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Conserved domains on  [gi|55670136|pdb|1U1Z|F]
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Chain F, (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;
23-165 1.47e-89

3-hydroxyacyl-ACP dehydratase FabZ;


:

Pssm-ID: 234568  Cd Length: 147  Bit Score: 257.74  E-value: 1.47e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U1Z_F        23 DINEIREYLPHRYPFLLVDRVVELDiEGKRIRAYKNVSINEPFFNGHFPEHPI*PGVLIIEA*AQAAGILGFK*LdvkPA 102
Cdd:PRK00006   8 DIEEILKLLPHRYPFLLVDRVLELE-PGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSE---EN 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
1U1Z_F       103 DGTLYYFVGSDKLRFRQPVLPGDQLQLHAKFISVKRSIWKFDCHATVDDKPVCSAEIICAERK 165
Cdd:PRK00006  84 KGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRD 146
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
23-165 1.47e-89

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 257.74  E-value: 1.47e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U1Z_F        23 DINEIREYLPHRYPFLLVDRVVELDiEGKRIRAYKNVSINEPFFNGHFPEHPI*PGVLIIEA*AQAAGILGFK*LdvkPA 102
Cdd:PRK00006   8 DIEEILKLLPHRYPFLLVDRVLELE-PGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSE---EN 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
1U1Z_F       103 DGTLYYFVGSDKLRFRQPVLPGDQLQLHAKFISVKRSIWKFDCHATVDDKPVCSAEIICAERK 165
Cdd:PRK00006  84 KGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRD 146
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 23-163 3.78e-83

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: 241.45  E-value: 3.78e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U1Z_F         23 DINEIREYLPHRYPFLLVDRVVELDiEGKRIRAYKNVSINEPFFNGHFPEHPI*PGVLIIEA*AQAAGILGFK*LDVKPA 102
Cdd:TIGR01750   1 DIQDIMELLPHRYPFLLVDRILELE-PGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILSLGGEKG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
1U1Z_F        103 DGTLYYFVGSDKLRFRQPVLPGDQLQLHAKFISVKRSIWKFDCHATVDDKPVCSAEIICAE 163
Cdd:TIGR01750  80 KGKLVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIMFAI 140
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 31-162 1.13e-74

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: 219.34  E-value: 1.13e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U1Z_F       31 LPHRYPFLLVDRVVELDiEGKRIRAYKNVSINEPFFNGHFPEHPI*PGVLIIEA*AQAAGILGFK*LDvkPADGTLYYFV 110
Cdd:cd01288   1 LPHRYPFLLVDRVLELE-PGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLE--DFEGKLVYFA 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
1U1Z_F      111 GSDKLRFRQPVLPGDQLQLHAKFISVKRSIWKFDCHATVDDKPVCSAEIICA 162
Cdd:cd01288  78 GIDKARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELMFA 129
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 24-165 1.71e-72

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: 214.29  E-value: 1.71e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U1Z_F       24 INEIREYLPHRYPFLLVDRVVELDiEGKRIRAYKNVSINEPFFNGHFPEHPI*PGVLIIEA*AQAAGILGFK*LDvKPAD 103
Cdd:COG0764   1 IEEILALLPHRYPFLLVDRVLEID-PGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEG-LEGK 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
1U1Z_F      104 GTLYYFVGSDKLRFRQPVLPGDQLQLHAKFISVKRSIWKFDCHATVDDKPVCSAEIICAERK 165
Cdd:COG0764  79 GRLVYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFALVE 140
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 31-158 9.24e-38

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 125.85  E-value: 9.24e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U1Z_F         31 LPHRYpFLLVDRVVELDIEGKR-----IRAYKNVSINEPFFNGHFPEHPI*PGVLIIEA*AQAAGI-LGFK*LDVKPADG 104
Cdd:pfam07977   1 LPHRY-FLMLDRVTEIDPDGGKfgkgyIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFyAIWSGGGEGRGRA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
1U1Z_F        105 tlyyfVGSDKLRFRQPVLPGDQ---LQLHAKFISV-KRSIWKFDCHATVDDKPVCSAE 158
Cdd:pfam07977  80 -----RGVDEVKFRGQVTPGDKqlrYEVEIKKIIEgRRGIGIADGRALVDGKVVYEAK 132
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
23-165 1.47e-89

