NAGL_RALSP
ID NAGL_RALSP Reviewed; 212 AA.
AC O86043;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Maleylpyruvate isomerase {ECO:0000303|PubMed:18824004, ECO:0000312|EMBL:AAD12621.1};
DE Short=MPI {ECO:0000303|PubMed:18824004};
DE EC=5.2.1.4 {ECO:0000269|PubMed:11133965};
DE AltName: Full=Naphthalene degradation protein L;
GN Name=nagL {ECO:0000312|EMBL:AAD12621.1};
OS Ralstonia sp.
OG Plasmid pWWU2 {ECO:0000312|EMBL:AAD12621.1}.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=54061;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAD12621.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=U2 {ECO:0000312|EMBL:AAD12621.1};
RX PubMed=11133965; DOI=10.1128/jb.183.2.700-708.2001;
RA Zhou N.Y., Fuenmayor S.L., Williams P.A.;
RT "nag genes of Ralstonia (formerly Pseudomonas) sp. strain U2 encoding
RT enzymes for gentisate catabolism.";
RL J. Bacteriol. 183:700-708(2001).
RN [2] {ECO:0000305, ECO:0000312|PDB:2JL4}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE,
RP COFACTOR, AND SUBUNIT.
RC STRAIN=U2 {ECO:0000269|PubMed:18824004};
RX PubMed=18824004; DOI=10.1016/j.jmb.2008.09.028;
RA Marsh M., Shoemark D.K., Jacob A., Robinson C., Cahill B., Zhou N.Y.,
RA Williams P.A., Hadfield A.T.;
RT "Structure of bacterial glutathione-S-transferase maleyl pyruvate isomerase
RT and implications for mechanism of isomerisation.";
RL J. Mol. Biol. 384:165-177(2008).
CC -!- FUNCTION: Catalyzes the GSH-dependent isomerization of maleylpyruvate
CC to fumarylpyruvate which is subsequently processed by NagK to form
CC pyruvate and fumarate. {ECO:0000269|PubMed:11133965}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-maleylpyruvate = 3-fumarylpyruvate; Xref=Rhea:RHEA:17393,
CC ChEBI:CHEBI:16727, ChEBI:CHEBI:16854; EC=5.2.1.4;
CC Evidence={ECO:0000269|PubMed:11133965};
CC -!- COFACTOR:
CC Name=glutathione; Xref=ChEBI:CHEBI:57925;
CC Evidence={ECO:0000269|PubMed:18824004};
CC -!- PATHWAY: Aromatic compound metabolism; naphthalene degradation.
CC {ECO:0000269|PubMed:11133965}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18824004}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Zeta family. {ECO:0000255}.
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DR EMBL; AF036940; AAD12621.1; -; Genomic_DNA.
DR PDB; 2JL4; X-ray; 2.30 A; A/B=1-212.
DR PDB; 2V6K; X-ray; 1.30 A; A/B=1-212.
DR PDBsum; 2JL4; -.
DR PDBsum; 2V6K; -.
DR AlphaFoldDB; O86043; -.
DR SMR; O86043; -.
DR KEGG; ag:AAD12621; -.
DR BioCyc; MetaCyc:MON-14770; -.
DR UniPathway; UPA00082; -.
DR EvolutionaryTrace; O86043; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0050077; F:maleylpyruvate isomerase activity; IDA:UniProtKB.
DR GO; GO:0009072; P:aromatic amino acid family metabolic process; IEA:InterPro.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:1901170; P:naphthalene catabolic process; IDA:UniProtKB.
DR CDD; cd03191; GST_C_Zeta; 1.
DR CDD; cd03042; GST_N_Zeta; 1.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR005955; GST_Zeta.
DR InterPro; IPR034330; GST_Zeta_C.
DR InterPro; IPR034333; GST_Zeta_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF13417; GST_N_3; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01262; maiA; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aromatic hydrocarbons catabolism; Isomerase; Plasmid;
KW Pyruvate.
FT CHAIN 1..212
FT /note="Maleylpyruvate isomerase"
FT /id="PRO_0000421469"
FT DOMAIN 1..80
FT /note="GST N-terminal"
FT /evidence="ECO:0000255"
FT DOMAIN 85..212
FT /note="GST C-terminal"
FT /evidence="ECO:0000255"
FT BINDING 9..11
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:18824004"
FT BINDING 38
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:18824004"
FT BINDING 52
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:18824004"
FT BINDING 64..65
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:18824004"
FT BINDING 102..104
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:18824004"
FT BINDING 108..110
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:18824004"
FT BINDING 176
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:18824004"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:2V6K"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:2V6K"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:2V6K"
FT TURN 33..36
FT /evidence="ECO:0007829|PDB:2V6K"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:2V6K"
FT HELIX 41..46
FT /evidence="ECO:0007829|PDB:2V6K"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:2V6K"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2V6K"
FT HELIX 65..75
FT /evidence="ECO:0007829|PDB:2V6K"
FT HELIX 86..102
FT /evidence="ECO:0007829|PDB:2V6K"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:2V6K"
FT HELIX 109..119
FT /evidence="ECO:0007829|PDB:2V6K"
FT HELIX 123..147
FT /evidence="ECO:0007829|PDB:2V6K"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:2V6K"
FT HELIX 162..176
FT /evidence="ECO:0007829|PDB:2V6K"
FT HELIX 185..194
FT /evidence="ECO:0007829|PDB:2V6K"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:2V6K"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:2V6K"
SQ SEQUENCE 212 AA; 23505 MW; 6554F3B95591EAEE CRC64;
MKLYNFWRSG TSHRLRIALN LKGVPYEYLA VHLGKEEHLK DAFKALNPQQ LVPALDTGAQ
VLIQSPAIIE WLEEQYPTPA LLPADADGRQ RVRALAAIVG CDIHPINNRR ILEYLRKTFG
ADEAAINAWC GTWISAGFDA YEALLAVDPK RGRYSFGDTP TLADCYLVPQ VESARRFQVD
LTPYPLIRAV DAACGELDAF RRAAPAAQPD SA
