ID B8J605_ANAD2 Unreviewed; 220 AA. AC B8J605; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 90. DE SubName: Full=Maleylacetoacetate isomerase {ECO:0000313|EMBL:ACL66900.1}; GN OrderedLocusNames=A2cp1_3570 {ECO:0000313|EMBL:ACL66900.1}; OS Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258). OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae; OC Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=455488 {ECO:0000313|EMBL:ACL66900.1, ECO:0000313|Proteomes:UP000007089}; RN [1] {ECO:0000313|EMBL:ACL66900.1, ECO:0000313|Proteomes:UP000007089} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2CP-1 / ATCC BAA-258 {ECO:0000313|Proteomes:UP000007089}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., RA Beliaev A.S., Richardson P.; RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1."; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0007829|PDB:4IGJ} RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS). RA Kim J., Toro R., Bhosle R., Al Obaidi N.F., Morisco L.L., Wasserman S.R., RA Sojitra S., Washington E., Scott Glenn A., Chowdhury S., Evans B., RA Hammonds J., Hillerich B., Love J., Seidel R.D., Imker H.J., RA Armstrong R.N., Gerlt J.A., Almo S.C.; RT "Crystal structure of Maleylacetoacetate isomerase from Anaeromyxobacter RT dehalogenans 2CP-1, target EFI-507175."; RL Submitted (DEC-2012) to the PDB data bank. RN [3] {ECO:0007829|PDB:4KAE} RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS). RG Enzyme Function Initiative (EFI); RA Kim J., Toro R., Bhosle R., Al Obaidi N.F., Morisco L.L., Wasserman S.R., RA Sojitra S., Washington E., Scott Glenn A., Chowdhury S., Evans B., RA Hammonds J., Hillerich B., Love J., Seidel R.D., Imker H.J., Stead M., RA Gerlt J.A., Almo S.C.; RT "Crystal structure of Maleylacetoacetate isomerase from Anaeromyxobacter RT dehalogenans 2CP-1, TARGET EFI-507175, with bound dicarboxyethyl RT glutathione and citrate in the active site."; RL Submitted (APR-2013) to the PDB data bank. RN [4] {ECO:0007829|PDB:4KDY} RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE. RG Enzyme Function Initiative (EFI); RA Kim J., Toro R., Bhosle R., Al Obaidi N.F., Morisco L.L., Wasserman S.R., RA Sojitra S., Washington E., Scott Glenn A., Chowdhury S., Evans B., RA Hammonds J., Hillerich B., Love J., Seidel R.D., Imker H.J., Stead M., RA Gerlt J.A., Almo S.C.; RT "Crystal structure of maleylacetoacetate isomerase from Anaeromyxobacter RT dehalogenans 2CP-1, Target EFI-507175, with bound GSH in the active site."; RL Submitted (APR-2013) to the PDB data bank. CC -!- SIMILARITY: Belongs to the GST superfamily. Zeta family. CC {ECO:0000256|ARBA:ARBA00010007}. 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 EMBL; CP001359; ACL66900.1; -; Genomic_DNA. DR RefSeq; WP_015934684.1; NC_011891.1. DR PDB; 4IGJ; X-ray; 1.48 A; A/B=1-220. DR PDB; 4KAE; X-ray; 1.50 A; A/B=1-220. DR PDB; 4KDY; X-ray; 1.50 A; A/B=1-220. DR PDBsum; 4IGJ; -. DR PDBsum; 4KAE; -. DR PDBsum; 4KDY; -. DR AlphaFoldDB; B8J605; -. DR SMR; B8J605; -. DR KEGG; acp:A2cp1_3570; -. DR HOGENOM; CLU_011226_20_1_7; -. DR Proteomes; UP000007089; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0009072; P:aromatic amino acid metabolic process; IEA:InterPro. DR CDD; cd03191; GST_C_Zeta; 1. DR CDD; cd03042; GST_N_Zeta; 1. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 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 NCBIfam; TIGR01262; maiA; 1. DR PANTHER; PTHR42673; MALEYLACETOACETATE ISOMERASE; 1. DR PANTHER; PTHR42673:SF4; MALEYLACETOACETATE ISOMERASE; 1. DR Pfam; PF13410; GST_C_2; 1. DR Pfam; PF02798; GST_N; 1. DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1. DR SFLD; SFLDG00358; Main_(cytGST); 1. DR SUPFAM; SSF47616; GST C-terminal domain-like; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS50405; GST_CTER; 1. DR PROSITE; PS50404; GST_NTER; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:4IGJ, ECO:0007829|PDB:4KAE}; KW Isomerase {ECO:0000313|EMBL:ACL66900.1}. FT DOMAIN 1..86 FT /note="GST N-terminal" FT /evidence="ECO:0000259|PROSITE:PS50404" FT DOMAIN 91..214 FT /note="GST C-terminal" FT /evidence="ECO:0000259|PROSITE:PS50405" FT REGION 201..220 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 13 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4KDY" FT BINDING 16 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4KDY" FT BINDING 16 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4KDY" FT BINDING 38 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4KDY" FT BINDING 42 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4KDY" FT BINDING 52 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4KDY" FT BINDING 54 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4KDY" FT BINDING 54 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4KDY" FT BINDING 71 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4KDY" FT BINDING 71 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4KDY" FT BINDING 106 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4KDY" FT BINDING 110 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4KDY" FT BINDING 139 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4KDY" SQ SEQUENCE 220 AA; 24997 MW; C7372DFECE10BD63 CRC64; MTLRLYSYWR SSSAWRVRLG LALKGLAYEY RAVDLLAQEQ FQAAHQARNP MSQVPVLEVE EDGRTHLLVQ SMAILEWLEE RHPEPALLPP DLWGRARVRA LAEHVNSGTQ PMQNALVLRM LREKVPGWDR EWARFFIARG LAALETAVRD GAGRFSHGDA PTLADCYLVP QLYNARRFGL DLEPYPTLRR VDEACAALAP FQAAHPDRQP DAPPPDRRTP //