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Conserved domains on  [gi|625113118|gb|KCA64047|]
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3-hydroxyacyl-thioester dehydratase HtdY [Mycobacterium tuberculosis TKK-01-0081]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02864 super family cl28571
enoyl-CoA hydratase
 2-268 5.41e-57

enoyl-CoA hydratase


The actual alignment was detected with superfamily member PLN02864:

Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 185.37  E-value: 5.41e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625113118   2 AIDPNSIGAVTEP-MLFEWTDRDTLLYAIGVGAGTGDLAFTTENS---HGIDQ---QVLPTYAVICcpAFGAAAKVGT-- 72
Cdd:PLN02864   7 PFDPDLVLAHKFPeVTYSYTERDVALYALGVGACGRDAVDEDELKyvyHRDGQqfiKVLPTFASLF--NLGSLDGFGLdl 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625113118  73 ----FNPAALLHGSQGIRLHAPLPAAGKLSVVTEVADIQDKGegKNAIVVLRGRGCDPESGSLVAETLTTLVLRGQGGFG 148
Cdd:PLN02864  85 pglnYDPSLLLHGQQYIEIYKPIPSSASVRNKVSIAGLHDKG--KAAILELETLSYEKDSGELLCMNRSTIFLRGAGGFS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625113118 149 GArgERP-----------AAPEFPDRHPDARIDMPTREDQALIYRLSGDRNPLHSDPWFAtQLAGFPKPILHGLCTYGVA 217
Cdd:PLN02864 163 NS--SQPfsysnyptnqvSAVKIPKSQPDAVFEDQTQPSQALLYRLSGDYNPLHSDPMFA-KVAGFTRPILHGLCTLGFA 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 625113118 218 GRALVAELGGGVAANITSIAARFTKPVFPGETLSTVIWRtEPGRAVFRTEV 268
Cdd:PLN02864 240 VRAVIKCFCNGDPTAVKTISGRFLLHVYPGETLVTEMWL-EGLRVIYQTKV 289
 
Name Accession Description Interval E-value
PLN02864 PLN02864
enoyl-CoA hydratase
 2-268 5.41e-57

enoyl-CoA hydratase


Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 185.37  E-value: 5.41e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625113118   2 AIDPNSIGAVTEP-MLFEWTDRDTLLYAIGVGAGTGDLAFTTENS---HGIDQ---QVLPTYAVICcpAFGAAAKVGT-- 72
Cdd:PLN02864   7 PFDPDLVLAHKFPeVTYSYTERDVALYALGVGACGRDAVDEDELKyvyHRDGQqfiKVLPTFASLF--NLGSLDGFGLdl 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625113118  73 ----FNPAALLHGSQGIRLHAPLPAAGKLSVVTEVADIQDKGegKNAIVVLRGRGCDPESGSLVAETLTTLVLRGQGGFG 148
Cdd:PLN02864  85 pglnYDPSLLLHGQQYIEIYKPIPSSASVRNKVSIAGLHDKG--KAAILELETLSYEKDSGELLCMNRSTIFLRGAGGFS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625113118 149 GArgERP-----------AAPEFPDRHPDARIDMPTREDQALIYRLSGDRNPLHSDPWFAtQLAGFPKPILHGLCTYGVA 217
Cdd:PLN02864 163 NS--SQPfsysnyptnqvSAVKIPKSQPDAVFEDQTQPSQALLYRLSGDYNPLHSDPMFA-KVAGFTRPILHGLCTLGFA 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 625113118 218 GRALVAELGGGVAANITSIAARFTKPVFPGETLSTVIWRtEPGRAVFRTEV 268
Cdd:PLN02864 240 VRAVIKCFCNGDPTAVKTISGRFLLHVYPGETLVTEMWL-EGLRVIYQTKV 289
HDE_HSD cd03448
HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), ...
 161-286 6.77e-55

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: 173.56  E-value: 6.77e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625113118 161 PDRHPDARIDMPTREDQALIYRLSGDRNPLHSDPWFAtQLAGFPKPILHGLCTYGVAGRALVAELGGGVAANITSIAARF 240
Cdd:cd03448    1 PDRAPDAVVEIPTSPDQALLYRLSGDYNPLHIDPAFA-KAAGFPRPILHGLCTYGFAARAVLEAFADGDPARFKAIKVRF 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 625113118 241 TKPVFPGETLSTVIWRtEPGRAVFRTEVAGSDgaeaRVVLDDGAVE 286
Cdd:cd03448   80 SSPVFPGETLRTEMWK-EGNRVIFQTKVVERD----VVVLSNGAAL 120
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 161-266 8.24e-35

