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Conserved domains on  [gi|795334921|ref|XP_011741551|]
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hydroxyacyl-thioester dehydratase type 2, mitochondrial [Macaca nemestrina]

Protein Classification

MaoC family dehydratase( domain architecture ID 10130975)

MaoC family dehydratase similar to Aeromonas caviae (R)-specific enoyl-CoA hydratase that is involved in polyhydroxyalkanoate biosynthesis, and Methylorubrum extorquens 3-hydroxybutyryl-CoA dehydratase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 36-162 1.37e-53

(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: 166.18  E-value: 1.37e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795334921  36 IKVGDRAELRRAFTQTDVATFSELTGDVNPLHLNEDFAKHTKFGNTIVHGVLINGLISALLGTKMPGPGCVFLSQEISFP 115
Cdd:cd03449    1 LKVGDSASLTRTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAVLGTLLPGPGTIYLSQSLRFL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 795334921 116 APLYIGEVVLASAEVKKL--KRFIAIIAVSCSViESKKTVMEGWVKVMV 162
Cdd:cd03449   81 RPVFIGDTVTATVTVTEKreDKKRVTLETVCTN-QNGEVVIEGEAVVLA 128
 
Name Accession Description Interval E-value
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 36-162 1.37e-53

(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: 166.18  E-value: 1.37e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795334921  36 IKVGDRAELRRAFTQTDVATFSELTGDVNPLHLNEDFAKHTKFGNTIVHGVLINGLISALLGTKMPGPGCVFLSQEISFP 115
Cdd:cd03449    1 LKVGDSASLTRTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAVLGTLLPGPGTIYLSQSLRFL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 795334921 116 APLYIGEVVLASAEVKKL--KRFIAIIAVSCSViESKKTVMEGWVKVMV 162
Cdd:cd03449   81 RPVFIGDTVTATVTVTEKreDKKRVTLETVCTN-QNGEVVIEGEAVVLA 128
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
36-166 3.64e-33

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 114.60  E-value: 3.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795334921  36 IKVGDRAELR-RAFTQTDVATFSELTGDVNPLHLNEDFAKHTKFGNTIVHGVLINGLISALLGTKMPGPGCVFL-SQEIS 113
Cdd:COG2030    5 LEVGDVLPHGgRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAVANLgLQEVR 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 795334921 114 FPAPLYIGEVVLASAEV--KKLKRFIAIIAVSCSVI-ESKKTVMEGWVKVMVPEAP 166
Cdd:COG2030   85 FLRPVRVGDTLRARVEVleKRESKSRGIVTLRTTVTnQDGEVVLTGEATVLVPRRP 140
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 36-163 7.49e-33

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 121.14  E-value: 7.49e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795334921  36 IKVGDRAELRRAFTQTDVATFSELTGDVNPLHLNEDFAKHTKFGNTIVHGVLINGLISALLGTKMPGPGCVFLSQEISFP 115
Cdd:PRK08190  14 IAIGDSASLVRTLTPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGGALISAVLGTRLPGPGTIYLGQSLRFR 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 795334921 116 APLYIGEVVLASAEV--KKLKRFIAIIAVSCsVIESKKTVMEGWVKVMVP 163
Cdd:PRK08190  94 RPVRIGDTLTVTVTVreKDPEKRIVVLDCRC-TNQDGEVVITGTAEVIAP 142
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 41-149 4.04e-16

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: 70.06  E-value: 4.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795334921   41 RAELRRAFTQTDVATFSELTGDVNPLHLNEDFAKHTKFGNTIVHGVLINGLISALLGTKMPGPG-CVFLSQEISFPAPLY 119
Cdd:pfam01575  11 DTEKPRTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDNViARFGEIKVRFTKPVF 90

                          90       100       110
                  ....*....|....*....|....*....|
gi 795334921  120 IGEVVLASAEVKKLKRFIAIIAVSCSVIES 149
Cdd:pfam01575  91 PGDTLRTEAEVVGKRDGRQTKVVEVTVEVT 120
 
Name Accession Description Interval E-value
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 36-162 1.37e-53

