NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|896139373|ref|WP_049159280|]
View 

MULTISPECIES: MaoC family dehydratase [Micrococcus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 11-154 5.32e-63

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: 190.88  E-value: 5.32e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896139373  11 GRYADELAVGQVYLHRPGRTLTEADNVLFTTLTMNPQALHLDHAYAAAQPFGRPLVNSMLTLSTLVGLAVGQTTQgTLVA 90
Cdd:cd03451    1 GLYFEDFTVGQVFEHAPGRTVTEADNVLFTLLTMNTAPLHFDAAYAAKTEFGRRLVNSLFTLSLALGLSVNDTSL-TAVA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896139373  91 QLGLGEIAFPKPVFHGDTLYGRSEVTAIRESSSRPGQRIVTFAMTGENQHGDVVVRAQRTCLMW 154
Cdd:cd03451   80 NLGYDEVRFPAPVFHGDTLYAESEVLSKRESKSRPDAGIVTVRTVGYNQDGEPVLSFERTALVP 143
 
Name Accession Description Interval E-value
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 11-154 5.32e-63

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: 190.88  E-value: 5.32e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896139373  11 GRYADELAVGQVYLHRPGRTLTEADNVLFTTLTMNPQALHLDHAYAAAQPFGRPLVNSMLTLSTLVGLAVGQTTQgTLVA 90
Cdd:cd03451    1 GLYFEDFTVGQVFEHAPGRTVTEADNVLFTLLTMNTAPLHFDAAYAAKTEFGRRLVNSLFTLSLALGLSVNDTSL-TAVA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896139373  91 QLGLGEIAFPKPVFHGDTLYGRSEVTAIRESSSRPGQRIVTFAMTGENQHGDVVVRAQRTCLMW 154
Cdd:cd03451   80 NLGYDEVRFPAPVFHGDTLYAESEVLSKRESKSRPDAGIVTVRTVGYNQDGEPVLSFERTALVP 143
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
13-155 4.56e-45

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 145.03  E-value: 4.56e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896139373  13 YADELAVGQVYLHRPgRTLTEADNVLFTTLTMNPQALHLDHAYAAAQPFGRPLVNSMLTLSTLVGLAVgQTTQGTLVAQL 92
Cdd:COG2030    1 YFEDLEVGDVLPHGG-RTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLV-DDLPGTAVANL 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896139373  93 GLGEIAFPKPVFHGDTLYGRSEVTAIRESSSRpgqRIVTFAMTGENQHGDVVVRAQRTCLMWT 155
Cdd:COG2030   79 GLQEVRFLRPVRVGDTLRARVEVLEKRESKSR---GIVTLRTTVTNQDGEVVLTGEATVLVPR 138
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 18-120 3.23e-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: 88.94  E-value: 3.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896139373   18 AVGQVYLHRPGRTLTEADNVLFTTLTMNPQALHLDHAYAAAQPFGRPLVNSMLTLSTLVGLavgqttqgtLVAQLGLGEI 97
Cdd:pfam01575   5 APGEPPDTEKPRTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGL---------VEEWGGDNVI 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 896139373   98 A--------FPKPVFHGDTLYGRSEVTAIRE 120
Cdd:pfam01575  76 ArfgeikvrFTKPVFPGDTLRTEAEVVGKRD 106
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 15-148 5.12e-12

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 62.98  E-value: 5.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896139373  15 DELAVGQVYLHRpgRTLTEADNVLFTTLTMNPQALHLDHAYAAAQPFGRPLVNSMLT---LSTLVGlavgqtTQ----GT 87
Cdd:PRK08190  12 DEIAIGDSASLV--RTLTPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGgalISAVLG------TRlpgpGT 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896139373  88 L-VAQlglgEIAFPKPVFHGDTLYGRSEVTAiressSRPGQRIVTFAMTGENQHGDVVVRAQ 148
Cdd:PRK08190  84 IyLGQ----SLRFRRPVRIGDTLTVTVTVRE-----KDPEKRIVVLDCRCTNQDGEVVITGT 136
 
Name Accession Description Interval E-value
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 11-154 5.32e-63

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: 190.88  E-value: 5.32e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896139373  11 GRYADELAVGQVYLHRPGRTLTEADNVLFTTLTMNPQALHLDHAYAAAQPFGRPLVNSMLTLSTLVGLAVGQTTQgTLVA 90
Cdd:cd03451    1 GLYFEDFTVGQVFEHAPGRTVTEADNVLFTLLTMNTAPLHFDAAYAAKTEFGRRLVNSLFTLSLALGLSVNDTSL-TAVA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896139373  91 QLGLGEIAFPKPVFHGDTLYGRSEVTAIRESSSRPGQRIVTFAMTGENQHGDVVVRAQRTCLMW 154
Cdd:cd03451   80 NLGYDEVRFPAPVFHGDTLYAESEVLSKRESKSRPDAGIVTVRTVGYNQDGEPVLSFERTALVP 143
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
13-155 4.56e-45

