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Database: UniProt
Entry: A0A0S2K3S6_9GAMM
LinkDB: A0A0S2K3S6_9GAMM
Original site: A0A0S2K3S6_9GAMM 
ID   A0A0S2K3S6_9GAMM        Unreviewed;       314 AA.
AC   A0A0S2K3S6;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:ALO42971.1};
GN   ORFNames=PP2015_2479 {ECO:0000313|EMBL:ALO42971.1};
OS   Pseudoalteromonas phenolica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=161398 {ECO:0000313|EMBL:ALO42971.1, ECO:0000313|Proteomes:UP000061457};
RN   [1] {ECO:0000313|EMBL:ALO42971.1, ECO:0000313|Proteomes:UP000061457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 12086 {ECO:0000313|EMBL:ALO42971.1,
RC   ECO:0000313|Proteomes:UP000061457};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-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; CP013187; ALO42971.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S2K3S6; -.
DR   STRING; 161398.PP2015_2479; -.
DR   KEGG; pphe:PP2015_2479; -.
DR   PATRIC; fig|161398.10.peg.2534; -.
DR   Proteomes; UP000061457; Chromosome I.
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   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000061457}.
SQ   SEQUENCE   314 AA;  34189 MW;  5A48D4B0BA63A9FB CRC64;
     MYKGNEMHTV FEKDNCMLFG NAMTFMRRPL VLNPLTVEAD VVVLGLPYDM ATSGRSGARM
     GPDAMRKAST NLAWEDTRYP WQFALNEHCN VVDAGDLTYM SGDSSEFTEK VEAAATSILE
     QGKSMLSFGG DHFVTLPLLR AHAKKFGKMA LVHFDAHTDT YSNGSAYDHG TMFYHAPNEG
     LIDKHRSVQV GIRTNYTEAD HGFTVIDGQQ GNELSASKIA EIITNTVGDL PVYLTFDIDA
     LDPAFAPGTG TPVCGGLTTD KVLNILRALK GLNLVGMDVV EVAPAYDSSE VTALAGASIA
     LELLHLWTYK HKTI
//
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