ID D7GKX8_PLEOS Unreviewed; 410 AA.
AC D7GKX8;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Spermidine synthase-saccharopine dehydrogenase {ECO:0000313|EMBL:CBL93264.1};
DE Flags: Fragment;
GN Name=spe-Sdh {ECO:0000313|EMBL:CBL93264.1};
OS Pleurotus ostreatus (Oyster mushroom) (White-rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Pleurotineae; Pleurotaceae; Pleurotus.
OX NCBI_TaxID=5322 {ECO:0000313|EMBL:CBL93264.1};
RN [1] {ECO:0000313|EMBL:CBL93264.1}
RP NUCLEOTIDE SEQUENCE.
RA Leon-Ramirez C.G., Valdes-Santiago L., Campos-Gongora E.,
RA Ortiz-Castellanos L., Arechiga-Carvajal E.T., Ruiz-Herrera J.;
RT "A molecular probe for Basidiomycota: the spermidine synthase-saccharopine
RT dehydrogenase chimeric gene.";
RL FEMS Microbiol. Lett. 312:77-83(2010).
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000256|ARBA:ARBA00007867, ECO:0000256|RuleBase:RU003836}.
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DR EMBL; FN822775; CBL93264.1; -; Genomic_DNA.
DR AlphaFoldDB; D7GKX8; -.
DR VEuPathDB; FungiDB:PC9H_001204; -.
DR VEuPathDB; FungiDB:PLEOSDRAFT_1091586; -.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR HAMAP; MF_00198; Spermidine_synth; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR030374; PABS.
DR InterPro; IPR030373; PABS_CS.
DR InterPro; IPR032095; Sacchrp_dh-like_C.
DR InterPro; IPR005097; Sacchrp_dh_NADP.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001045; Spermi_synthase.
DR NCBIfam; TIGR00417; speE; 1.
DR PANTHER; PTHR11558:SF11; SPERMIDINE SYNTHASE; 1.
DR PANTHER; PTHR11558; SPERMIDINE/SPERMINE SYNTHASE; 1.
DR Pfam; PF16653; Sacchrp_dh_C; 1.
DR Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR Pfam; PF01564; Spermine_synth; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00354}.
FT DOMAIN 1..174
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
FT ACT_SITE 94
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00354"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CBL93264.1"
FT NON_TER 410
FT /evidence="ECO:0000313|EMBL:CBL93264.1"
SQ SEQUENCE 410 AA; 44096 MW; C68FDB86B378C1C9 CRC64;
QEMIAHLPLA SHPNPKKVLV IGGGDGGVVR EVLKHDTVEE VVLCDIDEVL VRVSKQYLPH
MSALLSSPKV RVHIGDGFKF LAENEATYDV IVTDSSDPVG PAESLFQKPY FQLLHDALTP
GGSISTQGEC LWLHLPLITE LRATTKSIFP VCEYAYTTIP TYPSGQIGFT MCSKDPSRDL
KVPVREVKGT RYYNAEIHKA AFVLPEFGRA ILEEGKNVLP LFGHAALAAN LTKPKRKVLL
LGSGFVARPC AEYIVRDPHN ELTIACRTIE NAKKLAEGLP GTAAITLNAT DAAALEAAVA
AHDIVISLIP YTHHADVIKA AIKGKTHVVT TSYVSPAMRE LDAAAREAGI VVLNEIGLDP
GIDHLYAVKT IGEVHAKGGK ASSKQFLSYC GGLPAPECSD NPLGSKFSWS
//
