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Database: UniProt
Entry: E6JDK6_9ACTN
LinkDB: E6JDK6_9ACTN
Original site: E6JDK6_9ACTN 
ID   E6JDK6_9ACTN            Unreviewed;       740 AA.
AC   E6JDK6;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   31-JUL-2019, entry version 60.
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:EFV90356.1};
GN   ORFNames=ES5_16662 {ECO:0000313|EMBL:EFV90356.1};
OS   Dietzia cinnamea P4.
OC   Bacteria; Actinobacteria; Corynebacteriales; Dietziaceae; Dietzia.
OX   NCBI_TaxID=910954 {ECO:0000313|EMBL:EFV90356.1, ECO:0000313|Proteomes:UP000004165};
RN   [1] {ECO:0000313|EMBL:EFV90356.1, ECO:0000313|Proteomes:UP000004165}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P4 {ECO:0000313|EMBL:EFV90356.1,
RC   ECO:0000313|Proteomes:UP000004165};
RX   PubMed=21901521; DOI=10.1007/s10482-011-9633-7;
RA   Procopio L., Alvarez V.M., Jurelevicius D.A., Hansen L.,
RA   Sorensen S.J., Cardoso J.S., Padula M., Leitao A.C., Seldin L.,
RA   van Elsas J.D.;
RT   "Insight from the draft genome of Dietzia cinnamea P4 reveals
RT   mechanisms of survival in complex tropical soil habitats and
RT   biotechnology potential.";
RL   Antonie Van Leeuwenhoek 101:289-302(2012).
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|SAAS:SAAS01115728};
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       Note=Binds 2 nickel ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01953, ECO:0000256|PIRSR:PIRSR611612-51};
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:SAAS00779045}.
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       ECO:0000256|SAAS:SAAS00779069}.
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|SAAS:SAAS00849550}.
CC   -!- SIMILARITY: Belongs to the urease beta subunit family.
CC       {ECO:0000256|SAAS:SAAS00779065}.
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:EFV90356.1}.
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DR   EMBL; AEKG01000390; EFV90356.1; -; Genomic_DNA.
DR   EnsemblBacteria; EFV90356; EFV90356; ES5_16662.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000004165; 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   CDD; cd00407; Urease_beta; 1.
DR   Gene3D; 2.10.150.10; -; 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; IPR002019; Urease_beta.
DR   InterPro; IPR036461; Urease_betasu_sf.
DR   InterPro; IPR029754; Urease_Ni-bd.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF00449; Urease_alpha; 1.
DR   Pfam; PF00699; Urease_beta; 1.
DR   PRINTS; PR01752; UREASE.
DR   SUPFAM; SSF51278; SSF51278; 1.
DR   SUPFAM; SSF51338; SSF51338; 2.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR01792; urease_alph; 1.
DR   TIGRFAMs; TIGR00192; urease_beta; 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:UP000004165};
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|SAAS:SAAS00779062,
KW   ECO:0000313|EMBL:EFV90356.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01953,
KW   ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|SAAS:SAAS00321440};
KW   Nickel {ECO:0000256|HAMAP-Rule:MF_01953,
KW   ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|SAAS:SAAS00317628}.
FT   DOMAIN      293    740       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   REGION      119    152       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   ACT_SITE    484    484       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                52, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   METAL       298    298       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       300    300       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       381    381       Nickel 1; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       381    381       Nickel 2; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       410    410       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       436    436       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       524    524       Nickel 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                51}.
FT   BINDING     383    383       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     381    381       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01953, ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   740 AA;  77410 MW;  0BB3B8EF8064FB33 CRC64;
     MSGSVHYLYG SGDITLGAGR ATIEVRVTNT GDRAVQVGSH YHFFEANREL RFDRLAAYGR
     HLAIGAGLAV RFEPGQTRTV RLVDFAGERV CHGFSGLVDG PLDDPAVRER ALERMVAGGF
     LHSGGGGDSP DNNDDDEVSP PPDGVPVAEG PPTVLPRATY TDIYGPTVGD RLRLADTALT
     IEVTTDHNAV TTDGSPGYGD EAVYGGGKAI RDGMAQDPAG TRASGALDLV ITGATIVDAV
     LGVVKGDIGV RDGRIVAVGK AGNPHLQDGV HPELVIGPGT EVVAGEHKIV TAGGVDTHIH
     YIAPQQVEEA LSNGVTTLFG GGTGPAEGTK GTTCTPGAWN IGRMLQAADG LPVNIGVLGK
     GNTSQPESAV EQIVAGAAGL KIHEDWGTTP AAIRCVQEVA DEYDVQVAIH TDTLNESGFY
     EDTRAAFGDS TIHTFHSEGA GGGHAPDILR VCGEPNVLPA STNPTLPYTV NSVDELLDMV
     MVCHHLSHDI PEDVSFADSR VRAETIAAET VLHDEGIISI FSSDSQAMGR IGESWQRAFQ
     TAHHCRVERG PLPEDVAASP DGHGGARNDN ERVLRYVAKM TINPAIAAGI ADHLGSIEPG
     KLADLVVWPV ESFAAKPSLV IKGGMIVWAP MGDPNASLPT PQPVIYRPMF GAYGGALQST
     RVTFLSAAAI EAGVPEQLGL TSPCLPVRGC RGIGKKDMVR NDRCPTIEVD PETYVVTVDG
     EPATIAPATT LPLAQLHYLA
//
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