ID M1WUW3_PSEP2 Unreviewed; 284 AA.
AC M1WUW3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:CCH47923.1};
GN OrderedLocusNames=BN4_10686 {ECO:0000313|EMBL:CCH47923.1};
OS Pseudodesulfovibrio piezophilus (strain DSM 21447 / JCM 15486 / C1TLV30)
OS (Desulfovibrio piezophilus).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae.
OX NCBI_TaxID=1322246 {ECO:0000313|EMBL:CCH47923.1, ECO:0000313|Proteomes:UP000011724};
RN [1] {ECO:0000313|EMBL:CCH47923.1, ECO:0000313|Proteomes:UP000011724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011724};
RX PubMed=23383081; DOI=10.1371/journal.pone.0055130;
RA Pradel N., Ji B., Gimenez G., Talla E., Lenoble P., Garel M., Tamburini C.,
RA Fourquet P., Lebrun R., Bertin P., Denis Y., Pophillat M., Barbe V.,
RA Ollivier B., Dolla A.;
RT "The first genomic and proteomic characterization of a deep-sea sulfate
RT reducer: insights into the piezophilic lifestyle of Desulfovibrio
RT piezophilus.";
RL PLoS ONE 8:e55130-e55130(2013).
RN [2] {ECO:0000313|Proteomes:UP000011724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011724};
RX PubMed=23961312; DOI=10.4056/sigs.3777412;
RA Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M., Amann R.,
RA Schreiber L.;
RT "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT deltaproteobacterium specialized in disproportionating inorganic sulfur
RT compounds.";
RL Stand. Genomic Sci. 8:58-68(2013).
CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC {ECO:0000256|ARBA:ARBA00009227}.
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DR EMBL; FO203427; CCH47923.1; -; Genomic_DNA.
DR RefSeq; WP_015413977.1; NC_020409.1.
DR AlphaFoldDB; M1WUW3; -.
DR STRING; 1322246.BN4_10686; -.
DR KEGG; dpi:BN4_10686; -.
DR PATRIC; fig|879567.3.peg.709; -.
DR eggNOG; COG0010; Bacteria.
DR HOGENOM; CLU_039478_0_2_7; -.
DR OrthoDB; 9789727at2; -.
DR BioCyc; DPIE1322246:BN4_RS03525-MONOMER; -.
DR Proteomes; UP000011724; Chromosome.
DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:UniProt.
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 NCBIfam; TIGR01230; agmatinase; 1.
DR PANTHER; PTHR11358:SF44; AGMATINASE 1; 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; PS51409; ARGINASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000011724}.
SQ SEQUENCE 284 AA; 30788 MW; D75C3F46AEA95A1A CRC64;
MASHFLAGEI QNAKPENATF HVIPVPLEAS VSYGAGTAAG PEGILTASRQ LELWDGTSVP
ANFGIHTADP VDCSGKIAKT LDRIEDAVAY ALECEAMPLV LGGEHTVTLG ALRGMKQARR
KFGVVQFDAH ADLRDTYEGS PYSHACVMRR ATEDLNIPVF QIGVRALCEE EAVYRQKNEI
PHLDARQLHL KGIPTHILPS DFPDRIYISF DVDGLDPSVI RSTGTPVPGG LNWHNTLTLL
ERILENRTLI GADVVELAPQ SGDHASDFAA AQLVYTLLGL YETP
//
