ID A0A165G6G3_XYLHT Unreviewed; 496 AA.
AC A0A165G6G3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=allantoinase {ECO:0000256|ARBA:ARBA00012863};
DE EC=3.5.2.5 {ECO:0000256|ARBA:ARBA00012863};
GN ORFNames=L228DRAFT_160095 {ECO:0000313|EMBL:KZF21794.1};
OS Xylona heveae (strain CBS 132557 / TC161).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Xylonomycetes;
OC Xylonales; Xylonaceae; Xylona.
OX NCBI_TaxID=1328760 {ECO:0000313|EMBL:KZF21794.1, ECO:0000313|Proteomes:UP000076632};
RN [1] {ECO:0000313|EMBL:KZF21794.1, ECO:0000313|Proteomes:UP000076632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC161 {ECO:0000313|EMBL:KZF21794.1,
RC ECO:0000313|Proteomes:UP000076632};
RX PubMed=26693682; DOI=10.1016/j.funbio.2015.10.002;
RA Gazis R., Kuo A., Riley R., LaButti K., Lipzen A., Lin J., Amirebrahimi M.,
RA Hesse C.N., Spatafora J.W., Henrissat B., Hainaut M., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The genome of Xylona heveae provides a window into fungal endophytism.";
RL Fungal Biol. 120:26-42(2016).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Nitrogen metabolism; (S)-allantoin degradation; allantoate
CC from (S)-allantoin: step 1/1. {ECO:0000256|ARBA:ARBA00004968}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Allantoinase family. {ECO:0000256|ARBA:ARBA00010368}.
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DR EMBL; KV407460; KZF21794.1; -; Genomic_DNA.
DR RefSeq; XP_018187349.1; XM_018329389.1.
DR AlphaFoldDB; A0A165G6G3; -.
DR STRING; 1328760.A0A165G6G3; -.
DR GeneID; 28894526; -.
DR InParanoid; A0A165G6G3; -.
DR OMA; QHAQEPR; -.
DR OrthoDB; 5476894at2759; -.
DR UniPathway; UPA00395; UER00653.
DR Proteomes; UP000076632; Unassembled WGS sequence.
DR GO; GO:0004038; F:allantoinase activity; IEA:UniProtKB-EC.
DR GO; GO:0050897; F:cobalt ion binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000256; P:allantoin catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR017593; Allantoinase.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR002195; Dihydroorotase_CS.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR03178; allantoinase; 1.
DR PANTHER; PTHR43668; ALLANTOINASE; 1.
DR PANTHER; PTHR43668:SF2; ALLANTOINASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS00482; DIHYDROOROTASE_1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000076632}.
FT DOMAIN 63..468
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
SQ SEQUENCE 496 AA; 53530 MW; A2F16BAED6C2602A CRC64;
MPSAVDHPIS VVASERAVIA GRLTAATVVI SLTTGKITSI FDCVLPPSDF PEGTPYIDHS
PHVLLPGLVD AHVHLNEPGR TEWEGFETGT KAAAFGGVTT VVDMPLNAIP PTTTVSNFKE
KINAAQGKCW VDVGFYGGVI PGNHTELTAL VKEGVRGFKG FLIDSGVDEF PAVSSDDITL
AMKELADEPT TLMFHAEMIP PISDSVGDAV QHSEPPLFPH GALTSYNTFL LSRPPAFETY
AIAEILALAS VAPDLPLHIV HLSAIEAIPL LRQARARGVK ITAETCFHYL SIASEKINDG
DTRHKCCPPI RTQSNQDGLW EELQKDDKET VIQTVVSDHS PCTPDLKCLP PTVPRGTEAG
PNTGDFFNAW GGVSSVGLGL SILWTEGQHR GITIEDVVKW CCANTAKQVG LEHQKGDLAV
GFDGDIAVFD DQGSFMVEPS TMLFRNKCSP YEGRELKGVV RETYLRGQRI FSRADGFTKK
SGPQGQLLLE PRTTRT
//
