QADG_PARDE
ID QADG_PARDE Reviewed; 82 AA.
AC Q8VUS8;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Quinohemoprotein amine dehydrogenase subunit gamma;
DE Short=QH-AmDH {ECO:0000303|PubMed:10346915};
DE EC=1.4.2.- {ECO:0000269|PubMed:11168384, ECO:0000305|PubMed:10346915};
DE AltName: Full=Quinohemoprotein amine dehydrogenase 9 kDa subunit;
DE AltName: Full=Quinohemoprotein amine dehydrogenase catalytic subunit;
GN Name=qhnDH;
OS Paracoccus denitrificans.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=266;
RN [1] {ECO:0007744|PDB:1JJU}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 36-51, X-RAY
RP CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1-79, IDENTIFICATION BY MASS
RP SPECTROMETRY, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND ACTIVE SITE.
RC STRAIN=NBRC 12442;
RX PubMed=11717396; DOI=10.1073/pnas.241429098;
RA Datta S., Mori Y., Takagi K., Kawaguchi K., Chen Z.-W., Okajima T.,
RA Kuroda S., Ikeda T., Kano K., Tanizawa K., Mathews F.S.;
RT "Structure of a quinohemoprotein amine dehydrogenase with an uncommon redox
RT cofactor and highly unusual crosslinking.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14268-14273(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP AND INDUCTION.
RC STRAIN=NBRC 12442;
RX PubMed=10346915; DOI=10.1021/bi9828268;
RA Takagi K., Torimura M., Kawaguchi K., Kano K., Ikeda T.;
RT "Biochemical and electrochemical characterization of quinohemoprotein amine
RT dehydrogenase from Paracoccus denitrificans.";
RL Biochemistry 38:6935-6942(1999).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC STRAIN=NBRC 12442;
RX PubMed=11168384; DOI=10.1046/j.1432-1033.2001.01912.x;
RA Takagi K., Yamamoto K., Kano K., Ikeda T.;
RT "New pathway of amine oxidation respiratory chain of Paracoccus
RT denitrificans IFO 12442.";
RL Eur. J. Biochem. 268:470-476(2001).
RN [4] {ECO:0007744|PDB:1PBY}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-79 IN COMPLEX WITH THE
RP INHIBITOR PHENYLHYDRAZINE, COFACTOR, ACTIVITY REGULATION, SUBUNIT, AND
RP ACTIVE SITE.
RX PubMed=12925784; DOI=10.1107/s090744490301429x;
RA Datta S., Ikeda T., Kano K., Mathews F.S.;
RT "Structure of the phenylhydrazine adduct of the quinohemoprotein amine
RT dehydrogenase from Paracoccus denitrificans at 1.7 A resolution.";
RL Acta Crystallogr. D 59:1551-1556(2003).
CC -!- FUNCTION: Catalyzes the oxidative deamination of a wide range of
CC primary aliphatic and aromatic amines (PubMed:10346915). The
CC physiological electron acceptor is the constitutive cytochrome c550
CC (PubMed:11168384). {ECO:0000269|PubMed:10346915,
CC ECO:0000269|PubMed:11168384}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aliphatic amine + 2 Fe(III)-[cytochrome c550] + H2O = an
CC aldehyde + 2 Fe(II)-[cytochrome c550] + 2 H(+) + NH4(+);
CC Xref=Rhea:RHEA:21916, Rhea:RHEA-COMP:11209, Rhea:RHEA-COMP:11210,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:58001; Evidence={ECO:0000269|PubMed:11168384,
CC ECO:0000305|PubMed:10346915};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21917;
CC Evidence={ECO:0000269|PubMed:11168384, ECO:0000305|PubMed:10346915};
CC -!- COFACTOR:
CC Name=cysteine tryptophylquinone residue; Xref=ChEBI:CHEBI:20252;
CC Evidence={ECO:0000269|PubMed:11717396, ECO:0000269|PubMed:12925784};
CC Note=Contains 1 cysteine tryptophylquinone per subunit.
