ID A0A167IN54_9FLAO Unreviewed; 311 AA.
AC A0A167IN54;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:OAB79848.1};
GN ORFNames=ULVI_03670 {ECO:0000313|EMBL:OAB79848.1};
OS Cochleicola gelatinilyticus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cochleicola.
OX NCBI_TaxID=1763537 {ECO:0000313|EMBL:OAB79848.1, ECO:0000313|Proteomes:UP000077013};
RN [1] {ECO:0000313|EMBL:OAB79848.1, ECO:0000313|Proteomes:UP000077013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0005 {ECO:0000313|EMBL:OAB79848.1,
RC ECO:0000313|Proteomes:UP000077013};
RA Shin S.-K., Yi H.;
RT "Ulvibacter sp. LPB0005, isolated from Thais luteostoma.";
RL Submitted (FEB-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:OAB79848.1}.
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DR EMBL; LRXL01000026; OAB79848.1; -; Genomic_DNA.
DR RefSeq; WP_068589873.1; NZ_LRXL01000026.1.
DR AlphaFoldDB; A0A167IN54; -.
DR STRING; 1763537.ULVI_03670; -.
DR OrthoDB; 9788689at2; -.
DR Proteomes; UP000077013; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000077013}.
FT REGION 292..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 311 AA; 35102 MW; F8B0501B87E0D237 CRC64;
MSTKTYAGIP QKYATLETSK IVLIPVPYDG TSTWQKGADK GPEAFLNASE NMELYDIETK
TEVYKQGIHL TEPIEENSSP EAVVDAVHKM TKDFILRNKF VTVFGGEHSI SIGTIRAFNE
CFDDLTVLHI DAHADLRKEY DGSTCNHACA VYEASQNTNL VQVGIRSMDV SETTIIDEEK
TWFAHDMAGD EYWMDNVIEA LGDNVFITFD LDAFDPSIMP STGTPEPGGL FYYETLEFLK
QVFAERNVVG FDIVELCPNE NEKSSDFLAA KLYYKMLSYK FEGAEEEDEF ESNFNDSKRG
ISKFNDNEDD N
//
