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Database: UniProt
Entry: A0A1N6Q822_9SPHI
LinkDB: A0A1N6Q822_9SPHI
Original site: A0A1N6Q822_9SPHI 
ID   A0A1N6Q822_9SPHI        Unreviewed;       464 AA.
AC   A0A1N6Q822;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Arginine decarboxylase {ECO:0000313|EMBL:MBB6126414.1};
DE            EC=4.1.1.19 {ECO:0000313|EMBL:MBB6126414.1};
GN   ORFNames=HDF22_000515 {ECO:0000313|EMBL:MBB6126414.1};
OS   Mucilaginibacter lappiensis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=354630 {ECO:0000313|EMBL:MBB6126414.1, ECO:0000313|Proteomes:UP000548326};
RN   [1] {ECO:0000313|EMBL:MBB6126414.1, ECO:0000313|Proteomes:UP000548326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP601 {ECO:0000313|EMBL:MBB6126414.1,
RC   ECO:0000313|Proteomes:UP000548326};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing
RT   to study the core and pangenomes of soil and plant-associated
RT   prokaryotes.";
RL   Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:MBB6126414.1}.
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DR   EMBL; JACHCA010000001; MBB6126414.1; -; Genomic_DNA.
DR   RefSeq; WP_076370485.1; NZ_JACHCB010000001.1.
DR   AlphaFoldDB; A0A1N6Q822; -.
DR   STRING; 354630.SAMN05421821_101766; -.
DR   OrthoDB; 9802658at2; -.
DR   Proteomes; UP000548326; 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   Lyase {ECO:0000313|EMBL:MBB6126414.1}.
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;  54209 MW;  BA011FFC865CEFA7 CRC64;
     MQSYQEFLDL SVGFPQDGFE IIDDELYFQD LNLMEMIETY GTPLRFTYLP MITKKIQQAK
     LLFQQAIVKN NYRGSYKYCY CTKSSHFRHI VEEALKNEIH LETSSAFDMP MIDALEKKGA
     VNKDITVICN GFKTFQYKTY IIDMLHDGFK NIIPVLDNKE EFNLYDDEIE MDTPCNLGIR
     IAAEEQPDSQ FYTSRLGVRM EDVIDFYHNK IEENPNFQVK LLHFFINSGI SDTPYYWNEL
     EKYVTLYCKF KKVNPALDTL DIGGGMPFKD SLVFDFDYEY MINEIVSRIK EICADNDTME
     PDIITEFGKY TVAEASGILY KVLGRKQQND RERWLMLDGS FITNLPDVWA LNQKYILLPV
     NNWDSEYERV NLGGITCDGQ DYYNQEAHMN SVFMPKTRKV QYLGFFNTGA YQEVLSGYGG
     IHHCLLPSPK HVIIRRNRDE TFNFEVFGEE QNSKQVLKIL GYTT
//
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