ID F0G8M8_9BURK Unreviewed; 289 AA.
AC F0G8M8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:EGD02151.1};
GN ORFNames=B1M_22951 {ECO:0000313|EMBL:EGD02151.1};
OS Burkholderia sp. TJI49.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=987057 {ECO:0000313|EMBL:EGD02151.1, ECO:0000313|Proteomes:UP000003049};
RN [1] {ECO:0000313|EMBL:EGD02151.1, ECO:0000313|Proteomes:UP000003049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TJI49 {ECO:0000313|EMBL:EGD02151.1,
RC ECO:0000313|Proteomes:UP000003049};
RX PubMed=23653265; DOI=10.1007/s11274-013-1366-5;
RA Khan A., Asif H., Studholme D.J., Khan I.A., Azim M.K.;
RT "Genome characterization of a novel Burkholderia cepacia complex genomovar
RT isolated from dieback affected mango orchards.";
RL World J. Microbiol. Biotechnol. 29:2033-2044(2013).
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:EGD02151.1}.
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DR EMBL; AEXE01001374; EGD02151.1; -; Genomic_DNA.
DR AlphaFoldDB; F0G8M8; -.
DR PATRIC; fig|987057.7.peg.3599; -.
DR BioCyc; BSP987057:G10O5-5481-MONOMER; -.
DR Proteomes; UP000003049; 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 289 AA; 31238 MW; 210ED705F78B1EC0 CRC64;
MPSAEGLDAC FVGVPFDLGT SNRTGARFGP RQIRTESVLL RPYNMATRAA PFDSLQVADI
GDVAINPYNL HDSIARIEDA YDAILKHDCK PITLGGDHTI ALPILRAIHR KHGKVALIHV
DAHADVNDTM MGEKIAHGTP FRRAVEEGLL HGDKVTQIGL RGTGYHADDF DWCREQGFTV
VQAEECWNQS LAPLMEEVRA RIGDTPVYIS FDIDGIDPAY APGTGTPEIA GLTVPQALEI
IRGAKGLNIV GCDLVEVAPP YDPFGTTALL GANLAYELLC VLPGVAYRD
//
