URE1_UREUR
ID URE1_UREUR Reviewed; 598 AA.
AC P0CB00; P17272; Q56554; Q9R417;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 46.
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}; Synonyms=ureA;
OS Ureaplasma urealyticum (Ureaplasma urealyticum biotype 2).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=2130;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27618 / CIP 103755 / NCTC 10177 / T960 / Serovar 8;
RX PubMed=2191184; DOI=10.1111/j.1365-2958.1990.tb00636.x;
RA Blanchard A.;
RT "Ureaplasma urealyticum urease genes; use of a UGA tryptophan codon.";
RL Mol. Microbiol. 4:669-676(1990).
RN [2]
RP SEQUENCE REVISION TO 274-289.
RA Blanchard A.;
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27618 / CIP 103755 / NCTC 10177 / T960 / Serovar 8,
RC ATCC 27814 / 23 / Serovar 2, ATCC 27816 / 58 / Serovar 4,
RC ATCC 27817 / 354 / Serovar 5, ATCC 27819 / Co / Serovar 7,
RC ATCC 33175 / Vancouver / Serovar 9, ATCC 33695 / K2 / Serovar 11,
RC ATCC 33696 / U24 / Serovar 12, and ATCC 33698 / U38 / Serovar 13;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135.
RC STRAIN=ATCC 27618 / CIP 103755 / NCTC 10177 / T960 / Serovar 8,
RC ATCC 27814 / 23 / Serovar 2, ATCC 27816 / 58 / Serovar 4,
RC ATCC 27817 / 354 / Serovar 5, ATCC 27819 / Co / Serovar 7,
RC ATCC 33175 / Vancouver / Serovar 9, ATCC 33695 / K2 / Serovar 11,
RC ATCC 33696 / U24 / Serovar 12, and ATCC 33698 / U38 / Serovar 13;
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41, AND PROTEIN SEQUENCE OF 1-36.
RC STRAIN=ATCC 27618 / CIP 103755 / NCTC 10177 / T960 / Serovar 8;
RX PubMed=2050410; DOI=10.1128/iai.59.7.2463-2469.1991;
RA Willoughby J.J., Russell W.C., Thirkell D., Burdon M.G.;
RT "Isolation and detection of urease genes in Ureaplasma urealyticum.";
RL Infect. Immun. 59:2463-2469(1991).
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; X51315; CAA35697.1; -; Genomic_DNA.
DR EMBL; AF085720; AAD28106.2; -; Genomic_DNA.
DR EMBL; AF085721; AAD28109.2; -; Genomic_DNA.
DR EMBL; AF085722; AAD28112.2; -; Genomic_DNA.
DR EMBL; AF085723; AAD28115.2; -; Genomic_DNA.
DR EMBL; AF085724; AAD28118.2; -; Genomic_DNA.
DR EMBL; AF085725; AAD28121.2; -; Genomic_DNA.
DR EMBL; AF085727; AAD28127.2; -; Genomic_DNA.
DR EMBL; AF085728; AAD28130.2; -; Genomic_DNA.
DR EMBL; AF085729; AAD28133.2; -; Genomic_DNA.
DR EMBL; M36190; AAA79777.1; -; Genomic_DNA.
DR PIR; S10032; S10032.
DR RefSeq; WP_004025654.1; NZ_QOKT01000007.1.
DR AlphaFoldDB; P0CB00; -.
DR SMR; P0CB00; -.
DR GeneID; 45016020; -.
DR OMA; GFDSHIH; -.
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 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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Metal-binding; Nickel.
FT CHAIN 1..598
FT /note="Urease subunit alpha"
FT /id="PRO_0000067564"
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"
FT CONFLICT 29
FT /note="W -> E (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="K -> I (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="D -> DP (in Ref. 1; CAA35697)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="W -> R (in Ref. 1; CAA35697)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="A -> T (in Ref. 1; CAA35697)"
FT /evidence="ECO:0000305"
FT CONFLICT 181..187
FT /note="KFWVKSA -> NSELIC (in Ref. 1; CAA35697)"
FT /evidence="ECO:0000305"
FT CONFLICT 231..232
FT /note="TG -> NR (in Ref. 1; CAA35697)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="G -> E (in Ref. 1; CAA35697)"
FT /evidence="ECO:0000305"
FT CONFLICT 403..406
FT /note="NNRV -> KQPC (in Ref. 1; CAA35697)"
FT /evidence="ECO:0000305"
FT CONFLICT 582..598
FT /note="DAEPLTEAPLAQRYFLF -> ACRTSNRSSISTKILLILILELFWFSNSISN
FT YI (in Ref. 1; CAA35697)"
FT /evidence="ECO:0000305"
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
