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Carboxynorspermidine/carboxyspermidine decarboxylase (CANS DC/CAS DC) (CANSDC/CASDC) (EC 4.1.1.96)

 NSPC_CAMJ8              Reviewed;         382 AA.
A8FNH9;
28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
13-NOV-2007, sequence version 1.
28-FEB-2018, entry version 58.
RecName: Full=Carboxynorspermidine/carboxyspermidine decarboxylase {ECO:0000303|PubMed:20534592, ECO:0000303|PubMed:22025614, ECO:0000312|EMBL:ABV53016.1};
Short=CANS DC/CAS DC {ECO:0000250|UniProtKB:Q56575};
Short=CANSDC/CASDC {ECO:0000303|PubMed:20534592, ECO:0000303|PubMed:22025614};
EC=4.1.1.96 {ECO:0000269|PubMed:20534592};
Name=nspC {ECO:0000312|EMBL:ABV53016.1}; OrderedLocusNames=C8J_1418;
Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC
11828).
Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
Campylobacteraceae; Campylobacter.
NCBI_TaxID=407148;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=81116 / NCTC 11828;
PubMed=17873037; DOI=10.1128/JB.01404-07;
Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M.,
Nuijten P.J.M., van Vliet A.H.M.;
"The complete genome sequence of Campylobacter jejuni strain 81116
(NCTC11828).";
J. Bacteriol. 189:8402-8403(2007).
[2]
FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
STRAIN=81116 / NCTC 11828 {ECO:0000269|PubMed:22025614};
PubMed=22025614; DOI=10.1074/jbc.M111.307835;
Hanfrey C.C., Pearson B.M., Hazeldine S., Lee J., Gaskin D.J.,
Woster P.M., Phillips M.A., Michael A.J.;
"Alternative spermidine biosynthetic route is critical for growth of
Campylobacter jejuni and is the dominant polyamine pathway in human
gut microbiota.";
J. Biol. Chem. 286:43301-43312(2011).
[3]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF VARIANT GLU-184 IN COMPLEX
WITH REACTION PRODUCT NORSPERMIDINE AND PYRIDOXAL PHOSPHATE, FUNCTION,
CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
AND PYRIDOXAL PHOSPHATE AT LYS-41.
STRAIN=81116 / NCTC 11828 {ECO:0000269|PubMed:20534592};
PubMed=20534592; DOI=10.1074/jbc.M110.121137;
Deng X., Lee J., Michael A.J., Tomchick D.R., Goldsmith E.J.,
Phillips M.A.;
"Evolution of substrate specificity within a diverse family of
beta/alpha-barrel-fold basic amino acid decarboxylases: X-ray
structure determination of enzymes with specificity for L-arginine and
carboxynorspermidine.";
J. Biol. Chem. 285:25708-25719(2010).
-!- FUNCTION: Catalyzes the decarboxylation of carboxynorspermidine
and carboxyspermidine in vitro. In vivo, responsible for
synthesizing spermidine, but not sym-norspermidine.
{ECO:0000269|PubMed:20534592, ECO:0000269|PubMed:22025614}.
-!- CATALYTIC ACTIVITY: Carboxynorspermidine = bis(3-aminopropyl)amine
+ CO(2). {ECO:0000269|PubMed:20534592}.
-!- CATALYTIC ACTIVITY: Carboxyspermidine = spermidine + CO(2).
{ECO:0000269|PubMed:20534592}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000269|PubMed:20534592};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=4.1 mM for carboxyspermidine {ECO:0000269|PubMed:20534592};
KM=2.1 mM for carboxynorspermidine
{ECO:0000269|PubMed:20534592};
Note=KM values are given with the protein sequence containing
Glu instead of Lys at position 184, the effect of the variation
on activity is unclear.;
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20534592}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Growth is highly compromised in polyamine
auxotrophic bacteria, but can be restored by exogenous spermidine,
sym-homospermidine and to a lesser extent by sym-norspermidine.
{ECO:0000269|PubMed:22025614}.
-!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II
family. NspC subfamily. {ECO:0000255}.
-----------------------------------------------------------------------
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EMBL; CP000814; ABV53016.1; -; Genomic_DNA.
RefSeq; WP_002877469.1; NC_009839.1.
PDB; 3N29; X-ray; 1.90 A; A/B=1-382.
PDBsum; 3N29; -.
ProteinModelPortal; A8FNH9; -.
SMR; A8FNH9; -.
EnsemblBacteria; ABV53016; ABV53016; C8J_1418.
KEGG; cju:C8J_1418; -.
