ID A0A093ZTB9_9PEZI Unreviewed; 2395 AA.
AC A0A093ZTB9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 08-NOV-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=V492_02712 {ECO:0000313|EMBL:KFY14290.1};
OS Pseudogymnoascus sp. VKM F-4246.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420902 {ECO:0000313|EMBL:KFY14290.1, ECO:0000313|Proteomes:UP000029299};
RN [1] {ECO:0000313|EMBL:KFY14290.1, ECO:0000313|Proteomes:UP000029299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4246 {ECO:0000313|EMBL:KFY14290.1,
RC ECO:0000313|Proteomes:UP000029299};
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:KFY14290.1}.
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DR EMBL; JPJU01000835; KFY14290.1; -; Genomic_DNA.
DR STRING; 1420902.A0A093ZTB9; -.
DR MEROPS; M38.982; -.
DR HOGENOM; CLU_000980_1_1_1; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000029299; 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:0016279; F:protein-lysine N-methyltransferase activity; 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:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd19180; SET_SpSET10-like; 1.
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; 3.90.1410.10; set domain protein methyltransferase, domain 1; 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 HAMAP; MF_01954; Urease_beta; 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; IPR044432; Set10/Efm1_SET.
DR InterPro; IPR046341; SET_dom_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; SSF82199; SET domain; 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 Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nickel {ECO:0000256|ARBA:ARBA00022596, ECO:0000256|PIRSR:PIRSR611612-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000029299};
KW Transferase {ECO:0000256|ARBA:ARBA00022603};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1237..1255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1275..1297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1304..1321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1398..1419
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1448..1465
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1485..1505
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1512..1532
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1538..1558
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1578..1597
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1617..1637
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 399..835
FT /note="Urease"
FT /evidence="ECO:0000259|PROSITE:PS51368"
FT DOMAIN 1239..1639
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
FT REGION 1064..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1718..1747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1159..1177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1718..1746
