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Conserved domains on  [gi|1055298883|ref|WP_066965345|]
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MULTISPECIES: 3-hydroxyacyl-ACP dehydratase FabZ [Microbulbifer]

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;
1-145 5.91e-89

3-hydroxyacyl-ACP dehydratase FabZ;


:

Pssm-ID: 234568  Cd Length: 147  Bit Score: 255.04  E-value: 5.91e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055298883   1 MMDVQEIRQYLPHRYPFLLVDRVVELEEGKLIKGFKNISINEEVFNGHFPEVPIFPGVMIVEALAQVSGILGFKTLgqkP 80
Cdd:PRK00006    6 MLDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSE---E 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1055298883  81 EDGYLYLFAGIDNVRFKRQVVPGDRLQLESQVVSERRGIWKFAGKASVDGELAASADILCAVKKI 145
Cdd:PRK00006   83 NKGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRDK 147
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
1-145 5.91e-89

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 255.04  E-value: 5.91e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055298883   1 MMDVQEIRQYLPHRYPFLLVDRVVELEEGKLIKGFKNISINEEVFNGHFPEVPIFPGVMIVEALAQVSGILGFKTLgqkP 80
Cdd:PRK00006    6 MLDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSE---E 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1055298883  81 EDGYLYLFAGIDNVRFKRQVVPGDRLQLESQVVSERRGIWKFAGKASVDGELAASADILCAVKKI 145
Cdd:PRK00006   83 NKGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRDK 147
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 3-142 5.00e-73

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: 214.87  E-value: 5.00e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055298883   3 DVQEIRQYLPHRYPFLLVDRVVELEEGKLIKGFKNISINEEVFNGHFPEVPIFPGVMIVEALAQVSGILGFKTLGQKPED 82
Cdd:TIGR01750   1 DIQDIMELLPHRYPFLLVDRILELEPGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILSLGGEKGK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055298883  83 GYLYLFAGIDNVRFKRQVVPGDRLQLESQVVSERRGIWKFAGKASVDGELAASADILCAV 142
Cdd:TIGR01750  81 GKLVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIMFAI 140
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 11-143 3.12e-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: 209.71  E-value: 3.12e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055298883  11 LPHRYPFLLVDRVVELEEGKLIKGFKNISINEEVFNGHFPEVPIFPGVMIVEALAQVSGILGFKTLGQkpEDGYLYLFAG 90
Cdd:cd01288     1 LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLED--FEGKLVYFAG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1055298883  91 IDNVRFKRQVVPGDRLQLESQVVSERRGIWKFAGKASVDGELAASADILCAVK 143
Cdd:cd01288    79 IDKARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELMFAIA 131
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 4-144 3.34e-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: 205.04  E-value: 3.34e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055298883   4 VQEIRQYLPHRYPFLLVDRVVELEEGKLIKGFKNISINEEVFNGHFPEVPIFPGVMIVEALAQVSGILGFKTLGQKPEdG 83
Cdd:COG0764     1 IEEILALLPHRYPFLLVDRVLEIDPGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEGLEGK-G 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1055298883  84 YLYLFAGIDNVRFKRQVVPGDRLQLESQVVSERRGIWKFAGKASVDGELAASADILCAVKK 144
Cdd:COG0764    80 RLVYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFALVE 140
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 11-136 1.42e-34

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 116.99  E-value: 1.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055298883  11 LPHRYpFLLVDRVVELE-EGK-----LIKGFKNISINEEVFNGHFPEVPIFPGVMIVEALAQVSGILGFKTLGQKPEDGy 84
Cdd:pfam07977   1 LPHRY-FLMLDRVTEIDpDGGkfgkgYIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWSGGGEGRGR- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1055298883  85 lylFAGIDNVRFKRQVVPGD-RLQLE---SQVVSERRGIWKFAGKASVDGELAASA 136
Cdd:pfam07977  79 ---ARGVDEVKFRGQVTPGDkQLRYEveiKKIIEGRRGIGIADGRALVDGKVVYEA 131
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
1-145 5.91e-89

