NSPC_CAMJ8
ID NSPC_CAMJ8 Reviewed; 382 AA.
AC A8FNH9;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Carboxynorspermidine/carboxyspermidine decarboxylase {ECO:0000303|PubMed:20534592, ECO:0000303|PubMed:22025614, ECO:0000312|EMBL:ABV53016.1};
DE Short=CANS DC/CAS DC {ECO:0000250|UniProtKB:Q56575};
DE Short=CANSDC/CASDC {ECO:0000303|PubMed:20534592, ECO:0000303|PubMed:22025614};
DE EC=4.1.1.96 {ECO:0000269|PubMed:20534592};
GN Name=nspC {ECO:0000312|EMBL:ABV53016.1}; OrderedLocusNames=C8J_1418;
OS Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC
OS 11828).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=407148;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81116 / NCTC 11828;
RX PubMed=17873037; DOI=10.1128/jb.01404-07;
RA Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M.,
RA van Vliet A.H.M.;
RT "The complete genome sequence of Campylobacter jejuni strain 81116
RT (NCTC11828).";
RL J. Bacteriol. 189:8402-8403(2007).
RN [2]
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=81116 / NCTC 11828 {ECO:0000269|PubMed:22025614};
RX PubMed=22025614; DOI=10.1074/jbc.m111.307835;
RA Hanfrey C.C., Pearson B.M., Hazeldine S., Lee J., Gaskin D.J., Woster P.M.,
RA Phillips M.A., Michael A.J.;
RT "Alternative spermidine biosynthetic route is critical for growth of
RT Campylobacter jejuni and is the dominant polyamine pathway in human gut
RT microbiota.";
RL J. Biol. Chem. 286:43301-43312(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF VARIANT GLU-184 IN COMPLEX WITH
RP REACTION PRODUCT NORSPERMIDINE AND PYRIDOXAL PHOSPHATE, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND PYRIDOXAL
RP PHOSPHATE AT LYS-41.
RC STRAIN=81116 / NCTC 11828 {ECO:0000269|PubMed:20534592};
RX PubMed=20534592; DOI=10.1074/jbc.m110.121137;
RA Deng X., Lee J., Michael A.J., Tomchick D.R., Goldsmith E.J.,
RA Phillips M.A.;
RT "Evolution of substrate specificity within a diverse family of beta/alpha-
RT barrel-fold basic amino acid decarboxylases: X-ray structure determination
RT of enzymes with specificity for L-arginine and carboxynorspermidine.";
RL J. Biol. Chem. 285:25708-25719(2010).
CC -!- FUNCTION: Catalyzes the decarboxylation of carboxynorspermidine and
CC carboxyspermidine in vitro. In vivo, responsible for synthesizing
CC spermidine, but not sym-norspermidine. {ECO:0000269|PubMed:20534592,
CC ECO:0000269|PubMed:22025614}.
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:20534592};
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:20534592};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:20534592};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.1 mM for carboxyspermidine {ECO:0000269|PubMed:20534592};
CC KM=2.1 mM for carboxynorspermidine {ECO:0000269|PubMed:20534592};
CC Note=KM values are given with the protein sequence containing Glu
CC instead of Lys at position 184, the effect of the variation on
CC activity is unclear.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20534592}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Growth is highly compromised in polyamine
CC auxotrophic bacteria, but can be restored by exogenous spermidine, sym-
CC homospermidine and to a lesser extent by sym-norspermidine.
CC {ECO:0000269|PubMed:22025614}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC NspC subfamily. {ECO:0000255}.
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DR EMBL; CP000814; ABV53016.1; -; Genomic_DNA.
DR RefSeq; WP_002877469.1; NC_009839.1.
DR PDB; 3N29; X-ray; 1.90 A; A/B=1-382.
DR PDBsum; 3N29; -.
DR AlphaFoldDB; A8FNH9; -.
DR SMR; A8FNH9; -.
DR KEGG; cju:C8J_1418; -.
DR HOGENOM; CLU_038560_0_0_7; -.
DR OMA; YTMVKTT; -.
DR BioCyc; MetaCyc:MON-17344; -.
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; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA: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 3D-structure; Cytoplasm; Decarboxylase; Lyase; Polyamine biosynthesis;
KW Pyridoxal phosphate; Spermidine biosynthesis.
FT CHAIN 1..382
FT /note="Carboxynorspermidine/carboxyspermidine
FT decarboxylase"
FT /id="PRO_0000420244"
FT BINDING 236
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20534592"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20534592"
FT MOD_RES 41
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:20534592"
FT STRAND 8..14
FT /evidence="ECO:0007829|PDB:3N29"
FT HELIX 15..32
FT /evidence="ECO:0007829|PDB:3N29"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:3N29"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:3N29"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:3N29"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:3N29"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:3N29"
FT HELIX 64..73
FT /evidence="ECO:0007829|PDB:3N29"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:3N29"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:3N29"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:3N29"
FT HELIX 105..111
FT /evidence="ECO:0007829|PDB:3N29"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:3N29"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:3N29"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:3N29"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:3N29"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:3N29"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:3N29"
FT HELIX 173..187
FT /evidence="ECO:0007829|PDB:3N29"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:3N29"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:3N29"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:3N29"
FT HELIX 212..226
FT /evidence="ECO:0007829|PDB:3N29"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:3N29"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:3N29"
FT STRAND 242..264
FT /evidence="ECO:0007829|PDB:3N29"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:3N29"
FT HELIX 271..275
FT /evidence="ECO:0007829|PDB:3N29"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:3N29"
FT STRAND 304..309
FT /evidence="ECO:0007829|PDB:3N29"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:3N29"
FT STRAND 318..326
FT /evidence="ECO:0007829|PDB:3N29"
FT STRAND 333..338
FT /evidence="ECO:0007829|PDB:3N29"
FT STRAND 340..343
FT /evidence="ECO:0007829|PDB:3N29"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:3N29"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:3N29"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:3N29"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:3N29"
FT HELIX 376..379
FT /evidence="ECO:0007829|PDB:3N29"
SQ SEQUENCE 382 AA; 43265 MW; 10CCB2DA1E10B643 CRC64;
MFYEKIQTPA YILEEDKLRK NCELLASVGE KSGAKVLLAL KGFAFSGAMK IVGEYLKGCT
CSGLWEAKFA KEYMDKEIHT YSPAFKEDEI GEIASLSHHI VFNSLAQFHK FQSKTQKNSL
GLRCNVEFSL APKELYNPCG RYSRLGIRAK DFENVDLNAI EGLHFHALCE ESADALEAVL
KVFKEKFGKW IGQMKWVNFG GGHHITKKGY DVEKLIALCK NFSDKYGVQV YLEPGEAVGW
QTGNLVASVV DIIENEKQIA ILDTSSEAHM PDTIIMPYTS EVLNARILAT RENEKISDLK
ENEFAYLLTG NTCLAGDVMG EYAFDKKLKI GDKIVFLDQI HYTIVKNTTF NGIRLPNLML
LDHKNELQMI REFSYKDYSL RN
