ID A0A0S3EX48_9SPHN Unreviewed; 436 AA.
AC A0A0S3EX48;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=fumarylacetoacetase {ECO:0000256|ARBA:ARBA00012094};
DE EC=3.7.1.2 {ECO:0000256|ARBA:ARBA00012094};
GN ORFNames=ATN00_06425 {ECO:0000313|EMBL:ALR19994.1};
OS Sphingobium baderi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1332080 {ECO:0000313|EMBL:ALR19994.1, ECO:0000313|Proteomes:UP000056968};
RN [1] {ECO:0000313|EMBL:ALR19994.1, ECO:0000313|Proteomes:UP000056968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DE-13 {ECO:0000313|EMBL:ALR19994.1,
RC ECO:0000313|Proteomes:UP000056968};
RA Cheng M., Meng Q., Yang Y., Chu C., Yan X., He J., Li S.;
RT "A Two-component Flavoprotein Monooxygenase System MeaXY Responsible for
RT para-Hydroxylation of 2-Methyl-6-ethylaniline and 2,6-Diethylaniline in
RT Sphingobium baderi DE-13.";
RL Submitted (NOV-2015) 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; CP013264; ALR19994.1; -; Genomic_DNA.
DR RefSeq; WP_062063332.1; NZ_CP013264.1.
DR AlphaFoldDB; A0A0S3EX48; -.
DR STRING; 1332080.ATN00_06425; -.
DR KEGG; sbd:ATN00_06425; -.
DR OrthoDB; 3766879at2; -.
DR UniPathway; UPA00139; UER00341.
DR Proteomes; UP000056968; 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phenylalanine catabolism {ECO:0000256|ARBA:ARBA00023232};
KW Reference proteome {ECO:0000313|Proteomes:UP000056968};
KW Tyrosine catabolism {ECO:0000256|ARBA:ARBA00022878}.
FT DOMAIN 28..124
FT /note="Fumarylacetoacetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09298"
FT DOMAIN 132..428
FT /note="Fumarylacetoacetase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01557"
SQ SEQUENCE 436 AA; 47143 MW; 1DF155469E12A173 CRC64;
MARVDFTHDP AARSWVESAN GHSDFPVQNL PLGLFSPSSE RPRGGVAIGT KILDLGAVAP
LLPQDAGDAA RLADSSTLNN LLAAGKDALR ALRHGLFRLL TDPAAEKSAR PALYPVDQCK
LHLPVHIGDY TDFYAGIHHA VNVGKLFRPD NPLLPNYKYV PIGYHGRASS VRLSGEDVVR
PNGQTMPPGA ETPLFGPCKR LDHELEMAIW VGRGNALGHP IPIKQAADHM AGLSILNDWS
ARDIQAWEYQ PLGPFLAKSF HSSVSPWIVT MDALGPYRIA QPARPESDPA PLPYLFDSDD
QQNGALNVTM EVYLSTARMQ ADGQPLHRLS QGSMTAMYWT VAQLFTHHSV NGCNLSTGDL
LGTGTLSGAT DESKGSLLEL TRGGKVPIRL PNGESRTFLE DGDEIVITAF AEASGFVRIG
FGECRARIAP SPQWEL
//
