ID A0A2G7FWZ3_9EURO Unreviewed; 1067 AA.
AC A0A2G7FWZ3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Fumarylacetoacetate hydrolase {ECO:0000313|EMBL:PIG85110.1};
GN ORFNames=AARAC_000623 {ECO:0000313|EMBL:PIG85110.1}, BDV24DRAFT_121134
GN {ECO:0000313|EMBL:KAE8347634.1};
OS Aspergillus arachidicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=656916 {ECO:0000313|EMBL:PIG85110.1, ECO:0000313|Proteomes:UP000231358};
RN [1] {ECO:0000313|EMBL:PIG85110.1, ECO:0000313|Proteomes:UP000231358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117610 {ECO:0000313|EMBL:PIG85110.1,
RC ECO:0000313|Proteomes:UP000231358};
RA Moore G., Beltz S.B., Mack B.M.;
RT "Genome sequence for an aflatoxigenic pathogen of Argentinian peanut,
RT Aspergillus arachidicola.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAE8347634.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 117612 {ECO:0000313|EMBL:KAE8347634.1};
RG DOE Joint Genome Institute;
RA Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA Baker S.E., Andersen M.R.;
RT "Friends and foes A comparative genomics study of 23 Aspergillus species
RT from section Flavi.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the FAH family. {ECO:0000256|ARBA:ARBA00010211}.
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DR EMBL; ML737112; KAE8347634.1; -; Genomic_DNA.
DR EMBL; NEXV01000350; PIG85110.1; -; Genomic_DNA.
DR STRING; 656916.A0A2G7FWZ3; -.
DR OrthoDB; 1430490at2759; -.
DR Proteomes; UP000231358; Unassembled WGS sequence.
DR Proteomes; UP000325558; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01299; Met_dep_hydrolase_A; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.90.850.10; Fumarylacetoacetase-like, C-terminal domain; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11820; ACYLPYRUVASE; 1.
DR PANTHER; PTHR11820:SF115; FUMARYLACETOACETATE HYDROLASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF01557; FAA_hydrolase; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF56529; FAH; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:PIG85110.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000231358}.
FT DOMAIN 111..453
FT /note="Amidohydrolase-related"
FT /evidence="ECO:0000259|Pfam:PF01979"
FT DOMAIN 551..764
FT /note="Fumarylacetoacetase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01557"
FT DOMAIN 821..1052
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1067 AA; 115934 MW; 78DC57061777744C CRC64;
MAPGILVNGF HDRTTPSSTL PTRRCPYPHE GLRFDPKLKP KSYRMAGTSP DSKILFLDVN
ILDSTGNDPY RGDVLIHGER IVSVGSVPDV EGLRHDPKVR VVQGRGRTFM SGLGDAHTHW
TWNNIALELL GDIGVEEHTL ITARSALCYL DSGYTMCYGA ASAKDRLDCV VRDAINRGTL
PGPRLLANGR EIAKREGELA AGITAFAEGP LEMREVIRHH AKIGVDQIKL SMSGEAITET
VSAEECFFTD EETAACVDEA HRNGIRVCSH ARARDSVIQC ARHGVDVIYH ASYTDEEGMQ
MLEKVKDRVV VAPALNWLYA TVYEAEPFGY SMEKAEQVGY RRELETAIKA LKEMHKRGIT
VLPGGDYGFA WCPHGTYARD LEHFVKLLDF TPMESIVAAT AGIAKLFMQE DELGKILPGY
YADCILVDGD PLKDIAVLQD HSKLDVIMIN GRIHKAQPTE FLNTSAVPPS LQEKKSYFNF
VAFEDDLGRS RIGHLDLGDS TIQPLTMASG SPLANLSQVI ELGDEGVVRA AEAPFPLSSV
KLLPPLADRD VLCIGENYRK HIKEYRESGF AAADNKVTDS PQVPTVFTKR STSIAASGTD
IYPHPGFTQT MDYEGELGVI IGKAGFSIKE KDAMDYIWGY TIINDLSARE RQRDHRQYFM
GKSPDTFCPM GPVAVEAAAL SGEIRVQTHV NGEKRQDGTT ADLIFSIPKL IETVSSGITL
QPGDVIATGT PHGVGVGHHP PKFLKPGDLV EVSVTGLGKL SNRIADPGSK NPTIERVLQK
PSSIPTYNLD RTWGGVGLTK VAPDHYINVR ELGSKSADAE TIVFIHGLGA SLEYYSPLVQ
AAGLESNYRI ILYDLEGHGA TPARASSTAT LQTFARDLDL LFAAKSITSA TLVGWSLGGL
IAMFFAEKHP SRVTTLILLG PGPTPFPEPA VEVFTKRAAL VREKGMEASG VANAVATAAT
SGATKSRPLA ISAVRQSLLS THPEGYAKGC IALARSRGIV ITVENLRMPT LIVAGQEDAI
SPVKLAQGYR SKIPNSQVEL LKDVGHWHVF EDLEGTAEAI NRFLGRL
//
