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Database: UniProt
Entry: A0A1X4ITI9_9RHOB
LinkDB: A0A1X4ITI9_9RHOB
Original site: A0A1X4ITI9_9RHOB 
ID   A0A1X4ITI9_9RHOB        Unreviewed;       572 AA.
AC   A0A1X4ITI9;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   13-NOV-2019, entry version 14.
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=BV911_16765 {ECO:0000313|EMBL:OSP53656.1};
OS   Pseudoruegeria sp. SK021.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Pseudoruegeria; unclassified Pseudoruegeria.
OX   NCBI_TaxID=1933035 {ECO:0000313|EMBL:OSP53656.1, ECO:0000313|Proteomes:UP000194129};
RN   [1] {ECO:0000313|EMBL:OSP53656.1, ECO:0000313|Proteomes:UP000194129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK021 {ECO:0000313|EMBL:OSP53656.1,
RC   ECO:0000313|Proteomes:UP000194129};
RA   Pohlner M., Marshall I., Schreiber L., Cypionka H., Engelen B.;
RT   "Draft genome sequence of Pseudoruegeria str. SK021, a representative
RT   of the marine Rosebacter group, isolated from North Sea sediment.";
RL   Submitted (JAN-2017) 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|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:OSP53656.1}.
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DR   EMBL; MTBG01000044; OSP53656.1; -; Genomic_DNA.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000194129; 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:UP000194129};
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:UP000194129}.
FT   DOMAIN      134    572       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    325    325       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                52, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   METAL       139    139       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       141    141       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       222    222       Nickel 1; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       222    222       Nickel 2; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       251    251       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       277    277       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       365    365       Nickel 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                51}.
FT   BINDING     224    224       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     222    222       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01953, ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   572 AA;  60490 MW;  468DC95EC1F9BC16 CRC64;
     MAKISRQQYS DLYGPTTGDK IRLADTDLFI EIEKDLRVYG EEAVYGGGKT LRDGMGFDNE
     LTSVAGAPDL VITNVTIVDA VLGIIKADVG IKNGEICGIG KAGNPSVMSG VTPGLALGAG
     TDAISGEHLI LTAGGIDAHV HFVSPQQAEA ALSNGVTTLF GGGIGPSDGT NGTTITPGTW
     NIEMMLRSFD GWPVNAGVLG KGNCSGIAPL EEQLHAGAMG LKIHEDWGST PGAIRASLSV
     ADRYDVQVCI HTDTLNEAGF VENTIAAFEG RTIHTYHTEG AGGGHAPDII RVAGVSNVIP
     SSTNPTLPFG INSQAELFDM TMICHNLSPK IPTDVAFAES RVRVETIAAE NVLHDLGAIS
     IMSSDSQAMG RVGENWMRTI QTAHLMKDRM GPYSGDTSGN DNQRVLRFVA KVTINPAIAQ
     GVSHVVGSIE VGKMADLVLW EPAFFGAKPK MVIKGGFISW SLMGDPNASL PTPQPVLYRP
     MFGMMGSTLA KTRVTFTSRA AYDDGIADRY QLQSKVMPVY GTRTISKGSM VRNDALPEIE
     VNPETFAVTV DGKNATIEPA TTVPLAQLHF FS
//
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