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Aralkylamine dehydrogenase light chain (EC 1.4.9.2) (Aromatic amine dehydrogenase) (AADH)

 AAUA_ALCFA              Reviewed;         182 AA.
P84887; Q0VKG6;
15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
15-MAY-2007, sequence version 1.
25-OCT-2017, entry version 59.
RecName: Full=Aralkylamine dehydrogenase light chain;
EC=1.4.9.2;
AltName: Full=Aromatic amine dehydrogenase;
Short=AADH;
Flags: Precursor;
Name=aauA {ECO:0000303|PubMed:17087503};
Alcaligenes faecalis.
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
Alcaligenaceae; Alcaligenes.
NCBI_TaxID=511;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
PubMed=11495996;
Chistoserdov A.Y.;
"Cloning, sequencing and mutagenesis of the genes for aromatic amine
dehydrogenase from Alcaligenes faecalis and evolution of amine
dehydrogenases.";
Microbiology 147:2195-2202(2001).
[2] {ECO:0000305, ECO:0000312|EMBL:CAL23525.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 48-53,
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
AND SUBCELLULAR LOCATION.
STRAIN=ATCC 49677 / NBRC 14479 {ECO:0000269|PubMed:16279953,
ECO:0000312|EMBL:CAL23525.1};
PubMed=16279953; DOI=10.1111/j.1742-4658.2005.04990.x;
Hothi P., Khadra K.A., Combe J.P., Leys D., Scrutton N.S.;
"Tryptophan tryptophylquinone cofactor biogenesis in the aromatic
amine dehydrogenase of Alcaligenes faecalis. Cofactor assembly and
catalytic properties of recombinant enzyme expressed in Paracoccus
denitrificans.";
FEBS J. 272:5894-5909(2005).
[3] {ECO:0000305}
PROTEIN SEQUENCE OF 48-64, FUNCTION, COFACTOR, ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
STRAIN=ATCC 49677 / NBRC 14479 {ECO:0000269|PubMed:8188594};
PubMed=8188594; DOI=10.1128/jb.176.10.2922-2929.1994;
Govindaraj S., Eisenstein E., Jones L.H., Sanders-Loehr J.,
Chistoserdov A.Y., Davidson V.L., Edwards S.L.;
"Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone
enzyme.";
J. Bacteriol. 176:2922-2929(1994).
[4] {ECO:0000305}
FUNCTION, AND SUBUNIT.
PubMed=7876189; DOI=10.1074/jbc.270.9.4293;
Edwards S.L., Davidson V.L., Hyun Y.-L., Wingfield P.T.;
"Spectroscopic evidence for a common electron transfer pathway for two
tryptophan tryptophylquinone enzymes.";
J. Biol. Chem. 270:4293-4298(1995).
[5] {ECO:0000305}
CATALYTIC ACTIVITY.
STRAIN=ATCC 49677 / NBRC 14479 {ECO:0000269|PubMed:9494080};
PubMed=9494080; DOI=10.1042/bj3301159;
Bishop G.R., Zhu Z., Whitehead T.L., Hicks R.P., Davidson V.L.;
"Identification of reaction products and intermediates of aromatic-
amine dehydrogenase by 15N and 13C NMR.";
Biochem. J. 330:1159-1163(1998).
[6] {ECO:0000305}
SUBCELLULAR LOCATION.
PubMed=10515948;
Zhu Z., Sun D., Davidson V.L.;
"Localization of periplasmic redox proteins of Alcaligenes faecalis by
a modified general method for fractionating Gram-negative bacteria.";
J. Bacteriol. 181:6540-6542(1999).
[7] {ECO:0000305}
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB
AND AZURIN, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
SUBUNIT, AND DISULFIDE BONDS.
STRAIN=ATCC 49677 / NBRC 14479 {ECO:0000269|PubMed:17087503};
PubMed=17087503; DOI=10.1021/bi0612972;
Sukumar N., Chen Z.-W., Ferrari D., Merli A., Rossi G.L.,
Bellamy H.D., Chistoserdov A.Y., Davidson V.L., Mathews F.S.;
"Crystal structure of an electron transfer complex between aromatic
amine dehydrogenase and azurin from Alcaligenes faecalis.";
Biochemistry 45:13500-13510(2006).
[8] {ECO:0000305}
X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB
AND SUBSTRATE, FUNCTION, COFACTOR, SUBUNIT, AND DISULFIDE BONDS.
STRAIN=ATCC 49677 / NBRC 14479 {ECO:0000269|PubMed:17005560};
PubMed=17005560; DOI=10.1074/jbc.M605559200;
Roujeinikova A., Scrutton N.S., Leys D.;
"Atomic level insight into the oxidative half-reaction of aromatic
amine dehydrogenase.";
J. Biol. Chem. 281:40264-40272(2006).
[9] {ECO:0000305}
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB
AND SUBSTRATE, FUNCTION, COFACTOR, SUBUNIT, AND DISULFIDE BONDS.
STRAIN=ATCC 49677 / NBRC 14479 {ECO:0000269|PubMed:16614214};
PubMed=16614214; DOI=10.1126/science.1126002;
Masgrau L., Roujeinikova A., Johannissen L.O., Hothi P., Basran J.,
Ranaghan K.E., Mulholland A.J., Sutcliffe M.J., Scrutton N.S.,
Leys D.;
"Atomic description of an enzyme reaction dominated by proton
tunneling.";
Science 312:237-241(2006).
-!- FUNCTION: 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. {ECO:0000269|PubMed:11495996,
ECO:0000269|PubMed:16279953, ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503,
ECO:0000269|PubMed:7876189, ECO:0000269|PubMed:8188594}.
-!- CATALYTIC ACTIVITY: ArCH(2)NH(2) + H(2)O + 2 azurin = ArCHO +
NH(3) + 2 reduced azurin. {ECO:0000269|PubMed:16279953,
ECO:0000269|PubMed:9494080}.
-!- COFACTOR:
Name=tryptophan tryptophylquinone residue; Xref=ChEBI:CHEBI:20251;
Evidence={ECO:0000269|PubMed:16279953,
ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503, ECO:0000269|PubMed:8188594};
Note=Uses a protein-derived tryptophan tryptophylquinone (TTQ)
cofactor. {ECO:0000269|PubMed:16279953,
ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503, ECO:0000269|PubMed:8188594};
-!- ENZYME REGULATION: Irreversibly inhibited by phenylhydrazine,
hydroxylamine, semicarbazide, hydrazine and aminoguanidine.
Reversibly inhibited by isonicotinic acid hydrazide (isoniazid)
and isonicotinic acid 2-isopropyl hydrazide (iproniazid).
{ECO:0000269|PubMed:8188594}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Absorption:
Abs(max)=465 nm {ECO:0000269|PubMed:16279953,
ECO:0000269|PubMed:17087503, ECO:0000269|PubMed:8188594};
Note=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.
{ECO:0000269|PubMed:16279953, ECO:0000269|PubMed:17087503};
Kinetic parameters:
KM=5.4 uM for tyramine {ECO:0000269|PubMed:16279953,
ECO:0000269|PubMed:17087503, ECO:0000269|PubMed:8188594};
Vmax=17 umol/min/mg enzyme {ECO:0000269|PubMed:16279953,
ECO:0000269|PubMed:17087503, ECO:0000269|PubMed:8188594};
Note=The enzyme is substrate inhibited at high substrate
concentrations (Ki=1.08 mM for tyramine).
{ECO:0000269|PubMed:8188594};
-!- SUBUNIT: Heterotetramer of two light and two heavy chains. Binds
two azurin molecules per heterotetramer.
{ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503, ECO:0000269|PubMed:7876189,
ECO:0000269|PubMed:8188594}.
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10515948,
ECO:0000269|PubMed:16279953}.
-!- PTM: 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.
{ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503, ECO:0000269|PubMed:8188594}.
-!- PTM: Predicted to be exported by the Tat system. The position of
the signal peptide cleavage has been experimentally proven.
-!- SIMILARITY: Belongs to the aromatic amine dehydrogenase light
chain family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF302652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AM292629; CAL23525.1; -; Genomic_DNA.
