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Conserved domains on  [gi|493593220|ref|WP_006546024|]
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MaoC family dehydratase [Parafrankia sp. EUN1f]

Protein Classification

MaoC family dehydratase( domain architecture ID 10130985)

MaoC family dehydratase similar to Rhodobacter sphaeroides mesaconyl-CoA hydratase, also called 2-methylfumaryl-CoA hydratase, which catalyzes the reversible hydration of mesaconyl-CoA to form beta-methylmalyl-CoA in the ethylmalonyl-CoA pathway for acetate assimilation

CATH:  3.10.129.10
Gene Ontology:  GO:0016829
PubMed:  15307895

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 4-149 1.45e-73

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: 217.46  E-value: 1.45e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493593220   4 GRYYEEFEVGAVYKHWPGKTVTEYDDHLFCLLTMNHHPLHLDANYAEKTTqFKRNVVVGNYVYSLLLGMSVADVSGKAIA 83
Cdd:cd03451    1 GLYFEDFTVGQVFEHAPGRTVTEADNVLFTLLTMNTAPLHFDAAYAAKTE-FGRRLVNSLFTLSLALGLSVNDTSLTAVA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493593220  84 NLEVESLRHVAPVFHGDTIYGESTVLDKVESKSKDDRGIVTVETRGLNQDGTLVCIYRRKVMVPKR 149
Cdd:cd03451   80 NLGYDEVRFPAPVFHGDTLYAESEVLSKRESKSRPDAGIVTVRTVGYNQDGEPVLSFERTALVPKR 145
 
Name Accession Description Interval E-value
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 4-149 1.45e-73

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: 217.46  E-value: 1.45e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493593220   4 GRYYEEFEVGAVYKHWPGKTVTEYDDHLFCLLTMNHHPLHLDANYAEKTTqFKRNVVVGNYVYSLLLGMSVADVSGKAIA 83
Cdd:cd03451    1 GLYFEDFTVGQVFEHAPGRTVTEADNVLFTLLTMNTAPLHFDAAYAAKTE-FGRRLVNSLFTLSLALGLSVNDTSLTAVA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493593220  84 NLEVESLRHVAPVFHGDTIYGESTVLDKVESKSKDDRGIVTVETRGLNQDGTLVCIYRRKVMVPKR 149
Cdd:cd03451   80 NLGYDEVRFPAPVFHGDTLYAESEVLSKRESKSRPDAGIVTVRTVGYNQDGEPVLSFERTALVPKR 145
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
6-150 5.42e-49

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 154.66  E-value: 5.42e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493593220   6 YYEEFEVGAVYKHwPGKTVTEYDDHLFCLLTMNHHPLHLDANYAeKTTQFKRNVVVGNYVYSLLLGMSVADVSGKAIANL 85
Cdd:COG2030    1 YFEDLEVGDVLPH-GGRTVTEEDIVLFAGATGDPNPIHLDEEAA-AATGFGGRIAHGMLTLSLASGLLVDDLPGTAVANL 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493593220  86 EVESLRHVAPVFHGDTIYGESTVLDKVESKSkddRGIVTVETRGLNQDGTLVCIYRRKVMVPKRS 150
Cdd:COG2030   79 GLQEVRFLRPVRVGDTLRARVEVLEKRESKS---RGIVTLRTTVTNQDGEVVLTGEATVLVPRRP 140
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 11-128 7.62e-18

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: 74.68  E-value: 7.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493593220   11 EVGAVYKHWPGKTVTEYDDHLFCLLTMNHHPLHLDANYAeKTTQFKRNVVVGNYVYSLLLGMSVADVSGKAIANLEVESL 90
Cdd:pfam01575   5 APGEPPDTEKPRTVTEADIALFALVSGDHNPIHVDPEFA-KKAGFGGPIAHGMLTLAIVAGLVEEWGGDNVIARFGEIKV 83

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 493593220   91 RHVAPVFHGDTIYGESTVLDKvesksKDDRGIVTVETR 128
Cdd:pfam01575  84 RFTKPVFPGDTLRTEAEVVGK-----RDGRQTKVVEVT 116
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 23-155 1.22e-11

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 61.82  E-value: 1.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493593220  23 TVTEYDDHLFCLLTMNHHPLHLDANYAeKTTQFKRNVVVGNYVYSL---LLGmsvADVSGKAIANLEvESLRHVAPVFHG 99
Cdd:PRK08190  25 TLTPDDIELFAAMSGDVNPAHLDAAYA-ASDGFHHVVAHGMWGGALisaVLG---TRLPGPGTIYLG-QSLRFRRPVRIG 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 493593220 100 DTIygesTVLDKVESKsKDDRGIVTVETRGLNQDGTLVCIYRRKVMVPKRSYGEER 155
Cdd:PRK08190 100 DTL----TVTVTVREK-DPEKRIVVLDCRCTNQDGEVVITGTAEVIAPTEKVRRPR 150
 
Name Accession Description Interval E-value
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 4-149 1.45e-73

