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URE11_BRUAB
ID   URE11_BRUAB             Reviewed;         570 AA.
AC   Q93T81; Q57F85;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Urease subunit alpha 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01953};
GN   Name=ureC1 {ECO:0000255|HAMAP-Rule:MF_01953};
GN   OrderedLocusNames=BruAb1_0296;
OS   Brucella abortus biovar 1 (strain 9-941).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=262698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9-941;
RX   PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA   Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison to
RT   the highly similar genomes of Brucella melitensis and Brucella suis.";
RL   J. Bacteriol. 187:2715-2726(2005).
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; AE017223; AAX73699.1; -; Genomic_DNA.
DR   RefSeq; WP_002963434.1; NC_006932.1.
DR   AlphaFoldDB; Q93T81; -.
DR   SMR; Q93T81; -.
DR   EnsemblBacteria; AAX73699; AAX73699; BruAb1_0296.
DR   GeneID; 3789048; -.
DR   KEGG; bmb:BruAb1_0296; -.
DR   HOGENOM; CLU_000980_0_0_5; -.
DR   OMA; GFDSHIH; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000000540; Chromosome I.
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; 2.
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..570
FT                   /note="Urease subunit alpha 1"
FT                   /id="PRO_0000234139"
FT   DOMAIN          131..570
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   570 AA;  61011 MW;  648464AD7EDBB7EC CRC64;
     MPARISRATY AQMFGPTVGD KVRLADTDLI IEVERDLTTY GEEVKFGGGK VIRDGMGQSQ
     LSRAEGAMDT VITNALILDH SGIYKADIGL LDGRIALIGK AGNPDTQPGI SIIIGPGTEI
     IAGEGKIVTA GGIDTHVHFI SPQQVDEALN AGITCMVGGG TGPAHGTLAT TCTPGPWHIA
     RLIQSFDGLP MNIGVFGKGN ASLPGALEEM VRAGACGLKL HEDWGCTPAA IDNCLSVADH
     FDVQVAIHTD TLNEGGFVED TLNAFKGRTI HSFHTEGAGG GHAPDIIRVC QYPNVLPAST
     NPTRPYTVNT IAEHLDMLMV CHHLSPAIPE DIAFAESRIR KETIAAEDIL HDMGAFSIIS
     SDSQAMGRVG EMIIRCWQTA DKMKKQRGSL PDDRPGNDNY RARRYIAKYT INPAIAHGMA
     HEIGSVEVGK RADLVLWNPA FFGVKPDMVL LGGWIATAPM GDANGSIPTP QPMHTRPMFG
     SFGKALTNTS ITFVSQAAMD EGLREKIGVD KQLVAVVNTR GGIGKHSMIL NNAMPQMEVD
     PETYEVRADG ELLTCEPVDV VPMAQRYFLF
 
 
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