ID   SPEA_BACTN              Reviewed;         630 AA.
AC   Q8A2B1;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 115.
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=BT_3394;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(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; AE015928; AAO78500.1; -; Genomic_DNA.
DR   RefSeq; NP_812306.1; NC_004663.1.
DR   RefSeq; WP_008767598.1; NZ_UYXG01000003.1.
DR   AlphaFoldDB; Q8A2B1; -.
DR   SMR; Q8A2B1; -.
DR   STRING; 226186.BT_3394; -.
DR   PaxDb; 226186-BT_3394; -.
DR   DNASU; 1075986; -.
DR   EnsemblBacteria; AAO78500; AAO78500; BT_3394.
DR   GeneID; 60924573; -.
DR   KEGG; bth:BT_3394; -.
DR   PATRIC; fig|226186.12.peg.3462; -.
DR   eggNOG; COG1166; Bacteria.
DR   HOGENOM; CLU_027243_1_0_10; -.
DR   InParanoid; Q8A2B1; -.
DR   OrthoDB; 9802658at2; -.
DR   Proteomes; UP000001414; 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; 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   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.
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..630
FT                   /note="Biosynthetic arginine decarboxylase"
FT                   /id="PRO_0000149957"
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;  71246 MW;  C124255A68131F19 CRC64;
     MRKWRIEDSE ELYNITGWGT SYFSINDAGH VVVTPRRDGV TVDLKELVDE LQLRDVASPM
     LLRFPDILDN RIEKMSSCFK QAAEEYGYKA ENFIIYPIKV NQMRPVVEEI ISHGKKFNLG
     LEAGSKPELH AVIAVNTDSD SLIVCNGYKD ESYIELALLA QKMGKRIFLV VEKMNELKLI
     AKMAKQLNVQ PNIGIRIKLA SSGSGKWEES GGDASKFGLT SSELLEALDF MESKGLKDCL
     KLIHFHIGSQ VTKIRRIKTA LREASQFYVQ LHSMGFNVEF VDIGGGLGVD YDGTRSSNSE
     GSVNYSIQEY VNDSISTLVD VSDKNGIPHP NIITESGRAL TAHHSVLIFE VLETATLPEW
     DDEEEIAPDA HELVQELYSI WDSLNQNKML EAWHDAQQIR EEALDLFSHG IVDLKTRAQI
     ERLYWSITRE INQIAGGLKH APDEFRGLSK LLADKYFCNF SLFQSLPDSW AIDQIFPIMP
     IQRLDEKPER SATLQDITCD SDGKIANFIS TRNVAHYLPV HSLKKTEPYY LAVFLVGAYQ
     EILGDMHNLF GDTNAVHVSV NEKGYNIEQI IDGETVAEVL DYVQYNPKKL VRTLETWVTK
     SVKEGKISLE EGKEFLSNYR SGLYGYTYLE
//