DCAM_HUMAN
ID DCAM_HUMAN Reviewed; 334 AA.
AC P17707; E1P5F7; Q5VXN4; Q5VXN6; Q9BWK4;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=S-adenosylmethionine decarboxylase proenzyme;
DE Short=AdoMetDC;
DE Short=SAMDC;
DE EC=4.1.1.50 {ECO:0000269|PubMed:10029540, ECO:0000269|PubMed:10574985, ECO:0000269|PubMed:11583147, ECO:0000269|PubMed:1917972, ECO:0000269|PubMed:2460457, ECO:0000269|PubMed:2687270};
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase alpha chain;
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase beta chain;
DE Flags: Precursor;
GN Name=AMD1; Synonyms=AMD;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, CATALYTIC
RP ACTIVITY, PROTEOLYTIC CLEAVAGE, AND PYRUVATE FORMATION AT SER-68.
RX PubMed=2460457; DOI=10.1016/s0021-9258(18)37495-7;
RA Pajunen A., Crozat A., Jaenne O.A., Ihalainen R., Laitinen P.H.,
RA Stanley B., Madhubala R., Pegg A.E.;
RT "Structure and regulation of mammalian S-adenosylmethionine
RT decarboxylase.";
RL J. Biol. Chem. 263:17040-17049(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Heart;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP CATALYTIC ACTIVITY, PROTEOLYTIC CLEAVAGE, PYRUVATE FORMATION AT SER-68, AND
RP MUTAGENESIS OF SER-50; SER-66; SER-68 AND SER-69.
RX PubMed=2687270; DOI=10.1016/s0021-9258(19)30047-x;
RA Stanley B.A., Pegg A.E., Holm I.;
RT "Site of pyruvate formation and processing of mammalian S-
RT adenosylmethionine decarboxylase proenzyme.";
RL J. Biol. Chem. 264:21073-21079(1989).
RN [7]
RP MUTAGENESIS.
RX PubMed=1917972; DOI=10.1016/s0021-9258(18)55089-4;
RA Stanley B.A., Pegg A.E.;
RT "Amino acid residues necessary for putrescine stimulation of human S-
RT adenosylmethionine decarboxylase proenzyme processing and catalytic
RT activity.";
RL J. Biol. Chem. 266:18502-18506(1991).
RN [8]
RP CATALYTIC ACTIVITY, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF SER-229 AND
RP HIS-243.
RX PubMed=10574985; DOI=10.1074/jbc.274.49.35059;
RA Xiong H., Pegg A.E.;
RT "Mechanistic studies of the processing of human S-adenosylmethionine
RT decarboxylase proenzyme. Isolation of an ester intermediate.";
RL J. Biol. Chem. 274:35059-35066(1999).
RN [9]
RP CATALYTIC ACTIVITY, INHIBITION BY IODOACETIC ACID, AND MUTAGENESIS OF
RP CYS-82.
RX PubMed=10029540; DOI=10.1021/bi9825201;
RA Xiong H., Stanley B.A., Pegg A.E.;
RT "Role of cysteine-82 in the catalytic mechanism of human S-
RT adenosylmethionine decarboxylase.";
RL Biochemistry 38:2462-2470(1999).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
RX PubMed=10378277; DOI=10.1016/s0969-2126(99)80074-4;
RA Ekstrom J.L., Mathews I.I., Stanley B.A., Pegg A.E., Ealick S.E.;
RT "The crystal structure of human S-adenosylmethionine decarboxylase at 2.25-
RT A resolution reveals a novel fold.";
RL Structure 7:583-595(1999).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), CATALYTIC ACTIVITY, COFACTOR,
RP REACTION MECHANISM, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF PHE-7 AND
RP PHE-223.
RX PubMed=11583147; DOI=10.1021/bi010735w;
RA Tolbert W.D., Ekstrom J.L., Mathews I.I., Secrist J.A. III, Kapoor P.,
RA Pegg A.E., Ealick S.E.;
RT "The structural basis for substrate specificity and inhibition of human S-
RT adenosylmethionine decarboxylase.";
RL Biochemistry 40:9484-9494(2001).
CC -!- FUNCTION: Essential for biosynthesis of the polyamines spermidine and
CC spermine. Promotes maintenance and self-renewal of embryonic stem
CC cells, by maintaining spermine levels. {ECO:0000250|UniProtKB:P0DMN7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-
CC (methylsulfanyl)propylamine; Xref=Rhea:RHEA:15981, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57443, ChEBI:CHEBI:59789; EC=4.1.1.50;
CC Evidence={ECO:0000269|PubMed:10029540, ECO:0000269|PubMed:10574985,
CC ECO:0000269|PubMed:11583147, ECO:0000269|PubMed:1917972,
CC ECO:0000269|PubMed:2460457, ECO:0000269|PubMed:2687270};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000269|PubMed:11583147};
CC Note=Binds 1 pyruvoyl group covalently per subunit.
