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Conserved domains on  [gi|1563131590|gb|RXK11424|]
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hypothetical protein CRV05_02510 [Halarcobacter bivalviorum]

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 ...
 2-146 1.24e-56

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: 180.86  E-value: 1.24e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131590   2 GNFFEDFSIGQKIVHPLPRTITDGDVSLYIAFTGSRFALHSSDVVATEMGYEKRPIDDVLMFHLTFGKSVQDISLNAIAN 81
Cdd:cd03451     1 GLYFEDFTVGQVFEHAPGRTVTEADNVLFTLLTMNTAPLHFDAAYAAKTEFGRRLVNSLFTLSLALGLSVNDTSLTAVAN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1563131590  82 LGYAEISFPNPVYIGDTVSMTSTVIGLKEN-SNGKSGVVYVHSIGVNQNGAEVLNFKRWVMVHKKD 146
Cdd:cd03451    81 LGYDEVRFPAPVFHGDTLYAESEVLSKRESkSRPDAGIVTVRTVGYNQDGEPVLSFERTALVPKRG 146
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 187-343 1.18e-42

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: 145.04  E-value: 1.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131590 187 FFEDYEKGERLNHPEGITVDNSDHTLATKLYQNNAKVHFNDHMMKSTPMGQRLMYGGIVISMARAISFNGL-QNAQWMYA 265
Cdd:cd03451     3 YFEDFTVGQVFEHAPGRTVTEADNVLFTLLTMNTAPLHFDAAYAAKTEFGRRLVNSLFTLSLALGLSVNDTsLTAVANLG 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1563131590 266 INSGAHANPTYAGDTIYAYTEVLDVIEHK-RDDIGLLRLRTIAVkNQRPEeiespkdkdgkylpnVVLDLDYTVIIPKR 343
Cdd:cd03451    83 YDEVRFPAPVFHGDTLYAESEVLSKRESKsRPDAGIVTVRTVGY-NQDGE---------------PVLSFERTALVPKR 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 ...
 2-146 1.24e-56

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: 180.86  E-value: 1.24e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131590   2 GNFFEDFSIGQKIVHPLPRTITDGDVSLYIAFTGSRFALHSSDVVATEMGYEKRPIDDVLMFHLTFGKSVQDISLNAIAN 81
Cdd:cd03451     1 GLYFEDFTVGQVFEHAPGRTVTEADNVLFTLLTMNTAPLHFDAAYAAKTEFGRRLVNSLFTLSLALGLSVNDTSLTAVAN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1563131590  82 LGYAEISFPNPVYIGDTVSMTSTVIGLKEN-SNGKSGVVYVHSIGVNQNGAEVLNFKRWVMVHKKD 146
Cdd:cd03451    81 LGYDEVRFPAPVFHGDTLYAESEVLSKRESkSRPDAGIVTVRTVGYNQDGEPVLSFERTALVPKRG 146
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 187-343 1.18e-42

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: 145.04  E-value: 1.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131590 187 FFEDYEKGERLNHPEGITVDNSDHTLATKLYQNNAKVHFNDHMMKSTPMGQRLMYGGIVISMARAISFNGL-QNAQWMYA 265
Cdd:cd03451     3 YFEDFTVGQVFEHAPGRTVTEADNVLFTLLTMNTAPLHFDAAYAAKTEFGRRLVNSLFTLSLALGLSVNDTsLTAVANLG 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1563131590 266 INSGAHANPTYAGDTIYAYTEVLDVIEHK-RDDIGLLRLRTIAVkNQRPEeiespkdkdgkylpnVVLDLDYTVIIPKR 343
Cdd:cd03451    83 YDEVRFPAPVFHGDTLYAESEVLSKRESKsRPDAGIVTVRTVGY-NQDGE---------------PVLSFERTALVPKR 145
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
4-146 4.14e-35

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 125.00  E-value: 4.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131590   4 FFEDFSIGQKIVHPlPRTITDGDVSLYIAFTGSRFALHSSDVVATEMGYEKRPIDDVLMFHLTFGKSVQDISLNAIANLG 83
Cdd:COG2030     1 YFEDLEVGDVLPHG-GRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAVANLG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1563131590  84 YAEISFPNPVYIGDTVSMTSTVIGLKENSNGksGVVYVHSIGVNQNGAEVLNFKRWVMVHKKD 146
Cdd:COG2030    80 LQEVRFLRPVRVGDTLRARVEVLEKRESKSR--GIVTLRTTVTNQDGEVVLTGEATVLVPRRP 140
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
187-344 2.49e-21

