QADG_PSEPK
ID QADG_PSEPK Reviewed; 79 AA.
AC P0A181; Q88HA0; Q8VW83;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Quinohemoprotein amine dehydrogenase subunit gamma;
DE Short=QH-AmDH;
DE EC=1.4.9.- {ECO:0000250|UniProtKB:P0A182};
DE AltName: Full=Quinohemoprotein amine dehydrogenase 9 kDa subunit;
DE AltName: Full=Quinohemoprotein amine dehydrogenase catalytic subunit;
GN Name=qhnDH; OrderedLocusNames=PP_3460;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
CC -!- FUNCTION: Catalyzes the oxidative deamination of a wide range of
CC aliphatic monoamines and diamines (By similarity). The physiological
CC electron acceptor is an azurin-like blue protein (By similarity).
CC {ECO:0000250|UniProtKB:P0A182}.
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:0000250|UniProtKB:P0A182};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51129;
CC Evidence={ECO:0000250|UniProtKB:P0A182};
CC -!- COFACTOR:
CC Name=cysteine tryptophylquinone residue; Xref=ChEBI:CHEBI:20252;
CC Evidence={ECO:0000250|UniProtKB:P0A182};
CC Note=Contains 1 cysteine tryptophylquinone per subunit.
CC {ECO:0000250|UniProtKB:P0A182};
CC -!- SUBUNIT: Heterotrimer of an alpha, a beta and a gamma subunit.
CC {ECO:0000250|UniProtKB:P0A182}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P0A182}. 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:0000250|UniProtKB:P0A182}.
CC -!- SIMILARITY: Belongs to the quinohemoprotein amine dehydrogenase subunit
CC gamma family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN69062.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE015451; AAN69062.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_745598.1; NC_002947.4.
DR AlphaFoldDB; P0A181; -.
DR SMR; P0A181; -.
DR STRING; 160488.PP_3460; -.
DR EnsemblBacteria; AAN69062; AAN69062; PP_3460.
DR KEGG; ppu:PP_3460; -.
DR PATRIC; fig|160488.4.peg.3677; -.
DR eggNOG; ENOG50324ZB; Bacteria.
DR HOGENOM; CLU_177012_0_0_6; -.
DR OMA; CSDPCWW; -.
DR Proteomes; UP000000556; Chromosome.
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 3: Inferred from homology;
KW CTQ; Electron transport; Oxidoreductase; Periplasm; Reference proteome;
KW Thioether bond; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P0A182"
FT CHAIN 2..79
FT /note="Quinohemoprotein amine dehydrogenase subunit gamma"
FT /id="PRO_0000220550"
FT ACT_SITE 33
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0A182"
FT MOD_RES 43
FT /note="Tryptophylquinone"
FT /evidence="ECO:0000250|UniProtKB:P0A182"
FT CROSSLNK 7..16
FT /note="4-cysteinyl-glutamic acid (Cys-Glu)"
FT /evidence="ECO:0000250|UniProtKB:P0A182"
FT CROSSLNK 27..33
FT /note="3-cysteinyl-aspartic acid (Cys-Asp)"
FT /evidence="ECO:0000250|UniProtKB:P0A182"
FT CROSSLNK 37..43
FT /note="4'-cysteinyl-tryptophylquinone (Cys-Trp)"
FT /evidence="ECO:0000250|UniProtKB:P0A182"
FT CROSSLNK 41..49
FT /note="3-cysteinyl-aspartic acid (Cys-Asp)"
FT /evidence="ECO:0000250|UniProtKB:P0A182"
SQ SEQUENCE 79 AA; 8597 MW; 3B7EA9B9A4AB7298 CRC64;
MSAVAGCTAT TDPGWEVDAF GGVSSLCQPM EADLYGCSDP CWWPAQVPDM MSTYQDWNAQ
ASNSAEDWRN LGTVFPKDK
