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Conserved domains on  [gi|1850347667|gb|QKJ53863|]
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hydroxyphenylacetyl-CoA thioesterase PaaI [Klebsiella michiganensis]

Protein Classification

hydroxyphenylacetyl-CoA thioesterase PaaI( domain architecture ID 10798001)

hydroxyphenylacetyl-CoA thioesterase PaaI is an esterase with a preference for ring-hydroxylated phenylacetyl-CoA esters

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PaaD TIGR02286
phenylacetic acid degradation protein PaaD; This member of the domain family TIGR00369 (which ...
 19-132 3.99e-55

phenylacetic acid degradation protein PaaD; This member of the domain family TIGR00369 (which is, in turn, a member of the pfam03061 thioesterase superfamily) is nearly always found adjacent to other genes of the phenylacetic acid degradation pathway. Its function is currently unknown, but a role as a thioesterase is not inconsistent with the proposed overall pathway. Sequences scoring between trusted and noise include those from archaea and other species not known to catabolize phenylacetic acid and which are not adjacent to other genes potentially involved with such a pathway.


:

Pssm-ID: 131339  Cd Length: 114  Bit Score: 168.37  E-value: 3.99e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850347667  19 AKALGIEIIEMDQGYAQMTMAITPNMLNGHHTCHGGQLFSLADTAFAYACNSQGLAAVASAASIDFLRPAFVGELLTATA 98
Cdd:TIGR02286   1 AKALGIDILELGPGFARVAMTVRADMLNGHGTAHGGFLFSLADSAFAYACNSYGDAAVAAQCTIDFLRPGRAGERLEAEA 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1850347667  99 RVKHQGKLTGVYDIEIVNQQQKVVALFRGKSHRI 132
Cdd:TIGR02286  81 VEVSRGGRTGTYDVEVVNQEGELVALFRGTSRRL 114
 
Name Accession Description Interval E-value
PaaD TIGR02286
phenylacetic acid degradation protein PaaD; This member of the domain family TIGR00369 (which ...
 19-132 3.99e-55

phenylacetic acid degradation protein PaaD; This member of the domain family TIGR00369 (which is, in turn, a member of the pfam03061 thioesterase superfamily) is nearly always found adjacent to other genes of the phenylacetic acid degradation pathway. Its function is currently unknown, but a role as a thioesterase is not inconsistent with the proposed overall pathway. Sequences scoring between trusted and noise include those from archaea and other species not known to catabolize phenylacetic acid and which are not adjacent to other genes potentially involved with such a pathway.


Pssm-ID: 131339  Cd Length: 114  Bit Score: 168.37  E-value: 3.99e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850347667  19 AKALGIEIIEMDQGYAQMTMAITPNMLNGHHTCHGGQLFSLADTAFAYACNSQGLAAVASAASIDFLRPAFVGELLTATA 98
Cdd:TIGR02286   1 AKALGIDILELGPGFARVAMTVRADMLNGHGTAHGGFLFSLADSAFAYACNSYGDAAVAAQCTIDFLRPGRAGERLEAEA 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1850347667  99 RVKHQGKLTGVYDIEIVNQQQKVVALFRGKSHRI 132
Cdd:TIGR02286  81 VEVSRGGRTGTYDVEVVNQEGELVALFRGTSRRL 114
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 1-134 4.14e-37

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 123.51  E-value: 4.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850347667   1 MSnEAWQNARAMYENDNCAKALGIEIIEMDQGYAQMTMAITPNMLNGHHTCHGGQLFSLADTAFAYACNSQ---GLAAVA 77
Cdd:COG2050     1 MS-DPLERLEGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAlppGRRAVT 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1850347667  78 SAASIDFLRPAFVGELLTATARVKHQGKLTGVYDIEIVNQQQKVVALFRGKSHRIGG 134
Cdd:COG2050    80 IELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPK 136
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 21-127 5.50e-31

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: 106.87  E-value: 5.50e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850347667  21 ALGIEIIEMDQGYAQMTMAITPNMLNGHHTCHGGQLFSLADTAFAYACNSQ---GLAAVASAASIDFLRPAFVGElLTAT 97
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSAlppGALAVTVDLNVNYLRPARGGD-LTAR 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1850347667  98 ARVKHQGKLTGVYDIEIVNQQQKVVALFRG 127
Cdd:cd03443    80 ARVVKLGRRLAVVEVEVTDEDGKLVATARG 109
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 48-123 6.38e-20

