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URE1_UREU1
ID   URE1_UREU1              Reviewed;         598 AA.
AC   B5ZBS9; P17272; Q56554; Q9R417;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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}; OrderedLocusNames=UUR10_0477;
OS   Ureaplasma urealyticum serovar 10 (strain ATCC 33699 / Western).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX   NCBI_TaxID=565575;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15388749; DOI=10.1099/ijs.0.63073-0;
RA   Kong F., Gilbert G.L.;
RT   "Postgenomic taxonomy of human ureaplasmas - a case study based on multiple
RT   gene sequences.";
RL   Int. J. Syst. Evol. Microbiol. 54:1815-1821(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33699 / Western;
RA   Shrivastava S., Methe B.A., Glass J., White K., Duffy L.B.;
RT   "Genome sequence of Ureaplasma urealyticum serovar 10 ATCC-33699.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135.
RX   PubMed=10555372; DOI=10.1099/00207713-49-4-1879;
RA   Kong F., James G., Ma Z., Gordon S., Wang B., Gilbert G.L.;
RT   "Phylogenetic analysis of Ureaplasma urealyticum -- support for the
RT   establishment of a new species, Ureaplasma parvum.";
RL   Int. J. Syst. Bacteriol. 49:1879-1889(1999).
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   -!- 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   -!- 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. Three heterotrimers associate to form the active enzyme.
CC       {ECO:0000255|HAMAP-Rule:MF_01953}.
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; AF085726; AAD28124.2; -; Genomic_DNA.
DR   EMBL; CP001184; ACI59907.1; -; Genomic_DNA.
DR   RefSeq; WP_004025654.1; NC_011374.1.
DR   AlphaFoldDB; B5ZBS9; -.
DR   SMR; B5ZBS9; -.
DR   STRING; 565575.UUR10_0477; -.
DR   EnsemblBacteria; ACI59907; ACI59907; UUR10_0477.
DR   GeneID; 45016020; -.
DR   KEGG; uue:UUR10_0477; -.
DR   eggNOG; COG0804; Bacteria.
DR   HOGENOM; CLU_000980_0_0_14; -.
DR   OMA; GFDSHIH; -.
DR   OrthoDB; 157757at2; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000002018; Chromosome.
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   InterPro; IPR029754; Urease_Ni-bd.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF00449; Urease_alpha; 1.
DR   PRINTS; PR01752; UREASE.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01792; urease_alph; 1.
DR   PROSITE; PS01120; UREASE_1; 1.
DR   PROSITE; PS00145; UREASE_2; 1.
DR   PROSITE; PS51368; UREASE_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Metal-binding; Nickel.
FT   CHAIN           1..598
FT                   /note="Urease subunit alpha"
FT                   /id="PRO_1000188896"
FT   DOMAIN          136..598
FT                   /note="Urease"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   ACT_SITE        326
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         141
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         143
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         223
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         223
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         225
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         252
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         278
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         366
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         223
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
SQ   SEQUENCE   598 AA;  64491 MW;  1BF5DB65636CBDB0 CRC64;
     MFKISRKNYS DLYGITTGDS VRLGDTNLWV KVEKDLTTYG EESVFGGGKT LREGMGMNST
     MKLDDKLGNA EVMDLVITNA LILDYTGIYK ADIGIKNGKI ASIGKSGNPH LTDGVDMVVG
     ISTEVSAGEG KIYTAGGLDT HVHWLEPEIV PVALDGGITT VIAGGTGMND GTKATTVSPG
     KFWVKSALQA ADGLPINAGF LAKGQGMEDP IFEQIVAGAC GLKIHEDWGA TGNAIDLALT
     VAEKTDVAVA IHTDTLNEAG FVEHTIAAMK GRTIHAYHTE GAGGGHAPDI LESVKYAHIL
     PASTNPTIPY TVNTIAEHLD MLMVCHHLNP KVPEDVAFAD SRIRSQTIAA EDLLHDMGAI
     SIMSSDTLAM GRIGEVVTRS WQMAHKMKAQ FGALKGDSEF NDNNRVKRYV AKYTINPAIA
     HGIDSYVGSI EVGKLADIVA WEPKFFGAKP YYVVKMGVIA RCVAGDPNAS IPTCEPVIMR
     DQFGTYGRSL TSTSVSFVSK IGLENGIKEE YKLEKELLPV KNCRSINKKS MKWNSATPNL
     EVDPQTFDAA VDYNDLENWL EQPAAELAKK LKKTANGKYV LDAEPLTEAP LAQRYFLF
 
 
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