ID V2XNC3_9FIRM Unreviewed; 401 AA.
AC V2XNC3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Carboxynorspermidine/carboxyspermidine decarboxylase {ECO:0000256|ARBA:ARBA00013633};
DE EC=4.1.1.96 {ECO:0000256|ARBA:ARBA00012259};
GN ORFNames=GCWU0000282_000814 {ECO:0000313|EMBL:ESL03649.1};
OS Catonella morbi ATCC 51271.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Catonella.
OX NCBI_TaxID=592026 {ECO:0000313|EMBL:ESL03649.1, ECO:0000313|Proteomes:UP000018227};
RN [1] {ECO:0000313|EMBL:ESL03649.1, ECO:0000313|Proteomes:UP000018227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51271 {ECO:0000313|EMBL:ESL03649.1,
RC ECO:0000313|Proteomes:UP000018227};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JUN-2013) 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:ESL03649.1}.
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DR EMBL; ACIL03000007; ESL03649.1; -; Genomic_DNA.
DR AlphaFoldDB; V2XNC3; -.
DR STRING; 592026.GCWU0000282_000814; -.
DR eggNOG; COG0019; Bacteria.
DR HOGENOM; CLU_038560_0_0_9; -.
DR Proteomes; UP000018227; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000018227}.
FT DOMAIN 30..357
FT /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00278"
FT DOMAIN 108..266
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038941-1"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR038941-1"
SQ SEQUENCE 401 AA; 44779 MW; 5119CD39D13C6119 CRC64;
MSLSIKEFIL ISNNYPELKK AFEGLKTPCY VIDEAKIEEN CKILKAVMDE TGAKILLAQK
AFSGFYFYPL IGKYLAGATA SGLFEAKLGA EEMKKENHIF SPAYKDEDME EITKICDHII
FNSVNQLKKY KKYCVDKGVS IGIRINPEFS TQEGHEIYDP CASGSRLGIT LHTLENAITE
ESSLLDGVDG LHFHTLCEQG AEPLRDTLEV VYKNFGKHLK NMKWLNFGGG HHITREDYNR
ELLIKCIKEA KALFDVEVYL EPGEAVALNA GYSVTTILDK TTSGDTTNLI LDISAACHMP
DVIEMPYRPP LFTSGEAGEK KYTYRLGSCT CLAGDIIGDF SFDEEKNIGD MLIFGDMAIY
SFVKNNTFNG MPLPDLAVLK KDGKVENIKS FGYGDFKERL S
//