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: 122.06  E-value: 8.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625113118  161 PDRHPDARIDMPTREDQALIYRL-SGDRNPLHSDPWFAtQLAGFPKPILHGLCTYGVAGRALVAELGGGVAANITSIAAR 239
Cdd:pfam01575   6 PGEPPDTEKPRTVTEADIALFALvSGDHNPIHVDPEFA-KKAGFGGPIAHGMLTLAIVAGLVEEWGGDNVIARFGEIKVR 84

                          90       100
                  ....*....|....*....|....*..
gi 625113118  240 FTKPVFPGETLSTVIWRTEPgRAVFRT 266
Cdd:pfam01575  85 FTKPVFPGDTLRTEAEVVGK-RDGRQT 110
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
173-280 5.05e-19

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 81.09  E-value: 5.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625113118 173 TREDQALIYRLSGDRNPLHSDPWFAtQLAGFPKPILHGLCTYGVAGRALVAELGGGVAANITSIAARFTKPVFPGETLST 252
Cdd:COG2030   19 TEEDIVLFAGATGDPNPIHLDEEAA-AATGFGGRIAHGMLTLSLASGLLVDDLPGTAVANLGLQEVRFLRPVRVGDTLRA 97

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 625113118 253 VIWRTE------PGRAVFRTEVAGSDG-----AEARVVL 280
Cdd:COG2030   98 RVEVLEkresksRGIVTLRTTVTNQDGevvltGEATVLV 136
 
Name Accession Description Interval E-value
PLN02864 PLN02864
enoyl-CoA hydratase
 2-268 5.41e-57

enoyl-CoA hydratase


Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 185.37  E-value: 5.41e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625113118   2 AIDPNSIGAVTEP-MLFEWTDRDTLLYAIGVGAGTGDLAFTTENS---HGIDQ---QVLPTYAVICcpAFGAAAKVGT-- 72
Cdd:PLN02864   7 PFDPDLVLAHKFPeVTYSYTERDVALYALGVGACGRDAVDEDELKyvyHRDGQqfiKVLPTFASLF--NLGSLDGFGLdl 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625113118  73 ----FNPAALLHGSQGIRLHAPLPAAGKLSVVTEVADIQDKGegKNAIVVLRGRGCDPESGSLVAETLTTLVLRGQGGFG 148
Cdd:PLN02864  85 pglnYDPSLLLHGQQYIEIYKPIPSSASVRNKVSIAGLHDKG--KAAILELETLSYEKDSGELLCMNRSTIFLRGAGGFS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625113118 149 GArgERP-----------AAPEFPDRHPDARIDMPTREDQALIYRLSGDRNPLHSDPWFAtQLAGFPKPILHGLCTYGVA 217
Cdd:PLN02864 163 NS--SQPfsysnyptnqvSAVKIPKSQPDAVFEDQTQPSQALLYRLSGDYNPLHSDPMFA-KVAGFTRPILHGLCTLGFA 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 625113118 218 GRALVAELGGGVAANITSIAARFTKPVFPGETLSTVIWRtEPGRAVFRTEV 268
Cdd:PLN02864 240 VRAVIKCFCNGDPTAVKTISGRFLLHVYPGETLVTEMWL-EGLRVIYQTKV 289
HDE_HSD cd03448
HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), ...
 161-286 6.77e-55

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: 173.56  E-value: 6.77e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625113118 161 PDRHPDARIDMPTREDQALIYRLSGDRNPLHSDPWFAtQLAGFPKPILHGLCTYGVAGRALVAELGGGVAANITSIAARF 240
Cdd:cd03448    1 PDRAPDAVVEIPTSPDQALLYRLSGDYNPLHIDPAFA-KAAGFPRPILHGLCTYGFAARAVLEAFADGDPARFKAIKVRF 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 625113118 241 TKPVFPGETLSTVIWRtEPGRAVFRTEVAGSDgaeaRVVLDDGAVE 286
Cdd:cd03448   80 SSPVFPGETLRTEMWK-EGNRVIFQTKVVERD----VVVLSNGAAL 120
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 161-266 8.24e-35

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: 122.06  E-value: 8.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625113118  161 PDRHPDARIDMPTREDQALIYRL-SGDRNPLHSDPWFAtQLAGFPKPILHGLCTYGVAGRALVAELGGGVAANITSIAAR 239
Cdd:pfam01575   6 PGEPPDTEKPRTVTEADIALFALvSGDHNPIHVDPEFA-KKAGFGGPIAHGMLTLAIVAGLVEEWGGDNVIARFGEIKVR 84

                          90       100
                  ....*....|....*....|....*..
gi 625113118  240 FTKPVFPGETLSTVIWRTEPgRAVFRT 266
Cdd:pfam01575  85 FTKPVFPGDTLRTEAEVVGK-RDGRQT 110
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 163-268 1.23e-26

(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: 101.19  E-value: 1.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625113118 163 RHPDARIDMPTREDQALIYRLSGDRNPLHSDPWFATQlAGFPKPILHGLCTYGVAGRALVAELGGGVAANITSIAARFTK 242
Cdd:cd03441    1 GELDSSGRTVTEADIALFARLSGDPNPIHVDPEYAKA-AGFGGRIAHGMLTLSLASGLLVQWLPGTDGANLGSQSVRFLA 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 625113118 243 PVFPGETLSTVIWRTE------PGRAVFRTEV 268
Cdd:cd03441   80 PVFPGDTLRVEVEVLGkrpskgRGVVTVRTEA 111
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
173-280 5.05e-19

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 81.09  E-value: 5.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625113118 173 TREDQALIYRLSGDRNPLHSDPWFAtQLAGFPKPILHGLCTYGVAGRALVAELGGGVAANITSIAARFTKPVFPGETLST 252
Cdd:COG2030   19 TEEDIVLFAGATGDPNPIHLDEEAA-AATGFGGRIAHGMLTLSLASGLLVDDLPGTAVANLGLQEVRFLRPVRVGDTLRA 97

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 625113118 253 VIWRTE------PGRAVFRTEVAGSDG-----AEARVVL 280
Cdd:COG2030   98 RVEVLEkresksRGIVTLRTTVTNQDGevvltGEATVLV 136
FAS_MaoC cd03447
FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes ...
 182-286 8.53e-13

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: 63.84  E-value: 8.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625113118 182 RLSGDRNPLHSDPWFAtQLAGFPKPILHGLCTYGVAGRALVAELGGGVAANITSIAARFTKPVFPGETLSTVIWRT--EP 259
Cdd:cd03447   20 RVSGDFNPIHVSRVFA-SYAGLPGTITHGMYTSAAVRALVETWAADNDRSRVRSFTASFVGMVLPNDELEVRLEHVgmVD 98

                         90       100
                 ....*....|....*....|....*..
gi 625113118 260 GRAVFRTEvAGSDGAEARVVLDDGAVE 286
Cdd:cd03447   99 GRKVIKVE-ARNEETGELVLRGEAEVE 124
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 173-281 2.99e-12

(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: 62.56  E-value: 2.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625113118 173 TREDQALIYRLSGDRNPLHSDPWFATQlAGFPKPILHGLCTYGVAGRALVAELGGG--VAANITSiaaRFTKPVFPGETL 250
Cdd:cd03449   14 TEEDVELFAELSGDFNPIHLDEEYAKK-TRFGGRIAHGMLTASLISAVLGTLLPGPgtIYLSQSL---RFLRPVFIGDTV 89

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 625113118 251 sTVIW-----RTEPGRAVFRTEVAGSDGaeaRVVLD 281
Cdd:cd03449   90 -TATVtvtekREDKKRVTLETVCTNQNG---EVVIE 121
SAV4209_like cd03453
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot ...
 173-286 1.31e-11

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: 60.80  E-value: 1.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625113118 173 TREDQALIYRLSGDRNPLHSDPWFAtQLAGFPKPILHGLCTYGVAGRALVAELGGGVAanITSIAARFTKPVFPGETLST 252
Cdd:cd03453   13 SRADLVRYAGASGDFNPIHYDEDFA-KKVGLPGVIAHGMLTMGLLGRLVTDWVGDPGR--VVSFGVRFTKPVPVPDTLTC 89

                         90       100       110
                 ....*....|....*....|....*....|....
gi 625113118 253 ViwrtepGRAVFRTEVAGSDGAEARVVLDDGAVE 286
Cdd:cd03453   90 T------GIVVEKTVADGEDALTVTVDATDQAGG 117
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 163-282 1.17e-07

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: 49.90  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625113118 163 RHPDARidMPTREDQALIYRLSGDRNPLHSDPWFATQLaGFPKPILHGLCTYGVAGRALVAELGGGVAAN--ITSIaaRF 240
Cdd:cd03451   14 EHAPGR--TVTEADNVLFTLLTMNTAPLHFDAAYAAKT-EFGRRLVNSLFTLSLALGLSVNDTSLTAVANlgYDEV--RF 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 625113118 241 TKPVFPGETL---STVI------WRTEPGRAVFRTEVAGSDGaeaRVVLDD 282
Cdd:cd03451   89 PAPVFHGDTLyaeSEVLskreskSRPDAGIVTVRTVGYNQDG---EPVLSF 136
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 183-273 5.39e-07

MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but without the N-terminal PutA domain. This protein family has a hot-dog fold similar to that of (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.


Pssm-ID: 239530 [Multi-domain]  Cd Length: 140  Bit Score: 48.07  E-value: 5.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625113118 183 LSGDRNPLHSDPWFATQlAGFPKPILHGLCTYGVAgRALVAELGGgvaANITSIA------ARFTKPVFPGETL--STVI 254
Cdd:cd03446   29 LSGDWNPIHTDAEYAKK-TRFGERIAHGLLTLSIA-TGLLQRLGV---FERTVVAfygidnLRFLNPVFIGDTIraEAEV 103

                         90       100
                 ....*....|....*....|....*
gi 625113118 255 WRTEP------GRAVFRTEVAGSDG 273
Cdd:cd03446  104 VEKEEkdgedaGVVTRRIEVVNQRG 128
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 203-279 1.58e-05

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: 42.85  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625113118 203 FPKPILHGLCTYG----VAGRALVAELGGGVAANITSIAARFTKPVFPGETLSTVIWRTEPGRAVFRTEVAGSDGAEARV 278
Cdd:cd03440   13 DGGGIVHGGLLLAladeAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSSVTVEVEVRNEDGKLV 92


                 .
gi 625113118 279 V 279
Cdd:cd03440   93 A 93
SAV4209 cd03455
SAV4209 is a Streptomyces avermitilis protein with a hot dog fold that is similar to those of ...
 176-252 1.72e-04

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: 40.38  E-value: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625113118 176 DQALIYRLSG---DRNPLHSDPWFATQLaGFPKPILHGLCTYGVAGRALVAELGGGvaANITSIAARFTKPVFPGETLST 252
Cdd:cd03455   12 DPTLLFRYSAatrDFHRIHHDRDYARAV-GYPDLYVNGPTLAGLVIRYVTDWAGPD--ARVKSFAFRLGAPLYAGDTLRF 88
PRK13693 PRK13693
(3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional
 173-244 2.32e-04

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


Pssm-ID: 184249 [Multi-domain]  Cd Length: 142  Bit Score: 40.59  E-value: 2.32e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 625113118 173 TREDQALIYRLSGDRNPLHSDPWFAtQLAGFPKPILHGLCTYGVAGRALVAELGGGVAanITSIAARFTKPV 244
Cdd:PRK13693  23 TRQDLVNYAGVSGDLNPIHWDDEIA-KVVGLDTAIAHGMLTMGLGGGYVTSWVGDPGA--VTEYNVRFTAVV 91
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 173-279 1.50e-03

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 39.86  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 625113118 173 TREDQALIYRLSGDRNPLHSDPWFATQlAGFPKPILHGLCtygvaGRALVAELGG----GVAANITSIAARFTKPVFPGE 248
Cdd:PRK08190  27 TPDDIELFAAMSGDVNPAHLDAAYAAS-DGFHHVVAHGMW-----GGALISAVLGtrlpGPGTIYLGQSLRFRRPVRIGD 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 625113118 249 TLS---TVIW-RTEPGRAVFRTEVAGSDGA-----EARVV 279
Cdd:PRK08190 101 TLTvtvTVREkDPEKRIVVLDCRCTNQDGEvvitgTAEVI 140
 
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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