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Database: UniProt
Entry: R9GXG5_9SPHI
LinkDB: R9GXG5_9SPHI
Original site: R9GXG5_9SPHI 
ID   R9GXG5_9SPHI            Unreviewed;       293 AA.
AC   R9GXG5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:EOR96368.1};
DE            EC=3.5.3.11 {ECO:0000313|EMBL:EOR96368.1};
GN   ORFNames=ADIARSV_0445 {ECO:0000313|EMBL:EOR96368.1};
OS   Arcticibacter svalbardensis MN12-7.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Arcticibacter.
OX   NCBI_TaxID=1150600 {ECO:0000313|EMBL:EOR96368.1, ECO:0000313|Proteomes:UP000014174};
RN   [1] {ECO:0000313|EMBL:EOR96368.1, ECO:0000313|Proteomes:UP000014174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MN12-7 {ECO:0000313|EMBL:EOR96368.1,
RC   ECO:0000313|Proteomes:UP000014174};
RX   PubMed=23846277;
RA   Shivaji S., Ara S., Prasad S., Manasa B.P., Begum Z., Singh A.,
RA   Kumar Pinnaka A.;
RT   "Draft Genome Sequence of Arcticibacter svalbardensis Strain MN12-7T, a
RT   Member of the Family Sphingobacteriaceae Isolated from an Arctic Soil
RT   Sample.";
RL   Genome Announc. 1:E00484-13(2013).
CC   -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC       {ECO:0000256|ARBA:ARBA00009227}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EOR96368.1}.
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DR   EMBL; AQPN01000017; EOR96368.1; -; Genomic_DNA.
DR   RefSeq; WP_016193694.1; NZ_AQPN01000017.1.
DR   AlphaFoldDB; R9GXG5; -.
DR   STRING; 1150600.ADIARSV_0445; -.
DR   PATRIC; fig|1150600.3.peg.436; -.
DR   eggNOG; COG0010; Bacteria.
DR   OrthoDB; 9788689at2; -.
DR   Proteomes; UP000014174; Unassembled WGS sequence.
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   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, ECO:0000313|EMBL:EOR96368.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014174}.
SQ   SEQUENCE   293 AA;  32520 MW;  545B6ADB6CA7DA98 CRC64;
     MKATTDYHFL GLQDLSLHAY ESSKVVIQQI PYEHTSSYIT GSEDGPAAIV KASEFVECYD
     EEIDTEISER IGINTVAPLV FGSLVNADAL SLIEEATAEL LKDGKFVVSF GAEHTATYGI
     VKAFAKKYKN LSILQLDAHS DLRQSYMGNK LSHACVMARI HDMGLTICQA GVRALSREEA
     DLIKKSEDIN TFYAHQIRRN PLWMEEIIAP LSNDVYITID ADGFDPSIMP GVGTAEPNGL
     LWTETLQLLR RVCKERNVVG FDIVECVPIK GSIISEYTLA KLAYKLLGYR FIS
//
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