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Protein

3-hydroxyadipyl-CoA dehydrogenase

Gene

paaH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidation of 3-hydroxyadipyl-CoA to yield 3-oxoadipyl-CoA.2 Publications

Catalytic activityi

3-hydroxyadipyl-CoA + NAD+ = 3-oxoadipyl-CoA + NADH.1 Publication

Pathwayi: phenylacetate degradation

This protein is involved in the pathway phenylacetate degradation, which is part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the pathway phenylacetate degradation and in Aromatic compound metabolism.

GO - Molecular functioni

  • 3-hydroxyacyl-CoA dehydrogenase activity Source: EcoCyc
  • 3-hydroxybutyryl-CoA dehydrogenase activity Source: UniProtKB

GO - Biological processi

  • fatty acid metabolic process Source: InterPro
  • phenylacetate catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciEcoCyc:G6716-MONOMER.
ECOL316407:JW1390-MONOMER.
MetaCyc:G6716-MONOMER.
UniPathwayiUPA00930.

Names & Taxonomyi

Protein namesi
Recommended name:
3-hydroxyadipyl-CoA dehydrogenase (EC:1.1.1.-)
Gene namesi
Name:paaH
Synonyms:ydbU
Ordered Locus Names:b1395, JW1390
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13742. paaH.

Pathology & Biotechi

Disruption phenotypei

Mutants accumulate 3-hydroxyadipate and are unable to use phenylacetate as a carbon source.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4754753-hydroxyadipyl-CoA dehydrogenasePRO_0000109332Add
BLAST

Proteomic databases

PaxDbiP76083.

Expressioni

Inductioni

Activated by cAMP receptor protein (CRP), integration host factor (IHF) and by phenylacetyl-coenzyme A (PA-CoA) that prevents PaaX from binding its target sequences. Inhibited by PaaX.2 Publications

Interactioni

Subunit structurei

Homotrimer.Curated

Protein-protein interaction databases

BioGridi4259599. 406 interactions.
IntActiP76083. 1 interaction.
STRINGi511145.b1395.

