ID A0A9E8ZD71_9CYAN Unreviewed; 401 AA.
AC A0A9E8ZD71;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE SubName: Full=Agmatinase {ECO:0000313|EMBL:WAL60757.1};
DE EC=3.5.3.11 {ECO:0000313|EMBL:WAL60757.1};
GN Name=speB {ECO:0000313|EMBL:WAL60757.1};
GN ORFNames=OXH18_01800 {ECO:0000313|EMBL:WAL60757.1};
OS Thermocoleostomius sinensis A174.
OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Oculatellales;
OC Oculatellaceae; Thermocoleostomius.
OX NCBI_TaxID=2016057 {ECO:0000313|EMBL:WAL60757.1, ECO:0000313|Proteomes:UP001163152};
RN [1] {ECO:0000313|EMBL:WAL60757.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PKUAC-SCTA174 {ECO:0000313|EMBL:WAL60757.1};
RA Daroch M., Tang J., Jiang Y.;
RT "Polyphasic identification of a Novel Hot-Spring Cyanobacterium
RT Ocullathermofonsia sinensis gen nov. sp. nov. and Genomic Insights on its
RT Adaptations to the Thermal Habitat.";
RL Submitted (DEC-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC {ECO:0000256|ARBA:ARBA00009227}.
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DR EMBL; CP113797; WAL60757.1; -; Genomic_DNA.
DR RefSeq; WP_268610717.1; NZ_CP113797.1.
DR AlphaFoldDB; A0A9E8ZD71; -.
DR KEGG; tsin:OXH18_01800; -.
DR Proteomes; UP001163152; 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:0033389; P:putrescine biosynthetic process from arginine, via agmatine; IEA:TreeGrafter.
DR CDD; cd09990; Agmatinase-like; 1.
DR FunFam; 3.40.800.10:FF:000013; Agmatinase, putative; 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 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:UP001163152}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 401 AA; 44004 MW; C51415AF601133F4 CRC64;
MSANPDDTPT FQSPEVNGQV PTEAQRALDL ETRLPLTGWQ QEVSEGLEYG LEAADSIRDR
TIPTFSRGEL PHYAGINTFL KAPYLVDVRE VGKYDVAIVG VPHDSGTTYR PGTRFGPQGI
RRISALYTPY NFELGVDLRE QITLCDVGDI FTIPGNNEKS FDQISKGIAH IFSSGAFPII
LGGDHSIGFP TVRGVCRHLG DKKVGIIHFD RHVDTQETDL DERMHTCPWF HATNMANAPA
KNLVQLGIGG WQVPRQGVKV CRERATNILT VTDITEIGLD AAVEFALERA LDGTDCVYIS
FDIDCIDAGF VPGTGWPEPG GLLPREALYL LGKIVQRAPV CGLEVVEVSP PYDVSDMTAL
MATRVICDTM AHLVLSGQLP RQEKPAYINT EANMHVDMAW V
//
