ID A0A0R2X217_9FLAO Unreviewed; 311 AA.
AC A0A0R2X217;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:KRP27851.1};
GN ORFNames=ABS28_07325 {ECO:0000313|EMBL:KRP27851.1};
OS Cryomorphaceae bacterium BACL22 MAG-120619-bin32.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Cryomorphaceae.
OX NCBI_TaxID=1655630 {ECO:0000313|EMBL:KRP27851.1, ECO:0000313|Proteomes:UP000052139};
RN [1] {ECO:0000313|EMBL:KRP27851.1, ECO:0000313|Proteomes:UP000052139}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL3 MAG-120619-bin32 {ECO:0000313|EMBL:KRP27851.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
RL Submitted (OCT-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:KRP27851.1}.
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DR EMBL; LIDG01000206; KRP27851.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2X217; -.
DR Proteomes; UP000052139; Unassembled WGS sequence.
DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
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 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; PS51409; ARGINASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT REGION 284..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 311 AA; 34997 MW; 59F7515F39A860AA CRC64;
MKTYAGIPEN NATLGNSKIV LIPVPFEGAY RWQKGANKGP QAFLEASENM DLYDIETDSE
VYKEGVFLAD PISENSSPQA MVNAVHQNVK KFINKNKFVT VFGGEHSVSI GTIKAFNDCF
QSLTVLHFDA HANLCKEFEG SSFHHKCALY EANQTTNLVQ VGIRSMDISE KRTMNADKVF
FAHDMAVNEF WMDDVIDQLT SNVFITFDFS AFDASIFSAT GNPVSGGLFY YETLEFLKRV
FTKKNVVGFD MAEFCPIPNQ KTSDSLAAKL YYKMLSYKFS SKNDTYDTDD SSPNNNPFSK
LSKFKNDEDD F
//