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 88.40  E-value: 2.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131590 187 FFEDYEKGERLNHPeGITVDNSDHTLATKLYQNNAKVHFNDHMMKSTPMGQRLMYGGIVISMARAISFNGL-QNAQWMYA 265
Cdd:COG2030     1 YFEDLEVGDVLPHG-GRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLpGTAVANLG 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1563131590 266 INSGAHANPTYAGDTIYAYTEVLDVIEHKrdDIGLLRLRTiAVKNQRPEeiespkdkdgkylpnVVLDLDYTVIIPKRK 344
Cdd:COG2030    80 LQEVRFLRPVRVGDTLRARVEVLEKRESK--SRGIVTLRT-TVTNQDGE---------------VVLTGEATVLVPRRP 140
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 9-127 4.17e-11

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: 59.66  E-value: 4.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131590   9 SIGQKIVHPLPRTITDGDVSLYIAFTGSRFALHSSDVVATEMGYEKRPIDDVLMFHLTFGKSVQDISLNAIANLGYAEIS 88
Cdd:pfam01575   5 APGEPPDTEKPRTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDNVIARFGEIKVR 84

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1563131590  89 FPNPVYIGDTVSMTSTVIGLKENSNGKSGVVYVHSIGVN 127
Cdd:pfam01575  85 FTKPVFPGDTLRTEAEVVGKRDGRQTKVVEVTVEVTEVA 123
 
Name Accession Description Interval E-value
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 2-146 1.24e-56

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: 180.86  E-value: 1.24e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131590   2 GNFFEDFSIGQKIVHPLPRTITDGDVSLYIAFTGSRFALHSSDVVATEMGYEKRPIDDVLMFHLTFGKSVQDISLNAIAN 81
Cdd:cd03451     1 GLYFEDFTVGQVFEHAPGRTVTEADNVLFTLLTMNTAPLHFDAAYAAKTEFGRRLVNSLFTLSLALGLSVNDTSLTAVAN 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1563131590  82 LGYAEISFPNPVYIGDTVSMTSTVIGLKEN-SNGKSGVVYVHSIGVNQNGAEVLNFKRWVMVHKKD 146
Cdd:cd03451    81 LGYDEVRFPAPVFHGDTLYAESEVLSKRESkSRPDAGIVTVRTVGYNQDGEPVLSFERTALVPKRG 146
FkbR2 cd03451
FkbR2 is a Streptomyces hygroscopicus protein with a hot dog fold that belongs to a conserved ...
 187-343 1.18e-42

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: 145.04  E-value: 1.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131590 187 FFEDYEKGERLNHPEGITVDNSDHTLATKLYQNNAKVHFNDHMMKSTPMGQRLMYGGIVISMARAISFNGL-QNAQWMYA 265
Cdd:cd03451     3 YFEDFTVGQVFEHAPGRTVTEADNVLFTLLTMNTAPLHFDAAYAAKTEFGRRLVNSLFTLSLALGLSVNDTsLTAVANLG 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1563131590 266 INSGAHANPTYAGDTIYAYTEVLDVIEHK-RDDIGLLRLRTIAVkNQRPEeiespkdkdgkylpnVVLDLDYTVIIPKR 343
Cdd:cd03451    83 YDEVRFPAPVFHGDTLYAESEVLSKRESKsRPDAGIVTVRTVGY-NQDGE---------------PVLSFERTALVPKR 145
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
4-146 4.14e-35

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 125.00  E-value: 4.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131590   4 FFEDFSIGQKIVHPlPRTITDGDVSLYIAFTGSRFALHSSDVVATEMGYEKRPIDDVLMFHLTFGKSVQDISLNAIANLG 83
Cdd:COG2030     1 YFEDLEVGDVLPHG-GRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLPGTAVANLG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1563131590  84 YAEISFPNPVYIGDTVSMTSTVIGLKENSNGksGVVYVHSIGVNQNGAEVLNFKRWVMVHKKD 146
Cdd:COG2030    80 LQEVRFLRPVRVGDTLRARVEVLEKRESKSR--GIVTLRTTVTNQDGEVVLTGEATVLVPRRP 140
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 16-141 5.00e-22

