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Database: UniProt
Entry: A0A063BII7_9BURK
LinkDB: A0A063BII7_9BURK
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ID   A0A063BII7_9BURK        Unreviewed;       318 AA.
AC   A0A063BII7;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:KDB07503.1};
DE            EC=3.5.3.11 {ECO:0000313|EMBL:KDB07503.1};
GN   ORFNames=LIG30_3412 {ECO:0000313|EMBL:KDB07503.1};
OS   Burkholderia sp. lig30.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=1192124 {ECO:0000313|EMBL:KDB07503.1, ECO:0000313|Proteomes:UP000027020};
RN   [1] {ECO:0000313|EMBL:KDB07503.1, ECO:0000313|Proteomes:UP000027020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LIG30 {ECO:0000313|Proteomes:UP000027020};
RA   Woo H.L., Utturkar S.M., Klingeman D.M., Simmons B.A., DeAngelis K.M.,
RA   Brown S.D., Hazen T.C.;
RT   "Draft Genome of the Lignin-degrading Burkholderia sp. Strain LIG30,
RT   Isolated from Wet Tropical Forest Soil.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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:KDB07503.1}.
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DR   EMBL; JGVW01000086; KDB07503.1; -; Genomic_DNA.
DR   RefSeq; WP_038713717.1; NZ_JGVW01000086.1.
DR   AlphaFoldDB; A0A063BII7; -.
DR   STRING; 1192124.LIG30_3412; -.
DR   PATRIC; fig|1192124.4.peg.3468; -.
DR   eggNOG; COG0010; Bacteria.
DR   OrthoDB; 9789727at2; -.
DR   Proteomes; UP000027020; 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:UP000027020}.
SQ   SEQUENCE   318 AA;  34262 MW;  F8DED6023F464837 CRC64;
     MNAQNHFQPL GGNEMPRCGG IATMMRLPHV QTAEGLDACF VGVPFDLGTS NRTGARFGPR
     QIRTESVLLR PYNMATRAAP FDSLQVADIG DVAINPYNLH DSIARIESAY DAILVHGCKP
     ITLGGDHTIA LPILRAIHRQ HGKVALIHVD AHADVNDTMM GEKIAHGTPF RRAVEEGLLD
     CSKVVQIGLR GTGYAAEDFD WCRQQGFRVV QAETCWNQSL APLMAEVREQ IGDTPVYISF
     DIDGIDPAYA PGTGTPEIAG LTVPQALEIV RGAHGLNIVG CDLVEVAPPY DPFGTTALLG
     ANLAYELLCV LPGVAYRD
//
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