(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: 166.18  E-value: 1.37e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795334921  36 IKVGDRAELRRAFTQTDVATFSELTGDVNPLHLNEDFAKHTKFGNTIVHGVLINGLISALLGTKMPGPGCVFLSQEISFP 115
Cdd:cd03449    1 LKVGDSASLTRTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAVLGTLLPGPGTIYLSQSLRFL 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 795334921 116 APLYIGEVVLASAEVKKL--KRFIAIIAVSCSViESKKTVMEGWVKVMV 162
Cdd:cd03449   81 RPVFIGDTVTATVTVTEKreDKKRVTLETVCTN-QNGEVVIEGEAVVLA 128
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
36-166 3.64e-33

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 114.60  E-value: 3.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795334921  36 IKVGDRAELR-RAFTQTDVATFSELTGDVNPLHLNEDFAKHTKFGNTIVHGVLINGLISALLGTKMPGPGCVFL-SQEIS 113
Cdd:COG2030    5 LEVGDVLPHGgRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAVANLgLQEVR 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 795334921 114 FPAPLYIGEVVLASAEV--KKLKRFIAIIAVSCSVI-ESKKTVMEGWVKVMVPEAP 166
Cdd:COG2030   85 FLRPVRVGDTLRARVEVleKRESKSRGIVTLRTTVTnQDGEVVLTGEATVLVPRRP 140
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 36-163 7.49e-33

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 121.14  E-value: 7.49e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795334921  36 IKVGDRAELRRAFTQTDVATFSELTGDVNPLHLNEDFAKHTKFGNTIVHGVLINGLISALLGTKMPGPGCVFLSQEISFP 115
Cdd:PRK08190  14 IAIGDSASLVRTLTPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGGALISAVLGTRLPGPGTIYLGQSLRFR 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 795334921 116 APLYIGEVVLASAEV--KKLKRFIAIIAVSCsVIESKKTVMEGWVKVMVP 163
Cdd:PRK08190  94 RPVRIGDTLTVTVTVreKDPEKRIVVLDCRC-TNQDGEVVITGTAEVIAP 142
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 39-161 6.83e-31

(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: 108.12  E-value: 6.83e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795334921  39 GDRAELRRAFTQTDVATFSELTGDVNPLHLNEDFAKHTKFGNTIVHGVLINGLISALLGTKMPG-PGCVFLSQEISFPAP 117
Cdd:cd03441    1 GELDSSGRTVTEADIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGLLVQWLPGtDGANLGSQSVRFLAP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 795334921 118 LYIGEVVLASAEV--KKLKRFIAIIAVSCSVIE-SKKTVMEGWVKVM 161
Cdd:cd03441   81 VFPGDTLRVEVEVlgKRPSKGRGVVTVRTEARNqGGEVVLSGEATVL 127
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 35-136 1.26e-17

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: 74.65  E-value: 1.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795334921  35 HIKVGDRAELR-RAFTQTDVATFSELTGDVNPLHLNEDFAKHTKFGNTIVHGVLInglISALLGTKMPGPG---CV--FL 108
Cdd:cd03446    4 DFEIGQVFESVgRTVTEADVVMFAGLSGDWNPIHTDAEYAKKTRFGERIAHGLLT---LSIATGLLQRLGVferTVvaFY 80

                         90       100
                 ....*....|....*....|....*....
gi 795334921 109 S-QEISFPAPLYIGEVVLASAEVKKLKRF 136
Cdd:cd03446   81 GiDNLRFLNPVFIGDTIRAEAEVVEKEEK 109
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 41-149 4.04e-16

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: 70.06  E-value: 4.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795334921   41 RAELRRAFTQTDVATFSELTGDVNPLHLNEDFAKHTKFGNTIVHGVLINGLISALLGTKMPGPG-CVFLSQEISFPAPLY 119
Cdd:pfam01575  11 DTEKPRTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDNViARFGEIKVRFTKPVF 90

                          90       100       110
                  ....*....|....*....|....*....|
gi 795334921  120 IGEVVLASAEVKKLKRFIAIIAVSCSVIES 149
Cdd:pfam01575  91 PGDTLRTEAEVVGKRDGRQTKVVEVTVEVT 120
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 37-134 1.50e-10

FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved family of proteins found in prokaryotes and archaea but not in eukaryotes. FkbR2 has sequence similarity to (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. The function of FkbR2 is unknown.


