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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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
ChainiPRO_00001093321 – 4753-hydroxyadipyl-CoA dehydrogenaseAdd BLAST475

Proteomic databases

PaxDbiP76083.
PRIDEiP76083.

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 interactors.
IntActiP76083. 1 interactor.
STRINGi511145.b1395.

Structurei

Secondary structure

1475
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 11Combined sources4
Helixi15 – 26Combined sources12
Beta strandi31 – 34Combined sources4
Helixi38 – 53Combined sources16
Turni54 – 59Combined sources6
Helixi63 – 71Combined sources9
Beta strandi73 – 76Combined sources4
Helixi79 – 84Combined sources6
Beta strandi86 – 90Combined sources5
Helixi96 – 109Combined sources14
Beta strandi115 – 118Combined sources4
Beta strandi121 – 123Combined sources3
Helixi125 – 128Combined sources4
Turni129 – 131Combined sources3
Beta strandi132 – 134Combined sources3
Helixi135 – 137Combined sources3
Beta strandi138 – 143Combined sources6
Turni147 – 149Combined sources3
Beta strandi152 – 157Combined sources6
Helixi163 – 175Combined sources13
Beta strandi179 – 185Combined sources7
Turni187 – 190Combined sources4
Helixi191 – 194Combined sources4
Helixi196 – 207Combined sources12
Helixi213 – 222Combined sources10
Helixi230 – 237Combined sources8
Helixi239 – 252Combined sources14
Helixi257 – 259Combined sources3
Helixi263 – 270Combined sources8
Helixi276 – 278Combined sources3
Beta strandi280 – 284Combined sources5
Helixi300 – 302Combined sources3
Beta strandi307 – 309Combined sources3
Beta strandi314 – 317Combined sources4
Beta strandi320 – 324Combined sources5
Beta strandi326 – 328Combined sources3
Helixi330 – 337Combined sources8
Beta strandi341 – 345Combined sources5
Beta strandi348 – 356Combined sources9
Helixi362 – 373Combined sources12
Turni374 – 376Combined sources3
Beta strandi378 – 381Combined sources4
Turni386 – 389Combined sources4
Helixi390 – 406Combined sources17
Helixi412 – 422Combined sources11
Helixi429 – 436Combined sources8
Helixi438 – 452Combined sources15
Helixi455 – 457Combined sources3
Helixi461 – 470Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3MOGX-ray2.20A/B/C4-475[»]
ProteinModelPortaliP76083.
SMRiP76083.
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)DescriptionActionsGraphical viewLength
Natural varianti132I → V in strain: W. 1
Natural varianti344I → V in strain: W. 1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3MOGX-ray2.20A/B/C4-475[»]
ProteinModelPortaliP76083.
SMRiP76083.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259599. 406 interactors.
IntActiP76083. 1 interactor.
STRINGi511145.b1395.

Proteomic databases

PaxDbiP76083.
PRIDEiP76083.

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: November 2, 2016
This is version 133 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.