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Conserved domains on  [gi|550725321|gb|ERS25142|]
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hypothetical protein HMPREF1301_00536 [Propionibacterium sp. KPL2005]

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 ...
 7-132 4.86e-47

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 cd03453:

Pssm-ID: 469797 [Multi-domain]  Cd Length: 127  Bit Score: 148.24  E-value: 4.86e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550725321   7 EGQTFGPRAIGVTRTTLVRYAGASGDFNPIHHSDRAAREAGMDGVIAHGMWTMGAALGAVIEWVGGPEQVLSQRARFTRP 86
Cdd:cd03453    1 VGDELPPLTPPVSRADLVRYAGASGDFNPIHYDEDFAKKVGLPGVIAHGMLTMGLLGRLVTDWVGDPGRVVSFGVRFTKP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 550725321  87 VLVPDTKEGASIEVAATVRRVVDD-TATLGVDVKCGGQSVLGRVEVV 132
Cdd:cd03453   81 VPVPDTLTCTGIVVEKTVADGEDAlTVTVDATDQAGGKKVLGRAIVA 127
 
Name Accession Description Interval E-value
SAV4209_like cd03453
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot ...
 7-132 4.86e-47

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: 148.24  E-value: 4.86e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550725321   7 EGQTFGPRAIGVTRTTLVRYAGASGDFNPIHHSDRAAREAGMDGVIAHGMWTMGAALGAVIEWVGGPEQVLSQRARFTRP 86
Cdd:cd03453    1 VGDELPPLTPPVSRADLVRYAGASGDFNPIHYDEDFAKKVGLPGVIAHGMLTMGLLGRLVTDWVGDPGRVVSFGVRFTKP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 550725321  87 VLVPDTKEGASIEVAATVRRVVDD-TATLGVDVKCGGQSVLGRVEVV 132
Cdd:cd03453   81 VPVPDTLTCTGIVVEKTVADGEDAlTVTVDATDQAGGKKVLGRAIVA 127
fused_HadA_HadB NF040620
fused (3R)-hydroxyacyl-ACP dehydratase subunits HadA/HadB;
5-133 2.16e-33

fused (3R)-hydroxyacyl-ACP dehydratase subunits HadA/HadB;


Pssm-ID: 468592 [Multi-domain]  Cd Length: 329  Bit Score: 119.17  E-value: 2.16e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550725321   5 LTEGQTFGPRAIGVTRTTLVRYAGASGDFNPIHHSDRAAREAGMDGVIAHGMWTMGAALGAVIEWVGGPEQVLSQRARFT 84
Cdd:NF040620 199 LAVGDELPPRTVRLTRGDLVNYAGVSGDPNPIHWSDEVARLAGLPTVVAHGMLTMGLGAGYLTSWLGDPGAVTKYSVRFT 278

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 550725321  85 RPVLVPDTkEGASIEVAATVRRVVDD--TATLGVDVKCGGQSVLGRVEVVV 133
Cdd:NF040620 279 SPVYVPAD-APAEIEFTGKVKSLDPEtrTATIALTAKSGGRKIFGRATAEV 328
PRK13693 PRK13693
(3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional
 3-134 6.53e-32

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


Pssm-ID: 184249 [Multi-domain]  Cd Length: 142  Bit Score: 110.31  E-value: 6.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550725321   3 AQLTEGQTFGPRAIGVTRTTLVRYAGASGDFNPIHHSDRAAREAGMDGVIAHGMWTMGAALGAVIEWVGGPEQVLSQRAR 82
Cdd:PRK13693   7 SSVKVGDQLPEKTYPLTRQDLVNYAGVSGDLNPIHWDDEIAKVVGLDTAIAHGMLTMGLGGGYVTSWVGDPGAVTEYNVR 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 550725321  83 FTRPVLVPDTKEGASIEVAATVRRVVDDT--ATLGVDVKCGGQSVLGRVEVVVK 134
Cdd:PRK13693  87 FTAVVPVPNDGKGAELVFNGRVKSVDPESksVTIALTATTGGKKIFGRAIASAK 140
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
3-133 3.39e-28