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 145.03  E-value: 4.56e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896139373  13 YADELAVGQVYLHRPgRTLTEADNVLFTTLTMNPQALHLDHAYAAAQPFGRPLVNSMLTLSTLVGLAVgQTTQGTLVAQL 92
Cdd:COG2030    1 YFEDLEVGDVLPHGG-RTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLV-DDLPGTAVANL 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896139373  93 GLGEIAFPKPVFHGDTLYGRSEVTAIRESSSRpgqRIVTFAMTGENQHGDVVVRAQRTCLMWT 155
Cdd:COG2030   79 GLQEVRFLRPVRVGDTLRARVEVLEKRESKSR---GIVTLRTTVTNQDGEVVLTGEATVLVPR 138
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 24-150 2.14e-33

(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: 115.05  E-value: 2.14e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896139373  24 LHRPGRTLTEADNVLFTTLTMNPQALHLDHAYAAAQPFGRPLVNSMLTLSTLVGLaVGQTTQGTLVAQLGLGEIAFPKPV 103
Cdd:cd03441    3 LDSSGRTVTEADIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGL-LVQWLPGTDGANLGSQSVRFLAPV 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 896139373 104 FHGDTLYGRSEVTAIRESSsrpGQRIVTFAMTGENQHGDVVVRAQRT 150
Cdd:cd03441   82 FPGDTLRVEVEVLGKRPSK---GRGVVTVRTEARNQGGEVVLSGEAT 125
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 13-153 5.58e-27

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: 98.92  E-value: 5.58e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896139373  13 YADELAVGQVYLHRpGRTLTEADNVLFTTLTMNPQALHLDHAYAAAQPFGRPLVNSMLTLSTLVGLAV-GQTTQGTLVAQ 91
Cdd:cd03446    1 YFEDFEIGQVFESV-GRTVTEADVVMFAGLSGDWNPIHTDAEYAKKTRFGERIAHGLLTLSIATGLLQrLGVFERTVVAF 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896139373  92 LGLGEIAFPKPVFHGDTLYGRSEVTAIREsSSRPGQRIVTFAMTGENQHGDVVVRAQRTCLM 153
Cdd:cd03446   80 YGIDNLRFLNPVFIGDTIRAEAEVVEKEE-KDGEDAGVVTRRIEVVNQRGEVVQSGEMSLLV 140
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 15-144 2.16e-25

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: 94.94  E-value: 2.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896139373  15 DELAVGQVYLHRPgRTLTEADNVLFTTlTMNPQALHLDHAYAAAQPFG--------------RPLVNSMLTLSTLVGLAv 80
Cdd:cd03454    2 EDLVIGQRFTSGS-YTVTEEEIIAFAR-EFDPQPFHLDEEAAKESLFGglaasgwhtaaitmRLLVDAGLSGSASGGSP- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 896139373  81 gqttqgtlvaqlGLGEIAFPKPVFHGDTLYGRSEVTAIRESSSRPGQRIVTFAMTGENQHGDVV 144
Cdd:cd03454   79 ------------GIDELRWPRPVRPGDTLSVEVEVLDKRPSRSRPDRGIVTLRSETLNQRGEVV 130
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 18-120 3.23e-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: 88.94  E-value: 3.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896139373   18 AVGQVYLHRPGRTLTEADNVLFTTLTMNPQALHLDHAYAAAQPFGRPLVNSMLTLSTLVGLavgqttqgtLVAQLGLGEI 97
Cdd:pfam01575   5 APGEPPDTEKPRTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGL---------VEEWGGDNVI 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 896139373   98 A--------FPKPVFHGDTLYGRSEVTAIRE 120
Cdd:pfam01575  76 ArfgeikvrFTKPVFPGDTLRTEAEVVGKRD 106
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 17-146 2.53e-18

(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: 76.43  E-value: 2.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896139373  17 LAVGQVYlhRPGRTLTEADNVLFTTLT--MNPqaLHLDHAYAAAQPFGRPLVNSMLT---LSTLVG--------LAVGQT 83
Cdd:cd03449    1 LKVGDSA--SLTRTITEEDVELFAELSgdFNP--IHLDEEYAKKTRFGGRIAHGMLTaslISAVLGtllpgpgtIYLSQS 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896139373  84 TQgtlvaqlglgeiaFPKPVFHGDTLYGRSEVTAIRESSsrpgqRIVTFAMTGENQHGDVVVR 146
Cdd:cd03449   77 LR-------------FLRPVFIGDTVTATVTVTEKREDK-----KRVTLETVCTNQNGEVVIE 121
PRK08190 PRK08190
bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated
 15-148 5.12e-12

bifunctional enoyl-CoA hydratase/phosphate acetyltransferase; Validated


Pssm-ID: 236180 [Multi-domain]  Cd Length: 466  Bit Score: 62.98  E-value: 5.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896139373  15 DELAVGQVYLHRpgRTLTEADNVLFTTLTMNPQALHLDHAYAAAQPFGRPLVNSMLT---LSTLVGlavgqtTQ----GT 87
Cdd:PRK08190  12 DEIAIGDSASLV--RTLTPDDIELFAAMSGDVNPAHLDAAYAASDGFHHVVAHGMWGgalISAVLG------TRlpgpGT 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896139373  88 L-VAQlglgEIAFPKPVFHGDTLYGRSEVTAiressSRPGQRIVTFAMTGENQHGDVVVRAQ 148
Cdd:PRK08190  84 IyLGQ----SLRFRRPVRIGDTLTVTVTVRE-----KDPEKRIVVLDCRCTNQDGEVVITGT 136
MaoC_C cd03452
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory ...
 13-147 3.96e-11

