ID   URE3_PROS9              Reviewed;         100 AA.
AC   Q9L642;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Urease subunit gamma {ECO:0000255|HAMAP-Rule:MF_00739};
DE            EC=3.5.1.5 {ECO:0000255|HAMAP-Rule:MF_00739};
DE   AltName: Full=Urea amidohydrolase subunit gamma {ECO:0000255|HAMAP-Rule:MF_00739};
GN   Name=ureA {ECO:0000255|HAMAP-Rule:MF_00739};
OS   Prochlorococcus marinus subsp. pastoris (strain PCC 9511).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=100363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP   SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=11101668; DOI=10.1099/00221287-146-12-3099;
RA   Palinska K.A., Jahns T., Rippka R., Tandeau de Marsac N.;
RT   "Prochlorococcus marinus strain PCC 9511, a picoplanktonic cyanobacterium,
RT   synthesizes the smallest urease.";
RL   Microbiology 146:3099-3107(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00739,
CC         ECO:0000269|PubMed:11101668};
CC   -!- ACTIVITY REGULATION: Inhibited by HgCl2 and acetohydroxyamic acid
CC       slightly by EDTA, but not by boric acid or L-methionine-DL-sulfoximine.
CC       {ECO:0000269|PubMed:11101668}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.23 mM for urea {ECO:0000269|PubMed:11101668};
CC         Vmax=0.095 mmol/min/mg enzyme {ECO:0000269|PubMed:11101668};
CC       Temperature dependence:
CC         Optimum temperature is 55 degrees Celsius.
CC         {ECO:0000269|PubMed:11101668};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC       urea (urease route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00739}.
CC   -!- SUBUNIT: Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha)
CC       subunits. Two heterotrimers associate to form the active enzyme. In
CC       most bacteria it is thought that three heterotrimers form the active
CC       enzyme. {ECO:0000269|PubMed:11101668}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00739}.
CC   -!- SIMILARITY: Belongs to the urease gamma subunit family.
CC       {ECO:0000255|HAMAP-Rule:MF_00739}.
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DR   EMBL; AF242489; AAF70250.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9L642; -.
DR   SMR; Q9L642; -.
DR   UniPathway; UPA00258; UER00370.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR   GO; GO:0009039; F:urease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00390; Urease_gamma; 1.
DR   Gene3D; 3.30.280.10; -; 1.
DR   HAMAP; MF_00739; Urease_gamma; 1.
DR   InterPro; IPR012010; Urease_gamma.
DR   InterPro; IPR002026; Urease_gamma/gamma-beta_su.
DR   InterPro; IPR036463; Urease_gamma_sf.
DR   Pfam; PF00547; Urease_gamma; 1.
DR   PIRSF; PIRSF001223; Urease_gamma; 1.
DR   SUPFAM; SSF54111; SSF54111; 1.
DR   TIGRFAMs; TIGR00193; urease_gam; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase.
FT   CHAIN           1..100
FT                   /note="Urease subunit gamma"
FT                   /id="PRO_0000098026"
SQ   SEQUENCE   100 AA;  11173 MW;  56F3E15CC512CE73 CRC64;
     MHLSPQEKDK LLIFSAAQLA ERRLNRGLKL NYPETVAFLS FQVLEGARDG KSVSQLMSEG
     TTWLSKKQVM DGISEMVDEV QVEAVFPDGT KLVTIHNPIN