NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|522053661|ref|WP_020564870|]
View 

3-hydroxyacyl-ACP dehydratase FabZ [Methylosarcina fibrata]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
5-145 7.39e-88

3-hydroxyacyl-ACP dehydratase FabZ;


:

Pssm-ID: 234568  Cd Length: 147  Bit Score: 252.34  E-value: 7.39e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053661   5 LDILQIQDFLPHRYPFLLVDKVIECEPGIRLLGVKNVTYNEPFFQGHFPQRPVMPGVLILEALAQTTGLLASETSPDvlR 84
Cdd:PRK00006   7 LDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSEEN--K 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522053661  85 GMIYYLVGIDKAKFKRPVVPGDQLMLEAKFLKSKRNIWAFDCCAEVDGEFVASAEIRCAAV 145
Cdd:PRK00006  85 GKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIR 145
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
5-145 7.39e-88

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 252.34  E-value: 7.39e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053661   5 LDILQIQDFLPHRYPFLLVDKVIECEPGIRLLGVKNVTYNEPFFQGHFPQRPVMPGVLILEALAQTTGLLASETSPDvlR 84
Cdd:PRK00006   7 LDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSEEN--K 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522053661  85 GMIYYLVGIDKAKFKRPVVPGDQLMLEAKFLKSKRNIWAFDCCAEVDGEFVASAEIRCAAV 145
Cdd:PRK00006  85 GKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIR 145
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 14-145 2.74e-72

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: 212.40  E-value: 2.74e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053661  14 LPHRYPFLLVDKVIECEPGIRLLGVKNVTYNEPFFQGHFPQRPVMPGVLILEALAQTTGLLASEtSPDVLRGMIYYLVGI 93
Cdd:cd01288    1 LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLK-SLEDFEGKLVYFAGI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 522053661  94 DKAKFKRPVVPGDQLMLEAKFLKSKRNIWAFDCCAEVDGEFVASAEIRCAAV 145
Cdd:cd01288   80 DKARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELMFAIA 131
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 7-145 1.19e-71

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: 211.21  E-value: 1.19e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053661   7 ILQIQDFLPHRYPFLLVDKVIECEPGIRLLGVKNVTYNEPFFQGHFPQRPVMPGVLILEALAQTTGLLASETSPDVLRGM 86
Cdd:COG0764    1 IEEILALLPHRYPFLLVDRVLEIDPGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEGLEGKGR 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 522053661  87 IYYLVGIDKAKFKRPVVPGDQLMLEAKFLKSKRNIWAFDCCAEVDGEFVASAEIRCAAV 145
Cdd:COG0764   81 LVYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFALV 139
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 6-143 1.55e-71

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: 211.02  E-value: 1.55e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053661    6 DILQIQDFLPHRYPFLLVDKVIECEPGIRLLGVKNVTYNEPFFQGHFPQRPVMPGVLILEALAQTTGLLASeTSPDVLR- 84
Cdd:TIGR01750   1 DIQDIMELLPHRYPFLLVDRILELEPGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAI-LSLGGEKg 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053661   85 -GMIYYLVGIDKAKFKRPVVPGDQLMLEAKFLKSKRNIWAFDCCAEVDGEFVASAEIRCA 143
Cdd:TIGR01750  80 kGKLVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIMFA 139
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 14-139 4.95e-41

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 133.56  E-value: 4.95e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053661   14 LPHRYpFLLVDKVIECEPG------IRLLGVKNVTYNEPFFQGHFPQRPVMPGVLILEALAQTTGLLASETSPDVLRGMi 87
Cdd:pfam07977   1 LPHRY-FLMLDRVTEIDPDggkfgkGYIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWSGGGEGRGR- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 522053661   88 yyLVGIDKAKFKRPVVPGD-QLMLEAKFLK---SKRNIWAFDCCAEVDGEFVASAE 139
Cdd:pfam07977  79 --ARGVDEVKFRGQVTPGDkQLRYEVEIKKiieGRRGIGIADGRALVDGKVVYEAK 132
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
5-145 7.39e-88

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 252.34  E-value: 7.39e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053661   5 LDILQIQDFLPHRYPFLLVDKVIECEPGIRLLGVKNVTYNEPFFQGHFPQRPVMPGVLILEALAQTTGLLASETSPDvlR 84
Cdd:PRK00006   7 LDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSEEN--K 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 522053661  85 GMIYYLVGIDKAKFKRPVVPGDQLMLEAKFLKSKRNIWAFDCCAEVDGEFVASAEIRCAAV 145
Cdd:PRK00006  85 GKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIR 145
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 14-145 2.74e-72

