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Database: UniProt
Entry: Q0HJY2
LinkDB: Q0HJY2
Original site: Q0HJY2 
ID   SPEA_SHESM              Reviewed;         637 AA.
AC   Q0HJY2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   11-JUN-2014, entry version 61.
DE   RecName: Full=Biosynthetic arginine decarboxylase;
DE            Short=ADC;
DE            EC=4.1.1.19;
GN   Name=speA; OrderedLocusNames=Shewmr4_1557;
OS   Shewanella sp. (strain MR-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60480;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-4;
RG   US DOE Joint Genome Institute;
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., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nealson K., Konstantinidis K., Klappenbach J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella sp. MR-4.";
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: 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.
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DR   EMBL; CP000446; ABI38635.1; -; Genomic_DNA.
DR   RefSeq; YP_733692.1; NC_008321.1.
DR   ProteinModelPortal; Q0HJY2; -.
DR   STRING; 60480.Shewmr4_1557; -.
DR   EnsemblBacteria; ABI38635; ABI38635; Shewmr4_1557.
DR   GeneID; 4252135; -.
DR   KEGG; she:Shewmr4_1557; -.
DR   PATRIC; 23579758; VBISheSp133532_1622.
DR   eggNOG; COG1166; -.
DR   HOGENOM; HOG000029191; -.
DR   KO; K01585; -.
DR   OMA; IDHYVDG; -.
DR   OrthoDB; EOG676Z0R; -.
DR   BioCyc; SSP60480:GI2N-1641-MONOMER; -.
DR   UniPathway; UPA00186; UER00284.
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   Gene3D; 3.20.20.10; -; 1.
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; IPR022644; De-COase2_N.
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; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR01273; speA; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Decarboxylase; Lyase; Magnesium; Metal-binding;
KW   Polyamine biosynthesis; Pyridoxal phosphate; Spermidine biosynthesis.
FT   CHAIN         1    637       Biosynthetic arginine decarboxylase.
FT                                /FTId=PRO_1000024272.
FT   REGION      286    296       Substrate-binding (Potential).
FT   MOD_RES     101    101       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   637 AA;  71019 MW;  1E26995E7BB168BD CRC64;
     MNDWSIDAAR AGYNVTHWSQ GFYGISDQGE VTVSPDPKNP DHKIGLNELA KDMVKAGVAL
     PVLVRFPQIL HHRVNSLCQA FDQAIQKYEY QADYLLVYPI KVNQQKTVVE EILASQASKE
     VPQLGLEAGS KPELMAVLAM AQKASSVIVC NGYKDNEYIR LALIGEKLGH KVYIVLEKLS
     ELKMVLAESK RLGVKPRLGL RARLAFQGKG KWQASGGEKS KFGLSAAQIL TVVDQLKEND
     MLDSLQLLHF HLGSQIANIR DIRQGVSEAA RFYCELRELG ASINCFDVGG GLAVDYDGTR
     SQSNNSMNYG LSEYANNIVN VLTDICNEYE QPMPRIISES GRHLTAHHAV LITDVIGTEA
     YQVEDIQPPA EESPQLLHNM WQSWTELSGR ADQRALIEIY HDSQSDLQEA QSLFALGQLS
     LAERAWAEQA NLRVCHEVQG LLSTKNRYHR PIIDELNEKL ADKFFVNFSL FQSLPDAWGI
     DQVFPVLPLS GLDKAPERRA VMLDITCDSD GIVDQYVDGQ GIETTLPVPA WSAESPYLMG
     FFMVGAYQEI LGDMHNLFGD TNSAVVSIEE NGMTNIESVL AGDTVADVLR YVNLDAVDFM
     RTYEELVNQH IVEEERAQIL EELQVGLKGY TYLEDFS
//
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