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: 57.79  E-value: 3.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896139373  13 YADELAVGQVYL-HRpgRTLTEADNVLFTTLTMNPQALHLDHAYAAAQPFGRPLVNSMLTLSTLVGLAVgQTTQGTLVAQ 91
Cdd:cd03452    1 NLEQLRPGDSLLtHR--RTVTEADIVNFACLTGDHFYAHMDEIAAKASFFGKRVAHGYFVLSAAAGLFV-DPAPGPVLAN 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 896139373  92 LGLGEIAFPKPVFHGDTLYGRSEVTAIRESSSRPgQRIVTFAMTGENQHGDVVVRA 147
Cdd:cd03452   78 YGLENLRFLEPVYPGDTIQVRLTCKRKIPRDGQD-YGVVRWDAEVTNQNGELVASY 132
SAV4209 cd03455
SAV4209 is a Streptomyces avermitilis protein with a hot dog fold that is similar to those of ...
 30-148 6.37e-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: 40.76  E-value: 6.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896139373  30 TLTEADNVLFTTLTMNPQALHLDHAYAAAQPFGRPLVNSMLTLSTLVGLAVGQTTQGTLVAQLGLGEIAfpkPVFHGDTL 109
Cdd:cd03455   10 PPDPTLLFRYSAATRDFHRIHHDRDYARAVGYPDLYVNGPTLAGLVIRYVTDWAGPDARVKSFAFRLGA---PLYAGDTL 86

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 896139373 110 YGRSEVTAIResssrpGQRIVTFAMTGENQHGDVVVRAQ 148
Cdd:cd03455   87 RFGGRVTAKR------DDEVVTVELWARNSEGDHVMAGT 119
NodN cd03450
NodN (nodulation factor N) contains a single hot dog fold similar to those of the peroxisomal ...
 18-137 7.85e-05

NodN (nodulation factor N) contains a single hot dog fold similar to those of the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. Rhizobium and related species form nodules on the roots of their legume hosts, a symbiotic process that requires production of Nod factors, which are signal molecules involved in root hair deformation and meristematic cell division. The nodulation gene products, including NodN, are involved in producing the Nod factors, however the role played by NodN is unclear.


Pssm-ID: 239534 [Multi-domain]  Cd Length: 149  Bit Score: 40.62  E-value: 7.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896139373  18 AVGQVYLHRPGRTLTEADNVLFTTLTMNPQALHLDHAYAAAQPFGRPLVNSMLTLSTLVGLA--VGQTTQGTLVAQLGLG 95
Cdd:cd03450   11 LVGQELGVSDWVTVDQERIDQFADATGDHQWIHVDPERAAAEPFGGTIAHGFLTLSLLPALTpqLFRVEGVKMGVNYGLD 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 896139373  96 EIAFPKPVFHGDTLYGRSEVTAIREssSRPGQRIVTFAMTGE 137
Cdd:cd03450   91 KVRFPAPVPVGSRVRGRFTLLSVEE--LKGGGVQVTLEVTVE 130
SAV4209_like cd03453
SAV4209_like. Similar in sequence to the Streptomyces avermitilis SAV4209 protein, with a hot ...
 45-148 2.79e-04

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: 38.84  E-value: 2.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896139373  45 NPqaLHLDHAYAAAQPFGRPLVNSMLTLSTLVGLAVGQTTQGTLVAQLGlgeIAFPKPVFHGDTLYGRSEVTAIRESssr 124
Cdd:cd03453   28 NP--IHYDEDFAKKVGLPGVIAHGMLTMGLLGRLVTDWVGDPGRVVSFG---VRFTKPVPVPDTLTCTGIVVEKTVA--- 99

                         90       100
                 ....*....|....*....|....
gi 896139373 125 PGQRIVTFAMTGENQHGDVVVRAQ 148
Cdd:cd03453  100 DGEDALTVTVDATDQAGGKKVLGR 123
hot_dog cd03440
The hotdog fold was initially identified in the E. coli FabA (beta-hydroxydecanoyl-acyl ...
 58-152 1.59e-03

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: 36.30  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896139373  58 AQPFGRPLVNSMLTLS---TLVGLAVGQTTQGTLVAQLGLGEIAFPKPVFHGDTLYGRSEVTAIRESSsrpgqriVTFAM 134
Cdd:cd03440   10 EDIDGGGIVHGGLLLAladEAAGAAAARLGGRGLGAVTLSLDVRFLRPVRPGDTLTVEAEVVRVGRSS-------VTVEV 82

                         90
                 ....*....|....*...
gi 896139373 135 TGENQHGDVVVRAQRTCL 152
Cdd:cd03440   83 EVRNEDGKLVATATATFV 100
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH