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Protein

Aralkylamine dehydrogenase heavy chain

Gene

aauB

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.4 Publications

Catalytic activityi

ArCH2NH2 + H2O + 2 azurin = ArCHO + NH3 + 2 reduced azurin.1 Publication

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

Kineticsi

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

  1. KM=5.4 µM for tyramine1 Publication
  1. Vmax=17 µmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei54 – 541Substrate3 Publications
Binding sitei57 – 571Substrate3 Publications
Binding sitei81 – 811Substrate3 Publications

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16553.
BRENDAi1.4.9.2. 232.
SABIO-RKP84888.

Names & Taxonomyi

Protein namesi
Recommended name:
Aralkylamine dehydrogenase heavy chain (EC:1.4.9.2)
Alternative name(s):
Aromatic amine dehydrogenase
Short name:
AADH
Gene namesi
Name:aauB1 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 – 25255 PublicationsAdd
BLAST
Chaini26 – 390365Aralkylamine dehydrogenase heavy chain5 PublicationsPRO_0000287910Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei26 – 261Pyrrolidone carboxylic acid1 Publication
Disulfide bondi182 ↔ 1993 Publications

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Interactioni

Subunit structurei

Heterotetramer of two light and two heavy chains. Binds two azurin molecules per heterotetramer.4 Publications

Structurei

Secondary structure

1
390
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi43 – 453Combined sources
Beta strandi46 – 516Combined sources
Helixi54 – 596Combined sources
Beta strandi61 – 666Combined sources
Turni67 – 693Combined sources
Beta strandi72 – 776Combined sources
Beta strandi80 – 867Combined sources
Beta strandi90 – 10011Combined sources
Beta strandi103 – 1064Combined sources
Beta strandi108 – 1169Combined sources
Turni117 – 1193Combined sources
Beta strandi122 – 1287Combined sources
Helixi139 – 1413Combined sources
Beta strandi142 – 1443Combined sources
Beta strandi148 – 16619Combined sources
Turni167 – 1704Combined sources
Beta strandi171 – 1766Combined sources
Helixi177 – 1793Combined sources
Beta strandi182 – 1876Combined sources
Beta strandi191 – 1999Combined sources
Beta strandi202 – 2098Combined sources
Beta strandi213 – 2208Combined sources
Turni227 – 2293Combined sources
Beta strandi240 – 2478Combined sources
Beta strandi250 – 2567Combined sources
Beta strandi258 – 2614Combined sources
Beta strandi263 – 2708Combined sources
Helixi273 – 2775Combined sources
Beta strandi284 – 2863Combined sources
Beta strandi288 – 2914Combined sources
Turni292 – 2954Combined sources
Beta strandi296 – 3049Combined sources
Beta strandi315 – 3217Combined sources
Turni322 – 3254Combined sources
Beta strandi326 – 3327Combined sources
Beta strandi338 – 3425Combined sources
Turni343 – 3464Combined sources
Beta strandi347 – 3515Combined sources
Beta strandi356 – 3605Combined sources
Beta strandi362 – 3654Combined sources
Beta strandi367 – 3726Combined sources
Beta strandi381 – 3844Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AGLX-ray1.40A/B30-389[»]
2AGWX-ray1.45A/B30-389[»]
2AGXX-ray2.20A/B30-389[»]
2AGYX-ray1.10A/B30-389[»]
2AGZX-ray1.60A/B30-389[»]
2AH0X-ray1.45A/B30-389[»]
2AH1X-ray1.20A/B30-389[»]
2H3XX-ray2.50A/D1-390[»]
2H47X-ray2.60A/D/F/H1-390[»]
2HJ4X-ray1.80A/B30-389[»]
2HJBX-ray1.85A/B30-389[»]
2HKMX-ray1.50A/B29-389[»]
2HKRX-ray1.40A/B29-389[»]
2HXCX-ray1.45A/B30-389[»]
2I0RX-ray1.40A/B30-389[»]
2I0SX-ray1.40A/B31-389[»]
2I0TX-ray1.35A/B30-389[»]
2IAAX-ray1.95A/D1-390[»]
2IUPX-ray1.80A/B30-389[»]
2IUQX-ray1.50A/B30-389[»]
2IURX-ray1.30A/B30-389[»]
2IUVX-ray1.55A/B30-389[»]
2OIZX-ray1.05A/B30-389[»]
2OJYX-ray1.60A/B29-389[»]
2OK4X-ray1.45A/B30-389[»]
2OK6X-ray1.45A/B30-389[»]
2Q7QX-ray1.60A/B30-390[»]
ProteinModelPortaliP84888.
SMRiP84888. Positions 28-389.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP84888.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

