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Database: UniProt
Entry: F9ZBI6_ODOSD
LinkDB: F9ZBI6_ODOSD
Original site: F9ZBI6_ODOSD 
ID   F9ZBI6_ODOSD            Unreviewed;       572 AA.
AC   F9ZBI6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   13-NOV-2019, entry version 59.
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   OrderedLocusNames=Odosp_1244 {ECO:0000313|EMBL:ADY32294.1};
OS   Odoribacter splanchnicus (strain ATCC 29572 / DSM 20712 / CIP 104287 /
OS   JCM 15291 / NCTC 10825 / 1651/6) (Bacteroides splanchnicus).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Odoribacteraceae;
OC   Odoribacter.
OX   NCBI_TaxID=709991 {ECO:0000313|EMBL:ADY32294.1, ECO:0000313|Proteomes:UP000006657};
RN   [1] {ECO:0000313|EMBL:ADY32294.1, ECO:0000313|Proteomes:UP000006657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29572 / DSM 20712 / JCM 15291 / NCTC 10825 / 1651/6
RC   {ECO:0000313|Proteomes:UP000006657};
RX   PubMed=21677857; DOI=10.4056/sigs.1714269;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Goker M., Gronow S., Zeytun A., Nolan M., Lucas S., Lapidus A.,
RA   Hammon N., Deshpande S., Cheng J.F., Pitluck S., Liolios K.,
RA   Pagani I., Ivanova N., Mavromatis K., Ovchinikova G., Pati A.,
RA   Tapia R., Han C., Goodwin L., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Jeffries C.D., Brambilla E.M., Rohde M., Detter J.C.,
RA   Woyke T., Bristow J., Markowitz V., Hugenholtz P., Eisen J.A.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Odoribacter splanchnicus type strain
RT   (1651/6).";
RL   Stand. Genomic Sci. 4:200-209(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|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}.
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DR   EMBL; CP002544; ADY32294.1; -; Genomic_DNA.
DR   RefSeq; WP_013611513.1; NC_015160.1.
DR   STRING; 709991.Odosp_1244; -.
DR   EnsemblBacteria; ADY32294; ADY32294; Odosp_1244.
DR   GeneID; 41366094; -.
DR   KEGG; osp:Odosp_1244; -.
DR   eggNOG; ENOG4105CQM; Bacteria.
DR   eggNOG; COG0804; LUCA.
DR   KO; K01428; -.
DR   OMA; GFDSHIH; -.
DR   OrthoDB; 157757at2; -.
DR   BioCyc; OSPL709991:G1GRN-1251-MONOMER; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000006657; Chromosome.
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:UP000006657};
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:UP000006657}.
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;  61380 MW;  5D0201C3AC48A806 CRC64;
     MATISRQQYN DLYGPTVGDK IRLGDTDLYV EITKDLCVYG DEVVYGGGKT LRDGMGLANT
     TTSEGGTLDL VITNVTIIDP ILGVIKADVG VKDGKIAGIG KAGNPNIMRG VTPELVTGAA
     TDAISGEHLI LTAAAIDGHV HMIAPQQAYH CLSNGVTTLV GGGVGPTDGT NGTTITSGTW
     NMKRMLQSID GLPVNYGFLG KGNCSVRRPL VEQMLAGACG FKIHEDWGST PAAIRATMAV
     ADEFDVQVAI HTDTLNEGGY VEDTIAAIDG RTIHTYHTEG AGGGHAPDLL KVASLANVLP
     SSTNPTLPFG INSQAELFDM IMVCHNLNPK IPSDVAFAES RVRPETQAAE NILHDLGVIS
     MISSDSQAMG RVGENFLRAF QMASYMKQVR GKLAEDSADN DNFRVLRYLA KLTINPALTY
     GFSEVLGSVE KGKMADLVLW EPAFFGTKPK LVIKGGMINW ANMGDPNASL PTPQPVYYRP
     MYGSFGSAMP KSCISFVSRA SHDAGIKEKY GLQRIVYPVH GCRQIGKPHM VLNGNMPKID
     VNPETFEVFI DGRQAYVKPA QKFSLAQLYW FS
//
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