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Database: UniProt
Entry: E6KMI1_STROR
LinkDB: E6KMI1_STROR
Original site: E6KMI1_STROR 
ID   E6KMI1_STROR            Unreviewed;       375 AA.
AC   E6KMI1;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
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:EFU62760.1};
GN   ORFNames=HMPREF8578_1446 {ECO:0000313|EMBL:EFU62760.1};
OS   Streptococcus oralis ATCC 49296.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=888049 {ECO:0000313|EMBL:EFU62760.1, ECO:0000313|Proteomes:UP000004500};
RN   [1] {ECO:0000313|EMBL:EFU62760.1, ECO:0000313|Proteomes:UP000004500}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49296 {ECO:0000313|EMBL:EFU62760.1,
RC   ECO:0000313|Proteomes:UP000004500};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (NOV-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}.
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:EFU62760.1}.
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DR   EMBL; AEPO01000013; EFU62760.1; -; Genomic_DNA.
DR   RefSeq; WP_000764355.1; NZ_GL622183.1.
DR   AlphaFoldDB; E6KMI1; -.
DR   eggNOG; COG0019; Bacteria.
DR   HOGENOM; CLU_038560_0_0_9; -.
DR   Proteomes; UP000004500; 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;  42038 MW;  AEA9865DD1FF1BFB CRC64;
     MKLEQVPTPA YVIDLAKLEA NCRILQYVQE EAGCKVLLAQ KAYSLYKTYP LISQYLSGTT
     ASGLYEAKLA REEFPGEVHV FAPAFKDADL EELLEITDHI VFNSERQLRK HGARCREAGI
     SVGLRLNPQC STQGNHALYD PCAPGSRFGV SLDKIPSDLL DLVDGLHFHT LCEQGADDLE
     TTLKAVEEQF GPYLHEVKWL NMGGGHHITR EDYDVDLLIS EIKRIRDTYN LEVYIEPGEA
     IALNAGYLAT EVLDIVENGM DILVLDASAT CHMPDVLEMP YRPPLRNGFE PQEKAHTYRL
     SSNTCLTGDV IGDYSFENPI QIGDRLYFED MAIYSFVKNN TFNGIGLPSL YLMDEQGDCS
     LVKTFGYQDF KGRLS
//
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