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: 217.46  E-value: 1.45e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493593220   4 GRYYEEFEVGAVYKHWPGKTVTEYDDHLFCLLTMNHHPLHLDANYAEKTTqFKRNVVVGNYVYSLLLGMSVADVSGKAIA 83
Cdd:cd03451    1 GLYFEDFTVGQVFEHAPGRTVTEADNVLFTLLTMNTAPLHFDAAYAAKTE-FGRRLVNSLFTLSLALGLSVNDTSLTAVA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493593220  84 NLEVESLRHVAPVFHGDTIYGESTVLDKVESKSKDDRGIVTVETRGLNQDGTLVCIYRRKVMVPKR 149
Cdd:cd03451   80 NLGYDEVRFPAPVFHGDTLYAESEVLSKRESKSRPDAGIVTVRTVGYNQDGEPVLSFERTALVPKR 145
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
6-150 5.42e-49

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 154.66  E-value: 5.42e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493593220   6 YYEEFEVGAVYKHwPGKTVTEYDDHLFCLLTMNHHPLHLDANYAeKTTQFKRNVVVGNYVYSLLLGMSVADVSGKAIANL 85
Cdd:COG2030    1 YFEDLEVGDVLPH-GGRTVTEEDIVLFAGATGDPNPIHLDEEAA-AATGFGGRIAHGMLTLSLASGLLVDDLPGTAVANL 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493593220  86 EVESLRHVAPVFHGDTIYGESTVLDKVESKSkddRGIVTVETRGLNQDGTLVCIYRRKVMVPKRS 150
Cdd:COG2030   79 GLQEVRFLRPVRVGDTLRARVEVLEKRESKS---RGIVTLRTTVTNQDGEVVLTGEATVLVPRRP 140
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 18-145 9.17e-36

(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: 120.83  E-value: 9.17e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493593220  18 HWPGKTVTEYDDHLFCLLTMNHHPLHLDANYAeKTTQFKRNVVVGNYVYSLLLGMSVADVSGKAIANLEVESLRHVAPVF 97
Cdd:cd03441    4 DSSGRTVTEADIALFARLSGDPNPIHVDPEYA-KAAGFGGRIAHGMLTLSLASGLLVQWLPGTDGANLGSQSVRFLAPVF 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 493593220  98 HGDTIYGESTVLDKVESKskdDRGIVTVETRGLNQDGTLVCIYRRKVM 145
Cdd:cd03441   83 PGDTLRVEVEVLGKRPSK---GRGVVTVRTEARNQGGEVVLSGEATVL 127
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 6-137 1.15e-29

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: 105.46  E-value: 1.15e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493593220   6 YYEEFEVGAVYKHwPGKTVTEYDDHLFCLLTMNHHPLHLDANYAEKTtQFKRNVVVGNYVYSLLLG--MSVADVSGKAIA 83
Cdd:cd03446    1 YFEDFEIGQVFES-VGRTVTEADVVMFAGLSGDWNPIHTDAEYAKKT-RFGERIAHGLLTLSIATGllQRLGVFERTVVA 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 493593220  84 NLEVESLRHVAPVFHGDTIYGESTVLDKvESKSKDDRGIVTVETRGLNQDGTLV 137
Cdd:cd03446   79 FYGIDNLRFLNPVFIGDTIRAEAEVVEK-EEKDGEDAGVVTRRIEVVNQRGEVV 131
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 7-147 5.51e-20

YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown function. YdeM has sequence similarity to the hot-dog fold of (R)-specific enoyl-CoA hydratase. Other enzymes with this fold include the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.


Pssm-ID: 239538 [Multi-domain]  Cd Length: 140  Bit Score: 80.69  E-value: 5.51e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493593220   7 YEEFEVGAVYKHwPGKTVTE---------YDDHlfclltmnhhPLHLDANyAEKTTQFKRNVVVGNYVYSLLLGMSVAD- 76
Cdd:cd03454    1 FEDLVIGQRFTS-GSYTVTEeeiiafareFDPQ----------PFHLDEE-AAKESLFGGLAASGWHTAAITMRLLVDAg 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493593220  77 -VSGKAIANLEVESLRHVAPVFHGDTIYGESTVLDKVESKSKDDRGIVTVETRGLNQDGTLVCIYRRKVMVP 147
Cdd:cd03454   69 lSGSASGGSPGIDELRWPRPVRPGDTLSVEVEVLDKRPSRSRPDRGIVTLRSETLNQRGEVVLTFEATVLVR 140
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 22-138 7.90e-19

(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: 77.20  E-value: 7.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493593220  22 KTVTEYDDHLFCLLTMNHHPLHLDANYAEKtTQFKRNVVVGNYVYSL---LLGM------SVAdvsgkaianLEvESLRH 92
Cdd:cd03449   11 RTITEEDVELFAELSGDFNPIHLDEEYAKK-TRFGGRIAHGMLTASLisaVLGTllpgpgTIY---------LS-QSLRF 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 493593220  93 VAPVFHGDTIYGESTVLDKVEskskdDRGIVTVETRGLNQDGTLVC 138
Cdd:cd03449   80 LRPVFIGDTVTATVTVTEKRE-----DKKRVTLETVCTNQNGEVVI 120
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 11-128 7.62e-18