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 257.74  E-value: 1.47e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U1Z_F        23 DINEIREYLPHRYPFLLVDRVVELDiEGKRIRAYKNVSINEPFFNGHFPEHPI*PGVLIIEA*AQAAGILGFK*LdvkPA 102
Cdd:PRK00006   8 DIEEILKLLPHRYPFLLVDRVLELE-PGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSE---EN 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
1U1Z_F       103 DGTLYYFVGSDKLRFRQPVLPGDQLQLHAKFISVKRSIWKFDCHATVDDKPVCSAEIICAERK 165
Cdd:PRK00006  84 KGKLVYFAGIDKARFKRPVVPGDQLILEVELLKQRRGIWKFKGVATVDGKLVAEAELMFAIRD 146
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 23-163 3.78e-83

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: 241.45  E-value: 3.78e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U1Z_F         23 DINEIREYLPHRYPFLLVDRVVELDiEGKRIRAYKNVSINEPFFNGHFPEHPI*PGVLIIEA*AQAAGILGFK*LDVKPA 102
Cdd:TIGR01750   1 DIQDIMELLPHRYPFLLVDRILELE-PGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILSLGGEKG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
1U1Z_F        103 DGTLYYFVGSDKLRFRQPVLPGDQLQLHAKFISVKRSIWKFDCHATVDDKPVCSAEIICAE 163
Cdd:TIGR01750  80 KGKLVYFAGIDKARFRRPVVPGDQLILHVEFLKKRRGIGKFKGEATVDGKVVAEAEIMFAI 140
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 31-162 1.13e-74

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: 219.34  E-value: 1.13e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U1Z_F       31 LPHRYPFLLVDRVVELDiEGKRIRAYKNVSINEPFFNGHFPEHPI*PGVLIIEA*AQAAGILGFK*LDvkPADGTLYYFV 110
Cdd:cd01288   1 LPHRYPFLLVDRVLELE-PGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLE--DFEGKLVYFA 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
1U1Z_F      111 GSDKLRFRQPVLPGDQLQLHAKFISVKRSIWKFDCHATVDDKPVCSAEIICA 162
Cdd:cd01288  78 GIDKARFRKPVVPGDQLILEVELLKLRRGIGKFKGKAYVDGKLVAEAELMFA 129
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 24-165 1.71e-72

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: 214.29  E-value: 1.71e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U1Z_F       24 INEIREYLPHRYPFLLVDRVVELDiEGKRIRAYKNVSINEPFFNGHFPEHPI*PGVLIIEA*AQAAGILGFK*LDvKPAD 103
Cdd:COG0764   1 IEEILALLPHRYPFLLVDRVLEID-PGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEG-LEGK 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
1U1Z_F      104 GTLYYFVGSDKLRFRQPVLPGDQLQLHAKFISVKRSIWKFDCHATVDDKPVCSAEIICAERK 165
Cdd:COG0764  79 GRLVYFLGIDKVKFRGPVVPGDTLTLEVEIKRVRRGIGKADGKATVDGKLVAEAELTFALVE 140
FabA_FabZ cd00493
FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct ...
 32-162 5.24e-62

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: 187.49  E-value: 5.24e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U1Z_F       32 PHRYPFLLVDRVVELDiEGKRIRAYKNVSINEPFFNGHFPEHPI*PGVLIIEA*AQAAGILGFK*LDVKPADGTLYYFVG 111
Cdd:cd00493   1 PHRYPMLLVDRVLEID-PGGRIVAEKNVTPNEPFFQGHFPGDPVMPGVLGIEAMAQAAAALAGLLGLGKGNPPRLGYLAG 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
1U1Z_F      112 SDKLRFRQPVLPGDQLQLHAKFISVKRSIWKFDCHATVDDKPVCSAEIICA 162
Cdd:cd00493  80 VRKVKFRGPVLPGDTLTLEVELLKVRRGLGKFDGRAYVDGKLVAEAELMAA 130
PRK13188 PRK13188
bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R) ...
 23-158 3.02e-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: 3.02e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U1Z_F        23 DINEIREYLPHRYPFLLVDRVVELdiEGKRIRAYKNVSINEPFFNGHFPEHPI*PGVLIIEA*AQAAGILGFK*ldVKPA 102
Cdd:PRK13188 322 DINRIMKILPHRYPFLLVDKIIEL--GDTKIVGIKNVTMNEPFFQGHFPGNPVMPGVLQIEAMAQTGGILVLNT--VPDP 397

