ID A0A094DB64_9PEZI Unreviewed; 1716 AA.
AC A0A094DB64;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 13-SEP-2023, entry version 41.
DE RecName: Full=Urease {ECO:0000256|ARBA:ARBA00013883};
DE EC=3.5.1.5 {ECO:0000256|ARBA:ARBA00012934};
DE AltName: Full=Urea amidohydrolase {ECO:0000256|ARBA:ARBA00030395};
GN ORFNames=V497_02962 {ECO:0000313|EMBL:KFY61443.1};
OS Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY61443.1, ECO:0000313|Proteomes:UP000029268};
RN [1] {ECO:0000313|EMBL:KFY61443.1, ECO:0000313|Proteomes:UP000029268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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};
CC -!- COFACTOR:
CC Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC Evidence={ECO:0000256|PIRSR:PIRSR611612-51};
CC Note=Binds 2 nickel ions per subunit. {ECO:0000256|PIRSR:PIRSR611612-
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- PTM: Carbamylation allows a single lysine to coordinate two nickel
CC ions. {ECO:0000256|PIRSR:PIRSR611612-50}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the metallo-dependent
CC hydrolases superfamily. Urease alpha subunit family.
CC {ECO:0000256|ARBA:ARBA00007966}.
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:KFY61443.1}.
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DR EMBL; JPJZ01000718; KFY61443.1; -; Genomic_DNA.
DR STRING; 1420910.A0A094DB64; -.
DR MEROPS; M38.982; -.
DR HOGENOM; CLU_000980_1_1_1; -.
DR OrthoDB; 1408002at2759; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000029268; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035550; C:urease complex; IEA:InterPro.
DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; 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 CDD; cd00407; Urease_beta; 1.
DR CDD; cd00390; Urease_gamma; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 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; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
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; PTHR43440; UREASE; 1.
DR PANTHER; PTHR43440:SF1; UREASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF07690; MFS_1; 1.
DR Pfam; PF00449; Urease_alpha; 1.
DR Pfam; PF00699; Urease_beta; 1.
DR Pfam; PF00547; Urease_gamma; 1.
DR PRINTS; PR01752; UREASE.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR SUPFAM; SSF51278; Urease, beta-subunit; 1.
DR SUPFAM; SSF54111; Urease, gamma-subunit; 1.
DR PROSITE; PS50850; MFS; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00700}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR611612-51};
KW Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|PIRSR:PIRSR611612-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000029268};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1319..1337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1357..1380
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1386..1403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1410..1429
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1480..1498
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1567..1587
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1594..1614
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1620..1642
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 399..835
FT /note="Urease"
FT /evidence="ECO:0000259|PROSITE:PS51368"
FT DOMAIN 1321..1716
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
FT REGION 1058..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1216..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1217..1241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 590
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-52,
FT ECO:0000256|PROSITE-ProRule:PRU00700"
FT BINDING 404
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT BINDING 406
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT BINDING 487
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 487
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 489
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00700"
FT BINDING 516
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT BINDING 542
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT BINDING 630
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT MOD_RES 487
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-50"
SQ SEQUENCE 1716 AA; 184551 MW; B34BED08D668AD45 CRC64;
MHLIPREIDK LVISQLGLLA QRRLARGVRL NHSEACALIA NNLQELIRDG NHNVADLMSI
GTTMLGRRHV LPAVVSTLKQ IQVEGTFPQG TYLVTVQNPI SSDDGDLDKA LYASFLPIPD
ADLFKLPEDE ECKAENMPGA VIAVKGKITI NEGRKRIQLK VTNHGDRPIQ VGSHYHFIET
NPNLEFDRIR SYGYRLDIAA GTSIRFEAGD EKTVTLVEIA GRRIIRGGNN IASGVFDLSR
TDEILKNIEA GNFKHTLEPA GDAAHIKPFE IDRSVYASMF GPTVGDKIRL GDTDLWIKVE
KDLTSYGDEC KFGGGKTLRD GMGQTTGESD EDSLDLVIVN ALIVDWSGIY KADIGIKNGF
ISGIGKAGSP DVMEGVTDGM IVGACTDVMA GEGMIVTAGG IDTHIHYICP QQASECMATG
VTTLLGGGTG PTAATTATTC TPGKNNIRNM MQALDQLPLN YGITGKGNDS DPKALREQVE
AGACGLKLHE DWGCTPAAID SCLTVCDEYD VQCLIHTDTL NESGFVESTI AAFKDRAIHT
YHSEGAGGGH APDIISVVEH NNVLPSSTNP TRPYTRNTLD EHLDMVMVCH HLSKNIPEDI
AFAESRIRAE TIAAEDVLHD MGAISMMSSD SQAMGRCGEV VLRTWNTAHK NKVQRGFLKE
DEGTDADNFR VKRYVSKYTI NPAITQGMGH LLGSVEVGKL ADLVIWEPAW FGTKPTYVVK
SGLISYSMMG DPNASISTVQ PIIGRPMFAP HVPSSSVIFV SQASIDNGVI ESYGLKKRVE
AVKNCRKIRK KDMKHNFNMP KIHVDPENYR VEANGEHCTA EPSSELPLTQ AIGKVYVHFN
MKPSVASLTT AALAFVGQVL AAPQGQILSL SHDLKADTTT PARAANSLQW IGPIAPAGED
VGMQMVRVAR DAQVHHVGHL VRRKKVDASK APQDRIVCDR EDMALNQYGE TWAAYKLASV
VGALAATNES SVVVIGGGHG HCVDLTACDE AERARIQLCN DNPEPNHVKV QTIAEFAYRI
IYECARQDGS GIIWGQEFGD NEFNVIISGC PANYKKEGPK GPLLPSKVDG PKAPVTPPKT
EGPKTSVTPP KVKGPKGKDA NIETGHGYGA TWLAARSNKQ TTFPFGLDWT PSQKCRVPRN
AKATLKPAPQ PTRVSSERPD GYLEQRTDDT GSFLIEETIP YDRDKCDTVE ANYLGTAHAP
AGDDMATEDV KVKVGLSKND TGNSKDDNGI SNGNGNDAPE RIESTATRDE GATLGTASTG
ATKGGEGAAA AKKGWKRKGW FGRMNASAEG EALENMGSRD GLLEGGAGEV VWKVYKRRWF
GLLQLVLLNV VVSWDWLSFA PVSTTASEYF DTSMTAINWL STGFLFAFCV ATPFTIYVLH
KGGPKPAIIT ASVLLLIGNW IRYGGTRAQN FGVVMFGQIL TGFAQPFVLS SPTHYSDLWF
TNNGRVAATA VMTLANPLGG ALGQLIDPFF APNAKDIPNM VLYVSIIATV ASIPSFFIPA
APPTPSSPSA TDHKLDIIPS IKKLFNSREF IMMLVPYTVY VGFFNSISSL LNQILEPYGF
SEEQAGIAGA ILIVVGLVAA AASSPILDRS KKFLLAIKIQ VPLIALSYLA FIWAPPTRGL
AAPYTILAIL GASSFTLLPV ALEYVTEITH PVSPEVTSTI LWSGGQLLGG LFIVISDALQ
DGPQGGYNCA GGYGAAPMSG VVWEKRAGED EESGGG
//
