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Database: UniProt
Entry: A3LSP4_PICST
LinkDB: A3LSP4_PICST
Original site: A3LSP4_PICST 
ID   A3LSP4_PICST            Unreviewed;       293 AA.
AC   A3LSP4;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=Degradation of aromatic compounds {ECO:0000313|EMBL:ABN65932.1};
DE            EC=5.3.3.10 {ECO:0000313|EMBL:ABN65932.1};
GN   Name=UMH1 {ECO:0000313|EMBL:ABN65932.1};
GN   ORFNames=PICST_58067 {ECO:0000313|EMBL:ABN65932.1};
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN65932.1, ECO:0000313|Proteomes:UP000002258};
RN   [1] {ECO:0000313|EMBL:ABN65932.1, ECO:0000313|Proteomes:UP000002258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC   {ECO:0000313|Proteomes:UP000002258};
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
CC   -!- SIMILARITY: Belongs to the FAH family. {ECO:0000256|ARBA:ARBA00010211}.
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DR   EMBL; CP000497; ABN65932.1; -; Genomic_DNA.
DR   RefSeq; XP_001383961.1; XM_001383924.1.
DR   AlphaFoldDB; A3LSP4; -.
DR   STRING; 322104.A3LSP4; -.
DR   GeneID; 4838347; -.
DR   KEGG; pic:PICST_58067; -.
DR   eggNOG; KOG1535; Eukaryota.
DR   HOGENOM; CLU_028458_2_1_1; -.
DR   InParanoid; A3LSP4; -.
DR   OMA; PASECDW; -.
DR   OrthoDB; 9433at2759; -.
DR   Proteomes; UP000002258; Chromosome 3.
DR   GO; GO:0008704; F:5-carboxymethyl-2-hydroxymuconate delta-isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.850.10; Fumarylacetoacetase-like, C-terminal domain; 1.
DR   InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR   InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR   PANTHER; PTHR11820; ACYLPYRUVASE; 1.
DR   PANTHER; PTHR11820:SF100; FUMARYLACETOACETATE HYDROLASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_4G01490); 1.
DR   Pfam; PF01557; FAA_hydrolase; 1.
DR   SUPFAM; SSF56529; FAH; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000313|EMBL:ABN65932.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002258}.
FT   DOMAIN          80..290
FT                   /note="Fumarylacetoacetase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01557"
SQ   SEQUENCE   293 AA;  31996 MW;  49D2EA813AFA4CFE CRC64;
     MTPTWKRLIR FVAQDGKTYR GEPIVSDADY DVGKQFLQGK QIMAKVITGD IFDNAVVTDV
     IKEVKTLLGP LTPDDVPMVK CVGLNFMKHI QEGGRTPPPF PSIFYKTSFS VADFGEDIPI
     PKIAQSKCDY EGELCIVIGK TGKNIKEEEA LSYVAGYVTG NDVSSRNWQK DPEFAGSVPQ
     WCFSKSFDKY APLGPALVSP QVIQNPGNLS LQTTVNGEIR QDANTDDLLF GVPRIISFIS
     QSTTLEMGTV IMTGTPSGVA LGMKPTPVYL QNGDVVEVAI DQIGTLSNKM VFE
//
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