ID   CANSD_VIBCH             Reviewed;         414 AA.
AC   Q9KRL3;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Carboxynorspermidine synthase {ECO:0000303|PubMed:19196710};
DE            Short=C-NSPD synthase {ECO:0000305};
DE            EC=1.5.1.43 {ECO:0000305|PubMed:19196710};
DE   AltName: Full=Carboxynorspermidine dehydrogenase {ECO:0000303|PubMed:19196710};
DE            Short=CANSDH {ECO:0000303|PubMed:19196710};
GN   OrderedLocusNames=VC_1624;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=19196710; DOI=10.1074/jbc.m900110200;
RA   Lee J., Sperandio V., Frantz D.E., Longgood J., Camilli A., Phillips M.A.,
RA   Michael A.J.;
RT   "An alternative polyamine biosynthetic pathway is widespread in bacteria
RT   and essential for biofilm formation in Vibrio cholerae.";
RL   J. Biol. Chem. 284:9899-9907(2009).
CC   -!- FUNCTION: Involved in norspermidine biosynthesis. Catalyzes the
CC       synthesis of carboxynorspermidine from L-aspartate 4-semialdehyde and
CC       1,3-diaminopropane. Is also active with putrescine as a substrate.
CC       Essential for biofilm formation. {ECO:0000269|PubMed:19196710}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carboxynorspermidine + H2O + NADP(+) = H(+) + L-aspartate 4-
CC         semialdehyde + NADPH + propane-1,3-diamine; Xref=Rhea:RHEA:34115,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57484,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:65070,
CC         ChEBI:CHEBI:537519; EC=1.5.1.43;
CC         Evidence={ECO:0000305|PubMed:19196710};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carboxyspermidine + H2O + NADP(+) = H(+) + L-aspartate 4-
CC         semialdehyde + NADPH + putrescine; Xref=Rhea:RHEA:34111,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:65072, ChEBI:CHEBI:326268,
CC         ChEBI:CHEBI:537519; EC=1.5.1.43;
CC         Evidence={ECO:0000305|PubMed:19196710};
CC   -!- DISRUPTION PHENOTYPE: Deletion of the gene abolishes norspermidine and
CC       spermidine biosynthesis, and results in increased accumulation of
CC       diaminopropane. Deletion leads to a reduction in growth rate of
CC       planktonic cells and severely reduced biofilm formation.
CC       {ECO:0000269|PubMed:19196710}.
CC   -!- SIMILARITY: Belongs to the saccharopine dehydrogenase family.
CC       carboxynorspermidine synthase subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE003852; AAF94777.1; -; Genomic_DNA.
DR   PIR; A82177; A82177.
DR   RefSeq; NP_231263.1; NC_002505.1.
DR   RefSeq; WP_000025713.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KRL3; -.
DR   SMR; Q9KRL3; -.
DR   STRING; 243277.VC_1624; -.
DR   DNASU; 2613880; -.
DR   EnsemblBacteria; AAF94777; AAF94777; VC_1624.
DR   KEGG; vch:VC_1624; -.
DR   PATRIC; fig|243277.26.peg.1552; -.
DR   eggNOG; COG1748; Bacteria.
DR   HOGENOM; CLU_032114_0_0_6; -.
DR   OMA; KHHFDEI; -.
DR   BioCyc; MetaCyc:MON-15801; -.
DR   BioCyc; VCHO:VC1624-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0102143; F:carboxynorspermidine dehydrogenase I activity; IEA:RHEA.
DR   GO; GO:0102144; F:carboxyspermidine dehydrogenase II activity; IEA:RHEA.
DR   GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   NADP; Oxidoreductase; Polyamine biosynthesis; Reference proteome.
FT   CHAIN           1..414
FT                   /note="Carboxynorspermidine synthase"
FT                   /id="PRO_0000424232"
SQ   SEQUENCE   414 AA;  45948 MW;  9DD664E701E2A71D CRC64;
     MSILQIGAGG VGWVVAHKAA QNNDVLGDIT IASRSIAKCE KIIESIKGKN NLKDSSKKLE
     ARQVNADDIE SLVKLINEVK PDLVINAGPP WVNVAIMEAC YQAKVSYLDT SVSVDLCSKG
     QQVPEAYDAQ WAFRDKFKQA GITAILSAGF DPGVVSVFAA YAAKYLFDEI DTIDVLDINA
     GDHGKKFATN FDPETNLLEI QGDSIYWDAG EWKRVPCHTR MLEFDFPKCG KFKVYSMSHD
     ELRSLKEFIP AKRIEFWMGF GDRYLNYFNM MRDIGLLSPE PLTLQDGTVV KPLQVLKAML
     PDPTSLAPGY KGLTCIGTWV QGKKDGKARS VFIYNHADHE VAYHDVEHQA IAYTTGVPAI
     TAALQFFRGE WAEPGVFNME QLNPDPFLET MPSIGLGWDV MELEPGQPDI QVVK