CC {ECO:0000269|PubMed:11583147};
CC -!- ACTIVITY REGULATION: Both proenzyme processing and catalytic activity
CC are stimulated by putrescine. Catalytic activity is inhibited by
CC iodoacetic acid.
CC -!- PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine
CC biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine:
CC step 1/1. {ECO:0000269|PubMed:10029540, ECO:0000269|PubMed:10574985,
CC ECO:0000269|PubMed:11583147, ECO:0000269|PubMed:1917972,
CC ECO:0000269|PubMed:2460457, ECO:0000269|PubMed:2687270}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC {ECO:0000269|PubMed:11583147}.
CC -!- INTERACTION:
CC P17707; P17707: AMD1; NbExp=3; IntAct=EBI-6872827, EBI-6872827;
CC P17707; Q8WY91: THAP4; NbExp=3; IntAct=EBI-6872827, EBI-726691;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P17707-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P17707-2; Sequence=VSP_043209;
CC -!- PTM: Is synthesized initially as an inactive proenzyme. Formation of
CC the active enzyme involves a self-maturation process in which the
CC active site pyruvoyl group is generated from an internal serine residue
CC via an autocatalytic post-translational modification. Two non-identical
CC subunits are generated from the proenzyme in this reaction, and the
CC pyruvate is formed at the N-terminus of the alpha chain, which is
CC derived from the carboxyl end of the proenzyme. The post-translation
CC cleavage follows an unusual pathway, termed non-hydrolytic serinolysis,
CC in which the side chain hydroxyl group of the serine supplies its
CC oxygen atom to form the C-terminus of the beta chain, while the
CC remainder of the serine residue undergoes an oxidative deamination to
CC produce ammonia and the pyruvoyl group blocking the N-terminus of the
CC alpha chain. {ECO:0000269|PubMed:10574985, ECO:0000269|PubMed:1917972,
CC ECO:0000269|PubMed:2460457, ECO:0000269|PubMed:2687270}.
CC -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC family. {ECO:0000305}.
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DR EMBL; M21154; AAA51716.1; -; mRNA.
DR EMBL; AL832698; CAI46113.1; -; mRNA.
DR EMBL; AL357515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL365206; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48307.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48308.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48309.1; -; Genomic_DNA.
DR EMBL; BC000171; AAH00171.1; -; mRNA.
DR CCDS; CCDS5086.1; -. [P17707-1]
DR PIR; A31786; DCHUDM.
DR RefSeq; NP_001625.2; NM_001634.5. [P17707-1]
DR PDB; 1I72; X-ray; 2.00 A; A=68-334, B=1-67.
DR PDB; 1I79; X-ray; 2.01 A; A=68-334, B=1-67.
DR PDB; 1I7B; X-ray; 1.90 A; A=68-334, B=1-67.
DR PDB; 1I7C; X-ray; 2.40 A; A=68-334, B=1-67.
DR PDB; 1I7M; X-ray; 2.24 A; A/C=68-334, B/D=1-67.
DR PDB; 1JEN; X-ray; 2.25 A; A/C=69-334, B/D=1-67.
DR PDB; 1JL0; X-ray; 1.50 A; A/B=1-334.
DR PDB; 1MSV; X-ray; 1.75 A; A/B=1-334.
DR PDB; 3DZ2; X-ray; 1.86 A; A=69-334, B=1-67.
DR PDB; 3DZ3; X-ray; 2.62 A; A=69-334, B=1-67.
DR PDB; 3DZ4; X-ray; 1.84 A; A=69-334, B=1-67.
DR PDB; 3DZ5; X-ray; 2.43 A; A=69-334, B=1-67.
DR PDB; 3DZ6; X-ray; 1.83 A; A=69-334, B=1-67.
DR PDB; 3DZ7; X-ray; 1.91 A; A=69-334, B=1-67.
DR PDB; 3EP3; X-ray; 1.84 A; A=69-328, B=1-67.
DR PDB; 3EP4; X-ray; 1.89 A; A=69-328, B=1-67.
DR PDB; 3EP5; X-ray; 1.99 A; A=69-328, B=1-67.
DR PDB; 3EP6; X-ray; 1.70 A; A=69-328, B=1-67.
