QADG_PSEPU
ID QADG_PSEPU Reviewed; 79 AA.
AC P0A182; Q88HA0; Q8VW83;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Quinohemoprotein amine dehydrogenase subunit gamma;
DE Short=QH-AmDH {ECO:0000303|PubMed:11555656};
DE EC=1.4.9.- {ECO:0000269|PubMed:27315927};
DE AltName: Full=Quinohemoprotein amine dehydrogenase 9 kDa subunit;
DE AltName: Full=Quinohemoprotein amine dehydrogenase catalytic subunit;
GN Name=qhnDH;
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-79, MASS
RP SPECTROMETRY, AND COFACTOR.
RC STRAIN=ATCC 12633 / DSM 291 / JCM 13063 / CCUG 12690 / LMG 2257 / NBRC
RC 14164 / NCIMB 9494 / NCTC 10936 / VKM B-2187 / Stanier 90, and IFO 15633;
RX PubMed=11555656; DOI=10.1074/jbc.m107164200;
RA Vandenberghe I., Kim J.-K., Devreese B., Hacisalihoglu A., Iwabuki H.,
RA Okajima T., Kuroda S., Adachi O., Jongejan J.A., Duine J.A., Tanizawa K.,
RA van Beeumen J.;
RT "The covalent structure of the small subunit from Pseudomonas putida amine
RT dehydrogenase reveals the presence of three novel types of internal cross-
RT linkages, all involving cysteine in a thioether bond.";
RL J. Biol. Chem. 276:42923-42931(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=IFO 15366;
RX PubMed=27315927; DOI=10.1271/bbb.62.469;
RA Adachi O., Kubota T., Hacisalihoglu A., Toyama H., Shinagawa E.,
RA Duine J.A., Matsushita K.;
RT "Characterization of quinohemoprotein amine dehydrogenase from Pseudomonas
RT putida.";
RL Biosci. Biotechnol. Biochem. 62:469-478(1998).
RN [3] {ECO:0007744|PDB:1JMX, ECO:0007744|PDB:1JMZ}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), COFACTOR, SUBUNIT, AND ACTIVE SITE.
RX PubMed=11704672; DOI=10.1074/jbc.m109090200;
RA Satoh A., Kim J.K., Miyahara I., Devreese B., Vandenberghe I.,
RA Hacisalihoglu A., Okajima T., Kuroda S., Adachi O., Duine J.A.,
RA Van Beeumen J., Tanizawa K., Hirotsu K.;
RT "Crystal structure of quinohemoprotein amine dehydrogenase from Pseudomonas
RT putida. Identification of a novel quinone cofactor encaged by multiple
RT thioether cross-bridges.";
RL J. Biol. Chem. 277:2830-2834(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR PNPH,
RP SUBUNIT, AND ACTIVE SITE.
RX PubMed=12686145; DOI=10.1016/s1570-9639(03)00069-4;
RA Satoh A., Adachi O., Tanizawa K., Hirotsu K.;
RT "The active site structure of quinohemoprotein amine dehydrogenase
RT inhibited by p-nitrophenylhydrazine.";
RL Biochim. Biophys. Acta 1647:272-277(2003).
CC -!- FUNCTION: Catalyzes the oxidative deamination of a wide range of
CC aliphatic monoamines and diamines (PubMed:27315927). The physiological
CC electron acceptor is an azurin-like blue protein (PubMed:27315927).
CC {ECO:0000269|PubMed:27315927}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + an aliphatic amine + H2O = AH2 + an aldehyde + NH4(+);
CC Xref=Rhea:RHEA:51128, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:17499, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58001; Evidence={ECO:0000269|PubMed:27315927};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51129;
CC Evidence={ECO:0000269|PubMed:27315927};
CC -!- COFACTOR:
CC Name=cysteine tryptophylquinone residue; Xref=ChEBI:CHEBI:20252;
CC Evidence={ECO:0000269|PubMed:11555656, ECO:0000269|PubMed:11704672};
CC Note=Contains 1 cysteine tryptophylquinone per subunit.
CC {ECO:0000269|PubMed:11555656, ECO:0000269|PubMed:11704672};
CC -!- ACTIVITY REGULATION: Inhibited by various carbonyl reagents, such as p-
CC nitrophenylhydrazine (pNPH), 2,4-dinitrophenylhydrazine, semicarbazide
CC and hydroxylamine. {ECO:0000269|PubMed:27315927}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is around 8.0 for n-butylamine oxidation.
CC {ECO:0000269|PubMed:27315927};
CC -!- SUBUNIT: Heterotrimer of an alpha, a beta and a gamma subunit.
