KDHA_PAENI
ID KDHA_PAENI Reviewed; 296 AA.
AC O87681;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=6-hydroxypseudooxynicotine dehydrogenase complex subunit alpha;
DE EC=1.5.99.14;
DE AltName: Full=Ketone dehydrogenase medium FAD subunit;
GN Name=kdhA; Synonyms=kdhM;
OS Paenarthrobacter nicotinovorans (Arthrobacter nicotinovorans).
OG Plasmid pAO1.
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX NCBI_TaxID=29320;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-24, FUNCTION,
RP COFACTOR, AND SUBUNIT.
RX PubMed=9878353; DOI=10.1006/jmbi.1998.2227;
RA Schenk S., Hoelz A., Kraus B., Decker K.;
RT "Gene structures and properties of enzymes of the plasmid-encoded nicotine
RT catabolism of Arthrobacter nicotinovorans.";
RL J. Mol. Biol. 284:1323-1339(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11514508; DOI=10.1128/jb.183.18.5262-5267.2001;
RA Baitsch D., Sandu C., Brandsch R., Igloi G.L.;
RT "Gene cluster on pAO1 of Arthrobacter nicotinovorans involved in
RT degradation of the plant alkaloid nicotine: cloning, purification, and
RT characterization of 2,6-dihydroxypyridine 3-hydroxylase.";
RL J. Bacteriol. 183:5262-5267(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12618462; DOI=10.1128/jb.185.6.1976-1986.2003;
RA Igloi G.L., Brandsch R.;
RT "Sequence of the 165-kilobase catabolic plasmid pAO1 from Arthrobacter
RT nicotinovorans and identification of a pAO1-dependent nicotine uptake
RT system.";
RL J. Bacteriol. 185:1976-1986(2003).
CC -!- FUNCTION: Molybdo-flavoprotein enzyme complex involved in nicotine
CC degradation. The subunit gamma (large subunit) contains the substrate-
CC binding sites, the subunit alpha (medium subunit) binds FAD and the
CC subunit beta (small subunit) has a 2Fe-2S ferredoxin-type domain which
CC binds 2 2Fe-2S clusters. {ECO:0000269|PubMed:9878353}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-hydroxypseudooxynicotine + A + H2O = 2,6-
CC dihydroxypseudooxynicotine + AH2; Xref=Rhea:RHEA:34223,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:58682, ChEBI:CHEBI:66944; EC=1.5.99.14;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:9878353};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:9878353};
CC -!- PATHWAY: Alkaloid degradation; nicotine degradation.
CC -!- SUBUNIT: Heterohexamer of 2 alpha (kdhA), 2 beta (kdhB) and 2 gamma
CC (kdhC) subunit. Dimer of heterotrimers (Probable).
CC {ECO:0000305|PubMed:9878353}.
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DR EMBL; AF373840; AAK64248.1; -; Genomic_DNA.
DR EMBL; AJ306903; CAC37486.2; -; Genomic_DNA.
DR EMBL; AJ507836; CAD47945.1; -; Genomic_DNA.
DR RefSeq; WP_016359456.1; NC_021229.1.
DR RefSeq; YP_007988771.1; NC_021229.1.
DR PDB; 7DQX; X-ray; 3.44 A; B/E=1-296.
DR PDBsum; 7DQX; -.
DR AlphaFoldDB; O87681; -.
DR SMR; O87681; -.
DR KEGG; ag:CAC37486; -.
DR BioCyc; MetaCyc:MON-981; -.
DR UniPathway; UPA00106; -.
DR GO; GO:0034909; F:6-hydroxypseudooxynicotine dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0019608; P:nicotine catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR005107; CO_DH_flav_C.
DR InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR Pfam; PF03450; CO_deh_flav_C; 1.
DR Pfam; PF00941; FAD_binding_5; 1.
DR SMART; SM01092; CO_deh_flav_C; 1.
DR SUPFAM; SSF55447; SSF55447; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; FAD; Flavoprotein; Oxidoreductase;
KW Plasmid.
FT CHAIN 1..296
FT /note="6-hydroxypseudooxynicotine dehydrogenase complex
FT subunit alpha"
FT /id="PRO_0000424215"
FT DOMAIN 1..177
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 30..37
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 111..115
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 37..42
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 78..82
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 112..118
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:7DQX"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 144..148
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 177..186
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 195..205
FT /evidence="ECO:0007829|PDB:7DQX"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:7DQX"
FT STRAND 209..223
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 228..234
FT /evidence="ECO:0007829|PDB:7DQX"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 244..250
FT /evidence="ECO:0007829|PDB:7DQX"
FT TURN 251..254
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 265..270
FT /evidence="ECO:0007829|PDB:7DQX"
FT TURN 271..274
FT /evidence="ECO:0007829|PDB:7DQX"
FT HELIX 275..283
FT /evidence="ECO:0007829|PDB:7DQX"
SQ SEQUENCE 296 AA; 31429 MW; 7FCBD912AF400631 CRC64;
MKPPSFDYVV ADSVEHALRL LADGGDDAKI IAGGQSLVPL LNFRMSRPSL LVDINRVPGL
ANIRKSDQTI AIGALTRHAK LTTSKTISQN LPILSEAAAW IAHPQIRNRG TIGGSLAHAD
AAAELPVVLL ALDAYVTAQS LQGERKIPLK ELLVSHFVSS ILPGELIVEV NVPQLPHGSG
AAFDEFSRRH GDYAIGGAAS IVTLDEQGKC SRARITVLGG GSTAIRCQEA ENILIDSTLS
SHDIAAAAHA AVQGLDPVPT VHGSAQYRAQ VIRTMVERTL AKALHRARPT KESMDH
