ID C4JVM5_UNCRE Unreviewed; 837 AA.
AC C4JVM5;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Urease {ECO:0000256|ARBA:ARBA00013883, ECO:0000256|PIRNR:PIRNR001222};
DE EC=3.5.1.5 {ECO:0000256|ARBA:ARBA00012934, ECO:0000256|PIRNR:PIRNR001222};
DE AltName: Full=Urea amidohydrolase {ECO:0000256|ARBA:ARBA00030395, ECO:0000256|PIRNR:PIRNR001222};
GN ORFNames=UREG_06617 {ECO:0000313|EMBL:EEP81752.1};
OS Uncinocarpus reesii (strain UAMH 1704).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX NCBI_TaxID=336963 {ECO:0000313|EMBL:EEP81752.1, ECO:0000313|Proteomes:UP000002058};
RN [1] {ECO:0000313|Proteomes:UP000002058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 1704 {ECO:0000313|Proteomes:UP000002058};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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,
CC ECO:0000256|PIRNR:PIRNR001222};
CC -!- COFACTOR:
CC Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC Evidence={ECO:0000256|PIRSR:PIRSR001222-51};
CC Note=Binds 2 nickel ions per subunit. {ECO:0000256|PIRSR:PIRSR001222-
CC 51};
CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC urea (urease route): step 1/1. {ECO:0000256|ARBA:ARBA00004897,
CC ECO:0000256|PIRNR:PIRNR001222}.
CC -!- PTM: Carbamylation allows a single lysine to coordinate two nickel
CC ions. {ECO:0000256|PIRSR:PIRSR001222-50}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the metallo-dependent
CC hydrolases superfamily. Urease alpha subunit family.
CC {ECO:0000256|ARBA:ARBA00007966}.
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DR EMBL; CH476618; EEP81752.1; -; Genomic_DNA.
DR RefSeq; XP_002583650.1; XM_002583604.1.
DR AlphaFoldDB; C4JVM5; -.
DR STRING; 336963.C4JVM5; -.
DR MEROPS; M38.982; -.
DR GeneID; 8438446; -.
DR KEGG; ure:UREG_06617; -.
DR VEuPathDB; FungiDB:UREG_06617; -.
DR eggNOG; ENOG502QPKB; Eukaryota.
DR HOGENOM; CLU_000980_0_1_1; -.
DR InParanoid; C4JVM5; -.
DR OMA; DTMDGVH; -.
DR OrthoDB; 1408002at2759; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000002058; Unassembled WGS sequence.
DR GO; GO:0035550; C:urease complex; IEA:InterPro.
DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0009039; F:urease activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00375; Urease_alpha; 1.
DR CDD; cd00407; Urease_beta; 1.
DR CDD; cd00390; Urease_gamma; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.10.150.10; Urease, beta subunit; 1.
DR Gene3D; 3.30.280.10; Urease, gamma-like subunit; 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; IPR008221; Urease.
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; IPR002019; Urease_beta-like.
DR InterPro; IPR036461; Urease_betasu_sf.
DR InterPro; IPR002026; Urease_gamma/gamma-beta_su.
DR InterPro; IPR036463; Urease_gamma_sf.
DR InterPro; IPR029754; Urease_Ni-bd.
DR NCBIfam; TIGR01792; urease_alph; 1.
DR NCBIfam; TIGR00192; urease_beta; 1.
DR NCBIfam; TIGR00193; urease_gam; 1.
DR PANTHER; PTHR33569; UREASE; 1.
DR PANTHER; PTHR33569:SF1; UREASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF00449; Urease_alpha; 1.
DR Pfam; PF00699; Urease_beta; 1.
DR Pfam; PF00547; Urease_gamma; 1.
DR PIRSF; PIRSF001222; Urease; 1.
DR PRINTS; PR01752; UREASE.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51278; Urease, beta-subunit; 1.
DR SUPFAM; SSF54111; Urease, gamma-subunit; 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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001222};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR001222};
KW Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|PIRNR:PIRNR001222};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002058}.
FT DOMAIN 401..837
FT /note="Urease"
FT /evidence="ECO:0000259|PROSITE:PS51368"
FT ACT_SITE 592
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-52,
FT ECO:0000256|PROSITE-ProRule:PRU00700"
FT BINDING 406
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT BINDING 408
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT BINDING 489
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT BINDING 489
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT BINDING 491
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00700"
FT BINDING 518
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT BINDING 544
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT BINDING 632
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-51"
FT MOD_RES 489
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR001222-50"
SQ SEQUENCE 837 AA; 90457 MW; 3D79B688D4D6D2A1 CRC64;
MQLIPREIDK LTISNLGFLA QRRLARGVRL NHAEATALIA SNLQELIRDG NHSVADLMSI
GKEMLGRRHV LPGVVATLSQ IQVEGTFPTG TNLVTVVNPV SSDDGNLEKA LYGSFLPVPP
MDAFPDPNPD DYQPEKMPGA LIPVKTNKKI ELNAGRNRIM LKVTSRGDRP VQVGSHYHFI
EVNPQLDFDR AKAYGYRLDI PAGTSIRFEP GATKSVPLVE IGGIRFIRGG NAMASGLLDY
RRVDEILMKL QKAGFAYTPE PKAGPQLIEP CSMTREAYAR MFGPTTGDLV RLGSTNLWVK
VEKDLTRYGD ESSFGGGKSI RDGMGQATGR HSADTLDAVV TNALVIDWTG IYKADIGIKD
GLICGVGQAG NPDVMDGVTP NMIIGSTTDV ISGEAKIVTA GGIDTHVHFI CPQQVEEALA
SGVTTMLGGG TGPTEGSNAT TCTPAPNHFK RMMQACDRLP MNIALTGKGN DSGLPSLRDQ
CRAGAAGLKV HEDWGATPAA IDTCLKVCDE YDIQCLIHTD TLNESGFVEQ TIKAINGRVL
HTYHTEGAGG GHAPDIISVV EHPNVLPSST NPTRPFTTNT LDEHLDMVMV CHHLSKDIPE
DVAFAESRIR SETIAAEDVL HDMGAISMLS SDSQAMGRCG EVVTRTWTTA HKNKLQRGPL
KEDEGTGADN FRVKRYISKY TINPAIAQGM AHTIGSVEVG KTADLVLWKF ANFGTKPSMI
LKSGMVAASH MGDPNGSIPT IEPIIMRPSY ASLTPQASIM FVSEASIKLG IISSYNLQKR
IESVKNCRNV SKRDMKYNDT MPKMRVDPES YVVEADGEVC TADPVSELPL TQECYVY
//
