ID A0A1V6S9U9_9EURO Unreviewed; 1124 AA.
AC A0A1V6S9U9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 13-SEP-2023, entry version 32.
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=PENFLA_c083G02571 {ECO:0000313|EMBL:OQE10656.1};
OS Penicillium flavigenum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=254877 {ECO:0000313|EMBL:OQE10656.1, ECO:0000313|Proteomes:UP000191342};
RN [1] {ECO:0000313|Proteomes:UP000191342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 14082 {ECO:0000313|Proteomes:UP000191342};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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 -!- 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:OQE10656.1}.
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DR EMBL; MLQL01000083; OQE10656.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6S9U9; -.
DR STRING; 254877.A0A1V6S9U9; -.
DR OrthoDB; 1408002at2759; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000191342; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-UniRule.
DR GO; GO:0035550; C:urease complex; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
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; cd00375; Urease_alpha; 1.
DR CDD; cd00407; Urease_beta; 1.
DR CDD; cd00390; Urease_gamma; 1.
DR Gene3D; 1.10.30.10; High mobility group box domain; 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; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
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; PF00505; HMG_box; 1.
DR Pfam; PF00449; Urease_alpha; 1.
DR Pfam; PF00699; Urease_beta; 1.
DR Pfam; PF00547; Urease_gamma; 1.
DR PRINTS; PR01752; UREASE.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF47095; HMG-box; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51278; Urease, beta-subunit; 1.
DR SUPFAM; SSF54111; Urease, gamma-subunit; 1.
DR PROSITE; PS50118; HMG_BOX_2; 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 DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00700};
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 Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Reference proteome {ECO:0000313|Proteomes:UP000191342}.
FT DOMAIN 100..169
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DOMAIN 688..1124
FT /note="Urease"
FT /evidence="ECO:0000259|PROSITE:PS51368"
FT DNA_BIND 100..169
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 72..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..223
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 879
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-52,
FT ECO:0000256|PROSITE-ProRule:PRU00700"
FT BINDING 693
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT BINDING 695
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT BINDING 776
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 776
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 778
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00700"
FT BINDING 805
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT BINDING 831
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT BINDING 919
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-51"
FT MOD_RES 776
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611612-50"
SQ SEQUENCE 1124 AA; 122024 MW; DEA2F2C4C5C259B6 CRC64;
MASNQDDTTV QVNKEELRRA GDLIVMRLME VQSYIADLGK AYVQHVNNIT EGRDATIELP
AGPSGFMGHD VPFRAGSPGA KSEAGGPKKR KRAPVDPNAP KRALTPYFLY MQHNRSKIAD
DLGGDARPKD VADEGTRRWQ SMEDTQKEVW KKMYAANYDQ YKRDMAAYKA GGKVDEDHDP
AASQLQQDFA GAEPEAEAEP EAEAEPEAEA EAGAEESADE STESSDESQS PSPVKEKTPP
RSTTKRRRSE NKAKEAETPA KSPVKRGRKA AEPVSTPAVK TPAENKRRSK KRKSELDKLT
IAHLGFLAQR RLARGVRLNH AEAVALIASV LHELIRDGHY SVADLMSIGK TMLGRRHVLP
SVLATLVELQ VEGTFTSGTY LVTVHHPISS DEGDLERALY GSFLPVPAPE AFPDPDPEDF
KPEKMPGAVI PARHTRVELS SGKRRIKLKV MSKGDRPIQV GSHYHFIETN PQLHFDRMQS
YGFRLDIPAG TSIRFEPGDT KTVTLVEIGG HRIIRGGNWL ANGPLDMSRA DEITTKLQIA
GFGHVPEPQA DSALVSGFSM EREAYSRMFG PTTGDLVRLG LTDLWIKVEK DMTNYGDECA
FGGGKTLREG MGQASDRSHT ECIDTVITNA LIIDWTGIYK ADIGIKDGLI AGIGKAGNPD
VMDGVHPDLV VGSSTDVIAG ENKIVTAGGI DTHIHLICPQ QVDEALASGI TTFLGGGTGP
TTGSNATTCT PSPNLLRQMM QACDSLPINL GITGKGNDCG KKSLREQILA GAAGLKLHED
WGSTPAAIDN CLEVCDEYDV QCMIHTDTLN ESGFVEQSIE AFKGRTIHTY HTEGAGGGHA
PDIISVVEHP NVLPSSTNPT RPFTLNTLDE HLDMLMVCHH LSKNIPEDVA FAESRIRAET
IAAEDVLHDL GAISMMSSDS QAMGRCGEVV LRTWHTAHKN KMQRGPLGSD ADTGADNFRV
KRYISKYTIN PALAQGMAHV IGSVEVGKIA DLVMWKPATF GTKPVSVLKS GMIVTAEVGD
PNASIPTVEP MIMRPMYGVR VPATSIMFVS QASIDAGIVQ TYGLKKRVEA VRNCRSVGKK
DMKFNDVMPK MKVDPESYTV EADGMLCDAE PASELPLTQA YYIF
//
