ID A0A0X3U4W1_9GAMM Unreviewed; 640 AA.
AC A0A0X3U4W1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=arginine decarboxylase {ECO:0000256|ARBA:ARBA00012426};
DE EC=4.1.1.19 {ECO:0000256|ARBA:ARBA00012426};
GN ORFNames=AVO43_09770 {ECO:0000313|EMBL:KUJ82844.1};
OS Microbulbifer sp. ZGT114.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Microbulbiferaceae; Microbulbifer.
OX NCBI_TaxID=1685377 {ECO:0000313|EMBL:KUJ82844.1, ECO:0000313|Proteomes:UP000054457};
RN [1] {ECO:0000313|EMBL:KUJ82844.1, ECO:0000313|Proteomes:UP000054457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZGT114 {ECO:0000313|EMBL:KUJ82844.1,
RC ECO:0000313|Proteomes:UP000054457};
RA Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the biosynthesis of agmatine from arginine.
CC {ECO:0000256|ARBA:ARBA00002257}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR001336-50};
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC SpeA subfamily. {ECO:0000256|ARBA:ARBA00008357}.
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:KUJ82844.1}.
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DR EMBL; LQBR01000003; KUJ82844.1; -; Genomic_DNA.
DR RefSeq; WP_067084289.1; NZ_LQBR01000003.1.
DR AlphaFoldDB; A0A0X3U4W1; -.
DR STRING; 1685377.AVO43_09770; -.
DR Proteomes; UP000054457; Unassembled WGS sequence.
DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06830; PLPDE_III_ADC; 1.
DR Gene3D; 1.10.287.3440; -; 1.
DR Gene3D; 1.20.58.930; -; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR040634; Arg_decarb_HB.
DR InterPro; IPR041128; Arg_decarbox_C.
DR InterPro; IPR002985; Arg_decrbxlase.
DR InterPro; IPR022644; De-COase2_N.
DR InterPro; IPR022653; De-COase2_pyr-phos_BS.
DR InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR InterPro; IPR029066; PLP-binding_barrel.
DR NCBIfam; TIGR01273; speA; 1.
DR PANTHER; PTHR43295; ARGININE DECARBOXYLASE; 1.
DR PANTHER; PTHR43295:SF9; BIOSYNTHETIC ARGININE DECARBOXYLASE; 1.
DR Pfam; PF17810; Arg_decarb_HB; 1.
DR Pfam; PF17944; Arg_decarbox_C; 1.
DR Pfam; PF02784; Orn_Arg_deC_N; 1.
DR PIRSF; PIRSF001336; Arg_decrbxlase; 1.
DR PRINTS; PR01180; ARGDCRBXLASE.
DR PRINTS; PR01179; ODADCRBXLASE.
DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS00878; ODR_DC_2_1; 1.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR001336-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000054457};
KW Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066}.
FT DOMAIN 102..349
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 376..456
FT /note="Arginine decarboxylase helical bundle"
FT /evidence="ECO:0000259|Pfam:PF17810"
FT DOMAIN 585..638
FT /note="Arginine decarboxylase C-terminal helical"
FT /evidence="ECO:0000259|Pfam:PF17944"
FT ACT_SITE 507
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 107
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001336-50"
SQ SEQUENCE 640 AA; 71707 MW; B87A79D1ED50C15B CRC64;
MKQQQVKEWT CEDSAELYGI RNWGAGYFDL SADGDITVNV KNSAGQTNAV SLMDIASGAM
ERGLGMPLLL RIENLLDAQV SLLNQSFARA IEQCNYRNVF RGVFPIKVNQ QCQVIEEIAR
AGNPFSHGLE AGSKAELITA LSTLENTDSL IVCNGYKDEE FINLGLQAQR LGVQVFFVVE
TPSEVATIIQ CAEREQVRPN IGVRIKLASK VGGYWNATSG DRSIFGLGSN DLIAMVDELR
RHDMLDCLKL LHYHLGSQVP NIRDIRTGVL EACRYYADLV EEGAAMGYLD LGGGLAVDYD
GSKTNDTHSR NYSLDEYCVD VVEAIMGTLD SEGVEHPVII TESGRATVAY SSVLLFDILD
TTRYEPVAID TNKIGEDDHA MLRYLKEAVD GVDADNLQES YNDALYYRDE IRSLYLHGQV
SLRERANAEN LFLHGAQKIR ALLDEVDEVP ADLESLPEAL SDIYYGNFSL FQSLPDIWAI
DQVFPLVPIH RHQEAPTRSA IIADITCDCD GKIDRFIGRQ EEQRTLSLHE LRENEDYILG
AFLIGAYQET LGDLHNLFGD TNVVSVRIDE DGGFDYSREI HGDSISDVLS YVEYRPQDMF
ERFRKLAERA VKEGRISPQQ RKQILHTYTA SMSGYTYFEK
//
