AAUB_ALCFA
ID AAUB_ALCFA Reviewed; 390 AA.
AC P84888; Q0VKG7;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Aralkylamine dehydrogenase heavy chain;
DE EC=1.4.9.2;
DE AltName: Full=Aromatic amine dehydrogenase;
DE Short=AADH;
DE Flags: Precursor;
GN Name=aauB {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:CAL23524.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, MASS
RP SPECTROMETRY, AND PYROGLUTAMATE FORMATION AT GLN-26.
RC STRAIN=ATCC 49677 / NBRC 14479 {ECO:0000269|PubMed:16279953,
RC ECO:0000312|EMBL:CAL23524.1};
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 FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP BLOCKAGE OF THE N-TERMINUS.
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 INTERACTION WITH AZURIN.
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 26-390 IN COMPLEX WITH AAUA AND
RP AZURIN, SUBUNIT, AND DISULFIDE BOND.
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 (2.5 ANGSTROMS) OF 26-390 IN COMPLEX WITH AAUA AND
RP SUBSTRATE, SUBUNIT, AND DISULFIDE BOND.
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 (1.20 ANGSTROMS) OF 26-390 IN COMPLEX WITH AAUA AND
RP SUBSTRATE, FUNCTION, SUBUNIT, AND DISULFIDE BOND.
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: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:9494080};
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 Kinetic parameters:
CC KM=5.4 uM for tyramine {ECO:0000269|PubMed:8188594};
CC Vmax=17 umol/min/mg enzyme {ECO:0000269|PubMed:8188594};
CC Note=The enzyme is substrate inhibited at high substrate
CC concentrations (Ki=1.08 mM for tyramine).;
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:8188594}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10515948,
CC ECO:0000269|PubMed:16279953}.
CC -!- MASS SPECTROMETRY: Mass=40422; Mass_error=1; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:16279953};
CC -!- SIMILARITY: Belongs to the aromatic amine dehydrogenase heavy chain
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF302652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AM292628; CAL23524.1; -; Genomic_DNA.
DR RefSeq; WP_009462712.1; NZ_KQ954451.1.
DR PDB; 2AGL; X-ray; 1.40 A; A/B=30-389.
DR PDB; 2AGW; X-ray; 1.45 A; A/B=30-389.
DR PDB; 2AGX; X-ray; 2.20 A; A/B=30-389.
DR PDB; 2AGY; X-ray; 1.10 A; A/B=30-389.
DR PDB; 2AGZ; X-ray; 1.60 A; A/B=30-389.
DR PDB; 2AH0; X-ray; 1.45 A; A/B=30-389.
DR PDB; 2AH1; X-ray; 1.20 A; A/B=30-389.
DR PDB; 2H3X; X-ray; 2.50 A; A/D=1-390.
DR PDB; 2H47; X-ray; 2.60 A; A/D/F/H=1-390.
DR PDB; 2HJ4; X-ray; 1.80 A; A/B=30-389.
DR PDB; 2HJB; X-ray; 1.85 A; A/B=30-389.
DR PDB; 2HKM; X-ray; 1.50 A; A/B=29-389.
DR PDB; 2HKR; X-ray; 1.40 A; A/B=29-389.
DR PDB; 2HXC; X-ray; 1.45 A; A/B=30-389.
DR PDB; 2I0R; X-ray; 1.40 A; A/B=30-389.
DR PDB; 2I0S; X-ray; 1.40 A; A/B=31-389.
DR PDB; 2I0T; X-ray; 1.35 A; A/B=30-389.
DR PDB; 2IAA; X-ray; 1.95 A; A/D=1-390.
DR PDB; 2IUP; X-ray; 1.80 A; A/B=30-389.
DR PDB; 2IUQ; X-ray; 1.50 A; A/B=30-389.
DR PDB; 2IUR; X-ray; 1.30 A; A/B=30-389.
DR PDB; 2IUV; X-ray; 1.55 A; A/B=30-389.
