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Conserved domains on  [gi|469727659|gb|EMQ42100|]
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beta-hydroxyacyl-(acyl-carrier-protein) dehydratase FabZ [Vibrio cholerae O1 str. Nep-21113]

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;
1-142 3.65e-92

3-hydroxyacyl-ACP dehydratase FabZ;


:

Pssm-ID: 234568  Cd Length: 147  Bit Score: 263.13  E-value: 3.65e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469727659   1 MNITEIQSLLPHRYPFLLIDRVTDYEEGKYLIGLKNVSVNEPQFTGHFPQLPVFPGVLILEAMAQATGLLAFKTfgAPKE 80
Cdd:PRK00006   7 LDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKS--EENK 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 469727659  81 NELYYFASIDEAKFRKPVTPGDQLMVEVEFLKERRGIALFNGVAKVDGDVVCSAQLKCARRE 142
Cdd:PRK00006  85 GKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRD 146
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
1-142 3.65e-92

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 263.13  E-value: 3.65e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469727659   1 MNITEIQSLLPHRYPFLLIDRVTDYEEGKYLIGLKNVSVNEPQFTGHFPQLPVFPGVLILEAMAQATGLLAFKTfgAPKE 80
Cdd:PRK00006   7 LDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKS--EENK 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 469727659  81 NELYYFASIDEAKFRKPVTPGDQLMVEVEFLKERRGIALFNGVAKVDGDVVCSAQLKCARRE 142
Cdd:PRK00006  85 GKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRD 146
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 3-142 1.38e-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: 221.22  E-value: 1.38e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469727659   3 ITEIQSLLPHRYPFLLIDRVTDYEEGKYLIGLKNVSVNEPQFTGHFPQLPVFPGVLILEAMAQATGLLAFKTFGAPKENE 82
Cdd:COG0764    1 IEEILALLPHRYPFLLVDRVLEIDPGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEGLEGKGR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 469727659  83 LYYFASIDEAKFRKPVTPGDQLMVEVEFLKERRGIALFNGVAKVDGDVVCSAQLKCARRE 142
Cdd:COG0764   81 LVYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFALVE 140
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 10-141 1.80e-71

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: 210.48  E-value: 1.80e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469727659  10 LPHRYPFLLIDRVTDYEEGKYLIGLKNVSVNEPQFTGHFPQLPVFPGVLILEAMAQATGLLAFKTFGAPKeNELYYFASI 89
Cdd:cd01288    1 LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLEDFE-GKLVYFAGI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 469727659  90 DEAKFRKPVTPGDQLMVEVEFLKERRGIALFNGVAKVDGDVVCSAQLKCARR 141
Cdd:cd01288   80 DKARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELMFAIA 131
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 3-139 2.03e-70

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: 207.94  E-value: 2.03e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469727659    3 ITEIQSLLPHRYPFLLIDRVTDYEEGKYLIGLKNVSVNEPQFTGHFPQLPVFPGVLILEAMAQATGLLAFKTFGAPKEN- 81
Cdd:TIGR01750   2 IQDIMELLPHRYPFLLVDRILELEPGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILSLGGEKGKg 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 469727659   82 ELYYFASIDEAKFRKPVTPGDQLMVEVEFLKERRGIALFNGVAKVDGDVVCSAQLKCA 139
Cdd:TIGR01750  82 KLVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIMFA 139
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 10-135 7.93e-50

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 155.51  E-value: 7.93e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469727659   10 LPHRYpFLLIDRVTDYE-EGK-----YLIGLKNVSVNEPQFTGHFPQLPVFPGVLILEAMAQATGLLAFKTFGAPKENEL 83
Cdd:pfam07977   1 LPHRY-FLMLDRVTEIDpDGGkfgkgYIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWSGGGEGRGRA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 469727659   84 yyfASIDEAKFRKPVTPGD-QLMVEVEFLK---ERRGIALFNGVAKVDGDVVCSAQ 135
Cdd:pfam07977  80 ---RGVDEVKFRGQVTPGDkQLRYEVEIKKiieGRRGIGIADGRALVDGKVVYEAK 132
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
1-142 3.65e-92

