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Conserved domains on  [gi|740365217|ref|WP_038200747|]
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MaoC/PaaZ C-terminal domain-containing protein [Xenophilus azovorans]

Protein Classification

hotdog family protein( domain architecture ID 107)

hotdog family protein may have metabolic roles such as thioester hydrolysis in fatty acid metabolism and degradation of phenylacetic acid and the environmental pollutant 4-chlorobenzoate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hot_dog super family cl00509
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 13-153 9.76e-58

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.


The actual alignment was detected with superfamily member cd03446:

Pssm-ID: 469797 [Multi-domain]  Cd Length: 140  Bit Score: 176.73  E-value: 9.76e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740365217  13 FEDLEVGAAFDSPTRTMTEADVVNFAGLSADFNRLHVDAEYAAGTPYGQRIAHGLLVLALMSGLVTRMLLNQQLEPSLMG 92
Cdd:cd03446    2 FEDFEIGQVFESVGRTVTEADVVMFAGLSGDWNPIHTDAEYAKKTRFGERIAHGLLTLSIATGLLQRLGVFERTVVAFYG 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740365217  93 LLDIqcRFPKPIFIGDTLRVRVEVAAKNETSKPDRGVVAFRRQALNQRGEVVVEGTWKLLV 153
Cdd:cd03446   82 IDNL--RFLNPVFIGDTIRAEAEVVEKEEKDGEDAGVVTRRIEVVNQRGEVVQSGEMSLLV 140
 
Name Accession Description Interval E-value
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 13-153 9.76e-58

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: 176.73  E-value: 9.76e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740365217  13 FEDLEVGAAFDSPTRTMTEADVVNFAGLSADFNRLHVDAEYAAGTPYGQRIAHGLLVLALMSGLVTRMLLNQQLEPSLMG 92
Cdd:cd03446    2 FEDFEIGQVFESVGRTVTEADVVMFAGLSGDWNPIHTDAEYAKKTRFGERIAHGLLTLSIATGLLQRLGVFERTVVAFYG 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740365217  93 LLDIqcRFPKPIFIGDTLRVRVEVAAKNETSKPDRGVVAFRRQALNQRGEVVVEGTWKLLV 153
Cdd:cd03446   82 IDNL--RFLNPVFIGDTIRAEAEVVEKEEKDGEDAGVVTRRIEVVNQRGEVVQSGEMSLLV 140
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
12-157 5.16e-55

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 169.68  E-value: 5.16e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740365217  12 FFEDLEVGAAFDSPTRTMTEADVVNFAGLSADFNRLHVDAEYAAGTPYGQRIAHGLLVLALMSGLVTRMLLNqqlePSLM 91
Cdd:COG2030    1 YFEDLEVGDVLPHGGRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPG----TAVA 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740365217  92 GLLDIQCRFPKPIFIGDTLRVRVEVAAKNEtsKPDRGVVAFRRQALNQRGEVVVEGTWKLLVRRRP 157
Cdd:COG2030   77 NLGLQEVRFLRPVRVGDTLRARVEVLEKRE--SKSRGIVTLRTTVTNQDGEVVLTGEATVLVPRRP 140
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 24-121 3.60e-27

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: 98.18  E-value: 3.60e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740365217   24 SPTRTMTEADVVNFAGLSADFNRLHVDAEYAAGTPYGQRIAHGLLVLALMSGLVTRmllnQQLEPSLMGLLDIQCRFPKP 103
Cdd:pfam01575  13 EKPRTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEE----WGGDNVIARFGEIKVRFTKP 88

                          90
                  ....*....|....*...
gi 740365217  104 IFIGDTLRVRVEVAAKNE 121
Cdd:pfam01575  89 VFPGDTLRTEAEVVGKRD 106
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 13-148 1.61e-26

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 103.42  E-value: 1.61e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740365217  13 FEDLEVGAAfDSPTRTMTEADVVNFAGLSADFNRLHVDAEYAAGTPYGQRIAHGLLVLALMSGLVTRML-------LNQQ 85
Cdd:PRK08190  11 FDEIAIGDS-ASLVRTLTPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGGALISAVLGTRLpgpgtiyLGQS 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740365217  86 LepslmglldiqcRFPKPIFIGDTLRVRVEVAAKNetskPDRGVVAFRRQALNQRGEVVVEGT 148
Cdd:PRK08190  90 L------------RFRRPVRIGDTLTVTVTVREKD----PEKRIVVLDCRCTNQDGEVVITGT 136
 
Name Accession Description Interval E-value
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 13-153 9.76e-58

