ID L8JIG1_9GAMM Unreviewed; 308 AA.
AC L8JIG1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:ELR67227.1};
GN ORFNames=C942_02736 {ECO:0000313|EMBL:ELR67227.1};
OS Photobacterium marinum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=1056511 {ECO:0000313|EMBL:ELR67227.1, ECO:0000313|Proteomes:UP000011134};
RN [1] {ECO:0000313|EMBL:ELR67227.1, ECO:0000313|Proteomes:UP000011134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK15 {ECO:0000313|EMBL:ELR67227.1,
RC ECO:0000313|Proteomes:UP000011134};
RA Khatri I., Vaidya B., Srinivas T.N.R., Subramanian S., Pinnaka A.;
RT "Genome Assembly of Photobacterium sp. AK15.";
RL Submitted (DEC-2012) 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:ELR67227.1}.
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DR EMBL; AMZO01000003; ELR67227.1; -; Genomic_DNA.
DR RefSeq; WP_007462673.1; NZ_AMZO01000003.1.
DR AlphaFoldDB; L8JIG1; -.
DR PATRIC; fig|1056511.3.peg.798; -.
DR OrthoDB; 9789727at2; -.
DR Proteomes; UP000011134; 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 308 AA; 33875 MW; A04FB8F84774FF76 CRC64;
MQDLFSKTDY SLYSNAMTFL RRPLVSNPLV SEADVVVLGV PLDLATSGRS GARMGPDAIR
RASVNLAWEG KKYPWEYNLF ERRTVVDAGD LVFDLGDAED LTTRLEAAVS AIINQGKTTL
CFGGDHFITL PILRAHAKHY GKMALVHFDA HTDTYSNGSR YDHGTMFYHA PNEGLVSADH
SVQVGIRTEY DVPDHRFNVI DAMQANNMSA EEIAAQIRQT VGNRPVYLTF DIDCLDPAYA
PGTGTPVCGG LTSDKVLKII RQLQGINVVG MDVVEVAPAY DHGEITALAA ATIAYELLYL
WSENPYLK
//
