URE3_MYCTU
ID URE3_MYCTU Reviewed; 100 AA.
AC P9WFE7; L0TAS5; P0A676; P50043;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Urease subunit gamma {ECO:0000255|HAMAP-Rule:MF_00739};
DE EC=3.5.1.5 {ECO:0000255|HAMAP-Rule:MF_00739};
DE AltName: Full=Urea amidohydrolase subunit gamma {ECO:0000255|HAMAP-Rule:MF_00739};
GN Name=ureA {ECO:0000255|HAMAP-Rule:MF_00739}; OrderedLocusNames=Rv1848;
GN ORFNames=MTCY359.25c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-5, CATALYTIC
RP ACTIVITY, INTERACTION WITH UREB AND UREC, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=7559354; DOI=10.1128/jb.177.19.5644-5652.1995;
RA Clemens D.L., Lee B.-Y., Horwitz M.A.;
RT "Purification, characterization, and genetic analysis of Mycobacterium
RT tuberculosis urease, a potentially critical determinant of host-pathogen
RT interaction.";
RL J. Bacteriol. 177:5644-5652(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=7568014; DOI=10.1073/pnas.92.19.8768;
RA Reyrat J.-M., Berthet F.-X., Gicquel B.;
RT "The urease locus of Mycobacterium tuberculosis and its utilization for the
RT demonstration of allelic exchange in Mycobacterium bovis bacillus Calmette-
RT Guerin.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:8768-8772(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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_00739,
CC ECO:0000269|PubMed:7559354};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.3 mM for urea {ECO:0000269|PubMed:7559354};
CC Vmax=0.05 mmol/min/mg enzyme {ECO:0000269|PubMed:7559354};
CC pH dependence:
CC Optimum pH is 7.2. {ECO:0000269|PubMed:7559354};
CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC urea (urease route): step 1/1. {ECO:0000255|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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00739}.
CC -!- SIMILARITY: Belongs to the urease gamma subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_00739}.
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DR EMBL; U33011; AAC43473.1; -; Genomic_DNA.
DR EMBL; L41141; AAC37005.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP44614.1; -; Genomic_DNA.
DR PIR; H70664; H70664.
DR RefSeq; NP_216364.1; NC_000962.3.
DR RefSeq; WP_003409305.1; NZ_NVQJ01000013.1.
DR PDB; 2FVH; X-ray; 1.80 A; A/B/C=1-100.
DR PDBsum; 2FVH; -.
DR AlphaFoldDB; P9WFE7; -.
DR SMR; P9WFE7; -.
DR STRING; 83332.Rv1848; -.
DR PaxDb; P9WFE7; -.
DR GeneID; 885414; -.
DR KEGG; mtu:Rv1848; -.
DR TubercuList; Rv1848; -.
DR eggNOG; COG0831; Bacteria.
DR OMA; MQLTPHE; -.
DR PhylomeDB; P9WFE7; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000001584; Chromosome.
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; -; 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 Pfam; PF00547; Urease_gamma; 1.
DR PIRSF; PIRSF001223; Urease_gamma; 1.
DR SUPFAM; SSF54111; SSF54111; 1.
DR TIGRFAMs; TIGR00193; urease_gam; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Reference proteome.
FT CHAIN 1..100
FT /note="Urease subunit gamma"
FT /id="PRO_0000098019"
FT CONFLICT 75
FT /note="E -> V (in Ref. 2; AAC37005)"
FT /evidence="ECO:0000305"
FT HELIX 5..25
FT /evidence="ECO:0007829|PDB:2FVH"
FT HELIX 32..49
FT /evidence="ECO:0007829|PDB:2FVH"
FT HELIX 53..59
FT /evidence="ECO:0007829|PDB:2FVH"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:2FVH"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:2FVH"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:2FVH"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:2FVH"
FT STRAND 89..98
FT /evidence="ECO:0007829|PDB:2FVH"
SQ SEQUENCE 100 AA; 11090 MW; D603C57309AC6507 CRC64;
MRLTPHEQER LLLSYAAELA RRRRARGLRL NHPEAIAVIA DHILEGARDG RTVAELMASG
REVLGRDDVM EGVPEMLAEV QVEATFPDGT KLVTVHQPIA
