SPEB_BACCR
ID SPEB_BACCR Reviewed; 290 AA.
AC Q814Q2;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Agmatinase;
DE EC=3.5.3.11;
DE AltName: Full=Agmatine ureohydrolase;
DE Short=AUH;
GN Name=speB; OrderedLocusNames=BC_5370;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
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}.
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DR EMBL; AE016877; AAP12232.1; -; Genomic_DNA.
DR RefSeq; NP_835031.1; NC_004722.1.
DR RefSeq; WP_001209831.1; NZ_CP034551.1.
DR AlphaFoldDB; Q814Q2; -.
DR SMR; Q814Q2; -.
DR STRING; 226900.BC_5370; -.
DR EnsemblBacteria; AAP12232; AAP12232; BC_5370.
DR GeneID; 59156862; -.
DR GeneID; 64200606; -.
DR GeneID; 67509996; -.
DR KEGG; bce:BC5370; -.
DR PATRIC; fig|226900.8.peg.5545; -.
DR HOGENOM; CLU_039478_0_2_9; -.
DR OMA; YELTTIM; -.
DR UniPathway; UPA00534; UER00287.
DR Proteomes; UP000001417; 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 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..290
FT /note="Agmatinase"
FT /id="PRO_0000173726"
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 290 AA; 32389 MW; D538E9EBDE734B5B CRC64;
MRFDEAYSGK VFIKSHPSFE ESKVVIYGMP MDWTVSYRPG SRFGPARIRE VSIGLEEYSP
YLDRELEEVK YFDAGDIPLP FGNAQRSLDM IEEYVSKLLD ADKFPLGLGG EHLVSWPIFK
AMAKKYPDLA IIHMDAHTDL RESYEGEPLS HSTPIRKVCD LIGPENVYSF GIRSGMKEEF
EWAKEVGMNL YKFDVLEPLK EVLPKLAGRP VYVTIDIDVL DPAHAPGTGT LEAGGITSKE
LLDSIVAIAN SNINVVGADL VEVAPVYDHS DQTPVAASKF VREMLLGWVK