ID A0A252F3G4_9CLOT Unreviewed; 317 AA.
AC A0A252F3G4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:OUM20272.1};
GN ORFNames=CBW42_09525 {ECO:0000313|EMBL:OUM20272.1};
OS Butyricicoccus porcorum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Butyricicoccus.
OX NCBI_TaxID=1945634 {ECO:0000313|EMBL:OUM20272.1, ECO:0000313|Proteomes:UP000194903};
RN [1] {ECO:0000313|EMBL:OUM20272.1, ECO:0000313|Proteomes:UP000194903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BB10 {ECO:0000313|EMBL:OUM20272.1};
RA Trachsel J., Humphrey S., Allen H.K.;
RT "Butyricicoccus porcorum sp. nov. a butyrate-producing bacterium from the
RT swine intestinal tract.";
RL Submitted (MAY-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:OUM20272.1}.
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DR EMBL; NHOC01000007; OUM20272.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A252F3G4; -.
DR OrthoDB; 9788689at2; -.
DR Proteomes; UP000194903; 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 PRINTS; PR00116; ARGINASE.
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:UP000194903}.
SQ SEQUENCE 317 AA; 34548 MW; A22836182C488A8C CRC64;
MKYGTVNSLQ SPRFAGVKTF MRMQNIRTLD DIDFAVLGIP FDTCATYRAG ARFGPASIRE
MSSLAAKPYH PELEVDIFAQ CSGVDYGDIG SVPGYVEESF DVMQKEMKEI FARGIIPIAM
GGDHSVTLPE LRACSEVYGP VALVHFDAHY DTISEYFGKP YSHGTPFYHA AMEGLVDTAH
SIQLGIREGL YGAEDAENSA KLGYQSITAA QMHEMSGEDV IRCICARTEG KKVFLTFDID
FLDPAFAPGT GTPVPGGFST WEALKILRGL KELDIVGYDI VEVAPAFDGS GITSIAAAGI
IQEFMSLIAW RKKHGKL
//