ID   A0A1G6YVZ3_9SPHI        Unreviewed;       464 AA.
AC   A0A1G6YVZ3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Arginine decarboxylase {ECO:0000313|EMBL:SDD94518.1};
GN   ORFNames=SAMN05216464_103117 {ECO:0000313|EMBL:SDD94518.1};
OS   Mucilaginibacter pineti.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=1391627 {ECO:0000313|EMBL:SDD94518.1, ECO:0000313|Proteomes:UP000199072};
RN   [1] {ECO:0000313|EMBL:SDD94518.1, ECO:0000313|Proteomes:UP000199072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=47C3B {ECO:0000313|EMBL:SDD94518.1,
RC   ECO:0000313|Proteomes:UP000199072};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR   EMBL; FNAI01000003; SDD94518.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G6YVZ3; -.
DR   STRING; 1391627.SAMN05216464_103117; -.
DR   OrthoDB; 9802658at2; -.
DR   Proteomes; UP000199072; Unassembled WGS sequence.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:InterPro.
DR   GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:InterPro.
DR   CDD; cd06830; PLPDE_III_ADC; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR002985; Arg_decrbxlase.
DR   InterPro; IPR022643; De-COase2_C.
DR   InterPro; IPR022644; De-COase2_N.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   PANTHER; PTHR43295; ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43295:SF9; BIOSYNTHETIC ARGININE DECARBOXYLASE; 1.
DR   Pfam; PF02784; Orn_Arg_deC_N; 1.
DR   Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR   SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000199072}.
FT   DOMAIN          68..313
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          314..409
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
SQ   SEQUENCE   464 AA;  54249 MW;  77497ED11E4F95DC CRC64;
     MQSYQEFLDL SVGFPQDGFE IIDDELYFQD LNLMEMIETY GTPLRFTYLP MISKKIQQAK
     LLFQQAIIKN NYRGSYKYCY CTKSSHFRHI VEEALKNEIH LETSSAFDMP MIDALEKKGS
     VTKDITVICN GFKTFQYKTY IIDMLHDGFK NIIPVLDNKE EFNLYDDEIE MDTPCNLGIR
     IAAEEQPDSQ FYTSRLGVRM EDVIDFYHNK IEDNPNFQVK LLHFFINSGI SDTPYYWNEL
     EKYVTLYCKF KKVNPALDTL DIGGGMPFKD SLVFDFDYEY MINEIVSRIK EICAEHDTME
     PDIITEFGKY TVAEASGILY KVLGRKQQND RERWLMLDGS FITNLPDVWA LNQKYILLPI
     NNWDSEYERV NLGGITCDGQ DYYNQEAHMN SVFMPKTRKV QYLGFFNTGA YQEVLSGYGG
     IHHCLLPSPK HVIIRRNRDE TFNFEVFGEE QNSKQVLKIL GYTT
//