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Conserved domains on  [gi|302837524|ref|XP_002950321|]
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uncharacterized protein VOLCADRAFT_74622 [Volvox carteri f. nagariensis]

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;
1-141 1.76e-70

3-hydroxyacyl-ACP dehydratase FabZ;


:

Pssm-ID: 234568  Cd Length: 147  Bit Score: 208.43  E-value: 1.76e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302837524   1 MQIMQILPHRYPFLLVDRVVEWEKEKYAVGYKCITINDNFFPGHFPERAIMPGVLQVEAMAQLAGIVMLDPEDTEAKgLF 80
Cdd:PRK00006  10 EEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSEENKGK-LV 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 302837524  81 FFAGIENCRFRKPVVPGDVLMMRAEVTKynKRFGMVKVAATGHVGEDLVVEAELTLAMGKK 141
Cdd:PRK00006  89 YFAGIDKARFKRPVVPGDQLILEVELLK--QRRGIWKFKGVATVDGKLVAEAELMFAIRDK 147
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
1-141 1.76e-70

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 208.43  E-value: 1.76e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302837524   1 MQIMQILPHRYPFLLVDRVVEWEKEKYAVGYKCITINDNFFPGHFPERAIMPGVLQVEAMAQLAGIVMLDPEDTEAKgLF 80
Cdd:PRK00006  10 EEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSEENKGK-LV 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 302837524  81 FFAGIENCRFRKPVVPGDVLMMRAEVTKynKRFGMVKVAATGHVGEDLVVEAELTLAMGKK 141
Cdd:PRK00006  89 YFAGIDKARFKRPVVPGDQLILEVELLK--QRRGIWKFKGVATVDGKLVAEAELMFAIRDK 147
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 7-139 3.19e-63

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: 189.29  E-value: 3.19e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302837524   7 LPHRYPFLLVDRVVEWEKEKYAVGYKCITINDNFFPGHFPERAIMPGVLQVEAMAQLAGIVMLDPEDTEAKGLFFFAGIE 86
Cdd:cd01288    1 LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLEDFEGKLVYFAGID 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 302837524  87 NCRFRKPVVPGDVLMMRAEVTKynKRFGMVKVAATGHVGEDLVVEAELTLAMG 139
Cdd:cd01288   81 KARFRKPVVPGDQLILEVELLK--LRRGIGKFKGKAYVDGKLVAEAELMFAIA 131
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 1-141 1.31e-62

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: 188.10  E-value: 1.31e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302837524   1 MQIMQILPHRYPFLLVDRVVEWEKEKYAVGYKCITINDNFFPGHFPERAIMPGVLQVEAMAQLAGIVMLDPEDTEAKG-L 79
Cdd:COG0764    2 EEILALLPHRYPFLLVDRVLEIDPGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEGLEGKGrL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 302837524  80 FFFAGIENCRFRKPVVPGDVLMMRAEVTKynKRFGMVKVAATGHVGEDLVVEAELTLAMGKK 141
Cdd:COG0764   82 VYFLGIDKVKFRGPVVPGDTLTLEVEIKR--VRRGIGKADGKATVDGKLVAEAELTFALVEK 141
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 1-138 4.59e-54

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: 166.72  E-value: 4.59e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302837524    1 MQIMQILPHRYPFLLVDRVVEWEKEKYAVGYKCITINDNFFPGHFPERAIMPGVLQVEAMAQLAGIVMLDPEDTEAKG-- 78
Cdd:TIGR01750   3 QDIMELLPHRYPFLLVDRILELEPGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILSLGGEKGKgk 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 302837524   79 LFFFAGIENCRFRKPVVPGDVLMMRAEVTKynKRFGMVKVAATGHVGEDLVVEAELTLAM 138
Cdd:TIGR01750  83 LVYFAGIDKARFRRPVVPGDQLILHVEFLK--KRRGIGKFKGEATVDGKVVAEAEIMFAI 140
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 7-133 1.40e-29

