ID A0A369XY93_9FUSO Unreviewed; 282 AA.
AC A0A369XY93;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:RDE61097.1};
DE EC=3.5.3.11 {ECO:0000313|EMBL:RDE61097.1};
GN Name=speB {ECO:0000313|EMBL:RDE61097.1};
GN ORFNames=DV867_09655 {ECO:0000313|EMBL:RDE61097.1};
OS Psychrilyobacter sp. S5.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Psychrilyobacter.
OX NCBI_TaxID=2283384 {ECO:0000313|EMBL:RDE61097.1, ECO:0000313|Proteomes:UP000253914};
RN [1] {ECO:0000313|EMBL:RDE61097.1, ECO:0000313|Proteomes:UP000253914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S5 {ECO:0000313|EMBL:RDE61097.1,
RC ECO:0000313|Proteomes:UP000253914};
RA Yadav S., Villanueva L., Damste J.S.S.;
RT "Draft genome sequence of Psychrilyobacter sp. strain S5.";
RL Submitted (JUL-2018) 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:RDE61097.1}.
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DR EMBL; QQOU01000016; RDE61097.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369XY93; -.
DR Proteomes; UP000253914; 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 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:UP000253914}.
SQ SEQUENCE 282 AA; 31767 MW; D1E931F94BD312A3 CRC64;
MKNKNISTFI GFDNEYDESK IVVFGAPFDG TTSFRPGTRF APEVMRRESY GLETYSPYLE
KDLENYKVFD GGDLEFSFGN PGAVLDSIYK YTEEILKDDK VPFMVGGEHL VSYGSIKAVY
EKYPNLHVIH LDAHADLRAD YMGEQFSHAS VIRRCWDFLG DGKIYQFGIR SGCKEEFLWA
KDHTYMEKYS MNTLSEIVDK LKDVPVYITI DLDILDPSIF PGTGTPEPGG ITFKEMMDGI
KEFEKLNVVG GDIVELSPSY DTSGASTATA CKVLREVVLT MV
//