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: 176.73  E-value: 9.76e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740365217  13 FEDLEVGAAFDSPTRTMTEADVVNFAGLSADFNRLHVDAEYAAGTPYGQRIAHGLLVLALMSGLVTRMLLNQQLEPSLMG 92
Cdd:cd03446    2 FEDFEIGQVFESVGRTVTEADVVMFAGLSGDWNPIHTDAEYAKKTRFGERIAHGLLTLSIATGLLQRLGVFERTVVAFYG 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740365217  93 LLDIqcRFPKPIFIGDTLRVRVEVAAKNETSKPDRGVVAFRRQALNQRGEVVVEGTWKLLV 153
Cdd:cd03446   82 IDNL--RFLNPVFIGDTIRAEAEVVEKEEKDGEDAGVVTRRIEVVNQRGEVVQSGEMSLLV 140
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
12-157 5.16e-55

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 169.68  E-value: 5.16e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740365217  12 FFEDLEVGAAFDSPTRTMTEADVVNFAGLSADFNRLHVDAEYAAGTPYGQRIAHGLLVLALMSGLVTRMLLNqqlePSLM 91
Cdd:COG2030    1 YFEDLEVGDVLPHGGRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPG----TAVA 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740365217  92 GLLDIQCRFPKPIFIGDTLRVRVEVAAKNEtsKPDRGVVAFRRQALNQRGEVVVEGTWKLLVRRRP 157
Cdd:COG2030   77 NLGLQEVRFLRPVRVGDTLRARVEVLEKRE--SKSRGIVTLRTTVTNQDGEVVLTGEATVLVPRRP 140
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 21-152 1.69e-42

(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: 137.40  E-value: 1.69e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740365217  21 AFDSPTRTMTEADVVNFAGLSADFNRLHVDAEYAAGTPYGQRIAHGLLVLALMSGLVTRMLLNqqlePSLMGLLDIQCRF 100
Cdd:cd03441    2 ELDSSGRTVTEADIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGLLVQWLPG----TDGANLGSQSVRF 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 740365217 101 PKPIFIGDTLRVRVEVAAKNEtsKPDRGVVAFRRQALNQRGEVVVEGTWKLL 152
Cdd:cd03441   78 LAPVFPGDTLRVEVEVLGKRP--SKGRGVVTVRTEARNQGGEVVLSGEATVL 127
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 16-153 3.09e-40

(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: 131.90  E-value: 3.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740365217  16 LEVGAAFdSPTRTMTEADVVNFAGLSADFNRLHVDAEYAAGTPYGQRIAHGLLVLALMSGLVTRML-------LNQQLep 88
Cdd:cd03449    1 LKVGDSA-SLTRTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASLISAVLGTLLpgpgtiyLSQSL-- 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740365217  89 slmglldiqcRFPKPIFIGDTLRVRVEVAAKNetskPDRGVVAFRRQALNQRGEVVVEGTWKLLV 153
Cdd:cd03449   78 ----------RFLRPVFIGDTVTATVTVTEKR----EDKKRVTLETVCTNQNGEVVIEGEAVVLA 128
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 12-157 5.57e-38

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: 126.55  E-value: 5.57e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740365217  12 FFEDLEVGAAFDS-PTRTMTEADVVNFAGLSADFNRLHVDAEYAAGTPYGQRIAHGLLVLALMSGLVTRMLLNQqlepsL 90
Cdd:cd03451    3 YFEDFTVGQVFEHaPGRTVTEADNVLFTLLTMNTAPLHFDAAYAAKTEFGRRLVNSLFTLSLALGLSVNDTSLT-----A 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740365217  91 MGLLDI-QCRFPKPIFIGDTLRVRVEVAAKNET-SKPDRGVVAFRRQALNQRGEVVVEGTWKLLVRRRP 157
Cdd:cd03451   78 VANLGYdEVRFPAPVFHGDTLYAESEVLSKRESkSRPDAGIVTVRTVGYNQDGEPVLSFERTALVPKRG 146
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 13-154 1.29e-31

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: 110.35  E-value: 1.29e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740365217  13 FEDLEVGAAFDSPTRTMTEADVVNFAglsADFN--RLHVDAEYAAGTPYGQRIAHGLLVLALMsglvTRMLL--NQQLEP 88
Cdd:cd03454    1 FEDLVIGQRFTSGSYTVTEEEIIAFA---REFDpqPFHLDEEAAKESLFGGLAASGWHTAAIT----MRLLVdaGLSGSA 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740365217  89 SLMGLLDIQCRFPKPIFIGDTLRVRVEVAAKNE-TSKPDRGVVAFRRQALNQRGEVVVEGTWKLLVR 154
Cdd:cd03454   74 SGGSPGIDELRWPRPVRPGDTLSVEVEVLDKRPsRSRPDRGIVTLRSETLNQRGEVVLTFEATVLVR 140
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 24-121 3.60e-27

