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Protein

Acetaldehyde dehydrogenase

Gene

mhpF

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD+ and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds.UniRule annotation

Catalytic activityi

Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei127 – 1271Acyl-thioester intermediateUniRule annotation
Binding sitei277 – 2771NADUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 154NADUniRule annotation
Nucleotide bindingi158 – 1669NADUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Acetaldehyde dehydrogenaseUniRule annotation (EC:1.2.1.10UniRule annotation)
Alternative name(s):
Acetaldehyde dehydrogenase [acetylating]UniRule annotation
Gene namesi
Name:mhpFUniRule annotation
Ordered Locus Names:Rv3535c
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
ProteomesiUP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv3535c.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 303303Acetaldehyde dehydrogenasePRO_0000387688Add
BLAST

Structurei

Secondary structure

1
303
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 106Combined sources
Helixi14 – 2411Combined sources
Beta strandi27 – 359Combined sources
Helixi42 – 498Combined sources
Beta strandi53 – 575Combined sources
Helixi59 – 624Combined sources
Beta strandi70 – 745Combined sources
Helixi78 – 9114Combined sources
Beta strandi94 – 974Combined sources
Helixi109 – 1168Combined sources
Beta strandi120 – 1234Combined sources
Helixi127 – 14014Combined sources
Beta strandi148 – 1558Combined sources
Helixi156 – 1583Combined sources
Helixi161 – 1655Combined sources
Helixi167 – 18014Combined sources
Beta strandi185 – 19410Combined sources
Beta strandi202 – 2109Combined sources
Helixi216 – 23116Combined sources
Beta strandi237 – 2415Combined sources
Beta strandi244 – 2463Combined sources
Turni250 – 2545Combined sources
Beta strandi256 – 2649Combined sources
Beta strandi269 – 2713Combined sources
Helixi276 – 29520Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JN6X-ray1.93B/D1-303[»]
ProteinModelPortaliP9WQH3.
SMRiP9WQH3. Positions 3-298.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the acetaldehyde dehydrogenase family.UniRule annotation

Phylogenomic databases

KOiK04073.
OMAiHQGNVNM.
PhylomeDBiP9WQH3.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01657. Ac_ald_DH_ac.
InterProiIPR003361. Acetaldehyde_dehydrogenase.
IPR015426. Acetylaldehyde_DH_C.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
[Graphical view]
PfamiPF09290. AcetDehyd-dimer. 1 hit.
PF01118. Semialdhyde_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF015689. Actaldh_dh_actl. 1 hit.
SMARTiSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03215. ac_ald_DH_ac. 1 hit.

Sequencei

Sequence statusi: Complete.

P9WQH3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSKAKVAIV GSGNISTDLL YKLLRSEWLE PRWMVGIDPE SDGLARAAKL
60 70 80 90 100
GLETTHEGVD WLLAQPDKPD LVFEATSAYV HRDAAPKYAE AGIRAIDLTP
110 120 130 140 150
AAVGPAVIPP ANLREHLDAP NVNMITCGGQ ATIPIVYAVS RIVEVPYAEI
160 170 180 190 200
VASVASVSAG PGTRANIDEF TKTTARGVQT IGGAARGKAI IILNPADPPM
210 220 230 240 250
IMRDTIFCAI PTDADREAIA ASIHDVVKEV QTYVPGYRLL NEPQFDEPSI
260 270 280 290 300
NSGGQALVTT FVEVEGAGDY LPPYAGNLDI MTAAATKVGE EIAKETLVVG

GAR
Length:303
Mass (Da):32,009
Last modified:April 16, 2014 - v1
Checksum:iD52F1BEA88A56827
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP46357.1.
PIRiH70675.
RefSeqiNP_218052.1. NC_000962.3.
WP_003419251.1. NZ_KK339374.1.
YP_006517024.1. NC_018143.2.

Genome annotation databases

EnsemblBacteriaiCCP46357; CCP46357; Rv3535c.
GeneIDi888396.
KEGGimtu:Rv3535c.
mtv:RVBD_3535c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP46357.1.
PIRiH70675.
RefSeqiNP_218052.1. NC_000962.3.
WP_003419251.1. NZ_KK339374.1.
YP_006517024.1. NC_018143.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JN6X-ray1.93B/D1-303[»]
ProteinModelPortaliP9WQH3.
SMRiP9WQH3. Positions 3-298.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP46357; CCP46357; Rv3535c.
GeneIDi888396.
KEGGimtu:Rv3535c.
mtv:RVBD_3535c.

Organism-specific databases

TubercuListiRv3535c.

Phylogenomic databases

KOiK04073.
OMAiHQGNVNM.
PhylomeDBiP9WQH3.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01657. Ac_ald_DH_ac.
InterProiIPR003361. Acetaldehyde_dehydrogenase.
IPR015426. Acetylaldehyde_DH_C.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
[Graphical view]
PfamiPF09290. AcetDehyd-dimer. 1 hit.
PF01118. Semialdhyde_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF015689. Actaldh_dh_actl. 1 hit.
SMARTiSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03215. ac_ald_DH_ac. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25618 / H37Rv.
  2. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.

Entry informationi

Entry nameiACDH_MYCTU
AccessioniPrimary (citable) accession number: P9WQH3
Secondary accession number(s): L0TEF0, P71866, Q7D5C3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: May 27, 2015
This is version 12 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. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  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

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 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.