CC {ECO:0000269|PubMed:11717396, ECO:0000269|PubMed:12925784};
CC -!- ACTIVITY REGULATION: Inhibited by carbonyl reagents such as hydrazine,
CC hydroxylamine, phenylhydrazine and semicarbazide.
CC {ECO:0000269|PubMed:10346915, ECO:0000269|PubMed:12925784}.
CC -!- SUBUNIT: Heterotrimer of an alpha, a beta and a gamma subunit.
CC {ECO:0000269|PubMed:11717396, ECO:0000269|PubMed:12925784}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10346915,
CC ECO:0000269|PubMed:11168384}. Note=Is probably co-translocated into the
CC periplasm when associated with the alpha and/or beta subunit, which
CC contain both a signal peptide. {ECO:0000305|PubMed:11717396}.
CC -!- INDUCTION: Induced by growth on methylamine, n-butylamine or
CC benzylamine. {ECO:0000269|PubMed:10346915}.
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:11717396, ECO:0000269|PubMed:12925784}.
CC -!- SIMILARITY: Belongs to the quinohemoprotein amine dehydrogenase subunit
CC gamma family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB78728.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB063330; BAB78728.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011748000.1; NZ_PPGA01000004.1.
DR PDB; 1JJU; X-ray; 2.05 A; C=1-79.
DR PDB; 1PBY; X-ray; 1.70 A; C=1-79.
DR PDBsum; 1JJU; -.
DR PDBsum; 1PBY; -.
DR AlphaFoldDB; Q8VUS8; -.
DR SMR; Q8VUS8; -.
DR DrugBank; DB08646; TRW3-(2-AMINO-3-HYDROXY-PROPYL)-6-(N'-CYCLOHEXYL-HYDRAZINO)OCTAHYDRO-INDOL-7-OL.
DR BioCyc; MetaCyc:MON-15728; -.
DR SABIO-RK; Q8VUS8; -.
DR EvolutionaryTrace; Q8VUS8; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016638; F:oxidoreductase activity, acting on the CH-NH2 group of donors; IEA:InterPro.
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 Oxidoreductase; Periplasm; Thioether bond; Transport.
FT CHAIN 1..82
FT /note="Quinohemoprotein amine dehydrogenase subunit gamma"
FT /id="PRO_0000220552"
FT ACT_SITE 33
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:12925784,
FT ECO:0000305|PubMed:11717396"
FT MOD_RES 43
FT /note="Tryptophylquinone"
FT /evidence="ECO:0000269|PubMed:11717396,
FT ECO:0000269|PubMed:12925784"
FT CROSSLNK 7..16
FT /note="4-cysteinyl-glutamic acid (Cys-Glu)"
FT /evidence="ECO:0000269|PubMed:11717396"
FT CROSSLNK 27..33
FT /note="3-cysteinyl-aspartic acid (Cys-Asp)"
FT /evidence="ECO:0000269|PubMed:11717396"
FT CROSSLNK 37..43
FT /note="4'-cysteinyl-tryptophylquinone (Cys-Trp)"
FT /evidence="ECO:0000269|PubMed:11717396,
FT ECO:0000269|PubMed:12925784"
FT CROSSLNK 41..49
FT /note="3-cysteinyl-aspartic acid (Cys-Asp)"
FT /evidence="ECO:0000269|PubMed:11717396"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:1PBY"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1PBY"
FT HELIX 31..38
FT /evidence="ECO:0007829|PDB:1PBY"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:1PBY"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:1JJU"
FT TURN 50..53
FT /evidence="ECO:0007829|PDB:1PBY"
FT TURN 55..60
FT /evidence="ECO:0007829|PDB:1PBY"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:1PBY"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:1PBY"
SQ SEQUENCE 82 AA; 8966 MW; CFA1A0111B19A319 CRC64;
MNALVGCTTS FDPGWEVDAF GAVSNLCQPM EADLYGCADP CWWPAQVADT LNTYPNWSAG
ADDVMQDWRK LQSVFPETKG SS
