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Conserved domains on  [gi|145579410|pdb|2GLM|B]
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Chain B, (3R)-hydroxymyristoyl-acyl carrier protein dehydratase

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;
18-170 1.39e-81

3-hydroxyacyl-ACP dehydratase FabZ;


:

Pssm-ID: 234568  Cd Length: 147  Bit Score: 237.71  E-value: 1.39e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GLM_B        18 QNLQSQFFIEHILQILPHRYPMLLVDRITELQANQKIVAYKNITFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTS 97
Cdd:PRK00006   1 TTETMMLDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
2GLM_B        98 lwgfdpEIAKTKIVYFMTIDKVKFRIPVTPGDRLEYHLEVLKHKGMIWQVGGTAQVDGKVVAEAELKAMIAER 170
Cdd:PRK00006  81 ------EENKGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRDK 147
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
18-170 1.39e-81

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 237.71  E-value: 1.39e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GLM_B        18 QNLQSQFFIEHILQILPHRYPMLLVDRITELQANQKIVAYKNITFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTS 97
Cdd:PRK00006   1 TTETMMLDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
2GLM_B        98 lwgfdpEIAKTKIVYFMTIDKVKFRIPVTPGDRLEYHLEVLKHKGMIWQVGGTAQVDGKVVAEAELKAMIAER 170
Cdd:PRK00006  81 ------EENKGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRDK 147
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 25-167 4.44e-80

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: 233.75  E-value: 4.44e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GLM_B         25 FIEHILQILPHRYPMLLVDRITELQANQKIVAYKNITFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTSLWGfdpE 104
Cdd:TIGR01750   1 DIQDIMELLPHRYPFLLVDRILELEPGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILSLGG---E 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
2GLM_B        105 IAKTKIVYFMTIDKVKFRIPVTPGDRLEYHLEVLKHKGMIWQVGGTAQVDGKVVAEAELKAMI 167
Cdd:TIGR01750  78 KGKGKLVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIMFAI 140
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 33-168 1.18e-69

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: 207.01  E-value: 1.18e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GLM_B       33 LPHRYPMLLVDRITELQANQKIVAYKNITFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTSLWGFdpeiaKTKIVY 112
Cdd:cd01288   1 LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLEDF-----EGKLVY 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
2GLM_B      113 FMTIDKVKFRIPVTPGDRLEYHLEVLKHKGMIWQVGGTAQVDGKVVAEAELKAMIA 168
Cdd:cd01288  76 FAGIDKARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELMFAIA 131
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 26-170 3.12e-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: 206.20  E-value: 3.12e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GLM_B       26 IEHILQILPHRYPMLLVDRITELQANQKIVAYKNITFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTSLWgfdpEI 105
Cdd:COG0764   1 IEEILALLPHRYPFLLVDRVLEIDPGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEG----LE 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
2GLM_B      106 AKTKIVYFMTIDKVKFRIPVTPGDRLEYHLEVLKHKGMIWQVGGTAQVDGKVVAEAELKAMIAER 170
Cdd:COG0764  77 GKGRLVYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFALVEK 141
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 33-162 1.13e-39

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 130.86  E-value: 1.13e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GLM_B         33 LPHRYpMLLVDRITELQANQK------IVAYKNITFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTSlwGFDPEIA 106
Cdd:pfam07977   1 LPHRY-FLMLDRVTEIDPDGGkfgkgyIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWS--GGGEGRG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
2GLM_B        107 KtkivyFMTIDKVKFRIPVTPGD-RLEYHLEVLK---HKGMIWQVGGTAQVDGKVVAEAE 162
Cdd:pfam07977  78 R-----ARGVDEVKFRGQVTPGDkQLRYEVEIKKiieGRRGIGIADGRALVDGKVVYEAK 132
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
18-170 1.39e-81

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 237.71  E-value: 1.39e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GLM_B        18 QNLQSQFFIEHILQILPHRYPMLLVDRITELQANQKIVAYKNITFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTS 97
Cdd:PRK00006   1 TTETMMLDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
2GLM_B        98 lwgfdpEIAKTKIVYFMTIDKVKFRIPVTPGDRLEYHLEVLKHKGMIWQVGGTAQVDGKVVAEAELKAMIAER 170
Cdd:PRK00006  81 ------EENKGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRDK 147
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 25-167 4.44e-80

