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Database: UniProt
Entry: A0A0Q0C4U9_PSESX
LinkDB: A0A0Q0C4U9_PSESX
Original site: A0A0Q0C4U9_PSESX 
ID   A0A0Q0C4U9_PSESX        Unreviewed;       566 AA.
AC   A0A0Q0C4U9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   08-MAY-2019, entry version 31.
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   ORFNames=ALO94_200460 {ECO:0000313|EMBL:KPY97797.1}, ALP50_02336
GN   {ECO:0000313|EMBL:RMT27663.1};
OS   Pseudomonas syringae pv. spinaceae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=264459 {ECO:0000313|EMBL:KPY97797.1, ECO:0000313|Proteomes:UP000050384};
RN   [1] {ECO:0000313|EMBL:KPY97797.1, ECO:0000313|Proteomes:UP000050384}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICMP16929 {ECO:0000313|EMBL:KPY97797.1,
RC   ECO:0000313|Proteomes:UP000050384};
RA   Thakur S., Wang P.W., Gong Y., Weir B.S., Guttman D.S.;
RT   "Genome announcement of multiple Pseudomonas syringae strains.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RMT27663.1, ECO:0000313|Proteomes:UP000280047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICMP 16928 {ECO:0000313|EMBL:RMT27663.1,
RC   ECO:0000313|Proteomes:UP000280047};
RA   Dillon M., Thakur S., Almeida R.N.D., Weir B.S., Guttman D.S.;
RT   "Recombination of ecologically and evolutionarily significant loci
RT   maintains genetic cohesion in the Pseudomonas syringae species
RT   complex.";
RL   Submitted (AUG-2018) 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: May form a heterohexamer of 3 UreC (alpha) and 3 UreAB
CC       (gamma/beta) subunits. May also form a heterotrimer of UreA
CC       (gamma), UreB (beta) and UreC (alpha) subunits. Three
CC       heterotrimers associate to form the active enzyme.
CC       {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:KPY97797.1}.
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DR   EMBL; LJRI01000526; KPY97797.1; -; Genomic_DNA.
DR   EMBL; RBTF01000336; RMT27663.1; -; Genomic_DNA.
DR   RefSeq; WP_057426868.1; NZ_RBTF01000336.1.
DR   EnsemblBacteria; KPY97797; KPY97797; ALO94_200460.
DR   PATRIC; fig|264459.3.peg.6337; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000050384; Unassembled WGS sequence.
DR   Proteomes; UP000280047; 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; 1.
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:UP000050384,
KW   ECO:0000313|Proteomes:UP000280047};
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}.
FT   DOMAIN      128    566       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    319    319       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                52, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   METAL       133    133       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       135    135       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       216    216       Nickel 1; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       216    216       Nickel 2; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       245    245       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       271    271       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       359    359       Nickel 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                51}.
FT   BINDING     218    218       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     216    216       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01953, ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   566 AA;  60658 MW;  7383511EC4698813 CRC64;
     MKISRQAYAD MFGPTVGDKV RLADTELWIE VEKDFTTYGE EVKFGGGKVI RDGMGQGQLL
     AADVVDTLIT NALIIDHWGI VKADVGIKNG RIAAIGKAGN PDIQPDVTIA VGAATEVIAG
     EGMILTAGGV DTHIHFICPQ QIEEALMSGV TTMIGGGTGP ATGTNATTVT PGPWHMARML
     QASDSFPMNI GFTGKGNVSL PGPLIEQVKA GAIGLKLHED WGTTPAAIDN CLSVADEYDV
     QVAIHTDTLN ESGFVETTLA AFKNRTIHTY HTEGAGGGHA PDIIKACGSP NVLPSSTNPT
     RPFTRNTIDE HLDMLMVCHH LDPSIAEDVA FAESRIRLET IAAEDILHDL GAFSMLSSDS
     QAMGRVGEVI MRTWQTADKM KKQRGPLPQD GPGNDNFRAK RYIAKYTINP AITHGISHEV
     GSIEVGKWAD LVLWRPAFFG VKPTLILKGG AIAASLMGDA NASIPTPQPV HYRPMFASFG
     SSLHATSLTF ISQAAFDAGV PETLGLKKQI GVVKGCRTVQ KKDLIHNDYL PDIEVDPQTY
     QVKADGVLLW CEPADVLPMA QRYFLF
//
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