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 255.04  E-value: 5.91e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055298883   1 MMDVQEIRQYLPHRYPFLLVDRVVELEEGKLIKGFKNISINEEVFNGHFPEVPIFPGVMIVEALAQVSGILGFKTLgqkP 80
Cdd:PRK00006    6 MLDIEEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSE---E 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1055298883  81 EDGYLYLFAGIDNVRFKRQVVPGDRLQLESQVVSERRGIWKFAGKASVDGELAASADILCAVKKI 145
Cdd:PRK00006   83 NKGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRDK 147
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 3-142 5.00e-73

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: 214.87  E-value: 5.00e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055298883   3 DVQEIRQYLPHRYPFLLVDRVVELEEGKLIKGFKNISINEEVFNGHFPEVPIFPGVMIVEALAQVSGILGFKTLGQKPED 82
Cdd:TIGR01750   1 DIQDIMELLPHRYPFLLVDRILELEPGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILSLGGEKGK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055298883  83 GYLYLFAGIDNVRFKRQVVPGDRLQLESQVVSERRGIWKFAGKASVDGELAASADILCAV 142
Cdd:TIGR01750  81 GKLVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIMFAI 140
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 11-143 3.12e-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: 209.71  E-value: 3.12e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055298883  11 LPHRYPFLLVDRVVELEEGKLIKGFKNISINEEVFNGHFPEVPIFPGVMIVEALAQVSGILGFKTLGQkpEDGYLYLFAG 90
Cdd:cd01288     1 LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLED--FEGKLVYFAG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1055298883  91 IDNVRFKRQVVPGDRLQLESQVVSERRGIWKFAGKASVDGELAASADILCAVK 143
Cdd:cd01288    79 IDKARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELMFAIA 131
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 4-144 3.34e-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: 205.04  E-value: 3.34e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055298883   4 VQEIRQYLPHRYPFLLVDRVVELEEGKLIKGFKNISINEEVFNGHFPEVPIFPGVMIVEALAQVSGILGFKTLGQKPEdG 83
Cdd:COG0764     1 IEEILALLPHRYPFLLVDRVLEIDPGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEGLEGK-G 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1055298883  84 YLYLFAGIDNVRFKRQVVPGDRLQLESQVVSERRGIWKFAGKASVDGELAASADILCAVKK 144
Cdd:COG0764    80 RLVYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFALVE 140
FabA_FabZ cd00493
FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct ...
 12-142 2.20e-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: 174.78  E-value: 2.20e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055298883  12 PHRYPFLLVDRVVELEEGKLIKGFKNISINEEVFNGHFPEVPIFPGVMIVEALAQVSGILGFKTLGQKPEDGYLYLFAGI 91
Cdd:cd00493     1 PHRYPMLLVDRVLEIDPGGRIVAEKNVTPNEPFFQGHFPGDPVMPGVLGIEAMAQAAAALAGLLGLGKGNPPRLGYLAGV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1055298883  92 DNVRFKRQVVPGDRLQLESQVVSERRGIWKFAGKASVDGELAASADILCAV 142
Cdd:cd00493    81 RKVKFRGPVLPGDTLTLEVELLKVRRGLGKFDGRAYVDGKLVAEAELMAAA 131
PRK13188 PRK13188
bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R) ...
 2-144 8.26e-53

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: 172.81  E-value: 8.26e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055298883   2 MDVQEIRQYLPHRYPFLLVDRVVELEEGKLIkGFKNISINEEVFNGHFPEVPIFPGVMIVEALAQVSGILGFKTLGQkPE 81
Cdd:PRK13188  321 LDINRIMKILPHRYPFLLVDKIIELGDTKIV-GIKNVTMNEPFFQGHFPGNPVMPGVLQIEAMAQTGGILVLNTVPD-PE 398

