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Database: UniProt
Entry: V9W0G8_9RHOB
LinkDB: V9W0G8_9RHOB
Original site: V9W0G8_9RHOB 
ID   V9W0G8_9RHOB            Unreviewed;       323 AA.
AC   V9W0G8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:AHD03504.1};
GN   ORFNames=METH_22005 {ECO:0000313|EMBL:AHD03504.1};
OS   Leisingera methylohalidivorans DSM 14336.
OG   Plasmid unnamed {ECO:0000313|EMBL:AHD03504.1,
OG   ECO:0000313|Proteomes:UP000018780}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Leisingera.
OX   NCBI_TaxID=999552 {ECO:0000313|EMBL:AHD03504.1, ECO:0000313|Proteomes:UP000018780};
RN   [1] {ECO:0000313|EMBL:AHD03504.1, ECO:0000313|Proteomes:UP000018780}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14336 {ECO:0000313|EMBL:AHD03504.1,
RC   ECO:0000313|Proteomes:UP000018780};
RC   PLASMID=1 {ECO:0000313|Proteomes:UP000018780};
RG   DOE Joint Genome Institute;
RA   Klenk H.-P., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (SEP-2013) 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; CP006774; AHD03504.1; -; Genomic_DNA.
DR   RefSeq; WP_024092800.1; NC_023146.1.
DR   AlphaFoldDB; V9W0G8; -.
DR   KEGG; lmd:METH_22005; -.
DR   PATRIC; fig|999552.6.peg.4351; -.
DR   HOGENOM; CLU_039478_0_0_5; -.
DR   OrthoDB; 9788689at2; -.
DR   Proteomes; UP000018780; Plasmid 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   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   Plasmid {ECO:0000313|EMBL:AHD03504.1}.
SQ   SEQUENCE   323 AA;  34479 MW;  C5BA7E89502EFFE5 CRC64;
     MTDTSSVNPV QGDLAFTRAS DRGVIAEASY AGALSFMRRR YTRDLSGADV AVMGVPFDLS
     VSSRSGTRLG PRAVRSGSSH IAWSKPWPWE ADPYEALRVV DYGDCEFDYG YPHKVPGQIT
     QAARDVLASD TALLSIGGDH FITYPLLKAH AEKHGPLSLI QFDAHSDTWA DEEGRIDHGT
     MLWHAIREGL VDPACSVQVG IRTHNPDPMG MNIIDAIEVQ KSGPEAVAEK IRAITGGRKT
     YVTFDIDALE PASAPGTGTP VIGGLSPYQA QEIIRGLAGI DVVGMDVVEV APAYDISEIT
     AIAGATIAND LLCLYAAGKS GQR
//
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