ID   SPEA2_SYNY3             Reviewed;         659 AA.
AC   P72587;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   24-JAN-2024, entry version 142.
DE   RecName: Full=Biosynthetic arginine decarboxylase 2;
DE            Short=ADC 2;
DE            EC=4.1.1.19;
GN   Name=speA2; Synonyms=speA; OrderedLocusNames=slr1312;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC   Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-302.
RA   Mulo P., Eloranta T., Aro E.M., Maenpaeae P.;
RT   "Disruption of a spe-like open reading frame alters polyamine content and
RT   psbA-2 mRNA stability in the cyanobacterium Synechocystis sp. PCC 6803.";
RL   Bot. Acta 111:71-76(1998).
CC   -!- FUNCTION: Catalyzes the biosynthesis of agmatine from arginine.
CC       {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       SpeA subfamily. {ECO:0000305}.
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DR   EMBL; BA000022; BAA16587.1; -; Genomic_DNA.
DR   EMBL; X96602; CAA65422.1; -; Genomic_DNA.
DR   PIR; S74435; S74435.
DR   AlphaFoldDB; P72587; -.
DR   SMR; P72587; -.
DR   STRING; 1148.gene:10497442; -.
DR   PaxDb; 1148-1651659; -.
DR   EnsemblBacteria; BAA16587; BAA16587; BAA16587.
DR   KEGG; syn:slr1312; -.
DR   eggNOG; COG1166; Bacteria.
DR   InParanoid; P72587; -.
DR   PhylomeDB; P72587; -.
DR   BRENDA; 4.1.1.19; 6192.
DR   Proteomes; UP000001425; 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; 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.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Magnesium; Metal-binding; Polyamine biosynthesis;
KW   Pyridoxal phosphate; Reference proteome; Spermidine biosynthesis.
FT   CHAIN           1..659
FT                   /note="Biosynthetic arginine decarboxylase 2"
FT                   /id="PRO_0000149982"
FT   BINDING         311..321
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         119
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   659 AA;  74477 MW;  E8442002C8CD4629 CRC64;
     MGEEPVPADK ALGKKFKKKN ASWSIEESEA LYRVEAWGAP YFAINAAGNI TVSPNGDRGG
     SLDLLELVEA LRQRKLGLPL LIRFSDILAD RLERLNSCFA KAIARYNYPN TYQAVYPVKC
     NQQRHLVEAL VRFGQTSQCG LEAGSKPELM IALATLPPPL DRQDKHTKPL IICNGYKDQD
     YLETALLAKR LGHRPIIIIE QLRELEWVLH ISQQLNIKPM LGVRARLSCQ SLKSSEISSG
     NGDRAKLGLT MPDIVTVIHR LEENNCLDCL KMLHFHLGTQ VSDIALIKEA MREASQLYVE
     LVKLGAKMRY LNVGGGLAVD YDGSKTNYPA SKNYNMQNYA NDIVAAIQDA CELGQVSPPI
     LVSESGRAIM AHQSVLVFDV LGSNQTGFSE PHPPDENAHP LLKNLWECYE TITAEQYQEQ
     YHDALQLKTE ASSLFNFGYL SLTERGQAEQ IHWACCRKIF EITRQLEYIP EDFQALDKIM
     TDIYYVNLSV FQSAPESWSL DQLFPILPIH HLNEKPSQRV ILADLTCDSD GKIDRFIDLW
     DVKSYLEVHP LENDGNPYYL GMFLVGAYQE IMGNLHNLFG DINVVHIATT PQGYQIESVV
     RGDTMTEVLG YVQYDSDDLL EGLRRHTELA LSNGQITLEE SRRLLEDYEQ SLRRYTYLS
//