ID A0A0G8ASF9_9SYNE Unreviewed; 564 AA.
AC A0A0G8ASF9;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=Urease {ECO:0000256|ARBA:ARBA00012934, ECO:0000256|RuleBase:RU000510};
DE EC=3.5.1.5 {ECO:0000256|ARBA:ARBA00012934, ECO:0000256|RuleBase:RU000510};
DE Flags: Fragment;
GN Name=ureC {ECO:0000313|EMBL:KKZ10220.1};
GN ORFNames=TQ37_09145 {ECO:0000313|EMBL:KKZ10220.1};
OS Candidatus Synechococcus spongiarum 15L.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1608419 {ECO:0000313|EMBL:KKZ10220.1, ECO:0000313|Proteomes:UP000035037};
RN [1] {ECO:0000313|EMBL:KKZ10220.1, ECO:0000313|Proteomes:UP000035037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=15L {ECO:0000313|EMBL:KKZ10220.1};
RA Slaby B., Hentschel U.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKZ10220.1, ECO:0000313|Proteomes:UP000035037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=15L {ECO:0000313|EMBL:KKZ10220.1};
RA Burgsdorf I., Slaby B.M., Handley K.M., Haber M., Blom J., Marshall C.W.,
RA Gilbert J.A., Hentschel U., Steindler L.;
RT "Lifestyle Evolution in Cyanobacterial Symbionts of Sponges.";
RL Submitted (MAY-2015) 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:0000256|RuleBase:RU000510};
CC -!- COFACTOR:
CC Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC Evidence={ECO:0000256|PIRSR:PIRSR611612-51,
CC ECO:0000256|RuleBase:RU000510};
CC Note=Binds 2 nickel ions per subunit. {ECO:0000256|PIRSR:PIRSR611612-
CC 51, ECO:0000256|RuleBase:RU000510};
CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC urea (urease route): step 1/1. {ECO:0000256|ARBA:ARBA00004897}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PROSITE-ProRule:PRU00700}.
CC -!- PTM: Carbamylation allows a single lysine to coordinate two nickel
CC ions. {ECO:0000256|PIRSR:PIRSR611612-50}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Urease alpha subunit family. {ECO:0000256|RuleBase:RU004158}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKZ10220.1}.
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DR EMBL; JYFQ01000198; KKZ10220.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G8ASF9; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000035037; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR GO; GO:0009039; F:urease activity; IEA:UniProtKB-EC.
DR GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00375; Urease_alpha; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 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 NCBIfam; TIGR01792; urease_alph; 1.
DR PANTHER; PTHR43440; UREASE; 1.
DR PANTHER; PTHR43440:SF1; UREASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF00449; Urease_alpha; 1.
DR PRINTS; PR01752; UREASE.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 2.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 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 {ECO:0000256|PROSITE-ProRule:PRU00700};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00700};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR611612-51};
KW Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|PIRSR:PIRSR611612-51}.
FT DOMAIN 131..564
FT /note="Urease"
FT /evidence="ECO:0000259|PROSITE:PS51368"
FT ACT_SITE 322
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-52,
FT ECO:0000256|PROSITE-ProRule:PRU00700"
FT BINDING 136
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT BINDING 138
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT BINDING 219
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT BINDING 219
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00700"
FT BINDING 248
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT BINDING 274
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT BINDING 362
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT MOD_RES 219
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-50"
FT NON_TER 564
FT /evidence="ECO:0000313|EMBL:KKZ10220.1"
SQ SEQUENCE 564 AA; 59587 MW; 69F63C5992233CD2 CRC64;
MAYPLDRRTY AETYGPTVGD RLRLADTDLI LEVEKDCCVY GEEVKFGGGK VIRDGMGQSQ
VSRGEGAMDT VVTNALILDW WGVVKADVGL RDGRIAAIGK AGNPDIQDGV EVVIGPGTEI
VAGEGQILTA GAIDSHVHFI CPQQVEVALA SGVTTMLGGG TGPATGTNAT TCTPGAFHLA
RMLQAAEGLP VNLGFFGKGN ASVPEALAEQ VRAGACGLKL HEDWGTTPAA IDCCLTVADR
LDVQVCIHTD TLNEAGHVED TIAAIAGRTI HTFHTEGAGG GHAPDIIRIC GEANVLPSST
NPTRPYTANT LEEHLDMLMV CHHLDRSIPE DVAFAESRIR RETIAAEDVL HDLGAFSIVA
SDSQAMGRVG EVITRTFQTA HKMKVQRGAL AEDSDRNDNH RIRRYMAKVT INPAIAHGID
SQVGSVEVGK LADLCLWKPG FFAVKPELVL KGGSIVWAQM GDPNASIPTP EPVHGRPMFA
GFGAAMAPSC LTFVSQAAVD ADLPHRLGLR TPCVPVCNTR GGIGKAAMKM NTATPAIQVD
PQTYEVFADG ELLTCEPARV LPMA
//
