ID L0IW53_9MYCO Unreviewed; 315 AA.
AC L0IW53;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:AGB23334.1};
GN ORFNames=Mycsm_03012 {ECO:0000313|EMBL:AGB23334.1};
OS Mycobacterium sp. JS623.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=212767 {ECO:0000313|EMBL:AGB23334.1, ECO:0000313|Proteomes:UP000010844};
RN [1] {ECO:0000313|Proteomes:UP000010844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS623 {ECO:0000313|Proteomes:UP000010844};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A., Rutledge P.,
RA Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium smegmatis JS623.";
RL Submitted (OCT-2011) 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; CP003078; AGB23334.1; -; Genomic_DNA.
DR RefSeq; WP_015306913.1; NC_019966.1.
DR AlphaFoldDB; L0IW53; -.
DR STRING; 212767.Mycsm_03012; -.
DR KEGG; msa:Mycsm_03012; -.
DR PATRIC; fig|710686.3.peg.3040; -.
DR HOGENOM; CLU_039478_0_0_11; -.
DR OrthoDB; 9788689at2; -.
DR Proteomes; UP000010844; 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}.
SQ SEQUENCE 315 AA; 33707 MW; 460042892A1EFB49 CRC64;
MTSQPPIGPV DATRVPRYAG PATFARLPRT DQVTHTDVAV VGIPFDSGVS YRPGARFGPA
HIRAASKLLR PYHPRLDVEP FAVHQVADAG DIAVNPFDIA EAITTIERAS DELRYGGTKL
ITLGGDHTIA LPLLRSLHRD HGPIAVLHFD AHLDTWDTYF GAPFTHGTPF RRASEEGLLD
PEHCLHVGIR GPLYASTDLT DDKVLGFQVI GTDDFQLDGL AAVIERMRAR LGDAPVYVSV
DIDVLDPAHA PGTGTPEAGG ITSRELLHCL RNLVGVNLVG ADIVEVAPAY DHAEITGIAA
AHVAYELLSV LAASK
//
