ID H6BUF8_EXODN Unreviewed; 429 AA.
AC H6BUF8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Fumarylacetoacetase {ECO:0000256|ARBA:ARBA00012094, ECO:0000256|RuleBase:RU366008};
DE EC=3.7.1.2 {ECO:0000256|ARBA:ARBA00012094, ECO:0000256|RuleBase:RU366008};
DE AltName: Full=Fumarylacetoacetate hydrolase {ECO:0000256|RuleBase:RU366008};
GN ORFNames=HMPREF1120_03825 {ECO:0000313|EMBL:EHY55700.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY55700.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY55700.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY55700.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-fumarylacetoacetate + H2O = acetoacetate + fumarate + H(+);
CC Xref=Rhea:RHEA:10244, ChEBI:CHEBI:13705, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18034, ChEBI:CHEBI:29806; EC=3.7.1.2;
CC Evidence={ECO:0000256|RuleBase:RU366008};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU366008};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|RuleBase:RU366008};
CC -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC acetoacetate and fumarate from L-phenylalanine: step 6/6.
CC {ECO:0000256|ARBA:ARBA00004782, ECO:0000256|RuleBase:RU366008}.
CC -!- SIMILARITY: Belongs to the FAH family. {ECO:0000256|ARBA:ARBA00010211,
CC ECO:0000256|RuleBase:RU366008}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH226132; EHY55700.1; -; Genomic_DNA.
DR RefSeq; XP_009156161.1; XM_009157913.1.
DR AlphaFoldDB; H6BUF8; -.
DR STRING; 858893.H6BUF8; -.
DR GeneID; 20308464; -.
DR VEuPathDB; FungiDB:HMPREF1120_03825; -.
DR eggNOG; KOG2843; Eukaryota.
DR HOGENOM; CLU_026207_2_0_1; -.
DR InParanoid; H6BUF8; -.
DR OMA; YWTAAQQ; -.
DR OrthoDB; 275827at2759; -.
DR UniPathway; UPA00139; UER00341.
DR Proteomes; UP000007304; Unassembled WGS sequence.
DR GO; GO:0004334; F:fumarylacetoacetase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-UniRule.
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 Calcium {ECO:0000256|RuleBase:RU366008};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366008};
KW Magnesium {ECO:0000256|RuleBase:RU366008};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU366008};
KW Phenylalanine catabolism {ECO:0000256|ARBA:ARBA00023232,
KW ECO:0000256|RuleBase:RU366008};
KW Reference proteome {ECO:0000313|Proteomes:UP000007304};
KW Tyrosine catabolism {ECO:0000256|ARBA:ARBA00022878,
KW ECO:0000256|RuleBase:RU366008}.
FT DOMAIN 19..125
FT /note="Fumarylacetoacetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09298"
FT DOMAIN 133..404
FT /note="Fumarylacetoacetase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01557"
SQ SEQUENCE 429 AA; 46629 MW; A9261B37F93AED71 CRC64;
MAPLKSWFPI PKSSHFSLAN LPFGIISTAG KPTPRAAVAI GDHCLDLQEF SSSGAFQPLG
FDASVFSKPT LNDFAALGRP VHRAVRKYLQ DVFAENTSIP EVLQRNKELQ ERSLIRRDQV
TMHMPMHIGD YTDFYAGKNH AFNVGCLFRG PDNALQPNYT HLPVGYHGRA SSVVVSGTPI
TRPNGQILEN PAATPKAPTF SPCRRLDIEL ELGAFVCKGN AMGTNIPISE AADHIFGFVL
LNDWSARDIQ AWEYVPLGPF LAKNFGSTIS PWVVLTDALE PFRTTGIPNE TKLLPYLQEK
EEKNVYDIRL QVDIIPEGKE PTTILNSNGR HLLFSFAQML AHHTIGGCPM APGDLLGSGT
ISGKEPGTEG SMLEITQGGK QAIKLNGGVE RKFLEDGDTI TFYGVAGTEE TGLVGFGECS
GKILPAPKI
//