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: 74.68  E-value: 7.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493593220   11 EVGAVYKHWPGKTVTEYDDHLFCLLTMNHHPLHLDANYAeKTTQFKRNVVVGNYVYSLLLGMSVADVSGKAIANLEVESL 90
Cdd:pfam01575   5 APGEPPDTEKPRTVTEADIALFALVSGDHNPIHVDPEFA-KKAGFGGPIAHGMLTLAIVAGLVEEWGGDNVIARFGEIKV 83

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 493593220   91 RHVAPVFHGDTIYGESTVLDKvesksKDDRGIVTVETR 128
Cdd:pfam01575  84 RFTKPVFPGDTLRTEAEVVGK-----RDGRQTKVVEVT 116
MaoC_C cd03452
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory ...
 6-148 1.56e-16

MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory protein. Orthologs of MaoC include PaaZ [Escherichia coli] and PaaN [Pseudomonas putida], which are putative ring-opening enzymes involved in phenylacetic acid degradation. The C-terminal domain of MaoC has sequence similarity to (R)-specific enoyl-CoA hydratase,Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. MaoC also has an N-terminal PutA domain like that found in the E. coli PutA proline dehydrogenase and other members of the aldehyde dehydrogenase family.


Pssm-ID: 239536 [Multi-domain]  Cd Length: 142  Bit Score: 72.05  E-value: 1.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493593220   6 YYEEFEVGAVYKHwPGKTVTEYDDHLFCLLTMNHHPLHLDANyAEKTTQFKRNVVVGNYVYSLLLGMSVADVSGKAIANL 85
Cdd:cd03452    1 NLEQLRPGDSLLT-HRRTVTEADIVNFACLTGDHFYAHMDEI-AAKASFFGKRVAHGYFVLSAAAGLFVDPAPGPVLANY 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493593220  86 EVESLRHVAPVFHGDTIYGESTVLDKVEsKSKDDRGIVTVETRGLNQDGTLVCIYRRKVMVPK 148
Cdd:cd03452   79 GLENLRFLEPVYPGDTIQVRLTCKRKIP-RDGQDYGVVRWDAEVTNQNGELVASYDILTLVAK 140
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 23-155 1.22e-11

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 61.82  E-value: 1.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493593220  23 TVTEYDDHLFCLLTMNHHPLHLDANYAeKTTQFKRNVVVGNYVYSL---LLGmsvADVSGKAIANLEvESLRHVAPVFHG 99
Cdd:PRK08190  25 TLTPDDIELFAAMSGDVNPAHLDAAYA-ASDGFHHVVAHGMWGGALisaVLG---TRLPGPGTIYLG-QSLRFRRPVRIG 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 493593220 100 DTIygesTVLDKVESKsKDDRGIVTVETRGLNQDGTLVCIYRRKVMVPKRSYGEER 155
Cdd:PRK08190 100 DTL----TVTVTVREK-DPEKRIVVLDCRCTNQDGEVVITGTAEVIAPTEKVRRPR 150
SAV4209 cd03455
SAV4209 is a Streptomyces avermitilis protein with a hot dog fold that is similar to those of ...
 32-138 6.73e-05

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: 6.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493593220  32 FCLLTMNHHPLHLDANYAekTTQFKRNVVVGNYVYSLLLGMSVADVSGKAiANLEVESLRHVAPVFHGDTIYGESTVLdk 111
Cdd:cd03455   19 YSAATRDFHRIHHDRDYA--RAVGYPDLYVNGPTLAGLVIRYVTDWAGPD-ARVKSFAFRLGAPLYAGDTLRFGGRVT-- 93

                         90       100
                 ....*....|....*....|....*..
gi 493593220 112 veskSKDDRGIVTVETRGLNQDGTLVC 138
Cdd:cd03455   94 ----AKRDDEVVTVELWARNSEGDHVM 116
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 89-145 3.85e-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: 37.84  E-value: 3.85e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 493593220  89 SLRHVAPVFHGDTIYGESTVLdkvesksKDDRGIVTVETRGLNQDGTLVCIYRRKVM 145
Cdd:cd03440   51 DVRFLRPVRPGDTLTVEAEVV-------RVGRSSVTVEVEVRNEDGKLVATATATFV 100
PaaI COG2050
Acyl-CoA thioesterase PaaI, contains HGG motif [Secondary metabolites biosynthesis, transport ...
 72-149 5.51e-03

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


Pssm-ID: 441653 [Multi-domain]  Cd Length: 138  Bit Score: 35.30  E-value: 5.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493593220  72 MSVADVSGKAIANLEVE----------SLRHVAPVFHGDTIYGESTVLdkvesksKDDRGIVTVETRGLNQDGTLVCIYR 141
Cdd:COG2050   56 AALADSAAGLAANSALPpgrravtielNINFLRPARLGDRLTAEARVV-------RRGRRLAVVEVEVTDEDGKLVATAT 128


                 ....*...
gi 493593220 142 RKVMVPKR 149
Cdd:COG2050  129 GTFAVLPK 136
 
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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