ID A0A2T6BAY8_9RHOB Unreviewed; 319 AA.
AC A0A2T6BAY8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:PTX53176.1};
GN ORFNames=C8N34_10188 {ECO:0000313|EMBL:PTX53176.1};
OS Gemmobacter caeni.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Gemmobacter.
OX NCBI_TaxID=589035 {ECO:0000313|EMBL:PTX53176.1, ECO:0000313|Proteomes:UP000244224};
RN [1] {ECO:0000313|EMBL:PTX53176.1, ECO:0000313|Proteomes:UP000244224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21823 {ECO:0000313|EMBL:PTX53176.1,
RC ECO:0000313|Proteomes:UP000244224};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (APR-2018) 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:PTX53176.1}.
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DR EMBL; QBKP01000001; PTX53176.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6BAY8; -.
DR OrthoDB; 9788689at2; -.
DR Proteomes; UP000244224; 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; 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 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 319 AA; 34425 MW; 544DC50D63AD3B12 CRC64;
MSGHAYETGR LNLPFVGIST FGKRPYQADW SRIEADAAVM GAPFDFGTQF RAGARFGPRA
VREASTLFSF GHAGAYDHED DCTYLGSDVR IVDIGDADIV HTDTETSHAN IEAGVRAILK
AGALPVVIGG DHSVNIPCIR AFDDQGPIHI LQIDAHLDFV DVRHGVRHGH GNPMRRAAEK
DYVTGITALG IRNVSSTTQE GYEAARAMGD DILSVRQVRK LGCDGVLARI PKGARLYVTI
DIDGFCPSIA PGTGTPSHGG FLYYEVLEIL QGVARDHEIV GIDLVEVAPD YDPSQSTAIL
AAQVLLNFLG FIFHARSQR
//
