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Database: UniProt
Entry: A0A0A0ECR0_9RHOB
LinkDB: A0A0A0ECR0_9RHOB
Original site: A0A0A0ECR0_9RHOB 
ID   A0A0A0ECR0_9RHOB        Unreviewed;       580 AA.
AC   A0A0A0ECR0;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   13-NOV-2019, entry version 37.
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:KGM48080.1};
GN   ORFNames=ATO9_13945 {ECO:0000313|EMBL:KGM48080.1};
OS   Pseudooceanicola atlanticus.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Pseudooceanicola.
OX   NCBI_TaxID=1461694 {ECO:0000313|EMBL:KGM48080.1, ECO:0000313|Proteomes:UP000030004};
RN   [1] {ECO:0000313|EMBL:KGM48080.1, ECO:0000313|Proteomes:UP000030004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=22II-s11g {ECO:0000313|EMBL:KGM48080.1,
RC   ECO:0000313|Proteomes:UP000030004};
RX   PubMed=25663028; DOI=10.1007/s10482-015-0398-2;
RA   Lai Q., Li G., Liu X., Du Y., Sun F., Shao Z.;
RT   "Pseudooceanicola atlanticus gen. nov. sp. nov., isolated from surface
RT   seawater of the Atlantic Ocean and reclassification of Oceanicola
RT   batsensis, Oceanicola marinus, Oceanicola nitratireducens, Oceanicola
RT   nanhaiensis, Oceanicola antarcticus and Oceanicola flagellatus, as
RT   Pseudooceanicola batsensis comb. nov., Pseudooceanicola marinus comb.
RT   nov., Pseudooceanicola nitratireducens comb. nov., Pseudooceanicola
RT   nanhaiensis comb. nov., Pseudooceanicola antarcticus comb. nov., and
RT   Pseudooceanicola flagellatus comb. nov.";
RL   Antonie Van Leeuwenhoek 107:1065-1074(2015).
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|PIRSR:PIRSR611612-50}.
CC   -!- PTM: Carboxylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000256|HAMAP-Rule:MF_01953}.
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:KGM48080.1}.
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DR   EMBL; AQQX01000005; KGM48080.1; -; Genomic_DNA.
DR   RefSeq; WP_043750063.1; NZ_AQQX01000005.1.
DR   STRING; 1461694.ATO9_13945; -.
DR   EnsemblBacteria; KGM48080; KGM48080; ATO9_13945.
DR   OrthoDB; 157757at2; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000030004; 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:UP000030004};
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:UP000030004}.
FT   DOMAIN      142    580       Urease. {ECO:0000259|PROSITE:PS51368}.
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;  62025 MW;  77C7D6B4C8710D40 CRC64;
     MPTQISRADY AAMFGPTTGD KLRLADTDLI IEVERDLTAD LAGIGGNGPL YGEEVKFGGG
     KVIRDGMGQS QKTRAEGAVD TVITNALILD WTGIYKADVG LRDGRIHKIG KAGNPDTQPG
     VDIIVGPGTE VIAGEGKILT AGGFDSHIHF ICPQQIEDAL HSGLTTMLGG GTGPAHGTLA
     TTVTPGPWHM ARMLQAADAF PMNLAFAGKG NASLPAALEE QIKAGACSLK LHEDWGTTPG
     AIDCCLSVAD DYDVQVMIHT DTLNESGFVE NTVKAMKGRT IHAFHTEGAG GGHAPDIIKI
     CGEEHVLPSS TNPTRPFTVN TLDEHLDMLM VCHHLDKSIP EDVAFAESRI RRETIAAEDI
     LHDMGAFSII ASDSQAMGRV GEVIIRTWQT ADKMKKQRGK LPEETGDNDN MRVRRYVAKY
     TINPAIAHGI SHQIGSIEEG KRADLVLWSP AFFGVKPEMV LIGGSIVAAQ MGDPNASIPT
     PQPVYTRPMF GAFGRAVENS AVTFVSAAAQ AEGIRDSLGL AKETIAVLNT RNIGKKDLKL
     NDATPKVEVN PETYEVRADG ELLTCEPASE LPMAQRYFMF
//
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