HOGENOM; HOG000005225; -.
KO; K13747; -.
OMA; HFHTHCE; -.
BioCyc; CJEJ407148:G1G9V-1458-MONOMER; -.
BioCyc; MetaCyc:MONOMER-17344; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016831; F:carboxy-lyase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
GO; GO:0045312; P:nor-spermidine biosynthetic process; IDA:UniProtKB.
GO; GO:0008295; P:spermidine biosynthetic process; IDA:UniProtKB.
CDD; cd06829; PLPDE_III_CANSDC; 1.
Gene3D; 2.40.37.10; -; 2.
Gene3D; 3.20.20.10; -; 1.
InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
InterPro; IPR022643; De-COase2_C.
InterPro; IPR005730; Nsp_de-COase.
InterPro; IPR029066; PLP-binding_barrel.
PANTHER; PTHR43727:SF1; PTHR43727:SF1; 1.
Pfam; PF00278; Orn_DAP_Arg_deC; 1.
PIRSF; PIRSF038941; NspC; 1.
SUPFAM; SSF50621; SSF50621; 1.
SUPFAM; SSF51419; SSF51419; 1.
TIGRFAMs; TIGR01047; nspC; 1.
1: Evidence at protein level;
3D-structure; Cytoplasm; Decarboxylase; Lyase; Polyamine biosynthesis;
Pyridoxal phosphate; Spermidine biosynthesis.
CHAIN 1 382 Carboxynorspermidine/carboxyspermidine
decarboxylase.
/FTId=PRO_0000420244.
BINDING 236 236 Substrate. {ECO:0000269|PubMed:20534592}.
BINDING 272 272 Substrate. {ECO:0000269|PubMed:20534592}.
MOD_RES 41 41 N6-(pyridoxal phosphate)lysine.
{ECO:0000269|PubMed:20534592}.
STRAND 8 14 {ECO:0000244|PDB:3N29}.
HELIX 15 32 {ECO:0000244|PDB:3N29}.
STRAND 35 39 {ECO:0000244|PDB:3N29}.
TURN 40 42 {ECO:0000244|PDB:3N29}.
HELIX 46 48 {ECO:0000244|PDB:3N29}.
HELIX 49 55 {ECO:0000244|PDB:3N29}.
STRAND 58 63 {ECO:0000244|PDB:3N29}.
HELIX 64 73 {ECO:0000244|PDB:3N29}.
STRAND 76 84 {ECO:0000244|PDB:3N29}.
HELIX 87 96 {ECO:0000244|PDB:3N29}.
STRAND 98 104 {ECO:0000244|PDB:3N29}.
HELIX 105 111 {ECO:0000244|PDB:3N29}.
HELIX 112 114 {ECO:0000244|PDB:3N29}.
STRAND 118 124 {ECO:0000244|PDB:3N29}.
STRAND 145 147 {ECO:0000244|PDB:3N29}.
HELIX 149 152 {ECO:0000244|PDB:3N29}.
STRAND 162 164 {ECO:0000244|PDB:3N29}.
STRAND 169 171 {ECO:0000244|PDB:3N29}.
HELIX 173 187 {ECO:0000244|PDB:3N29}.
HELIX 188 190 {ECO:0000244|PDB:3N29}.
TURN 191 193 {ECO:0000244|PDB:3N29}.
STRAND 195 198 {ECO:0000244|PDB:3N29}.
HELIX 212 226 {ECO:0000244|PDB:3N29}.
STRAND 229 232 {ECO:0000244|PDB:3N29}.
HELIX 236 239 {ECO:0000244|PDB:3N29}.
STRAND 242 264 {ECO:0000244|PDB:3N29}.
HELIX 266 269 {ECO:0000244|PDB:3N29}.
HELIX 271 275 {ECO:0000244|PDB:3N29}.
STRAND 285 289 {ECO:0000244|PDB:3N29}.
STRAND 304 309 {ECO:0000244|PDB:3N29}.
STRAND 311 313 {ECO:0000244|PDB:3N29}.
STRAND 318 326 {ECO:0000244|PDB:3N29}.
STRAND 333 338 {ECO:0000244|PDB:3N29}.
STRAND 340 343 {ECO:0000244|PDB:3N29}.
HELIX 344 346 {ECO:0000244|PDB:3N29}.
HELIX 350 352 {ECO:0000244|PDB:3N29}.
STRAND 357 361 {ECO:0000244|PDB:3N29}.
STRAND 367 371 {ECO:0000244|PDB:3N29}.
HELIX 376 379 {ECO:0000244|PDB:3N29}.
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


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