AAUA_ALCFA
ID AAUA_ALCFA Reviewed; 182 AA.
AC P84887; Q0VKG6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Aralkylamine dehydrogenase light chain;
DE EC=1.4.9.2;
DE AltName: Full=Aromatic amine dehydrogenase;
DE Short=AADH;
DE Flags: Precursor;
GN Name=aauA {ECO:0000303|PubMed:17087503};
OS Alcaligenes faecalis.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Alcaligenes.
OX NCBI_TaxID=511;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=11495996; DOI=10.1099/00221287-147-8-2195;
RA Chistoserdov A.Y.;
RT "Cloning, sequencing and mutagenesis of the genes for aromatic amine
RT dehydrogenase from Alcaligenes faecalis and evolution of amine
RT dehydrogenases.";
RL Microbiology 147:2195-2202(2001).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAL23525.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 48-53, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 49677 / NBRC 14479 {ECO:0000269|PubMed:16279953,
RC ECO:0000312|EMBL:CAL23525.1};
RX PubMed=16279953; DOI=10.1111/j.1742-4658.2005.04990.x;
RA Hothi P., Khadra K.A., Combe J.P., Leys D., Scrutton N.S.;
RT "Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine
RT dehydrogenase of Alcaligenes faecalis. Cofactor assembly and catalytic
RT properties of recombinant enzyme expressed in Paracoccus denitrificans.";
RL FEBS J. 272:5894-5909(2005).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 48-64, FUNCTION, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 49677 / NBRC 14479 {ECO:0000269|PubMed:8188594};
RX PubMed=8188594; DOI=10.1128/jb.176.10.2922-2929.1994;
RA Govindaraj S., Eisenstein E., Jones L.H., Sanders-Loehr J.,
RA Chistoserdov A.Y., Davidson V.L., Edwards S.L.;
RT "Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone
RT enzyme.";
RL J. Bacteriol. 176:2922-2929(1994).
RN [4] {ECO:0000305}
RP FUNCTION, AND SUBUNIT.
RX PubMed=7876189; DOI=10.1074/jbc.270.9.4293;
RA Edwards S.L., Davidson V.L., Hyun Y.-L., Wingfield P.T.;
RT "Spectroscopic evidence for a common electron transfer pathway for two
RT tryptophan tryptophylquinone enzymes.";
RL J. Biol. Chem. 270:4293-4298(1995).
RN [5] {ECO:0000305}
RP CATALYTIC ACTIVITY.
RC STRAIN=ATCC 49677 / NBRC 14479 {ECO:0000269|PubMed:9494080};
RX PubMed=9494080; DOI=10.1042/bj3301159;
RA Bishop G.R., Zhu Z., Whitehead T.L., Hicks R.P., Davidson V.L.;
RT "Identification of reaction products and intermediates of aromatic-amine
RT dehydrogenase by 15N and 13C NMR.";
RL Biochem. J. 330:1159-1163(1998).
RN [6] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=10515948; DOI=10.1128/jb.181.20.6540-6542.1999;
RA Zhu Z., Sun D., Davidson V.L.;
RT "Localization of periplasmic redox proteins of Alcaligenes faecalis by a
RT modified general method for fractionating Gram-negative bacteria.";
RL J. Bacteriol. 181:6540-6542(1999).
RN [7] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB AND
RP AZURIN, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP DISULFIDE BONDS.
RC STRAIN=ATCC 49677 / NBRC 14479 {ECO:0000269|PubMed:17087503};
RX PubMed=17087503; DOI=10.1021/bi0612972;
RA Sukumar N., Chen Z.-W., Ferrari D., Merli A., Rossi G.L., Bellamy H.D.,
RA Chistoserdov A.Y., Davidson V.L., Mathews F.S.;
RT "Crystal structure of an electron transfer complex between aromatic amine
RT dehydrogenase and azurin from Alcaligenes faecalis.";
RL Biochemistry 45:13500-13510(2006).
RN [8] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB AND
RP SUBSTRATE, FUNCTION, COFACTOR, SUBUNIT, AND DISULFIDE BONDS.
