ID I3ICK1_9GAMM Unreviewed; 639 AA.
AC I3ICK1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=arginine decarboxylase {ECO:0000256|ARBA:ARBA00012426};
DE EC=4.1.1.19 {ECO:0000256|ARBA:ARBA00012426};
GN Name=speA {ECO:0000313|EMBL:EIK45786.1};
GN ORFNames=O59_001425 {ECO:0000313|EMBL:EIK45786.1};
OS Cellvibrio sp. BR.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1134474 {ECO:0000313|EMBL:EIK45786.1, ECO:0000313|Proteomes:UP000003395};
RN [1] {ECO:0000313|EMBL:EIK45786.1, ECO:0000313|Proteomes:UP000003395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BR {ECO:0000313|EMBL:EIK45786.1,
RC ECO:0000313|Proteomes:UP000003395};
RA Peng Y.Y., Li N.Z., Xia T., Qiu R.R.;
RL Submitted (MAY-2012) 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:EIK45786.1}.
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DR EMBL; AICM01000002; EIK45786.1; -; Genomic_DNA.
DR AlphaFoldDB; I3ICK1; -.
DR STRING; 1134474.O59_001425; -.
DR PATRIC; fig|1134474.3.peg.1275; -.
DR eggNOG; COG1166; Bacteria.
DR HOGENOM; CLU_027243_1_0_6; -.
DR Proteomes; UP000003395; 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, ECO:0000313|EMBL:EIK45786.1};
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 Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066}.
FT DOMAIN 103..349
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 378..455
FT /note="Arginine decarboxylase helical bundle"
FT /evidence="ECO:0000259|Pfam:PF17810"
FT DOMAIN 584..637
FT /note="Arginine decarboxylase C-terminal helical"
FT /evidence="ECO:0000259|Pfam:PF17944"
FT ACT_SITE 506
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 639 AA; 70953 MW; A96EA6C08127894A CRC64;
MNTSEQAAVW SSRTSAELYG IDEWSNGYFG ISPEGEVIVR APNVDGETSV SLMSIVDGLQ
QRGLQMPVLL RVENILDSRI SILNDSFAQA IEVSGYQGCY RGAFPIKVNQ QSNVIAEIAR
FGERYNHGLE AGSKAELMIA LATLTNRDSL IICNGYKDSE FISLGLQARK LGFKCFFVLE
TLSELQSVIE CSRSLDVEPL IGVRLKLSTK VEGHWSEDSG DRSLFGLNTN ELVSVIDTLR
DANLLHCFQL LHFHLGSQIP NIRSIRAGVL EACRYYIELV GEGAPLGYLD LGGGLAIDYD
GTCSTNGHSR NYSVQEYCID VVEAIQESLD QHQIPHPTIV TESGRATVAH TSVLLFNILD
VTHFEPTAMP ESLPAGCHEM IANLWHTLSV IRVANLQESY NDVIYYRDKI RDLFHSGDIS
LRHRVLGENI YLAALQKIAA LLPQMKRIPA ELESLPQLLA DIYYGNFSVF QSLPDSWAIG
QIFPVMPIHR LNEEPTRQAI IADLTCDCDG KLQKFATSAG ESTTLPLHAI NAGDEYYLGV
FLVGAYQETL GDLHNLFGDT NVASVRINAD KSIDFVHELH GDSIADVLSY VEYKPNSLYE
QFRQTAEQAV RDGVISIADR QQMLSAYSES LRGYTYFEK
//
