ID A0A1B1PPD7_9RHOB Unreviewed; 320 AA.
AC A0A1B1PPD7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:ANT60448.1};
GN ORFNames=AYJ57_08800 {ECO:0000313|EMBL:ANT60448.1};
OS Salipiger sp. CCB-MM3.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=1792508 {ECO:0000313|EMBL:ANT60448.1, ECO:0000313|Proteomes:UP000092483};
RN [1] {ECO:0000313|EMBL:ANT60448.1, ECO:0000313|Proteomes:UP000092483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCB-MM3 {ECO:0000313|EMBL:ANT60448.1,
RC ECO:0000313|Proteomes:UP000092483};
RA Lau N.-S., Sam K.K., Abdullah A.A.-A., Chong A.S.-C.;
RT "Genome feautures of moderately halophilic polyhydroxyalkanoate-producing
RT Yangia sp. CCB-MM3.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC {ECO:0000256|ARBA:ARBA00009227}.
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DR EMBL; CP014595; ANT60448.1; -; Genomic_DNA.
DR RefSeq; WP_066103843.1; NZ_CP014595.1.
DR AlphaFoldDB; A0A1B1PPD7; -.
DR STRING; 1792508.AYJ57_08800; -.
DR KEGG; yan:AYJ57_08800; -.
DR OrthoDB; 9788689at2; -.
DR Proteomes; UP000092483; Chromosome 1.
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 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:UP000092483}.
SQ SEQUENCE 320 AA; 34567 MW; B861D50B575F1AA7 CRC64;
MTSDPFFHPV SGMDLPRFAG IPTFMRLPLV QPDHARFSEV EIGLVGVPWD SGTTNRPGPR
HGPRQLRDAS TMIRAEHGHT GVRPFEAAAC ADLGDVGPNP ADIQDSMARI TAFYDKIVAA
GIRPLTGGGD HLCSLPVLRA LGKAKPLGMV HFDSHTDLWD SYFGGFKFTH GTPFRRAVEE
GLLDPKRVVQ IGIRGPMYDH EDRDFAKAVG IRIIPIEEFH ARGVEDVMAE AREIVGTEPT
YVSYDIDFVD PAFAPGTGTP EIGGPNSYQA LQVVRELMGL NIAGADLVEV SPPFDSTGGT
AFLGVTIMFE LLCAMVGQSA
//
