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Database: UniProt
Entry: F2SDN6_TRIRC
LinkDB: F2SDN6_TRIRC
Original site: F2SDN6_TRIRC 
ID   F2SDN6_TRIRC            Unreviewed;       556 AA.
AC   F2SDN6;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 2.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=fumarylacetoacetase {ECO:0000256|ARBA:ARBA00012094};
DE            EC=3.7.1.2 {ECO:0000256|ARBA:ARBA00012094};
GN   ORFNames=TERG_00069 {ECO:0000313|EMBL:EGD83786.2};
OS   Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD83786.2, ECO:0000313|Proteomes:UP000008864};
RN   [1] {ECO:0000313|Proteomes:UP000008864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC       acetoacetate and fumarate from L-phenylalanine: step 6/6.
CC       {ECO:0000256|ARBA:ARBA00004782}.
CC   -!- SIMILARITY: Belongs to the FAH family. {ECO:0000256|ARBA:ARBA00010211}.
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DR   EMBL; GG700648; EGD83786.2; -; Genomic_DNA.
DR   AlphaFoldDB; F2SDN6; -.
DR   STRING; 559305.F2SDN6; -.
DR   VEuPathDB; FungiDB:TERG_00069; -.
DR   eggNOG; KOG2843; Eukaryota.
DR   HOGENOM; CLU_026207_2_0_1; -.
DR   InParanoid; F2SDN6; -.
DR   OMA; YWTAAQQ; -.
DR   OrthoDB; 275827at2759; -.
DR   UniPathway; UPA00139; UER00341.
DR   Proteomes; UP000008864; Unassembled WGS sequence.
DR   GO; GO:0004334; F:fumarylacetoacetase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.30.230; Fumarylacetoacetase, N-terminal domain; 1.
DR   Gene3D; 3.90.850.10; Fumarylacetoacetase-like, C-terminal domain; 1.
DR   InterPro; IPR005959; Fumarylacetoacetase.
DR   InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR   InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR   InterPro; IPR015377; Fumarylacetoacetase_N.
DR   InterPro; IPR036462; Fumarylacetoacetase_N_sf.
DR   NCBIfam; TIGR01266; fum_ac_acetase; 1.
DR   PANTHER; PTHR43069; FUMARYLACETOACETASE; 1.
DR   PANTHER; PTHR43069:SF2; FUMARYLACETOACETASE; 1.
DR   Pfam; PF01557; FAA_hydrolase; 1.
DR   Pfam; PF09298; FAA_hydrolase_N; 1.
DR   SUPFAM; SSF56529; FAH; 1.
DR   SUPFAM; SSF63433; Fumarylacetoacetate hydrolase, FAH, N-terminal domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Phenylalanine catabolism {ECO:0000256|ARBA:ARBA00023232};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008864};
KW   Tyrosine catabolism {ECO:0000256|ARBA:ARBA00022878}.
FT   DOMAIN          139..248
FT                   /note="Fumarylacetoacetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF09298"
FT   DOMAIN          256..548
FT                   /note="Fumarylacetoacetase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01557"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          72..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   556 AA;  60704 MW;  D7FDAE97D21ED25C CRC64;
     MSQIADEEDK ISRRSSRSLY APLSAASNER SWSSNVLLAR HLISSSLPSE RNPELAGAGR
     FRGHGRASWH QTGARKLWPS ATPPAKNNKQ EAMTKLNNTN CPSPERRKSR EKETAFLFFF
     FPFVPSVFVI PRDSPFSLAN IPFGIISTAA LADPRPAVAI GDYALDLFAF SSAGGFSKLS
     SFSSHIDVFT KPTLNDFAAL GRPVHREVRG YLQDIFRDST PYPEILKTNE DLKGKALVPL
     KDVTNHLPMK IGDYTDFYAG LNHAFNVGVL FRGPDNALQP NYKHLPVGYH GRASSVIVSG
     QPVRRPNGQI LANPAATPKV PIFSPCKKLD IELELAVFVG KGNKLGEPIP IDQAEDHLFG
     VVLMNDWSAR DIQAWEYVPL GPFNAKNFAT SITPWVVLMD ALEPFRSTGL AAEEGLDNLL
     PYLREKRAEN VYDMQLQFDL KPANSSCTST VAKTNAKNLL YSFAQMLTHH SVTGCNMNTG
     DLLGSGTISG KETGTLGSLL ENTQGGKQPM KLSDGSERVF LEDGDEVTLK GICGEEGSYV
     GFGNCTATIL PAPVIN
//
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