SPEA_SHEPW
ID SPEA_SHEPW Reviewed; 637 AA.
AC B8CR70;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=swp_3024;
OS Shewanella piezotolerans (strain WP3 / JCM 13877).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=225849;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP3 / JCM 13877;
RX PubMed=18398463; DOI=10.1371/journal.pone.0001937;
RA Wang F., Wang J., Jian H., Zhang B., Li S., Wang F., Zeng X., Gao L.,
RA Bartlett D.H., Yu J., Hu S., Xiao X.;
RT "Environmental adaptation: genomic analysis of the piezotolerant and
RT psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans
RT WP3.";
RL PLoS ONE 3:E1937-E1937(2008).
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; CP000472; ACJ29742.1; -; Genomic_DNA.
DR RefSeq; WP_020913095.1; NC_011566.1.
DR AlphaFoldDB; B8CR70; -.
DR SMR; B8CR70; -.
DR STRING; 225849.swp_3024; -.
DR EnsemblBacteria; ACJ29742; ACJ29742; swp_3024.
DR KEGG; swp:swp_3024; -.
DR eggNOG; COG1166; Bacteria.
DR HOGENOM; CLU_027243_1_0_6; -.
DR OMA; AVEYTQH; -.
DR OrthoDB; 164471at2; -.
DR UniPathway; UPA00186; UER00284.
DR Proteomes; UP000000753; 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; IPR022644; De-COase2_N.
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; SSF51419; SSF51419; 1.
DR TIGRFAMs; TIGR01273; speA; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lyase; Magnesium; Metal-binding; Polyamine biosynthesis;
KW Pyridoxal phosphate; Spermidine biosynthesis.
FT CHAIN 1..637
FT /note="Biosynthetic arginine decarboxylase"
FT /id="PRO_1000145603"
FT BINDING 286..296
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 637 AA; 71415 MW; 049210A3D93B1F27 CRC64;
MNNWSIDDAR ASYNVNYWSQ GLYGISDEGE VTVSPDPNRP DCKIGLNELA KDMVKAGVAL
PVLVRFPQIL HHRVNSLCQA FNQAIQKYKY EADYLLVYPI KVNQQQTVVE EILASQVEKE
VPQLGLEAGS KPELLAVLAM AQKASSVIIC NGYKDKEYIR LALIGEKLGH KVYIVLEKMS
ELKVVLEQAK ELGVTPRLGL RVRLAFQGKG KWQASGGEKS KFGLSAAQVL KVIELLQHEE
MLDSLELLHF HLGSQIANIR DIRQGVSEAG RFYCELMKLG AQVKCFDVGG GLAVDYDGTR
SQSNNSMNYG LTEYANNIVS VLTDMCKEYE QPMPRIISES GRYLTAHHAV LLTDVIGTES
YKPETILPPS EDAPLLLQNM WQSWTEVSGK ADQRALIEIF HDCQSDLTEV HSLFALGQLS
LADRAWAEQI NLRVCHELQG SMSSKYRYHR PIIDELNEKL ADKFFVNFSL FQSLPDAWGI
DQVFPVMPLS GLDKAPERRA VMLDITCDSD GIVDQYVDGQ GIETTLPVPA WTQESPYLIG
FFLVGAYQEI LGDMHNLFGD TNSAVVRVDE NGRRNIDSVL EGDTVADVLR YVNLEAVSFM
RTYEELVNKH IVADERSNIL EELQLGLKGY TYLEDFS