ID   SPEA_SHEDO              Reviewed;         636 AA.
AC   Q12LW6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Biosynthetic arginine decarboxylase;
DE            Short=ADC;
DE            EC=4.1.1.19;
GN   Name=speA; OrderedLocusNames=Sden_2280;
OS   Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=318161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of Shewanella denitrificans OS217.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the biosynthesis of agmatine from arginine (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: L-arginine = agmatine + CO(2).
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADC
CC       pathway; agmatine from L-arginine: step 1/1.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II
CC       family. SpeA subfamily.
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DR   EMBL; CP000302; ABE55560.1; -; Genomic_DNA.
DR   RefSeq; YP_563283.1; -.
DR   GeneID; 4018772; -.
DR   GenomeReviews; CP000302_GR; Sden_2280.
DR   KEGG; sdn:Sden_2280; -.
DR   NMPDR; fig|318161.14.peg.2221; -.
DR   HOGENOM; Q12LW6; -.
DR   OMA; Q12LW6; LICNGYK.
DR   BioCyc; SDEN318161:SDEN_2280-MON; -.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_01417; -; 1.
DR   InterPro; IPR002985; Arg_decrbxlase.
DR   InterPro; IPR000183; De-COase2.
DR   PANTHER; PTHR11482:SF3; Arg_decrbxlase; 1.
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   TIGRFAMs; TIGR01273; speA; 1.
DR   PROSITE; PS00878; ODR_DC_2_1; FALSE_NEG.
DR   PROSITE; PS00879; ODR_DC_2_2; FALSE_NEG.
PE   3: Inferred from homology;
KW   Complete proteome; Decarboxylase; Lyase; Magnesium; Metal-binding;
KW   Polyamine biosynthesis; Pyridoxal phosphate; Spermidine biosynthesis.
FT   CHAIN         1    636       Biosynthetic arginine decarboxylase.
FT                                /FTId=PRO_1000024267.
FT   REGION      286    296       Substrate-binding (Potential).
FT   MOD_RES     101    101       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   636 AA;  71065 MW;  67F1E19B36DD55CA CRC64;
     MNDWTIEDAR AGYNVTHWSQ GFYGIGEAGE VTVSPDPLNP SNKVALDTLA QDLVQAGIAL
     PVLVRFPQIL HHRVESLCDA FNQAIQKYEY QNDYLLVYPI KVNQQKTVVE EILASQVSKE
     VPQLGLEAGS KPELMAVLAM AQKASSVIVC NGYKDKEYVR LALIGEKLGH KVYIVLEKMS
     ELKMVLEEAR ELGVTPRLGL RTRLAFQGKG KWQASGGEKS KFGLSAAQVL KVVDELKEAN
     MLESLQLLHF HLGSQIANIR DIRQGVSEAG RFYCELRQLG ASINCFDVGG GLAVDYDGTR
     SQSNNSMNYG LTEYANNIVN VLTDLCNEYE QPMPRIISES GRHLTAHHAV LITDVIGTEA
     YMPENIQAPA EDAPQLLHNM WQSWTEISGR HDQRAIIEIY HDSQSDIAEA HSLFAVGQLS
     LMDRAWAEQT NLRVCHEVKG LLSNNNRYHR PVIDELNEKL ADKLFVNFSL FQSLPDAWGI
     DQVFPVLPLT CLDKAPERRA VMLDITCDSD GIVDQYVDGQ GIETTLPVPA WDPANPYLIG
     FFMVGAYQEI LGDMHNLFGD TNSAVVFVED NGKARIESTL DGDTVADVLR YVNLDADEFM
     HTYEELVEQH IVEDERASIL EELQLGLKGY TYLEDF
//