NSPC_VIBCH
ID NSPC_VIBCH Reviewed; 387 AA.
AC Q9KRL4;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Carboxynorspermidine/carboxyspermidine decarboxylase {ECO:0000303|PubMed:19196710, ECO:0000312|EMBL:AAF94776.1};
DE Short=CANS DC/CAS DC {ECO:0000250|UniProtKB:Q56575};
DE Short=CANSDC/CASDC {ECO:0000250|UniProtKB:A8FNH9, ECO:0000303|PubMed:19196710};
DE EC=4.1.1.96 {ECO:0000250|UniProtKB:Q56575};
GN Name=nspC {ECO:0000250|UniProtKB:C6YCI2}; OrderedLocusNames=VC_1623;
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, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=El Tor C6709 / Serotype O1;
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. Essential for biofilm formation.
CC {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: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 -!- DISRUPTION PHENOTYPE: Abolishes sym-norspermidine and spermidine
CC accumulation and results in substantially increased accumulation of
CC diaminopropane, whereas putrescine levels remain unaffected.
CC Disappearance of norspermidine and accumulation of
CC carboxynorspermidine. 50-60% reduction in growth rate of planktonic
CC cells and severely reduced biofilm formation, which can be rescued by
CC exogenously supplied sym-norspermidine but not spermidine. Not required
CC for colonizing the small intestine in infant mouse model of infection.
CC {ECO:0000269|PubMed:19196710}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC NspC subfamily. {ECO:0000255}.
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DR EMBL; AE003852; AAF94776.1; -; Genomic_DNA.
DR PIR; H82176; H82176.
DR RefSeq; NP_231262.1; NC_002505.1.
DR AlphaFoldDB; Q9KRL4; -.
DR SMR; Q9KRL4; -.
DR STRING; 243277.VC_1623; -.
DR PRIDE; Q9KRL4; -.
DR DNASU; 2613879; -.
DR EnsemblBacteria; AAF94776; AAF94776; VC_1623.
DR KEGG; vch:VC_1623; -.
DR PATRIC; fig|243277.26.peg.1550; -.
DR eggNOG; COG0019; Bacteria.
DR HOGENOM; CLU_038560_0_0_6; -.
DR OMA; YTMVKTT; -.
DR BioCyc; MetaCyc:MON-15802; -.
DR BioCyc; VCHO:VC1623-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016831; F:carboxy-lyase activity; ISS:UniProtKB.
DR GO; GO:0008836; F:diaminopimelate decarboxylase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IBA:GO_Central.
DR GO; GO:0045312; P:nor-spermidine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0044010; P: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; Reference proteome; Spermidine biosynthesis.
FT CHAIN 1..387
FT /note="Carboxynorspermidine/carboxyspermidine
FT decarboxylase"
FT /id="PRO_0000420247"
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