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: 233.75  E-value: 4.44e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GLM_B         25 FIEHILQILPHRYPMLLVDRITELQANQKIVAYKNITFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTSLWGfdpE 104
Cdd:TIGR01750   1 DIQDIMELLPHRYPFLLVDRILELEPGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILSLGG---E 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
2GLM_B        105 IAKTKIVYFMTIDKVKFRIPVTPGDRLEYHLEVLKHKGMIWQVGGTAQVDGKVVAEAELKAMI 167
Cdd:TIGR01750  78 KGKGKLVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIMFAI 140
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 33-168 1.18e-69

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: 207.01  E-value: 1.18e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GLM_B       33 LPHRYPMLLVDRITELQANQKIVAYKNITFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTSLWGFdpeiaKTKIVY 112
Cdd:cd01288   1 LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLEDF-----EGKLVY 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
2GLM_B      113 FMTIDKVKFRIPVTPGDRLEYHLEVLKHKGMIWQVGGTAQVDGKVVAEAELKAMIA 168
Cdd:cd01288  76 FAGIDKARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELMFAIA 131
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 26-170 3.12e-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: 206.20  E-value: 3.12e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GLM_B       26 IEHILQILPHRYPMLLVDRITELQANQKIVAYKNITFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTSLWgfdpEI 105
Cdd:COG0764   1 IEEILALLPHRYPFLLVDRVLEIDPGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEG----LE 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
2GLM_B      106 AKTKIVYFMTIDKVKFRIPVTPGDRLEYHLEVLKHKGMIWQVGGTAQVDGKVVAEAELKAMIAER 170
Cdd:COG0764  77 GKGRLVYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFALVEK 141
FabA_FabZ cd00493
FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct ...
 34-167 5.52e-56

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: 172.47  E-value: 5.52e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GLM_B       34 PHRYPMLLVDRITELQANQKIVAYKNITFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTSLWGfdpEIAKTKIVYF 113
Cdd:cd00493   1 PHRYPMLLVDRVLEIDPGGRIVAEKNVTPNEPFFQGHFPGDPVMPGVLGIEAMAQAAAALAGLLGLG---KGNPPRLGYL 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
2GLM_B      114 MTIDKVKFRIPVTPGDRLEYHLEVLKHKGMIWQVGGTAQVDGKVVAEAELKAMI 167
Cdd:cd00493  78 AGVRKVKFRGPVLPGDTLTLEVELLKVRRGLGKFDGRAYVDGKLVAEAELMAAA 131
PRK13188 PRK13188
bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R) ...
 26-170 2.70e-54

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: 177.82  E-value: 2.70e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GLM_B        26 IEHILQILPHRYPMLLVDRITELQANqKIVAYKNITFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTSLwgfdpEI 105
Cdd:PRK13188 323 INRIMKILPHRYPFLLVDKIIELGDT-KIVGIKNVTMNEPFFQGHFPGNPVMPGVLQIEAMAQTGGILVLNTV-----PD 396

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
2GLM_B       106 AKTKIVYFMTIDKVKFRIPVTPGDRLEYHLEVLKH-KGMIWQVGGTAQVDGKVVAEAELKAMIAER 170
Cdd:PRK13188 397 PENYSTYFMKIDKVKFRQKVVPGDTLIFKVELLSPiRRGICQMQGKAYVNGKLVCEAELMAQIVKK 462
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 33-162 1.13e-39

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 130.86  E-value: 1.13e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GLM_B         33 LPHRYpMLLVDRITELQANQK------IVAYKNITFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTSlwGFDPEIA 106
Cdd:pfam07977   1 LPHRY-FLMLDRVTEIDPDGGkfgkgyIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWS--GGGEGRG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
2GLM_B        107 KtkivyFMTIDKVKFRIPVTPGD-RLEYHLEVLK---HKGMIWQVGGTAQVDGKVVAEAE 162
Cdd:pfam07977  78 R-----ARGVDEVKFRGQVTPGDkQLRYEVEIKKiieGRRGIGIADGRALVDGKVVYEAK 132
COG4706 COG4706
Predicted 3-hydroxylacyl-ACP dehydratase, HotDog domain [Lipid transport and metabolism];
26-169 1.33e-08

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


Pssm-ID: 443741  Cd Length: 149  Bit Score: 51.02  E-value: 1.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GLM_B       26 IEHILQILPHRYPMLLVDRITELQANQkIVAYKNITfNEDVF--NGHfpnkpiFPGVLIVEGMAQS----GGFLAFTSlw 99
Cdd:COG4706   7 RPPIAALIPHRGPMCLLDRVLAWDEES-AVAEVTIR-PDNPFrdDGG------LPAWVGIEYMAQAvaahGGLLARAA-- 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2GLM_B      100 GFDPEIAktkivYFMTIDKVKFRIPVTP-GDRLEYHLEVLKHKGMIWQVGGTAQVDGKVVAEAELKAMIAE 169
Cdd:COG4706  77 GEPPRLG-----FLLGVRKVELHVPRFPvGETLRIEAERLLQDEGLGLFECRIRAGGELLASGRLNVFQPA 142
FabA cd01287
FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the ...
 38-170 1.89e-07

