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URE1_SORC5
ID   URE1_SORC5              Reviewed;         571 AA.
AC   A9GP84;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Urease subunit alpha {ECO:0000255|HAMAP-Rule:MF_01953};
DE            EC=3.5.1.5 {ECO:0000255|HAMAP-Rule:MF_01953};
DE   AltName: Full=Urea amidohydrolase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01953};
GN   Name=ureC {ECO:0000255|HAMAP-Rule:MF_01953}; OrderedLocusNames=sce6549;
OS   Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS   ce56)).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; Sorangiineae;
OC   Polyangiaceae; Sorangium.
OX   NCBI_TaxID=448385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=So ce56;
RX   PubMed=17965706; DOI=10.1038/nbt1354;
RA   Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA   Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA   Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA   Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA   Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA   Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA   Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA   Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA   Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA   Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA   Puehler A., Mueller R.;
RT   "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL   Nat. Biotechnol. 25:1281-1289(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01953};
CC   -!- COFACTOR:
CC       Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01953};
CC       Note=Binds 2 nickel ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01953};
CC   -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC       urea (urease route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01953}.
CC   -!- SUBUNIT: Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha)
CC       subunits. Three heterotrimers associate to form the active enzyme.
CC       {ECO:0000255|HAMAP-Rule:MF_01953}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01953}.
CC   -!- PTM: Carboxylation allows a single lysine to coordinate two nickel
CC       ions. {ECO:0000255|HAMAP-Rule:MF_01953}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Urease alpha subunit family. {ECO:0000255|HAMAP-Rule:MF_01953}.
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DR   EMBL; AM746676; CAN96718.1; -; Genomic_DNA.
DR   RefSeq; WP_012239167.1; NC_010162.1.
DR   AlphaFoldDB; A9GP84; -.
DR   SMR; A9GP84; -.
DR   STRING; 448385.sce6549; -.
DR   MEROPS; M38.982; -.
DR   PRIDE; A9GP84; -.
DR   EnsemblBacteria; CAN96718; CAN96718; sce6549.
DR   KEGG; scl:sce6549; -.
DR   eggNOG; COG0804; Bacteria.
DR   HOGENOM; CLU_000980_0_0_7; -.
DR   OMA; GFDSHIH; -.
DR   OrthoDB; 157757at2; -.
DR   BioCyc; SCEL448385:SCE_RS33600-MON; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000002139; 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   Cytoplasm; Hydrolase; Metal-binding; Nickel; Reference proteome.
FT   CHAIN           1..571
FT                   /note="Urease subunit alpha"
FT                   /id="PRO_1000088497"
FT   ACT_SITE        324
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         138
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         140
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         221
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         221
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /note="via carbamate group"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         250
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         276
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   BINDING         364
FT                   /ligand="Ni(2+)"
FT                   /ligand_id="ChEBI:CHEBI:49786"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT   MOD_RES         221
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
SQ   SEQUENCE   571 AA;  61623 MW;  576EF11830444002 CRC64;
     MSHTMQRRHY VDIYGPTVGD RVRLGDTGLI AEVERDHTSY GDECKFGGGK VLRDRMGQMP
     GASNDEALDC VITNALIVDW TGVYKADIGI KRGRIAAIGK AGNPRVMAGV TPGMIVGVTT
     EVIAGEGHIV TAGGVDAHIH FICPQQGYEA LASGVTTFVG GGTGPATGTN ATTCTPGARH
     ISLMLQATDV LPLNIGLTGK GNTSSPEGLL EQVRAGAVGL KLHEDWGTTP PAIDCCLSFA
     EHEDIQVTLH TDTLNESGYV DDSIAAFKGR TIHSYHSEGA GGGHAPDILR ICGEPNVIPS
     STNPTRPYTV NTLDEHLDML MVCHHLDRNI PEDVAFAESR IRGETIAAED ILHDLGAISI
     ISSDSQAMGR VGEVITRTWQ TAHKMRDQRG RLPEEQGDND NFRIRRYVAK YTINPAIAHG
     MSHEIGSVEP GKLADLVLWR PQMFGVRPEL VIKGGLIAWA QMGDPNASIP TPQPYYMRPM
     FGSLGAAVGE TSIAFVSSRA MDEGSIRRLD LKKRLSAVRR CRKIGKADMR LNNTLLPITV
     DPETYEVRAG GELLRCDPAK ILPLAQRYSL F
 
 
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