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UniProtKB/Swiss-Prot entry O64411

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PAO_MAIZE
Primary accession number O64411
Secondary accession numbers None
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on August 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 66)
Name and origin of the protein
Protein name Polyamine oxidase [Precursor]
Synonym EC 1.5.3.11
Gene name
Name: PAO
From
Zea mays (Maize) [TaxID: 4577] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; PACCAD clade; Panicoideae; Andropogoneae; Zea.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, AND PARTIAL PROTEIN SEQUENCE.
STRAIN=cv. Paolo;
TISSUE=Etiolated seedling;
DOI=10.1016/S0014-5793(98)00311-1; PubMed=9598979 [NCBI, ExPASy, EBI, Israel, Japan]
Tavladoraki P., Schinina M.E., Cecconi F., Di Agostino S., Manera F., Rea G., Mariottini P., Federico R., Angelini R.;
"Maize polyamine oxidase: primary structure from protein and cDNA sequencing.";
FEBS Lett. 426:62-66(1998).
[2]
 X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), AND CRYSTALLIZATION.
DOI=10.1107/S0907444998005836; PubMed=10089528 [NCBI, ExPASy, EBI, Israel, Japan]
Binda C., Coda A., Angelini R., Federico R., Ascenzi P., Mattevi A.;
"Crystallization and preliminary X-ray analysis of polyamine oxidase from Zea mays L.";
Acta Crystallogr. D 54:1429-1431(1998).
[3]
 X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 29-500 IN COMPLEXES WITH FAD AND SYNTHETIC INHIBITOR.
DOI=10.1016/S0969-2126(99)80037-9; PubMed=10368296 [NCBI, ExPASy, EBI, Israel, Japan]
Binda C., Coda A., Angelini R., Federico R., Ascenzi P., Mattevi A.;
"A 30-A-long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase.";
Structure 7:265-276(1999).
[4]
 X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 29-500 IN COMPLEXES WITH FAD AND SYNTHETIC INHIBITORS.
DOI=10.1021/bi002751j; PubMed=11258887 [NCBI, ExPASy, EBI, Israel, Japan]
Binda C., Angelini R., Federico R., Ascenzi P., Mattevi A.;
"Structural bases for inhibitor binding and catalysis in polyamine oxidase.";
Biochemistry 40:2766-2776(2001).
Comments
  • FUNCTION: Catalyzes the oxidation of the secondary amino group of polyamines (spermine, spermidine and their acetyl derivatives). Plays an important role in the regulation of polyamine intracellular concentration.
  • CATALYTIC ACTIVITY: N1-acetylspermine + O2 + H2O = N1-acetylspermidine + 3-aminopropanal + H2O2.
  • COFACTOR: FAD.
  • SIMILARITY: Belongs to the flavin monoamine oxidase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ002204; CAA05249.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T03387; T03387.
RefSeq NP_001105106.1; -.
UniGene Zm.300
3D structure databases
PDB
1B37; X-ray; 1.90 A; A/B/C=29-500.[ExPASy / RCSB / EBI]
1B5Q; X-ray; 1.90 A; A/B/C=29-500.[ExPASy / RCSB / EBI]
1H81; X-ray; 2.10 A; A/B/C=29-500.[ExPASy / RCSB / EBI]
1H82; X-ray; 1.90 A; A/B/C=29-500.[ExPASy / RCSB / EBI]
1H83; X-ray; 1.90 A; A/B/C=29-500.[ExPASy / RCSB / EBI]
1H84; X-ray; 2.00 A; A/B/C=29-500.[ExPASy / RCSB / EBI]
1H86; X-ray; 2.00 A; A/B/C=29-500.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1B37; -.
1B5Q; -.
1H81; -.
1H82; -.
1H83; -.
1H84; -.
1H86; -.
ModBase O64411.
Enzyme and pathway databases
BioCyc MetaCyc:MON-9461; -.
Organism-specific databases
Gramene O64411; -.
Ontologies
GO
GO:0009055; Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0046592; Molecular function: polyamine oxidase activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001613; Amineoxid_fl.
IPR002937; Amino_oxidase.
IPR001100; Pyr_nuc-diS_OxRdtase.
Graphical view of domain structure.
Pfam PF01593; Amino_oxidase; 1.
Pfam graphical view of domain structure.
PRINTS PR00757; AMINEOXDASEF.
PR00411; PNDRDTASEI.
Genome annotation databases
GeneID 541983; -.
Other
ProtoNet O64411.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; FAD; Flavoprotein; Glycoprotein; Oxidoreductase; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    28  28      
CHAIN   29   500  472     Polyamine oxidase. PRO_0000001712
NP_BIND   42    43  2     FAD. 
NP_BIND   87    88  2     FAD. 
NP_BIND   467   468  2     FAD. 
BINDING   63    63        FAD. 
BINDING   71    71        FAD; via amide nitrogen. 
BINDING   265   265        FAD; via amide nitrogen and carbonyl oxygen. 
BINDING   427   427        FAD. 
BINDING   458   458        FAD; via amide nitrogen. 
CARBOHYD   105   105        N-linked (GlcNAc...). 
DISULFID   485   491         
STRAND   35    38  4      
HELIX   42    53  12      
STRAND   59    62  4      
STRAND   64    69  6      
STRAND   74    77  4      
STRAND   80    85  6      
STRAND   88    96  9      
HELIX   100   105  6      
STRAND   112   114  3      
HELIX   120   122  3      
STRAND   127   131  5      
HELIX   134   156  23      
HELIX   168   176  9      
STRAND   178   181  4      
HELIX   185   194  10      
HELIX   196   199  4      
TURN   203   205  3      
STRAND   206   208  3      
TURN   209   211  3      
HELIX   215   220  6      
STRAND   222   227  6      
HELIX   235   242  8      
TURN   249   251  3      
STRAND   259   262  4      
STRAND   265   270  6      
STRAND   275   279  5      
STRAND   284   292  9      
HELIX   296   300  5      
STRAND   303   308  6      
HELIX   312   320  9      
STRAND   321   324  4      
STRAND   326   332  7      
STRAND   345   349  5      
STRAND   359   362  4      
TURN   364   366  3      
STRAND   372   378  7      
HELIX   379   386  8      
HELIX   390   404  15      
STRAND   414   417  4      
TURN   421   423  3      
TURN   425   427  3      
STRAND   428   433  6      
HELIX   440   447  8      
STRAND   453   455  3      
HELIX   458   460  3      
TURN   462   466  5      
HELIX   468   488  21      
Sequence information
Length: 500 AA [This is the length of the unprocessed precursor] Molecular weight: 56344 Da [This is the MW of the unprocessed precursor] CRC64: 00BB4BAF7A2E41CB [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSSSPSFGLL AVAALLLALS LAQHGSLAAT VGPRVIVVGA GMSGISAAKR LSEAGITDLL 

