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Conserved domains on  [gi|1119500261|ref|WP_072465581|]
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MULTISPECIES: MaoC/PaaZ C-terminal domain-containing protein [Burkholderia]

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
 11-280 3.56e-79

enoyl-CoA hydratase


The actual alignment was detected with superfamily member PLN02864:

Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 243.15  E-value: 3.56e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119500261  11 RFDDVVKSYSERDAILYALGIG-LGAEPENEQALAYVYGP----HLKVLPTYGAV--LGSPGFFATD-SSFGLDARRVLH 82
Cdd:PLN02864   17 KFPEVTYSYTERDVALYALGVGaCGRDAVDEDELKYVYHRdgqqFIKVLPTFASLfnLGSLDGFGLDlPGLNYDPSLLLH 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119500261  83 GEQHVILHSPIPACATVVAENRITRVIDKGdKGAVLHVERALREQGSGHLLSISEQVLVCRADGGFSTASEP-----SDA 157
Cdd:PLN02864   97 GQQYIEIYKPIPSSASVRNKVSIAGLHDKG-KAAILELETLSYEKDSGELLCMNRSTIFLRGAGGFSNSSQPfsysnYPT 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119500261 158 SPEPLPGAPLRDADFVIDLPTRPEAALIYRLSGDMNPLHADPRVAQAAGFPRPILHGLATFGVAVHAVLRACCDYDPTAL 237
Cdd:PLN02864  176 NQVSAVKIPKSQPDAVFEDQTQPSQALLYRLSGDYNPLHSDPMFAKVAGFTRPILHGLCTLGFAVRAVIKCFCNGDPTAV 255

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1119500261 238 HAMRARFSSPAFPGDTIRTEIWRAGTQLNIRATVPDRGVTVLS 280
Cdd:PLN02864  256 KTISGRFLLHVYPGETLVTEMWLEGLRVIYQTKVKERNKAVLS 298
 
Name Accession Description Interval E-value
PLN02864 PLN02864
enoyl-CoA hydratase
 11-280 3.56e-79

enoyl-CoA hydratase


Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 243.15  E-value: 3.56e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119500261  11 RFDDVVKSYSERDAILYALGIG-LGAEPENEQALAYVYGP----HLKVLPTYGAV--LGSPGFFATD-SSFGLDARRVLH 82
Cdd:PLN02864   17 KFPEVTYSYTERDVALYALGVGaCGRDAVDEDELKYVYHRdgqqFIKVLPTFASLfnLGSLDGFGLDlPGLNYDPSLLLH 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119500261  83 GEQHVILHSPIPACATVVAENRITRVIDKGdKGAVLHVERALREQGSGHLLSISEQVLVCRADGGFSTASEP-----SDA 157
Cdd:PLN02864   97 GQQYIEIYKPIPSSASVRNKVSIAGLHDKG-KAAILELETLSYEKDSGELLCMNRSTIFLRGAGGFSNSSQPfsysnYPT 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119500261 158 SPEPLPGAPLRDADFVIDLPTRPEAALIYRLSGDMNPLHADPRVAQAAGFPRPILHGLATFGVAVHAVLRACCDYDPTAL 237
Cdd:PLN02864  176 NQVSAVKIPKSQPDAVFEDQTQPSQALLYRLSGDYNPLHSDPMFAKVAGFTRPILHGLCTLGFAVRAVIKCFCNGDPTAV 255

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1119500261 238 HAMRARFSSPAFPGDTIRTEIWRAGTQLNIRATVPDRGVTVLS 280
Cdd:PLN02864  256 KTISGRFLLHVYPGETLVTEMWLEGLRVIYQTKVKERNKAVLS 298
HDE_HSD cd03448
HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), ...
 166-287 3.29e-64

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: 198.21  E-value: 3.29e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119500261 166 PLRDADFVIDLPTRPEAALIYRLSGDMNPLHADPRVAQAAGFPRPILHGLATFGVAVHAVLRACCDYDPTALHAMRARFS 245
Cdd:cd03448     1 PDRAPDAVVEIPTSPDQALLYRLSGDYNPLHIDPAFAKAAGFPRPILHGLCTYGFAARAVLEAFADGDPARFKAIKVRFS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1119500261 246 SPAFPGDTIRTEIWRAGTQLNIRATVPDRGVTVLSNGLFELT 287
Cdd:cd03448    81 SPVFPGETLRTEMWKEGNRVIFQTKVVERDVVVLSNGAALLA 122
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 160-262 7.77e-23

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: 91.25  E-value: 7.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119500261 160 EPLPGAPLrdaDFVIDLPTRPEAALIYRL-SGDMNPLHADPRVAQAAGFPRPILHGLATFGVAVHAVLRACCDYDPTALH 238
Cdd:pfam01575   3 QNAPGEPP---DTEKPRTVTEADIALFALvSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDNVIARFG 79

                          90       100
                  ....*....|....*....|....
gi 1119500261 239 AMRARFSSPAFPGDTIRTEIWRAG 262
Cdd:pfam01575  80 EIKVRFTKPVFPGDTLRTEAEVVG 103
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
187-257 3.75e-14