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: 77.68  E-value: 6.38e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1850347667  48 HHTCHGGQLFSLADTAFAYACNSQGL---AAVASAASIDFLRPAFVGELLTATARVKHQGKLTGVYDIEIVNQQQKVVA 123
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGsqqVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
PRK04424 PRK04424
transcription factor FapR;
25-128 3.98e-07

transcription factor FapR;


Pssm-ID: 179847 [Multi-domain]  Cd Length: 185  Bit Score: 46.74  E-value: 3.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850347667  25 EIIEMDQG-YAQMTMAITPNML-------NGHHtchggqLFSLAdtafayacNSQGLA------AVASAASIDFLRPAFV 90
Cdd:PRK04424   76 ELIDLELGrSAISILEITEEMVfsktgiaRGHH------LFAQA--------NSLAVAvidaelALTGVANIRFKRPVKL 141

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1850347667  91 GELLTATARVKHQGKltGVYDIEIVNQ-QQKVValFRGK 128
Cdd:PRK04424  142 GERVVAKAEVVRKKG--NKYIVEVKSYvGDELV--FRGK 176
 
Name Accession Description Interval E-value
PaaD TIGR02286
phenylacetic acid degradation protein PaaD; This member of the domain family TIGR00369 (which ...
 19-132 3.99e-55

phenylacetic acid degradation protein PaaD; This member of the domain family TIGR00369 (which is, in turn, a member of the pfam03061 thioesterase superfamily) is nearly always found adjacent to other genes of the phenylacetic acid degradation pathway. Its function is currently unknown, but a role as a thioesterase is not inconsistent with the proposed overall pathway. Sequences scoring between trusted and noise include those from archaea and other species not known to catabolize phenylacetic acid and which are not adjacent to other genes potentially involved with such a pathway.


Pssm-ID: 131339  Cd Length: 114  Bit Score: 168.37  E-value: 3.99e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850347667  19 AKALGIEIIEMDQGYAQMTMAITPNMLNGHHTCHGGQLFSLADTAFAYACNSQGLAAVASAASIDFLRPAFVGELLTATA 98
Cdd:TIGR02286   1 AKALGIDILELGPGFARVAMTVRADMLNGHGTAHGGFLFSLADSAFAYACNSYGDAAVAAQCTIDFLRPGRAGERLEAEA 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1850347667  99 RVKHQGKLTGVYDIEIVNQQQKVVALFRGKSHRI 132
Cdd:TIGR02286  81 VEVSRGGRTGTYDVEVVNQEGELVALFRGTSRRL 114
unchar_dom_1 TIGR00369
uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a ...
 17-131 1.61e-38

uncharacterized domain 1; Most proteins containing this domain consist almost entirely of a single copy of this domain. A protein from C. elegans consists of two tandem copies of the domain. The domain is also found as the N-terminal region of an apparent initiation factor eIF-2B alpha subunit of Aquifex aeolicus. The function of the domain is unknown.


Pssm-ID: 161843 [Multi-domain]  Cd Length: 117  Bit Score: 126.31  E-value: 1.61e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850347667  17 NCAKALGIEIIEMDQGYAQMTMAITPNMLNGHHTCHGGQLFSLADTAFA---YACNSQGLAAVASAASIDFLRPAFVGEl 93
Cdd:TIGR00369   1 PLVSFLGIEIEELGDGFLEATMPVDERTLQPFGSLHGGVSAALADTAGSaagYLCNSGGQAVVGLELNANHLRPAREGK- 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1850347667  94 LTATARVKHQGKLTGVYDIEIVNQQQKVVALFRGKSHR 131
Cdd:TIGR00369  80 VRAIAQVVHLGRQTGVAEIEIVDEQGRLCALSRGTTAV 117
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 1-134 4.14e-37

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 123.51  E-value: 4.14e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850347667   1 MSnEAWQNARAMYENDNCAKALGIEIIEMDQGYAQMTMAITPNMLNGHHTCHGGQLFSLADTAFAYACNSQ---GLAAVA 77
Cdd:COG2050     1 MS-DPLERLEGFLAANPFAELLGIELVEVEPGRAVLRLPVRPEHLNPPGTVHGGALAALADSAAGLAANSAlppGRRAVT 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1850347667  78 SAASIDFLRPAFVGELLTATARVKHQGKLTGVYDIEIVNQQQKVVALFRGKSHRIGG 134
Cdd:COG2050    80 IELNINFLRPARLGDRLTAEARVVRRGRRLAVVEVEVTDEDGKLVATATGTFAVLPK 136
PaaI_thioesterase cd03443
PaaI_thioesterase is a tetrameric acyl-CoA thioesterase with a hot dog fold and one of several ...
 21-127 5.50e-31