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 104.28  E-value: 1.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302837524    7 LPHRYpFLLVDRVVEWEKE------KYAVGYKCITINDNFFPGHFPERAIMPGVLQVEAMAQLAGIVMLDPEDTEAKGLf 80
Cdd:pfam07977   1 LPHRY-FLMLDRVTEIDPDggkfgkGYIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWSGGGEGRGR- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 302837524   81 fFAGIENCRFRKPVVPGD-VLMMRAEVTKY-NKRFGMVKVAATGHVGEDLVVEAE 133
Cdd:pfam07977  79 -ARGVDEVKFRGQVTPGDkQLRYEVEIKKIiEGRRGIGIADGRALVDGKVVYEAK 132
 
Name Accession Description Interval E-value
fabZ PRK00006
3-hydroxyacyl-ACP dehydratase FabZ;
1-141 1.76e-70

3-hydroxyacyl-ACP dehydratase FabZ;


Pssm-ID: 234568  Cd Length: 147  Bit Score: 208.43  E-value: 1.76e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302837524   1 MQIMQILPHRYPFLLVDRVVEWEKEKYAVGYKCITINDNFFPGHFPERAIMPGVLQVEAMAQLAGIVMLDPEDTEAKgLF 80
Cdd:PRK00006  10 EEILKLLPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGYPVMPGVLIIEAMAQAAGVLALKSEENKGK-LV 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 302837524  81 FFAGIENCRFRKPVVPGDVLMMRAEVTKynKRFGMVKVAATGHVGEDLVVEAELTLAMGKK 141
Cdd:PRK00006  89 YFAGIDKARFKRPVVPGDQLILEVELLK--QRRGIWKFKGVATVDGKLVAEAELMFAIRDK 147
FabZ cd01288
FabZ is a 17kD beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase that primarily ...
 7-139 3.19e-63

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: 189.29  E-value: 3.19e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302837524   7 LPHRYPFLLVDRVVEWEKEKYAVGYKCITINDNFFPGHFPERAIMPGVLQVEAMAQLAGIVMLDPEDTEAKGLFFFAGIE 86
Cdd:cd01288    1 LPHRYPFLLVDRVLELEPGKSIVAIKNVTINEPFFQGHFPGNPIMPGVLIIEALAQAAGILGLKSLEDFEGKLVYFAGID 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 302837524  87 NCRFRKPVVPGDVLMMRAEVTKynKRFGMVKVAATGHVGEDLVVEAELTLAMG 139
Cdd:cd01288   81 KARFRKPVVPGDQLILEVELLK--LRRGIGKFKGKAYVDGKLVAEAELMFAIA 131
FabA COG0764
3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl carrier protein) dehydratase [Lipid transport and ...
 1-141 1.31e-62

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: 188.10  E-value: 1.31e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302837524   1 MQIMQILPHRYPFLLVDRVVEWEKEKYAVGYKCITINDNFFPGHFPERAIMPGVLQVEAMAQLAGIVMLDPEDTEAKG-L 79
Cdd:COG0764    2 EEILALLPHRYPFLLVDRVLEIDPGKSIVAEKNVTPNEPFFQGHFPGDPVMPGVLILEAMAQLGGFLLLKSEGLEGKGrL 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 302837524  80 FFFAGIENCRFRKPVVPGDVLMMRAEVTKynKRFGMVKVAATGHVGEDLVVEAELTLAMGKK 141
Cdd:COG0764   82 VYFLGIDKVKFRGPVVPGDTLTLEVEIKR--VRRGIGKADGKATVDGKLVAEAELTFALVEK 141
PRK13188 PRK13188
bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R) ...
 2-141 1.93e-56

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: 182.44  E-value: 1.93e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302837524   2 QIMQILPHRYPFLLVDRVVEWeKEKYAVGYKCITINDNFFPGHFPERAIMPGVLQVEAMAQLAGIVMLDPEDTEAKGLFF 81
Cdd:PRK13188 325 RIMKILPHRYPFLLVDKIIEL-GDTKIVGIKNVTMNEPFFQGHFPGNPVMPGVLQIEAMAQTGGILVLNTVPDPENYSTY 403