RC STRAIN=ATCC 49677 / NBRC 14479 {ECO:0000269|PubMed:17005560};
RX PubMed=17005560; DOI=10.1074/jbc.m605559200;
RA Roujeinikova A., Scrutton N.S., Leys D.;
RT "Atomic level insight into the oxidative half-reaction of aromatic amine
RT dehydrogenase.";
RL J. Biol. Chem. 281:40264-40272(2006).
RN [9] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 48-182 IN COMPLEX WITH AAUB AND
RP SUBSTRATE, FUNCTION, COFACTOR, SUBUNIT, AND DISULFIDE BONDS.
RC STRAIN=ATCC 49677 / NBRC 14479 {ECO:0000269|PubMed:16614214};
RX PubMed=16614214; DOI=10.1126/science.1126002;
RA Masgrau L., Roujeinikova A., Johannissen L.O., Hothi P., Basran J.,
RA Ranaghan K.E., Mulholland A.J., Sutcliffe M.J., Scrutton N.S., Leys D.;
RT "Atomic description of an enzyme reaction dominated by proton tunneling.";
RL Science 312:237-241(2006).
CC -!- FUNCTION: Oxidizes primary aromatic amines and, more slowly, some long-
CC chain aliphatic amines, but not methylamine or ethylamine. Uses azurin
CC as an electron acceptor to transfer electrons from the reduced
CC tryptophylquinone cofactor. {ECO:0000269|PubMed:11495996,
CC ECO:0000269|PubMed:16279953, ECO:0000269|PubMed:16614214,
CC ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503,
CC ECO:0000269|PubMed:7876189, ECO:0000269|PubMed:8188594}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aralkylamine + H2O + 2 oxidized [azurin] = an aromatic
CC aldehyde + 2 H(+) + NH4(+) + 2 reduced [azurin];
CC Xref=Rhea:RHEA:47796, Rhea:RHEA-COMP:11034, Rhea:RHEA-COMP:11035,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29036, ChEBI:CHEBI:33855, ChEBI:CHEBI:49552,
CC ChEBI:CHEBI:88332; EC=1.4.9.2; Evidence={ECO:0000269|PubMed:16279953,
CC ECO:0000269|PubMed:9494080};
CC -!- COFACTOR:
CC Name=tryptophan tryptophylquinone residue; Xref=ChEBI:CHEBI:20251;
CC Evidence={ECO:0000269|PubMed:16279953, ECO:0000269|PubMed:16614214,
CC ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503,
CC ECO:0000269|PubMed:8188594};
CC Note=Uses a protein-derived tryptophan tryptophylquinone (TTQ)
CC cofactor. {ECO:0000269|PubMed:16279953, ECO:0000269|PubMed:16614214,
CC ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503,
CC ECO:0000269|PubMed:8188594};
CC -!- ACTIVITY REGULATION: Irreversibly inhibited by phenylhydrazine,
CC hydroxylamine, semicarbazide, hydrazine and aminoguanidine. Reversibly
CC inhibited by isonicotinic acid hydrazide (isoniazid) and isonicotinic
CC acid 2-isopropyl hydrazide (iproniazid). {ECO:0000269|PubMed:8188594}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=465 nm {ECO:0000269|PubMed:16279953,
CC ECO:0000269|PubMed:17087503, ECO:0000269|PubMed:8188594};
CC Note=The above maximum is for the oxidized form. Shows a maximal peak
CC at 330 nm in the reduced form. These absorption peaks are for the
CC tryptophylquinone cofactor. {ECO:0000269|PubMed:16279953,
CC ECO:0000269|PubMed:17087503};
CC Kinetic parameters:
CC KM=5.4 uM for tyramine {ECO:0000269|PubMed:16279953,
CC ECO:0000269|PubMed:17087503, ECO:0000269|PubMed:8188594};
CC Vmax=17 umol/min/mg enzyme {ECO:0000269|PubMed:16279953,
CC ECO:0000269|PubMed:17087503, ECO:0000269|PubMed:8188594};
CC Note=The enzyme is substrate inhibited at high substrate
CC concentrations (Ki=1.08 mM for tyramine).
