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Database: UniProt
Entry: Q7V3M9
LinkDB: Q7V3M9
Original site: Q7V3M9 
ID   SPEA_PROMP              Reviewed;         648 AA.
AC   Q7V3M9;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   19-FEB-2014, entry version 66.
DE   RecName: Full=Biosynthetic arginine decarboxylase;
DE            Short=ADC;
DE            EC=4.1.1.19;
GN   Name=speA; OrderedLocusNames=PMM0045;
OS   Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4).
OC   Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1986 / MED4;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P.,
RA   Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R.,
RA   Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M.,
RA   Shaw S.L., Steglich C., Sullivan M.B., Ting C.S., Tolonen A.,
RA   Webb E.A., Zinser E.R., Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic
RT   niche differentiation.";
RL   Nature 424:1042-1047(2003).
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   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II
CC       family. SpeA subfamily.
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DR   EMBL; BX548174; CAE18504.1; -; Genomic_DNA.
DR   RefSeq; NP_892166.1; NC_005072.1.
DR   ProteinModelPortal; Q7V3M9; -.
DR   STRING; 59919.PMM0045; -.
DR   EnsemblBacteria; CAE18504; CAE18504; PMM0045.
DR   GeneID; 1726342; -.
DR   KEGG; pmm:PMM0045; -.
DR   PATRIC; 23030720; VBIProMar68066_0046.
DR   eggNOG; COG1166; -.
DR   HOGENOM; HOG000029191; -.
DR   KO; K01585; -.
DR   OMA; MIHFHIG; -.
DR   OrthoDB; EOG676Z0R; -.
DR   ProtClustDB; PRK05354; -.
DR   BioCyc; PMAR59919:GJMQ-45-MONOMER; -.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-HAMAP.
DR   Gene3D; 2.40.37.10; -; 2.
DR   HAMAP; MF_01417; SpeA; 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   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   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    648       Biosynthetic arginine decarboxylase.
FT                                /FTId=PRO_0000149970.
FT   REGION      291    301       Substrate-binding (Potential).
FT   MOD_RES     109    109       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   648 AA;  73425 MW;  E7878AB68E181CCE CRC64;
     MTDFDTKKLN KKWTIEDSIS TYGIDKWGEK YFSINSEGNI SISPDNKSQK KIDLFKLVKE
     FKSREINTPL IIRFNDILKD RIAELNNAFS QAIETYDYKN IYKGVFPIKC NQQRNVLEKI
     IEYGDRWNFG LEVGSKSELL IGLSILENQK SLLICNGYKD KKYIETAILA RKLGKHPIIV
     IEQRDEVKRI IEAVKDLKAT PILGIRSKLS SKSSGRWSKS VGDNSKFGLS IPEIMLTIKE
     LKEANLINEM MLLHFHVGSQ ISDISVIKDA LQEASQIFVE LSKLGAPMKY IDVGGGLGID
     FDGTKMSSNT STNYSLQNYA NDVIATVKDS CEVNNIQHPI IISESGRAII SHCSVLIFNI
     LGTSHVSSQV KVSDQKKQSL IITNLIETLN QIKNLRDKKE DLSEIIELWN DAKKFKEDCL
     VAFRLGFICL EERAYAEELT WACAKEIANQ LENNEIIHPD LSEITDTLAS TYYANLSVFK
     SIPDTWAINQ VFPIIPIHRH LEEPFCKGHF ADLTCDSDGK LNNFIDNGKI KSLLNLHPPE
     KNNDYLIGIF MAGAYQEALG NFHNLFGNTN VIHIDINEDN SYKIKNIIKE NSKSEILELL
     DYSSDNLVES IRVNTESAIN NKTLTIQEAR KLIDQIETSL RKSSYLSE
//
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