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