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Protein

4-hydroxy-2-oxo-heptane-1,7-dioate aldolase

Gene

hpcH

Organism
Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible retro-aldol cleavage of 4-hydroxy-2-ketoheptane-1,7-dioate (HKHD) to pyruvate and succinic semialdehyde.UniRule annotation

Catalytic activityi

4-hydroxy-2-oxoheptanedioate = pyruvate + succinate semialdehyde.UniRule annotation

Cofactori

a divalent metal cationUniRule annotationNote: Binds 1 divalent metal cation per subunit.UniRule annotation

Pathwayi: 4-hydroxyphenylacetate degradation

This protein is involved in step 7 of the subpathway that synthesizes pyruvate and succinate semialdehyde from 4-hydroxyphenylacetate.UniRule annotation
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. no protein annotated in this organism
  6. no protein annotated in this organism
  7. 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpcH)
This subpathway is part of the pathway 4-hydroxyphenylacetate degradation, which is itself part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate and succinate semialdehyde from 4-hydroxyphenylacetate, the pathway 4-hydroxyphenylacetate degradation and in Aromatic compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei45Proton acceptorUniRule annotation1
Sitei70Transition state stabilizerUniRule annotation1
Sitei84Increases basicity of active site HisUniRule annotation1
Binding sitei147SubstrateUniRule annotation1
Metal bindingi149Divalent metal cationUniRule annotation1
Binding sitei174Substrate; via amide nitrogenUniRule annotation1
Metal bindingi175Divalent metal cationUniRule annotation1
Binding sitei175SubstrateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BRENDAi4.1.2.52. 2026.
UniPathwayiUPA00208; UER00422.

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxy-2-oxo-heptane-1,7-dioate aldolaseUniRule annotation (EC:4.1.2.52UniRule annotation)
Alternative name(s):
2,4-dihydroxyhept-2-ene-1,7-dioic acid aldolaseUniRule annotation
Short name:
HHED aldolaseUniRule annotation
4-hydroxy-2-ketoheptane-1,7-dioate aldolaseUniRule annotation
Short name:
HKHD aldolaseUniRule annotation
Gene namesi
Name:hpcHUniRule annotation
Synonyms:hpaIUniRule annotation
Ordered Locus Names:EcolC_3707
OrganismiEscherichia coli (strain ATCC 8739 / DSM 1576 / Crooks)
Taxonomic identifieri481805 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003551031 – 2624-hydroxy-2-oxo-heptane-1,7-dioate aldolaseAdd BLAST262

Interactioni

Subunit structurei

Homohexamer; trimer of dimers.UniRule annotation

Protein-protein interaction databases

STRINGi481805.EcolC_3707.

Structurei

Secondary structure

1262
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 10Combined sources7
Beta strandi15 – 20Combined sources6
Helixi25 – 32Combined sources8
Beta strandi37 – 42Combined sources6
Turni43 – 45Combined sources3
Helixi50 – 60Combined sources11
Beta strandi63 – 70Combined sources8
Beta strandi72 – 74Combined sources3
Helixi76 – 84Combined sources9
Beta strandi89 – 93Combined sources5
Helixi98 – 107Combined sources10
Turni111 – 113Combined sources3
Helixi120 – 122Combined sources3
Helixi124 – 126Combined sources3
Turni127 – 130Combined sources4
Helixi134 – 137Combined sources4
Helixi139 – 141Combined sources3
Beta strandi143 – 148Combined sources6
Helixi151 – 155Combined sources5
Helixi157 – 161Combined sources5
Beta strandi166 – 171Combined sources6
Helixi173 – 180Combined sources8
Helixi189 – 204Combined sources16
Beta strandi207 – 212Combined sources6
Helixi216 – 224Combined sources9
Beta strandi228 – 234Combined sources7
Helixi235 – 249Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4B5SX-ray1.68A/B1-251[»]
4B5TX-ray1.92A/B1-251[»]
4B5UX-ray1.91A/B1-251[»]
4B5VX-ray2.04A/B1-251[»]
4B5WX-ray1.79A/B/C/D/E/F1-256[»]
4B5XX-ray1.80A/B1-262[»]
ProteinModelPortaliB1IS70.
SMRiB1IS70.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the HpcH/HpaI aldolase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CNV. Bacteria.
COG3836. LUCA.
HOGENOMiHOG000179750.
KOiK02510.
OMAiGLCSSYS.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
HAMAPiMF_01292. HKHD_aldolase. 1 hit.
InterProiIPR005000. Aldolase/citrate-lyase_domain.
IPR023701. HKHD_aldolase_ent.
IPR012689. HpaI.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamiPF03328. HpcH_HpaI. 1 hit.
[Graphical view]
SUPFAMiSSF51621. SSF51621. 1 hit.
TIGRFAMsiTIGR02311. HpaI. 1 hit.

Sequencei

Sequence statusi: Complete.

B1IS70-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENSFKAALK AGRPQIGLWL GLSSSYSAEL LAGAGFDWLL IDGEHAPNNV
60 70 80 90 100
QTVLTQLQAI APYPSQPVVR PSWNDPVQIK QLLDVGTQTL LVPMVQNADE
110 120 130 140 150
AREAVRATRY PPAGIRGVGS ALARASRWNR IPDYLQKAND QMCVLVQIET
160 170 180 190 200
REAMKNLPQI LDVEGVDGVF IGPADLSADM GYAGNPQHPE VQAAIEQAIV
210 220 230 240 250
QIRESGKAPG ILIANEQLAK RYLELGALFV AVGVDTTLLA RAAEALAARF
260
GAQATAVKPG VY
Length:262
Mass (Da):28,073
Last modified:April 29, 2008 - v1
Checksum:i374F576B6C53587F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000946 Genomic DNA. Translation: ACA79318.1.
RefSeqiWP_000431706.1. NC_010468.1.

Genome annotation databases

EnsemblBacteriaiACA79318; ACA79318; EcolC_3707.
KEGGiecl:EcolC_3707.
PATRICi18230546. VBIEscCol82905_3964.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000946 Genomic DNA. Translation: ACA79318.1.
RefSeqiWP_000431706.1. NC_010468.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4B5SX-ray1.68A/B1-251[»]
4B5TX-ray1.92A/B1-251[»]
4B5UX-ray1.91A/B1-251[»]
4B5VX-ray2.04A/B1-251[»]
4B5WX-ray1.79A/B/C/D/E/F1-256[»]
4B5XX-ray1.80A/B1-262[»]
ProteinModelPortaliB1IS70.
SMRiB1IS70.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi481805.EcolC_3707.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACA79318; ACA79318; EcolC_3707.
KEGGiecl:EcolC_3707.
PATRICi18230546. VBIEscCol82905_3964.

Phylogenomic databases

eggNOGiENOG4105CNV. Bacteria.
COG3836. LUCA.
HOGENOMiHOG000179750.
KOiK02510.
OMAiGLCSSYS.

Enzyme and pathway databases

UniPathwayiUPA00208; UER00422.
BRENDAi4.1.2.52. 2026.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
HAMAPiMF_01292. HKHD_aldolase. 1 hit.
InterProiIPR005000. Aldolase/citrate-lyase_domain.
IPR023701. HKHD_aldolase_ent.
IPR012689. HpaI.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamiPF03328. HpcH_HpaI. 1 hit.
[Graphical view]
SUPFAMiSSF51621. SSF51621. 1 hit.
TIGRFAMsiTIGR02311. HpaI. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHPCH_ECOLC
AccessioniPrimary (citable) accession number: B1IS70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: April 29, 2008
Last modified: November 2, 2016
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.