RefSeq; WP_021447059.1; NZ_MSZR01000001.1.
PDB; 2AGL; X-ray; 1.40 A; D/H=48-182.
PDB; 2AGW; X-ray; 1.45 A; D/H=48-182.
PDB; 2AGX; X-ray; 2.20 A; D/H=48-182.
PDB; 2AGY; X-ray; 1.10 A; D/H=48-182.
PDB; 2AGZ; X-ray; 1.60 A; D/H=48-182.
PDB; 2AH0; X-ray; 1.45 A; D/H=48-182.
PDB; 2AH1; X-ray; 1.20 A; D/H=48-182.
PDB; 2H3X; X-ray; 2.50 A; B/E=48-182.
PDB; 2H47; X-ray; 2.60 A; B/E/G/I=48-182.
PDB; 2HJ4; X-ray; 1.80 A; D/H=48-182.
PDB; 2HJB; X-ray; 1.85 A; D/H=48-182.
PDB; 2HKM; X-ray; 1.50 A; D/H=48-182.
PDB; 2HKR; X-ray; 1.40 A; D/H=59-180.
PDB; 2HXC; X-ray; 1.45 A; D/H=48-182.
PDB; 2I0R; X-ray; 1.40 A; D/H=59-182.
PDB; 2I0S; X-ray; 1.40 A; D/H=59-182.
PDB; 2I0T; X-ray; 1.35 A; D/H=59-180.
PDB; 2IAA; X-ray; 1.95 A; B/E=48-182.
PDB; 2IUP; X-ray; 1.80 A; D/H=48-182.
PDB; 2IUQ; X-ray; 1.50 A; D/H=48-182.
PDB; 2IUR; X-ray; 1.30 A; D/H=48-182.
PDB; 2IUV; X-ray; 1.55 A; D/H=48-182.
PDB; 2OIZ; X-ray; 1.05 A; D/H=48-182.
PDB; 2OJY; X-ray; 1.60 A; D/H=48-180.
PDB; 2OK4; X-ray; 1.45 A; D/H=48-182.
PDB; 2OK6; X-ray; 1.45 A; D/H=48-182.
PDB; 2Q7Q; X-ray; 1.60 A; D/H=59-182.
PDBsum; 2AGL; -.
PDBsum; 2AGW; -.
PDBsum; 2AGX; -.
PDBsum; 2AGY; -.
PDBsum; 2AGZ; -.
PDBsum; 2AH0; -.
PDBsum; 2AH1; -.
PDBsum; 2H3X; -.
PDBsum; 2H47; -.
PDBsum; 2HJ4; -.
PDBsum; 2HJB; -.
PDBsum; 2HKM; -.
PDBsum; 2HKR; -.
PDBsum; 2HXC; -.
PDBsum; 2I0R; -.
PDBsum; 2I0S; -.
PDBsum; 2I0T; -.
PDBsum; 2IAA; -.
PDBsum; 2IUP; -.
PDBsum; 2IUQ; -.
PDBsum; 2IUR; -.
PDBsum; 2IUV; -.
PDBsum; 2OIZ; -.
PDBsum; 2OJY; -.
PDBsum; 2OK4; -.
PDBsum; 2OK6; -.
PDBsum; 2Q7Q; -.
ProteinModelPortal; P84887; -.
SMR; P84887; -.
DrugBank; DB08649; (1S)-1-AMINO-2-(1H-INDOL-3-YL)ETHANOL.
DrugBank; DB08652; 2-(1H-INDOL-3-YL)ACETAMIDE.
DrugBank; DB08653; 2-(1H-INDOL-3-YL)ETHANAMINE.
DrugBank; DB08767; 2-(4-METHOXYPHENYL)ACETAMIDE.
GeneID; 29369385; -.
KEGG; ag:CAL23525; -.
KO; K13371; -.
BioCyc; MetaCyc:MONOMER-16554; -.
BRENDA; 1.4.9.2; 232.
SABIO-RK; P84887; -.