DR PDB; 3EP7; X-ray; 2.00 A; A=69-328, B=1-67.
DR PDB; 3EP8; X-ray; 1.97 A; A=69-328, B=1-67.
DR PDB; 3EP9; X-ray; 2.35 A; A=69-328, B=1-67.
DR PDB; 3EPA; X-ray; 2.10 A; A=69-328, B=1-67.
DR PDB; 3EPB; X-ray; 1.75 A; A=69-328, B=1-67.
DR PDB; 3H0V; X-ray; 2.24 A; A=69-334, B=1-67.
DR PDB; 3H0W; X-ray; 1.81 A; A=69-334, B=1-67.
DR PDBsum; 1I72; -.
DR PDBsum; 1I79; -.
DR PDBsum; 1I7B; -.
DR PDBsum; 1I7C; -.
DR PDBsum; 1I7M; -.
DR PDBsum; 1JEN; -.
DR PDBsum; 1JL0; -.
DR PDBsum; 1MSV; -.
DR PDBsum; 3DZ2; -.
DR PDBsum; 3DZ3; -.
DR PDBsum; 3DZ4; -.
DR PDBsum; 3DZ5; -.
DR PDBsum; 3DZ6; -.
DR PDBsum; 3DZ7; -.
DR PDBsum; 3EP3; -.
DR PDBsum; 3EP4; -.
DR PDBsum; 3EP5; -.
DR PDBsum; 3EP6; -.
DR PDBsum; 3EP7; -.
DR PDBsum; 3EP8; -.
DR PDBsum; 3EP9; -.
DR PDBsum; 3EPA; -.
DR PDBsum; 3EPB; -.
DR PDBsum; 3H0V; -.
DR PDBsum; 3H0W; -.
DR AlphaFoldDB; P17707; -.
DR SMR; P17707; -.
DR BioGRID; 106759; 52.
DR DIP; DIP-363N; -.
DR IntAct; P17707; 28.
DR MINT; P17707; -.
DR STRING; 9606.ENSP00000357880; -.
DR BindingDB; P17707; -.
DR ChEMBL; CHEMBL4181; -.
DR DrugBank; DB08163; 5'-{[4-(aminooxy)butyl](methyl)amino}-5'-deoxy-8-ethenyladenosine.
DR DrugBank; DB00118; Ademetionine.
DR DrugBank; DB01917; Putrescine.
DR iPTMnet; P17707; -.
DR PhosphoSitePlus; P17707; -.
DR BioMuta; AMD1; -.
DR DMDM; 116241324; -.
DR EPD; P17707; -.
DR jPOST; P17707; -.
DR MassIVE; P17707; -.
DR MaxQB; P17707; -.
DR PaxDb; P17707; -.
DR PeptideAtlas; P17707; -.
DR PRIDE; P17707; -.
DR ProteomicsDB; 53510; -. [P17707-1]
DR ProteomicsDB; 53511; -. [P17707-2]
DR Antibodypedia; 32343; 218 antibodies from 29 providers.
DR DNASU; 262; -.
DR Ensembl; ENST00000368882.8; ENSP00000357877.5; ENSG00000123505.19. [P17707-1]
DR Ensembl; ENST00000368885.8; ENSP00000357880.3; ENSG00000123505.19. [P17707-1]
DR GeneID; 262; -.
DR KEGG; hsa:262; -.
DR MANE-Select; ENST00000368885.8; ENSP00000357880.3; NM_001634.6; NP_001625.2.
DR UCSC; uc003puk.3; human. [P17707-1]
DR CTD; 262; -.
DR DisGeNET; 262; -.
DR GeneCards; AMD1; -.
DR HGNC; HGNC:457; AMD1.
DR HPA; ENSG00000123505; Tissue enhanced (prostate).
DR MalaCards; AMD1; -.
DR MIM; 180980; gene.
DR neXtProt; NX_P17707; -.
DR OpenTargets; ENSG00000123505; -.
DR PharmGKB; PA24763; -.
DR VEuPathDB; HostDB:ENSG00000123505; -.
DR eggNOG; KOG0788; Eukaryota.
DR GeneTree; ENSGT00390000011776; -.
DR HOGENOM; CLU_023050_1_0_1; -.
DR InParanoid; P17707; -.
DR OMA; LEIWFEE; -.
DR PhylomeDB; P17707; -.
DR TreeFam; TF313561; -.
DR BRENDA; 4.1.1.50; 2681.
DR PathwayCommons; P17707; -.
DR Reactome; R-HSA-351202; Metabolism of polyamines.
DR SABIO-RK; P17707; -.