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 302837524  82 FAGIENCRFRKPVVPGDVLMMRAEVTKyNKRFGMVKVAATGHVGEDLVVEAELTLAMGKK 141
Cdd:PRK13188 404 FMKIDKVKFRQKVVPGDTLIFKVELLS-PIRRGICQMQGKAYVNGKLVCEAELMAQIVKK 462
fabZ TIGR01750
beta-hydroxyacyl-[acyl carrier protein] dehydratase FabZ; This enzyme, FabZ, shows overlapping ...
 1-138 4.59e-54

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: 166.72  E-value: 4.59e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302837524    1 MQIMQILPHRYPFLLVDRVVEWEKEKYAVGYKCITINDNFFPGHFPERAIMPGVLQVEAMAQLAGIVMLDPEDTEAKG-- 78
Cdd:TIGR01750   3 QDIMELLPHRYPFLLVDRILELEPGKRIVAIKNVTINEPFFQGHFPEKPIMPGVLIIEAMAQAAGVLAILSLGGEKGKgk 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 302837524   79 LFFFAGIENCRFRKPVVPGDVLMMRAEVTKynKRFGMVKVAATGHVGEDLVVEAELTLAM 138
Cdd:TIGR01750  83 LVYFAGIDKARFRRPVVPGDQLILHVEFLK--KRRGIGKFKGEATVDGKVVAEAEIMFAI 140
FabA_FabZ cd00493
FabA/Z, beta-hydroxyacyl-acyl carrier protein (ACP)-dehydratases: One of several distinct ...
 8-138 1.22e-49

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: 155.14  E-value: 1.22e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302837524   8 PHRYPFLLVDRVVEWEKEKYAVGYKCITINDNFFPGHFPERAIMPGVLQVEAMAQLAGIVM--LDPEDTEAKGLFFFAGI 85
Cdd:cd00493    1 PHRYPMLLVDRVLEIDPGGRIVAEKNVTPNEPFFQGHFPGDPVMPGVLGIEAMAQAAAALAglLGLGKGNPPRLGYLAGV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 302837524  86 ENCRFRKPVVPGDVLMMRAEVTKynKRFGMVKVAATGHVGEDLVVEAELTLAM 138
Cdd:cd00493   81 RKVKFRGPVLPGDTLTLEVELLK--VRRGLGKFDGRAYVDGKLVAEAELMAAA 131
FabA pfam07977
FabA-like domain; This enzyme domain has a HotDog fold.
 7-133 1.40e-29

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


Pssm-ID: 429766  Cd Length: 132  Bit Score: 104.28  E-value: 1.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302837524    7 LPHRYpFLLVDRVVEWEKE------KYAVGYKCITINDNFFPGHFPERAIMPGVLQVEAMAQLAGIVMLDPEDTEAKGLf 80
Cdd:pfam07977   1 LPHRY-FLMLDRVTEIDPDggkfgkGYIVAEKDITPNEWFFQGHFPGDPVMPGVLGLEAMAQLMGFYAIWSGGGEGRGR- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 302837524   81 fFAGIENCRFRKPVVPGD-VLMMRAEVTKY-NKRFGMVKVAATGHVGEDLVVEAE 133
Cdd:pfam07977  79 -ARGVDEVKFRGQVTPGDkQLRYEVEIKKIiEGRRGIGIADGRALVDGKVVYEAK 132
FabA cd01287
FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the ...
 12-109 6.53e-08

FabA, beta-hydroxydecanoyl-acyl carrier protein (ACP)-dehydratase: Bacterial protein of the type II, fatty acid synthase system that binds ACP and catalyzes both dehydration and isomerization reactions, apparently in the same active site. The FabA structure is a homodimer with two independent active sites located at the dimer interface. Each active site is tunnel-shaped and completely inaccessible to solvent. No metal ions or cofactors are required for ligand binding or catalysis.