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
1U1Z_F       103 DGTLYYFVGSDKLRFRQPVLPGDQLQLHAKFIS-VKRSIWKFDCHATVDDKPVCSAE 158
Cdd:PRK13188 398 ENYSTYFMKIDKVKFRQKVVPGDTLIFKVELLSpIRRGICQMQGKAYVNGKLVCEAE 454
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 31-158 9.24e-38

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 125.85  E-value: 9.24e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U1Z_F         31 LPHRYpFLLVDRVVELDIEGKR-----IRAYKNVSINEPFFNGHFPEHPI*PGVLIIEA*AQAAGI-LGFK*LDVKPADG 104
Cdd:pfam07977   1 LPHRY-FLMLDRVTEIDPDGGKfgkgyIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFyAIWSGGGEGRGRA 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
1U1Z_F        105 tlyyfVGSDKLRFRQPVLPGDQ---LQLHAKFISV-KRSIWKFDCHATVDDKPVCSAE 158
Cdd:pfam07977  80 -----RGVDEVKFRGQVTPGDKqlrYEVEIKKIIEgRRGIGIADGRALVDGKVVYEAK 132
COG4706 COG4706
Predicted 3-hydroxylacyl-ACP dehydratase, HotDog domain [Lipid transport and metabolism];
23-159 2.86e-13

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


Pssm-ID: 443741  Cd Length: 149  Bit Score: 63.35  E-value: 2.86e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U1Z_F       23 DINEIREYLPHRYPFLLVDRVVELDieGKRIRAYKNVSINEPFF-NGHFPEhpi*pgVLIIEA*AQAAGILG---FK*LD 98
Cdd:COG4706   6 DRPPIAALIPHRGPMCLLDRVLAWD--EESAVAEVTIRPDNPFRdDGGLPA------WVGIEYMAQAVAAHGgllARAAG 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
1U1Z_F       99 VKPADGtlyYFVGSDKLRFRQPVLP-GDQLQLHAKFISVKRSIWKFDCHATVDDKPVCSAEI 159
Cdd:COG4706  78 EPPRLG---FLLGVRKVELHVPRFPvGETLRIEAERLLQDEGLGLFECRIRAGGELLASGRL 136
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 53-162 3.94e-10

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: 54.02  E-value: 3.94e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U1Z_F       53 IRAYKNVSINEPFFNGHFPehpi*pGVLIIEA*AQAAGILGFK*ldvkpADGTLYYFVGSDKLRFRQPVLPGDQLQLHAK 132
Cdd:cd03440   1 FVLRLTVTPEDIDGGGIVH------GGLLLALADEAAGAAAARL-----GGRGLGAVTLSLDVRFLRPVRPGDTLTVEAE 69

                        90       100       110
                ....*....|....*....|....*....|.
1U1Z_F      133 FISVKRSIWKFDCHATV-DDKPVCSAEIICA 162
Cdd:cd03440  70 VVRVGRSSVTVEVEVRNeDGKLVATATATFV 100
FabA cd01287
FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the ...
 36-154 3.50e-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: 47.25  E-value: 3.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U1Z_F       36 PFLLVDRVVELDIEGK-----RIRAYKNVSINEPFFNGHFPEHPI*PGVLIIEA*AQAAGI--------LGFK*LDVKPA 102
Cdd:cd01287   7 QLLMLDRVTEIDPGGGtfglgYLRAEKDIDPDDWFFPCHFHGDPVMPGSLGLEAMIQLLQFyliwlglgTGVDNPRFQGA 86

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
1U1Z_F      103 DGtlyyfvGSDKLRFRQPVLPGDQ---LQLHAKFISV--KRSIWKFDCHATVDDKPV 154
Cdd:cd01287  87 PG------GPGEWKYRGQITPHNKkvtYEVHIKEVGRdgPRPYIIADASLWVDGLRI 137
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
68-160 1.68e-06

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 45.26  E-value: 1.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U1Z_F       68 GHFPEhPI*PGVLIIea*AQAAGILgfk*ldVKPADGTLYYFVGSDKLRFRQPVLPGDQLQLHAKFISVK----RSIWKF 143
Cdd:COG2030  46 TGFGG-RIAHGMLTL---SLASGLL------VDDLPGTAVANLGLQEVRFLRPVRVGDTLRARVEVLEKResksRGIVTL 115

                        90
                ....*....|....*...
1U1Z_F      144 DCHAT-VDDKPVCSAEII 160
Cdd:COG2030 116 RTTVTnQDGEVVLTGEAT 133
FabA_like cd01289
Domain of unknown function, appears to be related to a diverse group of beta-hydroxydecanoyl ...
 27-157 2.16e-05

