ID I9YYX9_HELPX Unreviewed; 405 AA.
AC I9YYX9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Carboxynorspermidine/carboxyspermidine decarboxylase {ECO:0000256|ARBA:ARBA00013633};
DE EC=4.1.1.96 {ECO:0000256|ARBA:ARBA00012259};
GN Name=nspC {ECO:0000313|EMBL:EJC34145.1};
GN ORFNames=HPHPP15B_0246 {ECO:0000313|EMBL:EJC34145.1};
OS Helicobacter pylori Hp P-15b.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=992108 {ECO:0000313|EMBL:EJC34145.1, ECO:0000313|Proteomes:UP000004543};
RN [1] {ECO:0000313|EMBL:EJC34145.1, ECO:0000313|Proteomes:UP000004543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hp P-15b {ECO:0000313|EMBL:EJC34145.1,
RC ECO:0000313|Proteomes:UP000004543};
RA Blanchard T.G., Czinn S.J., McCracken C., Abolude K., Maroo A.,
RA Santana-Cruz I., Tallon L.J., Ficke F.W.F.;
RT "Genome sequence of Helicobacter pylori Hp P-15b.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001897};
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:0000256|ARBA:ARBA00001807};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC NspC subfamily. {ECO:0000256|ARBA:ARBA00025802}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJC34145.1}.
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DR EMBL; AKQJ01000001; EJC34145.1; -; Genomic_DNA.
DR RefSeq; WP_000760795.1; NZ_AKQJ01000001.1.
DR AlphaFoldDB; I9YYX9; -.
DR PATRIC; fig|992108.3.peg.235; -.
DR Proteomes; UP000004543; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0045312; P:nor-spermidine biosynthetic process; IEA:InterPro.
DR CDD; cd06829; PLPDE_III_CANSDC; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 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 NCBIfam; TIGR01047; nspC; 1.
DR PANTHER; PTHR43727:SF1; CARBOXYNORSPERMIDINE_CARBOXYSPERMIDINE DECARBOXYLASE; 1.
DR PANTHER; PTHR43727; DIAMINOPIMELATE DECARBOXYLASE; 1.
DR Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR PIRSF; PIRSF038941; NspC; 1.
DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}.
FT DOMAIN 147..363
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT BINDING 259
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038941-1"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038941-1"
SQ SEQUENCE 405 AA; 45851 MW; 7B519F4415109BB9 CRC64;
MKKYSAIPTP CYALESERLE KNAKILEIVR QQSGAKILLA LKGYAFWREF GILRQRLNGC
CASGFYEAKL AFEEFGGRES HKEICVYSPA FKEAEMSAIL PLATSIIFNS FYQYATYKDR
ILDKNKQLEN LGLSPIKMGL RINPLYSEVT PAIYNPCSKT SRLGITPSGF EKGVKEHGLE
GVSGLHFHTH CEQNADALCR TLEHVEKHFK PYLENMAWVN FGGGHHITKS DYDVNLLIQT
IKDFKERYHN IEVILEPGEA IGWQCGFLIA SVIDIVQNDQ EIAILDASFS THMPDCLEMP
YRPSILKVSV ENDEEIIEVE KGENQGAFSY FLGGPTCLAG DFMGSFSFET PLKRGDKIVF
QDMLHYTIVK NNSFNGVPLP SLAKLDQQGF KILKNFSYED YKNRN
//
