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Database: UniProt
Entry: A0A1H8T1N4_9BACL
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ID   A0A1H8T1N4_9BACL        Unreviewed;       289 AA.
AC   A0A1H8T1N4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:SEO84508.1};
GN   ORFNames=SAMN05518847_111167 {ECO:0000313|EMBL:SEO84508.1};
OS   Paenibacillus sp. OV219.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1884377 {ECO:0000313|EMBL:SEO84508.1, ECO:0000313|Proteomes:UP000199330};
RN   [1] {ECO:0000313|EMBL:SEO84508.1, ECO:0000313|Proteomes:UP000199330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV219 {ECO:0000313|EMBL:SEO84508.1,
RC   ECO:0000313|Proteomes:UP000199330};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOCJ01000011; SEO84508.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8T1N4; -.
DR   STRING; 1884377.SAMN05518847_111167; -.
DR   OrthoDB; 9788689at2; -.
DR   Proteomes; UP000199330; Unassembled WGS sequence.
DR   GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
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}.
SQ   SEQUENCE   289 AA;  31856 MW;  66FD5AD446CA92CE CRC64;
     MKLDQKYSGN VFILSSEDYN TSKAVIYGMP MDFTVSFRPG SRFGPPRIRE VSIGLEEYSP
     YLDRSLEDIE YFDAGDLLLP FGNAARSLDI ISEFVAGVLE DGKMPVGLGG EHLCSWPIFQ
     EVYKKYPDMA IIHFDAHADL RENYEGEPLS HSTPLRKAAG LIGGKNIYQF GIRSGSREEW
     QFARENINFH PFEVLEPLKK VLPELAGRPV YLTIDIDVLD PSAAPGTGTA EAGGITSKEL
     IDAVHAIAKA GINIVGCDLV EVAPAYDPTE QTQIVAAKVI REMLLGFIK
//
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