ID A0A086N2N7_9ACTN Unreviewed; 323 AA.
AC A0A086N2N7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:KFG75405.1};
GN ORFNames=FM21_04475 {ECO:0000313|EMBL:KFG75405.1};
OS Streptomyces mutabilis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67332 {ECO:0000313|EMBL:KFG75405.1, ECO:0000313|Proteomes:UP000029095};
RN [1] {ECO:0000313|EMBL:KFG75405.1, ECO:0000313|Proteomes:UP000029095}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TRM45540 {ECO:0000313|EMBL:KFG75405.1,
RC ECO:0000313|Proteomes:UP000029095};
RA Luo X., Zhang L.;
RT "Complete genome sequence of the Streptomyces mutabilis TRM45540.";
RL Submitted (MAY-2014) 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:KFG75405.1}.
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DR EMBL; JNFQ01000001; KFG75405.1; -; Genomic_DNA.
DR RefSeq; WP_043372723.1; NZ_KN039946.1.
DR AlphaFoldDB; A0A086N2N7; -.
DR STRING; 1915400.FM21_04475; -.
DR HOGENOM; CLU_039478_0_0_11; -.
DR Proteomes; UP000029095; 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}.
SQ SEQUENCE 323 AA; 34388 MW; C8F8C07BED249054 CRC64;
MSSNETPRGP VDSSRIPRYA GPATFARLPR LDEVGTADVA VVGVPFDSGV SYRPGARFGG
NAIREASRLL RPYNPAQDAS PFALAQVADG GDIAVNPFHI NEAVETVEAA ADDLLGTGAR
LMTLGGDHTI ALPLLRSVAK KHGPVALLHF DAHLDTWDTY FGAEYTHGTP FRRAVEEGIL
DTSALSHVGT RGPLYGKQDL TDDEKMGFGI VTSADVYRRG ADEVADQLRQ RIGDRPLYIS
IDIDCLDPAH APGTGTPEAG GMTSRELLEI LRGLASCNLV SADVVEVAPA YDHAEITSVA
ASHTAYELTT IMSRQIAQEK AAQ
//