        70         80         90        100        110        120 
ILEATDHIGG RMHKTNFAGI NVELGANWVE GVNGGKMNPI WPIVNSTLKL RNFRSDFDYL 

       130        140        150        160        170        180 
AQNVYKEDGG VYDEDYVQKR IELADSVEEM GEKLSATLHA SGRDDMSILA MQRLNEHQPN 

       190        200        210        220        230        240 
GPATPVDMVV DYYKFDYEFA EPPRVTSLQN TVPLATFSDF GDDVYFVADQ RGYEAVVYYL 

       250        260        270        280        290        300 
AGQYLKTDDK SGKIVDPRLQ LNKVVREIKY SPGGVTVKTE DNSVYSADYV MVSASLGVLQ 

       310        320        330        340        350        360 
SDLIQFKPKL PTWKVRAIYQ FDMAVYTKIF LKFPRKFWPE GKGREFFLYA SSRRGYYGVW 

       370        380        390        400        410        420 
QEFEKQYPDA NVLLVTVTDE ESRRIEQQSD EQTKAEIMQV LRKMFPGKDV PDATDILVPR 

       430        440        450        460        470        480 
WWSDRFYKGT FSNWPVGVNR YEYDQLRAPV GRVYFTGEHT SEHYNGYVHG AYLSGIDSAE 

       490        500 
ILINCAQKKM CKYHVQGKYD
O64411 in FASTA format

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