SPEE_BACSU
ID SPEE_BACSU Reviewed; 276 AA.
AC P70998;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Polyamine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198};
DE AltName: Full=Putrescine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198};
DE Short=PAPT {ECO:0000255|HAMAP-Rule:MF_00198};
DE AltName: Full=Spermidine synthase {ECO:0000255|HAMAP-Rule:MF_00198};
DE Short=SPDS {ECO:0000255|HAMAP-Rule:MF_00198};
DE Short=SPDSY {ECO:0000255|HAMAP-Rule:MF_00198};
DE EC=2.5.1.16 {ECO:0000255|HAMAP-Rule:MF_00198};
GN Name=speE {ECO:0000255|HAMAP-Rule:MF_00198}; Synonyms=ywhF;
GN OrderedLocusNames=BSU37500;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION IN THE POLYAMINE BIOSYNTHESIS.
RC STRAIN=168;
RX PubMed=9723923; DOI=10.1046/j.1365-2958.1998.00979.x;
RA Sekowska A., Bertin P., Danchin A.;
RT "Characterization of polyamine synthesis pathway in Bacillus subtilis
RT 168.";
RL Mol. Microbiol. 29:851-858(1998).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-276, AND SUBUNIT.
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure of spermidine synthase.";
RL Submitted (JAN-2005) to the PDB data bank.
CC -!- FUNCTION: Involved in the cell growth and proliferation. Catalyzes the
CC irreversible transfer of a propylamine group from the amino donor S-
CC adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-
CC diaminobutane) to yield spermidine (Probable).
CC {ECO:0000305|PubMed:9723923}.
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:0000255|HAMAP-Rule:MF_00198};
CC -!- PATHWAY: Amine and polyamine biosynthesis; spermidine biosynthesis;
CC spermidine from putrescine: step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00198}.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_00198,
CC ECO:0000269|Ref.4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198}.
CC -!- MISCELLANEOUS: B.subtilis has only one biosynthetic pathway from
CC agmatine to spermidine to produce polyamines.
CC {ECO:0000305|PubMed:9723923}.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_00198}.
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DR EMBL; Z80360; CAB02516.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15777.1; -; Genomic_DNA.
DR PIR; G70057; G70057.
DR RefSeq; NP_391630.1; NC_000964.3.
DR RefSeq; WP_003227543.1; NZ_JNCM01000034.1.
DR PDB; 1IY9; X-ray; 2.30 A; A/B/C/D=2-276.
DR PDBsum; 1IY9; -.
DR AlphaFoldDB; P70998; -.
DR SMR; P70998; -.
DR STRING; 224308.BSU37500; -.
DR PaxDb; P70998; -.
DR PRIDE; P70998; -.
DR EnsemblBacteria; CAB15777; CAB15777; BSU_37500.
DR GeneID; 937075; -.
DR KEGG; bsu:BSU37500; -.
DR PATRIC; fig|224308.179.peg.4061; -.
DR eggNOG; COG0421; Bacteria.
DR InParanoid; P70998; -.
DR OMA; LWPGQSF; -.
DR PhylomeDB; P70998; -.
DR BioCyc; BSUB:BSU37500-MON; -.
DR UniPathway; UPA00248; UER00314.
DR EvolutionaryTrace; P70998; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004766; F:spermidine synthase activity; IBA:GO_Central.
DR GO; GO:0008295; P:spermidine biosynthetic process; IBA:GO_Central.
DR Gene3D; 2.30.140.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00198; Spermidine_synth; 1.
DR InterPro; IPR030374; PABS.
DR InterPro; IPR030373; PABS_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001045; Spermi_synthase.
DR InterPro; IPR035246; Spermidine_synt_N.
DR InterPro; IPR037163; Spermidine_synt_N_sf.
DR PANTHER; PTHR11558; PTHR11558; 1.
DR Pfam; PF17284; Spermine_synt_N; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00417; speE; 1.
DR PROSITE; PS01330; PABS_1; 1.
DR PROSITE; PS51006; PABS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Polyamine biosynthesis; Reference proteome;
KW Spermidine biosynthesis; Transferase.
FT CHAIN 1..276
FT /note="Polyamine aminopropyltransferase"
FT /id="PRO_0000156470"
FT DOMAIN 3..236
FT /note="PABS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 32
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 63
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 87
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 107
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 138..139
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 156..159
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT BINDING 163
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00198"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:1IY9"
FT STRAND 14..28
FT /evidence="ECO:0007829|PDB:1IY9"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:1IY9"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:1IY9"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:1IY9"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:1IY9"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:1IY9"
FT HELIX 60..73
FT /evidence="ECO:0007829|PDB:1IY9"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1IY9"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1IY9"
FT HELIX 89..94
FT /evidence="ECO:0007829|PDB:1IY9"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:1IY9"
FT HELIX 110..119
FT /evidence="ECO:0007829|PDB:1IY9"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:1IY9"
FT TURN 125..128
FT /evidence="ECO:0007829|PDB:1IY9"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:1IY9"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:1IY9"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:1IY9"
FT HELIX 171..179
FT /evidence="ECO:0007829|PDB:1IY9"
FT STRAND 180..189
FT /evidence="ECO:0007829|PDB:1IY9"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:1IY9"
FT HELIX 197..208
FT /evidence="ECO:0007829|PDB:1IY9"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:1IY9"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:1IY9"
FT STRAND 229..237
FT /evidence="ECO:0007829|PDB:1IY9"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:1IY9"
FT HELIX 258..263
FT /evidence="ECO:0007829|PDB:1IY9"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:1IY9"
SQ SEQUENCE 276 AA; 31336 MW; A5E0725B80FBDD62 CRC64;
MSELWYTEKQ TKNFGITMKV NKTLHTEQTE FQHLEMVETE EFGNMLFLDG MVMTSEKDEF
VYHEMVAHVP LFTHPNPEHV LVVGGGDGGV IREILKHPSV KKATLVDIDG KVIEYSKKFL
PSIAGKLDDP RVDVQVDDGF MHIAKSENQY DVIMVDSTEP VGPAVNLFTK GFYAGIAKAL
KEDGIFVAQT DNPWFTPELI TNVQRDVKEI FPITKLYTAN IPTYPSGLWT FTIGSKKYDP
LAVEDSRFFD IETKYYTKDI HKAAFVLPKF VSDLIK
