ID A0A1E4RVA4_CYBJN Unreviewed; 570 AA.
AC A0A1E4RVA4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Allantoinase {ECO:0000313|EMBL:ODV71168.1};
GN ORFNames=CYBJADRAFT_169587 {ECO:0000313|EMBL:ODV71168.1};
OS Cyberlindnera jadinii (strain ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617
OS / NBRC 0987 / NRRL Y-1542) (Torula yeast) (Candida utilis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Cyberlindnera.
OX NCBI_TaxID=983966 {ECO:0000313|EMBL:ODV71168.1, ECO:0000313|Proteomes:UP000094389};
RN [1] {ECO:0000313|EMBL:ODV71168.1, ECO:0000313|Proteomes:UP000094389}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18201 / CBS 1600 / BCRC 20928 / JCM 3617 / NBRC 0987 /
RC NRRL Y-1542 {ECO:0000313|Proteomes:UP000094389};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; KV453943; ODV71168.1; -; Genomic_DNA.
DR RefSeq; XP_020068207.1; XM_020215849.1.
DR AlphaFoldDB; A0A1E4RVA4; -.
DR STRING; 983966.A0A1E4RVA4; -.
DR GeneID; 30990245; -.
DR OMA; QHAQEPR; -.
DR OrthoDB; 5476894at2759; -.
DR Proteomes; UP000094389; Unassembled WGS sequence.
DR GO; GO:0016812; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR002195; Dihydroorotase_CS.
DR InterPro; IPR018228; DNase_TatD-rel_CS.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43668; ALLANTOINASE; 1.
DR PANTHER; PTHR43668:SF2; ALLANTOINASE; 1.
DR Pfam; PF01979; Amidohydro_1; 2.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR PROSITE; PS01137; TATD_1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000094389}.
FT DOMAIN 62..254
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 403..545
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 570 AA; 62377 MW; 5063A5D193E355F0 CRC64;
MSRALASNHV VIGNKVIPAT VVFSQSSGKI LSIEHSVLSP DDPILKSYDV DEKSYRDVSP
FYVMPGLVDS HVHLNEPGRT EWEGFATGTQ AAAAGGVTTV VDMPLNAIPP TTNVKNLNIK
LDAAKGQCWV DVAFWGGLVP DNLDDLVPLI NAGVRGFKGF MIDSGVDEFP AINSFYIDKA
LEKVKGEDTL IMFHAEMQPA CNNHGLQSLE TYEPLDRIDE VEDFGFSLMP ATSLKTTLSN
NTTLEEAIDN DYINNHMLKR VLTNDQARAL AVAPILAPVE PRTGAPSEIV HHDHKIASPL
LEAQRDQDSL ANVDPTAYAS YLASRPDVFE VEAIRTLIGC AKKNPSVPLH IVHLASGEAV
PILAAAQSQG LKISAETCFH YLSFCAEKIP NCSTFFKCCP PIRTEKNRLE LWDALRRGII
KTVVSDHSPC TPELKNLAKG DFFSAWGGIS SVGLGLPVLH TEALKFIEFS IIDVVTWTCY
NTAKQVGLGH RKGNLKVGYD ADIVIFDPYT EQSIENAKTY FKNKLTAYNG RTLRGRVVET
ILRGNSIFAI DKGHSKIPMG RAILEKRSHA
//