ID A0A238LEW8_9RHOB Unreviewed; 318 AA.
AC A0A238LEW8;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 02-APR-2025, entry version 24.
DE SubName: Full=Guanidinobutyrase {ECO:0000313|EMBL:SMY08257.1};
DE EC=3.5.3.7 {ECO:0000313|EMBL:SMY08257.1};
GN Name=gbh {ECO:0000313|EMBL:SMY08257.1};
GN ORFNames=LOM8899_02407 {ECO:0000313|EMBL:SMY08257.1};
OS Flavimaricola marinus.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Paracoccaceae; Flavimaricola.
OX NCBI_TaxID=1819565 {ECO:0000313|EMBL:SMY08257.1, ECO:0000313|Proteomes:UP000201613};
RN [1] {ECO:0000313|Proteomes:UP000201613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8899 {ECO:0000313|Proteomes:UP000201613};
RA Rodrigo-Torres L., Arahal R. D., Lucena T.;
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR036979-1};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000256|PIRSR:PIRSR036979-1};
CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC {ECO:0000256|ARBA:ARBA00009227}.
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DR EMBL; FXZK01000004; SMY08257.1; -; Genomic_DNA.
DR RefSeq; WP_093992454.1; NZ_FXZK01000004.1.
DR AlphaFoldDB; A0A238LEW8; -.
DR OrthoDB; 9788689at2; -.
DR Proteomes; UP000201613; Unassembled WGS sequence.
DR GO; GO:0008783; F:agmatinase activity; IEA:TreeGrafter.
DR GO; GO:0047971; F:guanidinobutyrase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033389; P:putrescine biosynthetic process from arginine, via agmatine; IEA:TreeGrafter.
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; ARGINASE/AGMATINASE; 1.
DR PANTHER; PTHR11358:SF26; GUANIDINO ACID HYDROLASE, MITOCHONDRIAL; 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 Manganese {ECO:0000256|PIRSR:PIRSR036979-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036979-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000201613}.
FT BINDING 130
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT BINDING 152
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT BINDING 154
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT BINDING 156
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT BINDING 244
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
FT BINDING 246
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR036979-1"
SQ SEQUENCE 318 AA; 34358 MW; 559037BAB3AD5664 CRC64;
MADSYFQPIS GFDLPRFAGV PTFMRLPHVP LDSPRISEVD IGLIGTPWDG GTTNRPGPRH
GPRQLRDMST MIRAQNGATG VRPFEAMNCA DLGDVGPNPA DLMDSMTRIT AFYDQVVAAK
IKPLTAGGDH LCSLPILRAL GKAVPLGMIH FDSHTDLFHS YFNGTMFTHG TPFRRAIEEG
LLDPRKVIQI GIRGTAYDFE DRDFAEAVGV TIIPIEEFHA RGVLDVMAQA RELVGDMPTY
VTYDIDFVDP AFAPGTGTPE VGGPNSYQAL QCARELAGVN IVGADLVEVS PPFDQSGATA
FLGVSLMFEM LCNMVPAA
//
