NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|12722436|gb|AAK04079|]
View 

FabZ [Pasteurella multocida subsp. multocida str. Pm70]

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;
9-150 9.00e-93

3-hydroxyacyl-ACP dehydratase FabZ;


:

Pssm-ID: 234568  Cd Length: 147  Bit Score: 265.05  E-value: 9.00e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12722436    9 KIIEANEIMKLLPHRYPFLLVDRVVDYEEGKWLKAVKNISVNEPCFTGHFPEQPIFPGVLILEAMAQATGVLACKTYRQl 88
Cdd:PRK00006   5 MMLDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSEEN- 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12722436   89 ENEIYYFAAIDNARFKRPVLPGDQMVLEVHFLKERRGITRFTGVATVDGQVVCEAELMCARR 150
Cdd:PRK00006  84 KGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIR 145
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
9-150 9.00e-93

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 265.05  E-value: 9.00e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12722436    9 KIIEANEIMKLLPHRYPFLLVDRVVDYEEGKWLKAVKNISVNEPCFTGHFPEQPIFPGVLILEAMAQATGVLACKTYRQl 88
Cdd:PRK00006   5 MMLDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSEEN- 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12722436   89 ENEIYYFAAIDNARFKRPVLPGDQMVLEVHFLKERRGITRFTGVATVDGQVVCEAELMCARR 150
Cdd:PRK00006  84 KGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIR 145
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 14-152 7.50e-74

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: 216.99  E-value: 7.50e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12722436  14 NEIMKLLPHRYPFLLVDRVVDYEEGKWLKAVKNISVNEPCFTGHFPEQPIFPGVLILEAMAQATGVLACKTY-RQLENEI 92
Cdd:COG0764   2 EEILALLPHRYPFLLVDRVLEIDPGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEgLEGKGRL 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 12722436  93 YYFAAIDNARFKRPVLPGDQMVLEVHFLKERRGITRFTGVATVDGQVVCEAELMCARRPA 152
Cdd:COG0764  82 VYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFALVEK 141
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 20-150 4.21e-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: 214.71  E-value: 4.21e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12722436  20 LPHRYPFLLVDRVVDYEEGKWLKAVKNISVNEPCFTGHFPEQPIFPGVLILEAMAQATGVLACKTYRQLENEIYYFAAID 99
Cdd:cd01288   1 LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLEDFEGKLVYFAGID 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 12722436 100 NARFKRPVLPGDQMVLEVHFLKERRGITRFTGVATVDGQVVCEAELMCARR 150
Cdd:cd01288  81 KARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELMFAIA 131
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 12-148 1.47e-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: 208.71  E-value: 1.47e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12722436    12 EANEIMKLLPHRYPFLLVDRVVDYEEGKWLKAVKNISVNEPCFTGHFPEQPIFPGVLILEAMAQATGVLAcktYRQLENE 91
Cdd:TIGR01750   1 DIQDIMELLPHRYPFLLVDRILELEPGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLA---ILSLGGE 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12722436    92 -----IYYFAAIDNARFKRPVLPGDQMVLEVHFLKERRGITRFTGVATVDGQVVCEAELMCA 148
Cdd:TIGR01750  78 kgkgkLVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIMFA 139
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 20-144 5.38e-41

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 133.56  E-value: 5.38e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12722436    20 LPHRYpFLLVDRVVDYEE--GKW----LKAVKNISVNEPCFTGHFPEQPIFPGVLILEAMAQATGVLAckTYRQLENEIY 93
Cdd:pfam07977   1 LPHRY-FLMLDRVTEIDPdgGKFgkgyIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYA--IWSGGGEGRG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 12722436    94 YFAAIDNARFKRPVLPGD-QMVLEVHFLK---ERRGITRFTGVATVDGQVVCEAE 144
Cdd:pfam07977  78 RARGVDEVKFRGQVTPGDkQLRYEVEIKKiieGRRGIGIADGRALVDGKVVYEAK 132
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
9-150 9.00e-93

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 265.05  E-value: 9.00e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12722436    9 KIIEANEIMKLLPHRYPFLLVDRVVDYEEGKWLKAVKNISVNEPCFTGHFPEQPIFPGVLILEAMAQATGVLACKTYRQl 88
Cdd:PRK00006   5 MMLDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSEEN- 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12722436   89 ENEIYYFAAIDNARFKRPVLPGDQMVLEVHFLKERRGITRFTGVATVDGQVVCEAELMCARR 150
Cdd:PRK00006  84 KGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIR 145
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 14-152 7.50e-74

