SPEA_PSEAE
ID SPEA_PSEAE Reviewed; 636 AA.
AC Q9HUX1;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
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}; OrderedLocusNames=PA4839;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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 -!- 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; AE004091; AAG08224.1; -; Genomic_DNA.
DR PIR; H83040; H83040.
DR RefSeq; NP_253526.1; NC_002516.2.
DR RefSeq; WP_003095365.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; Q9HUX1; -.
DR SMR; Q9HUX1; -.
DR STRING; 287.DR97_2189; -.
DR PaxDb; Q9HUX1; -.
DR PRIDE; Q9HUX1; -.
DR EnsemblBacteria; AAG08224; AAG08224; PA4839.
DR GeneID; 879594; -.
DR KEGG; pae:PA4839; -.
DR PATRIC; fig|208964.12.peg.5070; -.
DR PseudoCAP; PA4839; -.
DR HOGENOM; CLU_027243_1_0_6; -.
DR InParanoid; Q9HUX1; -.
DR OMA; AVEYTQH; -.
DR PhylomeDB; Q9HUX1; -.
DR BioCyc; MetaCyc:MON-12; -.
DR BioCyc; PAER208964:G1FZ6-4953-MON; -.
DR BRENDA; 4.1.1.19; 5087.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0008792; F:arginine decarboxylase activity; IMP:CACAO.
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; IMP:PseudoCAP.
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 Pyridoxal phosphate; Reference proteome; Spermidine biosynthesis.
FT CHAIN 1..636
FT /note="Biosynthetic arginine decarboxylase"
FT /id="PRO_0000149971"
FT BINDING 290..300
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
FT MOD_RES 110
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
SQ SEQUENCE 636 AA; 70668 MW; E7274FD432E0D187 CRC64;
MAARRTRKDD GSNWTVADSR GVYGIRHWGA GYFAINDGGN VEVRPQGADS TPIDLYELVG
QLREAGLSLP LLVRFPDILQ DRVRKLTGAF DANIERLEYQ SRYTALYPIK VNQQEAVVEN
IIATENVSIG LEAGSKPELM AVLALAPKGG TIVCNGYKDR EFIKLALMGQ KLGHNVFIVI
EKESEVQLVI EEAANVGVQP QVGLRVRLSS LASSKWADTG GEKAKFGLSA AQLLSVVERF
RQAGLDQGVR LLHFHMGSQI ANLADYQHGF KEAIRYYGEL RALGLPVDHI DVGGGLGVDY
DGTHSRNASS INYDIDDYAG VVVGMLKEFC DAQGLPHPHI FSESGRALTA HHAVLITQVT
DVERHNDDVP KIVDLDEQPE IVRWLAELLG PTDAEMVTET YWRATHYIGD AAAQYADGKI
SLAQKALAEQ CYFAICRRLH NQLKARQRSH RQVLDELNDK LADKYICNFS VFQSLPDTWA
IGQVLPILPL HRLGEEPDRR AVLQDLTCDS DGKITQYVDE QSIETSLPVH EVKEGEDYLI
GVFLVGAYQE ILGDMHNLFG DTDSVNVYQR ADGGIYHAGI ETHDTIEDML RYVHLSPEEL
MTLYRDKVAG AKLTARERNQ YLDALRLGLT RSAYLS
