ID   SPEA_GLOVI              Reviewed;         644 AA.
AC   Q7NE10;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 106.
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=gll4070;
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Gloeobacterales; Gloeobacteraceae;
OC   Gloeobacter.
OX   NCBI_TaxID=251221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421;
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA   Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(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; BA000045; BAC92011.1; -; Genomic_DNA.
DR   RefSeq; NP_927016.1; NC_005125.1.
DR   RefSeq; WP_011144058.1; NC_005125.1.
DR   AlphaFoldDB; Q7NE10; -.
DR   SMR; Q7NE10; -.
DR   STRING; 251221.gene:10761588; -.
DR   EnsemblBacteria; BAC92011; BAC92011; BAC92011.
DR   KEGG; gvi:gll4070; -.
DR   PATRIC; fig|251221.4.peg.4102; -.
DR   eggNOG; COG1166; Bacteria.
DR   HOGENOM; CLU_027243_1_0_3; -.
DR   InParanoid; Q7NE10; -.
DR   OrthoDB; 9802658at2; -.
DR   PhylomeDB; Q7NE10; -.
DR   Proteomes; UP000000557; 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..644
FT                   /note="Biosynthetic arginine decarboxylase"
FT                   /id="PRO_0000149963"
FT   BINDING         282..292
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
FT   MOD_RES         100
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
SQ   SEQUENCE   644 AA;  72694 MW;  B70B2C69C7B352A2 CRC64;
     MQDWTIEDSA ELYQIHGWGE PYFKINDKGH VAVMPRGEGN GEIDLFHLVQ DIQKRGLNMP
     MLIRFSDILA DRIARLNACF VEAIREYDYP GIYKGVYPVK VNQQRHVVEE VVEFGRPFQY
     GLEAGSKPEL LIALATLKTP GALIICNGYK DSEYIETALL AQRLGHTPFV VIERFHELTL
     LIEAAQKLGI RPLIGVRAKL TARGIGRWGD STGDRAKFGL SAGEIMEVVA QLKAADLLSS
     LQLLHFHIGS QISAINVIKT ALREASCVYV ELAQMGAPMQ YCDVGGGLAI DYDGSKTNFR
     ASKNYNMQEY AYDVVAAFQD ACRTKNVPVP TLVSESGRAI TSHQSVLVFD VMGVSHLQFG
     EPEPPARNEH SIIRNLYETY TQITPDNVQE AFNDASQFKE EALSLFALGY LGLGERARAE
     RLYWGCCEKI LNLVRELDYI PDELADLEKN MASTYYCNFS VFQSAPDSWA IDQLFPIMPI
     HRLDEEPKAR GTLADLTCDS DGKIDQFIDL RDVKGVLELH PVRPEEPYYL GMFLNGAYQE
     ILGDMHNLFG DTNTVHIHLA SDEPGEQSYR LEHVVKGDTM TEVLKYVQYD HEAMLESIRR
     ETEQALRERR ITLSESRLLL QHYERSLSGY TYLTNELQVE LAAR
//