NSPC_VIBCO
ID NSPC_VIBCO Reviewed; 387 AA.
AC C6YCI2;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Carboxynorspermidine/carboxyspermidine decarboxylase {ECO:0000250|UniProtKB:Q56575, ECO:0000312|EMBL:EET22862.1};
DE Short=CANS DC/CAS DC {ECO:0000250|UniProtKB:Q56575};
DE Short=CANSDC/CASDC {ECO:0000250|UniProtKB:A8FNH9, ECO:0000250|UniProtKB:Q56575};
DE EC=4.1.1.96 {ECO:0000250|UniProtKB:Q56575};
GN Name=nspC {ECO:0000250|UniProtKB:Q56575}; ORFNames=VchoM_00889;
OS Vibrio cholerae (strain MO10).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345072;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MO10 / Serotype O139 {ECO:0000312|EMBL:EET22862.1};
RA Colwell R., Grim C.J., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Shea T., Sykes S., Yandava C., Alvarado L., Kodira C.,
RA Borodovsky M., Heidelberg J., Lander E., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Vibrio cholerae MO10.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND SYNTHESIS OF 221-238.
RC STRAIN=MO10 / Serotype O139 {ECO:0000269|PubMed:22239666};
RX PubMed=22239666; DOI=10.1111/j.1574-6968.2012.02498.x;
RA Parker Z.M., Pendergraft S.S., Sobieraj J., McGinnis M.M., Karatan E.;
RT "Elevated levels of the norspermidine synthesis enzyme NspC enhance Vibrio
RT cholerae biofilm formation without affecting intracellular norspermidine
RT concentrations.";
RL FEMS Microbiol. Lett. 329:18-27(2012).
CC -!- FUNCTION: Catalyzes the decarboxylation of carboxynorspermidine and
CC carboxyspermidine. Involved in the regulation of biofilm formation and
CC motility. {ECO:0000250|UniProtKB:Q56575, ECO:0000269|PubMed:22239666}.
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:Q56575};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A8FNH9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: Overexpression results in large increases in biofilm
CC formation and vpsL exopolysaccharide gene expression as well as in
CC significant decrease in motility. Overexpression does not lead to
CC increased concentrations of norspermidine, putrescine, diaminopropane
CC or spermidine in shaking cell cultures, planktonic cells or biofilm-
CC associated cells of static biofilm cultures. Cadaverine levels are
CC unchanged in shaking cell cultures, but largely increased in planktonic
CC and biofilm-associated cells. {ECO:0000269|PubMed:22239666}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC NspC subfamily. {ECO:0000255}.
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DR EMBL; DS990136; EET22862.1; -; Genomic_DNA.
DR AlphaFoldDB; C6YCI2; -.
DR SMR; C6YCI2; -.
DR EnsemblBacteria; EET22862; EET22862; VchoM_00889.
DR HOGENOM; CLU_038560_0_0_6; -.
DR Proteomes; UP000004687; Unassembled WGS sequence.
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:1900190; P:regulation of single-species biofilm formation; IDA: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 TIGRFAMs; TIGR01047; nspC; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Decarboxylase; Lyase; Polyamine biosynthesis;
KW Pyridoxal phosphate; Spermidine biosynthesis.
FT CHAIN 1..387
FT /note="Carboxynorspermidine/carboxyspermidine
FT decarboxylase"
FT /id="PRO_0000420246"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A8FNH9"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A8FNH9"
FT MOD_RES 51
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:A8FNH9"
SQ SEQUENCE 387 AA; 43099 MW; B75DE87C2BBC5C15 CRC64;
METLQDIGTN MLKDELRTPY FMIDEAKLIA NLEIAKHLKE ISGVKMVLAL KCFSTWGVFD
IIKPYLDGTT SSGPFEVKLG YETFGGETHA YSVGYSEEDV KEVIDICDKM IFNSQSQLAA
YRHLVEGKAS LGLRINPGVS YAGQDLANPA RQFSRLGVQA DHIDESVFDS INGVMFHMNC
ENKDVDAFIG LLDAISERFG RYLDKLDWVS LGGGVFFTWP GYDVEKLGAA LKAFAERHAV
QLYLEPGEAI ITKTTDLVVT VVDIVENGMK TAIVDSATEA HRLDTLIYKE PASVLEASDK
GQHEYVIGSC SCLAGDQFCV AKFDEPLQVG QKLHILDSAG YTMVKLNWFN GLKMPSVYCE
RKNGQIQKIN QFGYEDFKRT LSLWSIE
