ID   URE1_PROS9              Reviewed;         569 AA.
AC   Q9L644;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Urease subunit alpha {ECO:0000255|HAMAP-Rule:MF_01953};
DE            EC=3.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01953};
DE   AltName: Full=Urea amidohydrolase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01953};
GN   Name=ureC {ECO:0000255|HAMAP-Rule:MF_01953};
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_01953,
CC         ECO:0000269|PubMed:11101668};
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01953};
CC       Note=Binds 2 nickel ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01953};
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_01953}.
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_01953}.
CC   -!- PTM: Carboxylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000255|HAMAP-Rule:MF_01953}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Urease alpha subunit family. {ECO:0000255|HAMAP-Rule:MF_01953}.
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DR   EMBL; AF242489; AAF70248.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9L644; -.
DR   SMR; Q9L644; -.
DR   MEROPS; M38.982; -.
DR   UniPathway; UPA00258; UER00370.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009039; F:urease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00375; Urease_alpha; 1.
DR   Gene3D; 2.30.40.10; -; 1.
DR   HAMAP; MF_01953; Urease_alpha; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR011612; Urease_alpha_N_dom.
DR   InterPro; IPR017950; Urease_AS.
DR   InterPro; IPR005848; Urease_asu.
DR   InterPro; IPR017951; Urease_asu_c.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF00449; Urease_alpha; 1.
DR   PRINTS; PR01752; UREASE.
DR   SUPFAM; SSF51338; SSF51338; 2.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01792; urease_alph; 1.
DR   PROSITE; PS00145; UREASE_2; 1.
DR   PROSITE; PS51368; UREASE_3; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Metal-binding; Nickel.
FT   CHAIN           1..569
FT                   /note="Urease subunit alpha"
FT                   /id="PRO_0000234165"
FT   DOMAIN          131..569
FT                   /note="Urease"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   ACT_SITE        322
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         136
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         138
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         219
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         219
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         248
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         274
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         362
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   MOD_RES         219
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
SQ   SEQUENCE   569 AA;  61653 MW;  BA01CA894931C487 CRC64;
     MSYKINRKTY AQTYGPTKGD RVRLADTELI IEVEKDFTTY GDEVKFGGGK VIRDGMGQSQ
     VTREDGAVDT VITNALIVDW WGIVKADVGL KDGKIYEIGK AGNPDIQDNI NIIIGSSTEV
     IAGEGHILTA GSIDTHIHFI CPQQIETALA SGVTTMLGGG TGPATGTNAT TCTPGAFHIS
     RMIQSAEAFP VNLGFFGKGN SSNETNLFEQ VNAGACGLKL HEDWGTTPST INSCLNVADT
     LDVQVCIHTD TLNEAGFVED TIAAIAGRTI HTFHTEGAGG GHAPDIIKIC GENNVLPSST
     NPTRPYTKNT LEEHLDMLMV CHHLDSKIPE DIAFAESRIR RETIAAEDIL HDIGAFSIIA
     SDSQAMGRVG EVITRTFQTA HKMKVQRGPL PEDSDRNDNY RVKRYISKVT INPAIAHGIN
     RFVGSIEKGK IADLVLWKPS FFGVKPELVV KGGSIVWSQM GDANASIPTP GPVHGRPMFA
     NYGQSLLKSS FTFLSKNAIE LDIPNKLSLQ KNCLAVENTR SINKLDLKLN NKLPNITVDP
     QTYEVFADGV LLSCEPLEEV PMAQKYFLL