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: 106.87  E-value: 5.50e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850347667  21 ALGIEIIEMDQGYAQMTMAITPNMLNGHHTCHGGQLFSLADTAFAYACNSQ---GLAAVASAASIDFLRPAFVGElLTAT 97
Cdd:cd03443     1 LLGIRVVEVGPGRVVLRLPVRPRHLNPGGIVHGGAIATLADTAGGLAALSAlppGALAVTVDLNVNYLRPARGGD-LTAR 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1850347667  98 ARVKHQGKLTGVYDIEIVNQQQKVVALFRG 127
Cdd:cd03443    80 ARVVKLGRRLAVVEVEVTDEDGKLVATARG 109
4HBT pfam03061
Thioesterase superfamily; This family contains a wide variety of enzymes, principally ...
 48-123 6.38e-20

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: 77.68  E-value: 6.38e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1850347667  48 HHTCHGGQLFSLADTAFAYACNSQGL---AAVASAASIDFLRPAFVGELLTATARVKHQGKLTGVYDIEIVNQQQKVVA 123
Cdd:pfam03061   1 GGVVHGGVYLALADEAAGAAARRLGGsqqVVVVVELSIDFLRPARLGDRLTVEARVVRLGRTSAVVEVEVRDEDGRLVA 79
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 36-127 2.90e-17

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: 71.74  E-value: 2.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850347667  36 MTMAITPNMLNGHHTCHGGQLFSLADTAFAYACNS---QGLAAVASAASIDFLRPAFVGELLTATARVKHQGKLTGVYDI 112
Cdd:cd03440     3 LRLTVTPEDIDGGGIVHGGLLLALADEAAGAAAARlggRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEV 82

                          90
                  ....*....|....*
gi 1850347667 113 EIVNQQQKVVALFRG 127
Cdd:cd03440    83 EVRNEDGKLVATATA 97
YciA COG1607
Acyl-CoA hydrolase [Lipid transport and metabolism];
28-105 5.12e-13

Acyl-CoA hydrolase [Lipid transport and metabolism];


Pssm-ID: 441215 [Multi-domain]  Cd Length: 146  Bit Score: 61.73  E-value: 5.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850347667  28 EMDQGYAQMTMAITPNMLNGHHTCHGGQLFSLAD-TAFAYACN-SQGLAAVASAASIDFLRPAFVGELLTATARVKHQGK 105
Cdd:COG1607     1 PLPDSELTLRELVMPEDTNHHGTLFGGWLLSWMDeAAAIAAARhARGRVVTASVDSVDFLRPVRVGDIVELYARVVRVGR 80
BFIT_BACH cd03442
Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes ...
 27-105 1.17e-10

Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy.


Pssm-ID: 239526 [Multi-domain]  Cd Length: 123  Bit Score: 55.27  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850347667  27 IEMDQGYAQMTMAITPNMLNGHHTCHGGQLFSLAD-TAFAYACN-SQGLAAVASAASIDFLRPAFVGELLTATARVKHQG 104
Cdd:cd03442     1 VPMEDTELSTRELVLPEDTNHHGTIFGGWLLEWMDeLAGIAAYRhAGGRVVTASVDRIDFLKPVRVGDVVELSARVVYTG 80


                  .
gi 1850347667 105 K 105
Cdd:cd03442    81 R 81
PRK04424 PRK04424
transcription factor FapR;
25-128 3.98e-07

transcription factor FapR;


Pssm-ID: 179847 [Multi-domain]  Cd Length: 185  Bit Score: 46.74  E-value: 3.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850347667  25 EIIEMDQG-YAQMTMAITPNML-------NGHHtchggqLFSLAdtafayacNSQGLA------AVASAASIDFLRPAFV 90
Cdd:PRK04424   76 ELIDLELGrSAISILEITEEMVfsktgiaRGHH------LFAQA--------NSLAVAvidaelALTGVANIRFKRPVKL 141

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1850347667  91 GELLTATARVKHQGKltGVYDIEIVNQ-QQKVValFRGK 128
Cdd:PRK04424  142 GERVVAKAEVVRKKG--NKYIVEVKSYvGDELV--FRGK 176
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
52-126 2.94e-05

