ID A0A2A2FCG7_9GAMM Unreviewed; 629 AA.
AC A0A2A2FCG7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=arginine decarboxylase {ECO:0000256|ARBA:ARBA00012426};
DE EC=4.1.1.19 {ECO:0000256|ARBA:ARBA00012426};
GN ORFNames=CK501_03970 {ECO:0000313|EMBL:PAU82312.1};
OS Halovibrio salipaludis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halovibrio.
OX NCBI_TaxID=2032626 {ECO:0000313|EMBL:PAU82312.1, ECO:0000313|Proteomes:UP000218896};
RN [1] {ECO:0000313|EMBL:PAU82312.1, ECO:0000313|Proteomes:UP000218896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YL5-2 {ECO:0000313|EMBL:PAU82312.1,
RC ECO:0000313|Proteomes:UP000218896};
RA Dong X., Zhang G.;
RT "Halovibrio sewagensis sp. nov., isolated from wastewater of high
RT salinity.";
RL Submitted (AUG-2017) 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:PAU82312.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NSKD01000001; PAU82312.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2FCG7; -.
DR OrthoDB; 9802658at2; -.
DR Proteomes; UP000218896; 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; IPR022657; De-COase2_CS.
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.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:PAU82312.1};
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:UP000218896};
KW Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066}.
FT DOMAIN 84..340
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 365..451
FT /note="Arginine decarboxylase helical bundle"
FT /evidence="ECO:0000259|Pfam:PF17810"
FT DOMAIN 578..626
FT /note="Arginine decarboxylase C-terminal helical"
FT /evidence="ECO:0000259|Pfam:PF17944"
FT ACT_SITE 501
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 96
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001336-50"
SQ SEQUENCE 629 AA; 69811 MW; 98D67F7A15CA54CF CRC64;
MHSDTPGRTW NIDRWSEGYV TVGAGGELRI NPDTRSPGVA LAEVVAQVQH QGARLPVLIR
FSDILRHRVN RLCRAFNEPI RNLGYEGGYT AVYPIKVNQQ RRVVEEILRS EPAAREGQIG
LEAGSKPELF AVLALAPPNA RIICNGYKDR ETIRLALMGQ RLGHRVFIVV EKASELPLIL
DESRRLGLRP LIGVRARLAT IGEGNWQNTG GEKSKFGLSA QQVLTVVEQL READALDRLQ
LLHFHLGSQI ANIRDIQTGL REAARFHHTL HEAGAPLNTV DVGGGLGVDY EGTRSRSACS
MNYSMEEYAR QVVQTFHESC TRNNLPHPHL ITESGRAMTA HHAVLVTNII DREAPEAATP
EPVPETAPAP LRSLWADYQA LSGDGPERSA VEIHHDAAQA MADVQTEFAH GLLSLQQRAQ
AEQLQRQVAM RLRTRLNPGN RVHRDLLDEL NEQCAERLFM NLSIFQSLPD IWGIDQIFPI
LPLQGLDQPT TRRAVLRDMT CDSDGRIDHY VDGDGIETTL PLPDATDVDQ LAFFMTGAYQ
EILGDMHNLF GDTDAADVSL DAAGNAQVTH LARGETLASV LRQVNHDPEN LFRQLESRIE
TAGLSDEERL RLLEQIRQGL GSYTYLTGD
//