CC {ECO:0000269|PubMed:8188594};
CC -!- SUBUNIT: Heterotetramer of two light and two heavy chains. Binds two
CC azurin molecules per heterotetramer. {ECO:0000269|PubMed:16614214,
CC ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503,
CC ECO:0000269|PubMed:7876189, ECO:0000269|PubMed:8188594}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10515948,
CC ECO:0000269|PubMed:16279953}.
CC -!- PTM: Tryptophan tryptophylquinone (TTQ) is formed by oxidation of the
CC indole ring of a tryptophan to form tryptophylquinone followed by
CC covalent cross-linking with another tryptophan residue.
CC {ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560,
CC ECO:0000269|PubMed:17087503, ECO:0000269|PubMed:8188594}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has been experimentally proven.
CC -!- SIMILARITY: Belongs to the aromatic amine dehydrogenase light chain
CC family. {ECO:0000305}.
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DR EMBL; AF302652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AM292629; CAL23525.1; -; Genomic_DNA.
DR RefSeq; WP_021447059.1; NZ_RHXK01000003.1.
DR PDB; 2AGL; X-ray; 1.40 A; D/H=48-182.
DR PDB; 2AGW; X-ray; 1.45 A; D/H=48-182.
DR PDB; 2AGX; X-ray; 2.20 A; D/H=48-182.
DR PDB; 2AGY; X-ray; 1.10 A; D/H=48-182.
DR PDB; 2AGZ; X-ray; 1.60 A; D/H=48-182.
DR PDB; 2AH0; X-ray; 1.45 A; D/H=48-182.
DR PDB; 2AH1; X-ray; 1.20 A; D/H=48-182.
DR PDB; 2H3X; X-ray; 2.50 A; B/E=48-182.
DR PDB; 2H47; X-ray; 2.60 A; B/E/G/I=48-182.
DR PDB; 2HJ4; X-ray; 1.80 A; D/H=48-182.
DR PDB; 2HJB; X-ray; 1.85 A; D/H=48-182.
DR PDB; 2HKM; X-ray; 1.50 A; D/H=48-182.
DR PDB; 2HKR; X-ray; 1.40 A; D/H=59-180.
DR PDB; 2HXC; X-ray; 1.45 A; D/H=48-182.
DR PDB; 2I0R; X-ray; 1.40 A; D/H=59-182.
DR PDB; 2I0S; X-ray; 1.40 A; D/H=59-182.
DR PDB; 2I0T; X-ray; 1.35 A; D/H=59-180.
DR PDB; 2IAA; X-ray; 1.95 A; B/E=48-182.
DR PDB; 2IUP; X-ray; 1.80 A; D/H=48-182.
DR PDB; 2IUQ; X-ray; 1.50 A; D/H=48-182.
DR PDB; 2IUR; X-ray; 1.30 A; D/H=48-182.
DR PDB; 2IUV; X-ray; 1.55 A; D/H=48-182.
DR PDB; 2OIZ; X-ray; 1.05 A; D/H=48-182.
DR PDB; 2OJY; X-ray; 1.60 A; D/H=48-180.
DR PDB; 2OK4; X-ray; 1.45 A; D/H=48-182.
DR PDB; 2OK6; X-ray; 1.45 A; D/H=48-182.
DR PDB; 2Q7Q; X-ray; 1.60 A; D/H=59-182.
DR PDBsum; 2AGL; -.
DR PDBsum; 2AGW; -.
DR PDBsum; 2AGX; -.
DR PDBsum; 2AGY; -.
DR PDBsum; 2AGZ; -.
DR PDBsum; 2AH0; -.
DR PDBsum; 2AH1; -.
DR PDBsum; 2H3X; -.
DR PDBsum; 2H47; -.
DR PDBsum; 2HJ4; -.
DR PDBsum; 2HJB; -.
DR PDBsum; 2HKM; -.
DR PDBsum; 2HKR; -.
DR PDBsum; 2HXC; -.
DR PDBsum; 2I0R; -.
DR PDBsum; 2I0S; -.
DR PDBsum; 2I0T; -.
DR PDBsum; 2IAA; -.