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: 98.18  E-value: 3.60e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740365217   24 SPTRTMTEADVVNFAGLSADFNRLHVDAEYAAGTPYGQRIAHGLLVLALMSGLVTRmllnQQLEPSLMGLLDIQCRFPKP 103
Cdd:pfam01575  13 EKPRTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEE----WGGDNVIARFGEIKVRFTKP 88

                          90
                  ....*....|....*...
gi 740365217  104 IFIGDTLRVRVEVAAKNE 121
Cdd:pfam01575  89 VFPGDTLRTEAEVVGKRD 106
MaoC_C cd03452
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory ...
 13-157 4.49e-27

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: 98.63  E-value: 4.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740365217  13 FEDLEVGAAFDSPTRTMTEADVVNFAGLSADFNRLHVDAEYAAGTPYGQRIAHGLLVLALMSGLvtrmLLNQQLEPSL-- 90
Cdd:cd03452    2 LEQLRPGDSLLTHRRTVTEADIVNFACLTGDHFYAHMDEIAAKASFFGKRVAHGYFVLSAAAGL----FVDPAPGPVLan 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740365217  91 MGLLDIqcRFPKPIFIGDTLRVRVEVAAKNETSKPDRGVVAFRRQALNQRGEVVVEGTWKLLVRRRP 157
Cdd:cd03452   78 YGLENL--RFLEPVYPGDTIQVRLTCKRKIPRDGQDYGVVRWDAEVTNQNGELVASYDILTLVAKKG 142
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 13-148 1.61e-26

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 103.42  E-value: 1.61e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740365217  13 FEDLEVGAAfDSPTRTMTEADVVNFAGLSADFNRLHVDAEYAAGTPYGQRIAHGLLVLALMSGLVTRML-------LNQQ 85
Cdd:PRK08190  11 FDEIAIGDS-ASLVRTLTPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGGALISAVLGTRLpgpgtiyLGQS 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740365217  86 LepslmglldiqcRFPKPIFIGDTLRVRVEVAAKNetskPDRGVVAFRRQALNQRGEVVVEGT 148
Cdd:PRK08190  90 L------------RFRRPVRIGDTLTVTVTVREKD----PEKRIVVLDCRCTNQDGEVVITGT 136
SAV4209_like cd03453
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot ...
 18-148 2.70e-15

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: 67.73  E-value: 2.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740365217  18 VGAAFDSPTRTMTEADVVNFAGLSADFNRLHVDAEYAAGTPYGQRIAHGLLVLALMSGLVTRMLLNQQlepslmGLLDIQ 97
Cdd:cd03453    1 VGDELPPLTPPVSRADLVRYAGASGDFNPIHYDEDFAKKVGLPGVIAHGMLTMGLLGRLVTDWVGDPG------RVVSFG 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 740365217  98 CRFPKPIFIGDTLRVRVEVAAKNETSKPDRgvVAFRRQALNQRGEVVVEGT 148
Cdd:cd03453   75 VRFTKPVPVPDTLTCTGIVVEKTVADGEDA--LTVTVDATDQAGGKKVLGR 123
NodN cd03450
NodN (nodulation factor N) contains a single hot dog fold similar to those of the peroxisomal ...
 24-118 4.75e-11

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: 57.19  E-value: 4.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740365217  24 SPTRTMTEADVVNFAGLSADFNRLHVDAEYAAGTPYGQRIAHGLLVLALMSGLVTRMLlnqQLEPSLMGL---LDiQCRF 100
Cdd:cd03450   19 SDWVTVDQERIDQFADATGDHQWIHVDPERAAAEPFGGTIAHGFLTLSLLPALTPQLF---RVEGVKMGVnygLD-KVRF 94

                         90
                 ....*....|....*...
gi 740365217 101 PKPIFIGDTLRVRVEVAA 118
Cdd:cd03450   95 PAPVPVGSRVRGRFTLLS 112
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 60-148 1.09e-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: 55.17  E-value: 1.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740365217  60 GQRIAHGLLVLALMSGLVTRMLLNQQLEPSLMGLLDIQCRFPKPIFIGDTLRVRVEVAAKnetskpDRGVVAFRRQALNQ 139
Cdd:cd03440   14 GGGIVHGGLLLALADEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRV------GRSSVTVEVEVRNE 87


