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Database: UniProt
Entry: Q2HFY2_CHAGB
LinkDB: Q2HFY2_CHAGB
Original site: Q2HFY2_CHAGB 
ID   Q2HFY2_CHAGB            Unreviewed;       788 AA.
AC   Q2HFY2;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 105.
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=CHGG_00872 {ECO:0000313|EMBL:EAQ92637.1};
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ92637.1, ECO:0000313|Proteomes:UP000001056};
RN   [1] {ECO:0000313|Proteomes:UP000001056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC   {ECO:0000313|Proteomes:UP000001056};
RX   PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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|ARBA:ARBA00001948};
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; CH408029; EAQ92637.1; -; Genomic_DNA.
DR   RefSeq; XP_001220093.1; XM_001220092.1.
DR   AlphaFoldDB; Q2HFY2; -.
DR   STRING; 306901.Q2HFY2; -.
DR   MEROPS; M38.982; -.
DR   GeneID; 4386978; -.
DR   VEuPathDB; FungiDB:CHGG_00872; -.
DR   eggNOG; ENOG502QPKB; Eukaryota.
DR   HOGENOM; CLU_000980_0_0_1; -.
DR   InParanoid; Q2HFY2; -.
DR   OMA; DTMDGVH; -.
DR   OrthoDB; 1408002at2759; -.
DR   UniPathway; UPA00258; UER00370.
DR   Proteomes; UP000001056; 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:0009039; F:urease activity; IEA:UniProtKB-EC.
DR   GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00407; Urease_beta; 1.
DR   CDD; cd00390; Urease_gamma; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
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   NCBIfam; TIGR00192; urease_beta; 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; 3.
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; PS00145; UREASE_2; 1.
DR   PROSITE; PS51368; UREASE_3; 1.
PE   3: Inferred from homology;
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   Reference proteome {ECO:0000313|Proteomes:UP000001056}.
FT   DOMAIN          411..788
FT                   /note="Urease"
FT                   /evidence="ECO:0000259|PROSITE:PS51368"
FT   REGION          592..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..611
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        659..673
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        567
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611612-52,
FT                   ECO:0000256|PROSITE-ProRule:PRU00700"
FT   BINDING         466
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00700"
FT   MOD_RES         464
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001222-50"
SQ   SEQUENCE   788 AA;  85390 MW;  5EB919B16B362F6A CRC64;
     MHLVPKELDK ITISSLGFLA QRRLARGALI ASNLHELIRD GNHSVADLMS LGSTMLGRRH
     VLPEVCTTLH DIQVEGTFPA GTFLVTVQHP IATDDGDLAR ALYGSFIPVP ENAEELFPKY
     PDEEYTYEKQ PGAILVVKDS VIKLNEGKKR IKLQVTSRGD RPIQVGSHYH FIEVNPCLEF
     DRLRSYGYRL DQASGSSIRF EPGDTKTVTL VEIGGLKVIR GGNAMASGRV DFGNLKDIQD
     RLAEAGFAHV PDPAGDMSLT SETGNLFHNI EGATIDRNTY ATMFGPTTGD LVKLGKTDLW
     IRVEKDFTVY GDECKFGGGK TLRDGMGAAT GRTSAESLDL VVTNALIVDW TGIFKADIGV
     KDGYIVNIGK AGNPDVMDGV TPGMIVGSCT DVIAGEAGRR VYCVWHYHHG GRSATTCTPG
     PYFIREILRG ADRLPVNIGI TAKGNDSDPV ALHEMVKAGA CGLKLHEDWG CHPAAIDTCL
     TVCDELDVQC MIHTDTLNES GYVEQTLKAV NGRTLHAYHT EGAGGGHAPD IIRIAEYPNI
     LPSSTNPTRP YTRNTLEEHL DMLMVCHHLT KDIPEDVAFA ESRIRAETIA AEGRAARPGR
     HQHDEQRQPG HGPLRRGGPA NVAHGAQEQG PARPAARGRG HGCRQLPRQA KVSPFPSSSN
     LHKPPPVSNE PPTNQTPTPT QQGDANASIP SIEPLIMRPM FAPSIPQTSV AFVSQAGIDS
     GVVGTYGLKK RIVPVRNCRN VGKKDLKFND ATPRMSVDPE SYVVQADGVV MDSEPMAELP
     LAQTAYFY
//
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