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Database: UniProt
Entry: A0A0P1IKN2_9RHOB
LinkDB: A0A0P1IKN2_9RHOB
Original site: A0A0P1IKN2_9RHOB 
ID   A0A0P1IKN2_9RHOB        Unreviewed;       321 AA.
AC   A0A0P1IKN2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Guanidinobutyrase {ECO:0000313|EMBL:CUK19704.1};
DE            EC=3.5.3.7 {ECO:0000313|EMBL:CUK19704.1};
GN   Name=gbh_4 {ECO:0000313|EMBL:CUK19704.1};
GN   ORFNames=RUE5091_04423 {ECO:0000313|EMBL:CUK19704.1};
OS   Ruegeria denitrificans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=1715692 {ECO:0000313|EMBL:CUK19704.1, ECO:0000313|Proteomes:UP000051260};
RN   [1] {ECO:0000313|EMBL:CUK19704.1, ECO:0000313|Proteomes:UP000051260}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 5091 {ECO:0000313|EMBL:CUK19704.1,
RC   ECO:0000313|Proteomes:UP000051260};
RG   Swine Surveillance;
RL   Submitted (SEP-2015) 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; CYUD01000023; CUK19704.1; -; Genomic_DNA.
DR   RefSeq; WP_058284018.1; NZ_CYUD01000023.1.
DR   AlphaFoldDB; A0A0P1IKN2; -.
DR   STRING; 1715692.RUE5091_04423; -.
DR   OrthoDB; 9788689at2; -.
DR   Proteomes; UP000051260; Unassembled WGS sequence.
DR   GO; GO:0047971; F:guanidinobutyrase 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; cd11589; Agmatinase_like_1; 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}.
SQ   SEQUENCE   321 AA;  34962 MW;  D4B189BC843D8513 CRC64;
     MSGHGYEDGR LNLPFVGIAT FGKKPYVENW DKIDADVAVL GAPYDFGCQY RSGARFGPRA
     VREASTLFSF GHAGAYDHED DATYLASDVR IVDLGDADII HTKTEESHAN IEYGVKKILD
     AGALPVTIGG DHSINIPCIR AFAEDCAKNG PIHVVQIDAH LDFVDERKGI TEGHGNPMRR
     AIEKDYVSGM TQLGIRNVSS TAKEGYEDAR ARGSDILSVR QVRKLGTEGV LDRIPEGARY
     YVTIDIDAFC PSIAPGTGTP SHGGFQYYDV LEIVQGLSKR GNVVGIDLVE VAPAYDQTES
     TQILAAQLLL NFLGFIFHNR K
//
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