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Database: UniProt
Entry: A0A0X3U1T4_9RHOB
LinkDB: A0A0X3U1T4_9RHOB
Original site: A0A0X3U1T4_9RHOB 
ID   A0A0X3U1T4_9RHOB        Unreviewed;       322 AA.
AC   A0A0X3U1T4;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:KUJ82035.1};
GN   ORFNames=AVO44_01805 {ECO:0000313|EMBL:KUJ82035.1};
OS   Ruegeria profundi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=1685378 {ECO:0000313|EMBL:KUJ82035.1, ECO:0000313|Proteomes:UP000053690};
RN   [1] {ECO:0000313|Proteomes:UP000053690}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZGT108 {ECO:0000313|Proteomes:UP000053690};
RA   Zhang G., Stingl U.;
RL   Submitted (DEC-2015) 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:KUJ82035.1}.
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DR   EMBL; LQBP01000001; KUJ82035.1; -; Genomic_DNA.
DR   RefSeq; WP_068331722.1; NZ_LQBP01000001.1.
DR   AlphaFoldDB; A0A0X3U1T4; -.
DR   STRING; 1685378.AVO44_01805; -.
DR   OrthoDB; 9788689at2; -.
DR   Proteomes; UP000053690; 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}.
SQ   SEQUENCE   322 AA;  34411 MW;  45D5E7CD8D3EA29B CRC64;
     MALEDAKTQV DEAFTNPDLK GLSFENTFGG ATSFLRRLYT KTLTGVDIAV TGVPFDQAVT
     NRPGTRLGPR AIREASALQS PDAPYGWPFD ALSELAIIDY GDVAYDYANI PAFPDLLTDH
     IRTILAADVA SVSLGGDHYI SFPILKAYAE KYGPMSLLQF DAHTDTWADD DMSRVDHGTM
     FYKAVKSGIV DPKRSVQVGI RTTNEDTLGV NIINAREVYE AGPAAVAEKI KGILGDSPVY
     LSFDIDGLDP AFAPGTGTPV WGGLSSIQAQ IILRDIAGIN IKGGDVVEVS PPYDTSGATA
     IAGAHVATQI ICLLGWRKLE QG
//
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