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 100.73  E-value: 3.39e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550725321   3 AQLTEGQTFGPRAIGVTRTTLVRYAGASGDFNPIHHSDRAAREAGMDGVIAHGMWTMGAALGAVIEWVGG--PEQVLSQR 80
Cdd:COG2030    3 EDLEVGDVLPHGGRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGtaVANLGLQE 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 550725321  81 ARFTRPVLVPDTkegasIEVAATVRRVVDD----TATLGVDVKCGGQSVLGRVEVVV 133
Cdd:COG2030   83 VRFLRPVRVGDT-----LRARVEVLEKRESksrgIVTLRTTVTNQDGEVVLTGEATV 134
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 2-118 2.21e-21

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: 82.77  E-value: 2.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550725321    2 SAQLTEGQTFGPR-AIGVTRTTLVRYAGASGDFNPIHHSDRAAREAGMDGVIAHGMWTMGAALGAVIEWVGGPEQ--VLS 78
Cdd:pfam01575   1 DFQNAPGEPPDTEkPRTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDNVIarFGE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 550725321   79 QRARFTRPVLVPDTKEGASIEVAAT-VRRVVDDTATLGVDV 118
Cdd:pfam01575  81 IKVRFTKPVFPGDTLRTEAEVVGKRdGRQTKVVEVTVEVTE 121
 
Name Accession Description Interval E-value
SAV4209_like cd03453
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot ...
 7-132 4.86e-47

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: 148.24  E-value: 4.86e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550725321   7 EGQTFGPRAIGVTRTTLVRYAGASGDFNPIHHSDRAAREAGMDGVIAHGMWTMGAALGAVIEWVGGPEQVLSQRARFTRP 86
Cdd:cd03453    1 VGDELPPLTPPVSRADLVRYAGASGDFNPIHYDEDFAKKVGLPGVIAHGMLTMGLLGRLVTDWVGDPGRVVSFGVRFTKP 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 550725321  87 VLVPDTKEGASIEVAATVRRVVDD-TATLGVDVKCGGQSVLGRVEVV 132
Cdd:cd03453   81 VPVPDTLTCTGIVVEKTVADGEDAlTVTVDATDQAGGKKVLGRAIVA 127
fused_HadA_HadB NF040620
fused (3R)-hydroxyacyl-ACP dehydratase subunits HadA/HadB;
5-133 2.16e-33

fused (3R)-hydroxyacyl-ACP dehydratase subunits HadA/HadB;


Pssm-ID: 468592 [Multi-domain]  Cd Length: 329  Bit Score: 119.17  E-value: 2.16e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550725321   5 LTEGQTFGPRAIGVTRTTLVRYAGASGDFNPIHHSDRAAREAGMDGVIAHGMWTMGAALGAVIEWVGGPEQVLSQRARFT 84
Cdd:NF040620 199 LAVGDELPPRTVRLTRGDLVNYAGVSGDPNPIHWSDEVARLAGLPTVVAHGMLTMGLGAGYLTSWLGDPGAVTKYSVRFT 278

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 550725321  85 RPVLVPDTkEGASIEVAATVRRVVDD--TATLGVDVKCGGQSVLGRVEVVV 133
Cdd:NF040620 279 SPVYVPAD-APAEIEFTGKVKSLDPEtrTATIALTAKSGGRKIFGRATAEV 328
PRK13693 PRK13693
(3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional
 3-134 6.53e-32

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


Pssm-ID: 184249 [Multi-domain]  Cd Length: 142  Bit Score: 110.31  E-value: 6.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550725321   3 AQLTEGQTFGPRAIGVTRTTLVRYAGASGDFNPIHHSDRAAREAGMDGVIAHGMWTMGAALGAVIEWVGGPEQVLSQRAR 82
Cdd:PRK13693   7 SSVKVGDQLPEKTYPLTRQDLVNYAGVSGDLNPIHWDDEIAKVVGLDTAIAHGMLTMGLGGGYVTSWVGDPGAVTEYNVR 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 550725321  83 FTRPVLVPDTKEGASIEVAATVRRVVDDT--ATLGVDVKCGGQSVLGRVEVVVK 134
Cdd:PRK13693  87 FTAVVPVPNDGKGAELVFNGRVKSVDPESksVTIALTATTGGKKIFGRAIASAK 140
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
3-133 3.39e-28

