ID A0A372KC29_9BURK Unreviewed; 824 AA.
AC A0A372KC29;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Spermidine synthase {ECO:0000313|EMBL:RFU49839.1};
GN ORFNames=D0B32_03805 {ECO:0000313|EMBL:RFU49839.1};
OS Paraburkholderia sp. DHOC27.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=2303330 {ECO:0000313|EMBL:RFU49839.1, ECO:0000313|Proteomes:UP000263097};
RN [1] {ECO:0000313|EMBL:RFU49839.1, ECO:0000313|Proteomes:UP000263097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHOC27 {ECO:0000313|EMBL:RFU49839.1,
RC ECO:0000313|Proteomes:UP000263097};
RA Gao Z.-H., Qiu L.-H.;
RT "Paraburkholderia sp. DHOC27, isolated from subtropical forest soil.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000256|ARBA:ARBA00007867}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00354}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RFU49839.1}.
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DR EMBL; QVQV01000001; RFU49839.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372KC29; -.
DR OrthoDB; 5516475at2; -.
DR Proteomes; UP000263097; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR030374; PABS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; NF037959; MFS_SpdSyn; 2.
DR PANTHER; PTHR43317:SF9; POLYAMINE AMINOPROPYLTRANSFERASE 2; 1.
DR PANTHER; PTHR43317; THERMOSPERMINE SYNTHASE ACAULIS5; 1.
DR Pfam; PF01564; Spermine_synth; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51006; PABS_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115, ECO:0000256|PROSITE-
KW ProRule:PRU00354}; Reference proteome {ECO:0000313|Proteomes:UP000263097};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00354}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 220..239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 251..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 327..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 369..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 398..417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 429..447
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 441..691
FT /note="PABS"
FT /evidence="ECO:0000259|PROSITE:PS51006"
SQ SEQUENCE 824 AA; 86942 MW; 962BF6A8259C743D CRC64;
MLLLLVSGAA SLIYQLLWIK QLSLVVGVEV QAVTIGISGF FAGMALGGWL FGKLADRSAR
PLLLYAALEG GALLLALACT FGLAHAALLF VTLQKLTGPL AWALPFALVG VPAILMGGTL
PVLMRALAPR ENLIGHAGAR LYAANTAGAI AGTLVAPFVL IPWLGVQGAA CAAAVLNCVA
MLAALLLAPG GRARVAERAF ASVDARSADD TSPTAHQAHL ALVIYALAGG IGLGYEVIWS
QTIVQFIGTR SFAFAVVLAT YLLGLALGSA LVARRVDRAR DAWGSFGLLI AAAGVVALVE
LAVLGQWLPR WQADAAQAVM NATGNLLATM CARFAVASLA IVFVPTVLLG AAFPFALRLT
VHARRTGRDV GAVVALNTAG GIAGSLLAGF VLLPALGLIH ALAALAILAS VLGLLAVFGG
HAMQRGARWG VPLLAALAVI ASILTPADRL AAMLATAHGG ALRFYEESAG GTVAVIEQTS
GDNHFNRLYI QGVSNSGDAM TSLRYMRMQA LLPLLIHRDT PRSVLVIGLG TGITSGALLT
WPGLEQRVVA ELLPAVVRAS AQFKGNYGVT NDPRVQIRLH DGRHELLSST QRYDLITLEP
PPPSAAGIVN LYSSDFYRLA ASRLNDGGLV AQWLPLATQN EADTRSLIKS FVQTFPYATL
WTTELHEMML VGSMQPITLD LPGIRARFAQ PEVAKALGEV GIASPAALMS TWVTDRAGLE
YYAADAPEVT DDKPRIEYAK WVDEREFPRV LARLLALHIE PPVVGADDAF RAAMQTEQGT
LQTFYKAALD AYQGDRGAWQ DDIARVMQAD GDNPYYRWFV GMGG
//