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: 212.40  E-value: 2.74e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053661  14 LPHRYPFLLVDKVIECEPGIRLLGVKNVTYNEPFFQGHFPQRPVMPGVLILEALAQTTGLLASEtSPDVLRGMIYYLVGI 93
Cdd:cd01288    1 LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLK-SLEDFEGKLVYFAGI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 522053661  94 DKAKFKRPVVPGDQLMLEAKFLKSKRNIWAFDCCAEVDGEFVASAEIRCAAV 145
Cdd:cd01288   80 DKARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELMFAIA 131
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 7-145 1.19e-71

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: 211.21  E-value: 1.19e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053661   7 ILQIQDFLPHRYPFLLVDKVIECEPGIRLLGVKNVTYNEPFFQGHFPQRPVMPGVLILEALAQTTGLLASETSPDVLRGM 86
Cdd:COG0764    1 IEEILALLPHRYPFLLVDRVLEIDPGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEGLEGKGR 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 522053661  87 IYYLVGIDKAKFKRPVVPGDQLMLEAKFLKSKRNIWAFDCCAEVDGEFVASAEIRCAAV 145
Cdd:COG0764   81 LVYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFALV 139
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 6-143 1.55e-71

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: 211.02  E-value: 1.55e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053661    6 DILQIQDFLPHRYPFLLVDKVIECEPGIRLLGVKNVTYNEPFFQGHFPQRPVMPGVLILEALAQTTGLLASeTSPDVLR- 84
Cdd:TIGR01750   1 DIQDIMELLPHRYPFLLVDRILELEPGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAI-LSLGGEKg 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053661   85 -GMIYYLVGIDKAKFKRPVVPGDQLMLEAKFLKSKRNIWAFDCCAEVDGEFVASAEIRCA 143
Cdd:TIGR01750  80 kGKLVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIMFA 139
PRK13188 PRK13188
bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R) ...
 3-147 3.66e-58

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: 187.06  E-value: 3.66e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053661   3 VKLDILQIQDFLPHRYPFLLVDKVIECEPGiRLLGVKNVTYNEPFFQGHFPQRPVMPGVLILEALAQTTGLLASETSPDV 82
Cdd:PRK13188 319 PILDINRIMKILPHRYPFLLVDKIIELGDT-KIVGIKNVTMNEPFFQGHFPGNPVMPGVLQIEAMAQTGGILVLNTVPDP 397

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 522053661  83 lRGMIYYLVGIDKAKFKRPVVPGDQLMLEAKFLKS-KRNIWAFDCCAEVDGEFVASAEIRcAAVVD 147
Cdd:PRK13188 398 -ENYSTYFMKIDKVKFRQKVVPGDTLIFKVELLSPiRRGICQMQGKAYVNGKLVCEAELM-AQIVK 461
FabA_FabZ cd00493
FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct ...
 15-144 6.67e-57

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: 173.62  E-value: 6.67e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053661  15 PHRYPFLLVDKVIECEPGIRLLGVKNVTYNEPFFQGHFPQRPVMPGVLILEALAQTTGLLASETSPDVL-RGMIYYLVGI 93
Cdd:cd00493    1 PHRYPMLLVDRVLEIDPGGRIVAEKNVTPNEPFFQGHFPGDPVMPGVLGIEAMAQAAAALAGLLGLGKGnPPRLGYLAGV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 522053661  94 DKAKFKRPVVPGDQLMLEAKFLKSKRNIWAFDCCAEVDGEFVASAEIRCAA 144
Cdd:cd00493   81 RKVKFRGPVLPGDTLTLEVELLKVRRGLGKFDGRAYVDGKLVAEAELMAAA 131
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 14-139 4.95e-41

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 133.56  E-value: 4.95e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053661   14 LPHRYpFLLVDKVIECEPG------IRLLGVKNVTYNEPFFQGHFPQRPVMPGVLILEALAQTTGLLASETSPDVLRGMi 87
Cdd:pfam07977   1 LPHRY-FLMLDRVTEIDPDggkfgkGYIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWSGGGEGRGR- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 522053661   88 yyLVGIDKAKFKRPVVPGD-QLMLEAKFLK---SKRNIWAFDCCAEVDGEFVASAE 139
Cdd:pfam07977  79 --ARGVDEVKFRGQVTPGDkQLRYEVEIKKiieGRRGIGIADGRALVDGKVVYEAK 132
COG4706 COG4706
Predicted 3-hydroxylacyl-ACP dehydratase, HotDog domain [Lipid transport and metabolism];
1-140 2.32e-13