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: 216.99  E-value: 7.50e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12722436  14 NEIMKLLPHRYPFLLVDRVVDYEEGKWLKAVKNISVNEPCFTGHFPEQPIFPGVLILEAMAQATGVLACKTY-RQLENEI 92
Cdd:COG0764   2 EEILALLPHRYPFLLVDRVLEIDPGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEgLEGKGRL 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 12722436  93 YYFAAIDNARFKRPVLPGDQMVLEVHFLKERRGITRFTGVATVDGQVVCEAELMCARRPA 152
Cdd:COG0764  82 VYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFALVEK 141
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 20-150 4.21e-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: 214.71  E-value: 4.21e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12722436  20 LPHRYPFLLVDRVVDYEEGKWLKAVKNISVNEPCFTGHFPEQPIFPGVLILEAMAQATGVLACKTYRQLENEIYYFAAID 99
Cdd:cd01288   1 LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLEDFEGKLVYFAGID 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 12722436 100 NARFKRPVLPGDQMVLEVHFLKERRGITRFTGVATVDGQVVCEAELMCARR 150
Cdd:cd01288  81 KARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELMFAIA 131
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 12-148 1.47e-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: 208.71  E-value: 1.47e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12722436    12 EANEIMKLLPHRYPFLLVDRVVDYEEGKWLKAVKNISVNEPCFTGHFPEQPIFPGVLILEAMAQATGVLAcktYRQLENE 91
Cdd:TIGR01750   1 DIQDIMELLPHRYPFLLVDRILELEPGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLA---ILSLGGE 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12722436    92 -----IYYFAAIDNARFKRPVLPGDQMVLEVHFLKERRGITRFTGVATVDGQVVCEAELMCA 148
Cdd:TIGR01750  78 kgkgkLVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIMFA 139
PRK13188 PRK13188
bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R) ...
 10-146 6.00e-60

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: 191.68  E-value: 6.00e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12722436   10 IIEANEIMKLLPHRYPFLLVDRVVDYEEGKwLKAVKNISVNEPCFTGHFPEQPIFPGVLILEAMAQATGVLACKTYRQLE 89
Cdd:PRK13188 320 ILDINRIMKILPHRYPFLLVDKIIELGDTK-IVGIKNVTMNEPFFQGHFPGNPVMPGVLQIEAMAQTGGILVLNTVPDPE 398

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 12722436   90 NEIYYFAAIDNARFKRPVLPGDQMVLEVHFLKE-RRGITRFTGVATVDGQVVCEAELM 146
Cdd:PRK13188 399 NYSTYFMKIDKVKFRQKVVPGDTLIFKVELLSPiRRGICQMQGKAYVNGKLVCEAELM 456
FabA_FabZ cd00493
FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct ...
 21-148 8.47e-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: 176.32  E-value: 8.47e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12722436  21 PHRYPFLLVDRVVDYEEGKWLKAVKNISVNEPCFTGHFPEQPIFPGVLILEAMAQATGVLACKTYRQLENE--IYYFAAI 98
Cdd:cd00493   1 PHRYPMLLVDRVLEIDPGGRIVAEKNVTPNEPFFQGHFPGDPVMPGVLGIEAMAQAAAALAGLLGLGKGNPprLGYLAGV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 12722436  99 DNARFKRPVLPGDQMVLEVHFLKERRGITRFTGVATVDGQVVCEAELMCA 148
Cdd:cd00493  81 RKVKFRGPVLPGDTLTLEVELLKVRRGLGKFDGRAYVDGKLVAEAELMAA 130
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 20-144 5.38e-41

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 133.56  E-value: 5.38e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12722436    20 LPHRYpFLLVDRVVDYEE--GKW----LKAVKNISVNEPCFTGHFPEQPIFPGVLILEAMAQATGVLAckTYRQLENEIY 93
Cdd:pfam07977   1 LPHRY-FLMLDRVTEIDPdgGKFgkgyIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYA--IWSGGGEGRG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 12722436    94 YFAAIDNARFKRPVLPGD-QMVLEVHFLK---ERRGITRFTGVATVDGQVVCEAE 144
Cdd:pfam07977  78 RARGVDEVKFRGQVTPGDkQLRYEVEIKKiieGRRGIGIADGRALVDGKVVYEAK 132
COG4706 COG4706
Predicted 3-hydroxylacyl-ACP dehydratase, HotDog domain [Lipid transport and metabolism];
16-145 4.19e-10