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 2395 AA; 259838 MW; A53F739CED22EE47 CRC64;
MHLIPREIDK LVISQLGLLA QRRLARGVRL NHSEACALIA NNLQELIRDG NHNVADLMSI
GTTMLGRRHV LPAVVSTLKQ IQVEGTFPQG TYLVTVQNPI SSDDGDLDKA LFGSFLPIPD
ADLFKLPDDE ECKAENMPGA VIAVKGKITL NKGRKRIQLK VTNHGDRPIQ VGSHYHFIEV
NPQLEFDRVK SYGHRLDIAA GTSIRFEPGD EKTVTLVPIA GRKIIRGGNN IASGVFDLSR
TDEILKNIEA GNFRNILEPA GDAAHITPFA LDRSVYASMF GPTVGDKIRL GDTELWIKVE
KDLTSYGDEC KFGGGKTLRD GMGQTTGESD EDSLDLVIIN ALIVDWSGIY KADIGIKNGF
ISGIGKAGSP DVMDGVTEGM IVGSCTDVMA GEGMIVTAGG IDTHIHYICP QQATECMATG
VTTLLGGGTG PTAATTATTC TPGKNNIRDM LQALDTMPLN YGITGKGNDS DPKALREQVE
AGACGLKLHE DWGCTPAAID SCLTVCDEYD VQCLIHTDTL NESGFVESTI AAFKDRAIHT
YHTEGAGGGH APDIISVVEH DNVLPSSTNP TRPYTRNTLD EHLDMVMVCH HLSKNIPEDI
AFAESRIRAE TIAAEDVLHD MGAISMMSSD SQAMGRCGEV VLRTWNTAHK NKVQRGFLKE
DEGTDADNFR VKRYVSKYTI NPALAQGMSH LLGSVEVGKL ADLVIWDPAW FGTKPTMVVK
SGLISYSMMG DPNASISTVQ PVIGRPMFAP LVPSTSVLFV SQASVDNGNI ESYGLKKRVE
PVKACRTVRK KDMKHNFNRP KIHVDPENYR VEADGEHCTA EPSSELPLTQ AIIAILLYFN
MKTCAATLAA LAFASQAFGA PRPQGIISLA NERIADTTTP ARSASALEWI GPIAPAGEVY
SYYGNVKEVG MKMVEVARDA QVHHVGGLVR RKKTNASKAP QDRIVCDRED MTAAQYGETW
AAYKLAAVVG AVAATNESSV IVIGGGHGHC VDLTACDEAE RARIQLCNDN PEPNHVKVQT
IAEYAYRIIY ECARQDGSGL IWGQEFDAKE FNVIISGCPA NFKKDGPKAS LEPPKGKGPK
GKGPNSQSYD GLAVRRGTPL ESTVGRTSAY GGLRARAPVR DDMGSDAIAG AGLSKNEAGV
TKDGDSNGND NGAIEGIERA TTTTTGDSAT LGTATSSAAK GGEGDGAAAK KGWRRKGWFG
RMNASAEGEA LENMGSRDGL LEGEGGEVVW KVYKRRWFGL LQLVLLNVVV SWDWLSFAPV
STTAHEYFDI SMTAVNWLST GFLFAFCVAT PFTIYVLHNG GPKPAIITAS VLLLLGNWIR
YGGTRAHNFG VVMFGQILTG FAQPFVLASP THYSDLWFTN NGRVAATAVM TLANPLGGAL
GQLIDPFFAP AAKDIPNMVL YISIIATVAS IPSFFIPAAP PTPSSPSSTE HKLDIIPSIK
TLFKSPEFIM MLIPYTVYVG LFNSISSLLN QMLSPYGFTE EEAGIAGAIL IVVGLVAAAL
SSPILDRYKK FLLAIKIQVP LIAIAYLAFI WAPPTRDLAA PYAILAILGA ASFTLLPVAL
EYVTELTHPV SPEVTSTILW SGGQLLGGLF IVISDALQDG PNGGPGSDVP NNMQRALWFQ
AIIALVVMVP PLCLGLFGRS EQVKMRRVEA DRAPEIGSAM SSNDAKKAGG VESADLNAVD
DLVAWAKSHG AYLNDDVEIC HSPEFGISLR VKALQQKTPP NPTIGDVEEA SSATPQTTTP
STHLPPRSRI VSCPFPISLS YLNTVNAFPS LRSHSAPFPA EFLTTQPPKV IGCFFLIQQY
LTGSKSHWAP YIRSLPQPDE PLKLATPLYY PQEAQRWLGG TNLPAAIAQR EAMWRDEFER
GRAALDGGAG MAGLKGRWTW ELYKWASTIF SSRSFVSKLI PDEVYGDVLE RPVAGYANWR
EKIEEEGPYP VLFPLLDIAN HDAKARVEWF VNAQGPVKDF SIMVDEAVEG GAQVFNNYAP
KGNTELLLGY GFCIPGNDDV AIELRCPSGE KWQIREAQHG YRAPSTVSEK WIFHVRSRPY
PAREGDNKTE KFRLFEDGLI DTLSVLVAND REEEFLQENP EYSIEWNLAA SLYNFMGRNA
LCALSVLLAQ LQNAQAKILD AGKDLSEPTT QFEVIAHQYR SGQLATLGAT IDAIHPYLET
LKISDETEDF TIAEWPQSPI IDVRSAFFYL EANHPAAWNA VTRAIASEKK LKLYLGFSAS
SEADDSEDVG AIELPAKNCN FVEMMDNGWG VPMLCLWTWC VLMIHHSENN DLSDGLDMWL
EDVLQFHSTT PYFDSDPETT VATTLITGRT LAAWPDTYPT QSAARRRVNR MHPAVIPGDD
KDADFAKKMV DLAVRIVRGS LFETGISTKC PDTETTKQVA QDVMFVPRMV DGEGA
//
