SPEA_GEOSL
ID SPEA_GEOSL Reviewed; 635 AA.
AC A0A4W3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=GSU2537;
OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=243231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX PubMed=14671304; DOI=10.1126/science.1088727;
RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA Lovley D.R., Fraser C.M.;
RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT environments.";
RL Science 302:1967-1969(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;
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; AE017180; AAR35910.1; -; Genomic_DNA.
DR RefSeq; NP_953583.1; NC_002939.5.
DR RefSeq; WP_010943173.1; NC_002939.5.
DR AlphaFoldDB; A0A4W3; -.
DR SMR; A0A4W3; -.
DR STRING; 243231.GSU2537; -.
DR EnsemblBacteria; AAR35910; AAR35910; GSU2537.
DR KEGG; gsu:GSU2537; -.
DR PATRIC; fig|243231.5.peg.2566; -.
DR eggNOG; COG1166; Bacteria.
DR HOGENOM; CLU_027243_1_0_7; -.
DR InParanoid; A0A4W3; -.
DR OMA; AVEYTQH; -.
DR UniPathway; UPA00186; UER00284.
DR Proteomes; UP000000577; Chromosome.
DR GO; GO:0008792; F:arginine decarboxylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006527; P:arginine catabolic process; IEA:InterPro.
DR GO; GO:0033388; P:putrescine biosynthetic process from arginine; IBA:GO_Central.
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_1000068491"
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; 71637 MW; 5688D3984B1DAF99 CRC64;
MERWSINESA KIYNLPNWGA DLFSINKKGN VCVHPSPTSK HSIDLRALVD DLIKRKIKPP
ILLRFMDVLQ GRIASINRVF KNAIDENDYP ATYQTFYPIK VNQQRQVVEA IAKFGKRYNI
GLEVGSKPEL VIGISFATGN GIPIICNGYK DTEYIETVLY ATKIGYDITI VVEKMFELEK
IIALSKKTGI KPKLGIRVKL SSKGTGKWAT SGGEDAKFGL RMSEIIAAIG LLEQNDLLDR
VKLLHFHIGS QITKIDKIKS ALIEGTRIYA EMRKLGVGIR YVDIGGGLGV DYDGSKSSYF
SSVNYSIEEY ANDVIYQIKN ICEDAGVECP NIISESGRAT AAHYSVLVTN LLNTNTSNAM
PDFEETLNGT EKLAPTVKKL VDIYKSIDRY SLREDYHDTV QLIQEAVSLF NLGYLTLNER
AMAEWLHGKI LRKINGIVEK IKPIPEELQN FQLSLRQTYF ANFSLFQSIP DSWAIDQLFP
IVPIQRLNQK PDVMASIADI TCDSDGEITS FVGENGRTKY LPLHKMRKDE DYFVGFFLIG
AYQEILGDMH NLFGDTNAVH VTFNKKTGYK IDTVIHGDAT WESLKYVQYK GPEILKHVRD
TLEKDVALRK VTIEESSHFL ELLDRTLLGY TYLGE