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SPEB_ALKHC
ID   SPEB_ALKHC              Reviewed;         289 AA.
AC   Q9K6B9;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Agmatinase;
DE            EC=3.5.3.11;
DE   AltName: Full=Agmatine ureohydrolase;
DE            Short=AUH;
GN   Name=speB; OrderedLocusNames=BH3810;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
CC   -!- FUNCTION: Catalyzes the formation of putrescine from agmatine.
CC       {ECO:0000250}.
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   -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC       agmatine pathway; putrescine from agmatine: step 1/1.
CC   -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00742}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB07529.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; BA000004; BAB07529.1; ALT_FRAME; Genomic_DNA.
DR   PIR; B84126; B84126.
DR   AlphaFoldDB; Q9K6B9; -.
DR   SMR; Q9K6B9; -.
DR   STRING; 272558.10176435; -.
DR   EnsemblBacteria; BAB07529; BAB07529; BAB07529.
DR   KEGG; bha:BH3810; -.
DR   eggNOG; COG0010; Bacteria.
DR   HOGENOM; CLU_3040414_0_0_9; -.
DR   OMA; YELTTIM; -.
DR   UniPathway; UPA00534; UER00287.
DR   Proteomes; UP000001258; 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:0033388; P:putrescine biosynthetic process from arginine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-KW.
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; Polyamine biosynthesis;
KW   Putrescine biosynthesis; Reference proteome; Spermidine biosynthesis.
FT   CHAIN           1..289
FT                   /note="Agmatinase"
FT                   /id="PRO_0000173727"
FT   BINDING         112
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         135
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         137
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         139
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         216
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT   BINDING         218
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
SQ   SEQUENCE   289 AA;  32155 MW;  2F8B0C4CA4EB4B89 CRC64;
     MRFDEAYSGK VFIMSRSNYE KSKAVIFGMP MDWTVSFRPS SRFGPNRIRE ASLGLEEYSP
     YMDKHLEEVA YFDAGDMLLP FGNPQRSLEM IESYVDKLLA DQKMPIGLGG EHLVSWPIFK
     AMHKIYPDMA IIHIDAHADL REEYEGEPLS HSTPIRKACS LIGPENVYSF GIRSGMREEF
     QYAKDSGMYM AKFEVATPLK EVLPKLAGRN VYVTIDIDVL DPAFAPGTGT AEAGGISSKE
     LLEAIVAIAH SDVNVIGADL VEVAPAYDPS EKTPIAASKF VREMLLGWV
 
 
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