Pssm-ID: 239535 [Multi-domain]  Cd Length: 146  Bit Score: 56.06  E-value: 1.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795334921  37 KVGDRAE--LRRAFTQTDVATFSELTGDVNPLHLNEDFAKHTKFGNTIVHGVLInglISALLGTKMPGpgcvfLSQ---- 110
Cdd:cd03451    8 TVGQVFEhaPGRTVTEADNVLFTLLTMNTAPLHFDAAYAAKTEFGRRLVNSLFT---LSLALGLSVND-----TSLtava 79

                         90       100
                 ....*....|....*....|....*....
gi 795334921 111 -----EISFPAPLYIGEVVLASAEVKKLK 134
Cdd:cd03451   80 nlgydEVRFPAPVFHGDTLYAESEVLSKR 108
MaoC_C cd03452
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory ...
 36-132 1.69e-09

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: 53.17  E-value: 1.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795334921  36 IKVGDRAEL-RRAFTQTDVATFSELTGDVNPLHLNEDFAKHTKFGNTIVHGVLInglISALLGTKM-PGPGCV---FLSQ 110
Cdd:cd03452    5 LRPGDSLLThRRTVTEADIVNFACLTGDHFYAHMDEIAAKASFFGKRVAHGYFV---LSAAAGLFVdPAPGPVlanYGLE 81

                         90       100
                 ....*....|....*....|..
gi 795334921 111 EISFPAPLYIGEVVLASAEVKK 132
Cdd:cd03452   82 NLRFLEPVYPGDTIQVRLTCKR 103
SAV4209_like cd03453
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot ...
 38-131 1.51e-08

SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot dog fold that is similar to those of (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.


Pssm-ID: 239537 [Multi-domain]  Cd Length: 127  Bit Score: 50.40  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795334921  38 VGDR-AELRRAFTQTDVATFSELTGDVNPLHLNEDFAKHTKFGNTIVHGVLINGLISALLGTKMPGPGCVfLSQEISFPA 116
Cdd:cd03453    1 VGDElPPLTPPVSRADLVRYAGASGDFNPIHYDEDFAKKVGLPGVIAHGMLTMGLLGRLVTDWVGDPGRV-VSFGVRFTK 79

                         90
                 ....*....|....*
gi 795334921 117 PLYIGEVVLASAEVK 131
Cdd:cd03453   80 PVPVPDTLTCTGIVV 94
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 78-161 2.18e-06

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: 44.00  E-value: 2.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795334921  78 FGNTIVHGVLINGLISALLGT-----KMPGPGCVFLSQEISFPAPLYIGEVVLASAEVKKLKRFIAIIAVSCSViESKKT 152
Cdd:cd03440   13 DGGGIVHGGLLLALADEAAGAaaarlGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRN-EDGKL 91


                 ....*....
gi 795334921 153 VMEGWVKVM 161
Cdd:cd03440   92 VATATATFV 100
PRK13693 PRK13693
(3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional
 36-133 2.85e-06

(3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional


Pssm-ID: 184249 [Multi-domain]  Cd Length: 142  Bit Score: 44.44  E-value: 2.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795334921  36 IKVGDR-AELRRAFTQTDVATFSELTGDVNPLHLNEDFAKHTKFGNTIVHGVLINGLISALLGTKMPGPGCVfLSQEISF 114
Cdd:PRK13693   9 VKVGDQlPEKTYPLTRQDLVNYAGVSGDLNPIHWDDEIAKVVGLDTAIAHGMLTMGLGGGYVTSWVGDPGAV-TEYNVRF 87