DR SignaLink; P17707; -.
DR UniPathway; UPA00331; UER00451.
DR BioGRID-ORCS; 262; 265 hits in 1076 CRISPR screens.
DR ChiTaRS; AMD1; human.
DR EvolutionaryTrace; P17707; -.
DR GenomeRNAi; 262; -.
DR Pharos; P17707; Tchem.
DR PRO; PR:P17707; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P17707; protein.
DR Bgee; ENSG00000123505; Expressed in secondary oocyte and 209 other tissues.
DR ExpressionAtlas; P17707; baseline and differential.
DR Genevisible; P17707; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019810; F:putrescine binding; IBA:GO_Central.
DR GO; GO:0006595; P:polyamine metabolic process; TAS:Reactome.
DR GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IEA:Ensembl.
DR GO; GO:0008295; P:spermidine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006597; P:spermine biosynthetic process; IBA:GO_Central.
DR InterPro; IPR001985; S-AdoMet_decarboxylase.
DR InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR InterPro; IPR018166; S-AdoMet_deCO2ase_CS.
DR PANTHER; PTHR11570; PTHR11570; 1.
DR Pfam; PF01536; SAM_decarbox; 1.
DR PIRSF; PIRSF001355; S-AdenosylMet_decarboxylase; 1.
DR SUPFAM; SSF56276; SSF56276; 1.
DR TIGRFAMs; TIGR00535; SAM_DCase; 1.
DR PROSITE; PS01336; ADOMETDC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Autocatalytic cleavage; Decarboxylase;
KW Direct protein sequencing; Lyase; Phosphoprotein; Polyamine biosynthesis;
KW Pyruvate; Reference proteome; S-adenosyl-L-methionine; Schiff base;
KW Spermidine biosynthesis; Zymogen.
FT CHAIN 1..67
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /id="PRO_0000029959"
FT CHAIN 68..334
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /id="PRO_0000029960"
FT ACT_SITE 8
FT /evidence="ECO:0000269|PubMed:1917972"
FT ACT_SITE 11
FT /evidence="ECO:0000269|PubMed:1917972"
FT ACT_SITE 68
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000269|PubMed:11583147"
FT ACT_SITE 82
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000269|PubMed:10029540,
FT ECO:0000269|PubMed:11583147"
FT ACT_SITE 229
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000269|PubMed:11583147"
FT ACT_SITE 243
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000269|PubMed:11583147"
FT BINDING 7
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11583147"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11583147"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11583147"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:11583147"
FT SITE 67..68
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000269|PubMed:2460457,
FT ECO:0000269|PubMed:2687270"
FT MOD_RES 68
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000269|PubMed:2460457,
FT ECO:0000269|PubMed:2687270"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..148
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_043209"
FT MUTAGEN 7
FT /note="F->A: No effect."
FT /evidence="ECO:0000269|PubMed:11583147"
FT MUTAGEN 8
FT /note="E->Q: Loss of activity. Normal putrescine-stimulated
FT processing."
FT /evidence="ECO:0000269|PubMed:10029540,
FT ECO:0000269|PubMed:1917972"
FT MUTAGEN 11
FT /note="E->Q: Loss of activity. Loss of putrescine-
FT stimulated processing."
FT /evidence="ECO:0000269|PubMed:1917972"
FT MUTAGEN 15
FT /note="E->Q: Little effect."
FT /evidence="ECO:0000269|PubMed:1917972"
FT MUTAGEN 49
FT /note="C->A: Little effect."
FT /evidence="ECO:0000269|PubMed:1917972"
FT MUTAGEN 50
FT /note="S->A: 17 percent decrease in catalytic activity. No
FT effect on processing."
FT /evidence="ECO:0000269|PubMed:2687270"
FT MUTAGEN 61
FT /note="E->Q: Little effect."
FT /evidence="ECO:0000269|PubMed:1917972"
FT MUTAGEN 66
FT /note="S->A: 38 percent decrease in catalytic activity.
FT Slight reduction in processing."
FT /evidence="ECO:0000269|PubMed:2687270"
FT MUTAGEN 67
FT /note="E->Q: Little effect."
FT /evidence="ECO:0000269|PubMed:1917972"
FT MUTAGEN 68..69
FT /note="SS->II: Loss of catalytic activity and processing."
FT /evidence="ECO:0000269|PubMed:2687270"
FT MUTAGEN 68
FT /note="S->A: Loss of catalytic activity and processing."
FT /evidence="ECO:0000269|PubMed:2687270"
FT MUTAGEN 69
FT /note="S->A: 24 percent decrease in catalytic activity.
