ID   NSPC_VIBVU              Reviewed;         377 AA.
AC   Q8D8D2;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Carboxynorspermidine/carboxyspermidine decarboxylase {ECO:0000303|PubMed:19196710, ECO:0000312|EMBL:AAO11372.1};
DE            Short=CANS DC/CAS DC {ECO:0000250|UniProtKB:Q56575};
DE            Short=CANSDC/CASDC {ECO:0000250|UniProtKB:A8FNH9};
DE            EC=4.1.1.96 {ECO:0000269|PubMed:19196710};
GN   Name=nspC {ECO:0000312|EMBL:AAO11372.1}; OrderedLocusNames=VV1_3048;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=CMCP6 {ECO:0000269|PubMed:19196710};
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: Catalyzes the decarboxylation of carboxynorspermidine and
CC       carboxyspermidine. Carboxynorspermidine is decarboxylated 20-fold more
CC       efficiently than carboxyspermidine. Exhibits some activity with L-
CC       ornithine, but shows no activity with L-arginine, L-lysine or meso-
CC       diaminopimelate. {ECO:0000269|PubMed:19196710}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carboxynorspermidine + H(+) = CO2 + norspermidine;
CC         Xref=Rhea:RHEA:34099, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57920, ChEBI:CHEBI:65070; EC=4.1.1.96;
CC         Evidence={ECO:0000269|PubMed:19196710};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carboxyspermidine + H(+) = CO2 + spermidine;
CC         Xref=Rhea:RHEA:34095, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57834, ChEBI:CHEBI:65072; EC=4.1.1.96;
CC         Evidence={ECO:0000269|PubMed:19196710};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:A8FNH9};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.27 mM for carboxynorspermidine {ECO:0000269|PubMed:19196710};
CC         KM=1 mM for carboxyspermidine {ECO:0000269|PubMed:19196710};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A8FNH9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       NspC subfamily. {ECO:0000255}.
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DR   EMBL; AE016795; AAO11372.1; -; Genomic_DNA.
DR   RefSeq; WP_011080852.1; NC_004459.3.
DR   AlphaFoldDB; Q8D8D2; -.
DR   SMR; Q8D8D2; -.
DR   EnsemblBacteria; AAO11372; AAO11372; VV1_3048.
DR   KEGG; vvu:VV1_3048; -.
DR   HOGENOM; CLU_038560_0_0_6; -.
DR   OMA; YTMVKTT; -.
DR   BioCyc; MetaCyc:MON-15804; -.
DR   SABIO-RK; Q8D8D2; -.
DR   Proteomes; UP000002275; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016831; F:carboxy-lyase activity; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR   GO; GO:0045312; P:nor-spermidine biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IDA:UniProtKB.
DR   CDD; cd06829; PLPDE_III_CANSDC; 1.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR022643; De-COase2_C.
DR   InterPro; IPR005730; Nsp_de-COase.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   PANTHER; PTHR43727:SF1; PTHR43727:SF1; 1.
DR   Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR   PIRSF; PIRSF038941; NspC; 1.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR01047; nspC; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Decarboxylase; Lyase; Polyamine biosynthesis;
KW   Pyridoxal phosphate; Spermidine biosynthesis.
FT   CHAIN           1..377
FT                   /note="Carboxynorspermidine/carboxyspermidine
FT                   decarboxylase"
FT                   /id="PRO_0000420248"
FT   BINDING         238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A8FNH9"
FT   BINDING         274
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A8FNH9"
FT   MOD_RES         41
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:A8FNH9"
SQ   SEQUENCE   377 AA;  41912 MW;  336FE35DD3B80A32 CRC64;
     MNKEQLKTPF FMIDEAKLIQ NLEIAKQLKE ISGVKLVLAL KCFSTWGVFD IIKPYLDGTT
     SSGPFEVKLG YEKFGGETHA YSVGYSEDDV REVADLCDKI IFNSQSQLAA HRHIVEGKAS
     IGLRLNPGVS YASQDLANPA RQFSRLGVQA DHIDPAVFDS INGVMFHMNC ENKDVDAFIA
     LLDSISERFG AYLNKLDWVS MGGGVFFTWP GYDVEKLGLA LKAFSEKHGV QMYLEPGEAI
     ITKTTDLVVT VVDLVENGMK TAIVDSATEA HRLDTLIYKE PASVLEASEN GEHEYVIGSC
     SCLAGDQFCV AKFDQPLHVG QRLHILDSAG YTMVKLNWFN GLKMPSVYCE RTNGEIQKLN
     EFGYEDFKRS LSLWSVQ