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Quinohemoprotein amine dehydrogenase subunit gamma (QH-AmDH) (EC 1.4.99.-) (Quinohemoprotein amine dehydrogenase 9 kDa subunit) (Quinohemoprotein amine dehydrogenase catalytic subunit)

 QADG_PARDE              Reviewed;          82 AA.
Q8VUS8;
27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
27-JUN-2003, sequence version 2.
22-NOV-2017, entry version 73.
RecName: Full=Quinohemoprotein amine dehydrogenase subunit gamma;
Short=QH-AmDH;
EC=1.4.99.-;
AltName: Full=Quinohemoprotein amine dehydrogenase 9 kDa subunit;
AltName: Full=Quinohemoprotein amine dehydrogenase catalytic subunit;
Name=qhnDH;
Paracoccus denitrificans.
Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
Rhodobacteraceae; Paracoccus.
NCBI_TaxID=266;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 36-51, X-RAY
CRYSTALLOGRAPHY (2.05 ANGSTROMS), AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=11717396; DOI=10.1073/pnas.241429098;
Datta S., Mori Y., Takagi K., Kawaguchi K., Chen Z.-W., Okajima T.,
Kuroda S., Ikeda T., Kano K., Tanizawa K., Mathews F.S.;
"Structure of a quinohemoprotein amine dehydrogenase with an uncommon
redox cofactor and highly unusual crosslinking.";
Proc. Natl. Acad. Sci. U.S.A. 98:14268-14273(2001).
-!- FUNCTION: Catalyzes the oxidative deamination of a wide range of
aliphatic and aromatic amines.
-!- CATALYTIC ACTIVITY: RCH(2)NH(2) + H(2)O + acceptor = RCHO + NH(3)
+ reduced acceptor.
-!- COFACTOR:
Name=cysteine tryptophylquinone residue; Xref=ChEBI:CHEBI:20252;
Note=Contains 1 cysteine tryptophylquinone per subunit.;
-!- SUBUNIT: Heterotrimer of an alpha, a beta and a gamma subunit.
-!- SUBCELLULAR LOCATION: Periplasm.
-!- PTM: The cysteine tryptophylquinone (CTQ) is generated by
oxidation of the indole ring of a tryptophan residue to form
tryptophylquinone, followed by covalent cross-linking with a
cysteine residue.
-!- MISCELLANEOUS: Is probably co-translocated into the periplasm when
associated with the alpha and/or beta subunit, which contain both
a signal peptide.
-!- MISCELLANEOUS: The natural electron acceptor is cytochrome c-550.
-!- SEQUENCE CAUTION:
Sequence=BAB78728.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AB063330; BAB78728.1; ALT_INIT; Genomic_DNA.
RefSeq; WP_011748000.1; NZ_FOYK01000030.1.
PDB; 1JJU; X-ray; 2.05 A; C=1-79.
PDB; 1PBY; X-ray; 1.70 A; C=1-79.
PDBsum; 1JJU; -.
PDBsum; 1PBY; -.
ProteinModelPortal; Q8VUS8; -.
SMR; Q8VUS8; -.
DrugBank; DB08646; TRW3-(2-AMINO-3-HYDROXY-PROPYL)-6-(N'-CYCLOHEXYL-HYDRAZINO)OCTAHYDRO-INDOL-7-OL.
eggNOG; ENOG4105I7I; Bacteria.
eggNOG; ENOG4111QYC; LUCA.
BioCyc; MetaCyc:MONOMER-15728; -.
SABIO-RK; Q8VUS8; -.
EvolutionaryTrace; Q8VUS8; -.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0016638; F:oxidoreductase activity, acting on the CH-NH2 group of donors; IEA:InterPro.
InterPro; IPR015084; QH-AmDH_gsu_dom.
InterPro; IPR036487; QH-AmDH_gsu_sf.
Pfam; PF08992; QH-AmDH_gamma; 1.
ProDom; PD591508; QHaem_AmDH_gsu; 1.
SUPFAM; SSF69131; SSF69131; 1.
1: Evidence at protein level;
3D-structure; CTQ; Direct protein sequencing; Electron transport;
Oxidoreductase; Periplasm; Thioether bond; Transport.
CHAIN 1 82 Quinohemoprotein amine dehydrogenase
subunit gamma.
/FTId=PRO_0000220552.
ACT_SITE 33 33 Proton acceptor.
MOD_RES 43 43 Tryptophylquinone.
CROSSLNK 7 16 4-cysteinyl-glutamic acid (Cys-Glu).
CROSSLNK 27 33 3-cysteinyl-aspartic acid (Cys-Asp).
CROSSLNK 37 43 4'-cysteinyl-tryptophylquinone (Cys-Trp).
CROSSLNK 41 49 3-cysteinyl-aspartic acid (Cys-Asp).
STRAND 12 18 {ECO:0000244|PDB:1PBY}.
STRAND 21 23 {ECO:0000244|PDB:1PBY}.
HELIX 31 38 {ECO:0000244|PDB:1PBY}.
TURN 39 41 {ECO:0000244|PDB:1PBY}.
TURN 44 46 {ECO:0000244|PDB:1JJU}.
TURN 50 53 {ECO:0000244|PDB:1PBY}.
TURN 55 60 {ECO:0000244|PDB:1PBY}.
HELIX 64 67 {ECO:0000244|PDB:1PBY}.
HELIX 68 70 {ECO:0000244|PDB:1PBY}.
SEQUENCE 82 AA; 8966 MW; CFA1A0111B19A319 CRC64;
MNALVGCTTS FDPGWEVDAF GAVSNLCQPM EADLYGCADP CWWPAQVADT LNTYPNWSAG
ADDVMQDWRK LQSVFPETKG SS


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