ID   SPEA_CITBB              Reviewed;         635 AA.
AC   B5EIW4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Biosynthetic arginine decarboxylase;
DE            Short=ADC;
DE            EC=4.1.1.19;
GN   Name=speA; OrderedLocusNames=Gbem_2916;
OS   Citrifermentans bemidjiense (strain ATCC BAA-1014 / DSM 16622 / JCM 12645 /
OS   Bem) (Geobacter bemidjiensis).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Citrifermentans.
OX   NCBI_TaxID=404380;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1014 / DSM 16622 / JCM 12645 / Bem;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Lovley D., Richardson P.;
RT   "Complete sequence of Geobacter bemidjiensis BEM.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC       agmatine from L-arginine: step 1/1.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       SpeA subfamily. {ECO:0000305}.
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; CP001124; ACH39919.1; -; Genomic_DNA.
DR   RefSeq; WP_012531344.1; NC_011146.1.
DR   AlphaFoldDB; B5EIW4; -.
DR   SMR; B5EIW4; -.
DR   STRING; 404380.Gbem_2916; -.
DR   EnsemblBacteria; ACH39919; ACH39919; Gbem_2916.
DR   KEGG; gbm:Gbem_2916; -.
DR   eggNOG; COG1166; Bacteria.
DR   HOGENOM; CLU_027243_1_0_7; -.
DR   OMA; AVEYTQH; -.
DR   OrthoDB; 164471at2; -.
DR   UniPathway; UPA00186; UER00284.
DR   Proteomes; UP000008825; 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; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 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   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; SSF50621; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR01273; speA; 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..635
FT                   /note="Biosynthetic arginine decarboxylase"
FT                   /id="PRO_1000145594"
FT   BINDING         282..292
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         100
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   635 AA;  71687 MW;  0AF4EC3505D54F1D CRC64;
     MAKWTINDSS KIYNIDNWGA ELFSINKKGN VCVHPSPNSK YSIDLKVLVD DLIKRKIKPP
     ILLRFMNILE GRIASISRVF KNAISDNNYP AKYQTFYPIK VNQQRQVVEA IANFGKKYNI
     GLEVGSKPEL VAAISMSTGN NLPILCNGYK DTEFIETVLF ATRVGYDITI VVEKLFELEK
     IVEVSKRTGI VPKLGIRVKL SSKGIGKWST SGGDDAKFGL RISELIAAID MLKQNDMLDS
     VKLLHFHVGS QITKIDKIKN ALIEGTRIYA EMRKLGVNLE FLDIGGGLGV DYDGSKSSYF
     SSVNYSLEEY ANDVIYQVKN ICDDAGVPCP NIISESGRAT VAHYSVLVTD VLNNNTQTLM
     PDFESILTEP EKLSPTVKKL VDIYKSIDKH SLREDYHDTI QLIQESVSLF NLGYLNMAER
     ANAEWICSKI IRKINSIVEK MKPIPDELQN FQLSLRQTYF ANFSLFQSIP DSWAIDQLFP
     IVPIQRLDEK PDVLTSIADI TCDSDGEITS FVGENGRTKA LPLHKIKVDE QYYIGFFLIG
     AYQEILGDMH NLFGDTNAVH ITFNKKTNYK IDTVISGDAT WESLKYVQYD SQEILKRVRN
     NLEKDVSLQK VSIEESSHFL ELLDKTLQSY TYLGE