ID   NSPC_HERAR              Reviewed;         365 AA.
AC   Q5QCP2;
DT   28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Carboxynorspermidine/carboxyspermidine decarboxylase {ECO:0000250|UniProtKB:A8FNH9, ECO:0000312|EMBL:CAL61021.1};
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:0000250|UniProtKB:Q56575};
GN   Name=nspC {ECO:0000312|EMBL:CAL61021.1}; OrderedLocusNames=HEAR0832;
OS   Herminiimonas arsenicoxydans.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herminiimonas.
OX   NCBI_TaxID=204773;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=ULPAs1 {ECO:0000312|EMBL:AAV68371.1};
RX   PubMed=16380199; DOI=10.1016/j.biochi.2005.11.004;
RA   Carapito C., Muller D., Turlin E., Koechler S., Danchin A.,
RA   Van Dorsselaer A., Leize-Wagner E., Bertin P.N., Lett M.C.;
RT   "Identification of genes and proteins involved in the pleiotropic response
RT   to arsenic stress in Caenibacter arsenoxydans, a metalloresistant beta-
RT   proteobacterium with an unsequenced genome.";
RL   Biochimie 88:595-606(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULPAs1;
RX   PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA   Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA   Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA   Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA   Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA   Perdrial N., Schoepp B., Siguier P., Simeonova D.D., Rouy Z., Segurens B.,
RA   Turlin E., Vallenet D., van Dorsselaer A., Weiss S., Weissenbach J.,
RA   Lett M.-C., Danchin A., Bertin P.N.;
RT   "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT   environments.";
RL   PLoS Genet. 3:518-530(2007).
CC   -!- FUNCTION: Catalyzes the decarboxylation of carboxynorspermidine and
CC       carboxyspermidine. {ECO:0000250|UniProtKB:A8FNH9}.
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:0000250|UniProtKB:Q56575};
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:0000250|UniProtKB:Q56575};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:A8FNH9};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A8FNH9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: By arsenic. {ECO:0000269|PubMed:16380199}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       NspC subfamily. {ECO:0000255}.
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DR   EMBL; AY728032; AAV68371.1; -; Genomic_DNA.
DR   EMBL; CU207211; CAL61021.1; -; Genomic_DNA.
DR   RefSeq; WP_011870361.1; NC_009138.1.
DR   AlphaFoldDB; Q5QCP2; -.
DR   SMR; Q5QCP2; -.
DR   STRING; 204773.HEAR0832; -.
DR   PRIDE; Q5QCP2; -.
DR   EnsemblBacteria; CAL61021; CAL61021; HEAR0832.
DR   KEGG; har:HEAR0832; -.
DR   eggNOG; COG0019; Bacteria.
DR   HOGENOM; CLU_038560_0_0_4; -.
DR   OMA; YTMVKTT; -.
DR   OrthoDB; 861683at2; -.
DR   Proteomes; UP000006697; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016831; F:carboxy-lyase activity; ISS: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; ISS:UniProtKB.
DR   GO; GO:0008295; P:spermidine biosynthetic process; ISS: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   PROSITE; PS00879; ODR_DC_2_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Decarboxylase; Lyase; Polyamine biosynthesis;
KW   Pyridoxal phosphate; Reference proteome; Spermidine biosynthesis.
FT   CHAIN           1..365
FT                   /note="Carboxynorspermidine/carboxyspermidine
FT                   decarboxylase"
FT                   /id="PRO_0000420243"
FT   BINDING         233
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A8FNH9"
FT   BINDING         269
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:A8FNH9"
FT   MOD_RES         37
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:A8FNH9"
SQ   SEQUENCE   365 AA;  40598 MW;  10010FA2AD200CE1 CRC64;
     MISTPYYLID KSALLRNLQV IDQVRERSGA KVLLALKCFA TWSVFDLMQQ YMDGTTSSSL
     YEVKLGHQKF GGETHAYSVA FADHEIDEVV AHCDKIIFNS ISQFQRFSSH AGNKPKGLRL
     NPGVSCASFD LADPARPFSR LGESDPARIL SIIDQLDGVM IHNNCENRDF ERFDALLTEV
     EQRYGEILHR LSWVSLGGGI SFTTPGYSID AFCERLRRFA QTYDVQVYLE PGEATVRDTT
     TLEVSVVDIG FNGKNLAVVD SSTEAHMLDL LIYRETAPIK NAQGDHAYQI CGKTCLAGDI
     FGEARFEQPL QIGDRISIGD AGGYTMVKKN WFNGVHMPAI AIKEADGSVR AVREFSFDDY
     VSSLS