1SQI,1CJX,2R5V,1SQD,1T47,1SP8,3ISQ,3ZGJ,5EC3,1SP9


Conserved Protein Domain Family
HPPD_N_like

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cd08342: HPPD_N_like 
Click on image for an interactive view with Cn3D
N-terminal domain of 4-hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate Synthase (HmaS)
HppD and HmaS are non-heme iron-dependent dioxygenases, which modify a common substrate, 4-hydroxyphenylpyruvate (HPP), but yield different products. HPPD catalyzes the second reaction in tyrosine catabolism, the conversion of HPP to homogentisate (2,5-dihydroxyphenylacetic acid, HG). HmaS converts HPP to 4-hydroxymandelate, a committed step in the formation of hydroxyphenylglycerine, a structural component of nonproteinogenic macrocyclic peptide antibiotics, such as vancomycin. If the emphasis is on catalytic chemistry, HPPD and HmaS are classified as members of a large family of alpha-keto acid dependent mononuclear non-heme iron oxygenases most of which require Fe(II), molecular oxygen, and an alpha-keto acid (typically alpha-ketoglutarate) to either oxygenate or oxidize a third substrate. Both enzymes are exceptions in that they require two, instead of three, substrates, do not use alpha-ketoglutarate, and incorporate both atoms of dioxygen into the aromatic product. Both HPPD and HmaS exhibit duplicate beta barrel topology in their N- and C-terminal domains which share sequence similarity, suggestive of a gene duplication. Each protein has only one catalytic site located in at the C-terminal domain. This HPPD_N_like domain represents the N-terminal domain.
Statistics
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PSSM-Id: 319930
View PSSM: cd08342
Aligned: 56 rows
Threshold Bit Score: 82.6423
Threshold Setting Gi: 159186203
Created: 11-Mar-2009
Updated: 18-Aug-2016
Structure
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Program:
Drawing:
Aligned Rows:
 
dimer interface
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
Feature 1:dimer interface [polypeptide binding site]
Evidence:
  • Structure:1SQI_A/B; dimer interface of 4- hydroxyphenylpyruvate dioxygenase from Rattus norvegicus, 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                     ### ##                      # #                                    
1SQI_A        19 FHSVTFWVGn--aKQAASFYCnkmGFEPLAYKgletgsrevVSHVIKQgkIVFVLCSalnpwnke--------------- 81
1SQD_A        26 FHHIEFWCGd--aTNVARRFSwglGMRFSAKSdlstgnmvhASYLLTSgdLRFLFTApyspslsageikptttasipsfd 103
1SP8_A        32 FHHVELWCAd--aASAAGRFSfglGAPLAARSdlstgnsahASLLLRSgsLSFLFTApyahgadaataalp------sfs 103
gi 159473192  38 FHHIDFWCGd--aTNTSKRFSyglGMPLVAKSdqstnnqlfASYVLRSndLVFTFTApysrkcasvsegvpl----rhyn 111
gi 168006779  39 FHHVEFWCGd--aSNTWRRFSwglGMHLVAKSdqttgnqtyCSYAIQSneLVFAFTApysstidqtntkmph----pgyk 112
gi 262101174  31 FHHIEFYCAd--aTNASRRFAwglGMAQIGKSdqstgnhvsASYVIQSgeVKLVFTApyaletekapdavss---isgyd 105
gi 221535391 291 FEFVEFTADevsgAQLADMLSa-mCFRMERKHvs------kSVALWRQgaINIVVNTekegfa----------------- 346
gi 214045783 291 VSFVEFATRgeeaEALEAILDt-lGFQHSGTHia------kKLSLWTQgdIRIVINRetsgya----------------- 346
1SP9_A        47 FHHIEFWCGd--aTNVARRFSwglGMRFSAKSdlstgnmvhASYLLTSgdLRFLFTApyspslsageikptttasipsfd 124
gi 74751942    8 LCHIAFHVPa--gQPLARNLQrlfGFQPLASRevd----gwRQLALRSgdAVFLVNEgagsgepl--------------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                    #                                                                   
1SQI_A        82 ---mgdhlvkHGDGVKDIAFEVEDcEHIVQKARERGAKIVRepwvee--dkfgkVKFAVLQTYg-DTTHTLVEkinyt-- 153
1SQD_A       104 hgscrsffssHGLGVRAVAIEVEDaESAFSISVANGAIPSSppiv-----lneaVTIAEVKLYg-DVVLRYVSykaedte 177
1SP8_A       104 aaaarrfaadHGLAVRAVALRVADaEDAFRASVAAGARPAFgpvd-----lgrgFRLAEVELYg-DVVLRYVSypdgaa- 176
gi 159473192 112 idhayefinsHGLAVRAVGLLVDDaKTAYEVSVAHGAKGVLppvelrdeasgtsQVISEVLLYg-EVVLRYVSgsfqg-- 188
gi 168006779 113 sdearsftdsHGLAVRAVGILVDDaDEAFRISVEHGAVSVLephvlsddakggkMVMAEVKLYg-DVVLRYVSeqgyk-- 189
gi 262101174 106 pefaqkfvmkHGLAVRAVGILVGDaKAAYELSVQNGGVGVVepqtltdkesgktTTVSEVKLYg-DVVIRWVSgdfeg-- 182
gi 221535391 347 ----hsaflgHGPSVCDMGLRVKDaDQTVQRATALGAPDFSqpvg------tgeLDIPAIRGVg-GNVVHFIDeksdlh- 414
gi 214045783 347 ----ssayttHGTTVCDIGISVDAaAKTVSRAKSLGADPFEqaig------pgeLNIPAIRGQs-GSVLHFIDktsgls- 414
1SP9_A       125 hgscrsffssHGLGVRAVAIEVEDaESAFSISVANGAIPSSppiv-----lneaVTIAEVKLYg-DVVLRYVSykaedte 198
gi 74751942   67 ---ygldprhAVPSATNLCFDVADaGAATRELAALGCSVPVppvrvr--daqgaATYAVVSSPagILSLTLLEragyr-- 139
                        170
                 ....*....|
Feature 1                  
1SQI_A       154 -grflpGFEA 162
1SQD_A       178 kseflpGFER 187
1SP8_A       177 gepflpGFEG 186
gi 159473192 189 --pflaGYTP 196
gi 168006779 190 -gsmlpNYEE 198
gi 262101174 183 --pfvpGYEK 190
gi 221535391 415 -rvwdiEFEP 423
gi 214045783 415 -dvwsvEFIK 423
1SP9_A       199 kseflpGFER 208
gi 74751942  140 -gpflpGFRP 148

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