ID   A0A1A0FLY2_9GAMM        Unreviewed;       300 AA.
AC   A0A1A0FLY2;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:OBA00490.1};
GN   ORFNames=ADS46_10600 {ECO:0000313|EMBL:OBA00490.1};
OS   Halomonas sp. G11.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1684425 {ECO:0000313|EMBL:OBA00490.1, ECO:0000313|Proteomes:UP000092250};
RN   [1] {ECO:0000313|EMBL:OBA00490.1, ECO:0000313|Proteomes:UP000092250}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G11 {ECO:0000313|EMBL:OBA00490.1,
RC   ECO:0000313|Proteomes:UP000092250};
RA   Naifar M., Chouchane H., Najjari A., El Hidri D., Mahjoubi M., Ghedira K.,
RA   Soufi L., Salah A., Raddadi N., Sghaier H., Ouzari H.I.,
RA   Eddine Masmoudi A.S., Cherif A.;
RT   "Genomic basis for crude oil degradation, heavy metal resistance and high
RT   salt tolerance of Halomonas hydrocarbonoclasticus G11 isolated from
RT   Tunisian Chott El-Djerid salt lake.";
RL   Submitted (FEB-2016) 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:OBA00490.1}.
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DR   EMBL; LYXG01000004; OBA00490.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A0FLY2; -.
DR   SMR; A0A1A0FLY2; -.
DR   Proteomes; UP000092250; 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   300 AA;  32118 MW;  56319D4178EB4216 CRC64;
     MASFLRAPLA DSLEALDIAL VGIPFDGGVS NRPGTRHGPR EIRNQSSMMR SAHHITGLDP
     FAQARIADIG DVRFSSIYDL EKVSDDIATY YAAIRKAGVI PLSAGGDHSI TFPILRGLAA
     NGPVGLIQID AHTDTWDEFQ GSKFHHGGPF RLACEQGLID PERTVQIGIR GAQNTTQGWD
     YSRETGMRVM FMEEVDALGI DAVIAEARRV VGDGPVYLSF DIDSIDPAFA PGTGTPEVGG
     LTSLQALQLV RGFRGLPLIG ADVVEVSPPF DPSGNTALMG ATLMYELLCL MAEGVDHTRT
//