SPEA_XYLF2
ID SPEA_XYLF2 Reviewed; 628 AA.
AC B2I6M1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=XfasM23_0106;
OS Xylella fastidiosa (strain M23).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=405441;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M23;
RX PubMed=20601474; DOI=10.1128/jb.00651-10;
RA Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT causing almond leaf scorch disease in California.";
RL J. Bacteriol. 192:4534-4534(2010).
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; CP001011; ACB91563.1; -; Genomic_DNA.
DR RefSeq; WP_004087585.1; NC_010577.1.
DR AlphaFoldDB; B2I6M1; -.
DR SMR; B2I6M1; -.
DR EnsemblBacteria; ACB91563; ACB91563; XfasM23_0106.
DR GeneID; 58015672; -.
DR KEGG; xfn:XfasM23_0106; -.
DR HOGENOM; CLU_027243_1_0_6; -.
DR OMA; AVEYTQH; -.
DR UniPathway; UPA00186; UER00284.
DR Proteomes; UP000001698; 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: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; 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; PS00879; ODR_DC_2_2; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Magnesium; Metal-binding; Polyamine biosynthesis;
KW Pyridoxal phosphate; Spermidine biosynthesis.
FT CHAIN 1..628
FT /note="Biosynthetic arginine decarboxylase"
FT /id="PRO_1000145605"
FT BINDING 279..289
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
FT MOD_RES 99
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
SQ SEQUENCE 628 AA; 69214 MW; 0E820F250B06A04A CRC64;
MTWSQDLAHK TYSIRHWADG YFEVNDAGHM VVMPLGGDGV RISLPEVVDA ARAAGAKLPL
LLRFPDILGH RLGKLQAAFA QAQSEWEYAG GYTAVYPIKV NQHRGVAGVL ASHQGDGFGL
EAGSKPELMA VLALSRPGGL IVCNGYKDRE YIRLALIGRK LGLKTFIVIE KPSELRMVLE
EAKTLDVLPG LGVRVRLASL GAGKWQNSGG DKAKFGLSPR QVLDVWKVLR GTEYADCLNV
MHFHMGSQIS NVRDIAKGMR EATRYFVELS RLGAKITHVD VGGGLGIDYE GTRSRSDCSI
NYGLQAYASH IVQPLASACE DYDLVPPRIV TECGRAMTAH HAVLIANVTE VEAVPEGRVP
GVCDDEPAVV RHMREIYGEL DARPAIELFY EAQHFHAEGL AAYTLGQIDL VHRARIDDLF
YAISHGVRER LSHEEKSHRP VLDELNERLV DKYFVNFSVF ESIPDVWAIN QIFPIVPIER
LNEVPTRRGV VCDLTCDSDG TVKQYVENES LDSALPLHVL RHGEAYRIGF FLVGAYQEIL
GDIHNLFGDT DAVEVAVDGR GYRIAQQRCG DTTDVMLDYV GYALDEVRRV YAQRIAAAGM
SAAESKALSD MLEAGLTGYP YLSDVPLE