DR PDBsum; 2IUP; -.
DR PDBsum; 2IUQ; -.
DR PDBsum; 2IUR; -.
DR PDBsum; 2IUV; -.
DR PDBsum; 2OIZ; -.
DR PDBsum; 2OJY; -.
DR PDBsum; 2OK4; -.
DR PDBsum; 2OK6; -.
DR PDBsum; 2Q7Q; -.
DR AlphaFoldDB; P84887; -.
DR SMR; P84887; -.
DR STRING; 511.JT27_04310; -.
DR DrugBank; DB08649; (1S)-1-AMINO-2-(1H-INDOL-3-YL)ETHANOL.
DR DrugBank; DB08767; 2-(4-METHOXYPHENYL)ACETAMIDE.
DR DrugBank; DB08652; Indoleacetamide.
DR DrugBank; DB08653; Tryptamine.
DR GeneID; 29369385; -.
DR KEGG; ag:CAL23525; -.
DR eggNOG; ENOG502ZHBX; Bacteria.
DR OrthoDB; 1619371at2; -.
DR BioCyc; MetaCyc:MON-16554; -.
DR BRENDA; 1.4.9.2; 232.
DR SABIO-RK; P84887; -.
DR EvolutionaryTrace; P84887; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0030058; F:amine dehydrogenase activity; IEA:InterPro.
DR GO; GO:0030059; F:aralkylamine dehydrogenase (azurin) activity; IEA:UniProtKB-EC.
DR GO; GO:0009308; P:amine metabolic process; IEA:InterPro.
DR Gene3D; 2.60.30.10; -; 1.
DR InterPro; IPR016008; Amine_DH_Ltc.
DR InterPro; IPR036560; MADH/AADH_L_sf.
DR InterPro; IPR013504; MADH/AADH_Ltc_C_dom.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF02975; Me-amine-dh_L; 1.
DR PIRSF; PIRSF000192; Amine_dh_beta; 1.
DR SUPFAM; SSF57561; SSF57561; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Electron transport; Oxidoreductase; Periplasm; Signal; Transport; TTQ.
FT SIGNAL 1..47
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:16279953, ECO:0000269|PubMed:8188594"
FT CHAIN 48..182
FT /note="Aralkylamine dehydrogenase light chain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:8188594"
FT /id="PRO_0000287911"
FT ACT_SITE 109
FT /note="Tryptophylquinone 6'-substrate hemiaminal
FT intermediate"
FT ACT_SITE 128
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:16614214,
FT ECO:0000269|PubMed:17005560"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16614214,
FT ECO:0000269|PubMed:17005560"
FT BINDING 156..158
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16614214,
FT ECO:0000269|PubMed:17005560"
FT SITE 172
FT /note="Transition state stabilizer"
FT MOD_RES 109
FT /note="Tryptophylquinone"
FT /evidence="ECO:0000269|PubMed:16614214,
FT ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503"
FT DISULFID 75..140
FT /evidence="ECO:0000269|PubMed:16614214,
FT ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503"
FT DISULFID 81..113
FT /evidence="ECO:0000269|PubMed:16614214,
FT ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503"
FT DISULFID 88..171
FT /evidence="ECO:0000269|PubMed:16614214,
FT ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503"
FT DISULFID 90..138
FT /evidence="ECO:0000269|PubMed:16614214,
FT ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503"
FT DISULFID 91..135
FT /evidence="ECO:0000269|PubMed:16614214,
FT ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503"
FT DISULFID 98..129
FT /evidence="ECO:0000269|PubMed:16614214,
FT ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503"
FT DISULFID 130..161
FT /evidence="ECO:0000269|PubMed:16614214,
FT ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503"
FT CROSSLNK 109..160
FT /note="Tryptophan tryptophylquinone (Trp-Trp)"
FT /evidence="ECO:0000269|PubMed:16614214,
FT ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:2OIZ"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:2OIZ"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:2I0T"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:2OIZ"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:2IAA"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:2OIZ"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:2OIZ"
FT HELIX 149..154
FT /evidence="ECO:0007829|PDB:2OIZ"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:2OIZ"
SQ 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
