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Database: UniProt
Entry: A0A0F8BHF5_9EURY
LinkDB: A0A0F8BHF5_9EURY
Original site: A0A0F8BHF5_9EURY 
ID   A0A0F8BHF5_9EURY        Unreviewed;       570 AA.
AC   A0A0F8BHF5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   08-MAY-2019, entry version 27.
DE   RecName: Full=Urease subunit alpha {ECO:0000256|HAMAP-Rule:MF_01953};
DE            EC=3.5.1.5 {ECO:0000256|HAMAP-Rule:MF_01953};
DE   AltName: Full=Urea amidohydrolase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01953};
GN   Name=ureC {ECO:0000256|HAMAP-Rule:MF_01953,
GN   ECO:0000313|EMBL:KKF39648.1};
GN   ORFNames=FK85_26875 {ECO:0000313|EMBL:KKF39648.1};
OS   Halorubrum saccharovorum.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria;
OC   Haloferacales; Halorubraceae; Halorubrum.
OX   NCBI_TaxID=2248 {ECO:0000313|EMBL:KKF39648.1, ECO:0000313|Proteomes:UP000053331};
RN   [1] {ECO:0000313|EMBL:KKF39648.1, ECO:0000313|Proteomes:UP000053331}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H3 {ECO:0000313|EMBL:KKF39648.1,
RC   ECO:0000313|Proteomes:UP000053331};
RA   Rozanov A.S., Kotenko A.V., Bryanskaya A.V., Malup T.K., Peltek S.E.;
RT   "Full genome sequence of Halorubrum H3 strain isolated from
RT   Burlinskoye Salt Lake (Altai Krai, Russia).";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+);
CC         Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16199, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938;
CC         EC=3.5.1.5; Evidence={ECO:0000256|HAMAP-Rule:MF_01953,
CC         ECO:0000256|RuleBase:RU000510};
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01953,
CC         ECO:0000256|PIRSR:PIRSR611612-51,
CC         ECO:0000256|RuleBase:RU000510};
CC       Note=Binds 2 nickel ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01953, ECO:0000256|PIRSR:PIRSR611612-51,
CC       ECO:0000256|RuleBase:RU000510};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3)
CC       from urea (urease route): step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01953}.
CC   -!- SUBUNIT: Heterotrimer of UreA (gamma), UreB (beta) and UreC
CC       (alpha) subunits. Three heterotrimers associate to form the active
CC       enzyme. {ECO:0000256|HAMAP-Rule:MF_01953}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01953}.
CC   -!- PTM: Carbamylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000256|HAMAP-Rule:MF_01953,
CC       ECO:0000256|PIRSR:PIRSR611612-50}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. Urease alpha subunit family. {ECO:0000256|HAMAP-
CC       Rule:MF_01953, ECO:0000256|RuleBase:RU004158}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KKF39648.1}.
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DR   EMBL; JNFH02000029; KKF39648.1; -; Genomic_DNA.
DR   RefSeq; WP_050024820.1; NZ_JNFH02000029.1.
DR   EnsemblBacteria; KKF39648; KKF39648; FK85_26875.
DR   OrthoDB; 6384at2157; -.
DR   BioCyc; GCF_000700025:G1EIL-1453-MONOMER; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000053331; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000053331};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01953};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01953, ECO:0000256|PROSITE-
KW   ProRule:PRU00700, ECO:0000256|RuleBase:RU000510,
KW   ECO:0000313|EMBL:KKF39648.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01953,
KW   ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|RuleBase:RU000510};
KW   Nickel {ECO:0000256|HAMAP-Rule:MF_01953,
KW   ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|RuleBase:RU000510};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053331}.
FT   DOMAIN      135    570       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    322    322       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                52, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   METAL       140    140       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       142    142       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       219    219       Nickel 1; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       219    219       Nickel 2; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       248    248       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       274    274       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       362    362       Nickel 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                51}.
FT   BINDING     221    221       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     219    219       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01953, ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   570 AA;  61323 MW;  9494FE2A94E935A2 CRC64;
     MSRELSRKAY TDLFGATEGD RLRLGDTNLL AEIETDHGTY GDEAVFGGGK TMRDGMGMQP
     GTTQADGALD WVYTNVVVID PVLGVQKGDI GVRNGKVVGV GKAGNPDTMD GVDDDLIIGA
     STDTIPADGL IATPGAFDIH VHFNSKELFE HALASGITTM FGGGFGGGAT TCTPGPENIK
     RFLQAAEEWP MNVGFYAKGN SSRPEPIREQ IEAGATGLKL HEDWGSTPAV IDTALDVADE
     EDVQVCIHTD TLNESGFVED TFEVIDGRTI HTFHIEGAGG GHAPDVLELI GHEHMLPSST
     NPSMPYTVNT FDEHLDMVMV CHHLNPDVPE DVAFAESRIR SETIAAEDVL HDMGAISMMT
     SDSQAMGRMA EVICRTWQTA HKMKAQRGPL PADEGTDADN ARIERYVAKY TINPAKVAGI
     DEYIGSLETG KMADIVLWEP EFFGIKPKCV IKGGFPVHSE MGEANGSLMT CEPVMQRSRA
     GAVGKAKNAV STTFVSEAAY ENDVGDELDL DSTVRPVEGT RDVGKSDMLH NDYAPDDIDI
     DAQTFEVEVD GEHVTCEPAE EVPLAQRYTL
//
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