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 263.13  E-value: 3.65e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469727659   1 MNITEIQSLLPHRYPFLLIDRVTDYEEGKYLIGLKNVSVNEPQFTGHFPQLPVFPGVLILEAMAQATGLLAFKTfgAPKE 80
Cdd:PRK00006   7 LDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKS--EENK 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 469727659  81 NELYYFASIDEAKFRKPVTPGDQLMVEVEFLKERRGIALFNGVAKVDGDVVCSAQLKCARRE 142
Cdd:PRK00006  85 GKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRD 146
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 3-142 1.38e-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: 221.22  E-value: 1.38e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469727659   3 ITEIQSLLPHRYPFLLIDRVTDYEEGKYLIGLKNVSVNEPQFTGHFPQLPVFPGVLILEAMAQATGLLAFKTFGAPKENE 82
Cdd:COG0764    1 IEEILALLPHRYPFLLVDRVLEIDPGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEGLEGKGR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 469727659  83 LYYFASIDEAKFRKPVTPGDQLMVEVEFLKERRGIALFNGVAKVDGDVVCSAQLKCARRE 142
Cdd:COG0764   81 LVYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFALVE 140
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 10-141 1.80e-71

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: 210.48  E-value: 1.80e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469727659  10 LPHRYPFLLIDRVTDYEEGKYLIGLKNVSVNEPQFTGHFPQLPVFPGVLILEAMAQATGLLAFKTFGAPKeNELYYFASI 89
Cdd:cd01288    1 LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLEDFE-GKLVYFAGI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 469727659  90 DEAKFRKPVTPGDQLMVEVEFLKERRGIALFNGVAKVDGDVVCSAQLKCARR 141
Cdd:cd01288   80 DKARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELMFAIA 131
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 3-139 2.03e-70

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: 207.94  E-value: 2.03e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469727659    3 ITEIQSLLPHRYPFLLIDRVTDYEEGKYLIGLKNVSVNEPQFTGHFPQLPVFPGVLILEAMAQATGLLAFKTFGAPKEN- 81
Cdd:TIGR01750   2 IQDIMELLPHRYPFLLVDRILELEPGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILSLGGEKGKg 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 469727659   82 ELYYFASIDEAKFRKPVTPGDQLMVEVEFLKERRGIALFNGVAKVDGDVVCSAQLKCA 139
Cdd:TIGR01750  82 KLVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIMFA 139
PRK13188 PRK13188
bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R) ...
 1-136 5.09e-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: 188.99  E-value: 5.09e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469727659   1 MNITEIQSLLPHRYPFLLIDRVTDYEEgKYLIGLKNVSVNEPQFTGHFPQLPVFPGVLILEAMAQATGLLAFKTFGAPkE 80
Cdd:PRK13188 321 LDINRIMKILPHRYPFLLVDKIIELGD-TKIVGIKNVTMNEPFFQGHFPGNPVMPGVLQIEAMAQTGGILVLNTVPDP-E 398

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 469727659  81 NELYYFASIDEAKFRKPVTPGDQLMVEVEFLKE-RRGIALFNGVAKVDGDVVCSAQL 136
Cdd:PRK13188 399 NYSTYFMKIDKVKFRQKVVPGDTLIFKVELLSPiRRGICQMQGKAYVNGKLVCEAEL 455
FabA_FabZ cd00493
FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct ...
 11-139 6.99e-59

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: 178.63  E-value: 6.99e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469727659  11 PHRYPFLLIDRVTDYEEGKYLIGLKNVSVNEPQFTGHFPQLPVFPGVLILEAMAQATGLLAFKTFGAP-KENELYYFASI 89
Cdd:cd00493    1 PHRYPMLLVDRVLEIDPGGRIVAEKNVTPNEPFFQGHFPGDPVMPGVLGIEAMAQAAAALAGLLGLGKgNPPRLGYLAGV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 469727659  90 DEAKFRKPVTPGDQLMVEVEFLKERRGIALFNGVAKVDGDVVCSAQLKCA 139
Cdd:cd00493   81 RKVKFRGPVLPGDTLTLEVELLKVRRGLGKFDGRAYVDGKLVAEAELMAA 130
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 10-135 7.93e-50