(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: 90.02  E-value: 5.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131590  16 HPLPRTITDGDVSLYIAFTGSRFALHSSDVVATEMGYEKRPIDDVLMFHLTFGKSVQDISLNAIANLGYAEISFPNPVYI 95
Cdd:cd03441     4 DSSGRTVTEADIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGLLVQWLPGTDGANLGSQSVRFLAPVFP 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1563131590  96 GDTVSMTSTVIGLKENSngKSGVVYVHSIGVNQNGAEVLNFKRWVM 141
Cdd:cd03441    84 GDTLRVEVEVLGKRPSK--GRGVVTVRTEARNQGGEVVLSGEATVL 127
MaoC COG2030
Acyl-CoA dehydratase PaaZ [Lipid transport and metabolism];
187-344 2.49e-21

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


Pssm-ID: 441633 [Multi-domain]  Cd Length: 140  Bit Score: 88.40  E-value: 2.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131590 187 FFEDYEKGERLNHPeGITVDNSDHTLATKLYQNNAKVHFNDHMMKSTPMGQRLMYGGIVISMARAISFNGL-QNAQWMYA 265
Cdd:COG2030     1 YFEDLEVGDVLPHG-GRTVTEEDIVLFAGATGDPNPIHLDEEAAAATGFGGRIAHGMLTLSLASGLLVDDLpGTAVANLG 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1563131590 266 INSGAHANPTYAGDTIYAYTEVLDVIEHKrdDIGLLRLRTiAVKNQRPEeiespkdkdgkylpnVVLDLDYTVIIPKRK 344
Cdd:COG2030    80 LQEVRFLRPVRVGDTLRARVEVLEKRESK--SRGIVTLRT-TVTNQDGE---------------VVLTGEATVLVPRRP 140
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 5-135 9.02e-19

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: 81.58  E-value: 9.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131590   5 FEDFSIGQKIVhPLPRTITDGDVSLYIAFTGSRFALHSSDVVATEMGYEKRPIDDVLMFHLTFGKSVQDISLN--AIANL 82
Cdd:cd03446     2 FEDFEIGQVFE-SVGRTVTEADVVMFAGLSGDWNPIHTDAEYAKKTRFGERIAHGLLTLSIATGLLQRLGVFErtVVAFY 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1563131590  83 GYAEISFPNPVYIGDTVSMTSTVIGLKENSNGKSGVVYVHSIGVNQNGAEVLN 135
Cdd:cd03446    81 GIDNLRFLNPVFIGDTIRAEAEVVEKEEKDGEDAGVVTRRIEVVNQRGEVVQS 133
MaoC_like cd03446
MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but ...
 188-318 3.77e-13

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: 65.79  E-value: 3.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131590 188 FEDYEKGERLNhPEGITVDNSDHTLATKLYQNNAKVHFNDHMMKSTPMGQRLMYGGIVISMA-----RAISFNGlqNAQW 262
Cdd:cd03446     2 FEDFEIGQVFE-SVGRTVTEADVVMFAGLSGDWNPIHTDAEYAKKTRFGERIAHGLLTLSIAtgllqRLGVFER--TVVA 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1563131590 263 MYAINSGAHANPTYAGDTIYAYTEVLDVIEHKRDDIGLLRLRtIAVKNQRPEEIES 318
Cdd:cd03446    79 FYGIDNLRFLNPVFIGDTIRAEAEVVEKEEKDGEDAGVVTRR-IEVVNQRGEVVQS 133
R_hydratase_like cd03441
(R)-hydratase [(R)-specific enoyl-CoA hydratase]. Catalyzes the hydration of trans-2-enoyl ...
 202-312 1.63e-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. 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: 63.82  E-value: 1.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131590 202 GITVDNSDHTLATKLYQNNAKVHFNDHMMKSTPMGQRLMYGGIVISMARAISFNGL-QNAQWMYAINSGAHANPTYAGDT 280
Cdd:cd03441     7 GRTVTEADIALFARLSGDPNPIHVDPEYAKAAGFGGRIAHGMLTLSLASGLLVQWLpGTDGANLGSQSVRFLAPVFPGDT 86

