(data stored in SCRATCH zone)

SWISSPROT: Q3IJ44_PSEHT

ID   Q3IJ44_PSEHT            Unreviewed;       573 AA.
AC   Q3IJ44;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 77.
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   OrderedLocusNames=PSHAa0040 {ECO:0000313|EMBL:CAI85150.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85150.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85150.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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: S-adenosyl 3-(methylthio)propylamine +
CC       putrescine = 5'-S-methyl-5'-thioadenosine + spermidine.
CC       {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; CR954246; CAI85150.1; -; Genomic_DNA.
DR   RefSeq; WP_011326768.1; NC_007481.1.
DR   ProteinModelPortal; Q3IJ44; -.
DR   STRING; 326442.PSHAa0040; -.
DR   EnsemblBacteria; CAI85150; CAI85150; PSHAa0040.
DR   KEGG; pha:PSHAa0040; -.
DR   PATRIC; fig|326442.8.peg.38; -.
DR   eggNOG; ENOG4108JPV; Bacteria.
DR   eggNOG; COG4262; LUCA.
DR   HOGENOM; HOG000216627; -.
DR   KO; K00797; -.
DR   OMA; SFGEWGY; -.
DR   OrthoDB; POG091H029F; -.
DR   UniPathway; UPA00248; UER00314.
DR   Proteomes; UP000006843; Chromosome I.
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-HAMAP.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_00198; Spermidine_synth; 1.
DR   InterPro; IPR030374; PABS.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR001045; Spermi_synthase.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51006; PABS_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IJ44.
DR   SWISS-2DPAGE; Q3IJ44.
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00198};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
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:UP000006843};
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:CAI85150.1};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00198};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00198}.
FT   TRANSMEM     12     34       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00198}.
FT   TRANSMEM     54     74       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00198}.
FT   TRANSMEM     86    109       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00198}.
FT   TRANSMEM    139    160       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00198}.
FT   TRANSMEM    181    199       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00198}.
FT   TRANSMEM    205    222       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00198}.
FT   TRANSMEM    234    256       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_00198}.
FT   DOMAIN      253    502       PABS (polyamine biosynthesis).
FT                                {ECO:0000259|PROSITE:PS51006}.
FT   REGION      302    303       Polyamine binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00198}.
FT   REGION      401    402       S-adenosylmethioninamine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00198}.
FT   ACT_SITE    422    422       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00198, ECO:0000256|PROSITE-ProRule:
FT                                PRU00354}.
FT   BINDING     277    277       S-adenosylmethioninamine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00198}.
FT   BINDING     313    313       Polyamine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00198}.
FT   BINDING     337    337       Polyamine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00198}.
FT   BINDING     356    356       S-adenosylmethioninamine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00198}.
FT   BINDING     429    429       S-adenosylmethioninamine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00198}.
SQ   SEQUENCE   573 AA;  64336 MW;  96EDF622B8CA6127 CRC64;
     MSSTIKSPSK FSLLGHDILL ITVMAVLAGC GLIYEYLLSH YAGRVLGSVE SAIYAMIGTM
     IVAMGIGAFL ARWFKDAFTA FAWLESIIAL IGMGCILAIA GVIAVSYSLP HMFSSIFNLP
     PDVVLNGYVF QKLQEWSRFL PYVFGLILGL FIGMEIPLIA RIRQHVYGRF LENNAGTIYG
     ADYIGAGIGA AIWVSIMLSM PIMQAAAWTA LFNIIAGLAF LWRYHTYVRF AKLLLACHLL
     LLVLFAFILV LGSSWMDNLS NVLYKDKVIY SQATKYQHVV LTERLSKNQP QPITDLYLNG
     RLQFSSVDEQ IYHSMLVYPA MLASNRHERV LIIGGGDGLA LRDVLKWPVS KVTLIDLDGQ
     LLNLFGHKDA EFTSPEDISQ RLLSLNSKSM HDPRADIIVG DAFLEVEKLL DQAKQFDTIL
     IDLPDPNHPD LNKMYSDYFY NHVRQLLAPD GAMAVQSTSP YHAKKAFLSI AKTVKAAGFE
     YVEQYQQNIP SFGQWGWTIA TKMGQSASGR INDVTAMPIP SRWISKEYLL ASFIFPNNYF
     EHIKDIEVNR LGSGQLYDYY RTAWQIESEL YKN
//

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