ID A0A0C2FE76_9ACTN Unreviewed; 406 AA.
AC A0A0C2FE76;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=fumarylacetoacetase {ECO:0000256|ARBA:ARBA00012094};
DE EC=3.7.1.2 {ECO:0000256|ARBA:ARBA00012094};
GN ORFNames=LP52_18710 {ECO:0000313|EMBL:KIH97509.1};
OS Streptomonospora alba.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Streptomonospora.
OX NCBI_TaxID=183763 {ECO:0000313|EMBL:KIH97509.1, ECO:0000313|Proteomes:UP000031675};
RN [1] {ECO:0000313|Proteomes:UP000031675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 90003 {ECO:0000313|Proteomes:UP000031675};
RX PubMed=25601074; DOI=10.1016/j.chembiol.2014.11.017;
RA Metelev M., Tietz J.I., Melby J.O., Blair P.M., Zhu L., Livnat I.,
RA Severinov K., Mitchell D.A.;
RT "Structure, bioactivity, and resistance mechanism of streptomonomicin, an
RT unusual lasso Peptide from an understudied halophilic actinomycete.";
RL Chem. Biol. 22:241-250(2015).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIH97509.1}.
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DR EMBL; JROO01000037; KIH97509.1; -; Genomic_DNA.
DR RefSeq; WP_040275492.1; NZ_JROO01000037.1.
DR AlphaFoldDB; A0A0C2FE76; -.
DR STRING; 183763.LP52_18710; -.
DR OrthoDB; 3766879at2; -.
DR UniPathway; UPA00139; UER00341.
DR Proteomes; UP000031675; 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 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:UP000031675};
KW Tyrosine catabolism {ECO:0000256|ARBA:ARBA00022878}.
FT DOMAIN 18..111
FT /note="Fumarylacetoacetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF09298"
FT DOMAIN 119..401
FT /note="Fumarylacetoacetase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01557"
SQ SEQUENCE 406 AA; 43998 MW; D5B5A7CD56DBE866 CRC64;
MPHTWLGIAD DDPFGPATLP YGVFSTGDGG RPRVGVAAGE WVLDLAAAAH AQDAPFAEIV
DAPVLNPLMA AGPQTWRQVR ESLTAWLTDP AYEDTLNRYL FERARVRMHL PFEVGDYVDF
YSSEHHATNL GRILRPGQPP LSPNWKHLPL GYHGRSGTVV VSGTEIVRPM GQRKPPSAGE
PEFGPSTRLD IEAEVGFVVG VPAPGGRVPV SDFTEHVFGA FLVNDWSARD LQAWENMPLG
PFLGKSFATS VSPWVVPLEA LQEARVDPPE RDPEPLEYLR DAPGEPWGLD LRLEVRINGH
LVARPPFSRM YWTPAQQLAH LTVNGASLRT GDIYASGTVS GSEKEERGSL IELSWNGEEP
IELPDGSTRT FLEDGDTVTI TATTSGPGAE VIGLGEVAGR VLPAQG
//