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1563131590 281 IYAYTEVLDVIEHKrdDIGLLRLRTIAVkNQR 312
Cdd:cd03441    87 LRVEVEVLGKRPSK--GRGVVTVRTEAR-NQG 115
MaoC_C cd03452
MaoC_C The C-terminal hot dog fold of the MaoC (monoamine oxidase C) dehydratase regulatory ...
 5-146 5.44e-12

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: 62.80  E-value: 5.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131590   5 FEDFSIGQKIVHPLpRTITDGDVSLYIAFTGSRFALHSSDVVATEMGYEKRPIDDVLMFHLTFGKSVQDISLNAIANLGY 84
Cdd:cd03452     2 LEQLRPGDSLLTHR-RTVTEADIVNFACLTGDHFYAHMDEIAAKASFFGKRVAHGYFVLSAAAGLFVDPAPGPVLANYGL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1563131590  85 AEISFPNPVYIGDT--VSMTSTVIGLKENSngKSGVVYVHSIGVNQNGAEVLNFKRWVMVHKKD 146
Cdd:cd03452    81 ENLRFLEPVYPGDTiqVRLTCKRKIPRDGQ--DYGVVRWDAEVTNQNGELVASYDILTLVAKKG 142
MaoC_dehydratas pfam01575
MaoC like domain; The maoC gene is part of a operon with maoA which is involved in the ...
 9-127 4.17e-11

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: 59.66  E-value: 4.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131590   9 SIGQKIVHPLPRTITDGDVSLYIAFTGSRFALHSSDVVATEMGYEKRPIDDVLMFHLTFGKSVQDISLNAIANLGYAEIS 88
Cdd:pfam01575   5 APGEPPDTEKPRTVTEADIALFALVSGDHNPIHVDPEFAKKAGFGGPIAHGMLTLAIVAGLVEEWGGDNVIARFGEIKVR 84

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1563131590  89 FPNPVYIGDTVSMTSTVIGLKENSNGKSGVVYVHSIGVN 127
Cdd:pfam01575  85 FTKPVFPGDTLRTEAEVVGKRDGRQTKVVEVTVEVTEVA 123
R_hydratase cd03449
(R)-hydratase [(R)-specific enoyl-CoA hydratase] catalyzes the hydration of trans-2-enoyl CoA ...
 20-134 2.14e-07

(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: 49.08  E-value: 2.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131590  20 RTITDGDVSLYIAFTGSRFALHSSDVVATEMGYEKRpiddvlMFHLTFGKSVqdISlNAIANL----G--YAE--ISFPN 91
Cdd:cd03449    11 RTITEEDVELFAELSGDFNPIHLDEEYAKKTRFGGR------IAHGMLTASL--IS-AVLGTLlpgpGtiYLSqsLRFLR 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1563131590  92 PVYIGDTVSMTSTVIGLKENSNgksgVVYVHSIGVNQNGAEVL 134
Cdd:cd03449    82 PVFIGDTVTATVTVTEKREDKK----RVTLETVCTNQNGEVVI 120
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 83-143 4.70e-07

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: 48.33  E-value: 4.70e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1563131590  83 GYAEISFPNPVYIGDTVSMTSTVIGLKEnSNGKS--GVVYVHSIGVNQNGAEVLNFKRWVMVH 143
Cdd:cd03454    79 GIDELRWPRPVRPGDTLSVEVEVLDKRP-SRSRPdrGIVTLRSETLNQRGEVVLTFEATVLVR 140
YdeM cd03454
YdeM is a Bacillus subtilis protein that belongs to a family of prokaryotic proteins of unkown ...
 256-341 4.09e-06

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: 45.64  E-value: 4.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1563131590 256 GLQNAQWMyainsgahaNPTYAGDTIYAYTEVLDVIEHK-RDDIGLLRLRTiAVKNQRPEeiespkdkdgkylpnVVLDL 334
Cdd:cd03454    79 GIDELRWP---------RPVRPGDTLSVEVEVLDKRPSRsRPDRGIVTLRS-ETLNQRGE---------------VVLTF 133


                  ....*..
gi 1563131590 335 DYTVIIP 341
Cdd:cd03454   134 EATVLVR 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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