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 68.37  E-value: 3.75e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119500261 187 RLSGDMNPLHADPRVAQAAGFPRPILHGLATFGVAVHAVLRACCDYDPTALHAMRARFSSPAFPGDTIRTE 257
Cdd:COG2030    28 GATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAVANLGLQEVRFLRPVRVGDTLRAR 98
 
Name Accession Description Interval E-value
PLN02864 PLN02864
enoyl-CoA hydratase
 11-280 3.56e-79

enoyl-CoA hydratase


Pssm-ID: 178455 [Multi-domain]  Cd Length: 310  Bit Score: 243.15  E-value: 3.56e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119500261  11 RFDDVVKSYSERDAILYALGIG-LGAEPENEQALAYVYGP----HLKVLPTYGAV--LGSPGFFATD-SSFGLDARRVLH 82
Cdd:PLN02864   17 KFPEVTYSYTERDVALYALGVGaCGRDAVDEDELKYVYHRdgqqFIKVLPTFASLfnLGSLDGFGLDlPGLNYDPSLLLH 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119500261  83 GEQHVILHSPIPACATVVAENRITRVIDKGdKGAVLHVERALREQGSGHLLSISEQVLVCRADGGFSTASEP-----SDA 157
Cdd:PLN02864   97 GQQYIEIYKPIPSSASVRNKVSIAGLHDKG-KAAILELETLSYEKDSGELLCMNRSTIFLRGAGGFSNSSQPfsysnYPT 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119500261 158 SPEPLPGAPLRDADFVIDLPTRPEAALIYRLSGDMNPLHADPRVAQAAGFPRPILHGLATFGVAVHAVLRACCDYDPTAL 237
Cdd:PLN02864  176 NQVSAVKIPKSQPDAVFEDQTQPSQALLYRLSGDYNPLHSDPMFAKVAGFTRPILHGLCTLGFAVRAVIKCFCNGDPTAV 255

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1119500261 238 HAMRARFSSPAFPGDTIRTEIWRAGTQLNIRATVPDRGVTVLS 280
Cdd:PLN02864  256 KTISGRFLLHVYPGETLVTEMWLEGLRVIYQTKVKERNKAVLS 298
HDE_HSD cd03448
HDE_HSD The R-hydratase-like hot dog fold of the 17-beta-hydroxysteriod dehydrogenase (HSD), ...
 166-287 3.29e-64

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: 198.21  E-value: 3.29e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119500261 166 PLRDADFVIDLPTRPEAALIYRLSGDMNPLHADPRVAQAAGFPRPILHGLATFGVAVHAVLRACCDYDPTALHAMRARFS 245
Cdd:cd03448     1 PDRAPDAVVEIPTSPDQALLYRLSGDYNPLHIDPAFAKAAGFPRPILHGLCTYGFAARAVLEAFADGDPARFKAIKVRFS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1119500261 246 SPAFPGDTIRTEIWRAGTQLNIRATVPDRGVTVLSNGLFELT 287
Cdd:cd03448    81 SPVFPGETLRTEMWKEGNRVIFQTKVVERDVVVLSNGAALLA 122
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 168-262 2.03e-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: 93.10  E-value: 2.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119500261 168 RDADFVIDLPTRPEAALIYRLSGDMNPLHADPRVAQAAGFPRPILHGLATFGVAVHAVLRACCDYDPTALHAMRARFSSP 247
Cdd:cd03441     1 GELDSSGRTVTEADIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGLLVQWLPGTDGANLGSQSVRFLAP 80

                          90
                  ....*....|....*
gi 1119500261 248 AFPGDTIRTEIWRAG 262
Cdd:cd03441    81 VFPGDTLRVEVEVLG 95
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 160-262 7.77e-23

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: 91.25  E-value: 7.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119500261 160 EPLPGAPLrdaDFVIDLPTRPEAALIYRL-SGDMNPLHADPRVAQAAGFPRPILHGLATFGVAVHAVLRACCDYDPTALH 238
Cdd:pfam01575   3 QNAPGEPP---DTEKPRTVTEADIALFALvSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDNVIARFG 79

                          90       100
                  ....*....|....*....|....
gi 1119500261 239 AMRARFSSPAFPGDTIRTEIWRAG 262
Cdd:pfam01575  80 EIKVRFTKPVFPGDTLRTEAEVVG 103
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
187-257 3.75e-14

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 68.37  E-value: 3.75e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1119500261 187 RLSGDMNPLHADPRVAQAAGFPRPILHGLATFGVAVHAVLRACCDYDPTALHAMRARFSSPAFPGDTIRTE 257
Cdd:COG2030    28 GATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAVANLGLQEVRFLRPVRVGDTLRAR 98
FAS_MaoC cd03447
FAS_MaoC, the MaoC-like hot dog fold of the fatty acid synthase, beta subunit. Other enzymes ...
 170-280 3.87e-12

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: 62.30  E-value: 3.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119500261 170 ADFVIDLPTRPEAaliY-RLSGDMNPLHADPRVAQAAGFPRPILHGLATFGVAVHAVLRACCDYDPTALHAMRARFSSPA 248
Cdd:cd03447     5 ASLTITAPASNEP---YaRVSGDFNPIHVSRVFASYAGLPGTITHGMYTSAAVRALVETWAADNDRSRVRSFTASFVGMV 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1119500261 249 FPGDTIRTEIWRAGTQ-----LNIRATVPDRGVTVLS 280
Cdd:cd03447    82 LPNDELEVRLEHVGMVdgrkvIKVEARNEETGELVLR 118
SAV4209_like cd03453
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot ...
 189-254 9.05e-09

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: 52.71  E-value: 9.05e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1119500261 189 SGDMNPLHADPRVAQAAGFPRPILHGLATFGVAVhavlRACCDY--DPTALHAMRARFSSPAFPGDTI 254
Cdd:cd03453    24 SGDFNPIHYDEDFAKKVGLPGVIAHGMLTMGLLG----RLVTDWvgDPGRVVSFGVRFTKPVPVPDTL 87
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 188-294 1.09e-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: 50.00  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119500261 188 LSGDMNPLHADPRVAQAAGFPRPILHGLATFGVAVHAVLRAcCDYDPTALhAM----RARFSSPAFPGDTIRTEIWRAGT 263
Cdd:cd03446    29 LSGDWNPIHTDAEYAKKTRFGERIAHGLLTLSIATGLLQRL-GVFERTVV-AFygidNLRFLNPVFIGDTIRAEAEVVEK 106

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1119500261 264 QlniRATVPDRGVTVLsngLFELTTQGAEAL 294
Cdd:cd03446   107 E---EKDGEDAGVVTR---RIEVVNQRGEVV 131
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 188-258 2.49e-06

(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: 46.00  E-value: 2.49e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1119500261 188 LSGDMNPLHADPRVAQAAGFPRPILHGLATFGVaVHAVLRaccDYDP---TALHAMRARFSSPAFPGDTIRTEI 258
Cdd:cd03449    24 LSGDFNPIHLDEEYAKKTRFGGRIAHGMLTASL-ISAVLG---TLLPgpgTIYLSQSLRFLRPVFIGDTVTATV 93
PRK13693 PRK13693
(3R)-hydroxyacyl-ACP dehydratase subunit HadB; Provisional
 188-262 1.89e-05

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


Pssm-ID: 184249 [Multi-domain]  Cd Length: 142  Bit Score: 43.67  E-value: 1.89e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1119500261 188 LSGDMNPLHADPRVAQAAGFPRPILHGLATFGVAVHAVLRACCdyDPTALHAMRARFSSPAF-PGDTIRTEIWRAG 262
Cdd:PRK13693   33 VSGDLNPIHWDDEIAKVVGLDTAIAHGMLTMGLGGGYVTSWVG--DPGAVTEYNVRFTAVVPvPNDGKGAELVFNG 106
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 178-257 6.61e-05

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: 42.19  E-value: 6.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119500261 178 TRPEAALIYRLSGDMNPLHADPRVAQAAGFPRPILHGLATFGVAV-HAVlraccdYDpTALHAM------RARFSSPAFP 250
Cdd:cd03451    22 TEADNVLFTLLTMNTAPLHFDAAYAAKTEFGRRLVNSLFTLSLALgLSV------ND-TSLTAVanlgydEVRFPAPVFH 94


                  ....*..
gi 1119500261 251 GDTIRTE 257
Cdd:cd03451    95 GDTLYAE 101
SAV4209 cd03455
SAV4209 is a Streptomyces avermitilis protein with a hot dog fold that is similar to those of ...
 180-256 1.98e-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: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119500261 180 PEAALIYRLSG---DMNPLHADPRVAQAAGFPRPILHGLATFGVAVHAVLRacCDYDPTALHAMRARFSSPAFPGDTIRT 256
Cdd:cd03455    11 PDPTLLFRYSAatrDFHRIHHDRDYARAVGYPDLYVNGPTLAGLVIRYVTD--WAGPDARVKSFAFRLGAPLYAGDTLRF 88
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 200-259 3.11e-04

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: 39.38  E-value: 3.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1119500261 200 RVAQAAGFPRPILHGLATFGVAVHAVLRACCDYDP----TALHAMRARFSSPAFPGDTIRTEIW 259
Cdd:cd03440     6 TVTPEDIDGGGIVHGGLLLALADEAAGAAAARLGGrglgAVTLSLDVRFLRPVRPGDTLTVEAE 69
MaoC_dehydrat_N pfam13452
N-terminal half of MaoC dehydratase; It is clear from the structures of bacterial members of ...
 55-122 3.85e-04

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: 39.60  E-value: 3.85e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1119500261  55 PTYGAVLG--SPGFFATdssFGLDARRVLHGEQHVILHSPIPACATVVAENRITRVIDKGDKGAVLHVER 122
Cdd:pfam13452  51 PTFLFVLGwdAPGFMEQ---LGIDLSRLLHGEQRFTYHRPLRAGDELTCRSQIADVYDKKGNGALCFVVV 117
 
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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