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Entry: A0A0C1NEC7_9CYAN
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Original site: A0A0C1NEC7_9CYAN 
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}.
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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
//
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