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Database: UniProt
Entry: Q96412
LinkDB: Q96412
Original site: Q96412 
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   26-NOV-2014, entry version 73.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; Caryophyllales; Caryophyllaceae; 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
RT   carnation flowers.";
RL   (er) Plant Gene Register PGR96-092.
CC   -!- CATALYTIC ACTIVITY: L-arginine = agmatine + CO(2).
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
CC       family. SpeA subfamily. {ECO:0000305}.
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DR   EMBL; U63832; AAB67887.1; -; mRNA.
DR   PIR; T10721; T10721.
DR   ProteinModelPortal; 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   Gene3D; 2.40.37.10; -; 2.
DR   Gene3D; 3.20.20.10; -; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR002985; Arg_decrbxlase.
DR   InterPro; IPR022643; De-COase2_C.
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   Pfam; PF02784; Orn_Arg_deC_N; 1.
DR   Pfam; PF00278; Orn_DAP_Arg_deC; 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       Arginine decarboxylase.
FT                                /FTId=PRO_0000149950.
FT   REGION      340    350       Substrate-binding. {ECO:0000250}.
FT   MOD_RES     156    156       N6-(pyridoxal phosphate)lysine.
FT                                {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
//
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