ID A0A0J1FJD3_9FIRM Unreviewed; 290 AA.
AC A0A0J1FJD3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:KLU63532.1};
DE EC=3.5.3.11 {ECO:0000313|EMBL:KLU63532.1};
GN Name=speB {ECO:0000313|EMBL:KLU63532.1};
GN ORFNames=CEB3_c00810 {ECO:0000313|EMBL:KLU63532.1};
OS Peptococcaceae bacterium CEB3.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=999898 {ECO:0000313|EMBL:KLU63532.1, ECO:0000313|Proteomes:UP000035957};
RN [1] {ECO:0000313|EMBL:KLU63532.1, ECO:0000313|Proteomes:UP000035957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEB3 {ECO:0000313|EMBL:KLU63532.1,
RC ECO:0000313|Proteomes:UP000035957};
RA Poehlein A., Petzsch P., Johnson B.D., Schloemann M., Daniel R.,
RA Muehling M.;
RT "Genome sequence of the moderately acidophilic sulfate reducing
RT Peptococcaceae bacterium strain CEB3.";
RL Submitted (JUN-2015) 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:KLU63532.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LDXJ01000015; KLU63532.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J1FJD3; -.
DR STRING; 999898.CEB3_c00810; -.
DR PATRIC; fig|999898.3.peg.99; -.
DR OrthoDB; 9788689at2; -.
DR Proteomes; UP000035957; Unassembled WGS sequence.
DR GO; GO:0008783; F:agmatinase activity; IEA:UniProtKB-EC.
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:SF43; AGMATINASE; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000035957}.
SQ SEQUENCE 290 AA; 32233 MW; A6276C94DC915516 CRC64;
MAERDVSELV DAPGIFMGAD ALYDEAKAVI LGIPMDFTVS FRPGARLGPL SIRNVSAGIE
EYSVYQDKDL SNCVYRDLGD LSLPFGNVQR SLQIIERACH ILLADGKFPI FLGGEHLVSY
PLLRSFRKRY PDLRVLHFDA HADLREDYLG EKDSHATVMR QVAGLFEEKR LYQFGIRSGT
KEEFDFAREH THMHIDEVLE PLQKTLTELK GHPLYVTLDI DVVDPAYAPG TGTQEPGGCT
SREILTAVRS LAGQNVVGFD LVEVLPALDA SERTALLAAK IVREVILAFT
//
