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Database: UniProt
Entry: A0A1H8YXU5_9ACTN
LinkDB: A0A1H8YXU5_9ACTN
Original site: A0A1H8YXU5_9ACTN 
ID   A0A1H8YXU5_9ACTN        Unreviewed;       326 AA.
AC   A0A1H8YXU5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:SEP56857.1};
GN   ORFNames=SAMN05216481_101150 {ECO:0000313|EMBL:SEP56857.1};
OS   Streptomyces radiopugnans.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=403935 {ECO:0000313|EMBL:SEP56857.1, ECO:0000313|Proteomes:UP000199055};
RN   [1] {ECO:0000313|EMBL:SEP56857.1, ECO:0000313|Proteomes:UP000199055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3519 {ECO:0000313|EMBL:SEP56857.1,
RC   ECO:0000313|Proteomes:UP000199055};
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; FOET01000001; SEP56857.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8YXU5; -.
DR   STRING; 403935.SAMN05216481_101150; -.
DR   Proteomes; UP000199055; 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; cd11592; Agmatinase_PAH; 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:SF26; AGMATINASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11358; ARGINASE/AGMATINASE; 1.
DR   Pfam; PF00491; Arginase; 1.
DR   PIRSF; PIRSF036979; Arginase; 1.
DR   PRINTS; PR00116; ARGINASE.
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:UP000199055}.
SQ   SEQUENCE   326 AA;  34906 MW;  C0AB6B0285BD540A CRC64;
     MSSDQQQPRG PVDSSRIPRF AGPATFARLP RLDEVGRADV AVVGVPFDSG VSYRPGARFG
     SNAVREASRL LRPYNPAQDA SPFALAQVAD AGDIAANPFD IHEAVETVER AAGELLDTGA
     RLMTLGGDHT IALPLLRAVA RKHGPVALLH FDAHLDTWDT YFGAEYTHGT PFRRAVEEGI
     LDTSALSHVG TRGPLYGKKD LTDDAKMGFG IVTSADVMRR GVDEVADQLR QRIGDRPLYV
     SIDIDCLDPA HAPGTGTPEA GGMTSRELLE ILRGLASCNL VSADVVEVAP AYDHAEITSV
     AASHTAYELT TLMARRIAAE RESAER
//
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