ID A0A1E5AHE1_9RHOB Unreviewed; 323 AA.
AC A0A1E5AHE1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:OED49614.1};
GN ORFNames=AB838_06015 {ECO:0000313|EMBL:OED49614.1};
OS Rhodobacteraceae bacterium (ex Bugula neritina AB1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1868286 {ECO:0000313|EMBL:OED49614.1, ECO:0000313|Proteomes:UP000094333};
RN [1] {ECO:0000313|EMBL:OED49614.1, ECO:0000313|Proteomes:UP000094333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB1-7 {ECO:0000313|EMBL:OED49614.1};
RX PubMed=27681823; DOI=10.1038/srep34362;
RA Miller I.J., Weyna T.R., Vanee N., Fong S., Lim-Fong G.E.;
RT "Single sample resolution of rare microbial dark matter in a marine
RT invertebrate metagenome.";
RL Sci. Rep. 6:34362-34362(2016).
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:OED49614.1}.
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DR EMBL; MDLF01000047; OED49614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E5AHE1; -.
DR STRING; 1868286.AB838_06015; -.
DR Proteomes; UP000094333; 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; cd11592; Agmatinase_PAH; 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:SF26; AGMATINASE, MITOCHONDRIAL; 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}.
SQ SEQUENCE 323 AA; 34779 MW; 2B9B12A5AEC5505A CRC64;
MTDSSSVNPV QGDLAFTRES DRGVVAEASY AGALSFMRRR YSRDLSRADV AVMGVPFDLS
VSSRSGTRLG PRAVRSGSSH IAWSKPWPWE VDPYEVLRVV DYGDCEFDYG YPHKVPGEIV
QTARDVLATD TALLSIGGDH FITYPLLQAH VEKHGPLSLI QFDAHSDTWA DEEGRIDHGT
MLWHAIREGL VDPARSVQVG IRTHNPDPLG MNIIDAIEVQ KSGPEAVADK IRSIVGGHKT
YVTFDIDALE PDSAPGTGTP VIGGLTPYQA QEIIRGLAGT NVVGMDVVEV APAYDVSEIT
AIAAATIAND LLCLYAAGPS GRR
//
