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Database: UniProt
Entry: K8GFV3_9CYAN
LinkDB: K8GFV3_9CYAN
Original site: K8GFV3_9CYAN 
ID   K8GFV3_9CYAN            Unreviewed;       579 AA.
AC   K8GFV3;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   08-MAY-2019, entry version 49.
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};
DE   Flags: Precursor;
GN   Name=ureC {ECO:0000256|HAMAP-Rule:MF_01953};
GN   ORFNames=OsccyDRAFT_4103 {ECO:0000313|EMBL:EKQ67813.1};
OS   Oscillatoriales cyanobacterium JSC-12.
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   unclassified Oscillatoriales.
OX   NCBI_TaxID=864702 {ECO:0000313|EMBL:EKQ67813.1, ECO:0000313|Proteomes:UP000001332};
RN   [1] {ECO:0000313|EMBL:EKQ67813.1, ECO:0000313|Proteomes:UP000001332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JSC-12 {ECO:0000313|EMBL:EKQ67813.1,
RC   ECO:0000313|Proteomes:UP000001332};
RG   DOE Joint Genome Institute;
RA   Brown I., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C.,
RA   Tapia R., Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E.,
RA   Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RT   "Improved high quality draft of Oscillatoriales sp. JSC-12.";
RL   Submitted (OCT-2012) 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, ECO:0000256|SAAS:SAAS01119912};
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, ECO:0000256|SAAS:SAAS00317636}.
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       ECO:0000256|PROSITE-ProRule:PRU00700,
CC       ECO:0000256|SAAS:SAAS00548017}.
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       ECO:0000256|SAAS:SAAS00849550}.
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:EKQ67813.1}.
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DR   EMBL; AJUB01000015; EKQ67813.1; -; Genomic_DNA.
DR   RefSeq; WP_009768607.1; NZ_CM001633.1.
DR   STRING; 864702.OsccyDRAFT_4103; -.
DR   EnsemblBacteria; EKQ67813; EKQ67813; OsccyDRAFT_4103.
DR   PATRIC; fig|864702.5.peg.4395; -.
DR   OrthoDB; 157757at2; -.
DR   BioCyc; OCYA864702:G1HC7-3987-MONOMER; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000001332; 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; 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   Complete proteome {ECO:0000313|Proteomes:UP000001332};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01953, ECO:0000256|PROSITE-
KW   ProRule:PRU00700, ECO:0000256|SAAS:SAAS00317631};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01953, ECO:0000256|PROSITE-
KW   ProRule:PRU00700, ECO:0000256|RuleBase:RU000510,
KW   ECO:0000256|SAAS:SAAS00321417};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01953,
KW   ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|RuleBase:RU000510,
KW   ECO:0000256|SAAS:SAAS00321440};
KW   Nickel {ECO:0000256|HAMAP-Rule:MF_01953,
KW   ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|RuleBase:RU000510,
KW   ECO:0000256|SAAS:SAAS00317628};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001332}.
FT   DOMAIN      131    579       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       136    136       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       138    138       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   579 AA;  62333 MW;  C969B432DB7D92CD CRC64;
     MSYRMNRHAY AETFGPTVGD RVRLADTDLI IEVEQDHTTY GDEVKFGGGK VIRDGMGQSP
     ITNADGAVDA VITNALILDW WGIVKADVGI KDGKIHAIGK AGNPYIQDNV NIIIGPGTEA
     IAGEGMILTA GGIDSHIHFI CPQQIEVAIA SGITTMIGGG TGPASGTNAT TCTPGPWNIY
     RMLQAADAFP MNLGFLGKGN AAKPEGLREQ VEAGAIGLKL HEDWGTTPAS IDTCLTVADE
     YDVQVAIHTD TLNEAGFVED TIAAFKNRVI HTYHTEGAGG GHAPDIIKVC GQANVLPSST
     NPTRPYTINT LDEHLDMLMV CHHLDPGIAE DVAFAESRIR RETIAAEDIL HDLGAFSIIS
     SDSQAMGRIG EVIIRTWQTG HKMKYQRGWL PPAGEGGING VDLHNHNDNF RAKRYVAKYT
     INPAITHGIA DYVGSIEVGK LADLCLWRPA MFGVKPELVL KGGMIAWAQM GDANASIPTP
     QPVHMRPMFA SFGGAMTATS LTFLSKAAIA SGIPDQLKLQ KQTVAVANIR QLTKRDMKLN
     DVLPEMDVDP ETYEVRADGQ LLTCEPATEL PMTQRYFLF
//
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