1F1X,1F1R


Conserved Protein Domain Family
HPCD_N_class_II

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cd07266: HPCD_N_class_II 
Click on image for an interactive view with Cn3D
N-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD)
This subfamily contains the N-terminal, non-catalytic, domain of HPCD. HPCD catalyses the second step in the degradation of 4-hydroxyphenylacetate to succinate and pyruvate. The aromatic ring of 4-hydroxyphenylacetate is opened by this dioxygenase to yield the 3,4-diol product, 2-hydroxy-5-carboxymethylmuconate semialdehyde. HPCD is a homotetramer and each monomer contains two structurally homologous barrel-shaped domains at the N- and C-terminus. The active-site metal is located in the C-terminal barrel and plays an essential role in the catalytic mechanism. Most extradiol dioxygenases contain Fe(II) in their active site, but HPCD can be activated by either Mn(II) or Fe(II). These enzymes belong to the type I class II family of extradiol dioxygenases. The class III 3,4-dihydroxyphenylacetate 2,3-dioxygenases belong to a different superfamily.
Statistics
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PSSM-Id: 319927
View PSSM: cd07266
Aligned: 6 rows
Threshold Bit Score: 182.223
Threshold Setting Gi: 15807888
Created: 18-Mar-2009
Updated: 18-Aug-2016
Structure
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Program:
Drawing:
Aligned Rows:
 
tetramer
Conserved site includes 6 residues -Click on image for an interactive view with Cn3D
Feature 1:tetramer interface [polypeptide binding site]
Evidence:
  • Structure:1FIX_A/B/C/D: tetramer interface of homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum, by 4A distance.
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1          ##                                       #                         # #        
1F1X_A        14 DILRCAYAELVVTDLAKSRNFYVDvLGLHVSYEDeNQIYLRSFEefIHHNLVLTKGPv---AALKAMAFRVRTpeDVDKA 90
gi 206687525  13 NIVRLSHVEYAVTDLAASRAFYVDtLGLQVTHEDdSRIYLRAMEerGHHCIVLVQADt---ASVGVLGFKLYDepDLDKA 89
gi 41349767    1 MILRLGHAELFVTDLERAREFYVHiLGFRENDSDkEHIYLRGVDefDAHTLTLTKNSy---AGLGHFALRVSEheDLERL 77
gi 27378078   13 NIIRSSHVVLDVTDLKLSRAFYETtVGLHVEDADdKVVYLRAAEehQHHSLVLRKAAa---PACARLGFKVGNdkDLDKA 89
gi 15807888   20 DIIRIAQAVFTVSDLNASREFYVDlLGMNVLHEEsGALYLRGVEd-REWTLKLEQCRegelPRVRHLGYRVRDeaSLDTL 98
1F1R_A        14 DIVRCAYMEIVVTDLAKSREFYVDvLGLHVTEEDeNTIYLRSLEefIHHNLVLRQGPi---AAVAAFAYRVKSpaEVDAA 90
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
Feature 1                                                   #
1F1X_A        91 EAYYQELGCRTErrkdgfVKGIGDALRVEDPLGFPYEFFFETTH 134
gi 206687525  90 AEFFASKGLPVEwi---eRPHMGKTLRTRDPWGIPLEFYVKMDR 130
gi 41349767   78 ADQHKKLGIPCQlvpagvEPGQGMALRVIEPNGHPIEFYHEMQQ 121
gi 27378078   90 AAFLSENSLAYAfa---dQPFQGRTLQFTDPFGFQIELYAAMDK 130
gi 15807888   99 LALADAQGLPHRwe---eELDRPRMLRMQDPFGIPLAFYLEVKT 139
1F1R_A        91 EAYYKELGCRTErrkegfTKGIGDSVRVEDPLGFPYEFFYETEH 134

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