ID   A0A0J6WY64_9FIRM        Unreviewed;       484 AA.
AC   A0A0J6WY64;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Decarboxylase {ECO:0000313|EMBL:KMO87564.1};
GN   ORFNames=AB840_02310 {ECO:0000313|EMBL:KMO87564.1};
OS   Megasphaera cerevisiae DSM 20462.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Megasphaera.
OX   NCBI_TaxID=1122219 {ECO:0000313|EMBL:KMO87564.1, ECO:0000313|Proteomes:UP000036503};
RN   [1] {ECO:0000313|EMBL:KMO87564.1, ECO:0000313|Proteomes:UP000036503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20462 {ECO:0000313|EMBL:KMO87564.1,
RC   ECO:0000313|Proteomes:UP000036503};
RA   Kutumbaka K., Pasmowitz J., Mategko J., Reyes D., Friedrich A., Han S.,
RA   Martens-Habbena W., Neal-McKinney J., Janagama H.K., Nadala C.,
RA   Samadpour M.;
RT   "Draft genome sequence of beer spoilage bacterium Megasphaera cerevisiae
RT   type strain 20462.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-I family.
CC       {ECO:0000256|ARBA:ARBA00010671}.
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:KMO87564.1}.
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DR   EMBL; LEKT01000004; KMO87564.1; -; Genomic_DNA.
DR   RefSeq; WP_048513215.1; NZ_LEKT01000004.1.
DR   AlphaFoldDB; A0A0J6WY64; -.
DR   STRING; 39029.BSR42_03285; -.
DR   PATRIC; fig|1122219.3.peg.1703; -.
DR   InParanoid; A0A0J6WY64; -.
DR   OrthoDB; 9815233at2; -.
DR   Proteomes; UP000036503; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   Gene3D; 3.90.100.10; Orn/Lys/Arg decarboxylase, C-terminal domain; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000310; Orn/Lys/Arg_deCO2ase_major_dom.
DR   InterPro; IPR008286; Prn/Lys/Arg_de-COase_C.
DR   InterPro; IPR036633; Prn/Lys/Arg_de-COase_C_sf.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR43277; ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43277:SF4; ARGININE DECARBOXYLASE; 1.
DR   Pfam; PF01276; OKR_DC_1; 1.
DR   Pfam; PF03711; OKR_DC_1_C; 1.
DR   SUPFAM; SSF55904; Ornithine decarboxylase C-terminal domain; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00703; OKR_DC_1; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036503}.
FT   DOMAIN          223..237
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS00703"
SQ   SEQUENCE   484 AA;  52277 MW;  2D13FECCCFB6622E CRC64;
     MDRENQHKVP FVDALEDYCR CHMVPFHTPG HKLGCGASVY QKELFGSALD RDLGLMYALD
     DLFRPEGPLR EAMQLAADLY GAGRTFFSVN GTTACVEAMI LAVCRRGDEI ILPREAHRSV
     MNGLVLSGAV PVYMESRFAA VQQISLGPDL DGLKRAVKAH PGARAVLVTY PTYDGVAIQL
     EEMVRYAHAQ GLYVLVDEAH GAHLPFQAAF PKEALVCGAD CVAQSTHKLA GSLTQTSMLH
     CARAFPLTDK IAAAMALVQS TSPQYWFLAS LDSARRQLAL DGERLTGRAL ALARQLRHEL
     NLISGICSFG REIMDYSTVG GFDETKITID FSGLGLDGRE AERLLRRERV EVEMTAGSHV
     LALITIGDSE ASTAALLKAC RRIASSHSVC AVERSTEPPL PIPQVCVSPQ EAWNAEVETV
     PLTQALGRVS AEAISFYPPG IPVVGLGEKI TAACLEYIAR KMTAGYRPNG AAGGLLPTVR
     VLCL
//