ID F9PBR5_9STRE Unreviewed; 375 AA.
AC F9PBR5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
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:EGV15065.1};
GN ORFNames=HMPREF1124_1289 {ECO:0000313|EMBL:EGV15065.1};
OS Streptococcus infantis X.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=997830 {ECO:0000313|EMBL:EGV15065.1, ECO:0000313|Proteomes:UP000003399};
RN [1] {ECO:0000313|EMBL:EGV15065.1, ECO:0000313|Proteomes:UP000003399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X {ECO:0000313|EMBL:EGV15065.1,
RC ECO:0000313|Proteomes:UP000003399};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (JUL-2011) 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:EGV15065.1}.
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DR EMBL; AFUQ01000001; EGV15065.1; -; Genomic_DNA.
DR AlphaFoldDB; F9PBR5; -.
DR PATRIC; fig|997830.4.peg.761; -.
DR eggNOG; COG0019; Bacteria.
DR Proteomes; UP000003399; 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 140..331
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038941-1"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038941-1"
SQ SEQUENCE 375 AA; 42215 MW; 3B30CBEF9C0D0364 CRC64;
MKLEQVPTPS YIIDLGKLEE NCRILLEVQE KAGCKVLLAQ KAYSLYKTYP LISQYLSGTT
ASGLYEAKLA REEFPGEVHV FAPAFKESDM EELLQISDHI DFNSERQLRK YGQRCREAGI
SVGLRINPQC STQGDHALYD PCAPGSRFGV TSDKIPSDLL DLVDGLHFHT LCEQGADDLQ
TTLKAVEDQF GAYLHQVKWL NMGGGHHITR DDYDVYLLIS EIKRIRETYN VDVYIEPGEA
IALNAGYLAT EVLDIVENGI ETLVLDASAS CHMPDVLEMP YRPPLRDGFE AQEKPYTYRL
SSNTCLTGDI IGDYSFENPV EIGDRLYFED MAIYSFVKNN TFNGIGLPSL YLMDKEGECS
LVKAFGYQDF KERLS
//
