ID   SPEA_PARMW              Reviewed;         644 AA.
AC   Q7U3S0;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 114.
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=SYNW2359;
OS   Parasynechococcus marenigrum (strain WH8102).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC   Prochlorococcaceae; Parasynechococcus; Parasynechococcus marenigrum.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA   Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA   Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(2003).
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}.
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DR   EMBL; BX569695; CAE08874.1; -; Genomic_DNA.
DR   RefSeq; WP_011129212.1; NC_005070.1.
DR   AlphaFoldDB; Q7U3S0; -.
DR   SMR; Q7U3S0; -.
DR   STRING; 84588.SYNW2359; -.
DR   KEGG; syw:SYNW2359; -.
DR   eggNOG; COG1166; Bacteria.
DR   HOGENOM; CLU_027243_1_0_3; -.
DR   Proteomes; UP000001422; 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; 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; IPR022653; De-COase2_pyr-phos_BS.
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; 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..644
FT                   /note="Biosynthetic arginine decarboxylase"
FT                   /id="PRO_0000149980"
FT   BINDING         287..297
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
FT   MOD_RES         105
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
SQ   SEQUENCE   644 AA;  70760 MW;  FAAF6AE897BA61EC CRC64;
     MQVADSEGWS IQDSAALYGL DRWGEPYFTI NGRGHISVQP QGERGGSLDL VELVSELRGR
     NLGLPLLIRF DDILEDRLER LHAAFERAIA QYSYTGRYQG VFPVKCNQQR HVVEELVICG
     KRWNFGLEAG SKAELLIALS LLDDPEALLI CNGYKDRLYI ETAILARRLG RQPVVVIEQP
     DEVDRIIEAS KSLGAAPYIG VRAKLSSRST GRWGSSVGDK AKFGLSIPEL LATVERLRES
     NLLPDLRLLH FHIGSQINDI AVLKDALQEA GQIYVELTRL GAPMGFLDVG GGLGIDYDGS
     RTASAASTNY SLQNYANDVV ATVRECCEPN AVAVPTLVSE SGRAIASHFS LLVFDVLGSS
     ALSASIPNAS GDEPLTVRNL RDTLVTIQEL SGTADAQLVR LQEAWNDALK FKQDALAAFR
     LGYMGLPDRA SAEQLTWACA DAIAQRLPKE QAIPEELAAL SKALAGTYYA NLSIFRSAPD
     TWAIDQLFPV VPIQKLNQRP TRLANLADLT CDSDGRLDRF IGDGQPKQLL ELHELDDNNP
     YLIGLFLSGA YQEVMGNLHN LFGTTNAVHI RLSPGGSYRI DHVVRGDTNA DVLEAMEHDP
     RVLLERLRVA AEAAINDGQL RIDESRRLLD HLESSLRQTT YLQD
//