1F1V,1F1X


Conserved Protein Domain Family
HPCD_C_class_II

?
cd07256: HPCD_C_class_II 
Click on image for an interactive view with Cn3D
C-terminal domain of 3,4-dihydroxyphenylacetate 2,3-dioxygenase (HPCD)
This subfamily contains the C-terminal, 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
?
PSSM-Id: 319919
View PSSM: cd07256
Aligned: 5 rows
Threshold Bit Score: 270.527
Threshold Setting Gi: 41349767
Created: 18-Mar-2009
Updated: 18-Aug-2016
Structure
?
Program:
Drawing:
Aligned Rows:
 
Conserved site includes 14 residues -Click on image for an interactive view with Cn3D
Feature 1:active site [active site]
Evidence:
  • Structure:1F1V_A; active site of Arthrobacter globiformis 3,4-dihydroxyphenylacetate 2,3-dioxygenase complexed with substrate 3,4-dihydroxyphenylacetate and Mn(II), by 4A distance.
    View structure with Cn3D
  • Citation:PMID 9047314

Sequence Alignment
?
Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1             # #                                    #       #             #             
1F1V_A       150 LVRLDHFNQVTpDVPRGRAYLED-LGFRVSEDIKDs-DGVTYAAWMHRKQTVHDTALTGGNGPRMHHVAFATHEKHNIIQ 227
1F1X_A       150 LVRLDHFNQVTpDVPRGRKYLED-LGFRVTEDIQDd-EGTTYAAWMHRKGTVHDTALTGGNGPRLHHVAFSTHEKHNIIQ 227
gi 206678606 147 PLRIDHFNCFSnDVDASVEFYSD-FGFRVTEYTEDdeSKKIWAAWMHRKGGVHDMAFTNGTGPRMHHVAFWVPTPLNIID 225
gi 15807888  155 LQRVDHCNVRVpDVKATLDWYGAeLGFRVSEYTVDe-QEQYWAAWIQRRGGVHDFALTNGAGPCLHHWAYWMPDAMSIIK 233
gi 41349767  147 PLRIDHVNLRVaNVDYALRYWRDeLNFSVSEYVER--DGETFAAWTRRFPGTHDVALVKANGPSLHHIAYTVQGPAEIIR 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                       #    # ##     #         # #                       #            # 
1F1V_A       228 ICDKMGALRISDRIERGPGRHGVSNAFYLYILDPDGHRIEIYTQDYYTgdpdnPTITWDVHDNQRRd--WWGNPVVPSWY 305
1F1X_A       228 ICDKMGALRISDRIERGPGRHGVSNAFYLYILDPDNHRIEIYTQDYYTgdpdnPTITWNVHDNQRRd--WWGNPVVPSWY 305
gi 206678606 226 LLDLMATTGYVDNIERGPGRHGISNAFFLYVLDPDGHRIEIYCSDYQTvdpdlEPIKWDLQDPQRQt--LWGAAAPRSWF 303
gi 15807888  234 TCDILAGARMPERIERGPGRHGVSNAFFLYIRDPDGHRIELYTSDYITvdpdfEPIRWLRDDPRRQt--LWGAKTPRSWF 311
gi 41349767  225 TADLLADAGYQDAIEFGPGRHGLSNAFFLYIRDPDGNRMEIYTGDYLRdl-dmPPIKWTWEEYDQKgrlWWGPSYPERFL 303

                 ....
Feature 1            
1F1V_A       306 TEAS 309
1F1X_A       306 TEAS 309
gi 206678606 304 EHGT 307
gi 15807888  312 EDAS 315
gi 41349767  304 ETSP 307

| Disclaimer | Privacy statement | Accessibility |
NCBI Home NCBI Search NCBI SiteMap