ID   A0A2N5GZZ4_9BACI        Unreviewed;       290 AA.
AC   A0A2N5GZZ4;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Agmatinase {ECO:0000313|EMBL:PLR96588.1};
GN   Name=speB {ECO:0000313|EMBL:PLR96588.1};
GN   ORFNames=CVD19_11415 {ECO:0000313|EMBL:PLR96588.1};
OS   Bacillus sp. T33-2.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2054168 {ECO:0000313|EMBL:PLR96588.1, ECO:0000313|Proteomes:UP000235118};
RN   [1] {ECO:0000313|EMBL:PLR96588.1, ECO:0000313|Proteomes:UP000235118}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T33-2 {ECO:0000313|EMBL:PLR96588.1,
RC   ECO:0000313|Proteomes:UP000235118};
RA   Seuylemezian A., Cooper K., Vaishampayan P.;
RT   "Comparitive Functional Genomics of Dry Heat Resistant strains isolated
RT   from the Viking Spacecraft.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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:PLR96588.1}.
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DR   EMBL; PGVB01000013; PLR96588.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N5GZZ4; -.
DR   OrthoDB; 9788689at2; -.
DR   Proteomes; UP000235118; 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   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:UP000235118}.
SQ   SEQUENCE   290 AA;  32412 MW;  A434870A91129F87 CRC64;
     MRFDEAYSGN VFIRSHSNYM ESRAVLYGMP MDWTVSYRPG SRFGPTRIRE VSLGLEEYSP
     YLDRELEEIK YFDAGDIPLP FGNAQRSLDM IEEFVDKILA ADKFPLGMGG EHLVSWPVMK
     AVAKKYKDLA IIHMDAHADL REHYEGEPLS HSTPIRKIAG LIGPENVYSF GIRSGMKEEF
     DWAKQAGMHI SKFEVLEPLK EVLPKLAGRP VYVTIDIDVL DPAHAPGTGT VDAGGITSRE
     LLASIHEIAR SEVNVVGADL VEVAPIYDQS EQTANTASKL IREMLLGWVK
//