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Protein

Aralkylamine dehydrogenase light chain

Gene

aauA

Organism
Alcaligenes faecalis
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Oxidizes primary aromatic amines and, more slowly, some long-chain aliphatic amines, but not methylamine or ethylamine. Uses azurin as an electron acceptor to transfer electrons from the reduced tryptophylquinone cofactor.7 Publications

Catalytic activityi

ArCH2NH2 + H2O + 2 azurin = ArCHO + NH3 + 2 reduced azurin.2 Publications

Cofactori

tryptophan tryptophylquinone residue5 PublicationsNote: Uses a protein-derived tryptophan tryptophylquinone (TTQ) cofactor.5 Publications

Enzyme regulationi

Irreversibly inhibited by phenylhydrazine, hydroxylamine, semicarbazide, hydrazine and aminoguanidine. Reversibly inhibited by isonicotinic acid hydrazide (isoniazid) and isonicotinic acid 2-isopropyl hydrazide (iproniazid).1 Publication

Absorptioni

Abs(max)=465 nm3 Publications

The above maximum is for the oxidized form. Shows a maximal peak at 330 nm in the reduced form. These absorption peaks are for the tryptophylquinone cofactor.2 Publications

Kineticsi

The enzyme is substrate inhibited at high substrate concentrations (Ki=1.08 mM for tyramine).1 Publication

  1. KM=5.4 µM for tyramine3 Publications
  1. Vmax=17 µmol/min/mg enzyme3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei84 – 841Substrate2 Publications
Active sitei109 – 1091Tryptophylquinone 6'-substrate hemiaminal intermediate
Active sitei128 – 1281Proton acceptor2 Publications
Sitei172 – 1721Transition state stabilizer

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16554.
BRENDAi1.4.9.2. 232.
SABIO-RKP84887.

Names & Taxonomyi

Protein namesi
Recommended name:
Aralkylamine dehydrogenase light chain (EC:1.4.9.2)
Alternative name(s):
Aromatic amine dehydrogenase
Short name:
AADH
Gene namesi
Name:aauA1 Publication
OrganismiAlcaligenes faecalis
Taxonomic identifieri511 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeAlcaligenes

Subcellular locationi

  • Periplasm 2 Publications

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4747Tat-type signalPROSITE-ProRule annotation2 PublicationsAdd
BLAST
Chaini48 – 182135Aralkylamine dehydrogenase light chainPROSITE-ProRule annotation1 PublicationPRO_0000287911Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi75 ↔ 1403 Publications
Disulfide bondi81 ↔ 1133 Publications
Disulfide bondi88 ↔ 1713 Publications
Disulfide bondi90 ↔ 1383 Publications
Disulfide bondi91 ↔ 1353 Publications
Disulfide bondi98 ↔ 1293 Publications
Cross-linki109 ↔ 160Tryptophan tryptophylquinone (Trp-Trp)3 Publications
Modified residuei109 – 1091Tryptophylquinone3 Publications
Disulfide bondi130 ↔ 1613 Publications

Post-translational modificationi

Tryptophan tryptophylquinone (TTQ) is formed by oxidation of the indole ring of a tryptophan to form tryptophylquinone followed by covalent cross-linking with another tryptophan residue.4 Publications
Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

Keywords - PTMi

Disulfide bond, TTQ

Interactioni

Subunit structurei

Heterotetramer of two light and two heavy chains. Binds two azurin molecules per heterotetramer.5 Publications

