URE1_UREPA
ID URE1_UREPA Reviewed; 598 AA.
AC P0C7K7; Q60058; Q9PQ56; Q9R3U4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=UU432;
OS Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=273119;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27813 / 7 / Serovar 1;
RX PubMed=8550495; DOI=10.1128/jb.178.3.647-655.1996;
RA Neyrolles O., Ferris S., Behbahani N., Montagnier L., Blanchard A.;
RT "Organization of Ureaplasma urealyticum urease gene cluster and expression
RT in a suppressor strain of Escherichia coli.";
RL J. Bacteriol. 178:647-655(1996).
RN [2]
RP ERRATUM OF PUBMED:8550495.
RX PubMed=8626347; DOI=10.1128/jb.178.9.2725-2725.1996;
RA Neyrolles O., Ferris S., Behbahani N., Montagnier L., Blanchard A.;
RL J. Bacteriol. 178:2725-2725(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700970;
RX PubMed=11048724; DOI=10.1038/35037619;
RA Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA Cassell G.H.;
RT "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL Nature 407:757-762(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kong F., Gilbert G.L.;
RT "Phylogenetic study of Ureaplasma parvum and Ureaplasma urealyticum.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135.
RC STRAIN=ATCC 27813 / 7 / Serovar 1, ATCC 27818 / Pi / Serovar 6, and
RC ATCC 33697 / U26 / Serovar 14;
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; L40489; AAA89189.2; -; Genomic_DNA.
DR EMBL; AF222894; AAF30844.1; -; Genomic_DNA.
DR EMBL; AF085730; AAD28136.2; -; Genomic_DNA.
DR EMBL; AF085731; AAD28139.2; -; Genomic_DNA.
DR EMBL; AF085733; AAD28145.2; -; Genomic_DNA.
DR PIR; G82890; G82890.
DR RefSeq; WP_006688455.1; NC_002162.1.
DR AlphaFoldDB; P0C7K7; -.
DR SMR; P0C7K7; -.
DR STRING; 273119.UU432; -.
DR MEROPS; M38.982; -.
DR EnsemblBacteria; AAF30844; AAF30844; UU432.
DR GeneID; 29672358; -.
DR KEGG; uur:UU432; -.
DR eggNOG; COG0804; Bacteria.
DR HOGENOM; CLU_000980_0_0_14; -.
DR OMA; GFDSHIH; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000000423; 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; Reference proteome.
FT CHAIN 1..598
FT /note="Urease subunit alpha"
FT /id="PRO_0000067563"
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 100
FT /note="I -> L (in Ref. 1; AAA89189)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="K -> N (in Ref. 4; AAD28136/AAD28139)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="H -> A (in Ref. 1; AAA89189)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 598 AA; 64545 MW; 5760DA36AC021424 CRC64;
MFKISRKNYS DLYGITTGDS VRLGDTNLWV KVEKDLTTYG EESVFGGGKT LREGMGMNST
MKLDDKLGNA EVMDLVITNA LIVDYTGIYK ADIGIKNGKI AAIGKSGNPH LTDNVDMIVG
ISTEISAGEG KIYTAGGLDT HVHWLEPEIV PVALDGGITT VIAGGTGMND GTKATTVSPG
KFWVKSALQA ADGLSINAGF LAKGQGMEDP IFEQIAAGAC GLKIHEDWGA TGNAIDLALT
VADKTDVAVA IHTDTLNEAG FVEHTIAAMK GRTIHAYHTE GAGGGHAPDI LETVKYAHIL
PASTNPTIPY TVNTIAEHLD MLMVCHHLNP KVPEDVAFAD SRIRSQTIAA EDLLHDMGAI
SIMSSDTLAM GRIGEVATRT WQMAHKMKAQ FGSLKGDSEF SDNNRVKRYI SKYTINPAIA
HGVDSYIGSL EVGKLADIVA WEPKFFGAKP YYVVKMGVIA RCVAGDPNAS IPTCEPVIMR
DQFGTYGRLL TNTSVSFVSK IGLENGIKEE YKLEKELLPV KNCRSVNKKS MKWNSATPNL
EVDPQTFDAA VDFNDLENWL EQSASELAKK LKKTSSGKYI LDAEPLTEAP LAQRYFLF
