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Database: UniProt
Entry: A0A0S8C152_9PROT
LinkDB: A0A0S8C152_9PROT
Original site: A0A0S8C152_9PROT 
ID   A0A0S8C152_9PROT        Unreviewed;       302 AA.
AC   A0A0S8C152;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Fumarylacetoacetate hydrolase {ECO:0000313|EMBL:KPK17586.1};
GN   ORFNames=AMJ67_12835 {ECO:0000313|EMBL:KPK17586.1};
OS   Betaproteobacteria bacterium SG8_41.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1703391 {ECO:0000313|EMBL:KPK17586.1, ECO:0000313|Proteomes:UP000051544};
RN   [1] {ECO:0000313|EMBL:KPK17586.1, ECO:0000313|Proteomes:UP000051544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_41 {ECO:0000313|EMBL:KPK17586.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
CC   -!- SIMILARITY: Belongs to the FAH family. {ECO:0000256|ARBA:ARBA00010211}.
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:KPK17586.1}.
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DR   EMBL; LJTT01000050; KPK17586.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8C152; -.
DR   STRING; 1703391.AMJ67_12835; -.
DR   PATRIC; fig|1703391.3.peg.1355; -.
DR   Proteomes; UP000051544; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.850.10; Fumarylacetoacetase-like, C-terminal domain; 1.
DR   InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR   InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR   PANTHER; PTHR42796:SF4; FUMARYLACETOACETATE HYDROLASE DOMAIN-CONTAINING PROTEIN 2A; 1.
DR   PANTHER; PTHR42796; FUMARYLACETOACETATE HYDROLASE DOMAIN-CONTAINING PROTEIN 2A-RELATED; 1.
DR   Pfam; PF01557; FAA_hydrolase; 1.
DR   SUPFAM; SSF56529; FAH; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:KPK17586.1}.
FT   DOMAIN          86..266
FT                   /note="Fumarylacetoacetase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01557"
FT   REGION          64..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          281..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..302
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   302 AA;  33425 MW;  93EC71CF7E9B7118 CRC64;
     MKLAFFDDFK LGVLKGETVV DVSQVVRDIP HTGPHNLING VIERFADCRS RLEKAAADGK
     GVPVDQVRFR PPLPRPHNIE DGTRSEPAPI NAFHKSPSGV IGDGDTMVLP DVPATIFEGE
     AEVAVVIGKR AQNVRAADAM SHVFGYLNFI DGSARGLPPS GNTFYQMKSR DTFAPMGPYI
     VTADEIKDPH NLQIRLWVNG TLMQNFNTSD MAHKIPRCIE WVSSIHTLEP GDVLASGTNH
     RGLSPFQDGD LVELETECLG RLRIKVRDDL KRTWARVTRL ERQQKGQEGQ TPQLTGKYAK
     QP
//
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