ID   SPEA_SHEON              Reviewed;         637 AA.
AC   Q8EFU5;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
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}; OrderedLocusNames=SO_1870;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
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;
CC         Evidence={ECO:0000255|HAMAP-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; AE014299; AAN54922.1; -; Genomic_DNA.
DR   RefSeq; NP_717478.1; NC_004347.2.
DR   RefSeq; WP_011071982.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EFU5; -.
DR   SMR; Q8EFU5; -.
DR   STRING; 211586.SO_1870; -.
DR   PaxDb; Q8EFU5; -.
DR   KEGG; son:SO_1870; -.
DR   PATRIC; fig|211586.12.peg.1798; -.
DR   eggNOG; COG1166; Bacteria.
DR   HOGENOM; CLU_027243_1_0_6; -.
DR   OMA; AVEYTQH; -.
DR   OrthoDB; 164471at2; -.
DR   PhylomeDB; Q8EFU5; -.
DR   BioCyc; SONE211586:G1GMP-1726-MON; -.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0008792; F:arginine decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR   GO; GO:0033388; P:putrescine biosynthetic process from arginine; IBA:GO_Central.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06830; PLPDE_III_ADC; 1.
DR   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 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   PANTHER; PTHR43295; PTHR43295; 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; SSF51419; 1.
DR   TIGRFAMs; TIGR01273; speA; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Magnesium; Metal-binding; Polyamine biosynthesis;
KW   Pyridoxal phosphate; Reference proteome; Spermidine biosynthesis.
FT   CHAIN           1..637
FT                   /note="Biosynthetic arginine decarboxylase"
FT                   /id="PRO_0000149977"
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;  71004 MW;  8EAE2CF59061F7B8 CRC64;
     MNDWSIEAAR AGYNVTHWSQ GFYGISDEGE VTVSPDPKNP DHKIGLNELA KDMVKAGVAL
     PVLVRFPQIL HHRVNSLCQA FDQAIQKYEY QADYLLVYPI KVNQQKTVVE EILASQASKE
     VPQLGLEAGS KPELMAVLAM AQKASSVIVC NGYKDNEYIR LALIGEKLGH KVYIVLEKLS
     ELKMVLAESK RLGVKPRLGL RARLAFQGKG KWQASGGEKS KFGLSAAQIL TVVDQLKQSD
     MLDSLQLLHF HLGSQIANIR DIRQGVSEAA RFYCELRELG ASINCFDVGG GLAVDYDGTR
     SQSNNSMNYG LSEYANNIVN VLTDICNEYE QPMPRIISES GRHLTAHHAV LITDVIGTEA
     YQVEDIQPPE EESPQLLHNM WQSWTELSGR ADQRALIEIY HDSQSDLQEA QSLFALGQLS
     LAERAWAEQA NLRVCHEVQG LLSTKNRYHR PIIDELNEKL ADKFFVNFSL FQSLPDAWGI
     DQVFPVLPLS GLDKAPERRA VMLDITCDSD GIVDQYVDGQ GIETTLPVPA WSAESPYLIG
     FFMVGAYQEI LGDMHNLFGD TNSAVVSIEE NGMTNIESVL AGDTVADVLR YVNLDAVDFM
     RTYEELVNQH IAEDERAQIL EELQVGLKGY TYLEDFS