Structurei

Secondary structure

1
182
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi60 – 623Combined sources
Helixi64 – 663Combined sources
Helixi69 – 724Combined sources
Helixi78 – 803Combined sources
Beta strandi84 – 874Combined sources
Helixi88 – 903Combined sources
Beta strandi95 – 973Combined sources
Beta strandi109 – 1146Combined sources
Turni116 – 1183Combined sources
Beta strandi121 – 1266Combined sources
Beta strandi128 – 1325Combined sources
Beta strandi137 – 1415Combined sources
Helixi149 – 1546Combined sources
Turni160 – 1634Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi169 – 1724Combined sources
Beta strandi175 – 1795Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AGLX-ray1.40D/H48-182[»]
2AGWX-ray1.45D/H48-182[»]
2AGXX-ray2.20D/H48-182[»]
2AGYX-ray1.10D/H48-182[»]
2AGZX-ray1.60D/H48-182[»]
2AH0X-ray1.45D/H48-182[»]
2AH1X-ray1.20D/H48-182[»]
2H3XX-ray2.50B/E48-182[»]
2H47X-ray2.60B/E/G/I48-182[»]
2HJ4X-ray1.80D/H48-182[»]
2HJBX-ray1.85D/H48-182[»]
2HKMX-ray1.50D/H48-182[»]
2HKRX-ray1.40D/H59-180[»]
2HXCX-ray1.45D/H48-182[»]
2I0RX-ray1.40D/H59-182[»]
2I0SX-ray1.40D/H59-182[»]
2I0TX-ray1.35D/H59-180[»]
2IAAX-ray1.95B/E48-182[»]
2IUPX-ray1.80D/H48-182[»]
2IUQX-ray1.50D/H48-182[»]
2IURX-ray1.30D/H48-182[»]
2IUVX-ray1.55D/H48-182[»]
2OIZX-ray1.05D/H48-182[»]
2OJYX-ray1.60D/H48-180[»]
2OK4X-ray1.45D/H48-182[»]
2OK6X-ray1.45D/H48-182[»]
2Q7QX-ray1.60D/H59-182[»]
ProteinModelPortaliP84887.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP84887.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni156 – 1583Substrate-binding2 Publications

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

KOiK13371.

Family and domain databases

Gene3Di2.60.30.10. 1 hit.
InterProiIPR016008. Amine_DH_Ltc.
IPR013504. MADH/AADH_Ltc_C_dom.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF02975. Me-amine-dh_L. 1 hit.
[Graphical view]
PIRSFiPIRSF000192. Amine_dh_beta. 1 hit.
SUPFAMiSSF57561. SSF57561. 1 hit.
PROSITEiPS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P84887-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRWLDKFGES LSRSVAHKTS RRSVLRSVGK LMVGSAFVLP VLPVARAAGG
60 70 80 90 100
GGSSSGADHI SLNPDLANED EVNSCDYWRH CAVDGFLCSC CGGTTTTCPP
110 120 130 140 150
GSTPSPISWI GTCHNPHDGK DYLISYHDCC GKTACGRCQC NTQTRERPGY
160 170 180
EFFLHNDVNW CMANENSTFH CTTSVLVGLA KN
Length:182
Mass (Da):19,652
Last modified:May 15, 2007 - v1
Checksum:i74BC95478B172A41
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF302652 Genomic DNA. No translation available.
AM292629 Genomic DNA. Translation: CAL23525.1.
RefSeqiWP_021447059.1. NZ_KQ954451.1.

Genome annotation databases

KEGGiag:CAL23525.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF302652 Genomic DNA. No translation available.
AM292629 Genomic DNA. Translation: CAL23525.1.
RefSeqiWP_021447059.1. NZ_KQ954451.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AGLX-ray1.40D/H48-182[»]
2AGWX-ray1.45D/H48-182[»]
2AGXX-ray2.20D/H48-182[»]
2AGYX-ray1.10D/H48-182[»]
2AGZX-ray1.60D/H48-182[»]
2AH0X-ray1.45D/H48-182[»]
2AH1X-ray1.20D/H48-182[»]
2H3XX-ray2.50B/E48-182[»]
2H47X-ray2.60B/E/G/I48-182[»]
2HJ4X-ray1.80D/H48-182[»]
2HJBX-ray1.85D/H48-182[»]
2HKMX-ray1.50D/H48-182[»]
2HKRX-ray1.40D/H59-180[»]
2HXCX-ray1.45D/H48-182[»]
2I0RX-ray1.40D/H59-182[»]
2I0SX-ray1.40D/H59-182[»]
2I0TX-ray1.35D/H59-180[»]
2IAAX-ray1.95B/E48-182[»]
2IUPX-ray1.80D/H48-182[»]
2IUQX-ray1.50D/H48-182[»]
2IURX-ray1.30D/H48-182[»]
2IUVX-ray1.55D/H48-182[»]
2OIZX-ray1.05D/H48-182[»]
2OJYX-ray1.60D/H48-180[»]
2OK4X-ray1.45D/H48-182[»]
2OK6X-ray1.45D/H48-182[»]
2Q7QX-ray1.60D/H59-182[»]
ProteinModelPortaliP84887.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAL23525.

