ID   A0A438MD68_9ACTN        Unreviewed;       338 AA.
AC   A0A438MD68;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:RVX43664.1};
GN   ORFNames=EDD27_6358 {ECO:0000313|EMBL:RVX43664.1};
OS   Nonomuraea polychroma.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=46176 {ECO:0000313|EMBL:RVX43664.1, ECO:0000313|Proteomes:UP000284824};
RN   [1] {ECO:0000313|EMBL:RVX43664.1, ECO:0000313|Proteomes:UP000284824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43925 {ECO:0000313|EMBL:RVX43664.1,
RC   ECO:0000313|Proteomes:UP000284824};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC       {ECO:0000256|ARBA:ARBA00009227}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RVX43664.1}.
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DR   EMBL; SAUN01000001; RVX43664.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A438MD68; -.
DR   OrthoDB; 9788689at2; -.
DR   Proteomes; UP000284824; 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; cd09990; Agmatinase-like; 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:UP000284824}.
FT   REGION          319..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   338 AA;  36593 MW;  431658DE0D98A38C CRC64;
     MSRYGVMYGP DFTFLGVDRC DVGEPASYEG ADVVIIGAPF DGGTSNRPGA RFGPQALRQA
     CYLPFDGSRP SLALRVDALK DLRVLDAGDV ECYSGDVEGS LAAIEEAVHR VAASGAIPMV
     LGGDHTIALP DARGTARAHA PGRTSMIHFD AHADTGDHTF GHHLYGHGQP MRRLIESGAI
     RGDRFLQIGL RGYWPEPATL AWMARRNMRS YEMTEVVTRG LDEVLTEAFA IALDDCDQVF
     LSVDIDVCDP GHAPGTGTPE PGGLTARQLL DAVRRICYEL PVAGMELVEV APPYDHADIT
     AYLGNRVILE ALSAMARRRK DDEGGPRWDP RQPLLDGR
//