(data stored in SCRATCH zone)

SWISSPROT: A4F6Y0_SACEN

ID   A4F6Y0_SACEN            Unreviewed;       530 AA.
AC   A4F6Y0;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 79.
DE   RecName: Full=Polyamine aminopropyltransferase {ECO:0000256|HAMAP-Rule:MF_00198};
DE   AltName: Full=Putrescine aminopropyltransferase {ECO:0000256|HAMAP-Rule:MF_00198};
DE            Short=PAPT {ECO:0000256|HAMAP-Rule:MF_00198};
DE   AltName: Full=Spermidine synthase {ECO:0000256|HAMAP-Rule:MF_00198};
DE            Short=SPDS {ECO:0000256|HAMAP-Rule:MF_00198};
DE            Short=SPDSY {ECO:0000256|HAMAP-Rule:MF_00198};
DE            EC=2.5.1.16 {ECO:0000256|HAMAP-Rule:MF_00198};
GN   Name=speE {ECO:0000256|HAMAP-Rule:MF_00198,
GN   ECO:0000313|EMBL:CAL99804.1};
GN   OrderedLocusNames=SACE_0456 {ECO:0000313|EMBL:CAL99804.1};
GN   ORFNames=A8924_0853 {ECO:0000313|EMBL:PFG93605.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99804.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99804.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAL99804.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG93605.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93605.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the irreversible transfer of a propylamine
CC       group from the amino donor S-adenosylmethioninamine (decarboxy-
CC       AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
CC       {ECO:0000256|HAMAP-Rule:MF_00198}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=putrescine + S-adenosyl 3-(methylsulfanyl)propylamine =
CC         H(+) + S-methyl-5'-thioadenosine + spermidine;
CC         Xref=Rhea:RHEA:12721, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509,
CC         ChEBI:CHEBI:57443, ChEBI:CHEBI:57834, ChEBI:CHEBI:326268;
CC         EC=2.5.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00198};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; spermidine
CC       biosynthesis; spermidine from putrescine: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00198}.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP-
CC       Rule:MF_00198}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00198}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00198}.
CC   -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00198}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00198}.
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DR   EMBL; AM420293; CAL99804.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93605.1; -; Genomic_DNA.
DR   RefSeq; WP_009947424.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0456; -.
DR   EnsemblBacteria; CAL99804; CAL99804; SACE_0456.
DR   KEGG; sen:SACE_0456; -.
DR   eggNOG; ENOG4108JPV; Bacteria.
DR   eggNOG; COG4262; LUCA.
DR   HOGENOM; HOG000216627; -.
DR   KO; K00797; -.
DR   OMA; SFGEWGY; -.
DR   OrthoDB; 1613081at2; -.
DR   BioCyc; SERY405948:SACE_RS02245-MONOMER; -.
DR   UniPathway; UPA00248; UER00314.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00198; Spermidine_synth; 1.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR030374; PABS.
DR   InterPro; IPR030373; PABS_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR001045; Spermi_synthase.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS01330; PABS_1; 1.
DR   PROSITE; PS51006; PABS_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4F6Y0.
DR   SWISS-2DPAGE; A4F6Y0.
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00198};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006728,
KW   ECO:0000313|Proteomes:UP000225825};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00198};
KW   Polyamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00198,
KW   ECO:0000256|PROSITE-ProRule:PRU00354};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728};
KW   Spermidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00198};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00198, ECO:0000256|PROSITE-
KW   ProRule:PRU00354, ECO:0000313|EMBL:CAL99804.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00198};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00198}.
FT   TRANSMEM     27     54       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00198}.
FT   TRANSMEM     60     79       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00198}.
FT   TRANSMEM     86    112       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00198}.
FT   TRANSMEM    118    144       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00198}.
FT   TRANSMEM    156    179       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00198}.
FT   TRANSMEM    185    205       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00198}.
FT   TRANSMEM    217    237       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00198}.
FT   DOMAIN      228    470       PABS. {ECO:0000259|PROSITE:PS51006}.
FT   REGION      286    287       Polyamine binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00198}.
FT   REGION      373    374       S-adenosylmethioninamine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00198}.
FT   ACT_SITE    391    391       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00198, ECO:0000256|PROSITE-ProRule:
FT                                PRU00354}.
FT   BINDING     262    262       S-adenosylmethioninamine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00198}.
FT   BINDING     297    297       Polyamine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00198}.
FT   BINDING     319    319       Polyamine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00198}.
FT   BINDING     339    339       S-adenosylmethioninamine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00198}.
SQ   SEQUENCE   530 AA;  56680 MW;  944F9AE96F8283C2 CRC64;
     MSVSTEPRDE TEPAAAPRPR GRLARTAVLV AVFVCAACGL VYELALVALG SYLIGDTIGQ
     ASIVLSLMVF AMGVGALAAK PLQRWAAAAF ALVELVLALL GGLSVLLLYA AFAWVGLYLP
     ALIVTALVLG ALIGAEIPLL MVLLQRIRKQ DAGSAVADLF AADYVGGLVG GLAFPFLLLP
     LFGQIQGALL VGMLNAAAGL GLVLTVFRRE LSKRVRLVLV AASALVGGVL LVAYVFADDF
     EVTARQALYA DPVVHAERTD YQDVVLTERV SLSGRGDTRL FLNGDLQFSS VDEYRYHEAL
     VHPAMAGPRS RVLVLGGGDG LALREVLRYP DVQQVTLVEM DPAVLDLARE DPRVAGLNRH
     AFDDPRVRTV SADAFAWLRD NRERYDVVLV DMPDPDSTAT AKLYSTEFYA LVRHAMADGA
     RVNVQAGSPY FAPQAFWCIE ATTRAAGIST VPYEVSVPSF GEWGFHLGTA GAAPPLELPA
     GAPPLRSLDA GTLRAAAEFP PDRRRIPGME PSTLMHPTIL SYAQGEWTNY
//

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