URE12_PSYCK
ID URE12_PSYCK Reviewed; 611 AA.
AC Q1QC36;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Urease subunit alpha 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01953};
GN Name=ureC2 {ECO:0000255|HAMAP-Rule:MF_01953}; OrderedLocusNames=Pcryo_0986;
OS Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378
OS / K5).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=335284;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Sims D.R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Richardson P.;
RT "Complete sequence of chromosome of Psychrobacter cryohalolentis K5.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABE74767.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000323; ABE74767.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q1QC36; -.
DR SMR; Q1QC36; -.
DR STRING; 335284.Pcryo_0986; -.
DR KEGG; pcr:Pcryo_0986; -.
DR eggNOG; COG0804; Bacteria.
DR eggNOG; COG0832; Bacteria.
DR HOGENOM; CLU_000980_2_0_6; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000002425; 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.
FT CHAIN 1..611
FT /note="Urease subunit alpha 2"
FT /id="PRO_0000239881"
FT DOMAIN 154..611
FT /note="Urease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT REGION 411..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 345
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 159
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 161
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 242
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 242
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 244
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 271
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 297
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
FT BINDING 385
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 242
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01953"
SQ SEQUENCE 611 AA; 65952 MW; 14129E8E2B25CBE5 CRC64;
MGVVDPKTSQ NTSKKRIDRR IYAEHFGPTT GDKVRLADTN LWLEVEYDLT SHIDHQPDID
SVNIGEEVKF GGGKVIRDGM GQSQLLGEQV ADTIITNALI VDYSGIYKAD IAIKEGRISG
IGKAGNPDIQ PNVTLPIGAA TEIIAGEGKI LTAGGIDSHI HFIAPQQCET ALMSGVTTML
GGGTGPAEGT LATTCTPGAY HIHSMLKATD AIPMNIGFLG KGNVSLPAPI VEQIEAGAIG
LKLHEDWGST PKAIDNCLSV AEEYDVQVAI HTDTLNESGY LDSTLGAFKD RCIHTFHTEG
AGGGHAPDIL KAIGETNVLP SSTNPTRPFT INTIDEHLDM LMVCHHLSPA IAEDVAFAES
RIRKETIAAE DILQDMGAIS MMSSDSQAMG RVGEVIIRTW QTADKMKAQR GHLAPDQSAK
TEQSLDNIML SPTDSDSGND NFRIKRYLAK YTINPAITHG ISDEVGSLEL GKWADLVLWS
PAFFGVKPDL IIKGGLIAAA PMGDPNASIS TPQPVHYRSM FGSFPKTVAQ TCITFMSSAA
IDKGVDRQLG LEKVIKAVHN IRKVRKQDMK FNSYCPQMEV NPETYEVYAD GELLTCEPAE
HLPMAQRYFL F