FT Slight reduction in processing."
FT /evidence="ECO:0000269|PubMed:2687270"
FT MUTAGEN 80
FT /note="K->A: Greatly reduced catalytic activity. No
FT putrescine-stimulated processing."
FT /evidence="ECO:0000269|PubMed:1917972"
FT MUTAGEN 82
FT /note="C->A: Loss of activity. Greatly reduced putrescine-
FT stimulated processing."
FT /evidence="ECO:0000269|PubMed:1917972"
FT MUTAGEN 223
FT /note="F->A: No effect."
FT /evidence="ECO:0000269|PubMed:11583147"
FT MUTAGEN 226
FT /note="C->A: Little effect."
FT /evidence="ECO:0000269|PubMed:1917972"
FT MUTAGEN 229
FT /note="S->A: Loss of processing."
FT /evidence="ECO:0000269|PubMed:10574985"
FT MUTAGEN 229
FT /note="S->C: Greatly reduced processing."
FT /evidence="ECO:0000269|PubMed:10574985"
FT MUTAGEN 229
FT /note="S->T: Greatly reduced catalytic activity but little
FT effect on processing."
FT /evidence="ECO:0000269|PubMed:10574985"
FT MUTAGEN 243
FT /note="H->A: Greatly reduced catalytic activity and
FT processing."
FT /evidence="ECO:0000269|PubMed:10574985"
FT MUTAGEN 243
FT /note="H->E: Greatly reduced catalytic activity and
FT processing."
FT /evidence="ECO:0000269|PubMed:10574985"
FT MUTAGEN 243
FT /note="H->F: Loss of processing."
FT /evidence="ECO:0000269|PubMed:10574985"
FT MUTAGEN 243
FT /note="H->Y: Loss of processing."
FT /evidence="ECO:0000269|PubMed:10574985"
FT MUTAGEN 247
FT /note="E->Q: Little effect."
FT /evidence="ECO:0000269|PubMed:1917972"
FT MUTAGEN 249
FT /note="E->Q: Little effect."
FT /evidence="ECO:0000269|PubMed:1917972"
FT CONFLICT 146
FT /note="A -> G (in Ref. 1; AAA51716)"
FT /evidence="ECO:0000305"
FT STRAND 12..19
FT /evidence="ECO:0007829|PDB:1JL0"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:1JL0"
FT HELIX 37..45
FT /evidence="ECO:0007829|PDB:1JL0"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:1JL0"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:1JL0"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:1JL0"
FT STRAND 68..81
FT /evidence="ECO:0007829|PDB:1JL0"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:1JL0"
FT HELIX 91..102
FT /evidence="ECO:0007829|PDB:1JL0"
FT STRAND 106..115
FT /evidence="ECO:0007829|PDB:1JL0"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1JL0"
FT HELIX 130..138
FT /evidence="ECO:0007829|PDB:1JL0"
FT STRAND 142..150
FT /evidence="ECO:0007829|PDB:1JL0"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:1JL0"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:1JL0"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:1JL0"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:1JL0"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:1JL0"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:1JEN"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:1JL0"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:1JL0"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:1JL0"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:1JL0"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:1JL0"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:3H0W"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:1JL0"
FT HELIX 265..275
FT /evidence="ECO:0007829|PDB:1JL0"
FT STRAND 278..287
FT /evidence="ECO:0007829|PDB:1JL0"
FT HELIX 291..296
FT /evidence="ECO:0007829|PDB:3EPB"
FT STRAND 305..314
FT /evidence="ECO:0007829|PDB:1JL0"
FT STRAND 316..327
FT /evidence="ECO:0007829|PDB:1JL0"
SQ SEQUENCE 334 AA; 38340 MW; 1BB433AF412C9179 CRC64;
MEAAHFFEGT EKLLEVWFSR QQPDANQGSG DLRTIPRSEW DILLKDVQCS IISVTKTDKQ
EAYVLSESSM FVSKRRFILK TCGTTLLLKA LVPLLKLARD YSGFDSIQSF FYSRKNFMKP
SHQGYPHRNF QEEIEFLNAI FPNGAAYCMG RMNSDCWYLY TLDFPESRVI SQPDQTLEIL
MSELDPAVMD QFYMKDGVTA KDVTRESGIR DLIPGSVIDA TMFNPCGYSM NGMKSDGTYW
TIHITPEPEF SYVSFETNLS QTSYDDLIRK VVEVFKPGKF VTTLFVNQSS KCRTVLASPQ
KIEGFKRLDC QSAMFNDYNF VFTSFAKKQQ QQQS
