ID   HSS_RHILO               Reviewed;         485 AA.
AC   Q98H64;
DT   24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Homospermidine synthase;
DE            Short=HSS;
DE            EC=2.5.1.44;
GN   Name=hss; OrderedLocusNames=mlr3014;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
CC   -!- FUNCTION: Involved in the NAD(+)-dependent synthesis of the polyamine
CC       homospermidine from putrescine. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 putrescine = NH4(+) + sym-homospermidine;
CC         Xref=Rhea:RHEA:18645, ChEBI:CHEBI:28938, ChEBI:CHEBI:57811,
CC         ChEBI:CHEBI:326268; EC=2.5.1.44;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=putrescine + spermidine = propane-1,3-diamine + sym-
CC         homospermidine; Xref=Rhea:RHEA:11236, ChEBI:CHEBI:57484,
CC         ChEBI:CHEBI:57811, ChEBI:CHEBI:57834, ChEBI:CHEBI:326268;
CC         EC=2.5.1.44;
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the saccharopine dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; BA000012; BAB50002.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q98H64; -.
DR   SMR; Q98H64; -.
DR   STRING; 266835.14023396; -.
DR   EnsemblBacteria; BAB50002; BAB50002; BAB50002.
DR   KEGG; mlo:mlr3014; -.
DR   eggNOG; COG5310; Bacteria.
DR   HOGENOM; CLU_046538_0_0_5; -.
DR   OMA; RTWCPTP; -.
DR   Proteomes; UP000000552; Chromosome.
DR   GO; GO:0050514; F:homospermidine synthase (spermidine-specific) activity; IEA:RHEA.
DR   GO; GO:0047296; F:homospermidine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.360.30; -; 1.
DR   InterPro; IPR023181; Homospermid_syn-like_C.
DR   InterPro; IPR032095; Sacchrp_dh-like_C.
DR   InterPro; IPR005097; Sacchrp_dh_NADP.
DR   Pfam; PF16653; Sacchrp_dh_C; 1.
DR   Pfam; PF03435; Sacchrp_dh_NADP; 1.
PE   3: Inferred from homology;
KW   NAD; Transferase.
FT   CHAIN           1..485
FT                   /note="Homospermidine synthase"
FT                   /id="PRO_0000084083"
SQ   SEQUENCE   485 AA;  54248 MW;  D15E80EADCCAB6A0 CRC64;
     MLDKMANENW PVYGEITGPV VMIGFGSIGR GTLPLIERHF KFDKSRMTVL DPRDTDRKLL
     DERGIAFVQE AVTENNYKKL LTPLLTNGGG QGFCVNLSVD TGSVDLMRLC RKLGVLYIDT
     VVEPWLGFYF DAKADNASRT NYALREAMIK EKHDKPGGAT VVSTCGANPG MVSWFVKQAL
     VNLATDLGLE FSEPAQEDRE GWAKLMKKAG VKGIHIAERD TQRTKKPKPM DVFWNTWSVE
     GFISEGLQPA ELGWGTHEKW MPKNGKKHKH GSKAAIYLEQ PGANTRVRSW CPTPGAQYGL
     LVTHNEAISI ADFFTVRSKK GKVQYRPTCH YAYHPSNDAM LSLDEMFGAA GKPQPVHHVL
     DENELVDGVD ELGVLLYGHD KNAYWYGSQL SLAEARKLAP YQNATGMQVT SAVLAGMVWA
     LENPDAGIVE ADEMDYKRCL DVQSPYLGPV KGYYTDWTPL DRRPGLFPED LDRSDPWQFR
     NILVR