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P37352

- HPCE_ECOLX

UniProt

P37352 - HPCE_ECOLX

Protein

Homoprotocatechuate catabolism bifunctional isomerase/decarboxylase

Gene

hpcE

Organism
Escherichia coli
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 2 (01 Mar 2004)
      Previous versions | rss
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    Functioni

    Decarboxylates OPET (5-oxo-pent-3-ene-1,2,5-tricarboxylic acid) into HHDD (2-hydroxy-hept-2,4-diene-1,7-dioate) and isomerizes it to OHED (2-oxo-hept-3-ene-1,7-dioate).1 Publication

    Catalytic activityi

    5-carboxymethyl-2-hydroxymuconate = 5-carboxy-2-oxohept-3-enedioate.
    5-oxopent-3-ene-1,2,5-tricarboxylate = 2-oxohept-3-enedioate + CO2.

    Cofactori

    Magnesium.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi276 – 2761Divalent metal cation
    Metal bindingi278 – 2781Divalent metal cation
    Metal bindingi307 – 3071Divalent metal cation

    GO - Molecular functioni

    1. 5-carboxymethyl-2-hydroxymuconate delta-isomerase activity Source: UniProtKB-EC
    2. 5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase activity Source: UniProtKB-EC
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. 4-hydroxyphenylacetate catabolic process Source: InterPro

    Keywords - Molecular functioni

    Isomerase, Lyase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolism

    Keywords - Ligandi

    Calcium, Magnesium, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00208; UER00419.
    UPA00208; UER00420.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Homoprotocatechuate catabolism bifunctional isomerase/decarboxylase
    Including the following 2 domains:
    2-hydroxyhepta-2,4-diene-1,7-dioate isomerase (EC:5.3.3.10)
    Short name:
    HHDD isomerase
    Alternative name(s):
    5-carboxymethyl-2-hydroxymuconate Delta-isomerase
    5-carboxymethyl-2-oxo-hex-3-ene-1,7-dioate decarboxylase (EC:4.1.1.68)
    Alternative name(s):
    5-oxopent-3-ene-1,2,5-tricarboxylate decarboxylase
    Short name:
    OPET decarboxylase
    Gene namesi
    Name:hpcE
    OrganismiEscherichia coli
    Taxonomic identifieri562 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 427427Homoprotocatechuate catabolism bifunctional isomerase/decarboxylasePRO_0000156835Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    Secondary structure

    1
    427
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 106
    Helixi13 – 197
    Helixi22 – 243
    Turni26 – 283
    Beta strandi36 – 405
    Helixi42 – 443
    Beta strandi52 – 543
    Beta strandi56 – 583
    Beta strandi64 – 707
    Beta strandi74 – 763
    Helixi79 – 857
    Beta strandi86 – 938
    Beta strandi102 – 1043
    Helixi107 – 1104
    Beta strandi116 – 1183
    Beta strandi131 – 1366
    Beta strandi139 – 1457
    Helixi146 – 1483
    Beta strandi149 – 1513
    Helixi153 – 1619
    Beta strandi171 – 1733
    Beta strandi188 – 1936
    Beta strandi199 – 2057
    Helixi206 – 2083
    Beta strandi219 – 2213
    Beta strandi225 – 2306
    Beta strandi249 – 2524
    Helixi254 – 2563
    Beta strandi262 – 2665
    Beta strandi277 – 2837
    Beta strandi287 – 2893
    Turni292 – 2943
    Helixi295 – 2984
    Beta strandi299 – 3068
    Helixi311 – 3133
    Beta strandi316 – 3205
    Helixi322 – 3254
    Beta strandi331 – 3333
    Helixi340 – 3423
    Beta strandi350 – 3556
    Beta strandi358 – 3647
    Helixi365 – 3673
    Beta strandi368 – 3703
    Helixi372 – 3809
    Beta strandi390 – 3923
    Beta strandi405 – 4106
    Turni411 – 4133
    Beta strandi414 – 4229
    Helixi423 – 4264

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GTTX-ray1.70A/B/C/D1-427[»]
    1I7OX-ray1.70A/B/C/D1-427[»]
    ProteinModelPortaliP37352.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP37352.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati1 – 202202ApproximateAdd
    BLAST
    Repeati203 – 405203ApproximateAdd
    BLAST

