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Database: UniProt
Entry: A0A1G7PWA4_9ACTN
LinkDB: A0A1G7PWA4_9ACTN
Original site: A0A1G7PWA4_9ACTN 
ID   A0A1G7PWA4_9ACTN        Unreviewed;       337 AA.
AC   A0A1G7PWA4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:SDF90612.1};
GN   ORFNames=SAMN05660324_1245 {ECO:0000313|EMBL:SDF90612.1};
OS   Klenkia brasiliensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Klenkia.
OX   NCBI_TaxID=333142 {ECO:0000313|EMBL:SDF90612.1, ECO:0000313|Proteomes:UP000198863};
RN   [1] {ECO:0000313|EMBL:SDF90612.1, ECO:0000313|Proteomes:UP000198863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44526 {ECO:0000313|EMBL:SDF90612.1,
RC   ECO:0000313|Proteomes:UP000198863};
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; FNCF01000002; SDF90612.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7PWA4; -.
DR   OrthoDB; 9788689at2; -.
DR   Proteomes; UP000198863; 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}.
SQ   SEQUENCE   337 AA;  35969 MW;  0AF6EB904E379E19 CRC64;
     MARYGTQFGP DITFLGVDRC DHTDPASMAG ADVVVLGAPF DGGTSHRPGT RFGPQAIRMT
     DYLPHDGSRP SLALRTDGLR DLRVLDAGDV EMYSGGIEQA LPALRSAVAD VVRAGAIPVV
     LGGDHSIAFP DAGGVADVLG HGRVSMIHFD AHADTGDIEF GSLWGHGQPM RRLIESGALR
     GDRFLQVGLR GYWPPPETLD WMAQQRMRSY EMAEIGHRGL QTCLTEAFAI ATDECDGVFL
     SVDIDVCDPG HAPGTGTPEP GGLTARELLD SVRRICLELP VVGIDVVEVS PPYDHADITA
     ALANRVVLEA LSAIARRRSA LPPFDPSLPL LADRNLP
//
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