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Conserved domains on  [gi|24647430|ref|NP_732137|]
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uncharacterized protein Dmel_CG14881, isoform A [Drosophila melanogaster]

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 ...
 171-283 1.03e-36

(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: 127.28  E-value: 1.03e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647430 171 QVQVVKRFSQSDLEQFAQFTGDHNYIHSLE-----TPTEERRVHGALLNAVVAGIMGTQLPGPGTVVLEQNFKFLKPCRI 245
Cdd:cd03449   6 SASLTRTITEEDVELFAELSGDFNPIHLDEeyakkTRFGGRIAHGMLTASLISAVLGTLLPGPGTIYLSQSLRFLRPVFI 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 24647430 246 ETDTVVTVRLLQSR---KISTVEYDIR-QNDEVVFAGSAKLL 283
Cdd:cd03449  86 GDTVTATVTVTEKRedkKRVTLETVCTnQNGEVVIEGEAVVL 127
 
Name Accession Description Interval E-value
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 171-283 1.03e-36

(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: 127.28  E-value: 1.03e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647430 171 QVQVVKRFSQSDLEQFAQFTGDHNYIHSLE-----TPTEERRVHGALLNAVVAGIMGTQLPGPGTVVLEQNFKFLKPCRI 245
Cdd:cd03449   6 SASLTRTITEEDVELFAELSGDFNPIHLDEeyakkTRFGGRIAHGMLTASLISAVLGTLLPGPGTIYLSQSLRFLRPVFI 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 24647430 246 ETDTVVTVRLLQSR---KISTVEYDIR-QNDEVVFAGSAKLL 283
Cdd:cd03449  86 GDTVTATVTVTEKRedkKRVTLETVCTnQNGEVVIEGEAVVL 127
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
176-283 3.16e-14

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 68.37  E-value: 3.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647430 176 KRFSQSDLEQFAQFTGDHNYIH-----SLETPTEERRVHGALLNAVVAGIMGTQLPGPGTV-VLEQNFKFLKPCRIETD- 248
Cdd:COG2030  16 RTVTEEDIVLFAGATGDPNPIHldeeaAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAVAnLGLQEVRFLRPVRVGDTl 95

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 24647430 249 ----TVVTVRLLQSRKISTVEYDIR-QNDEVVFAGSAKLL 283
Cdd:COG2030  96 rarvEVLEKRESKSRGIVTLRTTVTnQDGEVVLTGEATVL 135
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 174-283 6.68e-14

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 71.45  E-value: 6.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647430  174 VVKRFSQSDLEQFAQFTGDHNYIHSLETPTEERR-----VHGALLNAVVAGIMGTQLPGPGTVVLEQNFKFLKPCRI-ET 247
Cdd:PRK08190  22 LVRTLTPDDIELFAAMSGDVNPAHLDAAYAASDGfhhvvAHGMWGGALISAVLGTRLPGPGTIYLGQSLRFRRPVRIgDT 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 24647430  248 DTV-VTVRLLQSRKiSTVEYDIR---QNDEVVFAGSAKLL 283
Cdd:PRK08190 102 LTVtVTVREKDPEK-RIVVLDCRctnQDGEVVITGTAEVI 140
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 179-252 5.50e-06

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: 44.64  E-value: 5.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647430   179 SQSDLEQFAQFTGDHNYIH-----SLETPTEERRVHGALLNAVVAGIMGTQLPGPG-TVVLEQNFKFLKPCRIeTDTVVT 252
Cdd:pfam01575  19 TEADIALFALVSGDHNPIHvdpefAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDNViARFGEIKVRFTKPVFP-GDTLRT 97
 
Name Accession Description Interval E-value
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 171-283 1.03e-36

(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: 127.28  E-value: 1.03e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647430 171 QVQVVKRFSQSDLEQFAQFTGDHNYIHSLE-----TPTEERRVHGALLNAVVAGIMGTQLPGPGTVVLEQNFKFLKPCRI 245
Cdd:cd03449   6 SASLTRTITEEDVELFAELSGDFNPIHLDEeyakkTRFGGRIAHGMLTASLISAVLGTLLPGPGTIYLSQSLRFLRPVFI 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 24647430 246 ETDTVVTVRLLQSR---KISTVEYDIR-QNDEVVFAGSAKLL 283
Cdd:cd03449  86 GDTVTATVTVTEKRedkKRVTLETVCTnQNGEVVIEGEAVVL 127
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 174-283 1.76e-14