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 155.51  E-value: 7.93e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469727659   10 LPHRYpFLLIDRVTDYE-EGK-----YLIGLKNVSVNEPQFTGHFPQLPVFPGVLILEAMAQATGLLAFKTFGAPKENEL 83
Cdd:pfam07977   1 LPHRY-FLMLDRVTEIDpDGGkfgkgYIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWSGGGEGRGRA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 469727659   84 yyfASIDEAKFRKPVTPGD-QLMVEVEFLK---ERRGIALFNGVAKVDGDVVCSAQ 135
Cdd:pfam07977  80 ---RGVDEVKFRGQVTPGDkQLRYEVEIKKiieGRRGIGIADGRALVDGKVVYEAK 132
FabA cd01287
FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the ...
 15-130 4.49e-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: 59.58  E-value: 4.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469727659  15 PFLLIDRVT--DYEEGK----YLIGLKNVSVNEPQFTGHFPQLPVFPGVLILEAMAQATGLLAFKTFGAPKENELYYFAS 88
Cdd:cd01287    7 QLLMLDRVTeiDPGGGTfglgYLRAEKDIDPDDWFFPCHFHGDPVMPGSLGLEAMIQLLQFYLIWLGLGTGVDNPRFQGA 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 469727659  89 IDEA---KFRKPVTPGDQLMV-EVEFLK---ERRGIalfngVAKVDGDV 130
Cdd:cd01287   87 PGGPgewKYRGQITPHNKKVTyEVHIKEvgrDGPRP-----YIIADASL 130
COG4706 COG4706
Predicted 3-hydroxylacyl-ACP dehydratase, HotDog domain [Lipid transport and metabolism];
1-137 1.22e-11

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


Pssm-ID: 443741  Cd Length: 149  Bit Score: 58.34  E-value: 1.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469727659   1 MNITEIQSLLPHRYPFLLIDRVTDYEEGKyLIGLKNVSVNEPQFTGHFpqlpvFPGVLILEAMAQA----TGLLAFKTFG 76
Cdd:COG4706    5 LDRPPIAALIPHRGPMCLLDRVLAWDEES-AVAEVTIRPDNPFRDDGG-----LPAWVGIEYMAQAvaahGGLLARAAGE 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 469727659  77 APKeneLYYFASIDEAK-FRKPVTPGDQLMVEVEFLKERRGIALFNGVAKVDGDVVCSAQLK 137
Cdd:COG4706   79 PPR---LGFLLGVRKVElHVPRFPVGETLRIEAERLLQDEGLGLFECRIRAGGELLASGRLN 137
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 52-139 6.56e-09

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: 50.17  E-value: 6.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469727659  52 PVFPGVLILEAMAQATGLLAFKTFGAPKeneLYYFASIDeAKFRKPVTPGDQLMVEVEFLKERRGIALFNGVAKV-DGDV 130
Cdd:cd03440   16 GIVHGGLLLALADEAAGAAAARLGGRGL---GAVTLSLD-VRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNeDGKL 91


                 ....*....
gi 469727659 131 VCSAQLKCA 139
Cdd:cd03440   92 VATATATFV 100
PRK05174 PRK05174
bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase;
15-137 3.51e-05

