ID   Q5SHU0_THET8            Unreviewed;       628 AA.
AC   Q5SHU0;
DT   21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   21-DEC-2004, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=Biosynthetic arginine decarboxylase {ECO:0000256|HAMAP-Rule:MF_01417};
DE            Short=ADC {ECO:0000256|HAMAP-Rule:MF_01417};
DE            EC=4.1.1.19 {ECO:0000256|HAMAP-Rule:MF_01417};
GN   Name=speA {ECO:0000256|HAMAP-Rule:MF_01417};
GN   OrderedLocusNames=TTHA1640 {ECO:0000313|EMBL:BAD71463.1};
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852 {ECO:0000313|EMBL:BAD71463.1, ECO:0000313|Proteomes:UP000000532};
RN   [1] {ECO:0000313|EMBL:BAD71463.1, ECO:0000313|Proteomes:UP000000532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8 {ECO:0000313|Proteomes:UP000000532};
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the biosynthesis of agmatine from arginine.
CC       {ECO:0000256|ARBA:ARBA00002257, ECO:0000256|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:0000256|HAMAP-
CC         Rule:MF_01417};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|HAMAP-
CC         Rule:MF_01417};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933, ECO:0000256|HAMAP-
CC         Rule:MF_01417, ECO:0000256|PIRSR:PIRSR001336-50};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; agmatine biosynthesis;
CC       agmatine from L-arginine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01417}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       SpeA subfamily. {ECO:0000256|ARBA:ARBA00008357, ECO:0000256|HAMAP-
CC       Rule:MF_01417}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01417}.
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DR   EMBL; AP008226; BAD71463.1; -; Genomic_DNA.
DR   RefSeq; YP_144906.1; NC_006461.1.
DR   AlphaFoldDB; Q5SHU0; -.
DR   SMR; Q5SHU0; -.
DR   EnsemblBacteria; BAD71463; BAD71463; BAD71463.
DR   KEGG; ttj:TTHA1640; -.
DR   PATRIC; fig|300852.9.peg.1610; -.
DR   eggNOG; COG1166; Bacteria.
DR   HOGENOM; CLU_027243_1_0_0; -.
DR   PhylomeDB; Q5SHU0; -.
DR   UniPathway; UPA00186; UER00284.
DR   Proteomes; UP000000532; 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; 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.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW   Rule:MF_01417};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01417};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01417};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01417};
KW   Polyamine biosynthesis {ECO:0000256|ARBA:ARBA00023115, ECO:0000256|HAMAP-
KW   Rule:MF_01417};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01417,
KW   ECO:0000256|PIRSR:PIRSR001336-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000532};
KW   Spermidine biosynthesis {ECO:0000256|ARBA:ARBA00023066, ECO:0000256|HAMAP-
KW   Rule:MF_01417}.
FT   DOMAIN          81..343
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   DOMAIN          369..450
FT                   /note="Arginine decarboxylase helical bundle"
FT                   /evidence="ECO:0000259|Pfam:PF17810"
FT   DOMAIN          578..626
FT                   /note="Arginine decarboxylase C-terminal helical"
FT                   /evidence="ECO:0000259|Pfam:PF17944"
FT   ACT_SITE        500
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   MOD_RES         101
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01417,
FT                   ECO:0000256|PIRSR:PIRSR001336-50"
SQ   SEQUENCE   628 AA;  70241 MW;  565F8577FDF8D999 CRC64;
     MAKRFTLKDA EELYLVPHWS GGFFRVGEKG DLEVTPLGPK GPAASLLEIV EALRDEGRPL
     PLVLRFPQIL EARVRDLNEA FLEAMAKYGY QGTYRGVYPV KVNQRRLVLE TVARAGRPYH
     LGLEAGSKPE LALILAQDLS EEALITTNGF KDDDFVRLAL MGRKLGRNVV ITLEKFAELF
     RVLRLSKELG VKPLLGIRYK LKAKGAGQWE ASGGENAKFG LTTPEIVRAV EVLQEEGLLD
     ALVMLHAHIG SQVTDIRRIK AAVREAAQTY VQLRKLGAPL RYLNLGGGLA VDYDGSKTNF
     YASANYTLSE YAENLVYVTK EVVEAQGEPH PILVTESGRA ITAYHEVLVL QVIDVIAPPG
     EARPSPPPPE AHPLVKELWE SLQSLSPKNF QEVYHDAFAD KETLQTLYDL GLVSLRDRAL
     AEEIFYHIAR RVQTIAQNLP YVPDELEDLE KLLADKLVCN FSVFQSLPDA WAIHQLFPVV
     PLSRLLEPPT RRATLVDISC DSDGKMDRFI DLHDVRQTLP VHPVRPGEPY YLGVFLVGAY
     QDVLGSNHNL FGQVGEAHVR VEEEGFAIER FVGGETAERV IEKMGFTARE LMLGVERLVR
     QSRLSPVEKG AFLERYAREL QGYTYLED
//