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Conserved domains on  [gi|695718478|ref|WP_032646165|]
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MULTISPECIES: YbgC/FadM family acyl-CoA thioesterase [Enterobacter]

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 ...
 4-120 1.02e-48

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 TIGR00051:

Pssm-ID: 469797 [Multi-domain]  Cd Length: 117  Bit Score: 151.80  E-value: 1.02e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695718478    4 KIKVRGFHLDVYQHVNNARYLEFLEEARWDGLENSESFQWLTAHN-IAFVVVNININYRRPAVLGDVLTVTSQVQQINGK 82
Cdd:TIGR00051   1 PVRVYYEDTDAQGIVYHANYLRYCERARTEFLRSLGFPQSVLRAEgVAFVVVNINIEYKKPARLDDVLEIRTQIEELNGF 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 695718478   83 SGVLSQVVTLDPEGQVVADALITFvCIDLKTQKALPLE 120
Cdd:TIGR00051  81 SFVFSQEIFNEDEALLKAATVIVV-CVDPKKQKPVAIP 117
 
Name Accession Description Interval E-value
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 4-120 1.02e-48

acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related acyl-CoA thioesterases that include several at least partially characterized proteins. YbgC is an acyl-CoA thioesterase associated with the Tol-Pal system. YbaW is part of the FadM regulon. [Unknown function, General]


Pssm-ID: 129161 [Multi-domain]  Cd Length: 117  Bit Score: 151.80  E-value: 1.02e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695718478    4 KIKVRGFHLDVYQHVNNARYLEFLEEARWDGLENSESFQWLTAHN-IAFVVVNININYRRPAVLGDVLTVTSQVQQINGK 82
Cdd:TIGR00051   1 PVRVYYEDTDAQGIVYHANYLRYCERARTEFLRSLGFPQSVLRAEgVAFVVVNINIEYKKPARLDDVLEIRTQIEELNGF 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 695718478   83 SGVLSQVVTLDPEGQVVADALITFvCIDLKTQKALPLE 120
Cdd:TIGR00051  81 SFVFSQEIFNEDEALLKAATVIVV-CVDPKKQKPVAIP 117
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 2-128 1.86e-41

Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440586 [Multi-domain]  Cd Length: 139  Bit Score: 134.26  E-value: 1.86e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695718478   2 QTKIKVRGFHLDVYQHVNNARYLEFLEEARWDGL-ENSESFQWLTAHNIAFVVVNININYRRPAVLGDVLTVTSQVQQIN 80
Cdd:COG0824    7 ETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLrALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVETRVVRLG 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 695718478  81 GKSGVLSQVVTLDPEGQVVADALITFVCIDLKTQKALPLEGELREKLE 128
Cdd:COG0824   87 GSSLTFEYEIFRADDGELLATGETVLVFVDLETGRPVPLPDELRAALE 134
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 3-110 2.98e-31

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: 107.31  E-value: 2.98e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695718478   3 TKIKVRGFHLDVYQHVNNARYLEFLEEARWDGLEN-SESFQWLTAHNIAFVVVNININYRRPAVLGDVLTVTSQVQQING 81
Cdd:cd00586    3 LEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRElGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRLGR 82

                         90       100
                 ....*....|....*....|....*....
gi 695718478  82 KSGVLSQVVTlDPEGQVVADALITFVCID 110
Cdd:cd00586   83 KSFTFEQEIF-REDGELLATAETVLVCVD 110
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 11-127 4.99e-22

Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally thioesterases. These enzymes are part of the Hotdog fold superfamily.


