SPEA_GEOMG
ID SPEA_GEOMG Reviewed; 635 AA.
AC Q39X78;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=Gmet_0904;
OS Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=269799;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Geobacter metallireducens GS-15.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000148; ABB31146.1; -; Genomic_DNA.
DR RefSeq; WP_004513934.1; NC_007517.1.
DR AlphaFoldDB; Q39X78; -.
DR SMR; Q39X78; -.
DR STRING; 269799.Gmet_0904; -.
DR EnsemblBacteria; ABB31146; ABB31146; Gmet_0904.
DR KEGG; gme:Gmet_0904; -.
DR eggNOG; COG1166; Bacteria.
DR HOGENOM; CLU_027243_1_0_7; -.
DR OMA; AVEYTQH; -.
DR OrthoDB; 164471at2; -.
DR UniPathway; UPA00186; UER00284.
DR Proteomes; UP000007073; 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..635
FT /note="Biosynthetic arginine decarboxylase"
FT /id="PRO_1000068490"
FT BINDING 282..292
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
FT MOD_RES 100
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
SQ SEQUENCE 635 AA; 71521 MW; 689186DAE924266B CRC64;
MERWSINDSA KIYNLPNWGA DLFSINKKGN VCVHPSPTSK HSIDLRALVD DLIKRKIKPP
ILLRFMDVLQ GRIAAINRAF KYAIDENDYP STYQTFYPIK VNQQRQVVEA IAKFGKRYNI
GIEVGSKPEL VIGISFATGN GIPIICNGYK DKEYIETVLY ATKIGYDITI VVEKMFELEK
IIALSKKTGI KPKLGIRVKL SSKGTGKWAT SGGEDAKFGL RMSEIIAAIG LLEQNELLDS
VKLIHFHIGS QITKIDKIKS ALIEGTRVYA EMRKLGVGIE YVDIGGGLGV DYDGSKSSYF
SSVNYSIEEY ANDVIYQIKN ICEDAGVECP NIISESGRAT AAHYSVLVTN LLNTNTQNLM
PDFEETLNGA EKLAPTVKKL VDIYKSIDRY SLREDYHDTV QLIQEAVSLF SLGYLTLAER
AMAEWLHGKI LRKINGIVEK IKPIPEELQN FQLSLRQTYF ANFSLFQSIP DSWAIDQLFP
IVPIQRLNQK PDVMASIADI TCDSDGEITS FVGENGRTKY LPLHKIRKDE DYFVGFFLIG
AYQEILGDMH NLFGDTNAVH VTFNKKTGYK IDTVINGDAT WESLKYVQYK GPEILKHVRD
TMEKDVALRK VSIEESSHFL ELLDRTLLGY TYLGE