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Database: UniProt
Entry: F1Z8F3_9SPHN
LinkDB: F1Z8F3_9SPHN
Original site: F1Z8F3_9SPHN 
ID   F1Z8F3_9SPHN            Unreviewed;       346 AA.
AC   F1Z8F3;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:EGD59072.1};
GN   ORFNames=Y88_1134 {ECO:0000313|EMBL:EGD59072.1};
OS   Novosphingobium nitrogenifigens DSM 19370.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=983920 {ECO:0000313|EMBL:EGD59072.1, ECO:0000313|Proteomes:UP000004728};
RN   [1] {ECO:0000313|EMBL:EGD59072.1, ECO:0000313|Proteomes:UP000004728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19370 {ECO:0000313|EMBL:EGD59072.1,
RC   ECO:0000313|Proteomes:UP000004728};
RX   PubMed=22156397; DOI=10.1128/JB.06381-11;
RA   Strabala T.J., Macdonald L., Liu V., Smit A.M.;
RT   "Draft Genome Sequence of Novosphingobium nitrogenifigens Y88T.";
RL   J. Bacteriol. 194:201-201(2012).
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:EGD59072.1}.
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DR   EMBL; AEWJ01000037; EGD59072.1; -; Genomic_DNA.
DR   RefSeq; WP_008065632.1; NZ_GL876926.1.
DR   AlphaFoldDB; F1Z8F3; -.
DR   STRING; 983920.Y88_1134; -.
DR   eggNOG; COG0010; Bacteria.
DR   HOGENOM; CLU_039478_0_0_5; -.
DR   InParanoid; F1Z8F3; -.
DR   OrthoDB; 9788689at2; -.
DR   Proteomes; UP000004728; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004728}.
SQ   SEQUENCE   346 AA;  36685 MW;  66FC3146916EC78D CRC64;
     MTDEPLDLET LRQLYTGASG SDIRDPHFRE AAGQQYKGDK RTWPFAGVPT LLDAPFLADG
     LTPEALDTLD VALIGVPMDL GVTNRPGARF GPRALRAIER VGPYEHVLRV APKGKLKVAD
     VGDVSMSSRY DLAACHADIE ACYRMIAGTK AIPLSVGGDH SITLPIMKGL AEKHGPVGMV
     HIDAHCDTGG TTEGSKFHHG APFREAVLEG VLDPRRSIQI GIRGASECLW EFSYLSGMTV
     IHAEEVDAMG IAAVVAKMRE VIGDGPTYIT FDVDGLDPAF APGTGTPEVG GLTTLQAQQI
     LRGLAGANII GGDVVEVAPE YDPSHNTAHA GAQMLFTMLS LLAVNK
//
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