    Sequence similaritiesi

    Belongs to the FAH family.Curated

    Keywords - Domaini

    Repeat

    Family and domain databases

    Gene3Di3.90.850.10. 2 hits.
    InterProiIPR002529. Fumarylacetoacetase_C.
    IPR011234. Fumarylacetoacetase_C-rel.
    IPR012684. HPA_isomer/decarb_C.
    IPR012686. HPA_isomer/decarb_N.
    [Graphical view]
    PfamiPF01557. FAA_hydrolase. 2 hits.
    [Graphical view]
    SUPFAMiSSF56529. SSF56529. 2 hits.
    TIGRFAMsiTIGR02303. HpaG-C-term. 1 hit.
    TIGR02305. HpaG-N-term. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P37352-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKGTIFAVAL NHRSQLDAWQ EAFQQSPIKA PPKTAVWFIK PRNTVIGCGE    50
    PIPFPQGENL LSGATVALIV GKTATKVREE DAAEYIAGYA LANDVSLPEE 100
    SFYRPAIKAK CRDGFCPIGE TVALSNVDNL TIYTEINGRP ADHWNTSDLQ 150
    RNAAQLLSAL SEFATLNPGD AILLGTPQAR VEIQPGDRVR VLAEGFPPLE 200
    NPVVDEREVT TRKSFPTLPH PHGTLFALGL NYADHASELE FKPPEEPLVF 250
    LKAPNTLTGD NQTSVRPNNI EYMHYEAELV VVIGKQARNV SEADAMDYVA 300
    GYTVCNDYAI RDYLENYYRP NLRVKSRDGL TPMLSTIVPK EAIPDPHNLT 350
    LRTFVNGELR QQGTTADLIF SVPFLIAYLS EFMTLNPGDM IATGTPKGLS 400
    DVGDEVVVEV EGVGRLVNRI VSEETAK 427
    Length:427
    Mass (Da):46,878
    Last modified:March 1, 2004 - v2
    Checksum:iD4CF62027017B295
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75028 Genomic DNA. Translation: CAA52936.2.
    S56952 Genomic DNA. Translation: AAB25803.1.
    PIRiS38348.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75028 Genomic DNA. Translation: CAA52936.2 .
    S56952 Genomic DNA. Translation: AAB25803.1 .
    PIRi S38348.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GTT X-ray 1.70 A/B/C/D 1-427 [» ]
    1I7O X-ray 1.70 A/B/C/D 1-427 [» ]
    ProteinModelPortali P37352.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00208 ; UER00419 .
    UPA00208 ; UER00420 .

    Miscellaneous databases

    EvolutionaryTracei P37352.

    Family and domain databases

    Gene3Di 3.90.850.10. 2 hits.
    InterProi IPR002529. Fumarylacetoacetase_C.
    IPR011234. Fumarylacetoacetase_C-rel.
    IPR012684. HPA_isomer/decarb_C.
    IPR012686. HPA_isomer/decarb_N.
    [Graphical view ]
    Pfami PF01557. FAA_hydrolase. 2 hits.
    [Graphical view ]
    SUPFAMi SSF56529. SSF56529. 2 hits.
    TIGRFAMsi TIGR02303. HpaG-C-term. 1 hit.
    TIGR02305. HpaG-N-term. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Purification, nucleotide sequence and some properties of a bifunctional isomerase/decarboxylase from the homoprotocatechuate degradative pathway of Escherichia coli C."
      Roper D.I., Cooper R.A.
      Eur. J. Biochem. 217:575-580(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20, FUNCTION.
      Strain: C.
    2. Roper D.I.
      Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO C-TERMINUS.
    3. "The Escherichia coli C homoprotocatechuate degradative operon: hpc gene order, direction of transcription and control of expression."
      Roper D.I., Fawcett T., Cooper R.A.
      Mol. Gen. Genet. 237:241-250(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
      Strain: C.
    4. "The crystal structure of HpcE, a bifunctional decarboxylase/isomerase with a multifunctional fold."
      Tame J.R.H., Namba K., Dodson E.J., Roper D.I.
      Biochemistry 41:2982-2989(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), SUBUNIT, COFACTOR.

    Entry informationi

    Entry nameiHPCE_ECOLX
    AccessioniPrimary (citable) accession number: P37352
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: March 1, 2004
    Last modified: October 1, 2014
    This is version 73 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing, Multifunctional enzyme

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3