ID A0A432YZJ9_9GAMM Unreviewed; 274 AA.
AC A0A432YZJ9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:RUO69007.1};
GN Name=speB {ECO:0000313|EMBL:RUO69007.1};
GN ORFNames=CWI80_12165 {ECO:0000313|EMBL:RUO69007.1};
OS Pseudidiomarina sediminum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Pseudidiomarina.
OX NCBI_TaxID=431675 {ECO:0000313|EMBL:RUO69007.1, ECO:0000313|Proteomes:UP000287022};
RN [1] {ECO:0000313|EMBL:RUO69007.1, ECO:0000313|Proteomes:UP000287022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=c121 {ECO:0000313|Proteomes:UP000287022};
RX PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA Liu Y., Lai Q., Shao Z.;
RT "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT Idiomarinaceae.";
RL Front. Microbiol. 9:2453-2453(2018).
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:RUO69007.1}.
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DR EMBL; PIQE01000006; RUO69007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432YZJ9; -.
DR STRING; 1122124.GCA_000423165_02406; -.
DR Proteomes; UP000287022; 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; cd11593; Agmatinase-like_2; 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:SF43; AGMATINASE; 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 274 AA; 30481 MW; 1376331D0B1C86B4 CRC64;
MIGFGFDGTA CFRKGTRNGP DGLRAVSEDI ESYSPYLDAD LFDHAFYDLG NLSLGNGDDI
EGQWQHATDQ FDTLFGPLDL AAHNIRVLTL GGEHSISYAP LRKYLAQYPD LVVLHLDAHA
DLRDGFLGYH YSHASIMRRA LDHFGPDHQL IQYGIRSGTR EEYQFMKEHG TVRTSRKDFL
DSVTAIAGDR PIYLTLDLDY FDPAFLPGTG TPEPGGEDFH SYVSLMKILR EKNLVGADVV
ELSPEIDPTG NSDVFAAKIV RELLIILNEK GARA
//
