ID   SPEA_BACFR              Reviewed;         630 AA.
AC   Q64ZT8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=BF0239;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT   regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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   -!- 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; AP006841; BAD46988.1; -; Genomic_DNA.
DR   RefSeq; WP_005783873.1; NZ_UYXF01000014.1.
DR   RefSeq; YP_097522.1; NC_006347.1.
DR   AlphaFoldDB; Q64ZT8; -.
DR   SMR; Q64ZT8; -.
DR   STRING; 295405.BF0239; -.
DR   EnsemblBacteria; BAD46988; BAD46988; BF0239.
DR   GeneID; 66330682; -.
DR   KEGG; bfr:BF0239; -.
DR   PATRIC; fig|295405.11.peg.269; -.
DR   HOGENOM; CLU_027243_1_0_10; -.
DR   OMA; AVEYTQH; -.
DR   UniPathway; UPA00186; UER00284.
DR   Proteomes; UP000002197; 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   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   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; Spermidine biosynthesis.
FT   CHAIN           1..630
FT                   /note="Biosynthetic arginine decarboxylase"
FT                   /id="PRO_1000024255"
FT   BINDING         281..291
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
FT   MOD_RES         99
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
SQ   SEQUENCE   630 AA;  71190 MW;  9A266E486AED6C19 CRC64;
     MRKWRIEDSE ELYNITGWGT SYFGINDKGH VVVTPRKDGV AVDLKELVDE LQLRDVAAPM
     LVRFPDILDN RIEKTAYCFK QASEEYGYKA QNFIIYPIKV NQMRPVVEEI ISHGKKFNLG
     LEAGSKPELH AVIAVNTDSD SLIICNGYKD ESYIELALLA QKMGKRIFLV VEKMNELKLI
     ARMAKQLNVQ PNIGIRIKLA SSGSGKWEES GGDASKFGLT SSELLEALDF LESKGMKDCL
     KLIHFHIGSQ VTKIRRIKTA LREASQFYVQ LHAMGFNVEF VDIGGGLGVD YDGTRSSSSE
     SSVNYSIQEY VNDSISTLVD ASDKNGIPHP NIITESGRAL TAHHSVLIFE VLETATLPQW
     DDEEEIAPDA HELVQELYGI WDTLNQNKML EAWHDAQQIR EEALDLFSHG IVDLKTRAQI
     ERLYWSITRE INQIAGGLKH APDEFRGLSK LLADKYFCNF SLFQSLPDSW AIDQIFPIMP
     IQRLDEKPDR SATLQDITCD SDGKIANFIS TRNVAHYMPV HSLKQKEPYY VAVFLVGAYQ
     EILGDMHNLF GDTNAVHVSV NEKGYNIEQI IDGETVAEVL DYVQYSPKKL VRTLETWVTK
     SVKEGKISVE EGKEFLSNYR SGLYGYTYLE