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: 48.02  E-value: 1.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GLM_B       38 PMLLVDRITELQANQ------KIVAYKNITFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGFLAFTSLWGFDPEIAKTKIV 111
Cdd:cd01287   7 QLLMLDRVTEIDPGGgtfglgYLRAEKDIDPDDWFFPCHFHGDPVMPGSLGLEAMIQLLQFYLIWLGLGTGVDNPRFQGA 86

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2GLM_B      112 YFMTIdKVKFRIPVTPGD-RLEYHLEV-----------LKHKGMIWqvggtaqVDGKVVAEA-ELKAMIAER 170
Cdd:cd01287  87 PGGPG-EWKYRGQITPHNkKVTYEVHIkevgrdgprpyIIADASLW-------VDGLRIYEAkDIAVRLVEA 150
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
116-171 2.05e-06

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 44.88  E-value: 2.05e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
2GLM_B      116 IDKVKFRIPVTPGDRLEYHLEVL-----KHKGMI-WQVGGTAQvDGKVVAEAELKAMIAERE 171
Cdd:COG2030  80 LQEVRFLRPVRVGDTLRARVEVLekresKSRGIVtLRTTVTNQ-DGEVVLTGEATVLVPRRP 140
PRK05174 PRK05174
bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase;
38-92 4.46e-06

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


Pssm-ID: 179953  Cd Length: 172  Bit Score: 44.43  E-value: 4.46e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
2GLM_B        38 PMLLVDRITELQANQ------KIVAYKNITFNEDVFNGHFPNKPIFPGVLIVEGMAQSGGF 92
Cdd:PRK05174  33 PMLMMDRITEISETGgefgkgYIVAELDINPDLWFFGCHFIGDPVMPGCLGLDAMWQLVGF 93
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 54-166 1.09e-05

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: 42.08  E-value: 1.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GLM_B       54 IVAYKNITFNEDVFNGHFPnkpifpGVLIVEGMAQSGGFLAFTSLWGfdpeiaktKIVYFMTIDKVKFRIPVTPGDRLEY 133
Cdd:cd03440   1 FVLRLTVTPEDIDGGGIVH------GGLLLALADEAAGAAAARLGGR--------GLGAVTLSLDVRFLRPVRPGDTLTV 66

                        90       100       110
                ....*....|....*....|....*....|....
2GLM_B      134 HLEVLKHKGMIWQVGGTA-QVDGKVVAEAELKAM 166
Cdd:cd03440  67 EAEVVRVGRSSVTVEVEVrNEDGKLVATATATFV 100
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 116-168 1.32e-03

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: 37.16  E-value: 1.32e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
2GLM_B      116 IDKVKFRIPVTPGDRLEYHLEVLKHK--------GMI-WQVGGTAQvDGKVVAEAELKAMIA 168
Cdd:cd03454  80 IDELRWPRPVRPGDTLSVEVEVLDKRpsrsrpdrGIVtLRSETLNQ-RGEVVLTFEATVLVR 140
FabA_like cd01289
Domain of unknown function, appears to be related to a diverse group of beta-hydroxydecanoyl ...
 28-94 4.42e-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: 35.70  E-value: 4.42e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2GLM_B       28 HILQILPHRYPMLLVDRITELQANQkIVAykNITFNEDVFNGHFPNKPIfPGVLIVEGMAQS----GGFLA 94
Cdd:cd01289   2 WIAALIPHDGPMCLLDRVISWDDDS-IHC--RATVHPDPLFPLRAHGRL-PAWVGIEYMAQAiaahGGLLA 68
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 76-166 9.88e-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: 9.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2GLM_B       76 IFPGvLIVEGMAQSGGFLAFTSLWGFDPEIAktkivyFMTIDKVKFRIPVTPGDRLEYHLEVL-----KHKGMI-WQVGG 149
Cdd:cd03441  39 GFGG-RIAHGMLTLSLASGLLVQWLPGTDGA------NLGSQSVRFLAPVFPGDTLRVEVEVLgkrpsKGRGVVtVRTEA 111

                        90
                ....*....|....*..
2GLM_B      150 TAQvDGKVVAEAELKAM 166
Cdd:cd03441 112 RNQ-GGEVVLSGEATVL 127
 
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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