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 41.02  E-value: 2.94e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1850347667  52 HGGQLFSLADTAFAYACNSQGLAAVASAaSIDFLRPAFVGELLTATARVK----HQGKLTGVYDIEIVNQQQKVVALFR 126
Cdd:COG2030    54 HGMLTLSLASGLLVDDLPGTAVANLGLQ-EVRFLRPVRVGDTLRARVEVLekreSKSRGIVTLRTTVTNQDGEVVLTGE 131
4HBT cd00586
4-hydroxybenzoyl-CoA thioesterase (4HBT). Catalyzes the final step in the 4-chlorobenzoate ...
 70-123 6.57e-05

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: 39.51  E-value: 6.57e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1850347667  70 SQGLAAVASAASIDFLRPAFVGELLTATARVKHQGKLTGVYDIEIVNQQQKVVA 123
Cdd:cd00586    47 EQGLGLVVVELEIDYLRPLRLGDRLTVETRVLRLGRKSFTFEQEIFREDGELLA 100
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 52-126 1.51e-04

(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: 38.78  E-value: 1.51e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1850347667  52 HGGQLFSLAdTAFAYACNSQGLAAVASAASIDFLRPAFVGELLTATARVK----HQGKLTGVYDIEIVNQQQKVVALFR 126
Cdd:cd03441    46 HGMLTLSLA-SGLLVQWLPGTDGANLGSQSVRFLAPVFPGDTLRVEVEVLgkrpSKGRGVVTVRTEARNQGGEVVLSGE 123
FadM COG0824
Acyl-CoA thioesterase FadM [Lipid transport and metabolism]; Acyl-CoA thioesterase FadM is ...
 71-123 4.75e-04

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: 37.96  E-value: 4.75e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1850347667  71 QGLAAVASAASIDFLRPAFVGELLTATARVKHQGKLTGVYDIEIVNQQ-QKVVA 123
Cdd:COG0824    53 EGIGLVVVEAEIDYLRPARYGDELTVETRVVRLGGSSLTFEYEIFRADdGELLA 106
DUF4442 pfam14539
Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea ...
 18-100 1.51e-03

Domain of unknown function (DUF4442); This family of proteins is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 139 and 165 amino acids in length. There is a conserved PYF sequence motif. There is a single completely conserved residue N that may be functionally important.


Pssm-ID: 434027  Cd Length: 131  Bit Score: 36.47  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850347667  18 CAKA-----LGIEIIEMDQGYAQMTMAITPNMLNGHHTCHGGQLFSLADTAFayacnsqGLAAVAS----------AASI 82
Cdd:pfam14539   9 CRKApyfgtIGPRITELRPGRCEVRLPKRRRVRNHIGTVHAIAICNLAELAM-------GLMAEASlpdthrwipkGMTV 81

                          90
                  ....*....|....*...
gi 1850347667  83 DFLRPAFVGelLTATARV 100
Cdd:pfam14539  82 DYLAKATGD--LTAVAEL 97
TIGR00051 TIGR00051
acyl-CoA thioester hydrolase, YbgC/YbaW family; This model describes a subset of related ...
 71-122 1.52e-03

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: 36.24  E-value: 1.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1850347667  71 QGLAAVASAASIDFLRPAFVGELLTATARVKHQGKLTGVYDIEIVNQQQKVV 122
Cdd:TIGR00051  45 EGVAFVVVNINIEYKKPARLDDVLEIRTQIEELNGFSFVFSQEIFNEDEALL 96
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 72-122 2.03e-03

(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: 35.98  E-value: 2.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1850347667  72 GLAAVASAASIDFLRPAFVGELLTATARV--KHQGKLTGVYDIEIVNQQQKVV 122
Cdd:cd03449    67 GPGTIYLSQSLRFLRPVFIGDTVTATVTVteKREDKKRVTLETVCTNQNGEVV 119
PS-DH pfam14765
Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. ...
 55-127 7.45e-03

Polyketide synthase dehydratase; This is the dehydratase domain of polyketide synthases. Structural analysis shows these DH domains are double hotdogs in which the active site contains a histidine from the N-terminal hotdog and an aspartate from the C-terminal hotdog. Studies have uncovered that a substrate tunnel formed between the DH domains may be essential for loading substrates and unloading products.


Pssm-ID: 434191  Cd Length: 296  Bit Score: 35.04  E-value: 7.45e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1850347667  55 QLFSLADTAFAyaCNSQGLAAVASAASIDFLRPAFVGELLTATARVKHQGKLTGVYDIEIVNQQQKVVALFRG 127
Cdd:pfam14765 213 QLLGAALPAEA--EHADQAYLPVGIERLRIYRSLPPGEPLWVHARLERRGGRTIVGDLTLVDEDGRVVARIEG 283
 
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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