EvolutionaryTrace; P84887; -.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0030058; F:amine dehydrogenase activity; IEA:InterPro.
GO; GO:0030059; F:aralkylamine dehydrogenase (azurin) activity; IEA:UniProtKB-EC.
GO; GO:0009308; P:amine metabolic process; IEA:InterPro.
Gene3D; 2.60.30.10; -; 1.
InterPro; IPR016008; Amine_DH_Ltc.
InterPro; IPR036560; MADH/AADH_L_sf.
InterPro; IPR013504; MADH/AADH_Ltc_C_dom.
InterPro; IPR006311; TAT_signal.
Pfam; PF02975; Me-amine-dh_L; 1.
PIRSF; PIRSF000192; Amine_dh_beta; 1.
SUPFAM; SSF57561; SSF57561; 1.
PROSITE; PS51318; TAT; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Disulfide bond;
Electron transport; Oxidoreductase; Periplasm; Signal; Transport; TTQ.
SIGNAL 1 47 Tat-type signal. {ECO:0000255|PROSITE-
ProRule:PRU00648,
ECO:0000269|PubMed:16279953,
ECO:0000269|PubMed:8188594}.
CHAIN 48 182 Aralkylamine dehydrogenase light chain.
{ECO:0000255|PROSITE-ProRule:PRU00648,
ECO:0000269|PubMed:8188594}.
/FTId=PRO_0000287911.
REGION 156 158 Substrate-binding.
{ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560}.
ACT_SITE 109 109 Tryptophylquinone 6'-substrate hemiaminal
intermediate.
ACT_SITE 128 128 Proton acceptor.
{ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560}.
BINDING 84 84 Substrate. {ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560}.
SITE 172 172 Transition state stabilizer.
MOD_RES 109 109 Tryptophylquinone.
{ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503}.
DISULFID 75 140 {ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503}.
DISULFID 81 113 {ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503}.
DISULFID 88 171 {ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503}.
DISULFID 90 138 {ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503}.
DISULFID 91 135 {ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503}.
DISULFID 98 129 {ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503}.
DISULFID 130 161 {ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503}.
CROSSLNK 109 160 Tryptophan tryptophylquinone (Trp-Trp).
{ECO:0000269|PubMed:16614214,
ECO:0000269|PubMed:17005560,
ECO:0000269|PubMed:17087503}.
HELIX 60 62 {ECO:0000244|PDB:2OIZ}.
HELIX 64 66 {ECO:0000244|PDB:2OIZ}.
HELIX 69 72 {ECO:0000244|PDB:2I0T}.
HELIX 78 80 {ECO:0000244|PDB:2OIZ}.
STRAND 84 87 {ECO:0000244|PDB:2OIZ}.
HELIX 88 90 {ECO:0000244|PDB:2OIZ}.
STRAND 95 97 {ECO:0000244|PDB:2IAA}.
STRAND 109 114 {ECO:0000244|PDB:2OIZ}.
TURN 116 118 {ECO:0000244|PDB:2OIZ}.
STRAND 121 126 {ECO:0000244|PDB:2OIZ}.
STRAND 128 132 {ECO:0000244|PDB:2OIZ}.
STRAND 137 141 {ECO:0000244|PDB:2OIZ}.
HELIX 149 154 {ECO:0000244|PDB:2OIZ}.
TURN 160 163 {ECO:0000244|PDB:2OIZ}.
STRAND 164 166 {ECO:0000244|PDB:2OIZ}.
STRAND 169 172 {ECO:0000244|PDB:2OIZ}.
STRAND 175 179 {ECO:0000244|PDB:2OIZ}.
SEQUENCE 182 AA; 19652 MW; 74BC95478B172A41 CRC64;
MRWLDKFGES LSRSVAHKTS RRSVLRSVGK LMVGSAFVLP VLPVARAAGG GGSSSGADHI
SLNPDLANED EVNSCDYWRH CAVDGFLCSC CGGTTTTCPP GSTPSPISWI GTCHNPHDGK
DYLISYHDCC GKTACGRCQC NTQTRERPGY EFFLHNDVNW CMANENSTFH CTTSVLVGLA
KN


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