ID   PDAD1_METAC             Reviewed;         165 AA.
AC   Q8TLM4;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   16-JUN-2009, entry version 48.
DE   RecName: Full=Pyruvoyl-dependent arginine decarboxylase 1;
DE            Short=PvlArgDC 1;
DE            EC=4.1.1.19;
DE   Contains:
DE     RecName: Full=Pyruvoyl-dependent arginine decarboxylase 1 subunit beta;
DE   Contains:
DE     RecName: Full=Pyruvoyl-dependent arginine decarboxylase 1 subunit alpha;
GN   Name=pdaD1; OrderedLocusNames=MA_3012;
OS   Methanosarcina acetivorans.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=2214;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   MEDLINE=21929760; PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P.,
RA   FitzHugh W., Calvo S., Engels R., Smirnov S., Atnoor D., Brown A.,
RA   Allen N., Naylor J., Stange-Thomann N., DeArellano K., Johnson R.,
RA   Linton L., McEwan P., McKernan K., Talamas J., Tirrell A., Ye W.,
RA   Zimmer A., Barber R.D., Cann I., Graham D.E., Grahame D.A., Guss A.M.,
RA   Hedderich R., Ingram-Smith C., Kuettner H.C., Krzycki J.A.,
RA   Leigh J.A., Li W., Liu J., Mukhopadhyay B., Reeve J.N., Smith K.,
RA   Springer T.A., Umayam L.A., White O., White R.H., de Macario E.C.,
RA   Ferry J.G., Jarrell K.F., Jing H., Macario A.J.L., Paulsen I.T.,
RA   Pritchett M., Sowers K.R., Swanson R.V., Zinder S.H., Lander E.,
RA   Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic
RT   and physiological diversity.";
RL   Genome Res. 12:532-542(2002).
CC   -!- CATALYTIC ACTIVITY: L-arginine = agmatine + CO(2).
CC   -!- COFACTOR: Pyruvoyl group (By similarity).
CC   -!- SIMILARITY: Belongs to the pdaD family.
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DR   EMBL; AE010299; AAM06385.1; -; Genomic_DNA.
DR   RefSeq; NP_617905.1; -.
DR   GeneID; 1474906; -.
DR   GenomeReviews; AE010299_GR; MA_3012.
DR   KEGG; mac:MA3012; -.
DR   NMPDR; fig|188937.1.peg.2931; -.
DR   HOGENOM; Q8TLM4; -.
DR   OMA; Q8TLM4; ISEYHAY.
DR   BioCyc; MACE188937:MA3012-MON; -.
DR   BRENDA; 4.1.1.19; 275708.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:HAMAP.
DR   GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR   HAMAP; MF_01404; -; 1.
DR   InterPro; IPR016105; Pyr-dep_his/arg-deCO2ase_sand.
DR   InterPro; IPR002724; Pyruvoyl-dep_arg_deCO2ase.
DR   Gene3D; G3DSA:3.50.20.10; Pyr-dep_his/arg-deCO2ase_sand; 1.
DR   Pfam; PF01862; PvlArgDC; 1.
DR   PIRSF; PIRSF005216; Pyruvoyl-dep_arg_deCO2ase; 1.
DR   ProDom; PD010449; DUF44; 1.
DR   TIGRFAMs; TIGR00286; PvlArgDC; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Decarboxylase; Lyase; Pyruvate.
FT   CHAIN         1     44       Pyruvoyl-dependent arginine decarboxylase
FT                                1 subunit beta (By similarity).
FT                                /FTId=PRO_0000023310.
FT   CHAIN        45    165       Pyruvoyl-dependent arginine decarboxylase
FT                                1 subunit alpha (By similarity).
FT                                /FTId=PRO_0000023311.
FT   SITE         44     45       Cleavage (non-hydrolytic) (By
FT                                similarity).
FT   MOD_RES      45     45       Pyruvic acid (Ser) (By similarity).
SQ   SEQUENCE   165 AA;  18075 MW;  CE50420335EE4139 CRC64;
     MITKLIPRKV FFTSGVGLHS EKLESFEVSL RDAGIEKFNL VTVSSILPPN CEIVTKEEGL
     KELSPGEVVF CVMSRISSNE PGKTLSTSVG CALPRDISKH GYISEYHAYE ENAQDVGEHA
     KKLAGSMYST WTNEAPLKTF SIPRSSSVQE SGDWMTVISA AVFII
//