SPEA_SALCH
ID SPEA_SALCH Reviewed; 632 AA.
AC Q57K30;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=SCH_3026;
OS Salmonella choleraesuis (strain SC-B67).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67;
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA Lee Y.-S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(2005).
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; AE017220; AAX66932.1; -; Genomic_DNA.
DR AlphaFoldDB; Q57K30; -.
DR SMR; Q57K30; -.
DR EnsemblBacteria; AAX66932; AAX66932; SCH_3026.
DR KEGG; sec:SCH_3026; -.
DR HOGENOM; CLU_027243_1_0_6; -.
DR OMA; AVEYTQH; -.
DR UniPathway; UPA00186; UER00284.
DR Proteomes; UP000000538; 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:0009446; P:putrescine biosynthetic process; IEA:UniProtKB-UniRule.
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 Putrescine biosynthesis; Pyridoxal phosphate; Spermidine biosynthesis.
FT CHAIN 1..632
FT /note="Biosynthetic arginine decarboxylase"
FT /id="PRO_1000024263"
FT BINDING 281..291
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
FT MOD_RES 101
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
SQ SEQUENCE 632 AA; 71163 MW; 98BB424D2BC97370 CRC64;
MSSQEASKML RTYNIAWWGN NYYDVNELGH ISVCPDPDVP EARVDLAKLV KAREAQGQRL
PALFCFPQIL QHRLRSINAA FKRARESYGY NGDYFLVYPI KVNQHRRVIE SLIHSGEPLG
LEAGSKAELM AVLAHAGMTR SVIVCNGYKD REYIRLALIG EKMGHKVYLV IEKMSEIAIV
LEEAERLNVV PRLGVRARLA SQGSGKWQSS GGEKSKFGLA ATQVLQLVET LRDAGRLDSL
QLLHFHLGSQ MANIRDIATG VRESARFYVE LHKLGVNIQC FDVGGGLGVD YEGTRSQSDC
SVNYGLNEYA NNIIWAIGDA CEEHGLPHPT VITESGRAVT AHHTVLVSNI IGVERNEYTD
PTAPAEDAPR ALQNLWETWQ EMHKPGTRRS LREWLHDSQM DLHDIHIGYS SGAFSLQERA
WAEQLYLSMC HEVQKQLDPQ NRAHRPIIDE LQERMADKMY VNFSLFQSMP DAWGIDQLFP
VLPLEGLDQV PERRAVLLDI TCDSDGAIDH YIDGDGIATT MPMPEYDPEN PPMLGFFMVG
AYQEILGNMH NLFGDTEAVD VFVFPDGSVE VELSDEGDTV ADMLQYVQLD PKTLLTHFRD
QVKQTDLDDA LQQQFLEEFE AGLYGYTYLE DE