Phylogenomic databases

KOiK13371.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16554.
BRENDAi1.4.9.2. 232.
SABIO-RKP84887.

Miscellaneous databases

EvolutionaryTraceiP84887.

Family and domain databases

Gene3Di2.60.30.10. 1 hit.
InterProiIPR016008. Amine_DH_Ltc.
IPR013504. MADH/AADH_Ltc_C_dom.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF02975. Me-amine-dh_L. 1 hit.
[Graphical view]
PIRSFiPIRSF000192. Amine_dh_beta. 1 hit.
SUPFAMiSSF57561. SSF57561. 1 hit.
PROSITEiPS51318. TAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning, sequencing and mutagenesis of the genes for aromatic amine dehydrogenase from Alcaligenes faecalis and evolution of amine dehydrogenases."
    Chistoserdov A.Y.
    Microbiology 147:2195-2202(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. "Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis. Cofactor assembly and catalytic properties of recombinant enzyme expressed in Paracoccus denitrificans."
    Hothi P., Khadra K.A., Combe J.P., Leys D., Scrutton N.S.
    FEBS J. 272:5894-5909(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 48-53, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
    Strain: ATCC 49677 / NBRC 144791 PublicationImported.
  3. "Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme."
    Govindaraj S., Eisenstein E., Jones L.H., Sanders-Loehr J., Chistoserdov A.Y., Davidson V.L., Edwards S.L.
    J. Bacteriol. 176:2922-2929(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 48-64, FUNCTION, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    Strain: ATCC 49677 / NBRC 144791 Publication.
  4. "Spectroscopic evidence for a common electron transfer pathway for two tryptophan tryptophylquinone enzymes."
    Edwards S.L., Davidson V.L., Hyun Y.-L., Wingfield P.T.
    J. Biol. Chem. 270:4293-4298(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  5. "Identification of reaction products and intermediates of aromatic-amine dehydrogenase by 15N and 13C NMR."
    Bishop G.R., Zhu Z., Whitehead T.L., Hicks R.P., Davidson V.L.
    Biochem. J. 330:1159-1163(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
    Strain: ATCC 49677 / NBRC 144791 Publication.
  6. "Localization of periplasmic redox proteins of Alcaligenes faecalis by a modified general method for fractionating Gram-negative bacteria."
    Zhu Z., Sun D., Davidson V.L.
    J. Bacteriol. 181:6540-6542(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis."
    Sukumar N., Chen Z.-W., Ferrari D., Merli A., Rossi G.L., Bellamy H.D., Chistoserdov A.Y., Davidson V.L., Mathews F.S.
    Biochemistry 45:13500-13510(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB AND AZURIN, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, DISULFIDE BONDS.
    Strain: ATCC 49677 / NBRC 144791 Publication.
  8. "Atomic level insight into the oxidative half-reaction of aromatic amine dehydrogenase."
    Roujeinikova A., Scrutton N.S., Leys D.
    J. Biol. Chem. 281:40264-40272(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB AND SUBSTRATE, FUNCTION, COFACTOR, SUBUNIT, DISULFIDE BONDS.
    Strain: ATCC 49677 / NBRC 144791 Publication.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB AND SUBSTRATE, FUNCTION, COFACTOR, SUBUNIT, DISULFIDE BONDS.
    Strain: ATCC 49677 / NBRC 144791 Publication.

Entry informationi

Entry nameiAAUA_ALCFA
AccessioniPrimary (citable) accession number: P84887
Secondary accession number(s): Q0VKG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 15, 2007
Last modified: May 11, 2016
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, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.