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: 41.87  E-value: 2.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U1Z_F       27 IREYLPHRYPFLLVDRVVELDIEGKRIRAykNVSINEPFFNghfPEHPI*PGVLIIEA*AQA----AGILGFK*LDvKPA 102
Cdd:cd01289   3 IAALIPHDGPMCLLDRVISWDDDSIHCRA--TVHPDPLFPL---RAHGRLPAWVGIEYMAQAiaahGGLLARQQGN-PPR 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
1U1Z_F      103 DGtlyYFVGSDKLRFRQPVLP-GDQLQLHAKFISVKRSI-WKFDCHATVDDKPVCSA 157
Cdd:cd01289  77 PG---FLLGSRKYEAHVDRFDlGSTLLIVVAELLQGDSGlGVFECTIEDQGGVLASG 130
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 110-159 9.40e-05

(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: 39.94  E-value: 9.40e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
1U1Z_F      110 VGSDKLRFRQPVLPGDQLQLHAKFISVKRS------IWKFDCHAtVDDKPVCSAEI 159
Cdd:cd03441  70 LGSQSVRFLAPVFPGDTLRVEVEVLGKRPSkgrgvvTVRTEARN-QGGEVVLSGEA 124
PRK05174 PRK05174
bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase;
36-94 5.87e-04

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


Pssm-ID: 179953  Cd Length: 172  Bit Score: 38.27  E-value: 5.87e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
1U1Z_F        36 PFLLVDRVVELDIEGK-----RIRAYKNVSINEPFFNGHFPEHPI*PGVLIIEA*AQaagILGF 94
Cdd:PRK05174  33 PMLMMDRITEISETGGefgkgYIVAELDINPDLWFFGCHFIGDPVMPGCLGLDAMWQ---LVGF 93
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 111-139 7.10e-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: 37.93  E-value: 7.10e-04
                        10        20
                ....*....|....*....|....*....
1U1Z_F      111 GSDKLRFRQPVLPGDQLQLHAKFISVKRS 139
Cdd:cd03454  79 GIDELRWPRPVRPGDTLSVEVEVLDKRPS 107
MaoC_C cd03452
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory ...
 68-160 1.35e-03

MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory protein. Orthologs of MaoC include PaaZ [Escherichia coli] and PaaN [Pseudomonas putida], which are putative ring-opening enzymes involved in phenylacetic acid degradation. The C-terminal domain of MaoC has sequence similarity to (R)-specific enoyl-CoA hydratase,Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. MaoC also has an N-terminal PutA domain like that found in the E. coli PutA proline dehydrogenase and other members of the aldehyde dehydrogenase family.


Pssm-ID: 239536 [Multi-domain]  Cd Length: 142  Bit Score: 36.99  E-value: 1.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U1Z_F       68 GHFPEHPI*PGVLIIEA*aqAAGILgfk*ldVKPADGTLYYFVGSDKLRFRQPVLPGDQLQLHakfISVKRSIWK----- 142
Cdd:cd03452  45 ASFFGKRVAHGYFVLSA---AAGLF------VDPAPGPVLANYGLENLRFLEPVYPGDTIQVR---LTCKRKIPRdgqdy 112

                        90       100
                ....*....|....*....|...
1U1Z_F      143 ----FDCHATVD-DKPVCSAEII 160
Cdd:cd03452 113 gvvrWDAEVTNQnGELVASYDIL 135
NodN cd03450
NodN (nodulation factor N) contains a single hot dog fold similar to those of the peroxisomal ...
 111-160 2.51e-03

NodN (nodulation factor N) contains a single hot dog fold similar to those of the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. Rhizobium and related species form nodules on the roots of their legume hosts, a symbiotic process that requires production of Nod factors, which are signal molecules involved in root hair deformation and meristematic cell division. The nodulation gene products, including NodN, are involved in producing the Nod factors, however the role played by NodN is unclear.


Pssm-ID: 239534 [Multi-domain]  Cd Length: 149  Bit Score: 36.39  E-value: 2.51e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
1U1Z_F      111 GSDKLRFRQPVLPGDQLQLHAKFISV---KRSIWKFDCHATVD----DKPVCSAEII 160
Cdd:cd03450  88 GLDKVRFPAPVPVGSRVRGRFTLLSVeelKGGGVQVTLEVTVEiegeDKPACVAEWI 144
 
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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