(data stored in ACNUC9543 zone)

SWISSPROT: A0A0E1NRC2_YERPA

ID   A0A0E1NRC2_YERPA        Unreviewed;       659 AA.
AC   A0A0E1NRC2;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   08-MAY-2019, entry version 35.
DE   RecName: Full=Biosynthetic arginine decarboxylase {ECO:0000256|HAMAP-Rule:MF_01417};
DE            Short=ADC {ECO:0000256|HAMAP-Rule:MF_01417};
DE            EC=4.1.1.19 {ECO:0000256|HAMAP-Rule:MF_01417};
GN   Name=speA {ECO:0000256|HAMAP-Rule:MF_01417};
GN   OrderedLocusNames=YPA_0336 {ECO:0000313|EMBL:ABG12304.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12304.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12304.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12304.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- FUNCTION: Catalyzes the biosynthesis of agmatine from arginine.
CC       {ECO:0000256|HAMAP-Rule:MF_01417, ECO:0000256|SAAS:SAAS01129446}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-arginine = agmatine + CO2; Xref=Rhea:RHEA:17641,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:32682,
CC         ChEBI:CHEBI:58145; EC=4.1.1.19; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01417, ECO:0000256|SAAS:SAAS01117636};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01417, ECO:0000256|SAAS:SAAS00722737};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01417,
CC         ECO:0000256|PIRSR:PIRSR001336-50,
CC         ECO:0000256|SAAS:SAAS00373528};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC       agmatine from L-arginine: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01417}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II
CC       family. SpeA subfamily. {ECO:0000256|HAMAP-Rule:MF_01417,
CC       ECO:0000256|SAAS:SAAS00722488}.
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DR   EMBL; CP000308; ABG12304.1; -; Genomic_DNA.
DR   RefSeq; WP_002209969.1; NZ_CP009906.1.
DR   SMR; A0A0E1NRC2; -.
DR   EnsemblBacteria; ABG12304; ABG12304; YPA_0336.
DR   EnsemblBacteria; AJJ79421; AJJ79421; CH58_3184.
DR   KEGG; ypa:YPA_0336; -.
DR   PATRIC; fig|360102.15.peg.3342; -.
DR   KO; K01585; -.
DR   OMA; LFPIMPI; -.
DR   UniPathway; UPA00186; UER00284.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR   GO; GO:0009446; P:putrescine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06830; PLPDE_III_ADC; 1.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 1.
DR   HAMAP; MF_01417; SpeA; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR040634; Arg_decarb_HB.
DR   InterPro; IPR041128; Arg_decarbox_C.
DR   InterPro; IPR002985; Arg_decrbxlase.
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   InterPro; IPR029066; PLP-binding_barrel.
DR   PANTHER; PTHR43295; PTHR43295; 1.
DR   Pfam; PF17810; Arg_decarb_HB; 1.
DR   Pfam; PF17944; Arg_decarbox_C; 1.
DR   Pfam; PF02784; Orn_Arg_deC_N; 1.
DR   PIRSF; PIRSF001336; Arg_decrbxlase; 1.
DR   PRINTS; PR01180; ARGDCRBXLASE.
DR   PRINTS; PR01179; ODADCRBXLASE.
DR   SUPFAM; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 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;
DR   PRODOM; A0A0E1NRC2.
DR   SWISS-2DPAGE; A0A0E1NRC2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_01417,
KW   ECO:0000256|SAAS:SAAS00773685};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01417, ECO:0000256|SAAS:SAAS00773690,
KW   ECO:0000313|EMBL:ABG12304.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01417,
KW   ECO:0000256|SAAS:SAAS00722569};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01417,
KW   ECO:0000256|SAAS:SAAS01129452};
KW   Polyamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01417,
KW   ECO:0000256|SAAS:SAAS01129445};
KW   Putrescine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01417};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01417,
KW   ECO:0000256|PIRSR:PIRSR001336-50, ECO:0000256|SAAS:SAAS00272807};
KW   Spermidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01417,
KW   ECO:0000256|SAAS:SAAS00722663}.
FT   DOMAIN      101    368       Orn_Arg_deC_N. {ECO:0000259|Pfam:
FT                                PF02784}.
FT   DOMAIN      393    479       Arg_decarb_HB. {ECO:0000259|Pfam:
FT                                PF17810}.
FT   DOMAIN      607    656       Arg_decarbox_C. {ECO:0000259|Pfam:
FT                                PF17944}.
FT   REGION      308    318       Substrate-binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01417}.
FT   MOD_RES     128    128       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01417,
FT                                ECO:0000256|PIRSR:PIRSR001336-50}.
SQ   SEQUENCE   659 AA;  74104 MW;  AD2795F60745B686 CRC64;
     MSDDNLISRP LTAGAHVSLR SMQEVAMNDR NASKMLSTYN VAYWGGNYYD VNELGHISVC
     PDPDIREARV DLAQLVKKMQ LEQGQRLPAL FCFPQILQHR LRSINAAFKR ARESFGYEGG
     YFLVYPIKVN QHRRVIESLV NSGEPLGLEA GSKAEMMAVL AHAGMTRSVI VCNGYKDREY
     IRLALIGEKL GHKVYLVIEK MSEIKMVLEE AERLNVVPRL GVRARLASQG SGKWQASGGE
     KSKFGLSATQ VLQLVDMLRE ANSLESLQLL HFHLGSQLSN IRDISTGVRE SARFYVELHK
     LGVNIQCFDV GGGLGVDYEG TRSQSDCSVN YGLNEYANNV IWGIGDACNE HGLPHPTVIT
     ESGRAVTAHH TVLVSNVIGV ERNEFCEPQP PEAGAPRALE SLWDTWQEMQ EPENRRSLRE
     WLHDSQMDLH DVHTQYAHGM LDLTHRAWAE QLYLSICNEI QKQLDPSNRA HRPIIDELQE
     RMADKLYVNF SLFQSMPDAW GIDQLFPVLP LEGLDKPPER RAVLLDITCD SDGTIDHYID
     GDGVATTMPM PPYDPENPPL LGFFMVGAYQ EILGNMHNLF GDTAAVDVYV FPDGTVEVEQ
     TDEGDTVADM LEYVQLNPEK LLEHFRGQVK ETDLDTELQA QFLEEFEAGL YGYTYLEDE
//

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