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Database: UniProt
Entry: A0A3Q8VEN0_9ACTN
LinkDB: A0A3Q8VEN0_9ACTN
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ID   A0A3Q8VEN0_9ACTN        Unreviewed;       322 AA.
AC   A0A3Q8VEN0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:AZM62158.1};
GN   Name=speB {ECO:0000313|EMBL:AZM62158.1};
GN   ORFNames=DLM49_23820 {ECO:0000313|EMBL:AZM62158.1};
OS   Streptomyces sp. WAC 01438.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2203204 {ECO:0000313|EMBL:AZM62158.1, ECO:0000313|Proteomes:UP000271045};
RN   [1] {ECO:0000313|EMBL:AZM62158.1, ECO:0000313|Proteomes:UP000271045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAC 01438 {ECO:0000313|EMBL:AZM62158.1,
RC   ECO:0000313|Proteomes:UP000271045};
RA   Waglechner N., Wright G.D.;
RT   "Evolution of GPA BGCs.";
RL   Submitted (MAY-2018) 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; CP029601; AZM62158.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3Q8VEN0; -.
DR   OrthoDB; 9788689at2; -.
DR   Proteomes; UP000271045; 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:UP000271045}.
SQ   SEQUENCE   322 AA;  34371 MW;  15DF5FC0CC379272 CRC64;
     MSSNETPRGP VDSSRVPRYA GPATFARLPR LDEVGRADVA VVGVPFDSGV SYRPGARFGG
     NAIREASRLL RPYNPAQDAS PFALAQVADG GDIAVNPFHI NEAVETVEAA ADDLLGTGAR
     LMTLGGDHTI ALPLLRSVAK RHGPVALLHF DAHLDTWDTY FGAEYTHGTP FRRAVEEGIL
     DTSALSHVGT RGPLYGKQDL TDDEKMGFGI VTSADVYRRG ADEVADQLRQ RIGDRPLYIS
     IDIDCLDPAH APGTGTPEAG GMTSRELLEI LRGLASCNLV SADVVEVAPA YDHAEITSVA
     ASHTAYELTT IMSRQIAEVR GK
//
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