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 100.73  E-value: 3.39e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550725321   3 AQLTEGQTFGPRAIGVTRTTLVRYAGASGDFNPIHHSDRAAREAGMDGVIAHGMWTMGAALGAVIEWVGG--PEQVLSQR 80
Cdd:COG2030    3 EDLEVGDVLPHGGRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGtaVANLGLQE 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 550725321  81 ARFTRPVLVPDTkegasIEVAATVRRVVDD----TATLGVDVKCGGQSVLGRVEVVV 133
Cdd:COG2030   83 VRFLRPVRVGDT-----LRARVEVLEKRESksrgIVTLRTTVTNQDGEVVLTGEATV 134
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 9-120 1.11e-23

(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: 88.86  E-value: 1.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550725321   9 QTFGPRAIGVTRTTLVRYAGASGDFNPIHHSDRAAREAGMDGVIAHGMWTMGAALGAVIEWVGGPEQ--VLSQRARFTRP 86
Cdd:cd03441    1 GELDSSGRTVTEADIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGLLVQWLPGTDGanLGSQSVRFLAP 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 550725321  87 VLVPDTkegasIEVAATVRRVVDDTATLGVDVKC 120
Cdd:cd03441   81 VFPGDT-----LRVEVEVLGKRPSKGRGVVTVRT 109
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 2-118 2.21e-21

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: 82.77  E-value: 2.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550725321    2 SAQLTEGQTFGPR-AIGVTRTTLVRYAGASGDFNPIHHSDRAAREAGMDGVIAHGMWTMGAALGAVIEWVGGPEQ--VLS 78
Cdd:pfam01575   1 DFQNAPGEPPDTEkPRTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDNVIarFGE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 550725321   79 QRARFTRPVLVPDTKEGASIEVAAT-VRRVVDDTATLGVDV 118
Cdd:pfam01575  81 IKVRFTKPVFPGDTLRTEAEVVGKRdGRQTKVVEVTVEVTE 121
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 18-124 1.38e-15

(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: 67.96  E-value: 1.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550725321  18 VTRTTLVRYAGASGDFNPIHHSDRAAREAGMDGVIAHGMWTMG---AALGAVIewvGGPEQV-LSQRARFTRPVLVPDTk 93
Cdd:cd03449   13 ITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASlisAVLGTLL---PGPGTIyLSQSLRFLRPVFIGDT- 88

                         90       100       110
                 ....*....|....*....|....*....|.
gi 550725321  94 egasIEVAATVRRVVDDTATLGVDVKCGGQS 124
Cdd:cd03449   89 ----VTATVTVTEKREDKKRVTLETVCTNQN 115
FAS_MaoC cd03447
FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes ...
 26-92 5.33e-15

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: 66.53  E-value: 5.33e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 550725321  26 YAGASGDFNPIHHSDRAAREAGMDGVIAHGMWTMGAALGAVIEWVGG--PEQVLSQRARFTRPVLVPDT 92
Cdd:cd03447   18 YARVSGDFNPIHVSRVFASYAGLPGTITHGMYTSAAVRALVETWAADndRSRVRSFTASFVGMVLPNDE 86
SAV4209 cd03455
SAV4209 is a Streptomyces avermitilis protein with a hot dog fold that is similar to those of ...
 13-132 2.81e-12

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: 59.25  E-value: 2.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550725321  13 PRAIGVTRTTLVRYAGASGDFNPIHHSDRAAREAGMDGVIAHGMWTMGAALGAVIEWVGGPEQVLSQRARFTRPVLVPDT 92
Cdd:cd03455    6 RLSIPPDPTLLFRYSAATRDFHRIHHDRDYARAVGYPDLYVNGPTLAGLVIRYVTDWAGPDARVKSFAFRLGAPLYAGDT 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 550725321  93 KEGaSIEVAAtVRRVVDDTATLGVDVKCGGQSVLGRVEVV 132
Cdd:cd03455   86 LRF-GGRVTA-KRDDEVVTVELWARNSEGDHVMAGTATVA 123
HDE_HSD cd03448
HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), ...
 30-115 4.50e-12

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: 58.77  E-value: 4.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550725321  30 SGDFNPIHHSDRAAREAGMDGVIAHGMWTMGAALGAVIEWVGG--PEQVLSQRARFTRPVLVPDT------KEGAsiEVA 101
Cdd:cd03448   24 SGDYNPLHIDPAFAKAAGFPRPILHGLCTYGFAARAVLEAFADgdPARFKAIKVRFSSPVFPGETlrtemwKEGN--RVI 101

