SPSY_BOVIN
ID SPSY_BOVIN Reviewed; 365 AA.
AC Q3SZA5; A1L596;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Spermine synthase;
DE Short=SPMSY;
DE EC=2.5.1.22 {ECO:0000250|UniProtKB:P52788};
DE AltName: Full=Spermidine aminopropyltransferase;
GN Name=SMS;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the production of spermine from spermidine and
CC decarboxylated S-adenosylmethionine (dcSAM).
CC {ECO:0000250|UniProtKB:P52788}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = H(+) +
CC S-methyl-5'-thioadenosine + spermine; Xref=Rhea:RHEA:19973,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:45725,
CC ChEBI:CHEBI:57443, ChEBI:CHEBI:57834; EC=2.5.1.22;
CC Evidence={ECO:0000250|UniProtKB:P52788};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19974;
CC Evidence={ECO:0000250|UniProtKB:P52788};
CC -!- PATHWAY: Amine and polyamine biosynthesis; spermine biosynthesis;
CC spermine from spermidine: step 1/1. {ECO:0000250|UniProtKB:P52788}.
CC -!- SUBUNIT: Homodimer. Dimerization is mediated through the N-terminal
CC domain and seems to be required for activity as deletion of the N-
CC terminal domain causes complete loss of activity.
CC {ECO:0000250|UniProtKB:P52788}.
CC -!- DOMAIN: Composed of 3 domains: the N-terminal domain has structural
CC similarity to S-adenosylmethionine decarboxylase, the central domain is
CC made up of four beta strands and the C-terminal domain is similar in
CC structure to spermidine synthase. The N- and C-terminal domains are
CC both required for activity. {ECO:0000250|UniProtKB:P52788}.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000305}.
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DR EMBL; BT029883; ABM21558.1; -; mRNA.
DR EMBL; BC103012; AAI03013.1; -; mRNA.
DR RefSeq; NP_001030548.1; NM_001035471.1.
DR AlphaFoldDB; Q3SZA5; -.
DR SMR; Q3SZA5; -.
DR STRING; 9913.ENSBTAP00000024458; -.
DR PaxDb; Q3SZA5; -.
DR PRIDE; Q3SZA5; -.
DR Ensembl; ENSBTAT00000081528; ENSBTAP00000071420; ENSBTAG00000018382.
DR GeneID; 615950; -.
DR KEGG; bta:615950; -.
DR CTD; 6611; -.
DR VEuPathDB; HostDB:ENSBTAG00000018382; -.
DR VGNC; VGNC:35035; SMS.
DR eggNOG; KOG1562; Eukaryota.
DR GeneTree; ENSGT00870000136506; -.
DR HOGENOM; CLU_048650_1_0_1; -.
DR InParanoid; Q3SZA5; -.
DR OMA; TIWKKQT; -.
DR OrthoDB; 1243182at2759; -.
DR UniPathway; UPA00249; UER00315.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000018382; Expressed in caput epididymis and 106 other tissues.
DR ExpressionAtlas; Q3SZA5; baseline.
DR GO; GO:0016768; F:spermine synthase activity; IBA:GO_Central.
DR GO; GO:0006597; P:spermine biosynthetic process; IBA:GO_Central.
DR Gene3D; 2.30.140.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR030374; PABS.
DR InterPro; IPR030373; PABS_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR035246; Spermidine_synt_N.
DR InterPro; IPR037163; Spermidine_synt_N_sf.
DR InterPro; IPR015576; Spermine_synthase_animal.
DR InterPro; IPR040900; SpmSyn_N.
DR PANTHER; PTHR46315; PTHR46315; 1.
DR Pfam; PF17284; Spermine_synt_N; 1.
DR Pfam; PF17950; SpmSyn_N; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS01330; PABS_1; 1.
DR PROSITE; PS51006; PABS_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Phosphoprotein; Polyamine biosynthesis; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P52788"
FT CHAIN 2..365
FT /note="Spermine synthase"
FT /id="PRO_0000239735"
FT DOMAIN 121..361
FT /note="PABS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00354"
FT ACT_SITE 275
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00354"
FT BINDING 147
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250|UniProtKB:P52788"
FT BINDING 176
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250|UniProtKB:P52788"
FT BINDING 200
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250|UniProtKB:P52788"
FT BINDING 219
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250|UniProtKB:P52788"
FT BINDING 254..255
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250|UniProtKB:P52788"
FT BINDING 350
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250|UniProtKB:P52788"
FT BINDING 352
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000250|UniProtKB:P52788"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P52788"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52788"
SQ SEQUENCE 365 AA; 41224 MW; 06BE20C409217A3B CRC64;
MAAARHSTLD FMLGAKADGE TILKGLQSIF QEQGMTESVH TWQDHGYLAT YINKNGSFAN
LRIYPHGLVL LDLQSYDGDA QGKEVDSLLN KVEERMKELS QDSTERVKRL PPIVRGGAID
RYWPTADGRL VEYDIDKVVY DEDSPYQNIK ILHSKQFGNI LILSGDVNLA ESDLAYTRAI
MGSGKEDYSG KDVLILGGGD GGILCEIVKL KPKMVTMVEI DQMVIDGCKK YMRKTCGDVL
DNLKGDCYQV LIEDCIPVLK RYAKEGREFD YVINDLTAVP ISTSPEEDST WEFLRLILDL
SMKVLKQDGK YFTQGNCVNL TEALSLYEEQ LGRLYCPVEF SKEIVCVPSY LELWVFYTVW
KKAKP
