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Database: UniProt
Entry: F3KP36_9BURK
LinkDB: F3KP36_9BURK
Original site: F3KP36_9BURK 
ID   F3KP36_9BURK            Unreviewed;       580 AA.
AC   F3KP36;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   31-JUL-2019, entry version 58.
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:EGI78437.1};
GN   ORFNames=HGR_00936 {ECO:0000313|EMBL:EGI78437.1};
OS   Hylemonella gracilis ATCC 19624.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hylemonella.
OX   NCBI_TaxID=887062 {ECO:0000313|EMBL:EGI78437.1, ECO:0000313|Proteomes:UP000016368};
RN   [1] {ECO:0000313|EMBL:EGI78437.1, ECO:0000313|Proteomes:UP000016368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19624 {ECO:0000313|EMBL:EGI78437.1,
RC   ECO:0000313|Proteomes:UP000016368};
RX   PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA   Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA   Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA   Jensen G.J.;
RT   "Structural diversity of bacterial flagellar motors.";
RL   EMBO J. 30:2972-2981(2011).
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:EGI78437.1}.
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DR   EMBL; AEGR01000014; EGI78437.1; -; Genomic_DNA.
DR   RefSeq; WP_006296156.1; NZ_AEGR01000014.1.
DR   STRING; 887062.HGR_00936; -.
DR   EnsemblBacteria; EGI78437; EGI78437; HGR_00936.
DR   eggNOG; ENOG4105CQM; Bacteria.
DR   eggNOG; COG0804; LUCA.
DR   OrthoDB; 157757at2; -.
DR   BioCyc; GCF_000211835:G1EEB-3138-MONOMER; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000016368; 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   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:UP000016368};
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:UP000016368}.
FT   DOMAIN      142    580       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   REGION       54     76       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   ACT_SITE    333    333       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                52, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   METAL       147    147       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       149    149       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       230    230       Nickel 1; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       230    230       Nickel 2; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       259    259       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       285    285       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       373    373       Nickel 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                51}.
FT   BINDING     232    232       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     230    230       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01953, ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   580 AA;  61558 MW;  17733F7125B652C7 CRC64;
     MSFITKRAYA EMYGPTQGDR VRLADTELIV EVEQDYTLRA GGYGEEVKFG GGKTIRDGMA
     QSQRTRDGTG SGPEAGGAVD TVLTNALIID HWGIVKADIG LKDGRIAAIG KAGNPDTQPG
     VDIVIGPGTE IISCEGNIVT AGGIDSHIHF ISPQQIEEAL CSGVTTMLGG GTGPATGTFA
     TTCTPGAWNI ERMLQAADAF PMNLGFLGKG NASLPAALHE QINAGVIGLK LHEDWGTTPS
     AISNCLDVAE ATDTQVAIHS DTLNESGFVE NTIAAVKGRG ICAFHTEGAG GGHAPDILKV
     VGEANFLPSS TNPTMPYTVN TLDEHVDMLM VCHHLDPAIA EDLAFAESRI RKETIAAEDI
     LHDLGAISMM SSDSQAMGRV GEVIMRTWQT AHKMKVQRGA LEGDGARNDN TRVKRYVAKY
     TINPAIAHGI SHEVGSIAPG KWADLVIWKP AFFGVKPALI LKGGFIAFAA MGDPNASIPT
     PQPVHYRPMF GAFGGAIART SLTFVSQAGL AADIGTRFGL AKRLSAVKNI RGVTKRHMVH
     NNYVPKMEID AQTYQVRADG VLLTCEPARS LPMAQRYFLF
//
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