SPEA_THEVB
ID SPEA_THEVB Reviewed; 637 AA.
AC Q8DHY6;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=tll1807;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(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; BA000039; BAC09359.1; -; Genomic_DNA.
DR RefSeq; NP_682597.1; NC_004113.1.
DR RefSeq; WP_011057644.1; NC_004113.1.
DR AlphaFoldDB; Q8DHY6; -.
DR SMR; Q8DHY6; -.
DR STRING; 197221.22295533; -.
DR EnsemblBacteria; BAC09359; BAC09359; BAC09359.
DR KEGG; tel:tll1807; -.
DR PATRIC; fig|197221.4.peg.1889; -.
DR eggNOG; COG1166; Bacteria.
DR OMA; AVEYTQH; -.
DR OrthoDB; 164471at2; -.
DR Proteomes; UP000000440; 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; Reference proteome; Spermidine biosynthesis.
FT CHAIN 1..637
FT /note="Biosynthetic arginine decarboxylase"
FT /id="PRO_0000149979"
FT BINDING 289..299
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
FT MOD_RES 107
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
SQ SEQUENCE 637 AA; 70856 MW; A924C72CB50F29C5 CRC64;
MALTVTKTSN WTIEDSEQLY RIQGWGEPYF GINAAGHVTV SPKGDRGGSL DLYELVQALQ
QRNISLPLLL RFSDILEDRI ERLNACFARA IARYGYQGAY KGVFPIKCNQ QRHIIEALVR
FGQSHQFGLE AGSKPELLIA LAMLNTPGAL LICNGYKDRS YIETAILARR LGHTSIIVLE
QPEEVAEVIA VSQALGIEPI VGVRAKLSTQ GVGRWGTSAG DRAKFGLTVP EILTAVEQLR
AAGMLNALQL LHFHIGSQIS AISVIKDAIR EAGQIYGELV RLGANMQYLD VGGGLGVDYD
GSKTNFHASK NYSMQNYASD VVAGIKDACR QRGIPDPTLI SESGRAIASH QSVLIFNVLG
VSEVPKITPE PATAEEHLII RNLYDTYQAI DENNYQEAYN DALQFKGEAI SLFNFGYLSL
PERARAESLF WACCAKILGI ARQQEYVPDD LEDLEKIMAS IYYINLSVFQ SVPDSWAIDQ
LFPIMPIHRL DEEPTERGIL ADLTCDSDGK IDQFIDLRDV KSVLELHPFR PGEPYYLGLF
LNGAYQEIMG NLHNLFGDTN AVHIRLTPKG YEIEHLVRGD TMQEVLGYVQ YQGDALLEKI
RCRTEAALAE EQITLAEAQH LLENYERSLR SYTYLSS
