ID A0A1A1Y756_9MYCO Unreviewed; 339 AA.
AC A0A1A1Y756;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:OBF27140.1};
GN ORFNames=A5724_03605 {ECO:0000313|EMBL:OBF27140.1};
OS Mycobacterium sp. ACS1612.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834117 {ECO:0000313|EMBL:OBF27140.1, ECO:0000313|Proteomes:UP000092025};
RN [1] {ECO:0000313|Proteomes:UP000092025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS1612 {ECO:0000313|Proteomes:UP000092025};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Kiyimba A., Mayanja H.,
RA Musoke P., Ssengooba W., Joloba M.;
RL Submitted (JUN-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:OBF27140.1}.
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DR EMBL; LZHZ01000067; OBF27140.1; -; Genomic_DNA.
DR RefSeq; WP_067810658.1; NZ_LZHZ01000067.1.
DR AlphaFoldDB; A0A1A1Y756; -.
DR STRING; 1834117.A5724_03605; -.
DR Proteomes; UP000092025; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000092025}.
FT REGION 320..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 339 AA; 35965 MW; F0B72B3CEF1093B3 CRC64;
MTSAPPIGPV DATRVPRYAG PATFARLPRT DEVTHTDVAV VGIPFDSGVS YRPGARFGPG
HIRASSKLLR PYHPRLDVEP FAVQQVADAG DIAVNPFDIA EAITTIERAS DELRDGGTKL
ITLGGDHTIA LPLLRSLHRD HGPVAVLHFD AHLDTWDTYF GAPFTHGTPF RRASEEGLLD
PEHCLHVGIR GPLYASTDLT DDKVLGFQVI GTDDFQIEGL AAVIERTRAR LGEAPVYVSV
DIDVLDPAHA PGTGTPEAGG MTSRELLHCL RSLVGVNVVG ADIVEVAPAY DHAEITGIAA
AHVAYELMSV LAASAGRSEA TRGMASAGRS EATRGMTQP
//