ID   SPEB1_SYNY3             Reviewed;         306 AA.
AC   P72703;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Agmatinase 1;
DE            EC=3.5.3.11;
DE   AltName: Full=Agmatine ureohydrolase 1;
DE            Short=AUH 1;
GN   Name=speB1; OrderedLocusNames=sll0228;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2]
RP   FUNCTION.
RX   PubMed=10648527; DOI=10.1128/jb.182.4.1008-1015.2000;
RA   Quintero M.J., Muro-Pastor A.M., Herrero A., Flores E.;
RT   "Arginine catabolism in the cyanobacterium Synechocystis sp. strain PCC
RT   6803 involves the urea cycle and arginase pathway.";
RL   J. Bacteriol. 182:1008-1015(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=agmatine + H2O = putrescine + urea; Xref=Rhea:RHEA:13929,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:58145,
CC         ChEBI:CHEBI:326268; EC=3.5.3.11;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00742};
CC   -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00742}.
CC   -!- CAUTION: Was originally annotated as an arginase by the genome
CC       sequencing project. {ECO:0000305}.
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DR   EMBL; BA000022; BAA16710.1; -; Genomic_DNA.
DR   PIR; S74558; S74558.
DR   AlphaFoldDB; P72703; -.
DR   SMR; P72703; -.
DR   IntAct; P72703; 1.
DR   STRING; 1148.1651783; -.
DR   PaxDb; P72703; -.
DR   EnsemblBacteria; BAA16710; BAA16710; BAA16710.
DR   KEGG; syn:sll0228; -.
DR   eggNOG; COG0010; Bacteria.
DR   InParanoid; P72703; -.
DR   OMA; YELTTIM; -.
DR   PhylomeDB; P72703; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0008783; F:agmatinase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0033389; P:putrescine biosynthetic process from arginine, using agmatinase; IBA:GO_Central.
DR   InterPro; IPR005925; Agmatinase-rel.
DR   InterPro; IPR006035; Ureohydrolase.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR   PANTHER; PTHR11358; PTHR11358; 1.
DR   Pfam; PF00491; Arginase; 1.
DR   PIRSF; PIRSF036979; Arginase; 1.
DR   SUPFAM; SSF52768; SSF52768; 1.
DR   TIGRFAMs; TIGR01230; agmatinase; 1.
DR   PROSITE; PS01053; ARGINASE_1; 1.
DR   PROSITE; PS51409; ARGINASE_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Manganese; Metal-binding; Putrescine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..306
FT                   /note="Agmatinase 1"
FT                   /id="PRO_0000173744"
FT   BINDING         121
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         145
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         147
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         149
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         228
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         230
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
SQ   SEQUENCE   306 AA;  33463 MW;  114A8A313A0C4605 CRC64;
     MHSPNKFTSG PKQFLESEAI TSYADAAVVV VPIPYEATTS YRKGCEHGPE AVLEASDQLE
     AYDEELGTSP CHDLGIYTCA PLADSNKHPA LAGDAMVTEV CDGIAPFVED GKFVVAIGGE
     HAITTGVVRA MQRGTSEPFT VVQIDAHGDM RDKFEGSCHN HACVMRRVLE LGLPTLPIAI
     RAICQEEADL IREKNIPVFW AREMADNPNW INEAIASITT QKVFLTIDMD GFDPGFMPGV
     GTPEPGGLGW YEGLNFFRRL FQTKQVIGCD LMELAPVRGS VVSEFSTAKL AYKLMGYWGE
     SQRKKL