ID I3Z967_BELBD Unreviewed; 415 AA.
AC I3Z967;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=fumarylacetoacetase {ECO:0000256|ARBA:ARBA00012094};
DE EC=3.7.1.2 {ECO:0000256|ARBA:ARBA00012094};
GN OrderedLocusNames=Belba_3275 {ECO:0000313|EMBL:AFL85785.1};
OS Belliella baltica (strain DSM 15883 / CIP 108006 / LMG 21964 / BA134).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Belliella.
OX NCBI_TaxID=866536 {ECO:0000313|EMBL:AFL85785.1, ECO:0000313|Proteomes:UP000006050};
RN [1] {ECO:0000313|Proteomes:UP000006050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15883 / CIP 108006 / LMG 21964 / BA134
RC {ECO:0000313|Proteomes:UP000006050};
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA Mikhailova N., Davenport K., Kyrpides N., Mavromatis K., Pagani I.,
RA Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Tindall B., Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Belliella baltica DSM 15883.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP003281; AFL85785.1; -; Genomic_DNA.
DR AlphaFoldDB; I3Z967; -.
DR STRING; 866536.Belba_3275; -.
DR KEGG; bbd:Belba_3275; -.
DR PATRIC; fig|866536.3.peg.3395; -.
DR eggNOG; COG0179; Bacteria.
DR HOGENOM; CLU_026207_2_0_10; -.
DR OrthoDB; 3766879at2; -.
DR UniPathway; UPA00139; UER00341.
DR Proteomes; UP000006050; Chromosome.
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 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AFL85785.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phenylalanine catabolism {ECO:0000256|ARBA:ARBA00023232};
KW Reference proteome {ECO:0000313|Proteomes:UP000006050};
KW Tyrosine catabolism {ECO:0000256|ARBA:ARBA00022878}.
FT DOMAIN 17..118
FT /note="Fumarylacetoacetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09298"
FT DOMAIN 125..393
FT /note="Fumarylacetoacetase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01557"
SQ SEQUENCE 415 AA; 46376 MW; 155247B0FB92E82C CRC64;
MVSWVPVSKN SDFTIYNLPF GIFETKRISA RAGIAIGDKI VDLSVLHDEG FFSDITQLPN
DIFLRDSLND FIALGKAVTK KVRERVQELL NDEKEDLKVH QCRGKAMVNR KEANLLLPVK
IGDYTDFYSS KEHATNVGTM FRDPDNALLP NWKHLPVGYH GRASSIIPSG VPIKRPKGQY
KDANMEAPEF GPSRRLDFEV ELAFITGKAT KMGDSISTAD AEDYIFGFVL FNDWSARDIQ
AWEYVPLGPF LGKNFASSIS PWIVTLEALD AFRVAGPKQE PEVLPYLQCE KDHGFDINLE
AYIQPEGKNS NKVCTSNYKY MYWNIAQQLA HHTVNGCNIN VGDMYASGTI SGPTEDSYGS
MLELAWKGTK PLTLEDGEER KFIEDGDTVI MKGYCEKEGI RVGFGEVSAK VLPAT
//
