ID   SPEA1_SYNY3             Reviewed;         695 AA.
AC   P74576;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Biosynthetic arginine decarboxylase 1;
DE            Short=ADC 1;
DE            EC=4.1.1.19;
GN   Name=speA1; Synonyms=speA; OrderedLocusNames=slr0662;
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).
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; BAA18683.1; -; Genomic_DNA.
DR   PIR; S76771; S76771.
DR   AlphaFoldDB; P74576; -.
DR   SMR; P74576; -.
DR   IntAct; P74576; 2.
DR   STRING; 1148.gene:10500454; -.
DR   PaxDb; 1148-1653772; -.
DR   EnsemblBacteria; BAA18683; BAA18683; BAA18683.
DR   KEGG; syn:slr0662; -.
DR   eggNOG; COG1166; Bacteria.
DR   InParanoid; P74576; -.
DR   PhylomeDB; P74576; -.
DR   BRENDA; 4.1.1.19; 382.
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; 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..695
FT                   /note="Biosynthetic arginine decarboxylase 1"
FT                   /id="PRO_0000149981"
FT   BINDING         332..342
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         141
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   695 AA;  78239 MW;  E90EB699D666320D CRC64;
     MEGQSIELEL SVMAMPELID STEAGHTAGV KTDSNPQAIA QDRRWTIDDS ENLYRITGWG
     EPYFSINAAG HVTVSPQADH GGALDLYELV KGLRQRNIGL PLLLRFSDIL ADRINRLNAA
     FARGIARYRY PNTYRGVYPI KCNQHRHIVE SLVRYGTPYN FGLEAGSKPE LMIALAMLQP
     QENPEPDQQN QPLLICNGYK DREYIETALL ARRLGHRPII VVEQVAEVAL AIEISSNLGI
     KPILGVRAKL STQGMGRWGI STGDRAKFGL TIPEMLTAIE QLRRADMLDS LQLLHFHIGS
     QISSISVIKE AMTEASQIFV QLAKLGANMR YLDVGGGLGV DYDGSKTNFY ASKNYNIQNY
     VNDVISAVQD ACVAAEVPCP VLISESGRAI ASHQSVLIFD VVATNDINPP LPKVKGKDHA
     ILRNLMETWE TITVDNYQEA YHDVEQFKTE AISLFNFGYL GLKERAKAEE LYWACCRKIL
     QICRQQEYVP DDLENLEVNL ASIYYANMSV FQSAPDSWAI DQLFPIMPIH RLDEEPTQRG
     ILADITCDSD GKIDQFIDLR DVKSVLELHP LIEVHQPGTP PRVEPYYLGM FLVGAYQEIM
     GNLHNLFGDI NVVHIQMNPK GYQIEHLVRG DTIAEVLGYV QYDPEDLLEN MRRYCEQAME
     DKRMSLEEAQ LLLENYERSL LQYTYLKPTS GIHTS
//