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


Pssm-ID: 443741  Cd Length: 149  Bit Score: 62.96  E-value: 2.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053661   1 MSVKLDILQIQDFLPHRYPFLLVDKVIECEPGiRLLGVKNVTYNEPFFQGHFpqrpvMPGVLILEALAQT----TGLLAS 76
Cdd:COG4706    1 MNPTLDRPPIAALIPHRGPMCLLDRVLAWDEE-SAVAEVTIRPDNPFRDDGG-----LPAWVGIEYMAQAvaahGGLLAR 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522053661  77 ETSPDVLRGmiyYLVGIDKAKFKRPVVP-GDQLMLEAKFLKSKRNIWAFDCCAEVDGEFVASAEI 140
Cdd:COG4706   75 AAGEPPRLG---FLLGVRKVELHVPRFPvGETLRIEAERLLQDEGLGLFECRIRAGGELLASGRL 136
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 39-143 2.20e-08

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: 49.01  E-value: 2.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053661  39 KNVTYNEPFFQGHfpqrpvMPGVLILEALAQTTGLLASETSPdvlRGMIYYLVGIDkAKFKRPVVPGDQLMLEAKFLKSK 118
Cdd:cd03440    5 LTVTPEDIDGGGI------VHGGLLLALADEAAGAAAARLGG---RGLGAVTLSLD-VRFLRPVRPGDTLTVEAEVVRVG 74

                         90       100
                 ....*....|....*....|....*.
gi 522053661 119 RNIWAFDCCAEV-DGEFVASAEIRCA 143
Cdd:cd03440   75 RSSVTVEVEVRNeDGKLVATATATFV 100
FabA cd01287
FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the ...
 19-77 3.08e-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: 49.56  E-value: 3.08e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 522053661  19 PFLLVDKVIECEPGI------RLLGVKNVTYNEPFFQGHFPQRPVMPGVLILEALAQTTGLLASE 77
Cdd:cd01287    7 QLLMLDRVTEIDPGGgtfglgYLRAEKDIDPDDWFFPCHFHGDPVMPGSLGLEAMIQLLQFYLIW 71
PRK05174 PRK05174
bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase;
47-72 2.03e-04

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


Pssm-ID: 179953  Cd Length: 172  Bit Score: 39.43  E-value: 2.03e-04
                         10        20
                 ....*....|....*....|....*.
gi 522053661  47 FFQGHFPQRPVMPGVLILEALAQTTG 72
Cdd:PRK05174  67 FFGCHFIGDPVMPGCLGLDAMWQLVG 92
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
49-139 3.43e-04

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 38.33  E-value: 3.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053661  49 QGHFPQRPVmPGVLILeALAqtTGLLAsetspDVLRGMIYYLVGIDKAKFKRPVVPGDQLMLEAKFL----KSKRNIWAF 124
Cdd:COG2030   45 ATGFGGRIA-HGMLTL-SLA--SGLLV-----DDLPGTAVANLGLQEVRFLRPVRVGDTLRARVEVLekreSKSRGIVTL 115

                         90
                 ....*....|....*.
gi 522053661 125 DC-CAEVDGEFVASAE 139
Cdd:COG2030  116 RTtVTNQDGEVVLTGE 131
FabA_like cd01289
Domain of unknown function, appears to be related to a diverse group of beta-hydroxydecanoyl ...
 9-138 1.03e-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: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053661   9 QIQDFLPHRYPFLLVDKVIECEP-GIRLlgvkNVTYNEpffQGHFP--QRPVMPGVLILEALAQTT----GLLASETSPD 81
Cdd:cd01289    2 WIAALIPHDGPMCLLDRVISWDDdSIHC----RATVHP---DPLFPlrAHGRLPAWVGIEYMAQAIaahgGLLARQQGNP 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 522053661  82 VLRGmiyYLVGIDKAKFKRPVVPGDQLML--EAKFLKSKRNIWAFDCCAEVDGEFVASA 138
Cdd:cd01289   75 PRPG---FLLGSRKYEAHVDRFDLGSTLLivVAELLQGDSGLGVFECTIEDQGGVLASG 130
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 31-145 4.15e-03

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 35.30  E-value: 4.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053661  31 PGIRLLGVKNVTYNEPFFQGHFPQRPVM---PGVL---ILEALAQTTGLLASETSPDVLRGMiyylVGID-KAKFKRPVV 103
Cdd:COG2050   16 PFAELLGIELVEVEPGRAVLRLPVRPEHlnpPGTVhggALAALADSAAGLAANSALPPGRRA----VTIElNINFLRPAR 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 522053661 104 PGDQLMLEAKFLKSKRNIWAFDccAEV---DGEFVASAEIRCAAV 145
Cdd:COG2050   92 LGDRLTAEARVVRRGRRLAVVE--VEVtdeDGKLVATATGTFAVL 134
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH