SPE1_DIACA
ID SPE1_DIACA Reviewed; 725 AA.
AC Q96412;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Arginine decarboxylase;
DE Short=ADC;
DE Short=ARGDC;
DE EC=4.1.1.19;
GN Name=ADC;
OS Dianthus caryophyllus (Carnation) (Clove pink).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Caryophyllaceae; Caryophylleae; Dianthus.
OX NCBI_TaxID=3570;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. White Sim;
RA Chang K.S., Nam K.H., Lee M.M., Lee S.H., Park K.Y.;
RT "Nucleotide sequence of cDNA encoding arginine decarboxylase from carnation
RT flowers.";
RL (er) Plant Gene Register PGR96-092(1996).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-arginine = agmatine + CO2; Xref=Rhea:RHEA:17641,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:58145; EC=4.1.1.19;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC agmatine from L-arginine: step 1/1.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC SpeA subfamily. {ECO:0000305}.
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DR EMBL; U63832; AAB67887.1; -; mRNA.
DR PIR; T10721; T10721.
DR AlphaFoldDB; Q96412; -.
DR SMR; Q96412; -.
DR UniPathway; UPA00186; UER00284.
DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR GO; GO:0009446; P:putrescine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06830; PLPDE_III_ADC; 1.
DR Gene3D; 2.40.37.10; -; 1.
DR Gene3D; 3.20.20.10; -; 1.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_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 PANTHER; PTHR43295; PTHR43295; 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; SSF50621; 1.
DR SUPFAM; SSF51419; SSF51419; 1.
DR TIGRFAMs; TIGR01273; speA; 1.
DR PROSITE; PS00878; ODR_DC_2_1; 1.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
PE 2: Evidence at transcript level;
KW Decarboxylase; Lyase; Magnesium; Putrescine biosynthesis;
KW Pyridoxal phosphate; Spermidine biosynthesis.
FT CHAIN 1..725
FT /note="Arginine decarboxylase"
FT /id="PRO_0000149950"
FT BINDING 340..350
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 156
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 725 AA; 77676 MW; 6B1C8BA09DE19355 CRC64;
MPAVACYVDT SAAVYGGAGA LSLPASEINF SGVPPTTTST TVNQPPPPQQ WSPSLSAELY
RIDRWGPPYF AVNSSGNVTV KPFGDATLPH QEIDLLKVVK KVSDSKSSSG LGLHLPVIIR
FPDVLKHRLE SLQSAFDFAV RTHGYGSHYQ GVYPVKCNQD RYIVEDIVEF GSGFRFGLEA
GSKPELLMAM SSLCKGSPDS LLVCNGFKDA EYISLAIIGR KLGLNTVIVI EQEEEVDMAI
ELSRKMGIRP VVGVRAKLRT KHSGHFGSTS GEKGKFGLTT TQILRVVRKL ENFGMLDCLQ
LLHFHIGSQI PTTTLLSDGV AEASQVYCEL TRLGAHMRVI DIGGGLGIDY DGSKSGDSDL
SVGYTLEEYA SAVVGTVMSV CDRKGVKSPV ICSESVRAIV SHHSILVFEA VSSSSSASPP
MPGSTLALDY LVDGLTDEVK GEYRSLTAAA MRGEYESCLM YSGMLKQRCV ELFKDGCLGM
EQLAAVDGLC ELVSKALGVA DGVCTYNVNL SVFTSIPDFW GIGQLFPIMP IHRLDQQPKA
RGILSDLTCD SDGKIDKFIG DESSLPLHEL SGGEGYYLGM FLGGAYEEAL GGVHNLFGGP
SVVRVQQSDG PQSYAVTRAV PGPSSSDVLR VMHHEPELMF QTLKHRAEEC DNDYTAGPLA
DMLAQSFNST PYLVPGHATG SCGFSNGSGL VNGCREYFYG VDDGCNAAAV DAAAGEEEQW
SYVCA