DR PDB; 2OIZ; X-ray; 1.05 A; A/B=30-389.
DR PDB; 2OJY; X-ray; 1.60 A; A/B=29-389.
DR PDB; 2OK4; X-ray; 1.45 A; A/B=30-389.
DR PDB; 2OK6; X-ray; 1.45 A; A/B=30-389.
DR PDB; 2Q7Q; X-ray; 1.60 A; A/B=30-390.
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; P84888; -.
DR SMR; P84888; -.
DR STRING; 511.JT27_04295; -.
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 KEGG; ag:CAL23524; -.
DR eggNOG; COG3391; Bacteria.
DR BioCyc; MetaCyc:MON-16553; -.
DR BRENDA; 1.4.9.2; 232.
DR SABIO-RK; P84888; -.
DR EvolutionaryTrace; P84888; -.
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 Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR009451; Metamine_DH_Hvc.
DR InterPro; IPR011044; Quino_amine_DH_bsu.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF06433; Me-amine-dh_H; 1.
DR SUPFAM; SSF50969; SSF50969; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Electron transport; Oxidoreductase;
KW Periplasm; Pyrrolidone carboxylic acid; Signal; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:16279953,
FT ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560,
FT ECO:0000269|PubMed:17087503, ECO:0000269|PubMed:8188594"
FT CHAIN 26..390
FT /note="Aralkylamine dehydrogenase heavy chain"
FT /evidence="ECO:0000269|PubMed:16279953,
FT ECO:0000269|PubMed:16614214, ECO:0000269|PubMed:17005560,
FT ECO:0000269|PubMed:17087503, ECO:0000269|PubMed:8188594"
FT /id="PRO_0000287910"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16614214,
FT ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16614214,
FT ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16614214,
FT ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503"
FT MOD_RES 26
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:16279953"
FT DISULFID 182..199
FT /evidence="ECO:0000269|PubMed:16614214,
FT ECO:0000269|PubMed:17005560, ECO:0000269|PubMed:17087503"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:2OIZ"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:2OIZ"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 90..100
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 108..116
FT /evidence="ECO:0007829|PDB:2OIZ"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:2OIZ"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 148..166
FT /evidence="ECO:0007829|PDB:2OIZ"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:2OIZ"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 191..199
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 202..209
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 213..220
FT /evidence="ECO:0007829|PDB:2OIZ"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 240..247
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 263..270
FT /evidence="ECO:0007829|PDB:2OIZ"
FT HELIX 273..277
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:2H3X"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:2OIZ"
FT TURN 292..295
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 296..304
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 315..321
FT /evidence="ECO:0007829|PDB:2OIZ"
FT TURN 322..325
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 326..332
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 338..342
FT /evidence="ECO:0007829|PDB:2OIZ"
FT TURN 343..346
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 367..372
FT /evidence="ECO:0007829|PDB:2OIZ"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:2OIZ"
SQ SEQUENCE 390 AA; 42925 MW; 0AFCC1129CC44FAC CRC64;
MKSKFKLTTA AAMLGLMVLA GGAQAQDKPR EVLTGGHSVS APQENRIYVM DSVFMHLTES
RVHVYDYTNG KFLGMVPTAF NGHVQVSNDG KKIYTMTTYH ERITRGKRSD VVEVWDADKL
TFEKEISLPP KRVQGLNYDG LFRQTTDGKF IVLQNASPAT SIGIVDVAKG DYVEDVTAAA
GCWSVIPQPN RPRSFMTICG DGGLLTINLG EDGKVASQSR SKQMFSVKDD PIFIAPALDK
DKAHFVSYYG NVYSADFSGD EVKVDGPWSL LNDEDKAKNW VPGGYNLVGL HRASGRMYVF
MHPDGKEGTH KFPAAEIWVM DTKTKQRVAR IPGRDALSMT IDQQRNLMLT LDGGNVNVYD
ISQPEPKLLR TIEGAAEASL QVQFHPVGGV
