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Database: UniProt
Entry: A0A3S8RRJ3_9BACL
LinkDB: A0A3S8RRJ3_9BACL
Original site: A0A3S8RRJ3_9BACL 
ID   A0A3S8RRJ3_9BACL        Unreviewed;       289 AA.
AC   A0A3S8RRJ3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:AZK45479.1};
DE            EC=3.5.3.11 {ECO:0000313|EMBL:AZK45479.1};
GN   Name=speB {ECO:0000313|EMBL:AZK45479.1};
GN   ORFNames=EIM92_04095 {ECO:0000313|EMBL:AZK45479.1};
OS   Paenibacillus lentus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1338368 {ECO:0000313|EMBL:AZK45479.1, ECO:0000313|Proteomes:UP000273145};
RN   [1] {ECO:0000313|EMBL:AZK45479.1, ECO:0000313|Proteomes:UP000273145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25539 {ECO:0000313|EMBL:AZK45479.1,
RC   ECO:0000313|Proteomes:UP000273145};
RA   Kook J.-K., Park S.-N., Lim Y.K.;
RT   "Genome sequencing of Paenibacillus lentus DSM25539(T).";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC       {ECO:0000256|ARBA:ARBA00009227}.
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DR   EMBL; CP034248; AZK45479.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S8RRJ3; -.
DR   KEGG; plen:EIM92_04095; -.
DR   OrthoDB; 9788689at2; -.
DR   Proteomes; UP000273145; Chromosome.
DR   GO; GO:0008783; F:agmatinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR   CDD; cd11593; Agmatinase-like_2; 1.
DR   Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR   InterPro; IPR005925; Agmatinase-rel.
DR   InterPro; IPR006035; Ureohydrolase.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR   NCBIfam; TIGR01230; agmatinase; 1.
DR   PANTHER; PTHR11358:SF43; AGMATINASE; 1.
DR   PANTHER; PTHR11358; ARGINASE/AGMATINASE; 1.
DR   Pfam; PF00491; Arginase; 1.
DR   PIRSF; PIRSF036979; Arginase; 1.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR   PROSITE; PS01053; ARGINASE_1; 1.
DR   PROSITE; PS51409; ARGINASE_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003684};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000273145}.
SQ   SEQUENCE   289 AA;  31757 MW;  A13315D1E4369B42 CRC64;
     MKLDQAYSGN VFICSSDSYE DAKAVIYGMP MDYTVSYRPG SRFGPARIRQ ASVGLEEYSP
     YLDKNILDAV YFDAGDLLLP FGNAARSLDV IGDYVRGLLA DDKFPIGLGG EHLVSWPVIQ
     AMYEKYPDLA VIHIDAHADL RDQYEGEPLS HSTPIRKAAE LMGGKNIYQF GIRSGSKEEF
     LYGRQNINFH PFEVAAPLKM ELPKMGSRPV YVTIDIDVLD PSCAPGTGTA EAGGITSKEL
     LEAIHLIARS DVNVVGCDLV EVAPIYDPTE QTQIVAAKLI REMLLGFVK
//
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