ID   HPCD_ECOLX              Reviewed;         126 AA.
AC   Q05354;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-MAY-2023, entry version 89.
DE   RecName: Full=5-carboxymethyl-2-hydroxymuconate Delta-isomerase;
DE            EC=5.3.3.10 {ECO:0000269|PubMed:2194841};
DE   AltName: Full=5-carboxymethyl-2-hydroxymuconic acid isomerase {ECO:0000303|PubMed:2194841};
DE            Short=CHM isomerase {ECO:0000303|PubMed:2194841};
DE            Short=CHMI;
GN   Name=hpcD;
OS   Escherichia coli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, FUNCTION,
RP   CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=C;
RX   PubMed=2194841; DOI=10.1016/0014-5793(90)81507-k;
RA   Roper D.I., Cooper R.A.;
RT   "Purification, some properties and nucleotide sequence of 5-carboxymethyl-
RT   2-hydroxymuconate isomerase of Escherichia coli C.";
RL   FEBS Lett. 266:63-66(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RC   STRAIN=C;
RX   PubMed=2261999; DOI=10.1016/0014-5793(90)81437-s;
RA   Roper D.I., Cooper R.A.;
RT   "Subcloning and nucleotide sequence of the 3,4-dihydroxyphenylacetate
RT   (homoprotocatechuate) 2,3-dioxygenase gene from Escherichia coli C.";
RL   FEBS Lett. 275:53-57(1990).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SUBUNIT.
RX   PubMed=8547259; DOI=10.1021/bi951732k;
RA   Subramanya H.S., Roper D.I., Dauter Z., Dodson E.J., Davies G.J.,
RA   Wilson K.S., Wigley D.B.;
RT   "Enzymatic ketonization of 2-hydroxymuconate: specificity and mechanism
RT   investigated by the crystal structures of two isomerases.";
RL   Biochemistry 35:792-802(1996).
CC   -!- FUNCTION: Transforms 5-carboxymethyl-2-hydroxy-muconic acid (CHM) into
CC       5-oxo-pent-3-ene-1,2,5-tricarboxylic acid (OPET).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,4Z)-5-hydroxypenta-2,4-diene-1,2,5-tricarboxylate =
CC         (3E,5R)-5-carboxy-2-oxohept-3-enedioate; Xref=Rhea:RHEA:18813,
CC         ChEBI:CHEBI:47961, ChEBI:CHEBI:87491; EC=5.3.3.10;
CC         Evidence={ECO:0000269|PubMed:2194841};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.6. {ECO:0000269|PubMed:2194841};
CC   -!- PATHWAY: Aromatic compound metabolism; 4-hydroxyphenylacetate
CC       degradation; pyruvate and succinate semialdehyde from 4-
CC       hydroxyphenylacetate: step 4/7.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:8547259}.
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DR   EMBL; X53666; CAA37707.1; -; Genomic_DNA.
DR   EMBL; X55200; CAA38986.1; -; Genomic_DNA.
DR   PDB; 1OTG; X-ray; 2.10 A; A/B/C=2-126.
DR   PDBsum; 1OTG; -.
DR   AlphaFoldDB; Q05354; -.
DR   SMR; Q05354; -.
DR   STRING; 585034.ECIAI1_4572; -.
DR   UniPathway; UPA00208; UER00419.
DR   EvolutionaryTrace; Q05354; -.
DR   GO; GO:0008704; F:5-carboxymethyl-2-hydroxymuconate delta-isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00580; CHMI; 1.
DR   Gene3D; 3.30.429.10; Macrophage Migration Inhibitory Factor; 1.
DR   InterPro; IPR004220; 5-COMe_2-OHmuconate_Isoase.
DR   InterPro; IPR014347; Tautomerase/MIF_sf.
DR   PANTHER; PTHR37950; 4-HYDROXYPHENYLACETATE CATABOLISM PROTEIN; 1.
DR   PANTHER; PTHR37950:SF1; 4-HYDROXYPHENYLACETATE CATABOLISM PROTEIN; 1.
DR   Pfam; PF02962; CHMI; 1.
DR   SUPFAM; SSF55331; Tautomerase/MIF; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Aromatic hydrocarbons catabolism; Direct protein sequencing;
KW   Isomerase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2194841"
FT   CHAIN           2..126
FT                   /note="5-carboxymethyl-2-hydroxymuconate Delta-isomerase"
FT                   /id="PRO_0000084041"
FT   ACT_SITE        2
FT                   /note="Proton acceptor; via imino nitrogen"
FT   STRAND          3..9
FT                   /evidence="ECO:0007829|PDB:1OTG"
FT   HELIX           10..12
FT                   /evidence="ECO:0007829|PDB:1OTG"
FT   HELIX           13..16
FT                   /evidence="ECO:0007829|PDB:1OTG"
FT   HELIX           18..30
FT                   /evidence="ECO:0007829|PDB:1OTG"
FT   STRAND          33..35
FT                   /evidence="ECO:0007829|PDB:1OTG"
FT   HELIX           37..39
FT                   /evidence="ECO:0007829|PDB:1OTG"
FT   STRAND          41..52
FT                   /evidence="ECO:0007829|PDB:1OTG"
FT   STRAND          59..68
FT                   /evidence="ECO:0007829|PDB:1OTG"
FT   HELIX           74..91
FT                   /evidence="ECO:0007829|PDB:1OTG"
FT   HELIX           93..96
FT                   /evidence="ECO:0007829|PDB:1OTG"
FT   STRAND          99..109
FT                   /evidence="ECO:0007829|PDB:1OTG"
FT   STRAND          112..119
FT                   /evidence="ECO:0007829|PDB:1OTG"
FT   HELIX           120..124
FT                   /evidence="ECO:0007829|PDB:1OTG"
SQ   SEQUENCE   126 AA;  14215 MW;  7494E625A76BBCEC CRC64;
     MPHFIVECSD NIREEADLPG LFAKVNPTLA ATGIFPLAGI RSRVHWVDTW QMADGQHDYA
     SVHMTLKIGA GRSLESRQQA GEMLFELIKT HFAALMESRL LALSFEIEEL HPTLNFKQNN
     VHALFK
//