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Database: UniProt
Entry: M9XCB5_MEIRD
LinkDB: M9XCB5_MEIRD
Original site: M9XCB5_MEIRD 
ID   M9XCB5_MEIRD            Unreviewed;       327 AA.
AC   M9XCB5;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:AGK04278.1};
GN   ORFNames=K649_04880 {ECO:0000313|EMBL:AGK04278.1};
OS   Meiothermus ruber (strain ATCC 35948 / DSM 1279 / VKM B-1258 / 21) (Thermus
OS   ruber).
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Meiothermus.
OX   NCBI_TaxID=504728 {ECO:0000313|EMBL:AGK04278.1, ECO:0000313|Proteomes:UP000013026};
RN   [1] {ECO:0000313|EMBL:AGK04278.1, ECO:0000313|Proteomes:UP000013026}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35948 / DSM 1279 / VKM B-1258 / 21
RC   {ECO:0000313|Proteomes:UP000013026};
RA   Chin J., Alexander D.H., Marks P., Korlach J., Clum A., Copeland A.;
RL   Submitted (APR-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; CP005385; AGK04278.1; -; Genomic_DNA.
DR   AlphaFoldDB; M9XCB5; -.
DR   STRING; 504728.K649_04880; -.
DR   KEGG; mre:K649_04880; -.
DR   PATRIC; fig|504728.9.peg.1006; -.
DR   eggNOG; COG0010; Bacteria.
DR   Proteomes; UP000013026; Chromosome.
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   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
SQ   SEQUENCE   327 AA;  36274 MW;  3842C32FAC49945D CRC64;
     MGAEPGPLAE ENVRYQPADS LESPRFAGVR TFMRLPHVRT LENVDFVVLG IPWDDATTHR
     PGARFGPEGI RRVSIMLRPW NPYWDVKIFD YLSGVDYGDV PVVPGYIEDT YARIEAEFER
     IARAGVTPIA MGGDHSVTLG ELRGLAKVHG PLALVHIDAH LDTLDQYFGR KYNHGTPFRR
     AVEEGLVDPH RSIQVGIRGS NYGPEDYQGT RDLGYELITM YELQEIGLEA TLERIHRRVG
     PAPCFISIDI DAVDPAYAPG TGTPEVDGFT SREILRLVRG LKGLNFKAAD VVEVLPALDP
     GEITAYLGGN LIYELISLLA LRKKEGR
//
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