SPEA_YERPE
ID SPEA_YERPE Reviewed; 659 AA.
AC Q8ZHG8; Q0WIB1;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Biosynthetic arginine decarboxylase {ECO:0000255|HAMAP-Rule:MF_01417};
DE Short=ADC {ECO:0000255|HAMAP-Rule:MF_01417};
DE EC=4.1.1.19 {ECO:0000255|HAMAP-Rule:MF_01417};
GN Name=speA {ECO:0000255|HAMAP-Rule:MF_01417};
GN OrderedLocusNames=YPO0929, y3313, YP_3513;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
CC -!- FUNCTION: Catalyzes the biosynthesis of agmatine from arginine.
CC {ECO:0000255|HAMAP-Rule:MF_01417}.
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:0000255|HAMAP-
CC Rule:MF_01417};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01417};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01417};
CC -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC agmatine from L-arginine: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01417}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC SpeA subfamily. {ECO:0000255|HAMAP-Rule:MF_01417}.
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DR EMBL; AL590842; CAL19596.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM86863.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS63667.1; -; Genomic_DNA.
DR PIR; AB0114; AB0114.
DR RefSeq; WP_002209969.1; NZ_WUCM01000030.1.
DR RefSeq; YP_002345977.1; NC_003143.1.
DR AlphaFoldDB; Q8ZHG8; -.
DR SMR; Q8ZHG8; -.
DR IntAct; Q8ZHG8; 7.
DR STRING; 214092.YPO0929; -.
DR PaxDb; Q8ZHG8; -.
DR DNASU; 1148260; -.
DR EnsemblBacteria; AAM86863; AAM86863; y3313.
DR EnsemblBacteria; AAS63667; AAS63667; YP_3513.
DR GeneID; 66844367; -.
DR KEGG; ype:YPO0929; -.
DR KEGG; ypk:y3313; -.
DR KEGG; ypm:YP_3513; -.
DR PATRIC; fig|214092.21.peg.1206; -.
DR eggNOG; COG1166; Bacteria.
DR HOGENOM; CLU_027243_1_0_6; -.
DR OMA; AVEYTQH; -.
DR BRENDA; 4.1.1.19; 4559.
DR UniPathway; UPA00186; UER00284.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0008792; F:arginine decarboxylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR GO; GO:0033388; P:putrescine biosynthetic process from arginine; IBA:GO_Central.
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;
KW Decarboxylase; Lyase; Magnesium; Metal-binding; Polyamine biosynthesis;
KW Putrescine biosynthesis; Pyridoxal phosphate; Reference proteome;
KW Spermidine biosynthesis.
FT CHAIN 1..659
FT /note="Biosynthetic arginine decarboxylase"
FT /id="PRO_0000149991"
FT BINDING 308..318
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
FT MOD_RES 128
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
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