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


Pssm-ID: 443741  Cd Length: 149  Bit Score: 54.49  E-value: 4.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12722436  16 IMKLLPHRYPFLLVDRVVDYEEGkWLKAVKNISVNEPCFTGHFpeqpiFPGVLILEAMAQATGVLACKTYRQLENEIY-- 93
Cdd:COG4706  10 IAALIPHRGPMCLLDRVLAWDEE-SAVAEVTIRPDNPFRDDGG-----LPAWVGIEYMAQAVAAHGGLLARAAGEPPRlg 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 12722436  94 YFAAIDNARFKRPVLP-GDQMVLEVHFLKERRGITRFTGVATVDGQVVCEAEL 145
Cdd:COG4706  84 FLLGVRKVELHVPRFPvGETLRIEAERLLQDEGLGLFECRIRAGGELLASGRL 136
FabA cd01287
FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the ...
 25-146 6.32e-10

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: 54.18  E-value: 6.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12722436  25 PFLLVDRV--VDYEEGKW----LKAVKNISVNEPCFTGHFPEQPIFPGVLILEAMAQATGVLACKTYRQLENEIYYFAAI 98
Cdd:cd01287   7 QLLMLDRVteIDPGGGTFglgyLRAEKDIDPDDWFFPCHFHGDPVMPGSLGLEAMIQLLQFYLIWLGLGTGVDNPRFQGA 86

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 12722436  99 DNA----RFKRPVLPGD-QMVLEVHFLKERRGITRFTGVA----TVDGQVVCEAELM 146
Cdd:cd01287  87 PGGpgewKYRGQITPHNkKVTYEVHIKEVGRDGPRPYIIAdaslWVDGLRIYEAKDI 143
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 61-148 1.03e-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: 49.78  E-value: 1.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12722436  61 QPIFPGVLILEAMAQATGVLAcktYRQLENEIYYFAAIDNARFKRPVLPGDQMVLEVHFLKERRGITRFTGVATV-DGQV 139
Cdd:cd03440  15 GGIVHGGLLLALADEAAGAAA---ARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNeDGKL 91


                ....*....
gi 12722436 140 VCEAELMCA 148
Cdd:cd03440  92 VATATATFV 100
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
55-151 5.82e-05

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 40.64  E-value: 5.82e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12722436  55 TGHFPeQPIFPGVLIleaMAQATGVLAcktyRQLENEIYYFAAIDNARFKRPVLPGDQMVLEVHFL----KERRGITRFT 130
Cdd:COG2030  45 ATGFG-GRIAHGMLT---LSLASGLLV----DDLPGTAVANLGLQEVRFLRPVRVGDTLRARVEVLekreSKSRGIVTLR 116

                        90       100
                ....*....|....*....|....
gi 12722436 131 GVAT-VDGQVVCEAE--LMCARRP 151
Cdd:COG2030 117 TTVTnQDGEVVLTGEatVLVPRRP 140
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 97-146 7.79e-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: 37.55  E-value: 7.79e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 12722436  97 AIDNARFKRPVLPGDQM-----VLEVHFLKER--RGITRFTGVATV-DGQVVCEAELM 146
Cdd:cd03454  79 GIDELRWPRPVRPGDTLsveveVLDKRPSRSRpdRGIVTLRSETLNqRGEVVLTFEAT 136
PRK05174 PRK05174
bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase;
25-78 3.72e-03

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


Pssm-ID: 179953  Cd Length: 172  Bit Score: 35.96  E-value: 3.72e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 12722436   25 PFLLVDRVVDYEE-----GK-WLKAVKNISVNEPCFTGHFPEQPIFPGVLILEAMAQATG 78
Cdd:PRK05174  33 PMLMMDRITEISEtggefGKgYIVAELDINPDLWFFGCHFIGDPVMPGCLGLDAMWQLVG 92
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 98-144 4.15e-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: 35.32  E-value: 4.15e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 12722436  98 IDNARFKRPVLPGDQMVLEVHFL----KERRGITRFTGVATV-DGQVVCEAE 144
Cdd:cd03441  72 SQSVRFLAPVFPGDTLRVEVEVLgkrpSKGRGVVTVRTEARNqGGEVVLSGE 123
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 61-145 9.49e-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: 34.59  E-value: 9.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12722436  61 QPIFPGVLILeamAQATGVLacKTYRQLENEIYYFAAIDNARFKRPVLPGD--QMVLEVHFLKERRG-----ITRFTGVA 133
Cdd:cd03446  50 ERIAHGLLTL---SIATGLL--QRLGVFERTVVAFYGIDNLRFLNPVFIGDtiRAEAEVVEKEEKDGedagvVTRRIEVV 124

                        90
                ....*....|..
gi 12722436 134 TVDGQVVCEAEL 145
Cdd:cd03446 125 NQRGEVVQSGEM 136
 
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