SPEA_PHOLL
ID SPEA_PHOLL Reviewed; 634 AA.
AC Q7N121;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=plu3681;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(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; BX571871; CAE16054.1; -; Genomic_DNA.
DR RefSeq; WP_011147844.1; NC_005126.1.
DR AlphaFoldDB; Q7N121; -.
DR SMR; Q7N121; -.
DR STRING; 243265.plu3681; -.
DR EnsemblBacteria; CAE16054; CAE16054; plu3681.
DR GeneID; 24168646; -.
DR KEGG; plu:plu3681; -.
DR eggNOG; COG1166; Bacteria.
DR HOGENOM; CLU_027243_1_0_6; -.
DR OMA; AVEYTQH; -.
DR OrthoDB; 164471at2; -.
DR BioCyc; PLUM243265:PLU_RS18235-MON; -.
DR UniPathway; UPA00186; UER00284.
DR Proteomes; UP000002514; 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; Reference proteome;
KW Spermidine biosynthesis.
FT CHAIN 1..634
FT /note="Biosynthetic arginine decarboxylase"
FT /id="PRO_0000149967"
FT BINDING 283..293
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
FT MOD_RES 103
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01417"
SQ SEQUENCE 634 AA; 71155 MW; A3268D93070FDCB5 CRC64;
MNDNIARKMQ QTYNIAYWGG SYYYVNDLGN VSVCPNPDLP GAKIDLAELV KRVQQEQKHL
RLPALFCFPQ ILQHRLRSIN AAFKRARESY GYKGDYFLVY PIKVNQQRRV IESLASSGEP
LGLEAGSKAE LMAVLAHAGM TRTVIVCNGY KDREYIRLAL IGEKLGHKVY LVIEKMSEIA
QVLEEAERLN VIPRLGVRAR LASQGSGKWQ ASGGEKSKFG LAATQVLQLV ETLRAVDRLD
SLQLLHFHLG SQLANIRDIA TGVRESARFY VELHKLGVNI QCFDVGGGLG VDYEGTRSQS
DCSVNYGLNE YANNVIWGIG DACDEHGLPH PTVITESGRA LTAHHTVLVS NVIGVERNEF
TQTTPPAEDA SRPLTSLWET WQEMHSEGNR RSLRESLHDG QLDLHDVHTQ YAHGMLDLTE
RAWAEELYLN ICRRIQQDLD PSNRAHRPII DELQERMADK FYVNFSLFQS LPDAWGIDQL
FPVLPIEGLD KPLDRRAVLL DITCDSDGIV DHYVDGDGVA ATMPMPAYDP DCPPMIGFFM
VGAYQEILGN MHNLFGDTAA IDVYVFDNGE VTYNQSEEGD SVADMLQYVK LDPNVLMARF
RDQVKGADLD TGLQEQFLLE FESGLYGYTY LEDE
