SPEB_METJA
ID SPEB_METJA Reviewed; 284 AA.
AC Q57757;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Agmatinase {ECO:0000303|PubMed:22439800};
DE EC=3.5.3.11 {ECO:0000269|PubMed:22439800};
GN Name=speB; OrderedLocusNames=MJ0309;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF CYS-71; CYS-136;
RP CYS-151 AND CYS-229.
RX PubMed=22439800; DOI=10.1021/bi300039f;
RA Miller D., Xu H., White R.H.;
RT "A new subfamily of agmatinases present in methanogenic Archaea is Fe(II)
RT dependent.";
RL Biochemistry 51:3067-3078(2012).
CC -!- FUNCTION: Catalyzes the formation of putrescine from agmatine.
CC {ECO:0000269|PubMed:22439800}.
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 Evidence={ECO:0000269|PubMed:22439800};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:22439800};
CC Note=Binds 2 Fe(2+) ions per subunit. Can also use Mn(2+), with lower
CC efficiency. {ECO:0000269|PubMed:22439800};
CC -!- ACTIVITY REGULATION: Inhibited by putrescine and by the substrate
CC analog arginine. Inactive when the purified enzyme is incubated with
CC dithiothreitol followed by excess iodoacetic acid or N-ethylmaleimide.
CC {ECO:0000269|PubMed:22439800}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.4 mM for agmatine {ECO:0000269|PubMed:22439800};
CC Note=kcat is 0.032 sec(-1). {ECO:0000269|PubMed:22439800};
CC -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC agmatine pathway; putrescine from agmatine: step 1/1. {ECO:0000305}.
CC -!- SUBUNIT: Forms multimers. {ECO:0000269|PubMed:22439800}.
CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L77117; AAB98295.1; -; Genomic_DNA.
DR PIR; F64338; F64338.
DR RefSeq; WP_010869807.1; NC_000909.1.
DR AlphaFoldDB; Q57757; -.
DR SMR; Q57757; -.
DR STRING; 243232.MJ_0309; -.
DR EnsemblBacteria; AAB98295; AAB98295; MJ_0309.
DR GeneID; 1451164; -.
DR KEGG; mja:MJ_0309; -.
DR eggNOG; arCOG01700; Archaea.
DR HOGENOM; CLU_039478_0_2_2; -.
DR InParanoid; Q57757; -.
DR OMA; YELTTIM; -.
DR OrthoDB; 52310at2157; -.
DR PhylomeDB; Q57757; -.
DR BRENDA; 3.5.3.11; 3260.
DR UniPathway; UPA00534; UER00287.
DR Proteomes; UP000000805; 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 PRINTS; PR00116; ARGINASE.
DR SUPFAM; SSF52768; SSF52768; 1.
DR TIGRFAMs; TIGR01230; agmatinase; 1.
DR PROSITE; PS01053; ARGINASE_1; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Iron; Metal-binding; Putrescine biosynthesis;
KW Reference proteome.
FT CHAIN 1..284
FT /note="Agmatinase"
FT /id="PRO_0000173784"
FT BINDING 71
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:22439800"
FT BINDING 110
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:22439800"
FT BINDING 133
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:22439800"
FT BINDING 133
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:22439800"
FT BINDING 135
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:22439800"
FT BINDING 137
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:22439800"
FT BINDING 151
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:22439800"
FT BINDING 211
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:22439800"
FT BINDING 211
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:22439800"
FT BINDING 213
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000305|PubMed:22439800"
FT MUTAGEN 71
FT /note="C->S: 24% of wild-type activity in the presence of
FT DTT."
FT /evidence="ECO:0000269|PubMed:22439800"
FT MUTAGEN 136
FT /note="C->A: 89% of wild-type activity in the presence of
FT DTT."
FT /evidence="ECO:0000269|PubMed:22439800"
FT MUTAGEN 151
FT /note="C->S: 5% of wild-type activity in the presence of
FT DTT."
FT /evidence="ECO:0000269|PubMed:22439800"
FT MUTAGEN 229
FT /note="C->A: 96% of wild-type activity in the presence of
FT DTT."
FT /evidence="ECO:0000269|PubMed:22439800"
SQ SEQUENCE 284 AA; 32477 MW; 0F76B94B1562236E CRC64;
MEEHFIDLSK FMMANCPYEE AEGVIFSIPY DETTSFKPGA REGGNAIRTA SWGLETYSPI
LDRDLAELKY CDLKDLDLYG SQEEIFGTIH SVSREILKEN KKIIVFGGEH SITYPIIKAV
KDIYDDFIVI QFDAHCDLRD EYLGNKLSHA CVMRRVYELT KNIFQFGIRS GDKEEWDLAR
KNNLYLKMDL MNKDDLEYIK SLDKPIYVTI DIDVLDPAYA PGTGTPEPCG FSTRELFNSL
YLLEEVKDKI IGFDIVEVSP IYDIANITAI TAAKIARELM LMIL
