ID   SPEA_SHEB5              Reviewed;         637 AA.
AC   A3D3G2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
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=Sbal_1768;
OS   Shewanella baltica (strain OS155 / ATCC BAA-1091).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=325240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS155 / ATCC BAA-1091;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brettar I.,
RA   Klappenbach J., Konstantinidis K., Rodrigues J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS155.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC       agmatine from L-arginine: step 1/1. {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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000563; ABN61275.1; -; Genomic_DNA.
DR   RefSeq; WP_006081274.1; NC_009052.1.
DR   AlphaFoldDB; A3D3G2; -.
DR   SMR; A3D3G2; -.
DR   STRING; 325240.Sbal_1768; -.
DR   KEGG; sbl:Sbal_1768; -.
DR   HOGENOM; CLU_027243_1_0_6; -.
DR   OrthoDB; 9802658at2; -.
DR   UniPathway; UPA00186; UER00284.
DR   Proteomes; UP000001557; 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; 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; SSF51419; PLP-binding barrel; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Magnesium; Metal-binding; Polyamine biosynthesis;
KW   Pyridoxal phosphate; Spermidine biosynthesis.
FT   CHAIN           1..637
FT                   /note="Biosynthetic arginine decarboxylase"
FT                   /id="PRO_1000024265"
FT   BINDING         286..296
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
FT   MOD_RES         101
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
SQ   SEQUENCE   637 AA;  70894 MW;  ADF1EB11628530BF CRC64;
     MNDWSIDDAR AGYNVTHWSQ GFYGISDHGE VTVSPDPKNP DYKIGLNELA KDMVKAGVAL
     PVLVRFPQIL HHRVNSLCQA FDQAIQKYEY QADYLLVYPI KVNQQQTVVE EILASQASKE
     VPQLGLEAGS KPELMAVLAM AQKASSVIVC NGYKDNEYIR LALIGEKLGH KVYIVLEKLS
     ELKMVLAESK RLGVTPRLGL RARLAFQGKG KWQASGGEKS KFGLSAAQIL LVVEQLKQND
     MLDSLQLLHF HLGSQIANIR DIRQGVSEAG RFYCELRALG ASVNCFDVGG GLAVDYDGTR
     SQSNNSMNYG LTEYANNIVN VLTDICNEYE QPMPRIISES GRYLTAHHAV LITDVIGTEA
     YQPEDIQPPA EESPQLLHNM WHSWSELSGR ADQRALIEIY HDSQSDLQEA HSLFALGQLS
     LAERAWAEQA NLRVCHEVQG LLSAKNRYHR PIIDELNEKL ADKFFVNFSL FQSLPDAWGI
     DQVFPVLPLS GLDKAPERRA VMLDITCDSD GIVDQYVDGQ GIETTLPVPA WSADSPYLIG
     FFLVGAYQEI LGDMHNLFGD TNSAVVRIED NGVTNIESVL AGDTVADVLR YVNLDAVAFM
     RTYEELVNLH IAEDERAQIL EELQVGLKGY TYLEDFS
//