*....|....*....|....*...
gi 613388745 115 IKGPIGKGNAKATV-DGQLACSCELTFA 141
Cdd:cd03440   73 VGRSSVTVEVEVRNeDGKLVATATATFV 100
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
51-142 2.34e-08

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 49.50  E-value: 2.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388745  51 HF-PEYA--------VMPGVLitealaqTGAVAI-LNSEENKGKIALFAGIDKCRFKRQVVPGDTLTLEVEITKIKGPIG 120
Cdd:COG2030   37 HLdEEAAaatgfggrIAHGML-------TLSLASgLLVDDLPGTAVANLGLQEVRFLRPVRVGDTLRARVEVLEKRESKS 109

                         90       100
                 ....*....|....*....|....*..
gi 613388745 121 KGNAKATV-----DGQLACSCELTFAI 142
Cdd:COG2030  110 RGIVTLRTtvtnqDGEVVLTGEATVLV 136
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 69-116 1.77e-05

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: 41.79  E-value: 1.77e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 613388745  69 QTGAVA-ILNSEENKGKIALFA--GIDKCRFKRQVVPGDTLTLEVEITKIK 116
Cdd:cd03454   55 HTAAITmRLLVDAGLSGSASGGspGIDELRWPRPVRPGDTLSVEVEVLDKR 105
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 55-141 5.69e-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. 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: 40.33  E-value: 5.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388745  55 YAVMPGVLITEALAQTGAVAilnseenkgkialfaGIDKCRFKRQVVPGDTLTLEVEITKIKGPIGKGNAKATV-----D 129
Cdd:cd03441   51 LSLASGLLVQWLPGTDGANL---------------GSQSVRFLAPVFPGDTLRVEVEVLGKRPSKGRGVVTVRTearnqG 115

                         90
                 ....*....|..
gi 613388745 130 GQLACSCELTFA 141
Cdd:cd03441  116 GEVVLSGEATVL 127
FabA_like cd01289
Domain of unknown function, appears to be related to a diverse group of beta-hydroxydecanoyl ...
 9-73 3.57e-04

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: 38.40  E-value: 3.57e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 613388745   9 QIKQIIPHRQPFLLIDKVVEYEEGQ-RCVAikQVSGNEPFFQghfPEYAVMPGVLITEALAQTGAV 73
Cdd:cd01289    2 WIAALIPHDGPMCLLDRVISWDDDSiHCRA--TVHPDPLFPL---RAHGRLPAWVGIEYMAQAIAA 62
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 94-141 1.88e-03

Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440586 [Multi-domain]  Cd Length: 139  Bit Score: 36.41  E-value: 1.88e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 613388745  94 CRFKRQVVPGDTLTLEVEITKIkgpigkGNAKATV--------DGQLACSCELTFA 141
Cdd:COG0824   64 IDYLRPARYGDELTVETRVVRL------GGSSLTFeyeifradDGELLATGETVLV 113
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 66-132 4.22e-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: 34.15  E-value: 4.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 613388745   66 ALAQTGAVAILNSEeNKGKIALFAGIDKCRFKRQVVPGDTLTLEVEITKIkgpigkGNAKATVDGQL 132
Cdd:pfam03061  11 ALADEAAGAAARRL-GGSQQVVVVVELSIDFLRPARLGDRLTVEARVVRL------GRTSAVVEVEV 70
PRK05174 PRK05174
bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase;
19-132 7.42e-03

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


Pssm-ID: 179953  Cd Length: 172  Bit Score: 34.80  E-value: 7.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613388745  19 PFLLIDKVVE-YEEGQ-----RCVAIKQVSGNEPFFQGHFPEYAVMPGVLITEALAQ-TGAVAILNSEENKGKiALfaGI 91
Cdd:PRK05174  33 PMLMMDRITEiSETGGefgkgYIVAELDINPDLWFFGCHFIGDPVMPGCLGLDAMWQlVGFYLGWLGGPGKGR-AL--GV 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 613388745  92 DKCRFKRQVVPG-DTLTLEVEITKI---KGPIGKGNAKATVDGQL 132
Cdd:PRK05174 110 GEVKFTGQVLPTaKKVTYEIDIKRVinrKLVMGIADGRVLVDGEE 154
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 88-142 9.97e-03

MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but without the N-terminal PutA domain. This protein family has a hot-dog fold similar to that of (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.


Pssm-ID: 239530 [Multi-domain]  Cd Length: 140  Bit Score: 34.20  E-value: 9.97e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 613388745  88 FAGIDKCRFKRQVVPGDTLTLEVEI--TKIKGP--IGKGNAKATV---DGQLACSCELTFAI 142
Cdd:cd03446   79 FYGIDNLRFLNPVFIGDTIRAEAEVveKEEKDGedAGVVTRRIEVvnqRGEVVQSGEMSLLV 140
 
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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