                         90       100
                 ....*....|....*....|....
gi 795334921 115 PAPLYI-----GEVVLASAEVKKL 133
Cdd:PRK13693  88 TAVVPVpndgkGAELVFNGRVKSV 111
NodN cd03450
NodN (nodulation factor N) contains a single hot dog fold similar to those of the peroxisomal ...
 49-134 7.30e-06

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: 43.32  E-value: 7.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795334921  49 TQTDVATFSELTGDVNPLHLNEDFAKHTKFGNTIVHGVLINGLISALLGTKMPGPGCV----FLSQEISFPAPLYIGEVV 124
Cdd:cd03450   25 DQERIDQFADATGDHQWIHVDPERAAAEPFGGTIAHGFLTLSLLPALTPQLFRVEGVKmgvnYGLDKVRFPAPVPVGSRV 104

                         90
                 ....*....|
gi 795334921 125 LASAEVKKLK 134
Cdd:cd03450  105 RGRFTLLSVE 114
HDE_HSD cd03448
HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), ...
 49-156 8.42e-06

HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), and Hydratase-Dehydrogenase-Epimerase (HDE) proteins. Other enzymes with this fold include MaoC dehydratase, and the fatty acid synthase beta subunit.


Pssm-ID: 239532 [Multi-domain]  Cd Length: 122  Bit Score: 42.98  E-value: 8.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795334921  49 TQTDVATFSELTGDVNPLHLNEDFAKHTKFGNTIVHGVLINGLIS-ALLgtKMPGPGCVFLSQEIS--FPAPLYIGEVVL 125
Cdd:cd03448   13 TSPDQALLYRLSGDYNPLHIDPAFAKAAGFPRPILHGLCTYGFAArAVL--EAFADGDPARFKAIKvrFSSPVFPGETLR 90

                         90       100       110
                 ....*....|....*....|....*....|.
gi 795334921 126 AsaevkKLKRFIAIIAVSCSVIESKKTVMEG 156
Cdd:cd03448   91 T-----EMWKEGNRVIFQTKVVERDVVVLSN 116
SAV4209 cd03455
SAV4209 is a Streptomyces avermitilis protein with a hot dog fold that is similar to those of ...
 49-130 2.84e-05

SAV4209 is a Streptomyces avermitilis protein with a hot dog fold that is similar to those of (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. The alpha- and gamma-proteobacterial members of this CD have, in addition to a hot dog fold, an N-terminal extension.


Pssm-ID: 239539 [Multi-domain]  Cd Length: 123  Bit Score: 41.53  E-value: 2.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795334921  49 TQTDVATFSELTGDVNPLHLNEDFAKHTKFGNTIVHGVLINGLISALLGTKMpGPGCVFLSQEISFPAPLYIGEVVLASA 128
Cdd:cd03455   12 DPTLLFRYSAATRDFHRIHHDRDYARAVGYPDLYVNGPTLAGLVIRYVTDWA-GPDARVKSFAFRLGAPLYAGDTLRFGG 90


                 ..
gi 795334921 129 EV 130
Cdd:cd03455   91 RV 92
FAS_MaoC cd03447
FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes ...
 55-98 3.34e-03

FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes with this fold include MaoC dehydratase, Hydratase-Dehydrogenase-Epimerase protein (HDE), and 17-beta-hydroxysteriod dehydrogenase (HSD).


Pssm-ID: 239531 [Multi-domain]  Cd Length: 126  Bit Score: 35.72  E-value: 3.34e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 795334921  55 TFSELTGDVNPLHLNEDFAKHTKFGNTIVHGVLINGLISALLGT 98
Cdd:cd03447   17 PYARVSGDFNPIHVSRVFASYAGLPGTITHGMYTSAAVRALVET 60
PLN02864 PLN02864
enoyl-CoA hydratase
 49-86 5.83e-03

enoyl-CoA hydratase


Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 36.30  E-value: 5.83e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 795334921  49 TQTDVATFSELTGDVNPLHLNEDFAKHTKFGNTIVHGV 86
Cdd:PLN02864 196 TQPSQALLYRLSGDYNPLHSDPMFAKVAGFTRPILHGL 233
 
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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