Structurei

Secondary structure

1
475
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 114Combined sources
Helixi15 – 2612Combined sources
Beta strandi31 – 344Combined sources
Helixi38 – 5316Combined sources
Turni54 – 596Combined sources
Helixi63 – 719Combined sources
Beta strandi73 – 764Combined sources
Helixi79 – 846Combined sources
Beta strandi86 – 905Combined sources
Helixi96 – 10914Combined sources
Beta strandi115 – 1184Combined sources
Beta strandi121 – 1233Combined sources
Helixi125 – 1284Combined sources
Turni129 – 1313Combined sources
Beta strandi132 – 1343Combined sources
Helixi135 – 1373Combined sources
Beta strandi138 – 1436Combined sources
Turni147 – 1493Combined sources
Beta strandi152 – 1576Combined sources
Helixi163 – 17513Combined sources
Beta strandi179 – 1857Combined sources
Turni187 – 1904Combined sources
Helixi191 – 1944Combined sources
Helixi196 – 20712Combined sources
Helixi213 – 22210Combined sources
Helixi230 – 2378Combined sources
Helixi239 – 25214Combined sources
Helixi257 – 2593Combined sources
Helixi263 – 2708Combined sources
Helixi276 – 2783Combined sources
Beta strandi280 – 2845Combined sources
Helixi300 – 3023Combined sources
Beta strandi307 – 3093Combined sources
Beta strandi314 – 3174Combined sources
Beta strandi320 – 3245Combined sources
Beta strandi326 – 3283Combined sources
Helixi330 – 3378Combined sources
Beta strandi341 – 3455Combined sources
Beta strandi348 – 3569Combined sources
Helixi362 – 37312Combined sources
Turni374 – 3763Combined sources
Beta strandi378 – 3814Combined sources
Turni386 – 3894Combined sources
Helixi390 – 40617Combined sources
Helixi412 – 42211Combined sources
Helixi429 – 4368Combined sources
Helixi438 – 45215Combined sources
Helixi455 – 4573Combined sources
Helixi461 – 47010Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MOGX-ray2.20A/B/C4-475[»]
ProteinModelPortaliP76083.
SMRiP76083. Positions 4-473.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP76083.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105DYT. Bacteria.
COG1250. LUCA.
HOGENOMiHOG000141500.
InParanoidiP76083.
KOiK00074.
OMAiGQKQVPA.
PhylomeDBiP76083.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR011967. 3-OHacyl-CoA_DH_PaaC.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR02279. PaaC-3OHAcCoADH. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P76083-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMINVQTVAV IGSGTMGAGI AEVAASHGHQ VLLYDISAEA LTRAIDGIHA
60 70 80 90 100
RLNSRVTRGK LTAETCERTL KRLIPVTDIH ALAAADLVIE AASERLEVKK
110 120 130 140 150
ALFAQLAEVC PPQTLLTTNT SSISITAIAA EIKNPERVAG LHFFNPAPVM
160 170 180 190 200
KLVEVVSGLA TAAEVVEQLC ELTLSWGKQP VRCHSTPGFI VNRVARPYYS
210 220 230 240 250
EAWRALEEQV AAPEVIDAAL RDGAGFPMGP LELTDLIGQD VNFAVTCSVF
260 270 280 290 300
NAFWQERRFL PSLVQQELVI GGRLGKKSGL GVYDWRAERE AVVGLEAVSD
310 320 330 340 350
SFSPMKVEKK SDGVTEIDDV LLIETQGETA QALAIRLARP VVVIDKMAGK
360 370 380 390 400
VVTIAAAAVN PDSATRKAIY YLQQQGKTVL QIADYPGMLI WRTVAMIINE
410 420 430 440 450
ALDALQKGVA SEQDIDTAMR LGVNYPYGPL AWGAQLGWQR ILRLLENLQH
460 470
HYGEERYRPC SLLRQRALLE SGYES
Length:475
Mass (Da):51,733
Last modified:February 1, 1997 - v1
Checksum:iDEB6190F08D527C6
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti132 – 1321I → V in strain: W.
Natural varianti344 – 3441I → V in strain: W.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97452 Genomic DNA. Translation: CAA66097.1.
U00096 Genomic DNA. Translation: AAC74477.1.
AP009048 Genomic DNA. Translation: BAA15001.2.
PIRiF64890.
RefSeqiNP_415913.1. NC_000913.3.
WP_000973360.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74477; AAC74477; b1395.
BAA15001; BAA15001; BAA15001.
GeneIDi945940.
KEGGiecj:JW1390.
eco:b1395.
PATRICi32118076. VBIEscCol129921_1458.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97452 Genomic DNA. Translation: CAA66097.1.
U00096 Genomic DNA. Translation: AAC74477.1.
AP009048 Genomic DNA. Translation: BAA15001.2.
PIRiF64890.
RefSeqiNP_415913.1. NC_000913.3.
WP_000973360.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3MOGX-ray2.20A/B/C4-475[»]
ProteinModelPortaliP76083.
SMRiP76083. Positions 4-473.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259599. 406 interactions.
IntActiP76083. 1 interaction.
STRINGi511145.b1395.

Proteomic databases

PaxDbiP76083.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74477; AAC74477; b1395.
BAA15001; BAA15001; BAA15001.
GeneIDi945940.
KEGGiecj:JW1390.
eco:b1395.
PATRICi32118076. VBIEscCol129921_1458.

Organism-specific databases

EchoBASEiEB3505.
EcoGeneiEG13742. paaH.

Phylogenomic databases

eggNOGiENOG4105DYT. Bacteria.
COG1250. LUCA.
HOGENOMiHOG000141500.
InParanoidiP76083.
KOiK00074.
OMAiGQKQVPA.
PhylomeDBiP76083.

Enzyme and pathway databases

UniPathwayiUPA00930.
BioCyciEcoCyc:G6716-MONOMER.
ECOL316407:JW1390-MONOMER.
MetaCyc:G6716-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP76083.
PROiP76083.

Family and domain databases

Gene3Di1.10.1040.10. 2 hits.
3.40.50.720. 1 hit.
InterProiIPR006180. 3-OHacyl-CoA_DH_CS.
IPR006176. 3-OHacyl-CoA_DH_NAD-bd.
IPR011967. 3-OHacyl-CoA_DH_PaaC.
IPR006108. 3HC_DH_C.
IPR008927. 6-PGluconate_DH_C-like.
IPR013328. 6PGD_dom_2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00725. 3HCDH. 2 hits.
PF02737. 3HCDH_N. 1 hit.
[Graphical view]
SUPFAMiSSF48179. SSF48179. 2 hits.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR02279. PaaC-3OHAcCoADH. 1 hit.
PROSITEiPS00067. 3HCDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPAAH_ECOLI
AccessioniPrimary (citable) accession number: P76083
Secondary accession number(s): O53016, P78289
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: September 7, 2016
This is version 131 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, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.