ID   D2YW46_OLEAN            Unreviewed;       224 AA.
AC   D2YW46;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Putative fumarylacetoacetate isomerase/hydrolase {ECO:0000313|PDB:3V77};
OS   Oleispira antarctica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Oleispira.
OX   NCBI_TaxID=188908;
RN   [1] {ECO:0007829|PDB:3V77}
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH ZINC.
RX   PubMed=23877221; DOI=10.1038/ncomms3156;
RA   Kube M., Chernikova T.N., Al-Ramahi Y., Beloqui A., Lopez-Cortez N.,
RA   Guazzaroni M.E., Heipieper H.J., Klages S., Kotsyurbenko O.R., Langer I.,
RA   Nechitaylo T.Y., Lunsdorf H., Fernandez M., Juarez S., Ciordia S.,
RA   Singer A., Kagan O., Egorova O., Petit P.A., Stogios P., Kim Y.,
RA   Tchigvintsev A., Flick R., Denaro R., Genovese M., Albar J.P., Reva O.N.,
RA   Martinez-Gomariz M., Tran H., Ferrer M., Savchenko A., Yakunin A.F.,
RA   Yakimov M.M., Golyshina O.V., Reinhardt R., Golyshin P.N.;
RT   "Genome sequence and functional genomic analysis of the oil-degrading
RT   bacterium Oleispira antarctica.";
RL   Nat. Commun. 4:2156-2156(2013).
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   PDB; 3V77; X-ray; 2.10 A; A/B/C/D/E/F=1-224.
DR   PDBsum; 3V77; -.
DR   AlphaFoldDB; D2YW46; -.
DR   SMR; D2YW46; -.
DR   EvolutionaryTrace; D2YW46; -.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; 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; PTHR11820; ACYLPYRUVASE; 1.
DR   PANTHER; PTHR11820:SF7; ACYLPYRUVASE FAHD1, MITOCHONDRIAL; 1.
DR   Pfam; PF01557; FAA_hydrolase; 1.
DR   SUPFAM; SSF56529; FAH; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3V77};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0007829|PDB:3V77};
KW   Zinc {ECO:0007829|PDB:3V77}.
FT   DOMAIN          17..209
FT                   /note="Fumarylacetoacetase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01557"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0007829|PDB:3V77"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0007829|PDB:3V77"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0007829|PDB:3V77"
SQ   SEQUENCE   224 AA;  23979 MW;  B79DD34D2E573058 CRC64;
     MAELILNQRP YPRDLGKIVC VGRNYAAHAK ELNNPIPSSP ILFIKPASSA VPFGPVFSIP
     KDQGSVHHEL EIAILIGKAL SRASTEQVAE SIAGIGLGLD LTLRDVQDQL KEKGHPWERA
     KSFDGACPLT EFVAVNLASE DEWQAIGLTL EKNGQFQQQG SSAEMLFPIL PLIAHMSEHF
     SLQPGDVILT GTPAGVGPLE VGDSLSAKLS LEDNVLLTCD GVVI
//