CC {ECO:0000269|PubMed:11704672, ECO:0000269|PubMed:12686145,
CC ECO:0000269|PubMed:27315927}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:27315927}. Note=Is
CC probably co-translocated into the periplasm when associated with the
CC alpha and/or beta subunit, which contain both a signal peptide.
CC {ECO:0000250|UniProtKB:Q8VUS8}.
CC -!- PTM: The cysteine tryptophylquinone (CTQ) is generated by oxidation of
CC the indole ring of a tryptophan residue to form tryptophylquinone,
CC followed by covalent cross-linking with a cysteine residue.
CC {ECO:0000269|PubMed:11555656, ECO:0000269|PubMed:11704672}.
CC -!- MASS SPECTROMETRY: Mass=8486.5; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11555656};
CC -!- MASS SPECTROMETRY: Mass=8504.0; Method=Electrospray; Note=With
CC methionine sulfoxide.; Evidence={ECO:0000269|PubMed:11555656};
CC -!- SIMILARITY: Belongs to the quinohemoprotein amine dehydrogenase subunit
CC gamma family. {ECO:0000305}.
CC -!- CAUTION: The oxidation form of Met-30 is subject of controversy and
CC could be the artifactual result of sample handling.
CC {ECO:0000305|PubMed:11555656}.
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DR EMBL; AB063331; BAB72010.1; -; Genomic_DNA.
DR PDB; 1JMX; X-ray; 1.90 A; G=1-79.
DR PDB; 1JMZ; X-ray; 2.00 A; G=1-79.
DR PDBsum; 1JMX; -.
DR PDBsum; 1JMZ; -.
DR AlphaFoldDB; P0A182; -.
DR SMR; P0A182; -.
DR STRING; 1240350.AMZE01000071_gene4491; -.
DR eggNOG; ENOG50324ZB; Bacteria.
DR BRENDA; 1.4.9.2; 5092.
DR EvolutionaryTrace; P0A182; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0030058; F:amine dehydrogenase activity; IEA:RHEA.
DR Gene3D; 4.10.940.10; -; 1.
DR InterPro; IPR015084; QH-AmDH_gsu_dom.
DR InterPro; IPR036487; QH-AmDH_gsu_sf.
DR Pfam; PF08992; QH-AmDH_gamma; 1.
DR SUPFAM; SSF69131; SSF69131; 1.
PE 1: Evidence at protein level;
KW 3D-structure; CTQ; Direct protein sequencing; Electron transport;
KW Oxidation; Oxidoreductase; Periplasm; Thioether bond; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11555656"
FT CHAIN 2..79
FT /note="Quinohemoprotein amine dehydrogenase subunit gamma"
FT /id="PRO_0000220551"
FT ACT_SITE 33
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:12686145,
FT ECO:0000305|PubMed:11704672"
FT MOD_RES 43
FT /note="Tryptophylquinone"
FT /evidence="ECO:0000269|PubMed:11555656,
FT ECO:0000269|PubMed:11704672"
FT CROSSLNK 7..16
FT /note="4-cysteinyl-glutamic acid (Cys-Glu)"
FT /evidence="ECO:0000269|PubMed:11555656,
FT ECO:0000269|PubMed:11704672"
FT CROSSLNK 27..33
FT /note="3-cysteinyl-aspartic acid (Cys-Asp)"
FT /evidence="ECO:0000269|PubMed:11555656,
FT ECO:0000269|PubMed:11704672"
FT CROSSLNK 37..43
FT /note="4'-cysteinyl-tryptophylquinone (Cys-Trp)"
FT /evidence="ECO:0000269|PubMed:11555656,
FT ECO:0000269|PubMed:11704672"
FT CROSSLNK 41..49
FT /note="3-cysteinyl-aspartic acid (Cys-Asp)"
FT /evidence="ECO:0000269|PubMed:11555656,
FT ECO:0000269|PubMed:11704672"
FT VARIANT 62
FT /note="S -> T (in strain: IFO 15366)"
FT /evidence="ECO:0000269|PubMed:11555656"
FT VARIANT 66
FT /note="E -> D (in strain: IFO 15366)"
FT /evidence="ECO:0000269|PubMed:11555656"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:1JMX"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:1JMX"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:1JMX"
FT HELIX 34..38
FT /evidence="ECO:0007829|PDB:1JMX"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:1JMX"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:1JMX"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:1JMX"
FT TURN 55..60
FT /evidence="ECO:0007829|PDB:1JMX"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:1JMX"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:1JMX"
SQ SEQUENCE 79 AA; 8597 MW; 3B7EA9B9A4AB7298 CRC64;
MSAVAGCTAT TDPGWEVDAF GGVSSLCQPM EADLYGCSDP CWWPAQVPDM MSTYQDWNAQ
ASNSAEDWRN LGTVFPKDK
