ID   SPEA_ALHEH              Reviewed;         628 AA.
AC   Q0ACK8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Biosynthetic arginine decarboxylase;
DE            Short=ADC;
DE            EC=4.1.1.19;
GN   Name=speA; OrderedLocusNames=Mlg_0072;
OS   Alkalilimnicola ehrlichei (strain MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
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., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T.,
RA   King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T.,
RA   Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-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; CP000453; ABI55429.1; -; Genomic_DNA.
DR   RefSeq; YP_740919.1; -.
DR   GeneID; 4270350; -.
DR   GenomeReviews; CP000453_GR; Mlg_0072.
DR   KEGG; aeh:Mlg_0072; -.
DR   NMPDR; fig|187272.6.peg.68; -.
DR   HOGENOM; Q0ACK8; -.
DR   OMA; Q0ACK8; LICNGYK.
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; 1.
DR   PROSITE; PS00879; ODR_DC_2_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Decarboxylase; Lyase; Magnesium; Metal-binding;
KW   Polyamine biosynthesis; Pyridoxal phosphate; Spermidine biosynthesis.
FT   CHAIN         1    628       Biosynthetic arginine decarboxylase.
FT                                /FTId=PRO_1000024253.
FT   REGION      281    291       Substrate-binding (Potential).
FT   MOD_RES     101    101       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   628 AA;  69264 MW;  984DD1693C8BB682 CRC64;
     MSDWSIGLAR QVWSVQHWSG GYFDISDEGR VVARPDRDPA RAPLDLAGIA AEARHQGLGL
     PVLVRFLDIL HDRVDSLCQA FRQAMVEDGY RGGYRAVYPI KVNQQRRVVE EIIRHGNGRV
     GLEAGSKPEL MAVLALTPPG GTVVCNGYKD REYVRLALRG RQLGLQVHLV IEKASELELV
     LEEAAALGVT PSLGMRVRLA TIGAGKWQNT GGEKSKFGLT AAQALAVVDR LRAAGCLDWL
     RLLHFHLGSQ IPNIRDIRRG MREAARYYAE LRALGAPVET VDVGGGLGVD YEGSRSRSFC
     SMNYTVAEYA HNVVHALWQV CEDEGLPHPD IITESGRAMT AHHAVLITDV IDGDRVPGGA
     DLLAPADAAP RVLHELWTVW TGLDRRHPLE AYHDAAHGLA EAQELYAHGV LNLTDRARAE
     RIWQAVCHAL LQRLDPRRRP HRELLDELNE KLADKLFCNF SLFQSMPDVW AIDQIFPVLP
     LQRLDEPPAS RAVLQDLTCD SDGCIRGYVD RDGVESTLPL PPWRPGEPYL LGIFLVGAYQ
     EILGDMHNLF GDTHSVNVRL TGEGYALSGA AHGDTITDVL RYVDFDAEVL RGIYRERVVA
     AAGLDATARA QCLADLEAGL RGYTYLDT
//