ID A0A1J0VV91_9NOCA Unreviewed; 400 AA.
AC A0A1J0VV91;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=S-adenosylmethionine decarboxylase proenzyme {ECO:0000256|HAMAP-Rule:MF_00464};
DE Short=AdoMetDC {ECO:0000256|HAMAP-Rule:MF_00464};
DE Short=SAMDC {ECO:0000256|HAMAP-Rule:MF_00464};
DE EC=4.1.1.50 {ECO:0000256|HAMAP-Rule:MF_00464};
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase beta chain {ECO:0000256|HAMAP-Rule:MF_00464};
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase alpha chain {ECO:0000256|HAMAP-Rule:MF_00464};
GN Name=speH {ECO:0000256|HAMAP-Rule:MF_00464};
GN Synonyms=speE {ECO:0000256|HAMAP-Rule:MF_00198};
GN ORFNames=BOX37_20610 {ECO:0000313|EMBL:APE35941.1};
OS Nocardia mangyaensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=2213200 {ECO:0000313|EMBL:APE35941.1, ECO:0000313|Proteomes:UP000183810};
RN [1] {ECO:0000313|EMBL:APE35941.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y48 {ECO:0000313|EMBL:APE35941.1};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the decarboxylation of S-adenosylmethionine to S-
CC adenosylmethioninamine (dcAdoMet), the propylamine donor required for
CC the synthesis of the polyamines spermine and spermidine from the
CC diamine putrescine. {ECO:0000256|HAMAP-Rule:MF_00464}.
CC -!- FUNCTION: Catalyzes the irreversible transfer of a propylamine group
CC from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to
CC putrescine (1,4-diaminobutane) to yield spermidine. {ECO:0000256|HAMAP-
CC Rule:MF_00198}.
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:0000256|HAMAP-Rule:MF_00464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) +
CC S-methyl-5'-thioadenosine + spermidine; Xref=Rhea:RHEA:12721,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:57443,
CC ChEBI:CHEBI:57834, ChEBI:CHEBI:326268; EC=2.5.1.16;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00198};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00464};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00464};
CC -!- PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine
CC biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine:
CC step 1/1. {ECO:0000256|HAMAP-Rule:MF_00464}.
CC -!- PATHWAY: Amine and polyamine biosynthesis; spermidine biosynthesis;
CC spermidine from putrescine: step 1/1. {ECO:0000256|HAMAP-
CC Rule:MF_00198}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged as a
CC dimer of alpha/beta heterodimers. {ECO:0000256|HAMAP-Rule:MF_00464}.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP-Rule:MF_00198}.
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:0000256|HAMAP-Rule:MF_00464}.
CC -!- SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 1
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00464}.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000256|ARBA:ARBA00007867, ECO:0000256|HAMAP-Rule:MF_00198}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00198}.
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DR EMBL; CP018082; APE35941.1; -; Genomic_DNA.
DR RefSeq; WP_071929129.1; NZ_CP018082.1.
DR AlphaFoldDB; A0A1J0VV91; -.
DR KEGG; nsl:BOX37_20610; -.
DR OrthoDB; 9793120at2; -.
DR UniPathway; UPA00248; UER00314.
DR UniPathway; UPA00331; UER00451.
DR Proteomes; UP000183810; Chromosome.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.60.90.10; S-adenosylmethionine decarboxylase; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_00464; AdoMetDC_1; 1.
DR HAMAP; MF_00198; Spermidine_synth; 1.
DR InterPro; IPR003826; AdoMetDC_fam_prok.
DR InterPro; IPR030374; PABS.
DR InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR InterPro; IPR017716; S-AdoMet_deCOase_pro-enz.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001045; Spermi_synthase.
DR NCBIfam; TIGR03330; SAM_DCase_Bsu; 1.
DR PANTHER; PTHR33866; S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME; 1.
DR PANTHER; PTHR33866:SF2; S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME; 1.
DR Pfam; PF02675; AdoMet_dc; 1.
DR Pfam; PF01564; Spermine_synth; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF56276; S-adenosylmethionine decarboxylase; 1.
DR PROSITE; PS51006; PABS_2; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813, ECO:0000256|HAMAP-
KW Rule:MF_00464};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW Rule:MF_00464};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00464};
KW Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115, ECO:0000256|HAMAP-
KW Rule:MF_00464};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|HAMAP-Rule:MF_00464};
KW Reference proteome {ECO:0000313|Proteomes:UP000183810};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00464};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_00464};
KW Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066, ECO:0000256|HAMAP-
KW Rule:MF_00464};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00198};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_00464}.
FT CHAIN 1..64
FT /note="S-adenosylmethionine decarboxylase beta chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT /id="PRO_5023534221"
FT CHAIN 65..400
FT /note="S-adenosylmethionine decarboxylase alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT /id="PRO_5023534220"
FT DOMAIN 117..366
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
FT ACT_SITE 65
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT ACT_SITE 70
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT ACT_SITE 85
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT ACT_SITE 280
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198,
FT ECO:0000256|PROSITE-ProRule:PRU00354"
FT BINDING 148
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT BINDING 178
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT BINDING 202
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT BINDING 221
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT BINDING 259..260
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00198"
FT SITE 64..65
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
FT MOD_RES 65
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00464"
SQ SEQUENCE 400 AA; 44246 MW; 0E3EE3741647C7F3 CRC64;
MTAEFTGWHV LAEFGGVDTD LCDDLERLES ALRESLVAAG VTICDVVHKK FEPQGVTVLA
LLSESHASIH TYPESGDIFV DVFTCGTIGA GATKAVDLLR DKLSPKEVRT KVVQRGHGAE
KIYEPVGEGL TRIWDLHEVI VDTNTPFQHM VIARTDQGIS LFSDDDRQST EFSQLTYHEA
MMVPAFVLAE KLDRVLIIGS GEGVASQMSV AAGATLVDHV DIDQREVELC ARHLPYGYTP
EELAAAVAGE GPIRVHYADG WDFLAKAQQA GTRYDVIVID LPDERVEDAQ HNRLYESEFL
SRCRALLAPG GVLSAQAGCA TLWRNETLKR SWGRFNAQFT TVVPYGSDEH EWTFLFGLNE
KIDDPVRGMT DRLALLPYRA ETIDARALER GAIEPYALRR
//
