ID E9FF95_9STRE Unreviewed; 375 AA.
AC E9FF95;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
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:EFX56844.1};
GN ORFNames=HMPREF0849_00015 {ECO:0000313|EMBL:EFX56844.1};
OS Streptococcus sp. C300.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=563036 {ECO:0000313|EMBL:EFX56844.1, ECO:0000313|Proteomes:UP000003809};
RN [1] {ECO:0000313|EMBL:EFX56844.1, ECO:0000313|Proteomes:UP000003809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C300 {ECO:0000313|EMBL:EFX56844.1,
RC ECO:0000313|Proteomes:UP000003809};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., Engels R.,
RA Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Mehta T.,
RA Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D.,
RA Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., Yandava C.,
RA Sibley C.D., Field T.R., Grinwis M., Eshaghurshan C.S., Surette M.G.,
RA Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Streptococcus sp. C300.";
RL Submitted (MAR-2010) 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}.
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DR EMBL; GL732466; EFX56844.1; -; Genomic_DNA.
DR RefSeq; WP_000764383.1; NZ_GL732466.1.
DR AlphaFoldDB; E9FF95; -.
DR HOGENOM; CLU_038560_0_0_9; -.
DR Proteomes; UP000003809; 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 12..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; 42034 MW; 547E31B8EFFA4280 CRC64;
MKLEQVPTPA YVIDLAKLEE NCRILQQVQE EAGCKVLLAQ KAYSLYKTYP LISQYLSGTT
ASGLYEAKLA REEFPGEVHV FAPAFKDADL EELLEITDHI VFNSERQLRK HGARCREAGI
SVGLRLNPQC STQGDHALYD PCAPGSRFGV SLDKVPSDLL DLVDGLHFHT LCEQGADDLE
TTLKAVEAQF GPYLHEVKWL NMGGGHHITR EDYDVDLLIS EIKRIRETYN LEVYIEPGEA
IALNAGYLAT EVLDIVENGM EILVLDASAT CHMPDVLEMP YRPPLRNGFE AQEKAHTYRL
SSNTCLTGDV IGDYSFENPV EIGDRLYFED MAIYSFVKNN TFNGIGLPSL YLMDEQGECN
LVKDFGYQDF KGRLS
//