                 ....*....
gi 740365217 140 RGEVVVEGT 148
Cdd:cd03440   88 DGKLVATAT 96
PRK13693 PRK13693
(3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional
 13-78 1.11e-09

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


Pssm-ID: 184249 [Multi-domain]  Cd Length: 142  Bit Score: 53.68  E-value: 1.11e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740365217  13 FEDLEVGAAFDSPTRTMTEADVVNFAGLSADFNRLHVDAEYAAGTPYGQRIAHGLLVLALMSGLVT 78
Cdd:PRK13693   6 FSSVKVGDQLPEKTYPLTRQDLVNYAGVSGDLNPIHWDDEIAKVVGLDTAIAHGMLTMGLGGGYVT 71
SAV4209 cd03455
SAV4209 is a Streptomyces avermitilis protein with a hot dog fold that is similar to those of ...
 30-148 2.35e-09

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: 52.32  E-value: 2.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740365217  30 TEADVVNFAGLSADFNRLHVDAEYAAGTPYGQRIAHGLLVLALMSGLVTRmllnqQLEPSLMgLLDIQCRFPKPIFIGDT 109
Cdd:cd03455   12 DPTLLFRYSAATRDFHRIHHDRDYARAVGYPDLYVNGPTLAGLVIRYVTD-----WAGPDAR-VKSFAFRLGAPLYAGDT 85

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 740365217 110 LRVRVEVAAKNETskpDRGVVAFRrqALNQRGEVVVEGT 148
Cdd:cd03455   86 LRFGGRVTAKRDD---EVVTVELW--ARNSEGDHVMAGT 119
HDE_HSD cd03448
HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), ...
 40-152 1.02e-08

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: 50.68  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740365217  40 LSADFNRLHVDAEYAAGTPYGQRIAHGLLVLalmsGLVTRMLLNQQLEPSLMGLLDIQCRFPKPIFIGDTLRVRVEVaak 119
Cdd:cd03448   23 LSGDYNPLHIDPAFAKAAGFPRPILHGLCTY----GFAARAVLEAFADGDPARFKAIKVRFSSPVFPGETLRTEMWK--- 95

                         90       100       110
                 ....*....|....*....|....*....|...
gi 740365217 120 netskpDRGVVAFRRQALNqRGEVVVEGTWKLL 152
Cdd:cd03448   96 ------EGNRVIFQTKVVE-RDVVVLSNGAALL 121
PLN02864 PLN02864
enoyl-CoA hydratase
 40-110 3.26e-04

enoyl-CoA hydratase


Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 39.77  E-value: 3.26e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740365217  40 LSADFNRLHVDAEYAAGTPYGQRIAHGLLVLALMSGLVTRMLLNQqlEPSLMGllDIQCRFPKPIFIGDTL 110
Cdd:PLN02864 206 LSGDYNPLHSDPMFAKVAGFTRPILHGLCTLGFAVRAVIKCFCNG--DPTAVK--TISGRFLLHVYPGETL 272
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 93-152 8.25e-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: 36.82  E-value: 8.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 740365217  93 LLDIQCRFPKPIFIGDTLRVRVEVAAKNETSkpdrgvVAFRRQALNQRGEVVVEGTWKLL 152
Cdd:cd00586   54 VVELEIDYLRPLRLGDRLTVETRVLRLGRKS------FTFEQEIFREDGELLATAETVLV 107
FAS_MaoC cd03447
FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes ...
 37-148 9.19e-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: 34.56  E-value: 9.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740365217  37 FAGLSADFNRLHVDAEYA--AGTPygQRIAHGLLVLALMSGLVTRMLLNqqlepSLMG-LLDIQCRFPKPIFIGDTLRVR 113
Cdd:cd03447   18 YARVSGDFNPIHVSRVFAsyAGLP--GTITHGMYTSAAVRALVETWAAD-----NDRSrVRSFTASFVGMVLPNDELEVR 90

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 740365217 114 VEVAAKnetskpDRGVVAFRRQALNQR-GEVVVEGT 148
Cdd:cd03447   91 LEHVGM------VDGRKVIKVEARNEEtGELVLRGE 120
PRK13188 PRK13188
bifunctional UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase/(3R) ...
 80-147 9.66e-03

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: 35.29  E-value: 9.66e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740365217  80 MLLNQQLEPS-----LMGLlDiQCRFPKPIFIGDTLRVRVEVaakneTSKPDRGVVAFRRQALnQRGEVVVEG 147
Cdd:PRK13188 389 LVLNTVPDPEnystyFMKI-D-KVKFRQKVVPGDTLIFKVEL-----LSPIRRGICQMQGKAY-VNGKLVCEA 453
 
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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