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Database: UniProt
Entry: G6A099_9PROT
LinkDB: G6A099_9PROT
Original site: G6A099_9PROT 
ID   G6A099_9PROT            Unreviewed;       294 AA.
AC   G6A099;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:EHI48134.1};
GN   ORFNames=HIMB100_00017090 {ECO:0000313|EMBL:EHI48134.1};
OS   SAR116 cluster alpha proteobacterium HIMB100.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; SAR116 cluster.
OX   NCBI_TaxID=909943 {ECO:0000313|EMBL:EHI48134.1, ECO:0000313|Proteomes:UP000004261};
RN   [1] {ECO:0000313|EMBL:EHI48134.1, ECO:0000313|Proteomes:UP000004261}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain HIMB100 {ECO:0000313|Proteomes:UP000004261};
RX   PubMed=22675578; DOI=10.4056/sigs.1854551;
RA   Grote J., Bayindirli C., Bergauer K., Carpintero de Moraes P., Chen H.,
RA   D'Ambrosio L., Edwards B., Fernandez-Gomez B., Hamisi M., Logares R.,
RA   Nguyen D., Rii Y.M., Saeck E., Schutte C., Widner B., Church M.J.,
RA   Steward G.F., Karl D.M., Delong E.F., Eppley J.M., Schuster S.C.,
RA   Kyrpides N.C., Rappe M.S.;
RT   "Draft genome sequence of strain HIMB100, a cultured representative of the
RT   SAR116 clade of marine Alphaproteobacteria.";
RL   Stand. Genomic Sci. 5:269-278(2011).
CC   -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00742, ECO:0000256|RuleBase:RU003684}.
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:EHI48134.1}.
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DR   EMBL; AFXB01000010; EHI48134.1; -; Genomic_DNA.
DR   AlphaFoldDB; G6A099; -.
DR   STRING; 909943.HIMB100_00017090; -.
DR   PATRIC; fig|909943.3.peg.1766; -.
DR   eggNOG; COG0010; Bacteria.
DR   OrthoDB; 9788689at2; -.
DR   Proteomes; UP000004261; Unassembled WGS sequence.
DR   GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd11593; Agmatinase-like_2; 1.
DR   Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR   InterPro; IPR006035; Ureohydrolase.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   InterPro; IPR020855; Ureohydrolase_Mn_BS.
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; 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:UP000004261}.
SQ   SEQUENCE   294 AA;  31222 MW;  22B3A725808BF1DA CRC64;
     MTGPADPLLS QFLGEELSAA ENSLDQALFE VMSCGLEKTV SYGAGTAAGP AAIIAASHQL
     ERLIDGDEPC RHGVFTHPEI DTSGPIEQVL DVLRQHIAAC VGRGHIPVTL GGEHSLTYGA
     VMGMKDNLDA PFGILQIDAH ADLRAAYQGE AHSHASVMHL CSEDGIPIYQ LGVRAFCAEE
     AEARRRYNVG YRDAGELVRH QITDLTLPDD FPEQIYISFD LDGLDPSVLP ATGTPVPGGL
     GFYQALDLVS SACSGRRIVG MDVVELAPSP AHPASDFTAA LITYHLIALA AGRR
//
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