CANSD_VIBAX
ID CANSD_VIBAX Reviewed; 414 AA.
AC P0DPE4; A0A2I3C6P1;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=Carboxynorspermidine synthase {ECO:0000303|PubMed:1955861};
DE Short=C-NSPD synthase {ECO:0000303|PubMed:1955861};
DE EC=1.5.1.43 {ECO:0000269|PubMed:1955861};
DE AltName: Full=Carboxynorspermidine dehydrogenase {ECO:0000250|UniProtKB:Q9KRL3};
DE Short=CANSDH {ECO:0000250|UniProtKB:Q9KRL3};
GN ORFNames=N646_1023 {ECO:0000312|EMBL:AGV16856.1};
OS Vibrio alginolyticus (strain ATCC 17749 / DSM 2171 / NBRC 15630 / NCIMB
OS 1903 / NCTC 12160 / XII-53).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1219076;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17749 / DSM 2171 / NBRC 15630 / NCIMB 1903 / NCTC 12160 /
RC XII-53;
RX PubMed=25635021; DOI=10.1128/genomea.01500-14;
RA Liu X.F., Cao Y., Zhang H.L., Chen Y.J., Hu C.J.;
RT "Complete genome sequence of Vibrio alginolyticus ATCC 17749.";
RL Genome Announc. 3:E01500-E01514(2015).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND SUBUNIT.
RC STRAIN=ATCC 17749 / DSM 2171 / NBRC 15630 / NCIMB 1903 / NCTC 12160 /
RC XII-53;
RX PubMed=1955861; DOI=10.1099/00221287-137-7-1737;
RA Nakao H., Shinoda S., Yamamoto S.;
RT "Purification and some properties of carboxynorspermidine synthase
RT participating in a novel biosynthetic pathway for norspermidine in Vibrio
RT alginolyticus.";
RL J. Gen. Microbiol. 137:1737-1742(1991).
CC -!- FUNCTION: Involved in norspermidine biosynthesis. Catalyzes the
CC synthesis of carboxynorspermidine from L-aspartate 4-semialdehyde and
CC 1,3-diaminopropane. Is also slightly active with putrescine as a
CC substrate. {ECO:0000269|PubMed:1955861}.
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:0000269|PubMed:1955861};
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:0000269|PubMed:1955861};
CC -!- ACTIVITY REGULATION: Activated by dithiothreitol and inhibited by SH-
CC reactive compounds. {ECO:0000269|PubMed:1955861}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.51 mM for NADPH {ECO:0000269|PubMed:1955861};
CC KM=2.97 mM for NADH {ECO:0000269|PubMed:1955861};
CC Vmax=31 umol/min/mg enzyme toward carboxynorspermidine (in the
CC presence of NADPH) {ECO:0000269|PubMed:1955861};
CC Vmax=13.5 umol/min/mg enzyme toward carboxynorspermidine (in the
CC presence of NADH) {ECO:0000269|PubMed:1955861};
CC pH dependence:
CC Optimum pH is 7.25-7.5. {ECO:0000269|PubMed:1955861};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:1955861};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:1955861}.
CC -!- SIMILARITY: Belongs to the saccharopine dehydrogenase family.
CC carboxynorspermidine synthase subfamily. {ECO:0000305}.
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DR EMBL; CP006718; AGV16856.1; -; Genomic_DNA.
DR RefSeq; WP_012841628.1; NZ_BATK01000017.1.
DR AlphaFoldDB; P0DPE4; -.
DR SMR; P0DPE4; -.
DR STRING; 1219076.N646_1023; -.
DR EnsemblBacteria; AGV16856; AGV16856; N646_1023.
DR GeneID; 61532761; -.
DR KEGG; vag:N646_1023; -.
DR HOGENOM; CLU_032114_0_0_6; -.
DR SABIO-RK; P0DPE4; -.
DR Proteomes; UP000016714; 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.
FT CHAIN 1..414
FT /note="Carboxynorspermidine synthase"
FT /id="PRO_0000443306"
SQ SEQUENCE 414 AA; 46105 MW; F083F2408288DE22 CRC64;
MAILQIGAGG VGWVVAHKAA QNNDVLGDIT IASRTVGKCE KIIESIQKKN NLKDSTKKLE
ARAVNADDVD SLVALIKEVQ PDLVINAGPP WVNMSIMEAC YQAKVSYLDT SVAVDLCSEG
QQVPQAYDWQ WGYREKFEEA GITGILGAGF DPGVVSVFAA YAVKHLFDEI DTIDVMDVNA
GDHGKKFATN FDPETNMLEI QGDSFYWENG EWKQVPCHSR MLEFEFPNCG SHKVYSMAHD
EVRSMQEFIP AKRIEFWMGF GDRYLNYFNV MRDIGLLSPD PLTLHDGTVV QPLHVLKALL
PDPTSLAPGY TGLTCIGTWV QGKKDGKERS VFIYNNADHE VAYEDVEHQA ISYTTGVPAI
TAALQFFRGK WADKGVFNME QLDPDPFLET MPSIGLDWHV QELEPGQPVI HKLK