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


Pssm-ID: 179953  Cd Length: 172  Bit Score: 41.35  E-value: 3.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469727659  15 PFLLIDRVTDYEE-----GK-YLIGLKNVSVNEPQFTGHFPQLPVFPGVLILEAMAQATGL-LAFKtfGAP-KENELyyf 86
Cdd:PRK05174  33 PMLMMDRITEISEtggefGKgYIVAELDINPDLWFFGCHFIGDPVMPGCLGLDAMWQLVGFyLGWL--GGPgKGRAL--- 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 469727659  87 aSIDEAKFRKPVTPGDQLMV-EVEFLKERR-----GIAlfNGVAKVDGDVVCSA-QLK 137
Cdd:PRK05174 108 -GVGEVKFTGQVLPTAKKVTyEIDIKRVINrklvmGIA--DGRVLVDGEEIYTAkDLK 162
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 89-133 1.25e-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: 39.47  E-value: 1.25e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 469727659  89 IDEAKFRKPVTPGDQLMVEVEFLKER-------RGIALFNGVAKV-DGDVVCS 133
Cdd:cd03454   80 IDELRWPRPVRPGDTLSVEVEVLDKRpsrsrpdRGIVTLRSETLNqRGEVVLT 132
FabA_like cd01289
Domain of unknown function, appears to be related to a diverse group of beta-hydroxydecanoyl ...
 6-79 1.05e-03

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: 36.86  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469727659   6 IQSLLPHRYPFLLIDRVTDYEEGKYLIGlknVSVNEpqfTGHFP-----QLPVFPGVlilEAMAQAT----GLLAFKTFG 76
Cdd:cd01289    3 IAALIPHDGPMCLLDRVISWDDDSIHCR---ATVHP---DPLFPlrahgRLPAWVGI---EYMAQAIaahgGLLARQQGN 73


                 ...
gi 469727659  77 APK 79
Cdd:cd01289   74 PPR 76
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 48-134 1.40e-03

FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved family of proteins found in prokaryotes and archaea but not in eukaryotes. FkbR2 has sequence similarity to (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. The function of FkbR2 is unknown.


Pssm-ID: 239535 [Multi-domain]  Cd Length: 146  Bit Score: 36.80  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469727659  48 FPQLPVFPGVLILEAMAQATGLLAFKTFGapkenELYYfasiDEAKFRKPVTPGDQLMVEVEFLKER-------RGIALF 120
Cdd:cd03451   51 FGRRLVNSLFTLSLALGLSVNDTSLTAVA-----NLGY----DEVRFPAPVFHGDTLYAESEVLSKResksrpdAGIVTV 121

                         90
                 ....*....|....*
gi 469727659 121 NGVA-KVDGDVVCSA 134
Cdd:cd03451  122 RTVGyNQDGEPVLSF 136
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
45-135 3.59e-03

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 35.25  E-value: 3.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469727659  45 TGHFPQLPVfPGVLIleaMAQATGLLAFKTFGAPKENelyyfASIDEAKFRKPVTPGDQLMVEVEFL----KERRGIALF 120
Cdd:COG2030   45 ATGFGGRIA-HGMLT---LSLASGLLVDDLPGTAVAN-----LGLQEVRFLRPVRVGDTLRARVEVLekreSKSRGIVTL 115

                         90
                 ....*....|....*.
gi 469727659 121 NGVAK-VDGDVVCSAQ 135
Cdd:COG2030  116 RTTVTnQDGEVVLTGE 131
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 91-142 5.56e-03

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 34.92  E-value: 5.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 469727659  91 EAKFRKPVTPGDQLMVEVEFLKERRGIALFNGVAKV-DGDVVCSAQLKCARRE 142
Cdd:COG2050   83 NINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDeDGKLVATATGTFAVLP 135
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 46-134 7.21e-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: 34.55  E-value: 7.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 469727659  46 GHFPQLPVfPGVLIL-EAMAQATGLLAFKTFGAPKENELyyfasideaKFRKPVTPGDQLMVEVEFL----KERRGIALF 120
Cdd:cd03441   38 AGFGGRIA-HGMLTLsLASGLLVQWLPGTDGANLGSQSV---------RFLAPVFPGDTLRVEVEVLgkrpSKGRGVVTV 107

                         90
                 ....*....|....*
gi 469727659 121 NGVAKV-DGDVVCSA 134
Cdd:cd03441  108 RTEARNqGGEVVLSG 122
 
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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