(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: 68.44  E-value: 1.76e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647430 174 VVKRFSQSDLEQFAQFTGDHNYIH-----SLETPTEERRVHGALLNAVVAGIMGTQLPG-PGTVVLEQNFKFLKPCRIET 247
Cdd:cd03441   6 SGRTVTEADIALFARLSGDPNPIHvdpeyAKAAGFGGRIAHGMLTLSLASGLLVQWLPGtDGANLGSQSVRFLAPVFPGD 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 24647430 248 D-----TVVTVRLLQSRKISTVEYDIR-QNDEVVFAGSAKLL 283
Cdd:cd03441  86 TlrvevEVLGKRPSKGRGVVTVRTEARnQGGEVVLSGEATVL 127
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
176-283 3.16e-14

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 68.37  E-value: 3.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647430 176 KRFSQSDLEQFAQFTGDHNYIH-----SLETPTEERRVHGALLNAVVAGIMGTQLPGPGTV-VLEQNFKFLKPCRIETD- 248
Cdd:COG2030  16 RTVTEEDIVLFAGATGDPNPIHldeeaAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAVAnLGLQEVRFLRPVRVGDTl 95

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 24647430 249 ----TVVTVRLLQSRKISTVEYDIR-QNDEVVFAGSAKLL 283
Cdd:COG2030  96 rarvEVLEKRESKSRGIVTLRTTVTnQDGEVVLTGEATVL 135
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 174-283 6.68e-14

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 71.45  E-value: 6.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647430  174 VVKRFSQSDLEQFAQFTGDHNYIHSLETPTEERR-----VHGALLNAVVAGIMGTQLPGPGTVVLEQNFKFLKPCRI-ET 247
Cdd:PRK08190  22 LVRTLTPDDIELFAAMSGDVNPAHLDAAYAASDGfhhvvAHGMWGGALISAVLGTRLPGPGTIYLGQSLRFRRPVRIgDT 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 24647430  248 DTV-VTVRLLQSRKiSTVEYDIR---QNDEVVFAGSAKLL 283
Cdd:PRK08190 102 LTVtVTVREKDPEK-RIVVLDCRctnQDGEVVITGTAEVI 140
MaoC_C cd03452
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory ...
 176-284 4.63e-08

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: 51.25  E-value: 4.63e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647430 176 KRFSQSDLEQFAQFTGDHNYIHSLETPT-----EERRVHGALLNAVVAGIMGTqlPGPGTVV----LEqNFKFLKPCRIe 246
Cdd:cd03452  16 RTVTEADIVNFACLTGDHFYAHMDEIAAkasffGKRVAHGYFVLSAAAGLFVD--PAPGPVLanygLE-NLRFLEPVYP- 91

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 24647430 247 tDTVVTVRLLQSRKI-------STVEYDIR---QNDEVVfaGSAKLLT 284
Cdd:cd03452  92 -GDTIQVRLTCKRKIprdgqdyGVVRWDAEvtnQNGELV--ASYDILT 136
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 180-283 6.59e-07

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: 47.68  E-value: 6.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647430 180 QSDLEQFAQFTGDHNYIHS-----LETPTEERRVHGALLNAVVAGIMgTQLPGPGTVVLE----QNFKFLKPCRIeTDT- 249
Cdd:cd03446  20 EADVVMFAGLSGDWNPIHTdaeyaKKTRFGERIAHGLLTLSIATGLL-QRLGVFERTVVAfygiDNLRFLNPVFI-GDTi 97

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 24647430 250 -----VVTVRLLQSRKISTVEYDIR---QNDEVVFAGSAKLL 283
Cdd:cd03446  98 raeaeVVEKEEKDGEDAGVVTRRIEvvnQRGEVVQSGEMSLL 139
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 179-252 5.50e-06

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: 44.64  E-value: 5.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24647430   179 SQSDLEQFAQFTGDHNYIH-----SLETPTEERRVHGALLNAVVAGIMGTQLPGPG-TVVLEQNFKFLKPCRIeTDTVVT 252
Cdd:pfam01575  19 TEADIALFALVSGDHNPIHvdpefAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDNViARFGEIKVRFTKPVFP-GDTLRT 97
 
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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