ID E2NJI3_9BACE Unreviewed; 386 AA.
AC E2NJI3;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
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:EEF87925.1};
GN ORFNames=BACCELL_04469 {ECO:0000313|EMBL:EEF87925.1};
OS Bacteroides cellulosilyticus DSM 14838.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=537012 {ECO:0000313|EMBL:EEF87925.1, ECO:0000313|Proteomes:UP000003711};
RN [1] {ECO:0000313|EMBL:EEF87925.1, ECO:0000313|Proteomes:UP000003711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14838 {ECO:0000313|EMBL:EEF87925.1,
RC ECO:0000313|Proteomes:UP000003711};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEF87925.1, ECO:0000313|Proteomes:UP000003711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14838 {ECO:0000313|EMBL:EEF87925.1,
RC ECO:0000313|Proteomes:UP000003711};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bacteroides cellulosilyticus (DSM 14838).";
RL Submitted (JAN-2009) 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:EEF87925.1}.
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DR EMBL; ACCH01000346; EEF87925.1; -; Genomic_DNA.
DR AlphaFoldDB; E2NJI3; -.
DR HOGENOM; CLU_038560_0_0_10; -.
DR Proteomes; UP000003711; 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; IPR022644; De-COase2_N.
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; PF02784; Orn_Arg_deC_N; 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 37..342
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT DOMAIN 125..251
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038941-1"
SQ SEQUENCE 386 AA; 44485 MW; 1FA6561AC7980F29 CRC64;
MVKKENMIDF NYFPSPCYIM DEELLRKNLT LIKSVADRAG VEIILAFKSF AMWRSFPIFR
EYIEHSTASS VYEARLALEE FGSKAHTYSP AYTEADFPEI MRCSSHITFN SLSQFCRFYP
EVVKEGSGIS CGIRINPEYS EVETELYNPC APGTRFGMTA DLLTEVLPQG IEGFHCHCHC
ESSSYELERT LKHLEEKFSR WFPQIKWLNL GGGHLMTRKD YDVEHLIQLL KDLRARYPHL
RIILEPGSAF TWQTGVLVSE VVDIVVSRGI RTAILNVSFT CHMPDCLEMP YQPAVRGAEI
GNNGGCHVYR LGGNSCLSGD YMGDWSFDHE LQIGERIVFE DMIHYTMVKT NMFNGIHHPA
IAMWTKERKA DIFKQFSYED YRDRMS
//