                         90
                 ....*....|....
gi 550725321 102 ATVRRVVDDTATLG 115
Cdd:cd03448  102 FQTKVVERDVVVLS 115
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 7-136 1.88e-11

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: 57.70  E-value: 1.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550725321   7 EGQTFGPRAIGVTRTTLVRYAGASGDFNPIHHSDRAAREAGMDGVIAHGMWTMGAALGAVIEWVGGPEQVLS----QRAR 82
Cdd:cd03446    7 IGQVFESVGRTVTEADVVMFAGLSGDWNPIHTDAEYAKKTRFGERIAHGLLTLSIATGLLQRLGVFERTVVAfygiDNLR 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 550725321  83 FTRPVLVPDTKEgASIEVAATVRRVVDDTATLGVDVKCGGQsvlgRVEVVVKQE 136
Cdd:cd03446   87 FLNPVFIGDTIR-AEAEVVEKEEKDGEDAGVVTRRIEVVNQ----RGEVVQSGE 135
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 1-136 3.61e-11

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 59.12  E-value: 3.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550725321   1 MSAQLTEGQTFGPRAIG----VTRTTLVR----YAGASGDFNPIHHSDRAAREAGMDGVIAHGMWTmGAALGAViewVG- 71
Cdd:PRK08190   1 MDLELIENRTFDEIAIGdsasLVRTLTPDdielFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWG-GALISAV---LGt 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 550725321  72 ---GPEQV-LSQRARFTRPVLVPDTkegasIEVAATVRRVVDDTATLGVDVKC---GGQSVL-GRVEVVVKQE 136
Cdd:PRK08190  77 rlpGPGTIyLGQSLRFRRPVRIGDT-----LTVTVTVREKDPEKRIVVLDCRCtnqDGEVVItGTAEVIAPTE 144
MaoC_dehydrat_N pfam13452
N-terminal half of MaoC dehydratase; It is clear from the structures of bacterial members of ...
 8-92 8.93e-07

N-terminal half of MaoC dehydratase; It is clear from the structures of bacterial members of MaoC dehydratase, pfam01575, that the full-length functional dehydratase enzyme is made up of two structures that dimerize to form a whole. Divergence of the N- and C- monomers in higher eukaryotes has led to two distinct domains, this one and MaoC_dehydratas. However, in order to function as an enzyme both are required together.


Pssm-ID: 433220 [Multi-domain]  Cd Length: 132  Bit Score: 44.99  E-value: 8.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550725321    8 GQTFGPRAIGVTRTTLVRYAGASGDFNPIHHSDRAAREAGMDGVIAHGMWTMGAALGAV--IEWVGGP-EQVL--SQRAR 82
Cdd:pfam13452   4 GVEFGPVKYEVERGAIREFARAIGETNPAYWDEAAARAAGYGDLPAPPTFLFVLGWDAPgfMEQLGIDlSRLLhgEQRFT 83

                          90
                  ....*....|
gi 550725321   83 FTRPVLVPDT 92
Cdd:pfam13452  84 YHRPLRAGDE 93
PLN02864 PLN02864
enoyl-CoA hydratase
 30-83 8.45e-06

enoyl-CoA hydratase


Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 43.62  E-value: 8.45e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 550725321  30 SGDFNPIHHSDRAAREAGMDGVIAHGMWTMGAALGAVIEWV--GGPEQVLSQRARF 83
Cdd:PLN02864 207 SGDYNPLHSDPMFAKVAGFTRPILHGLCTLGFAVRAVIKCFcnGDPTAVKTISGRF 262
MaoC_C cd03452
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory ...
 3-109 1.59e-04

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: 39.31  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550725321   3 AQLTEGQTFGPRAIGVTRTTLVRYAGASGDFNPIHHSDRAAREAGMDGVIAHGMWTMGAALGAVIEWVGGPeqVL----S 78
Cdd:cd03452    3 EQLRPGDSLLTHRRTVTEADIVNFACLTGDHFYAHMDEIAAKASFFGKRVAHGYFVLSAAAGLFVDPAPGP--VLanygL 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 550725321  79 QRARFTRPVLVPDTkegasIEVAATVRRVVD 109
Cdd:cd03452   81 ENLRFLEPVYPGDT-----IQVRLTCKRKIP 106
 
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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