ID A0A0F7N592_9ACTN Unreviewed; 323 AA.
AC A0A0F7N592;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:AKH82554.1};
GN ORFNames=AA958_10305 {ECO:0000313|EMBL:AKH82554.1};
OS Streptomyces sp. CNQ-509.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=444103 {ECO:0000313|EMBL:AKH82554.1, ECO:0000313|Proteomes:UP000034283};
RN [1] {ECO:0000313|EMBL:AKH82554.1, ECO:0000313|Proteomes:UP000034283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNQ-509 {ECO:0000313|EMBL:AKH82554.1,
RC ECO:0000313|Proteomes:UP000034283};
RA Ruckert C., Albersmeier A., Leipoldt F., Winkler A., Zeyhle P.,
RA Kalinowski J., Heide L., Kaysser L.;
RT "Complete Genome Sequence of Streptomyces sp. CNQ-509, a Prolific Producer
RT of Meroterpenoid Chemistry.";
RL Submitted (MAY-2015) 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; CP011492; AKH82554.1; -; Genomic_DNA.
DR RefSeq; WP_047015896.1; NZ_CP011492.1.
DR AlphaFoldDB; A0A0F7N592; -.
DR STRING; 444103.AA958_10305; -.
DR KEGG; strc:AA958_10305; -.
DR PATRIC; fig|444103.5.peg.2172; -.
DR OrthoDB; 9788689at2; -.
DR Proteomes; UP000034283; Chromosome.
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:UP000034283}.
SQ SEQUENCE 323 AA; 34171 MW; 4D927FBDA7662B5A CRC64;
MSSTGTPRGP VDSSRVPRYA GPATFARLPR LDEVGRTDVA VVGVPFDSGV SYRPGARFGG
NAIREASRLL RPYNPAQDAA PFALAQVADA GDIAVNPFDI GEAVATVEGA ADELLATGAR
LMTLGGDHTI ALPLLRAVAR RHGPVALLHF DAHLDTWDTY FGAAYTHGTP FRRAVEEGVV
DTAALSHVGI RGPLYGRKDL DDDEKMGFGI VTSADVMRRG VDEVTDQLRQ RIGDRPLYVS
IDIDVLDPAH APGTGTPEAG GLTSRELLEI LRGLAGCRLV SADLVEVAPA YDHAEITSVA
ASHTAYELTT LMARQIAGER DAG
//
