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SPEE_NEUCR
ID   SPEE_NEUCR              Reviewed;         291 AA.
AC   Q9Y8H7; Q7RVC3;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Spermidine synthase;
DE            Short=SPDSY;
DE            EC=2.5.1.16;
DE   AltName: Full=Putrescine aminopropyltransferase;
GN   Name=spe-3; ORFNames=B11H7.120, NCU06727;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=74A;
RX   PubMed=9850006; DOI=10.1177/074873098129000282;
RA   Katagiri S., Onai K., Nakashima H.;
RT   "Spermidine determines the sensitivity to the calmodulin antagonist,
RT   chlorpromazine, for the circadian conidiation rhythm but not for the
RT   mycelial growth in Neurospora crassa.";
RL   J. Biol. Rhythms 13:452-460(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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   -!- PATHWAY: Amine and polyamine biosynthesis; spermidine biosynthesis;
CC       spermidine from putrescine: step 1/1.
CC   -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC       {ECO:0000305}.
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DR   EMBL; AB001598; BAA81738.1; -; Genomic_DNA.
DR   EMBL; BX294092; CAD71251.1; -; Genomic_DNA.
DR   EMBL; CM002240; EAA31671.1; -; Genomic_DNA.
DR   RefSeq; XP_960907.1; XM_955814.3.
DR   AlphaFoldDB; Q9Y8H7; -.
DR   SMR; Q9Y8H7; -.
DR   STRING; 5141.EFNCRP00000006597; -.
DR   PRIDE; Q9Y8H7; -.
DR   EnsemblFungi; EAA31671; EAA31671; NCU06727.
DR   GeneID; 3877045; -.
DR   KEGG; ncr:NCU06727; -.
DR   VEuPathDB; FungiDB:NCU06727; -.
DR   HOGENOM; CLU_048199_1_0_1; -.
DR   InParanoid; Q9Y8H7; -.
DR   OMA; LWPGQSF; -.
DR   UniPathway; UPA00248; UER00314.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR   GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IBA:GO_Central.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0006596; P:polyamine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR030668; Spermi_synthase_euk.
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   PIRSF; PIRSF000502; Spermidine_synth; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00417; speE; 1.
DR   PROSITE; PS01330; PABS_1; 1.
DR   PROSITE; PS51006; PABS_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Spermidine biosynthesis; Transferase.
FT   CHAIN           1..291
FT                   /note="Spermidine synthase"
FT                   /id="PRO_0000156460"
FT   DOMAIN          11..246
FT                   /note="PABS"
FT   ACT_SITE        166
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         42
FT                   /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT                   /ligand_id="ChEBI:CHEBI:57443"
FT                   /evidence="ECO:0000250"
FT   BINDING         72
FT                   /ligand="putrescine"
FT                   /ligand_id="ChEBI:CHEBI:326268"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT                   /ligand_id="ChEBI:CHEBI:57443"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT                   /ligand_id="ChEBI:CHEBI:57443"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT                   /ligand_id="ChEBI:CHEBI:57443"
FT   BINDING         148..149
FT                   /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT                   /ligand_id="ChEBI:CHEBI:57443"
FT                   /evidence="ECO:0000250"
FT   BINDING         166..169
FT                   /ligand="putrescine"
FT                   /ligand_id="ChEBI:CHEBI:326268"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT                   /ligand_id="ChEBI:CHEBI:57443"
FT                   /evidence="ECO:0000250"
FT   BINDING         234
FT                   /ligand="putrescine"
FT                   /ligand_id="ChEBI:CHEBI:326268"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   291 AA;  33075 MW;  4BE58D18E7B089BC CRC64;
     MSEIAHPTIQ DGWFREISNM WPGQAMTLKV EKVLHHEKSL YQDVLIFKST DHGNVLVLDN
     VIQCTERDEF SYQEMITHLA MNSHPNPKKV LVIGGGDGGV LREVVKHDCV EEAILCDIDE
     AVIRLSKQFL PHMSAGFEHP KVKVHVGDGF KFLEDFKNTF DVIITDSSDP EGPAESLFQK
     PYFQLLHDAL REGGVITTQA ENQWLHLPLI TKLKKDCKEV FPVAEYAYTT IPTYPSGQIG
     FMVCSKDPNA NVKVPLRSWS QEEEEKLCRY YNSEIHKASF ILPTFAKKAL E
 
 
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