ID U1J6U4_9GAMM Unreviewed; 626 AA.
AC U1J6U4;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=arginine decarboxylase {ECO:0000256|ARBA:ARBA00012426};
DE EC=4.1.1.19 {ECO:0000256|ARBA:ARBA00012426};
GN ORFNames=PCIT_18494 {ECO:0000313|EMBL:ERG17091.1};
OS Pseudoalteromonas citrea DSM 8771.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1117314 {ECO:0000313|EMBL:ERG17091.1, ECO:0000313|Proteomes:UP000016487};
RN [1] {ECO:0000313|EMBL:ERG17091.1, ECO:0000313|Proteomes:UP000016487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8771 {ECO:0000313|Proteomes:UP000016487};
RX PubMed=22535931; DOI=10.1128/JB.00265-12;
RA Xie B.B., Shu Y.L., Qin Q.L., Rong J.C., Zhang X.Y., Chen X.L., Shi M.,
RA He H.L., Zhou B.C., Zhang Y.Z.;
RT "Genome sequences of type strains of seven species of the marine bacterium
RT Pseudoalteromonas.";
RL J. Bacteriol. 194:2746-2747(2012).
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:ERG17091.1}.
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DR EMBL; AHBZ02000187; ERG17091.1; -; Genomic_DNA.
DR AlphaFoldDB; U1J6U4; -.
DR STRING; 1117314.PCIT_18494; -.
DR eggNOG; COG1166; Bacteria.
DR OrthoDB; 9802658at2; -.
DR Proteomes; UP000016487; 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; 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; 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:ERG17091.1};
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:UP000016487};
KW Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066}.
FT DOMAIN 87..340
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 366..448
FT /note="Arginine decarboxylase helical bundle"
FT /evidence="ECO:0000259|Pfam:PF17810"
FT DOMAIN 575..624
FT /note="Arginine decarboxylase C-terminal helical"
FT /evidence="ECO:0000259|Pfam:PF17944"
FT ACT_SITE 498
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 100
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001336-50"
SQ SEQUENCE 626 AA; 69632 MW; 64614811E2CD92D5 CRC64;
MKWGLDTARD IYNVAHWSDG YFDINEQGEL VAFPDGKKAA PAISFPDLVE QFKAQGLTLP
VLVRFTDILQ HRVDTMTDAF SLACEQKAYQ GEYTCVYPIK VNQQRSVVSK LLAHPSGLVG
LEAGSKPELM AILGIATSPI TIVCNGYKDS EFLRLACIAQ AMGHKVNIVV EKLSELTSLI
KEIDDLGIEP SIGIRIRLNS VGKGKWQNTG GEKGKFGLTA GQVLEAVETL KQHDKLHLMN
LVHFHIGSQI ANIRDIQRAL IECARHFAEL TRLGVPLKTV DVGGGLGVDY EGSGSRSACS
MNYTVEEYAR NVVSAFAEVC EQHDLTHPAI ITESGRALTA HHAVLVTDVI DIEQAPKQTC
GTAPNKTDHV ILHQLWQVLH RITPRLALEA YHDAMHLFSE AHGQYVHGLV SMTQWAQIEL
LYFTILHQVR ETLNENARSH REVLDDLNEK LADKLFVNFS LFQSLPDVWG IQQLFPVMPI
EALEQPLTQR AIIQDITCDS DGQIREYVEG SGIESSLPIP PYQFGDQYHL AMFMVGAYQE
ILGDLHNLFG DTDSVHVEMT EQGYMLTNAI KGDSVADVLK VVHYDHEKLS DNFSEQVSKL
DITKQIKAQY LAELNAGLAG YTYFED
//
