ID A0A1Y3TDP7_9FIRM Unreviewed; 289 AA.
AC A0A1Y3TDP7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:OUN34473.1};
GN ORFNames=B5G27_06865 {ECO:0000313|EMBL:OUN34473.1};
OS Lachnoclostridium sp. An76.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1965654 {ECO:0000313|EMBL:OUN34473.1, ECO:0000313|Proteomes:UP000199802};
RN [1] {ECO:0000313|Proteomes:UP000199802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000199802};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUN34473.1}.
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DR EMBL; NFHL01000003; OUN34473.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3TDP7; -.
DR OrthoDB; 9788689at2; -.
DR Proteomes; UP000199802; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000199802}.
SQ SEQUENCE 289 AA; 31503 MW; F47265740D67646B CRC64;
MQKNIVNFIG CDAGYDEADV VIFGAPFDST TSFRPGTRFA GAAIRGDSYG LEIYSPYQDK
ELTEGRVYDL GDLELAIGSS ERVLGQIEEC AAGIFADGKL PFMIGGEHLV TLGSVRAAVK
KYPDMHILHF DAHTDLREDY LGVELSHACV IRRCWELVGD GRIHQFGIRS GEKYEFDWAK
SGHTDFHPFS LEGLGEVLAE LGDVPVYFTV DLDVMDPSVF PGTGTPEPGG VDFLTAMRAV
TEVCEKVNLI GCDVNELCPP CDPTGASTAA ACKIIREMLI AVVNRDRKP
//
