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Database: UniProt
Entry: A0A1M7AKR3_9FLAO
LinkDB: A0A1M7AKR3_9FLAO
Original site: A0A1M7AKR3_9FLAO 
ID   A0A1M7AKR3_9FLAO        Unreviewed;       313 AA.
AC   A0A1M7AKR3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:SHL43371.1};
GN   ORFNames=SAMN05216293_3458 {ECO:0000313|EMBL:SHL43371.1};
OS   Allomuricauda taeanensis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Allomuricauda.
OX   NCBI_TaxID=1005926 {ECO:0000313|EMBL:SHL43371.1, ECO:0000313|Proteomes:UP000184031};
RN   [1] {ECO:0000313|Proteomes:UP000184031}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12174 {ECO:0000313|Proteomes:UP000184031};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-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; FRAT01000010; SHL43371.1; -; Genomic_DNA.
DR   RefSeq; WP_072882152.1; NZ_FRAT01000010.1.
DR   AlphaFoldDB; A0A1M7AKR3; -.
DR   STRING; 1055723.SAMN05216293_3458; -.
DR   OrthoDB; 9788689at2; -.
DR   Proteomes; UP000184031; 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; cd11593; Agmatinase-like_2; 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:SF44; AGMATINASE 1; 1.
DR   PANTHER; PTHR11358; ARGINASE/AGMATINASE; 1.
DR   Pfam; PF00491; Arginase; 1.
DR   PIRSF; PIRSF036979; Arginase; 1.
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   313 AA;  35853 MW;  A87CF06C34CAE6DB CRC64;
     MKTNRIYAGI PKEYASPEKA KVVLLPVPYD ATSTWGKGAD KGPEAFLEAS ENMEWYDIET
     DTEAYRQGIY LANPIDVLDS PENMVDAVHK TVKEYIKRNK LVTMIGGEHS ISIGAIRAFN
     ECFEDLTVLH LDAHADLRKE YNGSPYNHAC AMREANETTN LVQVGIRSMD HSETLVMDRD
     KVFFAHEMVT DDFWMDTALD LMTDHVYISF DLDAFDPSIL PSTGTPEPGG LFWYETLDFL
     KRVFEEKKVV GFDIVELCPN TQERSSDFLA AKLYYKMLSY KFLKKNDYLE DGFDENNDNF
     KKSVNPIDDY DEQ
//
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