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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei45 – 451Proton acceptorUniRule annotation
Sitei70 – 701Transition state stabilizerUniRule annotation
Sitei84 – 841Increases basicity of active site HisUniRule annotation
Binding sitei147 – 1471SubstrateUniRule annotation
Metal bindingi149 – 1491Divalent metal cationUniRule annotation
Binding sitei174 – 1741Substrate; via amide nitrogenUniRule annotation
Metal bindingi175 – 1751Divalent metal cationUniRule annotation
Binding sitei175 – 1751SubstrateUniRule annotation

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

BioCyciECOL481805:GI3G-3792-MONOMER.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2622624-hydroxy-2-oxo-heptane-1,7-dioate aldolasePRO_0000355103Add
BLAST

Proteomic databases

PRIDEiB1IS70.

Interactioni

Subunit structurei

Homohexamer; trimer of dimers.UniRule annotation

Protein-protein interaction databases

STRINGi481805.EcolC_3707.

Structurei

Secondary structure

1
262
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 107Combined sources
Beta strandi15 – 206Combined sources
Helixi25 – 328Combined sources
Beta strandi37 – 426Combined sources
Turni43 – 453Combined sources
Helixi50 – 6011Combined sources
Beta strandi63 – 708Combined sources
Beta strandi72 – 743Combined sources
Helixi76 – 849Combined sources
Beta strandi89 – 935Combined sources
Helixi98 – 10710Combined sources
Turni111 – 1133Combined sources
Helixi120 – 1223Combined sources
Helixi124 – 1263Combined sources
Turni127 – 1304Combined sources
Helixi134 – 1374Combined sources
Helixi139 – 1413Combined sources
Beta strandi143 – 1486Combined sources
Helixi151 – 1555Combined sources
Helixi157 – 1615Combined sources
Beta strandi166 – 1716Combined sources
Helixi173 – 1808Combined sources
Helixi189 – 20416Combined sources
Beta strandi207 – 2126Combined sources
Helixi216 – 2249Combined sources
Beta strandi228 – 2347Combined sources
Helixi235 – 24915Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-259.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the HpcH/HpaI aldolase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CNV. Bacteria.
COG3836. LUCA.
HOGENOMiHOG000179750.
KOiK02510.
OMAiGLCSSYS.
OrthoDBiEOG6NPM5P.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
HAMAPiMF_01292. HKHD_aldolase.
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
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. Positions 1-259.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi481805.EcolC_3707.

Proteomic databases

PRIDEiB1IS70.

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.
OrthoDBiEOG6NPM5P.

Enzyme and pathway databases

UniPathwayiUPA00208; UER00422.
BioCyciECOL481805:GI3G-3792-MONOMER.
BRENDAi4.1.2.52. 2026.

Family and domain databases

Gene3Di3.20.20.60. 1 hit.
HAMAPiMF_01292. HKHD_aldolase.
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...

Publicationsi

  1. "Complete sequence of Escherichia coli C str. ATCC 8739."
    Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.
    , Kyrpides N., Mikhailova N., Ingram L., Richardson P.
    Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 8739 / DSM 1576 / Crooks.

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 11, 2015
This is version 53 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.