ID A0A0H5C6P1_CYBJN Unreviewed; 293 AA.
AC A0A0H5C6P1; A0A1E4RXL7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=K00797 spermidine synthase {ECO:0000313|EMBL:CEP23761.1};
DE SubName: Full=Spermine synthase {ECO:0000313|EMBL:ODV71941.1};
GN Name=SPE3 {ECO:0000313|EMBL:CEP23761.1};
GN ORFNames=BN1211_4418 {ECO:0000313|EMBL:CEP23761.1}, CYBJADRAFT_154022
GN {ECO:0000313|EMBL:ODV71941.1};
OS Cyberlindnera jadinii (strain ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617
OS / NBRC 0987 / NRRL Y-1542) (Torula yeast) (Candida utilis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX NCBI_TaxID=983966 {ECO:0000313|EMBL:CEP23761.1, ECO:0000313|Proteomes:UP000038830};
RN [1] {ECO:0000313|EMBL:CEP23761.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS1600 {ECO:0000313|EMBL:CEP23761.1};
RA Jaenicke S.;
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000038830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617 / NBRC 0987 /
RC NRRL Y-1542 {ECO:0000313|Proteomes:UP000038830};
RX PubMed=26150016; DOI=10.1016/j.jbiotec.2015.06.423;
RA Rupp O., Brinkrolf K., Buerth C., Kunigo M., Schneider J., Jaenicke S.,
RA Goesmann A., Puehler A., Jaeger K.-E., Ernst J.F.;
RT "The structure of the Cyberlindnera jadinii genome and its relation to
RT Candida utilis analyzed by the occurrence of single nucleotide
RT polymorphisms.";
RL J. Biotechnol. 211:20-30(2015).
RN [3] {ECO:0000313|EMBL:ODV71941.1, ECO:0000313|Proteomes:UP000094389}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617 / NBRC 0987 /
RC NRRL Y-1542 {ECO:0000313|Proteomes:UP000094389}, and NRRL Y-1542
RC {ECO:0000313|EMBL:ODV71941.1};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000256|ARBA:ARBA00007867, ECO:0000256|RuleBase:RU003836}.
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DR EMBL; CDQK01000005; CEP23761.1; -; Genomic_DNA.
DR EMBL; KV453937; ODV71941.1; -; Genomic_DNA.
DR RefSeq; XP_020068980.1; XM_020213427.1.
DR STRING; 983966.A0A0H5C6P1; -.
DR GeneID; 30987823; -.
DR OMA; HIYNEMI; -.
DR OrthoDB; 1126121at2759; -.
DR Proteomes; UP000038830; Unassembled WGS sequence.
DR Proteomes; UP000094389; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 2.30.140.10; Spermidine synthase, tetramerisation domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 NCBIfam; NF037959; MFS_SpdSyn; 1.
DR NCBIfam; TIGR00417; speE; 1.
DR PANTHER; PTHR11558:SF11; SPERMIDINE SYNTHASE; 1.
DR PANTHER; PTHR11558; SPERMIDINE/SPERMINE SYNTHASE; 1.
DR Pfam; PF17284; Spermine_synt_N; 1.
DR Pfam; PF01564; Spermine_synth; 1.
DR PIRSF; PIRSF000502; Spermidine_synth; 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 Polyamine biosynthesis {ECO:0000256|PROSITE-ProRule:PRU00354};
KW Reference proteome {ECO:0000313|Proteomes:UP000094389};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00354}.
FT DOMAIN 13..250
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00354"
SQ SEQUENCE 293 AA; 33490 MW; 7137FF8344103768 CRC64;
MDPQELTHAT ISNGWFREVS DESFPGQALE LRVKKILYTG KSAFQDILVF ESTDYGNVLV
LDGIIQVSER DEFAYQEMIT HIPLLSHPDP KRVLVIGGGD GGVLREVLKH PGVEELILVE
IDATVIELSK KYLPNMSKSF DDPRVKVELC DGFKYLQENS KRFDVIITDS SDPDGPAAVF
YEKNYFQLLH ECLSDRGIVI MQASENIWLK ISLLQRLKEL MKQVFPVVEY CYTMVPTYTS
GQLGLMICSK DETLDLKTPT RTMPNEDELF KYYNADIHKS SFVLPTWAKK YLK
//