Pssm-ID: 463826  Cd Length: 121  Bit Score: 84.31  E-value: 4.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695718478   11 HLDVYQHVNNARYLEFLEEARWDGLE-NSESFQWLTAHNIAFVVVNININYRRPAVLGDVLTVTSQVQQINGKSGVLSQV 89
Cdd:pfam13279   5 DIDANGHMNNARYLRYFEEARDRFLErLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRFHLEHR 84

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 695718478   90 VtLDPEGQVVADALITFVCIDLKTQKALPLEGELREKL 127
Cdd:pfam13279  85 F-LSPDGKLVATAETRLVFVDYETRKPAPIPEELLEAL 121
PRK10800 PRK10800
acyl-CoA thioesterase YbgC; Provisional
 18-119 2.43e-13

acyl-CoA thioesterase YbgC; Provisional


Pssm-ID: 182742  Cd Length: 130  Bit Score: 62.07  E-value: 2.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695718478  18 VNNARYLEFLEEARWDGL-ENSESFQWLTAHNIAFVVVNININYRRPAVLGDVLTVTSQVQQINGKSGVLSQVVtLDPEG 96
Cdd:PRK10800  20 VYHASYVAFYERARTEMLrHHHFSQQALLAERVAFVVRKMTVEYYAPARLDDMLEVQSEITSMRGTSLTFTQRI-VNAEG 98

                         90       100
                 ....*....|....*....|...
gi 695718478  97 QVVADALITFVCIDLKTQKALPL 119
Cdd:PRK10800  99 TLLNEAEVLIVCVDPLKMKPRAL 121
 
Name Accession Description Interval E-value
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 4-120 1.02e-48

acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related acyl-CoA thioesterases that include several at least partially characterized proteins. YbgC is an acyl-CoA thioesterase associated with the Tol-Pal system. YbaW is part of the FadM regulon. [Unknown function, General]


Pssm-ID: 129161 [Multi-domain]  Cd Length: 117  Bit Score: 151.80  E-value: 1.02e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695718478    4 KIKVRGFHLDVYQHVNNARYLEFLEEARWDGLENSESFQWLTAHN-IAFVVVNININYRRPAVLGDVLTVTSQVQQINGK 82
Cdd:TIGR00051   1 PVRVYYEDTDAQGIVYHANYLRYCERARTEFLRSLGFPQSVLRAEgVAFVVVNINIEYKKPARLDDVLEIRTQIEELNGF 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 695718478   83 SGVLSQVVTLDPEGQVVADALITFvCIDLKTQKALPLE 120
Cdd:TIGR00051  81 SFVFSQEIFNEDEALLKAATVIVV-CVDPKKQKPVAIP 117
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 2-128 1.86e-41

Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440586 [Multi-domain]  Cd Length: 139  Bit Score: 134.26  E-value: 1.86e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695718478   2 QTKIKVRGFHLDVYQHVNNARYLEFLEEARWDGL-ENSESFQWLTAHNIAFVVVNININYRRPAVLGDVLTVTSQVQQIN 80
Cdd:COG0824    7 ETPIRVRFGDTDAMGHVNNANYLRYFEEARTEFLrALGLSYAELEEEGIGLVVVEAEIDYLRPARYGDELTVETRVVRLG 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 695718478  81 GKSGVLSQVVTLDPEGQVVADALITFVCIDLKTQKALPLEGELREKLE 128
Cdd:COG0824   87 GSSLTFEYEIFRADDGELLATGETVLVFVDLETGRPVPLPDELRAALE 134
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 3-110 2.98e-31

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: 107.31  E-value: 2.98e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695718478   3 TKIKVRGFHLDVYQHVNNARYLEFLEEARWDGLEN-SESFQWLTAHNIAFVVVNININYRRPAVLGDVLTVTSQVQQING 81
Cdd:cd00586    3 LEIRVRFGDTDAAGHVNNARYLRYFEEAREEFLRElGLGYDELEEQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRLGR 82

                         90       100
                 ....*....|....*....|....*....
gi 695718478  82 KSGVLSQVVTlDPEGQVVADALITFVCID 110
Cdd:cd00586   83 KSFTFEQEIF-REDGELLATAETVLVCVD 110
4HBT_2 pfam13279
Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally ...
 11-127 4.99e-22

Thioesterase-like superfamily; This family contains a wide variety of enzymes, principally thioesterases. These enzymes are part of the Hotdog fold superfamily.


