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Database: UniProt
Entry: A0A428XSZ9_9ACTN
LinkDB: A0A428XSZ9_9ACTN
Original site: A0A428XSZ9_9ACTN 
ID   A0A428XSZ9_9ACTN        Unreviewed;       369 AA.
AC   A0A428XSZ9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:RSM58466.1};
GN   ORFNames=DMB66_29700 {ECO:0000313|EMBL:RSM58466.1};
OS   Actinoplanes sp. ATCC 53533.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=1288362 {ECO:0000313|EMBL:RSM58466.1, ECO:0000313|Proteomes:UP000287606};
RN   [1] {ECO:0000313|EMBL:RSM58466.1, ECO:0000313|Proteomes:UP000287606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53533 {ECO:0000313|EMBL:RSM58466.1,
RC   ECO:0000313|Proteomes:UP000287606};
RA   Waglechner N., Wright G.D.;
RT   "Evolution of GPA BGCs.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00742, ECO:0000256|RuleBase:RU003684}.
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:RSM58466.1}.
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DR   EMBL; QHHV01000099; RSM58466.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A428XSZ9; -.
DR   OrthoDB; 9788689at2; -.
DR   Proteomes; UP000287606; 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   CDD; cd09990; Agmatinase-like; 1.
DR   Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR   InterPro; IPR006035; Ureohydrolase.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   InterPro; IPR020855; Ureohydrolase_Mn_BS.
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:UP000287606}.
SQ   SEQUENCE   369 AA;  40169 MW;  928726536B1D9923 CRC64;
     MHDRYGPEAA YAVAAEAKLP TTKWQEEIAR GLEYGLPGAD SIKDRTIPTF SRGELPHFAG
     INTFLKAPYV EDVRRCGEYD VAVLGAPFDG GTTYRSGTRF GPQGIRKISA LYGPYSFELG
     VDLRESITIA DLGDIFTIPA NIEKTFDQIS KAVGHVFESG AFPVVLGGDH SIGYPTVRGV
     AQHLQGNLGI IHFDRHVDTQ ETDLDERMHT TPWFHATDIP NVPPKNLVQI GIGGWQAPRP
     GVKVGRERGT TIMTVTDCVE MGIEQAAERA LEVAWDGAEA VWLSFDVDCL DAAFVPGTGW
     PEPGGFLPRE VLKFIQIIAD ARPLAGIEVV ECAPAYDTAE ITALLATRVI CDTLGCLVRS
     GHLPQEKKR
//
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