1PHZ


Conserved Protein Domain Family
ACT_AAAH

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cd04904: ACT_AAAH 
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ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH)
ACT domain of the nonheme iron-dependent, aromatic amino acid hydroxylases (AAAH): Phenylalanine hydroxylases (PAH), tyrosine hydroxylases (TH) and tryptophan hydroxylases (TPH), both peripheral (TPH1) and neuronal (TPH2) enzymes. This family of enzymes shares a common catalytic mechanism, in which dioxygen is used by an active site containing a single, reduced iron atom to hydroxylate an unactivated aromatic substrate, concomitant with a two-electron oxidation of tetrahydropterin (BH4) cofactor to its quinonoid dihydropterin form. PAH catalyzes the hydroxylation of L-Phe to L-Tyr, the first step in the catabolic degradation of L-Phe; TH catalyses the hydroxylation of L-Tyr to 3,4-dihydroxyphenylalanine, the rate limiting step in the biosynthesis of catecholamines; and TPH catalyses the hydroxylation of L-Trp to 5-hydroxytryptophan, the rate limiting step in the biosynthesis of 5-hydroxytryptamine (serotonin) and the first reaction in the synthesis of melatonin. Eukaryotic AAAHs have an N-terminal ACT (regulatory) domain, a middle catalytic domain and a C-terminal domain which is responsible for the oligomeric state of the enzyme forming a domain-swapped tetrameric coiled-coil. The PAH, TH, and TPH enzymes contain highly conserved catalytic domains but distinct N-terminal ACT domains (this CD) and differ in their mechanisms of regulation. One commonality is that all three eukaryotic enzymes are regulated in part by the phosphorylation of serine residues N-terminal of the ACT domain. Members of this CD belong to the superfamily of ACT regulatory domains.
Statistics
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PSSM-Id: 153176
View PSSM: cd04904
Aligned: 31 rows
Threshold Bit Score: 86.4585
Threshold Setting Gi: 4883767
Created: 9-Aug-2005
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
putative amino
Conserved site includes 8 residues -Click on image for an interactive view with Cn3D
Feature 1:putative amino acid binding site [chemical binding site]
Evidence:
  • Comment:based on sequence similarity to and mutational studies on phenylalanine hydroxylase and prephenate dehydratase

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                     ####                ####                                           
1PHZ_A        35 ISLIFSLKe--eVGALAKVLRLFEENDINLTHIESRPSRln----kDEYEFFTYLDkr-tKPVLGSIIKSLRNd--iGAT 105 Norway rat
NP_990136     76 LNLFFMLKga-kTSPLSRALKVFETFEAKIHHLETRLSRkpr-egtAELEYFVRCEv--hSSDLNTFISSIKRv---AED 148 chicken
AAD31643      30 TTIVFTLRe--kAGALAETLKLFQAHDVNLSHIESRPSRlm----kDAMRCSLNLLklktIVRLKELLSISNKklkrRFL 103 nematode
NP_954986    113 LNLLFSPRat-kPSALSRAVKVFETFEAKIHHLETRPAQrpr-aggPHLEYFVRLEv--rRGDLAALLSGVRQv---SED 185 human
AAR23931      74 VSLLFSLKgs-kPSSLSRTLKVFETFEAKIQHLETRPGRksv-gtaEELEYFVRCEv--hRSDLSTLMSSVRRv---CED 146 African clawed ...
NP_001001829  55 LNILFALKne-kNAGFFKAGKVFETFETKLLHLESRASRkskrssgEDLEFFMRCEv--hCSDTDIFINSLKRv---ADD 128 zebrafish
CAA53802      88 AALVVRLKe--gISSLGRILKAIETFHGTVQHVESRQSRve----gVDHDVLIKLDm--tRGNLLQLIRSLRQsg-sFSS 158 fruit fly
AAW47987      88 AALVLRLRe--gIGSLARILKTIENFKGTVTHVESRPSKke----gLQFDVLVKVDm--tRQYLLQLIRNLRQss-aLDG 158 honey bee
XP_001373552  58 MTVLFSLG----KTSLSRIAQVFESFEAKIHHLETRPAPkak-ntlHPLEVFMKFEi--hNSGINLLINSLRKv---VED 127 gray short-tail...
XP_786206    106 FTVTFSSKedmgFGSLSEALRVFQKRKVTLTHVESRPSNki----dGQIEFLMQCEt--kGSSSKNVLTALQKv---ADN 176 purple urchin
Feature 1             
1PHZ_A       106 VHELS 110 Norway rat
NP_990136    149 VRTTK 153 chicken
AAD31643     104 FKTGT 108 nematode
NP_954986    186 VRSPA 190 human
AAR23931     147 VRSTR 151 African clawed frog
NP_001001829 129 VRIVQ 133 zebrafish
CAA53802     159 MNLMA 163 fruit fly
AAW47987     159 VTLLA 163 honey bee
XP_001373552 128 VKIHW 132 gray short-tailed opossum
XP_786206    177 VRLEK 181 purple urchin

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