1ID2,1AAC


Conserved Protein Domain Family
Amicyanin

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cd13921: Amicyanin 
Click on image for an interactive view with Cn3D
Amicyanin is a type I blue copper protein that plays an essential role in electron transfer
In Paracoccus denitrificans bacteria, amicyanin acts as an intermediary of a three-member redox complex along with methylamine dehydrogenase (MADH) and cytochrome c-551i. The electron is transferred from the active site of MADH via the amicyanin copper ion to the cytochrome heme iron. The electron transfer from MADH to cytochrome c-551i does not involve a ternary complex but occurs via a ping-pong mechanism in which amicyanin uses the same interface for the reactions with MADH and cytochrome c-551i.
Statistics
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PSSM-Id: 259988
Aligned: 19 rows
Threshold Bit Score: 100.865
Created: 19-Dec-2012
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Type 1 (T1) Cu
Conserved site includes 4 residues -Click on image for an interactive view with Cn3D
Feature 1: Type 1 (T1) Cu binding site [ion binding site], 4 residue positions
Conserved feature residue pattern:H C H MClick to see conserved feature residue pattern help
Evidence:
  • Comment:Blue copper proteins are characterized by their conserved H...C...H...M copper ligands
  • Structure:1ID2; Paracoccus versutus Amicyanin binds to copper at T1 copper binding site.
    View structure with Cn3D
  • Citation:PMID 8120896

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                      #                                       #  #  #
1ID2_C     21 AVVVGIEkMKYLTPEVTIKAGETVYWVNGEvMPHNVAFKkgivgedAFRGEMMTkdqAYAITFNE-AGSYDYFCTPHPFM 99  Paracoccus versutus
NP_769655  32 DMDVHIDnFVFQPAELKIKVGATVTWTNRDdIPHTIVSAg------KFRSKTLDtddKFSFTFTN-AGDYKYFCSLHPHM 104 Bradyrhizobium jap...
AAV93576   28 PVVVDIRsFVFEPAEITIRAGETIVWINHDfAPHTATDDe-----vNWDTGELEkdaQAAIRFDT-PGTYPYFCAYHPHM 101 Silicibacter pomer...
AAQ61158   24 TQTVEISkFAFTPKEVTVAPGTKVAWVNHDeIPHTVSTRd-----kAFTSKALDtddRYEHVFDK-EGDYAYFCAVHPYM 97  Chromobacterium vi...
BAB53762   26 TIEVTIDkLVFSPATVEAKVGDTIEWVNNDvVAHTATVK-------GGWDVMIPpkkSASLTLKA-AGAVDYFCRFHPNM 97  Mesorhizobium loti...
NP_438046  26 TIQVAIDrLVYLPAEIEAKVGDEVEWINRDaLVHTATVE-------GGADVLLPankTGRLVLQE-AGSFDYICRYHPNM 97  Sinorhizobium meli...
BAB51265   20 NHAVQIKgMKFNPSKISVAVGDTITFTNADsMTHTATALd-----gSFDTGHLAtgkSAKVKVSA-AGAHPFHCAIHSSM 93  Mesorhizobium loti...
YP_110080  16 THTVAIEgMRFNPDSLTVERGDKIVWVNKDlVAHTATATaa----hAFDSHEIApnaSWAYVARS-PGRFAYVCALHPTM 90  Burkholderia pseud...
NP_631713  50 GTQVTIKdFTFEPASLTVSPGAKVTVVNKDsTTHTLTASkg----gSFDTGDIApgkSATFTAPStAGDFPYACTIHPFM 125 Streptomyces coeli...
BAC88121   28 ATVIAIEsFQFTPEAVVIPKGSRVTFLNKDaAPHTATPEedg-akfAGTGRLLAg-eSKTLTFPD-KGVYNYFCEFHTTM 104 Gloeobacter violac...
Feature 1            
1ID2_C    100 RGKVIVE 106 Paracoccus versutus
NP_769655 105 TGMIKVE 111 Bradyrhizobium japonicum USDA 110
AAV93576  102 TGTVIVT 108 Silicibacter pomeroyi DSS-3
AAQ61158   98 TGVVHVR 104 Chromobacterium violaceum ATCC 12472
BAB53762   98 RGHLDVS 104 Mesorhizobium loti MAFF303099
NP_438046  98 KGRITVR 104 Sinorhizobium meliloti 1021
BAB51265   94 KGIVTAK 100 Mesorhizobium loti MAFF303099
YP_110080  91 KANLIVK 97  Burkholderia pseudomallei K96243
NP_631713 126 KGTLTVE 132 Streptomyces coelicolor A3(2)
BAC88121  105 KGRVTVR 111 Gloeobacter violaceus PCC 7421

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