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Database: UniProt
Entry: H8MRU3_CORCM
LinkDB: H8MRU3_CORCM
Original site: H8MRU3_CORCM 
ID   H8MRU3_CORCM            Unreviewed;       571 AA.
AC   H8MRU3;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   08-MAY-2019, entry version 53.
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:AFE10617.1};
GN   OrderedLocusNames=COCOR_07674 {ECO:0000313|EMBL:AFE10617.1};
OS   Corallococcus coralloides (strain ATCC 25202 / DSM 2259 / NBRC 100086
OS   / M2) (Myxococcus coralloides).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Corallococcus.
OX   NCBI_TaxID=1144275 {ECO:0000313|EMBL:AFE10617.1, ECO:0000313|Proteomes:UP000007587};
RN   [1] {ECO:0000313|EMBL:AFE10617.1, ECO:0000313|Proteomes:UP000007587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2
RC   {ECO:0000313|Proteomes:UP000007587};
RX   PubMed=22582372; DOI=10.1128/JB.00397-12;
RA   Huntley S., Zhang Y., Treuner-Lange A., Kneip S., Sensen C.W.,
RA   Sogaard-Andersen L.;
RT   "Complete Genome Sequence of the Fruiting Myxobacterium Corallococcus
RT   coralloides DSM 2259.";
RL   J. Bacteriol. 194:3012-3013(2012).
RN   [2] {ECO:0000313|Proteomes:UP000007587}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2
RC   {ECO:0000313|Proteomes:UP000007587};
RA   Huntley S., Zhang Y., Treuner-Lange A., Sensen C.W.,
RA   Sogaard-Andersen L.;
RT   "Genome sequence of the fruiting myxobacterium Corallococcus
RT   coralloides DSM 2259.";
RL   Submitted (MAR-2012) 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|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}.
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DR   EMBL; CP003389; AFE10617.1; -; Genomic_DNA.
DR   RefSeq; WP_014400454.1; NC_017030.1.
DR   STRING; 1144275.COCOR_07674; -.
DR   MEROPS; M38.982; -.
DR   EnsemblBacteria; AFE10617; AFE10617; COCOR_07674.
DR   KEGG; ccx:COCOR_07674; -.
DR   KO; K01428; -.
DR   OMA; GFDSHIH; -.
DR   OrthoDB; 157757at2; -.
DR   BioCyc; CCOR1144275:G1H4B-7639-MONOMER; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000007587; 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; 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:UP000007587};
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:UP000007587}.
FT   DOMAIN      133    571       Urease. {ECO:0000259|PROSITE:PS51368}.
FT   ACT_SITE    324    324       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                52, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   METAL       138    138       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       140    140       Nickel 1; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       221    221       Nickel 1; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       221    221       Nickel 2; via carbamate group.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       250    250       Nickel 2; via pros nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       276    276       Nickel 2; via tele nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01953,
FT                                ECO:0000256|PIRSR:PIRSR611612-51}.
FT   METAL       364    364       Nickel 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PIRSR:PIRSR611612-
FT                                51}.
FT   BINDING     223    223       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01953, ECO:0000256|PROSITE-ProRule:
FT                                PRU00700}.
FT   MOD_RES     221    221       N6-carboxylysine. {ECO:0000256|HAMAP-
FT                                Rule:MF_01953, ECO:0000256|PIRSR:
FT                                PIRSR611612-50}.
SQ   SEQUENCE   571 AA;  60918 MW;  9E11EDCFE7CDAF06 CRC64;
     MSRKLDRRHY ADMFGPTTGD RVRLGDTGLW LQVERDATVY GDECKFGGGK VLREGMGQRA
     GTGDADALDC VITNALVVDW TGIFKADVGI KAGRISAIGK AGNPDVMAGV TPGMVVGVTT
     EVIAGEGLIL TAGGLDTHIH FISPQQADEA IASGITTWVG GGTGPATGTN ATTCTPGAWN
     LARMLEATDT LPLNIGLTGK GNTSLPEGLL DQVRAGAIGL KLHEDWGTTP AAIDTCLTLA
     DAEDVQVTIH TDTLNESGYV DDSLAAFKGR TIHTYHSEGA GGGHAPDIIR VCGAPNVLPS
     STNPTRPYTV NTLDEHLDML MVCHHLDREI PEDVAFAESR IRGETIAAED ILHDLGAISM
     MASDSQAMGR VGEVITRTWQ TAHKMREQRG RLPGEQGDND NLRIRRYVAK YTINPAIAHG
     LSHEVGSVEP GKLADLVLWR PAFFGAKPEL VLKGGFIAWG QMGDANASIP TPQPYLMRPM
     FGARGRARGS TSLAFVSGRA LREGTVQGLG LTKRLSAVVN CRALGKKDMR LNDALPVITV
     DPETYEVRAD GELLRCEPAT WLPLAQRYSL F
//
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