Pssm-ID: 238614  Cd Length: 150  Bit Score: 48.41  E-value: 6.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302837524  12 PFLLVDRVVEWEKE--KYAVGY----KCITINDNFFPGHFPERAIMPGVLQVEAMAQLAGIVMLDPEDTEAKGLFFFAGI 85
Cdd:cd01287    7 QLLMLDRVTEIDPGggTFGLGYlraeKDIDPDDWFFPCHFHGDPVMPGSLGLEAMIQLLQFYLIWLGLGTGVDNPRFQGA 86

                         90       100
                 ....*....|....*....|....*....
gi 302837524  86 EN----CRFRKPVVPGD-VLMMRAEVTKY 109
Cdd:cd01287   87 PGgpgeWKYRGQITPHNkKVTYEVHIKEV 115
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 50-137 1.13e-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: 46.70  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302837524  50 IMPGVLQVEAMAQLAGIVMLDPEDteaKGLFFFAGIENCRFRKPVVPGDVLMMRAEVTKYNKRFGMVKVAATGHVGEdLV 129
Cdd:cd03440   17 IVHGGLLLALADEAAGAAAARLGG---RGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNEDGK-LV 92


                 ....*...
gi 302837524 130 VEAELTLA 137
Cdd:cd03440   93 ATATATFV 100
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
39-141 1.50e-06

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 44.49  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302837524  39 NFFPGHF-PERA--------IMPGVLqveAMAQLAGIVMLDPEDTEAKGLfffaGIENCRFRKPVVPGDVLMMRAEVTKY 109
Cdd:COG2030   32 DPNPIHLdEEAAaatgfggrIAHGML---TLSLASGLLVDDLPGTAVANL----GLQEVRFLRPVRVGDTLRARVEVLEK 104

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 302837524 110 --NKRFGMVKVAATGHVGED-LVVEAELTLAMGKK 141
Cdd:COG2030  105 reSKSRGIVTLRTTVTNQDGeVVLTGEATVLVPRR 139
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 39-138 9.16e-06

(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: 42.25  E-value: 9.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302837524  39 NFFPGHF-PERA--------IMPGVLqveamaqLAGIVMLDPEDTEAKGLFFFAGIENCRFRKPVVPGDVLMMRAEVT-- 107
Cdd:cd03441   24 DPNPIHVdPEYAkaagfggrIAHGML-------TLSLASGLLVQWLPGTDGANLGSQSVRFLAPVFPGDTLRVEVEVLgk 96

                         90       100       110
                 ....*....|....*....|....*....|.
gi 302837524 108 KYNKRFGMVKVAATGHVGEDLVVEAELTLAM 138
Cdd:cd03441   97 RPSKGRGVVTVRTEARNQGGEVVLSGEATVL 127
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 84-130 1.05e-05

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: 42.17  E-value: 1.05e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 302837524  84 GIENCRFRKPVVPGDVLMMRAEVTkyNKRF-------GMVKVAATGHVGEDLVV 130
Cdd:cd03454   79 GIDELRWPRPVRPGDTLSVEVEVL--DKRPsrsrpdrGIVTLRSETLNQRGEVV 130
PRK05174 PRK05174
bifunctional 3-hydroxydecanoyl-ACP dehydratase/trans-2-decenoyl-ACP isomerase;
12-65 2.85e-05

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


Pssm-ID: 179953  Cd Length: 172  Bit Score: 41.74  E-value: 2.85e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 302837524  12 PFLLVDRVVEWEKE--KYAVGYKC----ITINDNFFPGHFPERAIMPGVLQVEAMAQLAG 65
Cdd:PRK05174  33 PMLMMDRITEISETggEFGKGYIVaeldINPDLWFFGCHFIGDPVMPGCLGLDAMWQLVG 92
COG4706 COG4706
Predicted 3-hydroxylacyl-ACP dehydratase, HotDog domain [Lipid transport and metabolism];
3-136 3.99e-05

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


Pssm-ID: 443741  Cd Length: 149  Bit Score: 41.01  E-value: 3.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302837524   3 IMQILPHRYPFLLVDRVVEWEkEKYAVGYKCITINDNFFPGHFperaiMPGVLQVEAMAQLAGIV--MLDPEDTEAKGLF 80
Cdd:COG4706   10 IAALIPHRGPMCLLDRVLAWD-EESAVAEVTIRPDNPFRDDGG-----LPAWVGIEYMAQAVAAHggLLARAAGEPPRLG 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 302837524  81 FFAGIENCRFRKPVVP-GDVLMMRAE-VTKYNkrfGMVKVAATGHVGEDLVVEAELTL 136
Cdd:COG4706   84 FLLGVRKVELHVPRFPvGETLRIEAErLLQDE---GLGLFECRIRAGGELLASGRLNV 138
FabA_like cd01289
Domain of unknown function, appears to be related to a diverse group of beta-hydroxydecanoyl ...
 2-62 1.40e-04

