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Database: UniProt
Entry: A0A2D0AFW8_9BACT
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ID   A0A2D0AFW8_9BACT        Unreviewed;       362 AA.
AC   A0A2D0AFW8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:OWP63302.1};
GN   ORFNames=CDA63_09760 {ECO:0000313|EMBL:OWP63302.1};
OS   Hymenobacter amundsenii.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=2006685 {ECO:0000313|EMBL:OWP63302.1, ECO:0000313|Proteomes:UP000197277};
RN   [1] {ECO:0000313|EMBL:OWP63302.1, ECO:0000313|Proteomes:UP000197277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCM 8682 {ECO:0000313|EMBL:OWP63302.1,
RC   ECO:0000313|Proteomes:UP000197277};
RA   Sedlacek I., Kralova S., Pantucek R., Svec P., Holochova P., Stankova E.,
RA   Vrbovska V., Busse H.-J.;
RT   "Hymenobacter amundsenii sp. nov. isolated from regoliths in Antarctica.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00742, ECO:0000256|RuleBase:RU003684}.
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:OWP63302.1}.
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DR   EMBL; NIRR01000013; OWP63302.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D0AFW8; -.
DR   OrthoDB; 9788689at2; -.
DR   Proteomes; UP000197277; 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   CDD; cd11593; Agmatinase-like_2; 1.
DR   Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR   InterPro; IPR006035; Ureohydrolase.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR   PANTHER; PTHR11358; ARGINASE/AGMATINASE; 1.
DR   Pfam; PF00491; Arginase; 1.
DR   PIRSF; PIRSF036979; Arginase; 2.
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}.
SQ   SEQUENCE   362 AA;  39421 MW;  06063067E0000D4B CRC64;
     MADSASLDQK IASFDPNALG DAAGGLFGLP FTPEEAQVVV VPVPWEVTVS YRAGTAQGPE
     AMRAASLQVD LYDADLPQAW RLGLAMEEPD AAIAAESHEL RPLAEGYIGW LEDGQPESGR
     GEHSSVPARI NQRGRALLEW LKAKTGALLD SGKGVVVLGG DHSTPLGYLH ALAERHEEFG
     ILQIDAHCDL RPAYEGFEFS HASIMYNALQ LPQVKKLVQV GIRDYCQQEA DYIDQSNGRV
     ALFADRFLQA GMLGGKSWKK QCQKIIAQLP PKVYLSFDID GLDPKLCPGT GTPVPGGLEF
     EQALYLLRQV VRSGRTIIGC DLNEVAPGDT DWNAIVGARL LYHMANWMAV SQGRLQAREM
     EK
//
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