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1055298883  82 DgYLYLFAGIDNVRFKRQVVPGDRLQLESQVVSE-RRGIWKFAGKASVDGELAASADILCAVKK 144
Cdd:PRK13188  399 N-YSTYFMKIDKVKFRQKVVPGDTLIFKVELLSPiRRGICQMQGKAYVNGKLVCEAELMAQIVK 461
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 11-136 1.42e-34

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 116.99  E-value: 1.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055298883  11 LPHRYpFLLVDRVVELE-EGK-----LIKGFKNISINEEVFNGHFPEVPIFPGVMIVEALAQVSGILGFKTLGQKPEDGy 84
Cdd:pfam07977   1 LPHRY-FLMLDRVTEIDpDGGkfgkgYIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWSGGGEGRGR- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1055298883  85 lylFAGIDNVRFKRQVVPGD-RLQLE---SQVVSERRGIWKFAGKASVDGELAASA 136
Cdd:pfam07977  79 ---ARGVDEVKFRGQVTPGDkQLRYEveiKKIIEGRRGIGIADGRALVDGKVVYEA 131
COG4706 COG4706
Predicted 3-hydroxylacyl-ACP dehydratase, HotDog domain [Lipid transport and metabolism];
1-136 9.73e-10

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


Pssm-ID: 443741  Cd Length: 149  Bit Score: 53.33  E-value: 9.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055298883   1 MMDVQEIRQYLPHRYPFLLVDRVVELEEGKLIKGFKnisINEE-VF--NGHFPEvpifpgVMIVEALAQ----VSGILGF 73
Cdd:COG4706     4 TLDRPPIAALIPHRGPMCLLDRVLAWDEESAVAEVT---IRPDnPFrdDGGLPA------WVGIEYMAQavaaHGGLLAR 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1055298883  74 KTlGQKPEDGYLylfAGIDNVRFKRQVVP-GDRLQLESQVVSERRGIWKFAGKASVDGELAASA 136
Cdd:COG4706    75 AA-GEPPRLGFL---LGVRKVELHVPRFPvGETLRIEAERLLQDEGLGLFECRIRAGGELLASG 134
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 53-141 2.08e-07

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: 46.31  E-value: 2.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055298883  53 PIFPGVMIVEALAQVSGILGFKTLGQkpedGYLYLFAGIDnVRFKRQVVPGDRLQLESQVVSERRGIWKFAGKASV-DGE 131
Cdd:cd03440    16 GIVHGGLLLALADEAAGAAAARLGGR----GLGAVTLSLD-VRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNeDGK 90

                          90
                  ....*....|
gi 1055298883 132 LAASADILCA 141
Cdd:cd03440    91 LVATATATFV 100
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
90-144 8.05e-06

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 42.57  E-value: 8.05e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055298883  90 GIDNVRFKRQVVPGDRLQLESQVV----SERRGIWKFAGKAS-VDGELAASADILCAVKK 144
Cdd:COG2030    79 GLQEVRFLRPVRVGDTLRARVEVLekreSKSRGIVTLRTTVTnQDGEVVLTGEATVLVPR 138
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 90-117 1.77e-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: 39.09  E-value: 1.77e-04
                          10        20
                  ....*....|....*....|....*...
gi 1055298883  90 GIDNVRFKRQVVPGDRLQLESQVVSERR 117
Cdd:cd03454    79 GIDELRWPRPVRPGDTLSVEVEVLDKRP 106
FabA cd01287
FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the ...
 16-106 7.32e-04

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: 37.62  E-value: 7.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1055298883  16 PFLLVDRVVELEEGK------LIKGFKNISINEEVFNGHFPEVPIFPGVMIVEALAQVSGI-LGFKTLGQKPEDGYLYLF 88
Cdd:cd01287     7 QLLMLDRVTEIDPGGgtfglgYLRAEKDIDPDDWFFPCHFHGDPVMPGSLGLEAMIQLLQFyLIWLGLGTGVDNPRFQGA 86

                          90
                  ....*....|....*....
gi 1055298883  89 AGID-NVRFKRQVVPGDRL 106
Cdd:cd01287    87 PGGPgEWKYRGQITPHNKK 105
 
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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