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: 39.17  E-value: 1.40e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 302837524   2 QIMQILPHRYPFLLVDRVVEWEKEKYAVgykCITINDNffpGHFPERAI--MPGVLQVEAMAQ 62
Cdd:cd01289    2 WIAALIPHDGPMCLLDRVISWDDDSIHC---RATVHPD---PLFPLRAHgrLPAWVGIEYMAQ 58
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 61-138 5.48e-04

4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate degradation pathway in which 4-chlorobenzoate is converted to 4-hydroxybenzoate in certain soil-dwelling bacteria. 4HBT forms a homotetramer with four active sites. There is no evidence to suggest that 4HBT is related to the type I thioesterases functioning in primary or secondary metabolic pathways. Each subunit of the 4HBT tetramer adopts a so-called hot-dog fold similar to those of beta-hydroxydecanoyl-ACP dehydratase, (R)-specific enoyl-CoA hydratase, and type II, thioesterase (TEII).


Pssm-ID: 238329 [Multi-domain]  Cd Length: 110  Bit Score: 37.20  E-value: 5.48e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 302837524  61 AQLAGIVMLDPEDTEAKGLFFFAGIEnCRFRKPVVPGDVLMMRAEVTKYNKRFGMVKVAATGHVGEdLVVEAELTLAM 138
Cdd:cd00586   33 EFLRELGLGYDELEEQGLGLVVVELE-IDYLRPLRLGDRLTVETRVLRLGRKSFTFEQEIFREDGE-LLATAETVLVC 108
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 39-138 1.02e-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: 36.90  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302837524  39 NFFPGH----------FPERaIMPGVLqveAMAQLAGIVMLDPedTEAKGLFFFAGIENCRFRKPVVPGDVLMMRAEVT- 107
Cdd:cd03446   32 DWNPIHtdaeyakktrFGER-IAHGLL---TLSIATGLLQRLG--VFERTVVAFYGIDNLRFLNPVFIGDTIRAEAEVVe 105

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 302837524 108 ---KYNKRFGMVKVAATG-HVGEDLVVEAELTLAM 138
Cdd:cd03446  106 keeKDGEDAGVVTRRIEVvNQRGEVVQSGEMSLLV 140
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 87-134 1.87e-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. (R)-hydratase contains a hot-dog fold similar to those of thioesterase II, and beta-hydroxydecanoyl-ACP dehydratase, MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and the fatty acid synthase beta subunit. The active site lies within a substrate-binding tunnel formed by the (R)-hydratase homodimer. A subset of the bacterial (R)-hydratases contain a C-terminal phosphotransacetylase (PTA) domain.


Pssm-ID: 239533 [Multi-domain]  Cd Length: 128  Bit Score: 35.98  E-value: 1.87e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 302837524  87 NCRFRKPVVPGDVLMMRAEVTKYNKRFGMVKVAATGHVGEDLVV---EAEL 134
Cdd:cd03449   76 SLRFLRPVFIGDTVTATVTVTEKREDKKRVTLETVCTNQNGEVViegEAVV 126
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 82-121 2.14e-03

MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the synthesis of monoamine oxidase. The MaoC protein is found to share similarity with a wide variety of enzymes; estradiol 17 beta-dehydrogenase 4, peroxisomal hydratase-dehydrogenase-epimerase, fatty acid synthase beta subunit. Several bacterial proteins that are composed solely of this domain have (R)-specific enoyl-CoA hydratase activity. This domain is also present in the NodN nodulation protein N.


Pssm-ID: 396243 [Multi-domain]  Cd Length: 123  Bit Score: 35.78  E-value: 2.14e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 302837524   82 FAGIENCRFRKPVVPGDVLMMRAEVTKYNKRFGMVKVAAT 121
Cdd:pfam01575  77 RFGEIKVRFTKPVFPGDTLRTEAEVVGKRDGRQTKVVEVT 116
 
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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