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Database: UniProt
Entry: S9QC72_9RHOB
LinkDB: S9QC72_9RHOB
Original site: S9QC72_9RHOB 
ID   S9QC72_9RHOB            Unreviewed;       313 AA.
AC   S9QC72;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:EPX79011.1};
DE            EC=3.5.3.11 {ECO:0000313|EMBL:EPX79011.1};
GN   ORFNames=thalar_01828 {ECO:0000313|EMBL:EPX79011.1};
OS   Litoreibacter arenae DSM 19593.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Litoreibacter.
OX   NCBI_TaxID=1123360 {ECO:0000313|EMBL:EPX79011.1, ECO:0000313|Proteomes:UP000015351};
RN   [1] {ECO:0000313|Proteomes:UP000015351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19593 {ECO:0000313|Proteomes:UP000015351};
RX   PubMed=24501650; DOI=10.4056/sigs.4258318;
RA   Riedel T., Fiebig A., Petersen J., Gronow S., Kyrpides N.C., Goker M.,
RA   Klenk H.P.;
RT   "Genome sequence of the Litoreibacter arenae type strain (DSM 19593(T)), a
RT   member of the Roseobacter clade isolated from sea sand.";
RL   Stand. Genomic Sci. 9:117-127(2013).
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:EPX79011.1}.
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DR   EMBL; AONI01000010; EPX79011.1; -; Genomic_DNA.
DR   RefSeq; WP_021100391.1; NZ_KE557306.1.
DR   AlphaFoldDB; S9QC72; -.
DR   STRING; 1123360.thalar_01828; -.
DR   PATRIC; fig|1123360.3.peg.1811; -.
DR   eggNOG; COG0010; Bacteria.
DR   HOGENOM; CLU_039478_0_0_5; -.
DR   OrthoDB; 9788689at2; -.
DR   Proteomes; UP000015351; Unassembled WGS sequence.
DR   GO; GO:0008783; F:agmatinase activity; IEA:UniProtKB-EC.
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:UP000015351}.
SQ   SEQUENCE   313 AA;  33979 MW;  80AE93BF5F190AD6 CRC64;
     MPNQPISGND LARFAGQGTF MRLPRVETAD GLDVAFVGIP MDHGSSWRSG TRFGPAQVRS
     ESSMIRPYAV QTGAAPFDAL QCADVGDVAI NTFNLQESIH IITEHYDDLL KHDVIPMTIG
     GDHTITLPIL RAIAKKHGPV GLVHVDAHAD VNDEMFGERE THGTVFRRAY EEGLLRPKDV
     YQIGLRGTGY TAEDFDEPRD WGFNLTLAQE LWHKSTAPLA ARIKDSMGEG PVYITYDIDS
     LDPSIAPGTG TPEIGGLTTP QALELIRGLR GLPIVGCDLV EVSPPYDTSG NTALTGANIM
     FEMLSILPGV PYR
//
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