Pssm-ID: 463826  Cd Length: 121  Bit Score: 84.31  E-value: 4.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695718478   11 HLDVYQHVNNARYLEFLEEARWDGLE-NSESFQWLTAHNIAFVVVNININYRRPAVLGDVLTVTSQVQQINGKSGVLSQV 89
Cdd:pfam13279   5 DIDANGHMNNARYLRYFEEARDRFLErLGLDLAYREALGIGLILAEAHVRYRRELKLGDELTVETRLIDWDAKRFHLEHR 84

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 695718478   90 VtLDPEGQVVADALITFVCIDLKTQKALPLEGELREKL 127
Cdd:pfam13279  85 F-LSPDGKLVATAETRLVFVDYETRKPAPIPEELLEAL 121
FatA COG3884
Acyl-ACP thioesterase [Lipid transport and metabolism];
3-106 5.43e-15

Acyl-ACP thioesterase [Lipid transport and metabolism];


Pssm-ID: 443092 [Multi-domain]  Cd Length: 242  Bit Score: 68.44  E-value: 5.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695718478   3 TKIKVRGFHLDVYQHVNNARYLEFLEEARWDglensesfQWLTAHniafVVVNININYRRPAVLGDVLTVTSQVQQingk 82
Cdd:COG3884  152 KEFTVRYSDIDTNGHVNNARYLEWALDALPL--------EFLKNH----RLKRLEINYLKEVRLGDTVEVRSARDE---- 215

                         90       100
                 ....*....|....*....|....
gi 695718478  83 SGVLSQVVTLDPEGQVVADALITF 106
Cdd:COG3884  216 DGRTLHRIVGDDDGKELARARIEW 239
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 3-107 9.28e-15

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: 64.80  E-value: 9.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695718478   3 TKIKVRGFHLDVYQHVNNARYLEFLEEARWdglensESFQWLTAHNIAFVVVNININYRRPAVLGDVLTVTSQVQQINGK 82
Cdd:cd03440    3 LRLTVTPEDIDGGGIVHGGLLLALADEAAG------AAAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRS 76

                         90       100
                 ....*....|....*....|....*
gi 695718478  83 SGVLSQVVTlDPEGQVVADALITFV 107
Cdd:cd03440   77 SVTVEVEVR-NEDGKLVATATATFV 100
PRK10800 PRK10800
acyl-CoA thioesterase YbgC; Provisional
 18-119 2.43e-13

acyl-CoA thioesterase YbgC; Provisional


Pssm-ID: 182742  Cd Length: 130  Bit Score: 62.07  E-value: 2.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695718478  18 VNNARYLEFLEEARWDGL-ENSESFQWLTAHNIAFVVVNININYRRPAVLGDVLTVTSQVQQINGKSGVLSQVVtLDPEG 96
Cdd:PRK10800  20 VYHASYVAFYERARTEMLrHHHFSQQALLAERVAFVVRKMTVEYYAPARLDDMLEVQSEITSMRGTSLTFTQRI-VNAEG 98

                         90       100
                 ....*....|....*....|...
gi 695718478  97 QVVADALITFVCIDLKTQKALPL 119
Cdd:PRK10800  99 TLLNEAEVLIVCVDPLKMKPRAL 121
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 15-99 5.76e-13

Thioesterase superfamily; This family contains a wide variety of enzymes, principally thioesterases. This family includes 4HBT (EC 3.1.2.23) which catalyzes the final step in the biosynthesis of 4-hydroxybenzoate from 4-chlorobenzoate in the soil dwelling microbe Pseudomonas CBS-3. This family includes various cytosolic long-chain acyl-CoA thioester hydrolases. Long-chain acyl-CoA hydrolases hydrolyse palmitoyl-CoA to CoA and palmitate, they also catalyze the hydrolysis of other long chain fatty acyl-CoA thioesters.


Pssm-ID: 427116 [Multi-domain]  Cd Length: 79  Bit Score: 59.58  E-value: 5.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695718478   15 YQHVNNARYLEFLEEARWDGLENSESFQwltahnIAFVVVNININYRRPAVLGDVLTVTSQVQQINGKSGVLSQVVTLDP 94
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGSQ------QVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDED 74


                  ....*
gi 695718478   95 EGQVV 99
Cdd:pfam03061  75 GRLVA 79
Acyl-ACP_TE pfam01643
Acyl-ACP thioesterase; This family consists of various acyl-acyl carrier protein (ACP) ...
 5-106 9.11e-09

Acyl-ACP thioesterase; This family consists of various acyl-acyl carrier protein (ACP) thioesterases (TE) these terminate fatty acyl group extension via hydrolysing an acyl group on a fatty acid.


