ID A0A0C1NEC7_9CYAN Unreviewed; 100 AA.
AC A0A0C1NEC7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 47.
DE RecName: Full=Urease subunit gamma {ECO:0000256|HAMAP-Rule:MF_00739, ECO:0000256|RuleBase:RU003850};
DE EC=3.5.1.5 {ECO:0000256|HAMAP-Rule:MF_00739, ECO:0000256|RuleBase:RU003850};
DE AltName: Full=Urea amidohydrolase subunit gamma {ECO:0000256|HAMAP-Rule:MF_00739};
GN Name=ureA {ECO:0000256|HAMAP-Rule:MF_00739,
GN ECO:0000313|EMBL:KIE11146.1};
GN ORFNames=DA73_0222385 {ECO:0000313|EMBL:KIE11146.1}, DA73_0400018185
GN {ECO:0000313|EMBL:KAF3887199.1};
OS Tolypothrix bouteillei VB521301.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1479485 {ECO:0000313|EMBL:KIE11146.1};
RN [1] {ECO:0000313|EMBL:KIE11146.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KIE11146.1};
RX PubMed=25700407;
RA Chandrababunaidu M.M., Singh D., Sen D., Bhan S., Das S., Gupta A.,
RA Adhikary S.P., Tripathy S.;
RT "Draft Genome Sequence of Tolypothrix boutellei Strain VB521301.";
RL Genome Announc. 3:e00001-15(2015).
RN [2] {ECO:0000313|EMBL:KAF3887199.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KAF3887199.1};
RA Sarangi A.N., Mukherjee M., Ghosh S., Singh D., Das A., Kant S., Prusty A.,
RA Tripathy S.;
RT "Improved Assembly of Tolypothrix boutellei genome.";
RL Submitted (NOV-2019) 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|ARBA:ARBA00000242, ECO:0000256|HAMAP-
CC Rule:MF_00739, ECO:0000256|RuleBase:RU003850};
CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC urea (urease route): step 1/1. {ECO:0000256|HAMAP-Rule:MF_00739}.
CC -!- SUBUNIT: Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha)
CC subunits. Three heterotrimers associate to form the active enzyme.
CC {ECO:0000256|HAMAP-Rule:MF_00739}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00739,
CC ECO:0000256|RuleBase:RU003850}.
CC -!- SIMILARITY: Belongs to the urease gamma subunit family.
CC {ECO:0000256|HAMAP-Rule:MF_00739, ECO:0000256|RuleBase:RU003850}.
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:KIE11146.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JHEG04000001; KAF3887199.1; -; Genomic_DNA.
DR EMBL; JHEG02000048; KIE11146.1; -; Genomic_DNA.
DR RefSeq; WP_038085035.1; NZ_JHEG04000001.1.
DR AlphaFoldDB; A0A0C1NEC7; -.
DR STRING; 1479485.DA73_0222385; -.
DR OrthoDB; 9793527at2; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000029738; 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-UniRule.
DR GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00390; Urease_gamma; 1.
DR Gene3D; 3.30.280.10; Urease, gamma-like subunit; 1.
DR HAMAP; MF_00739; Urease_gamma; 1.
DR InterPro; IPR012010; Urease_gamma.
DR InterPro; IPR002026; Urease_gamma/gamma-beta_su.
DR InterPro; IPR036463; Urease_gamma_sf.
DR NCBIfam; TIGR00193; urease_gam; 1.
DR PANTHER; PTHR33569; UREASE; 1.
DR PANTHER; PTHR33569:SF1; UREASE; 1.
DR Pfam; PF00547; Urease_gamma; 1.
DR PIRSF; PIRSF001223; Urease_gamma; 1.
DR SUPFAM; SSF54111; Urease, gamma-subunit; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00739};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00739};
KW Reference proteome {ECO:0000313|Proteomes:UP000029738}.
SQ SEQUENCE 100 AA; 11038 MW; 673E08A785148060 CRC64;
MQLTPQEKDK LLIFTAALLA ERRKARGLKL NYPEAIAFIS AAILEGARDG QTVAELMSYG
TTLLSRDDVM EGVPEMIHDV QVEATFPDGT KLVTVHNPIR
//