ID Q18F18_HALWD Unreviewed; 275 AA.
AC Q18F18;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:CAJ53446.1};
DE EC=3.5.3.11 {ECO:0000313|EMBL:CAJ53446.1};
GN Name=speB {ECO:0000313|EMBL:CAJ53446.1};
GN OrderedLocusNames=HQ_3349A {ECO:0000313|EMBL:CAJ53446.1};
OS Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=362976 {ECO:0000313|EMBL:CAJ53446.1, ECO:0000313|Proteomes:UP000001975};
RN [1] {ECO:0000313|EMBL:CAJ53446.1, ECO:0000313|Proteomes:UP000001975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16790 / HBSQ001 {ECO:0000313|Proteomes:UP000001975};
RX PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA Bolhuis H.H., Palm P.P., Wende A.W., Falb M.M., Rampp M.M.,
RA Rodriguez-Valera F.F., Pfeiffer F.F., Oesterhelt D.D.;
RT "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT limits of water activity.";
RL BMC Genomics 7:169-169(2006).
CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC {ECO:0000256|ARBA:ARBA00009227}.
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DR EMBL; AM180088; CAJ53446.1; -; Genomic_DNA.
DR RefSeq; WP_011572544.1; NC_008212.1.
DR AlphaFoldDB; Q18F18; -.
DR STRING; 362976.HQ_3349A; -.
DR GeneID; 4194705; -.
DR KEGG; hwa:HQ_3349A; -.
DR eggNOG; arCOG01700; Archaea.
DR HOGENOM; CLU_039478_0_2_2; -.
DR Proteomes; UP000001975; Chromosome.
DR GO; GO:0008783; F:agmatinase activity; IEA:UniProtKB-EC.
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:UP000001975}.
SQ SEQUENCE 275 AA; 29863 MW; D763CCB649077510 CRC64;
MFPGTRESID RDAAEYVIIG APLDVSTSFL PGTRFGPDRI RQFARPFDDY DRRTDLHFSA
CGVIDQGNVR AWDDATEYLE WLNGELTAII RDDALPVLLG GEHTITRAGV DAVMPDVFVC
LDAHLDLRQT YDGNTNSHAT VTHHISKIDT IEEILIIGAR TGTETEWERA TAADVTIVSP
TDLTAGFDVT TWIGDRSSYI SVDIDAVDPG FAPGTGTPEP GGITPQDARE TVRAAASSAV
GFDIVEVTDR DDGQTASLAG KLVRDFIYTH YAAKT
//