KOiK13372.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR009451. Metamine_DH_Hvc.
IPR011044. Quino_amine_DH_bsu.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PfamiPF06433. Me-amine-dh_H. 1 hit.
[Graphical view]
SUPFAMiSSF50969. SSF50969. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P84888-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSKFKLTTA AAMLGLMVLA GGAQAQDKPR EVLTGGHSVS APQENRIYVM
60 70 80 90 100
DSVFMHLTES RVHVYDYTNG KFLGMVPTAF NGHVQVSNDG KKIYTMTTYH
110 120 130 140 150
ERITRGKRSD VVEVWDADKL TFEKEISLPP KRVQGLNYDG LFRQTTDGKF
160 170 180 190 200
IVLQNASPAT SIGIVDVAKG DYVEDVTAAA GCWSVIPQPN RPRSFMTICG
210 220 230 240 250
DGGLLTINLG EDGKVASQSR SKQMFSVKDD PIFIAPALDK DKAHFVSYYG
260 270 280 290 300
NVYSADFSGD EVKVDGPWSL LNDEDKAKNW VPGGYNLVGL HRASGRMYVF
310 320 330 340 350
MHPDGKEGTH KFPAAEIWVM DTKTKQRVAR IPGRDALSMT IDQQRNLMLT
360 370 380 390
LDGGNVNVYD ISQPEPKLLR TIEGAAEASL QVQFHPVGGV
Length:390
Mass (Da):42,925
Last modified:May 15, 2007 - v1
Checksum:i0AFCC1129CC44FAC
GO

Mass spectrometryi

Molecular mass is 40422±1 Da from positions 26 - 390. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF302652 Genomic DNA. No translation available.
AM292628 Genomic DNA. Translation: CAL23524.1.
RefSeqiWP_009462712.1. NZ_KQ954451.1.

Genome annotation databases

KEGGiag:CAL23524.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF302652 Genomic DNA. No translation available.
AM292628 Genomic DNA. Translation: CAL23524.1.
RefSeqiWP_009462712.1. NZ_KQ954451.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AGLX-ray1.40A/B30-389[»]
2AGWX-ray1.45A/B30-389[»]
2AGXX-ray2.20A/B30-389[»]
2AGYX-ray1.10A/B30-389[»]
2AGZX-ray1.60A/B30-389[»]
2AH0X-ray1.45A/B30-389[»]
2AH1X-ray1.20A/B30-389[»]
2H3XX-ray2.50A/D1-390[»]
2H47X-ray2.60A/D/F/H1-390[»]
2HJ4X-ray1.80A/B30-389[»]
2HJBX-ray1.85A/B30-389[»]
2HKMX-ray1.50A/B29-389[»]
2HKRX-ray1.40A/B29-389[»]
2HXCX-ray1.45A/B30-389[»]
2I0RX-ray1.40A/B30-389[»]
2I0SX-ray1.40A/B31-389[»]
2I0TX-ray1.35A/B30-389[»]
2IAAX-ray1.95A/D1-390[»]
2IUPX-ray1.80A/B30-389[»]
2IUQX-ray1.50A/B30-389[»]
2IURX-ray1.30A/B30-389[»]
2IUVX-ray1.55A/B30-389[»]
2OIZX-ray1.05A/B30-389[»]
2OJYX-ray1.60A/B29-389[»]
2OK4X-ray1.45A/B30-389[»]
2OK6X-ray1.45A/B30-389[»]
2Q7QX-ray1.60A/B30-390[»]
ProteinModelPortaliP84888.
SMRiP84888. Positions 28-389.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAL23524.

Phylogenomic databases

KOiK13372.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16553.
BRENDAi1.4.9.2. 232.
SABIO-RKP84888.

Miscellaneous databases

EvolutionaryTraceiP84888.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR009451. Metamine_DH_Hvc.
IPR011044. Quino_amine_DH_bsu.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PfamiPF06433. Me-amine-dh_H. 1 hit.
[Graphical view]
SUPFAMiSSF50969. SSF50969. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAAUB_ALCFA
AccessioniPrimary (citable) accession number: P84888
Secondary accession number(s): Q0VKG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 15, 2007
Last modified: September 7, 2016
This is version 51 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

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.