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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

Manual assertion based on experiment ini

Kineticsi

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

Manual assertion based on experiment ini

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei84Substrate2 Publications1
Active sitei109Tryptophylquinone 6'-substrate hemiaminal intermediate1
Active sitei128Proton acceptor2 Publications1
Sitei172Transition state stabilizer1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 47Tat-type signalPROSITE-ProRule annotation2 PublicationsAdd BLAST47
ChainiPRO_000028791148 – 182Aralkylamine dehydrogenase light chainPROSITE-ProRule annotation1 PublicationAdd BLAST135

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 residuei109Tryptophylquinone3 Publications1
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

1182
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi60 – 62Combined sources3
Helixi64 – 66Combined sources3
Helixi69 – 72Combined sources4
Helixi78 – 80Combined sources3
Beta strandi84 – 87Combined sources4
Helixi88 – 90Combined sources3
Beta strandi95 – 97Combined sources3
Beta strandi109 – 114Combined sources6
Turni116 – 118Combined sources3
Beta strandi121 – 126Combined sources6
Beta strandi128 – 132Combined sources5
Beta strandi137 – 141Combined sources5
Helixi149 – 154Combined sources6
Turni160 – 163Combined sources4
Beta strandi164 – 166Combined sources3
Beta strandi169 – 172Combined sources4
Beta strandi175 – 179Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiP84887.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP84887.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni156 – 158Substrate-binding2 Publications3

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_LSUO01000003.1.

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_LSUO01000003.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiP84887.
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...

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: November 2, 2016
This is version 56 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.