AGMT_PYRHO
ID AGMT_PYRHO Reviewed; 283 AA.
AC O57839;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Agmatinase {ECO:0000303|PubMed:15752699};
DE EC=3.5.3.11 {ECO:0000269|PubMed:15752699};
GN OrderedLocusNames=PH0083 {ECO:0000312|EMBL:BAA29152.1};
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBUNIT.
RX PubMed=15752699; DOI=10.1016/j.bbapap.2004.12.010;
RA Goda S., Sakuraba H., Kawarabayasi Y., Ohshima T.;
RT "The first archaeal agmatinase from anaerobic hyperthermophilic archaeon
RT Pyrococcus horikoshii: cloning, expression, and characterization.";
RL Biochim. Biophys. Acta 1748:110-115(2005).
CC -!- FUNCTION: Catalyzes the formation of putrescine from agmatine. Cannot
CC use arginine. {ECO:0000269|PubMed:15752699}.
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:15752699};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:15752699};
CC Note=Binds 2 divalent metal cations per subunit (By similarity). Co(2+)
CC is the most effection cation. Can also use Ca(2+), Mn(2+), Zn(2+) or
CC Mg(2+) (PubMed:15752699). {ECO:0000250|UniProtKB:P0DJQ3,
CC ECO:0000269|PubMed:15752699};
CC -!- ACTIVITY REGULATION: Inhibited by putrescine. Activity is not affected
CC by arginine and ornithine. {ECO:0000269|PubMed:15752699}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.53 mM for agmatine {ECO:0000269|PubMed:15752699};
CC pH dependence:
CC Optimum pH is 11.0. {ECO:0000269|PubMed:15752699};
CC Temperature dependence:
CC Optimum temperature is 100 degrees Celsius.
CC {ECO:0000269|PubMed:15752699};
CC -!- PATHWAY: Amine and polyamine biosynthesis; putrescine biosynthesis via
CC agmatine pathway; putrescine from agmatine: step 1/1.
CC {ECO:0000305|PubMed:15752699}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15752699}.
CC -!- SIMILARITY: Belongs to the arginase family. Agmatinase subfamily.
CC {ECO:0000305}.
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DR EMBL; BA000001; BAA29152.1; -; Genomic_DNA.
DR PIR; A71228; A71228.
DR RefSeq; WP_010884203.1; NC_000961.1.
DR AlphaFoldDB; O57839; -.
DR SMR; O57839; -.
DR STRING; 70601.3256469; -.
DR EnsemblBacteria; BAA29152; BAA29152; BAA29152.
DR GeneID; 1443985; -.
DR KEGG; pho:PH0083; -.
DR eggNOG; arCOG01700; Archaea.
DR OMA; YELTTIM; -.
DR OrthoDB; 52310at2157; -.
DR UniPathway; UPA00534; UER00287.
DR Proteomes; UP000000752; 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 InterPro; IPR005925; Agmatinase-rel.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
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; PS51409; ARGINASE_2; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Putrescine biosynthesis.
FT CHAIN 1..283
FT /note="Agmatinase"
FT /id="PRO_0000448918"
FT BINDING 112
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0DJQ3"
FT BINDING 131
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0DJQ3"
FT BINDING 131
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0DJQ3"
FT BINDING 133
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0DJQ3"
FT BINDING 135
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0DJQ3"
FT BINDING 211
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0DJQ3"
FT BINDING 211
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0DJQ3"
FT BINDING 213
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0DJQ3"
SQ SEQUENCE 283 AA; 31445 MW; 439A2E181D113BB0 CRC64;
MLLYTYRSFD MELPTVDIKD ADYIILGLPF DGTTSYKPGA RFGPVLIRQA TLNLESYILD
YDIDIAELKI ADAGDVALPV SIEDAIKVAV ETIKEVRSIN PRALPIFLGG EHSMTYPPVK
VLEPKSYVVF DAHLDLRDSY QGSRFNHACV ARRIHEMGVK VAIFGVRSGT REEVMFASQS
GIEWVHARDY NFDAFVDLVS SLPEPVYVSI DVDVFDLPLV PETGTPEPGG LGFWEVIEAL
EWLTKRKKVA GFDIMEVSGD RLGNSTSITA AKLLFYVIGM SAR
