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Database: UniProt
Entry: A0A0Q4R2M3_9BACL
LinkDB: A0A0Q4R2M3_9BACL
Original site: A0A0Q4R2M3_9BACL 
ID   A0A0Q4R2M3_9BACL        Unreviewed;       508 AA.
AC   A0A0Q4R2M3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Amino acid decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ASF12_29830 {ECO:0000313|EMBL:KQO14194.1};
OS   Paenibacillus sp. Leaf72.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1736234 {ECO:0000313|EMBL:KQO14194.1, ECO:0000313|Proteomes:UP000051722};
RN   [1] {ECO:0000313|EMBL:KQO14194.1, ECO:0000313|Proteomes:UP000051722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf72 {ECO:0000313|EMBL:KQO14194.1,
RC   ECO:0000313|Proteomes:UP000051722};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQO14194.1, ECO:0000313|Proteomes:UP000051722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf72 {ECO:0000313|EMBL:KQO14194.1,
RC   ECO:0000313|Proteomes:UP000051722};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KQO14194.1}.
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DR   EMBL; LMLV01000006; KQO14194.1; -; Genomic_DNA.
DR   RefSeq; WP_056034961.1; NZ_LMLV01000006.1.
DR   AlphaFoldDB; A0A0Q4R2M3; -.
DR   STRING; 1736234.ASF12_29830; -.
DR   OrthoDB; 9815233at2; -.
DR   Proteomes; UP000051722; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   Gene3D; 3.90.105.10; Molybdopterin biosynthesis moea protein, domain 2; 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:SF3; LYSINE 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.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051722}.
FT   DOMAIN          7..325
FT                   /note="Orn/Lys/Arg decarboxylases family 1 pyridoxal-P
FT                   attachment site"
FT                   /evidence="ECO:0000259|Pfam:PF01276"
FT   DOMAIN          432..495
FT                   /note="Orn/Lys/Arg decarboxylase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03711"
SQ   SEQUENCE   508 AA;  55009 MW;  8FC533064FAB1AB6 CRC64;
     MQHIHAPLYE MLLKHTASQP VSFHVPGHRY GQAFGPDKPE REGEGQESDF IKAMKETFTA
     IMRLDVTELS ATDDLHHPEG AIAEAQDLAA RCFGAEESFF LVGGSTSGNL AMLLAVCEPG
     DYILVQRNVH KSVINGLKLA GARAVFIMPQ IDEPTGIATQ PSLAQVKMMM DLYPQAKAVF
     LNNPNYYGMS MNLQPYAEAI HQCGMLLLVD EAHGAHYGLH PKLPGSAIAA GADAVVQSTH
     KTLTALTMGA MLHVQGEFLN RTAIREALAT IQSSSPSFPI MASLDISRAM IEASGADWFD
     DALAVAAYLR KGIEECCAAI EILKQSDDRL AAMPAYNQLD PLRIVLWDRT GALSGFEILK
     LLEQQGCWAE MADMRHVVLL LGIGIQSEDA DRLIQACQAV EMIIASKGRV IAEQPLARAS
     NPLFLPESVE PIAFSRVSKG TMVRVKLEDA INCRAAEMIV PYPPGIPIVY PGELLTAEML
     GYIKELASSG AKFQGAVDPA MQSIAIVE
//
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