Pssm-ID: 366738 [Multi-domain]  Cd Length: 248  Bit Score: 51.58  E-value: 9.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695718478    5 IKVRGFHLDVYQHVNNARYLEFLEEarwdglenSESFQWLTAHNIAfvvvNININYRRPAVLGDVLTVTSQVQQINGKSG 84
Cdd:pfam01643 159 YHVRYSDIDMNQHVNNVKYLEWILE--------VLPLDFLDTHEPK----KITLKYEKEVQYGDDIEIITESAGSEEGLK 226

                          90       100
                  ....*....|....*....|..
gi 695718478   85 VLsQVVTLDpEGQVVADALITF 106
Cdd:pfam01643 227 TL-HEIRNS-TGEEIAQARTDW 246
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 48-112 3.39e-08

Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 48.79  E-value: 3.39e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695718478  48 NIAFVVVNININYRRPAVLGDVLTVTSQVQQINGKSGVLSQVVTlDPEGQVVADALITFVCIDLK 112
Cdd:COG2050   74 GRRAVTIELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVT-DEDGKLVATATGTFAVLPKR 137
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 50-107 2.71e-05

PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several proteins responsible for phenylacetic acid (PA) degradation in bacteria. Although orthologs of PaaI exist in archaea and eukaryotes, their function has not been determined. Sequence similarity between PaaI, E. coli medium chain acyl-CoA thioesterase II, and human thioesterase III suggests they all belong to the same thioesterase superfamily. The conserved fold present in these thioesterases is referred to as an asymmetric hot dog fold, similar to those of 4-hydroxybenzoyl-CoA thioesterase (4HBT) and the beta-hydroxydecanoyl-ACP dehydratases (FabA/FabZ).


Pssm-ID: 239527 [Multi-domain]  Cd Length: 113  Bit Score: 40.62  E-value: 2.71e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 695718478  50 AFVVVNININYRRPAVLGDvLTVTSQVQQInGKSGVLSQVVTLDPEGQVVADALITFV 107
Cdd:cd03443   57 LAVTVDLNVNYLRPARGGD-LTARARVVKL-GRRLAVVEVEVTDEDGKLVATARGTFA 112
Acyl-ACP_TE pfam01643
Acyl-ACP thioesterase; This family consists of various acyl-acyl carrier protein (ACP) ...
 47-128 5.82e-05

Acyl-ACP thioesterase; This family consists of various acyl-acyl carrier protein (ACP) thioesterases (TE) these terminate fatty acyl group extension via hydrolysing an acyl group on a fatty acid.


Pssm-ID: 366738 [Multi-domain]  Cd Length: 248  Bit Score: 40.80  E-value: 5.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695718478   47 HNIAFVVVNININYRRPAVLGDVLTVTSQVQQINgKSGVLSQVVTLDPEGQVVADALITFVCIDLKTQKALPLEGELREK 126
Cdd:pfam01643  52 YNLVWVVYRYEIDIERLPEFGDMIEIETWASSYN-KFFCYRRFRVYDEKGEKIIEAKSTWVLMDRETRRPHRVPDEIRAP 130


                  ..
gi 695718478  127 LE 128
Cdd:pfam01643 131 YQ 132
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
40-107 5.18e-03

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 34.86  E-value: 5.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695718478  40 SFQWLTAHNIAFVVVNiNINYRRPAVLGDVLTVTSQVQQINGKSG---VLSQVVTLDPEGQVVADALITFV 107
Cdd:COG2030   66 LVDDLPGTAVANLGLQ-EVRFLRPVRVGDTLRARVEVLEKRESKSrgiVTLRTTVTNQDGEVVLTGEATVL 135
 
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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