ID A0A7K4UK73_9SYLV Unreviewed; 359 AA.
AC A0A7K4UK73;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 13.
DE RecName: Full=Spermine synthase {ECO:0000256|ARBA:ARBA00074757};
DE EC=2.5.1.22 {ECO:0000256|ARBA:ARBA00066441};
DE AltName: Full=Spermidine aminopropyltransferase {ECO:0000256|ARBA:ARBA00082182};
DE Flags: Fragment;
GN Name=Sms {ECO:0000313|EMBL:NWR10676.1};
GN ORFNames=SINWEB_R07985 {ECO:0000313|EMBL:NWR10676.1};
OS Sinosuthora webbiana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Telluraves; Australaves;
OC Passeriformes; Sylvioidea; Sylviidae; Sinosuthora.
OX NCBI_TaxID=337173 {ECO:0000313|EMBL:NWR10676.1, ECO:0000313|Proteomes:UP000580691};
RN [1] {ECO:0000313|EMBL:NWR10676.1, ECO:0000313|Proteomes:UP000580691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B10K-DU-002-08 {ECO:0000313|EMBL:NWR10676.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NWR10676.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl 3-(methylsulfanyl)propylamine + spermidine =
CC spermine + S-methyl-5'-thioadenosine + H(+); 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:0000256|ARBA:ARBA00051838};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19974;
CC Evidence={ECO:0000256|ARBA:ARBA00051838};
CC -!- PATHWAY: Amine and polyamine biosynthesis; spermine biosynthesis;
CC spermine from spermidine: step 1/1. {ECO:0000256|ARBA:ARBA00060581}.
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:0000256|ARBA:ARBA00063314}.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000256|ARBA:ARBA00007867}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NWR10676.1}.
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DR EMBL; VXBN01014816; NWR10676.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7K4UK73; -.
DR OrthoDB; 5953636at2759; -.
DR Proteomes; UP000580691; Unassembled WGS sequence.
DR GO; GO:0016768; F:spermine synthase activity; IEA:InterPro.
DR GO; GO:0006597; P:spermine biosynthetic process; IEA:InterPro.
DR FunFam; 2.30.140.10:FF:000005; Spermine synthase; 1.
DR FunFam; 3.30.160.110:FF:000002; spermine synthase; 1.
DR FunFam; 3.40.50.150:FF:000059; spermine synthase; 1.
DR Gene3D; 3.30.160.110; Siroheme synthase, domain 2; 1.
DR Gene3D; 2.30.140.10; Spermidine synthase, tetramerisation domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; SPERMINE SYNTHASE; 1.
DR PANTHER; PTHR46315:SF1; SPERMINE SYNTHASE; 1.
DR Pfam; PF17284; Spermine_synt_N; 1.
DR Pfam; PF01564; Spermine_synth; 1.
DR Pfam; PF17950; SpmSyn_N; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS01330; PABS_1; 1.
DR PROSITE; PS51006; PABS_2; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115, ECO:0000256|PROSITE-
KW ProRule:PRU00354}; Reference proteome {ECO:0000313|Proteomes:UP000580691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00354}.
FT DOMAIN 112..354
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
FT ACT_SITE 268
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00354"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NWR10676.1"
FT NON_TER 359
FT /evidence="ECO:0000313|EMBL:NWR10676.1"
SQ SEQUENCE 359 AA; 40977 MW; 7651D29F06BC1623 CRC64;
FFLHLAADCN AVLKALQPIF QEQGMTETVH NWEDHGYLVT YVKKNGSFAN LRIHPHGLVL
VDLQSYSDDM KGREEVDQLL NKVEERMKEL FHGNIKRVKR LPAILRGGVI DRYWPTADGR
LVEYDIDEVV YDEDSPFQNI KILHSKQFGN ILILSGDVNL AESDLAYTQA IMGSGKEDYT
GKEVLILGGG DGGILYEIVK LKPKMVTMVA SNIDQMVIDG CKKHMRKTCG DVLDNLKGEC
YQVLIEDCIP VLKRYAKEGR MFDYVINDLT AVPISTSPEE DSTWEFLRLI LDLSMKVLKQ
DGKYFTQGNC INLTDALTLY EEQLSRLYCP VEFSKETVCV PSYMELWVFY TIWKKQTGI
//
