ID   SPEA_XANCP              Reviewed;         628 AA.
AC   Q8P448;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2004, sequence version 2.
DT   27-MAR-2024, entry version 108.
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=XCC3868;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
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; Evidence={ECO:0000255|HAMAP-
CC         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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM43099.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008922; AAM43099.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_639208.2; NC_003902.1.
DR   RefSeq; WP_011038943.1; NC_003902.1.
DR   AlphaFoldDB; Q8P448; -.
DR   SMR; Q8P448; -.
DR   STRING; 190485.XCC3868; -.
DR   EnsemblBacteria; AAM43099; AAM43099; XCC3868.
DR   GeneID; 58015160; -.
DR   KEGG; xcc:XCC3868; -.
DR   PATRIC; fig|190485.4.peg.4139; -.
DR   eggNOG; COG1166; Bacteria.
DR   HOGENOM; CLU_027243_1_0_6; -.
DR   OrthoDB; 9802658at2; -.
DR   Proteomes; UP000001010; 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; 1.10.287.3440; -; 1.
DR   Gene3D; 1.20.58.930; -; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 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   NCBIfam; TIGR01273; speA; 1.
DR   PANTHER; PTHR43295; ARGININE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43295:SF9; BIOSYNTHETIC ARGININE DECARBOXYLASE; 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; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 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..628
FT                   /note="Biosynthetic arginine decarboxylase"
FT                   /id="PRO_0000149988"
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;  69036 MW;  4500A6D75CDC12F2 CRC64;
     MSDWSLDQAR KTYSIPHWAD GYFDVNDAGH VVVRPTADGP AVSLPEVVDA ARAAGAKLPL
     LVRFPDILGQ RLGKLQAAFA QAQADWDYAG GYTAVYPIKV NQHRGVAGTL ASHHGEGFGL
     EAGSKPELMA VLALSRPGGL IVCNGYKDRE YIRLALIGRK LGLQTFIVIE KPSELNLVLE
     EARALDVKPG LGVRMRLASL GAGKWQNSGG DKAKFGLSPR QVLDLWKSLR DTEYADSLNL
     LHFHMGSQIS NVRDIANGMR EATRYFVELS RLGAKISHVD VGGGLGIDYE GTRSRSYCSI
     NYGLHSYASN IVQPLASACE EHGLPPPRIV TECGRAMTAH HAVLIANVSE VEQAPEGRVP
     DAHDDEPAAI RHLREIHDEL DVRPAVELFQ EAQHFHAEGL SAYALGQIDL THRARIDDLF
     YAIAHGVRAR LSFDEKSHRP VLDELNERLV DKYFVNFSVF ESIPDVWAID QVFPIVPIER
     LNEAPQRRGI IADMTCDSDG MVKTYVENES LDSSLPLHGL NPGESYRIGF FLVGAYQEIL
     GDIHNLFGDT DAVEVAVDGT GYRIAQQRRG DTTDVMLDYV GYQLDTLRAT YAERIAAAQL
     PPERAQELHD ALEAGLTGYT YLSDEPLG
//