ID A0A0U5H664_9EURY Unreviewed; 272 AA.
AC A0A0U5H664;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:CQH59929.1};
DE EC=3.5.3.11 {ECO:0000313|EMBL:CQH59929.1};
GN Name=speB {ECO:0000313|EMBL:CQH59929.1};
GN ORFNames=HHUB_3090 {ECO:0000313|EMBL:CQH59929.1};
OS Halobacterium hubeiense.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=1407499 {ECO:0000313|EMBL:CQH59929.1, ECO:0000313|Proteomes:UP000066737};
RN [1] {ECO:0000313|Proteomes:UP000066737}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JI20-1 {ECO:0000313|Proteomes:UP000066737};
RX PubMed=26628271; DOI=10.1111/1462-2920.13130;
RA Jaakkola S.T., Pfeiffer F., Ravantti J.J., Guo Q., Liu Y., Chen X., Ma H.,
RA Yang C., Oksanen H.M., Bamford D.H.;
RT "The complete genome of a viable archaeum isolated from 123-million-year-
RT old rock salt.";
RL Environ. Microbiol. 18:565-579(2016).
CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC {ECO:0000256|ARBA:ARBA00009227}.
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DR EMBL; LN831302; CQH59929.1; -; Genomic_DNA.
DR RefSeq; WP_059057472.1; NZ_LN831302.1.
DR AlphaFoldDB; A0A0U5H664; -.
DR STRING; 1407499.HHUB_3090; -.
DR GeneID; 26659712; -.
DR KEGG; hhb:Hhub_3090; -.
DR OrthoDB; 7186at2157; -.
DR Proteomes; UP000066737; Chromosome I.
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 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:UP000066737}.
SQ SEQUENCE 272 AA; 29029 MW; 3E71B22FB11F7F5B CRC64;
MFPGASPVDE SADAPFDDAD YVAVGAPLDV STSFRPGARF GPDRIRKFAR TFEDFHPATG
THFSELNVTD HGDVHAWHDT AEYLEYLEGV LTDVHWADAV PVLLGGEHTV SVAGVRAADP
DVFVALDAHL DLREELGGDE LSHSTVTRHA LDVADEAVVV GARSGNEAEW ERATESDVTV
VEPGDAADWT PDFDGSVYLS VDIDAADPAY APGTGTPEPF GLDSATMRDH VRALAPQSVG
FDVVEVNDRD DGQAATLAAK LVREFVHAHA DA
//