ID A0A3E0I8U6_9PSEU Unreviewed; 336 AA.
AC A0A3E0I8U6;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:REH55090.1};
GN ORFNames=BCF44_101106 {ECO:0000313|EMBL:REH55090.1};
OS Kutzneria buriramensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1045776 {ECO:0000313|EMBL:REH55090.1, ECO:0000313|Proteomes:UP000256269};
RN [1] {ECO:0000313|EMBL:REH55090.1, ECO:0000313|Proteomes:UP000256269}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45791 {ECO:0000313|EMBL:REH55090.1,
RC ECO:0000313|Proteomes:UP000256269};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (AUG-2018) 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:REH55090.1}.
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DR EMBL; QUNO01000001; REH55090.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E0I8U6; -.
DR Proteomes; UP000256269; 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; cd09990; Agmatinase-like; 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 336 AA; 36140 MW; 2760F63F714AFBD6 CRC64;
MRYGAMYGPD VTFLGVERCA LAEPASFAGA DVVIVGAPYD GGTSHRPGTR FGPMAIRTTD
YLGHNGSRPS LALRVDALKD LRVLDAGDVE MYAGDEMESH AAIEEAVHTI TASGAIPVVL
GGDHSIALPD ARGVARHYGF GRVSMIHFDA HADTGDIEFG HLYGHGQPMR RLLECGAIRG
DRFLQLGLRG YWPEPDTLDW MAEQRMRSYE MTEIVTRGFD ECLAEASAIA MDDCDGVYLS
VDVDVCDPGH APGTGTPEPG GISARQLLDA VRGICYRLPV VGVEIVEVSP PYDHAEITAA
LGNRVVLEAL SGIARRRKDA ESGHTWDPAQ PLLDGR
//