ID B5Z806_HELPG Unreviewed; 615 AA.
AC B5Z806;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=arginine decarboxylase {ECO:0000256|ARBA:ARBA00012426};
DE EC=4.1.1.19 {ECO:0000256|ARBA:ARBA00012426};
GN OrderedLocusNames=HPG27_951 {ECO:0000313|EMBL:ACI27705.1};
OS Helicobacter pylori (strain G27).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=563041 {ECO:0000313|EMBL:ACI27705.1, ECO:0000313|Proteomes:UP000001735};
RN [1] {ECO:0000313|EMBL:ACI27705.1, ECO:0000313|Proteomes:UP000001735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G27 {ECO:0000313|EMBL:ACI27705.1,
RC ECO:0000313|Proteomes:UP000001735};
RX PubMed=18952803; DOI=10.1128/JB.01416-08;
RA Baltrus D.A., Amieva M.R., Covacci A., Lowe T.M., Merrell D.S.,
RA Ottemann K.M., Stein M., Salama N.R., Guillemin K.;
RT "The complete genome sequence of Helicobacter pylori strain G27.";
RL J. Bacteriol. 191:447-448(2009).
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}.
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DR EMBL; CP001173; ACI27705.1; -; Genomic_DNA.
DR RefSeq; WP_001158578.1; NC_011333.1.
DR AlphaFoldDB; B5Z806; -.
DR KEGG; hpg:HPG27_951; -.
DR HOGENOM; CLU_027243_1_1_7; -.
DR Proteomes; UP000001735; Chromosome.
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; 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.
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 Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066}.
FT DOMAIN 77..331
FT /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02784"
FT DOMAIN 359..431
FT /note="Arginine decarboxylase helical bundle"
FT /evidence="ECO:0000259|Pfam:PF17810"
FT DOMAIN 561..611
FT /note="Arginine decarboxylase C-terminal helical"
FT /evidence="ECO:0000259|Pfam:PF17944"
FT ACT_SITE 487
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT MOD_RES 89
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001336-50"
SQ SEQUENCE 615 AA; 70257 MW; 49A7F60467B8184C CRC64;
MQEVHDYGIN FWSNNEFKIE KGLVKVCHGK NPSLLEIVQS VRDKGYRGPL LVRFPHLVQK
QIKSLFDAFS LAIKEYQYSG AFKAVFPLKV NQMPSFVFPL VQGAKGLDYG LEAGSKSELI
IAMSYTNPKA PITVNGFKDK EMIELGFIAK SMQHEITLTI EGLNELKTII AVAKQNDFVA
CPKIGIRIRL HSAGTGVWAK SGGINSKFGL SSTEVLEAMR LLEENDLLEH FHMIHFHIGS
QISDISPLKK ALREAGNLYA ELRKMGAKNL NSVNIGGGLA VEYTQHKHHQ DKNYTLEEFS
ADVVFLLREI VKNKQEIEPD IFIESGRYIS ANHAVLVAPV LELFSHEYNE KSLKIKESNN
PPLIDEMLDL LANINEKNAI EYLHDSFDHT ESLFTLFDLG YIDLIDRSNT EVLAHLIVKK
AVQLLYVKDH NDILRIQEQV QERYLLNCSF FQSLPDYWGL RQNFPVMPLN KLDEKPTRSA
SLWDITCDSD GEIAFDSTKP LFLHDIDIDE EEYFLAFFLV GAYQEVLGMK HNLFTHPTEF
SVVFDEKGDY EVEDICEAQT ILDVLDDLDY DTKEIERLLK QKIEDNNQLD MEEKKEIMGR
LYVMLSENGY LRTIS
//
