ID A0A0S8JPP7_9BACT Unreviewed; 284 AA.
AC A0A0S8JPP7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Agmatinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMJ85_03355 {ECO:0000313|EMBL:KPL11695.1};
OS candidate division BRC1 bacterium SM23_51.
OC Bacteria; Candidatus Sumerlaeota.
OX NCBI_TaxID=1703761 {ECO:0000313|EMBL:KPL11695.1, ECO:0000313|Proteomes:UP000051549};
RN [1] {ECO:0000313|EMBL:KPL11695.1, ECO:0000313|Proteomes:UP000051549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_51 {ECO:0000313|EMBL:KPL11695.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPL11695.1}.
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DR EMBL; LJUL01000047; KPL11695.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8JPP7; -.
DR PATRIC; fig|1703761.3.peg.505; -.
DR Proteomes; UP000051549; 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 284 AA; 30692 MW; 0742C081CB3CE84F CRC64;
MASAAVCILP VPYDGTASYQ PGARFGPAAL IAASHQVELF DEQLQRETYR IGIHTCPPVP
PNASGPAAMV DDVRQACETL LDQGKFVAVV GGEHTAALGA IAAHRQKRAD RPFGVVQFDA
HRDLRSIYDS SPWSHACVAA RIIEWQLPLA QLGIRAWSRE EQETAVSASV AALTARELLE
GELVPSLDRA LADLPEEVYL TFDLDVLDPS IMPATGTPEP GGLPWYRTLE LVEQLARCRR
VIGLDIVELA PISGLAAPSY LAARLLYRLI GLVARDWPTL EAGT
//
